Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis. - Wikidata - awgldk - TriplyDB

Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis.

Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis.

http://www.wikidata.org/entity/Q33854131

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Use of human cancer cell lines mitochondria to explore the mechanisms of BH3 peptides and ABT-737-induced mitochondrial membrane permeabilization Active Bax and Bak are functional holins tBid undergoes multiple conformational changes at the membrane required for Bax activation The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release Protein oligomerization mediated by the transmembrane carboxyl terminal domain of Bcl-XL The Bcl-2 apoptotic switch in cancer development and therapy Mitochondrial potassium channel Kv1.3 mediates Bax-induced apoptosis in lymphocytes Bcl-2 family proteins as regulators of cancer cell invasion and metastasis: a review focusing on mitochondrial respiration and reactive oxygen species Intracellular ion channels and cancer Cardiolipin and its different properties in mitophagy and apoptosis BAX activation is initiated at a novel interaction site Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA Infarct-induced steroidogenic acute regulatory protein: a survival role in cardiac fibroblasts Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis Lipids in the assembly of membrane proteins and organization of protein supercomplexes: implications for lipid-linked disorders Structural and functional similarity between the bacterial type III secretion system needle protein PrgI and the eukaryotic apoptosis Bcl-2 proteins Upregulation of Bcl2 inhibits apoptosis-driven BAX insertion but favors BAX relocalization in mitochondria Bax inserts into the mitochondrial outer membrane by different mechanisms Nerve growth factor blocks thapsigargin-induced apoptosis at the level of the mitochondrion via regulation of Bim Active fragments from pro- and antiapoptotic BCL-2 proteins have distinct membrane behavior reflecting their functional divergence Bcl-XL is qualitatively different from and ten times more effective than Bcl-2 when expressed in a breast cancer cell line Direct Activation of Bax Protein for Cancer Therapy Synthetic Antibodies Inhibit Bcl-2-associated X Protein (BAX) through Blockade of the N-terminal Activation Site.Pro-apoptotic Bax molecules densely populate the edges of membrane pores.Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2 HIV-1 Vpr-induced apoptosis is cell cycle dependent and requires Bax but not ANT The N-terminus and alpha-5, alpha-6 helices of the pro-apoptotic protein Bax, modulate functional interactions with the anti-apoptotic protein Bcl-xL.Bcl-XL inhibits membrane permeabilization by competing with Bax.Unravelling the bcl-2 apoptosis code with a simple model system.Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes Bax contains two functional mitochondrial targeting sequences and translocates to mitochondria in a conformational change- and homo-oligomerization-driven process.Facilitation of mitochondrial outer and inner membrane permeabilization and cell death in oxidative stress by a novel Bcl-2 homology 3 domain protein.Release of Cytochrome C from Bax Pores at the Mitochondrial Membrane.Helix insertion into bilayers and the evolution of membrane proteins.A dual-targeting, p53-independent, apoptosis-inducing platinum(II) anticancer complex, [Pt(BDI(QQ))]Cl.Mitochondrial ion channels as therapeutic targets.Bax forms an oligomer via separate, yet interdependent, surfaces.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

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P2860

Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis.

http://www.wikidata.org/entity/Q33854131

description

2005 nî lūn-bûn

@nan

2005 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի մայիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Bax forms multispanning monome ...... ze membranes during apoptosis.

@ast

Bax forms multispanning monome ...... ze membranes during apoptosis.

@en

type

label

Bax forms multispanning monome ...... ze membranes during apoptosis.

@ast

Bax forms multispanning monome ...... ze membranes during apoptosis.

@en

prefLabel

Bax forms multispanning monome ...... ze membranes during apoptosis.

@ast

Bax forms multispanning monome ...... ze membranes during apoptosis.

@en

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P356

SJ.EMBOJ.7600675

P1433

The EMBO Journal

P1476

Bax forms multispanning monome ...... ze membranes during apoptosis.

@en

P2093

Brian Leber

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

Jorge A Cruz-Aguado

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

Matthew G Annis

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

Paulina J Dlugosz

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

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

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

Movement of Bax from the cytosol to mitochondria during apoptosis

Structure of Bax: coregulation of dimer formation and intracellular localization

Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis

Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane

Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis

Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane

Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes.

P304

2096-2103

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scholarly article

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10.1038/SJ.EMBOJ.7600675

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12

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24

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David W Andrews

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2005-05-26T00:00:00Z

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P5875

7822293

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15920484

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P932

1150878

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