Activation of mitochondrial voltage-dependent anion channel by apro-apoptotic BH3-only protein Bim (Q28214708)

2

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Yosuke Matsuoka

3

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Yoshihiro Yoneda

4

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Yoshihide Tsujimoto

The Bcl-2 protein family: arbiters of cell survival

5

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language of work or name

English

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publication date

25 July 2002

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published in

Oncogene

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volume

21

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issue

32

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page(s)

4944-56

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cites work

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Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases

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Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity

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BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis

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A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues

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

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Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane

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Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL.

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Kinetic and mechanistic studies of prolyl oligopeptidase from the hyperthermophile Pyrococcus furiosus

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The biochemistry of apoptosis

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A monoclonal antibody to the COOH-terminal acidic portion of Ran inhibits both the recycling of Ran and nuclear protein import in living cells

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Programmed cell death in animal development

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Bax directly induces release of cytochrome c from isolated mitochondria

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The pro-apoptotic proteins, Bid and Bax, cause a limited permeabilization of the mitochondrial outer membrane that is enhanced by cytosol

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VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release

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Release of cytochrome c and decrease of cytochrome c oxidase in Bax-expressing yeast cells, and prevention of these effects by coexpression of Bcl-xL

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Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier

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Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria

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Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, and cyclosporin A-sensitive channel.

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Efficient selection for high-expression transfectants with a novel eukaryotic vector

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The proapoptotic BH3-only protein bim is expressed in hematopoietic, epithelial, neuronal, and germ cells

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Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore

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A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast

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Investigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirement

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The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex

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BAX-dependent transport of cytochrome c reconstituted in pure liposomes

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

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

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Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c.

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Bax and Bcl-xL independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator

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Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells

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Caspases: enemies within

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Bcl-2 family: life-or-death switch

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VDAC regulation by the Bcl-2 family of proteins

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Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death

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BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak

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7 January 2021

The mitochondrial permeability transition.

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