Death receptors leave a caspase footprint that Smacs of XIAP
- 1 January 2003
- journal article
- review article
- Published by Springer Nature in Cell Death & Differentiation
- Vol. 10 (1) , 4-6
- https://doi.org/10.1038/sj.cdd.4401176
Abstract
No abstract availableKeywords
This publication has 7 references indexed in Scilit:
- Structural and biochemical basis of apoptotic activation by Smac/DIABLONature, 2000
- Identification of DIABLO, a Mammalian Protein that Promotes Apoptosis by Binding to and Antagonizing IAP ProteinsCell, 2000
- Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP InhibitionCell, 2000
- The CD95 (APO-1/Fas) and the TRAIL (APO-2L) Apoptosis SystemsExperimental Cell Research, 2000
- Activation of Fas by FasL induces apoptosis by a mechanism that cannot be blocked by Bcl-2 or Bcl-xLProceedings of the National Academy of Sciences, 1999
- Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosisNature, 1999
- Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death ReceptorsCell, 1998