Evidence for alpha-helical conformation of an essential N-terminal region in the human Bcl2 protein.
about
The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4Molecular basis of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2The structure and interactions of the proline-rich domain of ASPP2BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell deathCrystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein familyStudying protein-protein interactions using peptide arrays.The anti-apoptosis function of Bcl-2 can be genetically separated from its inhibitory effect on cell cycle entryPeptides in apoptosis research.Alpha-helical destabilization of the Bcl-2-BH4-domain peptide abolishes its ability to inhibit the IP3 receptor.Involvement of BH4 domain of bcl-2 in the regulation of HIF-1-mediated VEGF expression in hypoxic tumor cells.Selective regulation of IP3-receptor-mediated Ca2+ signaling and apoptosis by the BH4 domain of Bcl-2 versus Bcl-Xl.Targeting Bcl-2 based on the interaction of its BH4 domain with the inositol 1,4,5-trisphosphate receptor.Using peptides to study protein-protein interactions.Interactions of HIV-1 proteins as targets for developing anti-HIV-1 peptides.BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo.Deletion of the BH1 domain of Bcl-2 accelerates apoptosis by acting in a dominant negative fashion.NH2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis.Inhibition of Pro-apoptotic BAX by a noncanonical interaction mechanism.Evidence for crucial electrostatic interactions between Bcl-2 homology domains BH3 and BH4 in the anti-apoptotic Nr-13 protein.The study of cell-death proteins in the outer mitochondrial membrane by chemical cross-linking.NMR determination that an extended BH3 motif of pro-apoptotic BID is specifically bound to BCL-XL.Effects of microinjection of synthetic Bcl-2 domain peptides on apoptosis of renal tubular epithelial cells.A double point mutation at residues Ile14 and Val15 of Bcl-2 uncovers a role for the BH4 domain in both protein stability and function.B cell lymphoma 2 (Bcl-2) residues essential for Bcl-2's apoptosis-inducing interaction with Nur77/Nor-1 orphan steroid receptors.CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.The BH4 domain of Bcl-XL rescues astrocyte degeneration in amyotrophic lateral sclerosis by modulating intracellular calcium signals
P2860
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P2860
Evidence for alpha-helical conformation of an essential N-terminal region in the human Bcl2 protein.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh-hant
name
Evidence for alpha-helical con ...... ion in the human Bcl2 protein.
@en
Evidence for alpha-helical con ...... ion in the human Bcl2 protein.
@nl
type
label
Evidence for alpha-helical con ...... ion in the human Bcl2 protein.
@en
Evidence for alpha-helical con ...... ion in the human Bcl2 protein.
@nl
prefLabel
Evidence for alpha-helical con ...... ion in the human Bcl2 protein.
@en
Evidence for alpha-helical con ...... ion in the human Bcl2 protein.
@nl
P2093
P2860
P356
P1476
Evidence for alpha-helical con ...... ion in the human Bcl2 protein.
@en
P2093
P2860
P304
23284-23288
P356
10.1074/JBC.271.38.23284
P407
P577
1996-09-01T00:00:00Z