Cleavage of the Apoptosis Inhibitor DIAP1 by the Apical Caspase DRONC in Both Normal and Apoptotic Drosophila Cells
Open Access
- 1 May 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (19) , 18683-18688
- https://doi.org/10.1074/jbc.m501206200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- The two cytochrome c species, DC3 and DC4, are not required for caspase activation and apoptosis in Drosophila cellsThe Journal of cell biology, 2004
- Ubiquitin protein ligase activity of the anti-apoptotic baculovirus protein Op-IAP3Virus Research, 2004
- The N-end rule and regulation of apoptosisNature Cell Biology, 2003
- The Drosophila DIAP1 Protein Is Required to Prevent Accumulation of a Continuously Generated, Processed Form of the Apical Caspase DRONCJournal of Biological Chemistry, 2002
- IAP proteins: blocking the road to death's doorNature Reviews Molecular Cell Biology, 2002
- Down-regulation of DIAP1 Triggers a NovelDrosophila Cell Death Pathway Mediated by Dark and DRONCJournal of Biological Chemistry, 2002
- The role of cytochrome c in caspase activation in Drosophila melanogaster cellsThe Journal of cell biology, 2002
- c-IAP1 Is Cleaved by Caspases to Produce a Proapoptotic C-terminal FragmentJournal of Biological Chemistry, 2001
- The Drosophila caspase DRONC is a glutamate/aspartate protease whose activity is regulated by DIAP1, HID and GRIMJournal of Biological Chemistry, 2000
- Ubiquitin Protein Ligase Activity of IAPs and Their Degradation in Proteasomes in Response to Apoptotic StimuliScience, 2000