A Death Effector Domain Chain DISC Model Reveals a Crucial Role for Caspase-8 Chain Assembly in Mediating Apoptotic Cell Death
Open Access
- 27 July 2012
- journal article
- research article
- Published by Elsevier BV in Molecular Cell
- Vol. 47 (2), 291-305
- https://doi.org/10.1016/j.molcel.2012.05.004
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosisNature, 2011
- The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutationsNature Structural & Molecular Biology, 2010
- Membrane-bound Fas ligand only is essential for Fas-induced apoptosisNature, 2009
- Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced InflammationCell, 2009
- Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-αCell, 2009
- Cullin3-Based Polyubiquitination and p62-Dependent Aggregation of Caspase-8 Mediate Extrinsic Apoptosis SignalingCell, 2009
- Protein structure prediction on the Web: a case study using the Phyre serverNature Protocols, 2009
- The Fas–FADD death domain complex structure unravels signalling by receptor clusteringNature, 2008
- Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signalingThe EMBO Journal, 2006
- Empirical Statistical Model To Estimate the Accuracy of Peptide Identifications Made by MS/MS and Database SearchAnalytical Chemistry, 2002