Dissociation of Bak α1 helix from the core and latch domains is required for apoptosis
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/ncomms7841.pdf
Reference42 articles.
1. Czabotar, P. E., Lessene, G., Strasser, A. & Adams, J. M. Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy. Nat. Rev. Mol. Cell. Biol. 15, 49–63 (2014).
2. Westphal, D., Kluck, R. M. & Dewson, G. Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis. Cell Death Differ. 21, 196–205 (2014).
3. Moldoveanu, T. et al. The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol. Cell 24, 677–688 (2006).
4. Suzuki, M., Youle, R. J. & Tjandra, N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103, 645–654 (2000).
5. Ferrer, P. E., Frederick, P., Gulbis, J. M., Dewson, G. & Kluck, R. M. Translocation of a Bak C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak and Bax apoptotic function. PLoS ONE 7, e31510 (2012).
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