The Binding Properties and Biological Activities of Bcl-2 and Bax in Cells Exposed to Apoptotic Stimuli
Open Access
- 1 March 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (11) , 6110-6120
- https://doi.org/10.1074/jbc.273.11.6110
Abstract
No abstract availableKeywords
This publication has 60 references indexed in Scilit:
- Direct Interaction of the Mitochondrial Membrane Protein Carnitine Palmitoyltransferase I with Bcl-2Biochemical and Biophysical Research Communications, 1997
- The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of ApoptosisScience, 1997
- Bcl-xL forms an ion channel in synthetic lipid membranesNature, 1997
- Bcl-2 Overexpression Blocks Activation of the Death Protease CPP32/Yama/ApopainBiochemical and Biophysical Research Communications, 1996
- Molecular Ordering of the Cell Death Pathway: Bcl-2 AND Bcl-xL FUNCTION UPSTREAM OF THE CED-3-LIKE APOPTOTIC PROTEASESPublished by Elsevier ,1996
- The protein bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis.The Journal of cell biology, 1994
- Bcl-2 and the regulation of programmed cell deathThe Journal of cell biology, 1994
- Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell deathCell, 1993
- Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell deathNature, 1990
- Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocationCell, 1986