Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
about
Boo, a novel negative regulator of cell death, interacts with Apaf-1.MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domainsThe conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteinsA common binding site mediates heterodimerization and homodimerization of Bcl-2 family membersharakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L)Bim: a novel member of the Bcl-2 family that promotes apoptosisEnforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosisConformation of the Bax C-terminus regulates subcellular location and cell deathCell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosisRegulated necrotic cell death: the passive aggressive side of Bax and BakEvidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAXCrystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein familyAPOL1 toxin, innate immunity, and kidney injuryHuman homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosisMolecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with BaxBH3 domain of BAD is required for heterodimerization with BCL-XL and pro-apoptotic activityBlk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonistBuilding blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosisInduction of apoptosis in prostate carcinoma cells by BH3 peptides which inhibit Bak/Bcl-2 interactionsThe structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes.Flow cytometric analysis of BDE 47 mediated injury to rainbow trout gill epithelial cellsMtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-XLProapoptotic activity of ITM2B(s), a BH3-only protein induced upon IL-2-deprivation which interacts with Bcl-2Bax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membraneBax directly induces release of cytochrome c from isolated mitochondriaApoptosis and the airway epitheliumDirect Activation of Bax Protein for Cancer TherapyRecent advances in the development of anticancer agents targeting cell death inhibitors in the Bcl-2 protein family.Screening for novel protein targets of indomethacin in HCT116 human colon cancer cells using proteomicsResistance to induced apoptosis in the human neuroblastoma cell line SK-N-SH in relation to neuronal differentiation. Role of Bcl-2 protein family.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.Role of the Bcl-2 gene family in prostate cancer progression and its implications for therapeutic intervention.Apoptosis and its clinical significance for bladder cancer therapy.Control of cell cycle entry and apoptosis in B lymphocytes infected by Epstein-Barr virus.Mst1 promotes cardiac myocyte apoptosis through phosphorylation and inhibition of Bcl-xLE1B 19K blocks Bax oligomerization and tumor necrosis factor alpha-mediated apoptosis.Bax forms an oligomer via separate, yet interdependent, surfaces.Apoptosis and predisposition to oral cancer.
P2860
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P2860
Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
description
1996 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1996
@ast
im März 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1996/03/29)
@sk
vědecký článek publikovaný v roce 1996
@cs
wetenschappelijk artikel (gepubliceerd op 1996/03/29)
@nl
наукова стаття, опублікована в березні 1996
@uk
name
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@ast
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@en
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@nl
type
label
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@ast
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@en
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@nl
prefLabel
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@ast
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@en
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@nl
P2093
P3181
P356
P1476
Proapoptotic protein Bax heter ...... BH3) distinct from BH1 and BH2
@en
P2093
P304
P3181
P356
10.1074/JBC.271.13.7440
P407
P577
1996-03-29T00:00:00Z