Movement of Bax from the cytosol to mitochondria during apoptosis - Wikidata - awgldk - TriplyDB

Movement of Bax from the cytosol to mitochondria during apoptosis

Movement of Bax from the cytosol to mitochondria during apoptosis

http://www.wikidata.org/entity/Q24677881

about

Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins.Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria Cerium oxide nanoparticles attenuate monocrotaline induced right ventricular hypertrophy following pulmonary arterial hypertension tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c Bcl-G, a novel pro-apoptotic member of the Bcl-2 family Bcl-2 family interaction with the mitochondrial morphogenesis machinery Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast Humanin peptide suppresses apoptosis by interfering with Bax activation Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.BH3 domains other than Bim and Bid can directly activate Bax/Bak Apoptosis repressor with caspase recruitment domain protects against cell death by interfering with Bax activation The tyrosine kinase Lck is a positive regulator of the mitochondrial apoptosis pathway by controlling Bak expression Interaction of pro-apoptotic protein HGTD-P with heat shock protein 90 is required for induction of mitochondrial apoptotic cascades MAP-1 is a mitochondrial effector of Bax.The permeability transition pore triggers Bax translocation to mitochondria during neuronal apoptosis Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis Conformation of the Bax C-terminus regulates subcellular location and cell death Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosis The bacterial redox protein azurin induces apoptosis in J774 macrophages through complex formation and stabilization of the tumor suppressor protein p53.Hsp27 as a negative regulator of cytochrome C release.Therapeutic efficacy of PUMA for malignant glioma cells regardless of p53 status.Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis G-CSF improves murine G6PC3-deficient neutrophil function by modulating apoptosis and energy homeostasis The Bcl-2 apoptotic switch in cancer development and therapy UXT (Ubiquitously Expressed Transcript) causes mitochondrial aggregation Insig2 is associated with colon tumorigenesis and inhibits Bax-mediated apoptosis Ceramide generated by sphingomyelin hydrolysis and the salvage pathway is involved in hypoxia/reoxygenation-induced Bax redistribution to mitochondria in NT-2 cells An internal EELD domain facilitates mitochondrial targeting of Mcl-1 via a Tom70-dependent pathway Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity Endophilin B1 is required for the maintenance of mitochondrial morphology Regulation of Bim in Health and Disease BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore Integration and oligomerization of Bax protein in lipid bilayers characterized by single molecule fluorescence study BAX activation is initiated at a novel interaction site Small molecule induced reactivation of mutant p53 in cancer cells Growth Arrest-Specific 6 (GAS6) Promotes Prostate Cancer Survival by G1 Arrest/S Phase Delay and Inhibition of Apoptosis During Chemotherapy in Bone Marrow

P2860

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P2860

Movement of Bax from the cytosol to mitochondria during apoptosis

http://www.wikidata.org/entity/Q24677881

description

1997 nî lūn-bûn

@nan

1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

1997年の論文

@ja

1997年論文

@yue

1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

name

Movement of Bax from the cytosol to mitochondria during apoptosis

@ast

Movement of Bax from the cytosol to mitochondria during apoptosis

@en

Movement of Bax from the cytosol to mitochondria during apoptosis

@nl

type

label

Movement of Bax from the cytosol to mitochondria during apoptosis

@ast

Movement of Bax from the cytosol to mitochondria during apoptosis

@en

Movement of Bax from the cytosol to mitochondria during apoptosis

@nl

prefLabel

Movement of Bax from the cytosol to mitochondria during apoptosis

@ast

Movement of Bax from the cytosol to mitochondria during apoptosis

@en

Movement of Bax from the cytosol to mitochondria during apoptosis

@nl

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P1433

Journal of Cell Biology

P1476

Movement of Bax from the cytosol to mitochondria during apoptosis

@en

P2093

A Nechushtan

http://www.w3.org/2001/XMLSchema#string

C L Smith

http://www.w3.org/2001/XMLSchema#string

K G Wolter

http://www.w3.org/2001/XMLSchema#string

R J Youle

http://www.w3.org/2001/XMLSchema#string

X G Xi

http://www.w3.org/2001/XMLSchema#string

Y T Hsu

http://www.w3.org/2001/XMLSchema#string

P2860

Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c

Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death

Overexpressed full-length human BCL2 extends the survival of baculovirus-infected Sf9 insect cells

Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes

Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis

Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

Bax-deficient mice with lymphoid hyperplasia and male germ cell death

BAX is required for neuronal death after trophic factor deprivation and during development

bcl-XL is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria

FACS-optimized mutants of the green fluorescent protein (GFP)

P304

1281-92

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scholarly article

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1412816

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P356

10.1083/JCB.139.5.1281

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5

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P478

139

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P577

1997-12-01T00:00:00Z

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P698

9382873

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P921

apoptotic process

P932

2140220

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