Molecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs
The Mitochondrial Porin, VDAC, Has Retained the Ability to Be Assembled in the Bacterial Outer Membrane
Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer's disease
18Mitochondrial translocation of GSK-3beta, a trigger of mitochondrial permeability transition, is mediated by its N-terminal domain and promoted by interaction with VDAC2.
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Voltage-dependent anion channel. See porins.
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