The role of Bcl-2 family member BNIP3 in cell death and disease: NIPping at the heels of cell death
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/cdd2008185.pdf
Reference80 articles.
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2. Chen G, Cizeau J, Vande Velde C, Park JH, Bozek G, Bolton J et al. Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins. J Biol Chem 1999; 274: 7–10.
3. Ray R, Chen G, Vande Velde C, Cizeau J, Park JH, Reed JC et al. BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites. J Biol Chem 2000; 275: 1439–1448.
4. Cizeau J, Ray R, Chen G, Gietz RD, Greenberg AH . The C. elegans orthologue ceBNIP3 interacts with CED-9 and CED-3 but kills through a BH3- and caspase-independent mechanism. Oncogene 2000; 19: 5453–5463.
5. Bocharov EV, Pustovalova YE, Pavlov KV, Volynsky PE, Goncharuk MV, Ermolyuk YS et al. Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger. J Biol Chem 2007; 282: 16256–16266.
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