Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.
about
Genome-wide prediction and validation of peptides that bind human prosurvival Bcl-2 proteinsGene expression profiling of monkeypox virus-infected cells reveals novel interfaces for host-virus interactionsTwo independent positive feedbacks and bistability in the Bcl-2 apoptotic switchUse of human cancer cell lines mitochondria to explore the mechanisms of BH3 peptides and ABT-737-induced mitochondrial membrane permeabilizationProteasome inhibitors induce apoptosis in human lung cancer cells through a positive feedback mechanism and the subsequent Mcl-1 protein cleavageTRAIL and proteasome inhibitors combination induces a robust apoptosis in human malignant pleural mesothelioma cells through Mcl-1 and Akt protein cleavagesBif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesisNoxa/Bcl-2 protein interactions contribute to bortezomib resistance in human lymphoid cellsBcl-x(L) retrotranslocates Bax from the mitochondria into the cytosolApoptosis induced by knockdown of uPAR and MMP-9 is mediated by inactivation of EGFR/STAT3 signaling in medulloblastomaHuman Bop is a novel BH3-only member of the Bcl-2 protein familyInteraction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosisHeterodimerization of BAK and MCL-1 activated by detergent micellesBH3 domains other than Bim and Bid can directly activate Bax/BakMcl-1 is critical for survival in a subgroup of non-small-cell lung cancer cell linesThe tyrosine kinase Lck is a positive regulator of the mitochondrial apoptosis pathway by controlling Bak expressionVaccinia 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 apoptosisThe Bcl-2 apoptotic switch in cancer development and therapySmall-molecule Bcl-2 antagonists as targeted therapy in oncologyAn internal EELD domain facilitates mitochondrial targeting of Mcl-1 via a Tom70-dependent pathwayInhibition of ubiquitin-mediated degradation of MOAP-1 by apoptotic stimuli promotes Bax function in mitochondriaTargeting Cell Survival Proteins for Cancer Cell DeathPotential of apoptotic pathway-targeted cancer therapeutic research: Where do we stand?Targeting BCL2-Proteins for the Treatment of Solid TumoursAnti-apoptotic BCL-2 family proteins in acute neural injuryThe BCL2 Family: Key Mediators of the Apoptotic Response to Targeted Anticancer TherapeuticsAnaplasma phagocytophilum Ats-1 is imported into host cell mitochondria and interferes with apoptosis inductionStructural insights into the degradation of Mcl-1 induced by BH3 domainsCrystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 familyA novel BH3 ligand that selectively targets Mcl-1 reveals that apoptosis can proceed without Mcl-1 degradationBAX activation is initiated at a novel interaction siteConformational Changes in Bcl-2 Pro-survival Proteins Determine Their Capacity to Bind LigandsMcl-1-Bim complexes accommodate surprising point mutations via minor structural changesDeterminants of BH3 Binding Specificity for Mcl-1 versus Bcl-xLApoptotic Regulation by MCL-1 through HeterodimerizationEvidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAXStructural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-Peptide Generated by Sequence-Based DesignEvaluation of Diverse α/β-Backbone Patterns for Functional α-Helix Mimicry: Analogues of the Bim BH3 DomainStructure-Guided Rational Design of α/β-Peptide Foldamers with High Affinity for BCL-2 Family Prosurvival Proteins
P2860
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P248
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P2860
Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.
description
2005 nî lūn-bûn
@nan
2005 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
Proapoptotic Bak is sequestere ...... displaced by BH3-only proteins
@nl
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@ast
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@en
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@en-gb
type
label
Proapoptotic Bak is sequestere ...... displaced by BH3-only proteins
@nl
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@ast
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@en
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@en-gb
prefLabel
Proapoptotic Bak is sequestere ...... displaced by BH3-only proteins
@nl
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@ast
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@en
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@en-gb
P2093
P2860
P921
P3181
P356
P1433
P1476
Proapoptotic Bak is sequestere ...... isplaced by BH3-only proteins.
@en
P2093
Andrew Wei
David C S Huang
Edwina Naik
Grant Dewson
Jamie I Fletcher
Jerry M Adams
Simon N Willis
P2860
P304
P3181
P356
10.1101/GAD.1304105
P407
P577
2005-05-18T00:00:00Z