| pubmed-article:7642622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7642622 | lifeskim:mentions | umls-concept:C0001975 | lld:lifeskim |
| pubmed-article:7642622 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:7642622 | lifeskim:mentions | umls-concept:C1522642 | lld:lifeskim |
| pubmed-article:7642622 | lifeskim:mentions | umls-concept:C0032824 | lld:lifeskim |
| pubmed-article:7642622 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:7642622 | lifeskim:mentions | umls-concept:C1853126 | lld:lifeskim |
| pubmed-article:7642622 | lifeskim:mentions | umls-concept:C0002915 | lld:lifeskim |
| pubmed-article:7642622 | lifeskim:mentions | umls-concept:C2699782 | lld:lifeskim |
| pubmed-article:7642622 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:7642622 | pubmed:dateCreated | 1995-9-18 | lld:pubmed |
| pubmed-article:7642622 | pubmed:abstractText | The molecular basis of general anesthetic action on membrane proteins that control ion transport is not yet understood. In a previous report (Covarrubias, M., and Rubin, E. (1993) Proc. Natl. Acad. Sci. 90, 6957-6960), we found that low concentrations of ethanol (17-170mM) selectively inhibited a noninactivating cloned K+ channel encoded by Drosophila Shaw2. Here, we have conducted equilibrium dos-inhibition experiments, single channel recording, and mutagenesis in vitro to study the mechanism underlying the inhibition of Shaw2K+ channels by a homologous series of n-alkanols (ethanol to 1-hexanol). The results showed that: (i) these alcohols inhibited Shaw2 whole-cell currents, the equilibrium dose-inhibition relations were hyperbolic, and competition experiments revealed the presence of a discrete site of action, possibly a hydrophobic pocket; (ii) this pocket may be part of the protein because n-alkanol sensitivity can be transferred to novel hybrid K+ channels composed of Shaw2 subunits and homologous ethanol-insensitive subunits: (iii) moreover, a hydrophobic point mutation within a cytoplasmic loop of an ethanol-insensitive K+ channel (human Kv3.4) was sufficient to allow significant inhibition by n-alkanols, with a dose-inhibition relation that closely resembled that of wildtype Shaw2 channels; and (iv) 1-butanol selectively inhibited long duration single channel openings in a manner consistent with a direct effect on channel gating. These results strongly suggest that a discrete site within the ion channel protein is the primary locus of alcohol and general anesthetic action. | lld:pubmed |
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| pubmed-article:7642622 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7642622 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7642622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7642622 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7642622 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7642622 | pubmed:author | pubmed-author:CovarrubiasMM | lld:pubmed |
| pubmed-article:7642622 | pubmed:author | pubmed-author:EscobarLL | lld:pubmed |
| pubmed-article:7642622 | pubmed:author | pubmed-author:WeiAA | lld:pubmed |
| pubmed-article:7642622 | pubmed:author | pubmed-author:VyasT BTB | lld:pubmed |
| pubmed-article:7642622 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7642622 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:7642622 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7642622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7642622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7642622 | pubmed:pagination | 19408-16 | lld:pubmed |
| pubmed-article:7642622 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7642622 | pubmed:meshHeading | pubmed-meshheading:7642622-... | lld:pubmed |
| pubmed-article:7642622 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7642622 | pubmed:articleTitle | Alcohols inhibit a cloned potassium channel at a discrete saturable site. Insights into the molecular basis of general anesthesia. | lld:pubmed |
| pubmed-article:7642622 | pubmed:affiliation | Department of Pathology, Anatomy, and Cell Biology, Jefferson Medical College, Philadelphia, Pennsylvania 19107, USA. | lld:pubmed |
| pubmed-article:7642622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7642622 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7642622 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:33599 | entrezgene:pubmed | pubmed-article:7642622 | lld:entrezgene |
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