The Crystal Structure of Mouse VDAC1 at 2.3 Å Resolution Reveals Mechanistic Insights into Metabolit...
The Crystal Structure of Mouse VDAC1 at 2.3 Å Resolution Reveals Mechanistic Insights into Metabolite Gating
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United States: National Academy of Sciences
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English
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United States: National Academy of Sciences
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The voltage-dependent anion channel (VDAC) constitutes the major pathway for the entry and exit of metabolites across the outer membrane of the mitochondria and can serve as a scaffold for molecules that modulate the organelle. We report the crystal structure of a β-barrel eukaryotic membrane protein, the murine VDAC1 (mVDAC1) at 2.3 Å resolution,...
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The Crystal Structure of Mouse VDAC1 at 2.3 Å Resolution Reveals Mechanistic Insights into Metabolite Gating
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TN_cdi_osti_scitechconnect_1007071
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_osti_scitechconnect_1007071
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.0809634105
