BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization. - Wikidata - awgldk - TriplyDB

BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization.

BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization.

http://www.wikidata.org/entity/Q42598140

about

Two independent positive feedbacks and bistability in the Bcl-2 apoptotic switch Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation BH3 domains other than Bim and Bid can directly activate Bax/Bak Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis.Regulated necrotic cell death: the passive aggressive side of Bax and Bak Infarct-induced steroidogenic acute regulatory protein: a survival role in cardiac fibroblasts Evaluating cytochrome c diffusion in the intermembrane spaces of mitochondria during cytochrome c release MTCH2/MIMP is a major facilitator of tBID recruitment to mitochondria Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2 Bcl-XL inhibits membrane permeabilization by competing with Bax.Dynamical systems analysis of mitochondrial BAK activation kinetics predicts resistance to BH3 domains.Pharmacologic inhibition of fatty acid oxidation sensitizes human leukemia cells to apoptosis induction Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis.Bax forms an oligomer via separate, yet interdependent, surfaces.Bcl-2 and Bax interact via the BH1-3 groove-BH3 motif interface and a novel interface involving the BH4 motif Inhibition of Bak activation by VDAC2 is dependent on the Bak transmembrane anchor Elucidating cytochrome C release from mitochondria: insights from an in silico three-dimensional model Mitochondrial DNA mutations may contribute to aging via cell death caused by peptides that induce cytochrome c release.Levels of pro-apoptotic regulator Bad and anti-apoptotic regulator Bcl-xL determine the type of the apoptotic logic gate.The Bcl-2 family: roles in cell survival and oncogenesis.Tailored fragments of roseophilin selectively antagonize Mcl-1 in vitro Obatoclax is a direct and potent antagonist of membrane-restricted Mcl-1 and is synthetic lethal with treatment that induces Bim.Key role for Bak activation and Bak-Bax interaction in the apoptotic response to vinblastine c-Myc primed mitochondria determine cellular sensitivity to TRAIL-induced apoptosis.Modeling of the role of a Bax-activation switch in the mitochondrial apoptosis decision Bcl-2 family in inter-organelle modulation of calcium signaling; roles in bioenergetics and cell survival.Bcl-xl does not have to bind Bax to protect T cells from death.Small molecule obatoclax (GX15-070) antagonizes MCL-1 and overcomes MCL-1-mediated resistance to apoptosis.Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax.Delivery of drugs and macromolecules to mitochondria.Oligomerization of BAK by p53 utilizes conserved residues of the p53 DNA binding domain Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes.Bid: a Bax-like BH3 protein.Apoptosis: it's BAK to VDAC.Controlling subcellular delivery to optimize therapeutic effect Programming cancer cells for high expression levels of Mcl1.Dissociation of Bak α1 helix from the core and latch domains is required for apoptosis.The ethyl acetate fraction of Sargassum muticum attenuates ultraviolet B radiation-induced apoptotic cell death via regulation of MAPK- and caspase-dependent signaling pathways in human HaCaT keratinocytes.The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation

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P2860

BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization.

http://www.wikidata.org/entity/Q42598140

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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name

BCL-2 selectively interacts wi ...... ting BAK auto-oligomerization.

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BCL-2 selectively interacts wi ...... ting BAK auto-oligomerization.

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type

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BCL-2 selectively interacts wi ...... ting BAK auto-oligomerization.

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BCL-2 selectively interacts wi ...... ting BAK auto-oligomerization.

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BCL-2 selectively interacts wi ...... ting BAK auto-oligomerization.

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Journal of Biological Chemistry

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BCL-2 selectively interacts wi ...... ting BAK auto-oligomerization.

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P2093

Gordon C Shore

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

Salvatore C Ruffolo

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P2860

PUMA, a novel proapoptotic gene, is induced by p53

Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K

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

Conformation of the Bax C-terminus regulates subcellular location and cell death

Caspase-resistant BAP31 inhibits fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria

Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis

Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol

Movement of Bax from the cytosol to mitochondria during apoptosis

Solution structure of BID, an intracellular amplifier of apoptotic signaling

P304

25039-25045

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scholarly article

P356

10.1074/JBC.M302930200

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P433

27

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278

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2003-04-29T00:00:00Z

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12721291

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