Distinct domains control the addressing and the insertion of Bax into mitochondria.
about
The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeastThe vaccinia virus protein F1L interacts with Bim and inhibits activation of the pro-apoptotic protein BaxBAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreTCTP protects from apoptotic cell death by antagonizing bax functionDirect Activation of Bax Protein for Cancer TherapyAuto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2Modulation of Nr-13 antideath activity by peptide aptamers.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.Bim, Bak, and Bax regulate osteoblast survival.GSK3beta promotes apoptosis after renal ischemic injury.Bax forms an oligomer via separate, yet interdependent, surfaces.TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax.BimS-induced apoptosis requires mitochondrial localization but not interaction with anti-apoptotic Bcl-2 proteins.Bax-derived membrane-active peptides act as potent and direct inducers of apoptosis in cancer cells.BaxΔ2 is a novel bax isoform unique to microsatellite unstable tumorsEmbedded together: the life and death consequences of interaction of the Bcl-2 family with membranes.Conformational Heterogeneity of Bax Helix 9 Dimer for Apoptotic Pore FormationBax activation by the BH3-only protein Puma promotes cell dependence on antiapoptotic Bcl-2 family membersThe fowlpox virus BCL-2 homologue, FPV039, interacts with activated Bax and a discrete subset of BH3-only proteins to inhibit apoptosis.Bid: a Bax-like BH3 protein.Evaluation of Bax and Bak gene mutations and expression in breast cancer.Death upon a kiss: mitochondrial outer membrane composition and organelle communication govern sensitivity to BAK/BAX-dependent apoptosis.Systemic Delivery of Tumor-Targeted Bax-Derived Membrane-Active Peptides for the Treatment of Melanoma Tumors in a Humanized SCID Mouse Model.The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activationBax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms.Control of Bax homodimerization by its carboxyl terminus.Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex.Lysosomal membrane permeabilization during apoptosis--involvement of Bax?Cholesterol effects on BAX pore activation.Substitutions of potentially phosphorylatable serine residues of Bax reveal how they may regulate its interaction with mitochondria.BaxΔ2 sensitizes colorectal cancer cells to proteasome inhibitor-induced cell death.The functional domains for Bax∆2 aggregate-mediated caspase 8-dependent cell death.Evaluation of the roles of apoptosis, autophagy, and mitophagy in the loss of plating efficiency induced by Bax expression in yeast.JNK3 phosphorylates Bax protein and induces ability to form pore on bilayer lipid membrane.Suppression of AURKA alleviates p27 inhibition on Bax cleavage and induces more intensive apoptosis in gastric cancer.
P2860
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P2860
Distinct domains control the addressing and the insertion of Bax into mitochondria.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
Distinct domains control the addressing and the insertion of Bax into mitochondria.
@en
Distinct domains control the addressing and the insertion of Bax into mitochondria.
@nl
type
label
Distinct domains control the addressing and the insertion of Bax into mitochondria.
@en
Distinct domains control the addressing and the insertion of Bax into mitochondria.
@nl
prefLabel
Distinct domains control the addressing and the insertion of Bax into mitochondria.
@en
Distinct domains control the addressing and the insertion of Bax into mitochondria.
@nl
P2093
P2860
P356
P1476
Distinct domains control the addressing and the insertion of Bax into mitochondria
@en
P2093
François M Vallette
Hubert Arokium
Khaled Meflah
Stephen Manon
P2860
P304
10587-10598
P356
10.1074/JBC.M409714200
P407
P577
2004-12-07T00:00:00Z