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Literature DB >> 20437141

Backbone and ILV side chain methyl group assignments of the integral human membrane protein VDAC-1.

Sebastian Hiller¹, Thomas J Malia, Robert G Garces, Vladislav Y Orekhov, Gerhard Wagner.

Abstract

The voltage dependent anion channel (VDAC) forms a channel for metabolites and nutrients in the outer membrane of mitochondria, and it is also involved in apoptotic pathways. Here, we report sequence-specific NMR assignments for the isoform 1 of human VDAC reconstituted in lauryldimethylamine oxide (LDAO) detergent micelles. The assignments were deposited in the BMRB data base with accession number 16381.

Entities: CellLine Chemical Gene Species

Mesh：

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Year: 2009 PMID： 20437141 PMCID： PMC2896003 DOI： 10.1007/s12104-009-9194-0

Source DB: PubMed Journal: Biomol NMR Assign ISSN： 1874-270X Impact factor: 0.746

12 in total

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

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Review 5. Mitochondrial membrane permeabilization in cell death.

Authors: Guido Kroemer; Lorenzo Galluzzi; Catherine Brenner
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6. A candidate for the permeability pathway of the outer mitochondrial membrane.

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7. A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteins.

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