ArticleThe Journal of general physiology2007
The role of a conserved lysine in chloride- and voltage-dependent ClC-0 fast gating.
Article in The Journal of general physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Molecular mechanism of exchange coupling in CLC chloride/proton antiporters.Nature communications · 2026Article
- Chloride Ion Transport by theFrontiers in chemistry · 2018Article
- 13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.Journal of biomolecular NMR · 2015Article
- Influences of mutations on the electrostatic binding free energies of chloride ions in Escherichia coli ClC.The journal of physical chemistry. B · 2012Article
- A three-state multi-ion kinetic model for conduction properties of ClC-0 chloride channel.Biophysical journal · 2010Article
- Paul F. Cranefield Award to Merritt C. Maduke.The Journal of general physiology · 2010Article
- Intracellular proton regulation of ClC-0.The Journal of general physiology · 2008Article
- The mechanism of fast-gate opening in ClC-0.The Journal of general physiology · 2007Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
ClC-0 is a chloride channel whose gating is sensitive to voltage, chloride, and pH. In a previous publication, we showed that the K149C mutation causes a +70-mV shift in the voltage dependence of ClC-0 fast gating. In this paper we analyze the effects of a series of mutations at K149 on the voltage and chloride dependence of gating. By fitting our data to the previously proposed four-state model for ClC-0 fast gating, we show which steps in fast-gate opening are likely to be affected by these mutations. Computational analysis of mutant ClC-0 homology models show electrostatic contributions to chloride binding that may partially account for the effects of K149 on gating. The analysis of gating kinetics in combination with the available structural information suggests some of the structural changes likely to underpin fast-gate opening.
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Registered trials
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