The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
High-Level Expression, Functional Reconstitution, and Quaternary Structure of a Prokaryotic Clc-Type Chloride Channel
Open accessAbstract
ClC-type anion-selective channels are widespread throughout eukaryotic organisms. BLAST homology searches reveal that many microbial genomes also contain members of the ClC family. An Escherichia coli–derived ClC Cl− channel homologue, “EriC,” the product of the yadQ gene, was overexpressed in E. coli and purified in milligram quantities in a single-step procedure. Reconstitution of purified EriC into liposomes confers on these membranes permeability to anions with selectivity similar to that observed electrophysiologically in mammalian ClC channels. Cross-linking studies argue that EriC is a homodimer in both detergent micelles and reconstituted liposomes, a conclusion corroborated by gel filtration and analytical sedimentation experiments.
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Cites
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Hydration forces between phospholipid bilayers
Rand, R. P., & Parsegian, V. A. (1989) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(89)90010-5 · Cited by 1,125
Cited by
X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T., & MacKinnon, R. (2002) · Nature · doi:10.1038/415287a · Cited by 1,446
Molecular Structure and Physiological Function of Chloride Channels
Jentsch, T. J., Stein, V., Weinreich, F., & Zdebik, A. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00029.2001 · Cited by 1,256
Widespread genetic switches and toxicity resistance proteins for fluoride
Baker, J. L., Sudarsan, N., Weinberg, Z., Roth, A., Stockbridge, R. B., & Breaker, R. R. (2012) · Science · doi:10.1126/science.1215063 · Cited by 438
The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes
Graves, A. R., Curran, P. K., Smith, C. L., & Mindell, J. A. (2008) · Nature · doi:10.1038/nature06907 · Cited by 399
Wackett, L. P. (2022) · Microbial Biotechnology · doi:10.1111/1751-7915.13928 · Cited by 165
Metadata
- Authors
- Maduke, M., Pheasant, D. J., & Miller, C.
- Venue
- The Journal of General Physiology
- Publisher
- Rockefeller University Press
- Published
- 1999-10-25
- Volume
- 114
- Issue
- 5
- Pages
- 713-722
- ISSN
- 0022-1295 (ISSN-L)
- 1540-7748
- OpenAlex
- W2080861274
- Cited by
- 158
- References
- 2
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- green
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- Maduke, M., Pheasant, D. J., & Miller, C. (1999). High-Level Expression, Functional Reconstitution, and Quaternary Structure of a Prokaryotic Clc-Type Chloride Channel. The Journal of General Physiology. https://doi.org/10.1085/jgp.114.5.713
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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