tBid Undergoes Multiple Conformational Changes at the Membrane Required for Bax Activation
Published 2013 View Full Article
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Title
tBid Undergoes Multiple Conformational Changes at the Membrane Required for Bax Activation
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 30, Pages 22111-22127
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2013-06-07
DOI
10.1074/jbc.m113.482109
References
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Note: Only part of the references are listed.- Mechanisms of Action of Bcl-2 Family Proteins
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- Interaction of the full-length Bax protein with biomimetic mitochondrial liposomes: A small-angle neutron scattering and fluorescence study
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- Effects of Curvature and Composition on α-Synuclein Binding to Lipid Vesicles
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- Bid: a Bax-like BH3 protein
- (2009) L P Billen et al. ONCOGENE
- Membrane Binding by tBid Initiates an Ordered Series of Events Culminating in Membrane Permeabilization by Bax
- (2008) Jonathan F. Lovell et al. CELL
- Fluorescence Mapping of Mitochondrial TIM23 Complex Reveals a Water-Facing, Substrate-Interacting Helix Surface
- (2008) Nathan N. Alder et al. CELL
- Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands
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- Bcl-XL Inhibits Membrane Permeabilization by Competing with Bax
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- The BCL-2 protein family: opposing activities that mediate cell death
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