tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
about
Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1.tBid undergoes multiple conformational changes at the membrane required for Bax activationIdentification 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.Heterodimerization of BAK and MCL-1 activated by detergent micellesBH3 domains other than Bim and Bid can directly activate Bax/BakIdentification of novel in vivo phosphorylation sites of the human proapoptotic protein BAD: pore-forming activity of BAD is regulated by phosphorylationMAP-1 is a mitochondrial effector of Bax.Mitochondrial carrier homolog 2 is a target of tBID in cells signaled to die by tumor necrosis factor alpha.Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis.Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosisActivation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix.The Bax subfamily of Bcl2-related proteins is essential for apoptotic signal transduction by c-Jun NH(2)-terminal kinaseHexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondriaMitochondrial potassium channel Kv1.3 mediates Bax-induced apoptosis in lymphocytesProapoptotic 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 pathwayOnto better TRAILs for cancer treatmentCathepsin B is a New Drug Target for Traumatic Brain Injury Therapeutics: Evidence for E64d as a Promising Lead Drug CandidateThe role of BH3-mimetic drugs in the treatment of pediatric hepatoblastomaBAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial poreThe role of VDAC in cell death: friend or foe?Bim and Bmf synergize to induce apoptosis in Neisseria gonorrhoeae infectionBH3 peptides induce mitochondrial fission and cell death independent of BAX/BAKApoptotic Regulation by MCL-1 through HeterodimerizationBID-induced structural changes in BAK promote apoptosisEssential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cellsBioactive lipids and the control of Bax pro-apoptotic activityThe OPA1-dependent mitochondrial cristae remodeling pathway controls atrophic, apoptotic, and ischemic tissue damageBuilding blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosisProapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and deathDamage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate.The structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes.Mitochondria: diversity in the regulation of the NLRP3 inflammasome.Potential therapeutic approaches for modulating expression and accumulation of defective lamin A in laminopathies and age-related diseasesThe Effect of Growth Hormone Administration on the Regulation of Mitochondrial Apoptosis in-VivoCIL-102-Induced Cell Cycle Arrest and Apoptosis in Colorectal Cancer Cells via Upregulation of p21 and GADD45Up-regulation of Mcl-1 and Bak by coronavirus infection of human, avian and animal cells modulates apoptosis and viral replication
P2860
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P248
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P2860
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
description
2000 nî lūn-bûn
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2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2000 թվականի օգոստոսին հրատարակված գիտական հոդված
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2000年の論文
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2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年学术文章
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name
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@ast
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@en
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@en-gb
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@nl
type
label
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@ast
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@en
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@en-gb
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@nl
prefLabel
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@ast
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@en
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@en-gb
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@nl
P2093
P2860
P921
P3181
P1433
P1476
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
@en
P2093
C B Thompson
S J Korsmeyer
T Lindsten
V K Mootha
P2860
P304
P3181
P407
P577
2000-08-15T00:00:00Z