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The N-terminus of VDAC: Structure, mutational analysis, and a potential role in regulating barrel shape.

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Solution structure and oligomeric state of the E. coli glycerol facilitator.

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A Cholesterol Analog Induces an Oligomeric Reorganization of VDAC.

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A deletion variant partially complements a porin-less strain of Neurospora crassa.

Analysis of mitochondrial proteomes from a wild-type strain FGSC9718, a strain lacking porin (ΔPor-1), and one expressing only 238porin revealed that the major differences between the variant strains were in the levels of subunits of the NADH:ubiquinone oxidoreductase (complex I) of the electron transport chain, which were reduced only in the ΔPorn-1 strain.
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A C-Terminally Truncated Variant of Neurospora crassa VDAC Assembles Into a Partially Functional Form in the Mitochondrial Outer Membrane and Forms Multimers in vitro

It is demonstrated that the putative 18-stranded β-barrel formed by VDAC-ΔC can be imported and assembled in the MOM in vivo and can also partially rescue the phenotype associated with the deletion of VDac from a strain of N. crassa.
PubMed (opens in a new tab)
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