Structure assembly of Bcl-xL through α5–α5 and α6–α6 interhelix interactions in lipid membranes
TLDR
The results indicated that Bcl-x(L) dimer trapped by cross-linking in lipids is distinct from the domain swapped dimer, suggesting that B Cl-x (L) transits through a structural change from the water-soluble state to the membrane-bound state and there are multiple possibilities for structural reorganization of B cl-x-L) protein.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2009-11-01 and is currently open access. It has received 4 citations till now. The article focuses on the topics: Protein structure & Lipid bilayer.read more
Citations
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Journal ArticleDOI
Mechanisms of Action of Bcl-2 Family Proteins
TL;DR: These dynamic interactions cause conformational changes in the Bcl-2 proteins that modulate their apoptotic function, providing additional potential modes of regulation.
Journal ArticleDOI
Protein oligomerization mediated by the transmembrane carboxyl terminal domain of Bcl-XL
TL;DR: Bcl‐Xl physically interacts with Bcl‐ Xl by cross‐linking study (View interaction) and the results show clear signal-to-noise correspondence between the two systems.
DissertationDOI
Beyond the Active Site of the Bacterial Rhomboid Protease: Novel Interactions at the Membrane to Modulate Function
Journal ArticleDOI
Combined hypoxia hypercapnia delays apoptosis and maintains CD34 cell surface antigen
Hawraa Elhossaini,Mouna Hamad,Mohammad R. Irhimeh,Shirley Nakhla,Gobinath Pillai Rajarathnam,Ali Mohsin Abbas +5 more
TL;DR: In this article , the interactive effect of varying the concentrations of O2 (1, 5, 20 %) and CO2 (5, 15, 20 percent) on human BM-derived promyeloblast (KG-1a) apoptosis, necrosis, proliferation, and CD34 maintenance was examined.
References
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Journal ArticleDOI
Movement of Bax from the Cytosol to Mitochondria during Apoptosis
TL;DR: In cells undergoing apoptosis, an early, dramatic change occurs in the intracellular localization of Bax, and this redistribution of soluble Bax to organelle-bound GFP–Bax appears important for Bx to promote cell death.
Journal ArticleDOI
Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function
Lin Chen,Simon N. Willis,Andrew H. Wei,Brian J. Smith,Jamie I. Fletcher,Mark G. Hinds,Peter M. Colman,Catherine L. Day,Jerry M. Adams,David C.S. Huang +9 more
TL;DR: The results suggest that apoptosis relies on selective interactions between particular subsets of these proteins and that it should be feasible to discover BH3-mimetic drugs that inactivate specific prosurvival targets.
Journal ArticleDOI
BCL-2, BCL-XL Sequester BH3 Domain-Only Molecules Preventing BAX- and BAK-Mediated Mitochondrial Apoptosis
Emily H. Cheng,Michael C. Wei,Solly Weiler,Richard A. Flavell,Tak W. Mak,Tullia Lindsten,Stanley J. Korsmeyer +6 more
TL;DR: In mammals, BH3 domain-only molecules activate multidomain proapoptotic members to trigger a mitochondrial pathway, which both releases cytochrome c to activate caspases and initiates caspase-independent mitochondrial dysfunction.
Journal ArticleDOI
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.
Michael Sattler,Heng Liang,David G. Nettesheim,Robert P. Meadows,John E. Harlan,Matthias Eberstadt,Ho Sup Yoon,Suzanne B. Shuker,Brian S. Chang,Andy J. Minn,Craig B. Thompson,Stephen W. Fesik +11 more
TL;DR: The structure and binding affinities of mutant Bak peptides indicate that the Bak peptide adopts an amphipathic α helix that interacts with Bcl-xL through hydrophobic and electrostatic interactions.
Journal ArticleDOI
X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death.
Steven W. Muchmore,Michael Sattler,Heng Liang,Robert P. Meadows,John E. Harlan,Ho Sup Yoon,David G. Nettesheim,Brian S. Chang,Brian S. Chang,Craig B. Thompson,Craig B. Thompson,Sui-Lam Wong,Shi-Chung Ng,Stephen W. Fesik +13 more
TL;DR: The arrangement of the α-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphia toxin and the colicins, and may provide a clue to the mechanism of action of the B cl-2 family of proteins.