The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Selectivity Changes in Site-Directed Mutants of the VDAC Ion Channel: Structural Implications
Abstract
The gene encoding the yeast mitochondrial outer membrane channel VDAC was subjected to site-directed mutagenesis to change amino acids at 29 positions to residues differing in charge from the wild-type sequence. The mutant genes were then expressed in yeast, and the physiological consequences of single and multiple amino acid changes were assessed after isolation and insertion of mutant channels into phospholipid bilayers. Selectivity changes were observed at 14 sites distributed throughout the length of the molecule. These sites are likely to define the position of the protein walls lining the aqueous pore and hence, the transmembrane segments. These results have been used to develop a model of the open state of the channel in which each polypeptide contributes 12 β strands and one α helix to form the aqueous transmembrane pathway.
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Cites
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[12] One-step gene disruption in yeast
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Mitochondrial targeting sequences may form amphiphilic helices.
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Self-citationRoise, D., Horvath, S. J., Tomich, J. M., Richards, J. H., & Schatz, G. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04363.x · Cited by 500
The gapped duplex DNA approach to oligonucleotide-directed mutation construction
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A candidate for the permeability pathway of the outer mitochondrial membrane
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Self-citationVoltage gating in the mitochondrial channel, VDAC
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Self-citationVoltage-sensitive ion channels
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Cited by
Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178
VDAC, a multi-functional mitochondrial protein regulating cell life and death
Shoshan-Barmatz, V., De Pinto, V., Zweckstetter, M., Raviv, Z., Keinan, N., & Arbel, N. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.03.002 · Cited by 782
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Self-citationTubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respiration
Rostovtseva, T. K., Sheldon, K. L., Hassanzadeh, E., Monge, C., Saks, V., Bezrukov, S. M., & Sackett, D. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806303105 · Cited by 366
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Metadata
- Authors
- Blachly-Dyson, E., Peng, S., Colombini, M., & Forte, M.
- Venue
- Science
- Published
- 1990-03-09
- Volume
- 247
- Issue
- 4947
- Pages
- 1233-1236
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1991143182
- Cited by
- 273
- References
- 23
- FWCI
- 5.54
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Selectivity Changes in Site-Directed Mutants of the VDAC Ion Channel: Structural Implications. https://app.cochat.ai/papers/10.1126/science.1690454
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- Blachly-Dyson, E., Peng, S., Colombini, M., & Forte, M. (1990). Selectivity Changes in Site-Directed Mutants of the VDAC Ion Channel: Structural Implications. Science. https://doi.org/10.1126/science.1690454
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
