Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process - Wikidata - wikimedia - TriplyDB

Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process

Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process

http://www.wikidata.org/entity/Q41975085

about

Dual function of mitochondrial Nm23-H4 protein in phosphotransfer and intermembrane lipid transfer: a cardiolipin-dependent switch Mitochondria, cholesterol and cancer cell metabolism Glutathione and mitochondria A new view of the lethal apoptotic pore BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore Mitochondrial glutathione: features, regulation and role in disease Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis Minimalist Model Systems Reveal Similarities and Differences between Membrane Interaction Modes of MCL1 and BAK Specific interaction with cardiolipin triggers functional activation of Dynamin-Related Protein 1 Cytochrome c causes pore formation in cardiolipin-containing membranes The rheostat in the membrane: BCL-2 family proteins and apoptosis Beta-amyloid oligomers activate apoptotic BAK pore for cytochrome c release.Visual and functional demonstration of growing Bax-induced pores in mitochondrial outer membranes.The dynamics of Bax channel formation: influence of ionic strength Direct activation of full-length proapoptotic BAK Mechanisms of action of Bcl-2 family proteins Three-dimensional structure of Bax-mediated pores in membrane bilayers.Biguanides sensitize leukemia cells to ABT-737-induced apoptosis by inhibiting mitochondrial electron transport Death upon a kiss: mitochondrial outer membrane composition and organelle communication govern sensitivity to BAK/BAX-dependent apoptosis.The secrets of the Bcl-2 family.Apoptosis regulation at the mitochondrial outer membrane.Triatoma virus recombinant VP4 protein induces membrane permeability through dynamic pores.Emerging understanding of Bcl-2 biology: Implications for neoplastic progression and treatment.The deadly landscape of pro-apoptotic BCL-2 proteins in the outer mitochondrial membrane.Bax and Bak Pores: Are We Closing the Circle?Apoptotic foci at mitochondria: in and around Bax pores.Pore formation by dimeric Bak and Bax: an unusual pore?cBid, Bax and Bcl-xL exhibit opposite membrane remodeling activities.Toxicity of an α-pore-forming toxin depends on the assembly mechanism on the target membrane as revealed by single molecule imaging.Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size.MOMP, cell suicide as a BCL-2 family business.Bax, Bak and beyond - mitochondrial performance in apoptosis.NME4/nucleoside diphosphate kinase D in cardiolipin signaling and mitophagy.The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID.Mitochondrial NM23-H4/NDPK-D: a bifunctional nanoswitch for bioenergetics and lipid signaling.

P2860

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P2860

Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process

http://www.wikidata.org/entity/Q41975085

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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2011年论文

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name

Reconstitution of proapoptotic ...... brane permeabilization process

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Reconstitution of proapoptotic ...... brane permeabilization process

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Reconstitution of proapoptotic ...... brane permeabilization process

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JBC.M110.165852

P1433

Journal of Biological Chemistry

P1476

Reconstitution of proapoptotic ...... brane permeabilization process

@en

P2093

Ane Landajuela

http://www.w3.org/2001/XMLSchema#string

Begoña Sot

http://www.w3.org/2001/XMLSchema#string

Carmelo Di Primo

http://www.w3.org/2001/XMLSchema#string

Gorka Basañez

http://www.w3.org/2001/XMLSchema#string

Mikel Valle

http://www.w3.org/2001/XMLSchema#string

Olatz Landeta

http://www.w3.org/2001/XMLSchema#string

Stefka Taneva

http://www.w3.org/2001/XMLSchema#string

P2860

Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function

Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak

Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis

Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization

Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.

A stapled BID BH3 helix directly binds and activates BAX

Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax

Endophilin B1/Bif-1 stimulates BAX activation independently from its capacity to produce large scale membrane morphological rearrangements

The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site

BAX activation is initiated at a novel interaction site

P304

8213-8230

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scholarly article

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10.1074/JBC.M110.165852

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10

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286

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Vadim A. Frolov

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2011-01-01T00:00:00Z

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21196599

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3048708

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