The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating
Open accessAbstract
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, revealing a high-resolution image of its architecture formed by 19 β-strands. Unlike the recent NMR structure of human VDAC1, the position of the voltage-sensing N-terminal segment is clearly resolved. The α-helix of the N-terminal segment is oriented against the interior wall, causing a partial narrowing at the center of the pore. This segment is ideally positioned to regulate the conductance of ions and metabolites passing through the VDAC pore.
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Voltage-dependent Anion Channels Modulate Mitochondrial Metabolism in Cancer Cells
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Metadata
- Authors
- Ujwal, R., Cascio, D., Colletier, J.-P., Faham, S., Zhang, J., Toro, L., Ping, P., & Abramson, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-11-18
- Volume
- 105
- Issue
- 46
- Pages
- 17742-17747
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2129141040
- Cited by
- 543
- References
- 45
- FWCI
- 13.77
- Type
- journal article
- Language
- en
- Open access
- green
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- Ujwal, R., Cascio, D., Colletier, J.-P., Faham, S., Zhang, J., Toro, L., Ping, P., & Abramson, J. (2008). The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0809634105
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