Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1-Reference-Cited by-同舟云学术

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Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1

Published:2014-06-08 Issue:7 Volume:21 Page:626-632
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Choudhary Om P,Paz Aviv,Adelman Joshua L,Colletier Jacques-Philippe,Abramson Jeff,Grabe Michael

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2841.pdf

Reference73 articles.

1. Törnroth-Horsefield, S. & Neutze, R. Opening and closing the metabolite gate. Proc. Natl. Acad. Sci. USA 105, 19565–19566 (2008).

2. Rostovtseva, T.K. et al. Tubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respiration. Proc. Natl. Acad. Sci. USA 105, 18746–18751 (2008).

3. Schwarzer, C., Barnikol-Watanabe, S., Thinnes, F.P. & Hilschmann, N. Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74. Int. J. Biochem. Cell Biol. 34, 1059–1070 (2002).

4. Shimizu, S., Narita, M. & Tsujimoto, Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399, 483–487 (1999).

5. Min, C.K. et al. Coupling of ryanodine receptor 2 and voltage-dependent anion channel 2 is essential for Ca2+ transfer from the sarcoplasmic reticulum to the mitochondria in the heart. Biochem. J. 447, 371–379 (2012).

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