Bax forms an oligomer via separate, yet interdependent, surfaces. - Wikidata - awgldk - TriplyDB

Bax forms an oligomer via separate, yet interdependent, surfaces.

Bax forms an oligomer via separate, yet interdependent, surfaces.

http://www.wikidata.org/entity/Q33885192

about

Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis The rheostat in the membrane: BCL-2 family proteins and apoptosis Bcl-2 and Bax interact via the BH1-3 groove-BH3 motif interface and a novel interface involving the BH4 motif Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics.Resveratrol induces p53-independent, X-linked inhibitor of apoptosis protein (XIAP)-mediated Bax protein oligomerization on mitochondria to initiate cytochrome c release and caspase activation.Bax forms two types of channels, one of which is voltage-gated Mitochondria and apoptosis: emerging concepts.Natural diterpenoid compound elevates expression of Bim protein, which interacts with antiapoptotic protein Bcl-2, converting it to proapoptotic Bax-like molecule.Translocation of a Bak C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak and Bax apoptotic function.Bax dimerizes via a symmetric BH3:groove interface during apoptosis BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes Where killers meet--permeabilization of the outer mitochondrial membrane during apoptosis.Mechanisms of action of Bcl-2 family proteins Assembly of the Bak apoptotic pore: a critical role for the Bak protein α6 helix in the multimerization of homodimers during apoptosis Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes.Activation of the proapoptotic Bcl-2 protein Bax by a small molecule induces tumor cell apoptosis.After embedding in membranes antiapoptotic Bcl-XL protein binds both Bcl-2 homology region 3 and helix 1 of proapoptotic Bax protein to inhibit apoptotic mitochondrial permeabilization.Apoptosis and oncogenesis: give and take in the BCL-2 family.The secrets of the Bcl-2 family.Cell death and the mitochondria: therapeutic targeting of the BCL-2 family-driven pathway.Emerging understanding of Bcl-2 biology: Implications for neoplastic progression and treatment.Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores.Disordered clusters of Bak dimers rupture mitochondria during apoptosis.Pore formation by dimeric Bak and Bax: an unusual pore?Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics.BH3-triggered structural reorganization drives the activation of proapoptotic BAX.Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers.Structural model of active Bax at the membrane.Doughnuts, daisy chains and crescent moons: the quest for the elusive apoptotic pore.Insights into the structural stability of Bax from molecular dynamics simulations at high temperatures.The functional domains for Bax∆2 aggregate-mediated caspase 8-dependent cell death.BAK α6 permits activation by BH3-only proteins and homooligomerization via the canonical hydrophobic groove.Bax channel triplet: co-operativity and voltage gating.Allostery in BAX protein activation.

P2860

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P2860

Bax forms an oligomer via separate, yet interdependent, surfaces.

http://www.wikidata.org/entity/Q33885192

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Bax forms an oligomer via separate, yet interdependent, surfaces.

@ast

Bax forms an oligomer via separate, yet interdependent, surfaces.

@en

type

label

Bax forms an oligomer via separate, yet interdependent, surfaces.

@ast

Bax forms an oligomer via separate, yet interdependent, surfaces.

@en

prefLabel

Bax forms an oligomer via separate, yet interdependent, surfaces.

@ast

Bax forms an oligomer via separate, yet interdependent, surfaces.

@en

P1433

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P356

JBC.M110.113456

P1433

Journal of Biological Chemistry

P1476

Bax forms an oligomer via separate, yet interdependent, surfaces.

@en

P2093

Arthur E Johnson

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

Doug Boreham

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

Jialing Lin

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

Jingzhen Ding

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

Mina Falcone

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

Nicole McFarlane

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

Suzanne M Lapolla

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

Weijia Zhu

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

Xuejun C Zhang

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

Yiwei Miao

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

P2860

Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria

tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c

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

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

Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death

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

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

Conformation of the Bax C-terminus regulates subcellular location and cell death

Movement of Bax from the cytosol to mitochondria during apoptosis

P304

17614-17627

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

P31

scholarly article

P356

10.1074/JBC.M110.113456

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

P407

P433

23

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P478

285

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

P50

David W Andrews

P577

2010-04-09T00:00:00Z

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

P698

20382739

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P932

2878526

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