Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death (Q28242653)

GOA release 2020-03-11

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1 reference

Roberta A Gottlieb

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Jeffery D. Molkentin

object named as

Jeffery D Molkentin

12

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author name string

Christopher P Baines

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Robert A Kaiser

2

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Nicole H Purcell

3

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N Scott Blair

4

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Hanna Osinska

5

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Michael A Hambleton

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Eric W Brunskill

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M Richard Sayen

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Gerald W Dorn

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Jeffrey Robbins

The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore

11

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language of work or name

English

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publication date

31 March 2005

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published in

Nature

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volume

434

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issue

7033

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page(s)

658-62

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cites work

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Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis

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

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Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization

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A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis

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The permeability transition pore complex: another view.

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On the involvement of mitochondrial intermembrane junctional complexes in apoptosis

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Mitochondrial permeability: dual role for the ADP/ATP translocator?

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Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function?

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Bid acts on the permeability transition pore complex to induce apoptosis

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The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition

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Bax-induced cytochrome C release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions

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Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release

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Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization.

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Protection by Cyclosporin A of ischemia/reperfusion-induced damage in isolated rat hearts.

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Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A.

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Cardiomyocyte apoptosis induced by Galphaq signaling is mediated by permeability transition pore formation and activation of the mitochondrial death pathway.

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Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion

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Contribution of the mitochondrial permeability transition to lethal injury after exposure of hepatocytes to t-butylhydroperoxide

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Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis

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Targeted inhibition of p38 mitogen-activated protein kinase antagonizes cardiac injury and cell death following ischemia-reperfusion in vivo

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Isolation and subfractionation of mitochondria from animal cells and tissue culture lines

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The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ

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A binary adenoviral vector system for expressing high levels of the proapoptotic gene bax.

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