Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. - Wikidata - awgldk - TriplyDB

Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis.

Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis.

http://www.wikidata.org/entity/Q38326924

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Use of human cancer cell lines mitochondria to explore the mechanisms of BH3 peptides and ABT-737-induced mitochondrial membrane permeabilization Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria NF-kappa B inhibition causes spontaneous apoptosis in Epstein-Barr virus-transformed lymphoblastoid cells tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence 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 Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts as a functional link coupling mitotic arrest and apoptosis The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis MAP-1 is a mitochondrial effector of Bax.Oligomeric Bax is a component of the putative cytochrome c release channel MAC, mitochondrial apoptosis-induced channel 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.Hsp27 as a negative regulator of cytochrome C release.The Bax subfamily of Bcl2-related proteins is essential for apoptotic signal transduction by c-Jun NH(2)-terminal kinase Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper Caspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis Ceramide generated by sphingomyelin hydrolysis and the salvage pathway is involved in hypoxia/reoxygenation-induced Bax redistribution to mitochondria in NT-2 cells NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-kappaB and JNK pathways by inducing reactive oxygen species production Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein rR and Bcl-2 Gene expression during ER stress-induced apoptosis in neurons: induction of the BH3-only protein Bbc3/PUMA and activation of the mitochondrial apoptosis pathway Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway Xanthurenic acid translocates proapoptotic Bcl-2 family proteins into mitochondria and impairs mitochondrial function Marine Drugs Regulating Apoptosis Induced by Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL)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 Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA BH3-only proteins: a 20-year stock-take Putting the pieces together: How is the mitochondrial pathway of apoptosis regulated in cancer and chemotherapy?Aspirin induces apoptosis through release of cytochrome c from mitochondria Role of mitochondria in aspirin-induced apoptosis in human gastric epithelial cells

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Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis.

http://www.wikidata.org/entity/Q38326924

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1999 nî lūn-bûn

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1999年の論文

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1999年学术文章

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1999年学术文章

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1999年学术文章

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Bid-induced conformational cha ...... me c release during apoptosis.

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Bid-induced conformational cha ...... me c release during apoptosis.

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Bid-induced conformational cha ...... me c release during apoptosis.

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Bid-induced conformational cha ...... me c release during apoptosis.

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P2093

Antonsson B

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

Desagher S

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Eskes R

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Lauper S

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Martinou JC

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Maundrell K

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Montessuit S

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Nichols A

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Osen-Sand A

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P2860

Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

Inhibition of Bax channel-forming activity by Bcl-2

Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked

BID: a novel BH3 domain-only death agonist

Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis

Multiple Bcl-2 family members demonstrate selective dimerizations with Bax

A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions

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

Movement of Bax from the cytosol to mitochondria during apoptosis

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891-901

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10.1083/JCB.144.5.891

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5

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144

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277431967

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10085289

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apoptotic process

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2148190

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