The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA.
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Heterodimerization of BAK and MCL-1 activated by detergent micellesThe vaccinia virus protein F1L interacts with Bim and inhibits activation of the pro-apoptotic protein BaxPUMA Dissociates Bax and Bcl-X(L) to induce apoptosis in colon cancer cellsVaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligandsMutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosisMcl-1(128-350) fragment induces apoptosis through direct interaction with BaxMAP-1 is a mitochondrial effector of Bax.The Bcl-2 apoptotic switch in cancer development and therapyPhosphorylation of Puma modulates its apoptotic function by regulating protein stabilityPUMA, a potent killer with or without p53BH3 mimetics to improve cancer therapy; mechanisms and examplesBH3 profiling--measuring integrated function of the mitochondrial apoptotic pathway to predict cell fate decisionsBim and Bmf synergize to induce apoptosis in Neisseria gonorrhoeae infectionEvidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAXStructural Basis for Apoptosis Inhibition by Epstein-Barr Virus BHRF1Structural Insights of tBid, the Caspase-8-activated Bid, and Its BH3 DomainBuilding blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosisBid participates in genotoxic drug-induced apoptosis of HeLa cells and is essential for death receptor ligands' apoptotic and synergistic effectsp53 initiates apoptosis by transcriptionally targeting the antiapoptotic protein ARCDirect Activation of Bax Protein for Cancer TherapyAuto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2The N-terminus and alpha-5, alpha-6 helices of the pro-apoptotic protein Bax, modulate functional interactions with the anti-apoptotic protein Bcl-xL.Mcl-1 determines the Bax dependency of Nbk/Bik-induced apoptosis.Dynamical systems analysis of mitochondrial BAK activation kinetics predicts resistance to BH3 domains.Endogenous Bak inhibitors Mcl-1 and Bcl-xL: differential impact on TRAIL resistance in Bax-deficient carcinoma.Bax contains two functional mitochondrial targeting sequences and translocates to mitochondria in a conformational change- and homo-oligomerization-driven process.Cyanide-induced apoptosis of dopaminergic cells is promoted by BNIP3 and Bax modulation of endoplasmic reticulum-mitochondrial Ca2+ levels.Deletion of Puma protects hippocampal neurons in a model of severe status epilepticus.Bax forms an oligomer via separate, yet interdependent, surfaces.Akt-phosphorylated mitogen-activated kinase-activating death domain protein (MADD) inhibits TRAIL-induced apoptosis by blocking Fas-associated death domain (FADD) association with death receptor 4BH3-only proteins in apoptosis and beyond: an overview.Bcl-2 and Bax interact via the BH1-3 groove-BH3 motif interface and a novel interface involving the BH4 motifHuman herpesvirus 8 interferon regulatory factor-mediated BH3-only protein inhibition via Bid BH3-B mimicry.Androgen and its receptor promote Bax-mediated apoptosisPro-apoptotic Bax is the major and Bak an auxiliary effector in cytokine deprivation-induced mast cell apoptosisTOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax.Data-driven modeling of SRC control on the mitochondrial pathway of apoptosis: implication for anticancer therapy optimization.Levels of pro-apoptotic regulator Bad and anti-apoptotic regulator Bcl-xL determine the type of the apoptotic logic gate.Ceramide synthase-dependent ceramide generation and programmed cell death: involvement of salvage pathway in regulating postmitochondrial events.Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak-dependent apoptosis.
P2860
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P2860
The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
The first alpha helix of Bax p ...... H3-only proteins Bid and PUMA.
@en
type
label
The first alpha helix of Bax p ...... H3-only proteins Bid and PUMA.
@en
prefLabel
The first alpha helix of Bax p ...... H3-only proteins Bid and PUMA.
@en
P2093
P1433
P1476
The first alpha helix of Bax p ...... BH3-only proteins Bid and PUMA
@en
P2093
Fabien Gautier
Florence Manero
François M Vallette
Gwenola Bougras
Khaled Meflah
Patricia Vusio
Philippe Juin
Tristan Gallenne
P304
P356
10.1016/J.MOLCEL.2004.10.028
P577
2004-12-01T00:00:00Z