(Q28261309)

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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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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 (English)

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author name string

G Beutner

1

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A Rück

2

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B Riede

3

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D Brdiczka

4

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publication date

5 January 1998

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Biochimica et Biophysica Acta

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1368

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1

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7-18

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Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore

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Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane

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The mitochondrial permeability transition.

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The Ca2+-induced membrane transition in mitochondria. I. The protective mechanisms

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Mitochondrial control of nuclear apoptosis.

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Bcl-2 inhibits the mitochondrial release of an apoptogenic protease

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Inhibition of Ca2(+)-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adeni

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Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase

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Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2+

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Mitochondrial channel activity studied by patch-clamping mitoplasts

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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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Mitochondrial benzodiazepine receptor linked to inner membrane ion channels by nanomolar actions of ligands

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The influence of the cytosolic oncotic pressure on the permeability of the mitochondrial outer membrane for ADP: implications for the kinetic properties of mitochondrial creatine kinase and for ADP channelling into the intermembrane space.

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Macromolecules Increase the Channeling of ADP from Externally Associated Hexokinase to the Matrix of Mitochondria

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Complexes between hexokinase, mitochondrial porin and adenylate translocator in brain: regulation of hexokinase, oxidative phosphorylation and permeability transition pore

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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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Location and regulation of octameric mitochondrial creatine kinase in the contact sites

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cDNA cloning of rat mitochondrial cyclophilin.

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Chaotropic agents and increased matrix volume enhance binding of mitochondrial cyclophilin to the inner mitochondrial membrane and sensitize the mitochondrial permeability transition to [Ca2+]

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Inhibition of peptidyl-prolyl cis/trans isomerase activity by substrate analog structures: thioxo tetrapeptide-4-nitroanilides

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Kinetics of assembly and dissociation of the mitochondrial creatine kinase octamer. A fluorescence study

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Dimer-dimer interactions in octameric mitochondrial creatine kinase

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Adenine Nucleotide Translocation of Mitochondria. 1. Specificity and Control

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Effect of macromolecules on the structure of the mitochondrial inter-membrane space and the regulation of hexokinase

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Contact sites between mitochondrial envelope membranes. Structure and function in energy- and protein-transfer

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Only one of the two interconvertible forms of mitochondrial creatine kinase binds to heart mitoplasts

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The mitochondrial aspartate/glutamate and ADP/ATP carrier switch from obligate counterexchange to unidirectional transport after modification by SH-reagents

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Pore-like and carrier-like properties of the mitochondrial aspartate/glutamate carrier after modification by SH-reagents: evidence for a preformed channel as a structural requirement of carrier-mediated transport

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Interaction of mitochondrial porin with cytosolic proteins

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10.1016/S0005-2736(97)00175-2

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