A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions
about
Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondriaBoo, a novel negative regulator of cell death, interacts with Apaf-1.Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins.ei24, a p53 response gene involved in growth suppression and apoptosisProapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4Bim: a novel member of the Bcl-2 family that promotes apoptosisActivation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix.Expression of bbc3, a pro-apoptotic BH3-only gene, is regulated by diverse cell death and survival signalsInduction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19KBok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family membersCell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosisA surface groove essential for viral Bcl-2 function during chronic infection in vivo.BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreAn African swine fever virus Bc1-2 homolog, 5-HL, suppresses apoptotic cell deathEvidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAXInduction 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.Characterization 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 mitochondriaBid induces the oligomerization and insertion of Bax into the outer mitochondrial membraneDNA IR-Double Strand Breaks (DSBs) and cellular response via ATMA functional gene discovery in the Fas-mediated pathway to apoptosis by analysis of transiently expressed randomized hybrid-ribozyme librariesFunctional proteomic analysis reveals the involvement of KIAA1199 in breast cancer growth, motility and invasiveness.New targets for the treatment of follicular lymphoma.BclxL changes conformation upon binding to wild-type but not mutant p53 DNA binding domain.Antiapoptotic herpesvirus Bcl-2 homologs escape caspase-mediated conversion to proapoptotic proteins.Bax-mediated cell death by the Gax homeoprotein requires mitogen activation but is independent of cell cycle activityThe US3 protein kinase of herpes simplex virus 1 mediates the posttranslational modification of BAD and prevents BAD-induced programmed cell death in the absence of other viral proteins.Strategies for manipulating the p53 pathway in the treatment of human cancer.BH3-only proteins in apoptosis and beyond: an overview.BIK, the founding member of the BH3-only family proteins: mechanisms of cell death and role in cancer and pathogenic processes.Mitochondria-specific transgenic overexpression of connexin-43 simulates preconditioning-induced cytoprotection of stem cellsThe herpes simplex virus 1 US3 protein kinase blocks caspase-dependent double cleavage and activation of the proapoptotic protein BADExpression of Bcl-2 family member Bid in normal and malignant tissues.Bcl-2 is a monomeric protein: prevention of homodimerization by structural constraints.BAX supports the mitochondrial network, promoting bioenergetics in nonapoptotic cellsNovel mechanism of anti-apoptotic function of 78-kDa glucose-regulated protein (GRP78): endocrine resistance factor in breast cancer, through release of B-cell lymphoma 2 (BCL-2) from BCL-2-interacting killer (BIK).Attenuation of nonsense-mediated mRNA decay facilitates the response to chemotherapeutics.Modulation of cell death by Bcl-XL through caspase interaction.
P2860
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P2860
A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions
description
1995 nî lūn-bûn
@nan
1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
A conserved domain in Bak, dis ...... and protein binding functions
@ast
A conserved domain in Bak, dis ...... and protein binding functions
@en
A conserved domain in Bak, dis ...... and protein binding functions
@nl
type
label
A conserved domain in Bak, dis ...... and protein binding functions
@ast
A conserved domain in Bak, dis ...... and protein binding functions
@en
A conserved domain in Bak, dis ...... and protein binding functions
@nl
prefLabel
A conserved domain in Bak, dis ...... and protein binding functions
@ast
A conserved domain in Bak, dis ...... and protein binding functions
@en
A conserved domain in Bak, dis ...... and protein binding functions
@nl
P2093
P2860
P3181
P1433
P1476
A conserved domain in Bak, dis ...... and protein binding functions
@en
P2093
A B Houghton
B Elangovan
C Flemington
G Chinnadurai
T Chittenden
P2860
P304
P3181
P407
P577
1995-11-15T00:00:00Z