Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size.
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Control of adult neurogenesis by programmed cell death in the mammalian brainMinimalist Model Systems Reveal Similarities and Differences between Membrane Interaction Modes of MCL1 and BAKAssembling the puzzle: Oligomerization of α-pore forming proteins in membranesRelease of Cytochrome C from Bax Pores at the Mitochondrial Membrane.Pycnogenol Induces Nuclear Translocation of Apoptosis-inducing Factor and Caspase-independent Apoptosis in MC-3 Human Mucoepidermoid Carcinoma Cell Line.Visual and functional demonstration of growing Bax-induced pores in mitochondrial outer membranes.Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric speciesBH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranesIn Situ Characterization of Bak Clusters Responsible for Cell Death Using Single Molecule Localization Microscopy.Oncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane.Molecular basis of hair cell loss.Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores.Milestones and recent discoveries on cell death mediated by mitochondria and their interactions with biologically active amines.Bax and Bak Pores: Are We Closing the Circle?BAX to basics: How the BCL2 gene family controls the death of retinal ganglion cells.Apoptotic foci at mitochondria: in and around Bax pores.Pore formation by dimeric Bak and Bax: an unusual pore?Automated analysis of giant unilamellar vesicles using circular Hough transformation.cBid, Bax and Bcl-xL exhibit opposite membrane remodeling activities.Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation.Effect of Content of Sulfate Groups in Seaweed Polysaccharides on Antioxidant Activity and Repair Effect of Subcellular Organelles in Injured HK-2 Cells.Live-cell imaging to measure BAX recruitment kinetics to mitochondria during apoptosis.Toxicity of an α-pore-forming toxin depends on the assembly mechanism on the target membrane as revealed by single molecule imaging.Structural model of active Bax at the membrane.Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains.Membrane insertion of the BAX core, but not latch domain, drives apoptotic pore formation.BCL-2 family proteins: changing partners in the dance towards death.Bax, Bak and beyond - mitochondrial performance in apoptosis.Effect of Src Kinase inhibition on Cytochrome c, Smac/DIABLO and Apoptosis Inducing Factor (AIF) Following Cerebral Hypoxia-Ischemia in Newborn Piglets.Melilotus indicus extract induces apoptosis in hepatocellular carcinoma cells via a mechanism involving mitochondria-mediated pathways.The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID.Bcl-2 proteins: Unraveling the details of a complex and dynamic network.Regulatory role of calpain in neuronal death.Micro-Economics of Apoptosis in Cancer: ncRNAs Modulation of BCL-2 Family Members.
P2860
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P2860
Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size.
@en
type
label
Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size.
@en
prefLabel
Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size.
@en
P2093
P2860
P356
P1476
Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size.
@en
P2093
Ane Landajuela
Gorka Basañez
Olatz Landeta
P2860
P304
33241-33252
P356
10.1074/JBC.M113.512087
P407
P577
2013-10-07T00:00:00Z