Bax directly induces release of cytochrome c from isolated mitochondria
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Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondriaOrdering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent mannerBax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondriaThe HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition poreBAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteinsAdenovirus-mediated overexpression of p14(ARF) induces p53 and Bax-independent apoptosisHumanin peptide suppresses apoptosis by interfering with Bax activationApoptosis repressor with caspase recruitment domain protects against cell death by interfering with Bax activationIdentification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylationInhibition of mitochondrial neural cell death pathways by protein transduction of Bcl-2 family proteinsMAP-1 is a mitochondrial effector of Bax.The permeability transition pore triggers Bax translocation to mitochondria during neuronal apoptosisTherapeutic efficacy of PUMA for malignant glioma cells regardless of p53 status.Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlationMitochondrial release of caspase-2 and -9 during the apoptotic processBH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell deathProapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activityInduction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathwayEquine estrogens differentially inhibit DNA fragmentation induced by glutamate in neuronal cells by modulation of regulatory proteins involved in programmed cell deathGlutamate-induced apoptosis in primary cortical neurons is inhibited by equine estrogens via down-regulation of caspase-3 and prevention of mitochondrial cytochrome c releaseMolecular and cellular mechanisms of cardiotoxicity.BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreA review of ceramide analogs as potential anticancer agentsAnticancer Effect of Lycopene in Gastric CarcinogenesisBH3-only proteins: a 20-year stock-takeInvestigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirementInteraction of Alzheimer's presenilin-1 and presenilin-2 with Bcl-X(L). A potential role in modulating the threshold of cell deathAspirin induces apoptosis through release of cytochrome c from mitochondriaThe oat mitochondrial permeability transition and its implication in victorin binding and induced cell deathEssential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells14-3-3 Interacts directly with and negatively regulates pro-apoptotic BaxCaspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondriaSurvivin splice variants regulate the balance between proliferation and cell deathInduction of apoptosis in prostate carcinoma cells by BH3 peptides which inhibit Bak/Bcl-2 interactionsEffects and mechanisms of emodin on cell death in human lung squamous cell carcinomaSpatial and temporal changes in Bax subcellular localization during anoikisBax and Bak independently promote cytochrome C release from mitochondriaTemporal profiles of the subcellular localization of Bim, a BH3-only protein, during middle cerebral artery occlusion in miceBax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6Activation of pro-death Bcl-2 family proteins and mitochondria apoptosis pathway in tumor necrosis factor-alpha-induced liver injury
P2860
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P2860
Bax directly induces release of cytochrome c from isolated mitochondria
description
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
article publié dans les Procee ...... f the United States of America
@fr
artículu científicu espublizáu en 1998
@ast
im April 1998 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1998/04/28)
@sk
vědecký článek publikovaný v roce 1998
@cs
wetenschappelijk artikel (gepubliceerd op 1998/04/28)
@nl
наукова стаття, опублікована у квітні 1998
@uk
name
Bax directly induces release of cytochrome c from isolated mitochondria
@ast
Bax directly induces release of cytochrome c from isolated mitochondria
@en
Bax directly induces release of cytochrome c from isolated mitochondria
@nl
type
label
Bax directly induces release of cytochrome c from isolated mitochondria
@ast
Bax directly induces release of cytochrome c from isolated mitochondria
@en
Bax directly induces release of cytochrome c from isolated mitochondria
@nl
prefLabel
Bax directly induces release of cytochrome c from isolated mitochondria
@ast
Bax directly induces release of cytochrome c from isolated mitochondria
@en
Bax directly induces release of cytochrome c from isolated mitochondria
@nl
P2093
P2860
P921
P3181
P356
P1476
Bax directly induces release of cytochrome c from isolated mitochondria
@en
P2093
D. Bredesen
J. C. Reed
J. M. Jürgensmeier
L. Ellerby
Q. Deveraux
P2860
P304
P3181
P356
10.1073/PNAS.95.9.4997
P407
P577
1998-04-28T00:00:00Z