A Peptide Sequence from Bax That Converts Bcl-2 into an Activator of Apoptosis
Open Access
- 12 April 1996
- journal article
- Published by Elsevier
- Vol. 271 (15), 8521-8524
- https://doi.org/10.1074/jbc.271.15.8521
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Structure-Function Analysis of Bcl-2 ProteinJournal of Biological Chemistry, 1995
- Regulation of Lymphocyte Survival by the BCL-2 Gene FamilyAnnual Review of Immunology, 1995
- Bad, a heterodimeric partner for Bcl-xL and Bcl-2, displaces bax and promotes cell deathCell, 1995
- Checkpoints of dueling dimers foil death wishesCell, 1994
- Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system.Proceedings of the National Academy of Sciences, 1994
- The protein bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis.The Journal of cell biology, 1994
- BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with BaxNature, 1994
- Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3Cell, 1993
- Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell deathCell, 1993
- bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell deathCell, 1993