Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
about
Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repairBax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondriaMAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domainsBcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimersIdentification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosisBcl-x(L) retrotranslocates Bax from the mitochondria into the cytosolProapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activationUV irradiation resistance-associated gene suppresses apoptosis by interfering with BAX activationHeterodimerization of BAK and MCL-1 activated by detergent micellesASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathwayQuantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosisThe vaccinia virus protein F1L interacts with Bim and inhibits activation of the pro-apoptotic protein BaxFas-mediated apoptosis is regulated by the extracellular matrix protein CCN1 (CYR61) in vitro and in vivoClusterin inhibits apoptosis by interacting with activated BaxMutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosisSpatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosisPP2A regulates BCL-2 phosphorylation and proteasome-mediated degradation at the endoplasmic reticulumSmall-Molecule Bcl2 BH4 Antagonist for Lung Cancer TherapyOligomeric Bax is a component of the putative cytochrome c release channel MAC, mitochondrial apoptosis-induced channelConformation of the Bax C-terminus regulates subcellular location and cell deathLoss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosisGrowth factors can influence cell growth and survival through effects on glucose metabolismThe Bcl-2 apoptotic switch in cancer development and therapyInsig2 is associated with colon tumorigenesis and inhibits Bax-mediated apoptosisCeramide generated by sphingomyelin hydrolysis and the salvage pathway is involved in hypoxia/reoxygenation-induced Bax redistribution to mitochondria in NT-2 cellsAn internal EELD domain facilitates mitochondrial targeting of Mcl-1 via a Tom70-dependent pathwayProapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activityInduction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathwayBAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreThe role of VDAC in cell death: friend or foe?Integration and oligomerization of Bax protein in lipid bilayers characterized by single molecule fluorescence studyEvidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAXMolecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with BaxProtein kinase Cepsilon interacts with Bax and promotes survival of human prostate cancer cellsBuilding blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosisDamage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate.Mono- or double-site phosphorylation distinctly regulates the proapoptotic function of Bax2,2'-diphenyl-3,3'-diindolylmethane: a potent compound induces apoptosis in breast cancer cells by inhibiting EGFR pathwayConstitutive association of the proapoptotic protein Bim with Bcl-2-related proteins on mitochondria in T cells
P2860
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P2860
Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
description
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1998
@ast
im April 1998 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1998/04/24)
@sk
vědecký článek publikovaný v roce 1998
@cs
wetenschappelijk artikel (gepubliceerd op 1998/04/24)
@nl
наукова стаття, опублікована у квітні 1998
@uk
name
Bax in murine thymus is a solu ...... etergent-induced conformations
@ast
Bax in murine thymus is a solu ...... etergent-induced conformations
@en
Bax in murine thymus is a solu ...... etergent-induced conformations
@nl
type
label
Bax in murine thymus is a solu ...... etergent-induced conformations
@ast
Bax in murine thymus is a solu ...... etergent-induced conformations
@en
Bax in murine thymus is a solu ...... etergent-induced conformations
@nl
prefLabel
Bax in murine thymus is a solu ...... etergent-induced conformations
@ast
Bax in murine thymus is a solu ...... etergent-induced conformations
@en
Bax in murine thymus is a solu ...... etergent-induced conformations
@nl
P3181
P356
P1476
Bax in murine thymus is a solu ...... etergent-induced conformations
@en
P2093
R. J. Youle
P304
10777–10783
P3181
P356
10.1074/JBC.273.17.10777
P407
P577
1998-04-24T00:00:00Z