(Q51951248)

18 April 2018

title

Approaching the structure of human VDAC1, a key molecule in mitochondrial cross-talk. (English)

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18 April 2018

author name string

Kornelius Zeth

series ordinal

1

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18 April 2018

Thomas Meins

series ordinal

2

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18 April 2018

Clemens Vonrhein

series ordinal

3

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18 April 2018

publication date

1 June 2008

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18 April 2018

Journal of Bioenergetics and Biomembranes

published in

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18 April 2018

volume

40

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18 April 2018

issue

3

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18 April 2018

page(s)

127-132

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18 April 2018

https://scigraph.springernature.com/pub.10.1007/s10863-008-9144-z

exact match

0 references

cites work

The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition

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Crossref

https://api.crossref.org/works/10.1007%2FS10863-008-9144-Z

Bacterial expression and characterization of the mitochondrial outer membrane channel. Effects of n-terminal modifications

21 January 2018

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12 December 2020

Fluoxetine (Prozac) interaction with the mitochondrial voltage-dependent anion channel and protection against apoptotic cell death

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Bid, but not Bax, regulates VDAC channels.

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Multiple pathways for sorting mitochondrial precursor proteins

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Cigarette smoke decreases mitochondrial porin expression and steroidogenesis.

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New insights into the mechanism of permeation through large channels

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The voltage-dependent anion channel, a major component of the tRNA import machinery in plant mitochondria

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RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels

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The mitochondrial permeability transition pore

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Tracking the unfolding and refolding pathways of outer membrane protein porin from Paracoccus denitrificans.

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Circular dichroism studies of the mitochondrial channel, VDAC, from Neurospora crassa

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12 December 2020

NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL.

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VDAC2 inhibits BAK activation and mitochondrial apoptosis

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12 December 2020

Crystallization of the Human, Mitochondrial Voltage-Dependent Anion-Selective Channel in the Presence of Phospholipids

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Structural and functional analysis of a salt stress inducible gene encoding voltage dependent anion channel (VDAC) from pearl millet (Pennisetum glaucum).

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12 December 2020

Myocardial ischemia/reperfusion causes VDAC phosphorylation which is reduced by cardioprotection with a p38 MAP kinase inhibitor

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12 December 2020

Molecular design of the voltage-dependent, anion-selective channel in the mitochondrial outer membrane

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12 December 2020

Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications

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12 December 2020

Caspase-dependent apoptosis in yeast

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Hexokinase II: the integration of energy metabolism and control of apoptosis

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The evolutionary history of mitochondrial porins.

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Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis. Conformational stability and porin activity.

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The permeability transition pore in cell death

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12 December 2020

Evidence for titratable gating charges controlling the voltage dependence of the outer mitochondrial membrane channel, VDAC.

1 reference

12 December 2020

10.1007/S10863-008-9144-Z

Identifiers

DOI

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18 April 2018

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18 April 2018