Bid, but not Bax, regulates VDAC channels. - Wikidata - wikimedia - TriplyDB

Bid, but not Bax, regulates VDAC channels.

Bid, but not Bax, regulates VDAC channels.

http://www.wikidata.org/entity/Q53849605

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Charged residues distribution modulates selectivity of the open state of human isoforms of the voltage dependent anion-selective channel Nek1 regulates cell death and mitochondrial membrane permeability through phosphorylation of VDAC1 Regulation of mitochondrial function by voltage dependent anion channels in ethanol metabolism and the Warburg effect Mitochondria and the autophagy-inflammation-cell death axis in organismal aging The role of VDAC in cell death: friend or foe?Mitochondria in traumatic brain injury and mitochondrial-targeted multipotential therapeutic strategies Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles The proapoptotic protein BNIP3 interacts with VDAC to induce mitochondrial release of endonuclease G Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death Lytic and non-lytic permeabilization of cardiolipin-containing lipid bilayers induced by cytochrome C Mitochondrial adenine nucleotide transport and cardioprotection The evolutionary history of mitochondrial porins.Bid-induced mitochondrial membrane permeabilization waves propagated by local reactive oxygen species (ROS) signaling.Bax-dependent regulation of Bak by voltage-dependent anion channel 2.HIV-1 Vpr-induced apoptosis is cell cycle dependent and requires Bax but not ANT A novel inhibitory mechanism of mitochondrion-dependent apoptosis by a herpesviral protein.Voltage-dependent anion channel (VDAC) is involved in apoptosis of cell lines carrying the mitochondrial DNA mutation.Facilitation of mitochondrial outer and inner membrane permeabilization and cell death in oxidative stress by a novel Bcl-2 homology 3 domain protein.Origami in outer membrane mimetics: correlating the first detailed images of refolded VDAC with over 20 years of biochemical data.Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity.Mitochondrial VDAC1: A Key Gatekeeper as Potential Therapeutic Target Computational investigation of cholesterol binding sites on mitochondrial VDAC.Critical role for voltage-dependent anion channel 2 in infectious bursal disease virus-induced apoptosis in host cells via interaction with VP5 Inhibition of Bak activation by VDAC2 is dependent on the Bak transmembrane anchor Oligomerization of the mitochondrial protein voltage-dependent anion channel is coupled to the induction of apoptosis Free tubulin modulates mitochondrial membrane potential in cancer cells.Bax channel inhibitors prevent mitochondrion-mediated apoptosis and protect neurons in a model of global brain ischemia.A pharmacologic target of G3139 in melanoma cells may be the mitochondrial VDAC.Is mPTP the gatekeeper for necrosis, apoptosis, or both?BID is a critical factor controlling cell viability regulated by IFN-α.Adult neuron survival strategies--slamming on the brakes.Bcl-2 family in inter-organelle modulation of calcium signaling; roles in bioenergetics and cell survival.Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein The therapeutic potential of mitochondrial channels in cancer, ischemia-reperfusion injury, and neurodegeneration.Warburg revisited: regulation of mitochondrial metabolism by voltage-dependent anion channels in cancer cells.BCL2 family of apoptosis-related genes: functions and clinical implications in cancer.Sphingosine forms channels in membranes that differ greatly from those formed by ceramide.VDAC1: from structure to cancer therapy.Is the mitochondrial outermembrane protein VDAC1 therapeutic target for Alzheimer's disease?Proapoptotic multidomain Bcl-2/Bax-family proteins: mechanisms, physiological roles, and therapeutic opportunities.

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P2860

Bid, but not Bax, regulates VDAC channels.

http://www.wikidata.org/entity/Q53849605

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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name

Bid, but not Bax, regulates VDAC channels.

@en

Bid, but not Bax, regulates VDAC channels.

@nl

type

label

Bid, but not Bax, regulates VDAC channels.

@en

Bid, but not Bax, regulates VDAC channels.

@nl

prefLabel

Bid, but not Bax, regulates VDAC channels.

@en

Bid, but not Bax, regulates VDAC channels.

@nl

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P1433

Journal of Biological Chemistry

P1476

Bid, but not Bax, regulates VDAC channels.

@en

P2093

Bruno Antonsson

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

Marco Colombini

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

Motoshi Suzuki

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

Richard J Youle

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

Sergey M Bezrukov

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

Tatiana K Rostovtseva

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

P2860

Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria

Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis

Inhibition of Bax channel-forming activity by Bcl-2

BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death

Solution structure of BID, an intracellular amplifier of apoptotic signaling

Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists

Structure of Bax: coregulation of dimer formation and intracellular localization

Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition

Two pathways for tBID-induced cytochrome c release from rat brain mitochondria: BAK- versus BAX-dependence

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13575-13583

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10.1074/JBC.M310593200

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14

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279

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14729675

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