| pubmed-article:9199780 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C0028778 | lld:lifeskim |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C0006685 | lld:lifeskim |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C0014406 | lld:lifeskim |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C0486616 | lld:lifeskim |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C0057583 | lld:lifeskim |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C0392760 | lld:lifeskim |
| pubmed-article:9199780 | lifeskim:mentions | umls-concept:C0597214 | lld:lifeskim |
| pubmed-article:9199780 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9199780 | pubmed:dateCreated | 1997-8-27 | lld:pubmed |
| pubmed-article:9199780 | pubmed:abstractText | The pore-forming alpha 1 subunit of L-type calcium (Ca2+) channels is the molecular target of Ca2+ channel blockers such as phenylalkylamines (PAAs). Association and dissociation rates of (-)devapamil were compared for a highly PAA-sensitive L-type Ca2+ channel chimera (Lh) and various class A Ca2+ channel mutants. These mutants carry the high-affinity determinants of the PAA receptor site in a class A sequence environment. Apparent drug association and dissociation rate constants were significantly affected by the sequence environment (class A or L-type) of the PAA receptor site. Single point mutations affecting the high-affinity determinants in segments IVS6 of the PAA receptor site, introduced into a class A environment, reduced the apparent drug association rates. Mutation I1811M in transmembrane segment IVS6 (mutant AL25/-I) had the highest impact and decreased the apparent association rate for (-)devapamil by approximately 30-fold, suggesting that this pore-lining isoleucine in transmembrane segment IVS6 plays a key role in the formation of the PAA receptor site. In contrast, apparent drug dissociation rates of Ca2+ channels in the resting state were almost unaffected by point mutations of the PAA receptor site. | lld:pubmed |
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| pubmed-article:9199780 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9199780 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9199780 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9199780 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9199780 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9199780 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9199780 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:9199780 | pubmed:author | pubmed-author:TiminE NEN | lld:pubmed |
| pubmed-article:9199780 | pubmed:author | pubmed-author:KimballDD | lld:pubmed |
| pubmed-article:9199780 | pubmed:author | pubmed-author:HeringSS | lld:pubmed |
| pubmed-article:9199780 | pubmed:author | pubmed-author:DöringFF | lld:pubmed |
| pubmed-article:9199780 | pubmed:author | pubmed-author:MitterdorferJ... | lld:pubmed |
| pubmed-article:9199780 | pubmed:author | pubmed-author:DegtiarV EVE | lld:pubmed |
| pubmed-article:9199780 | pubmed:author | pubmed-author:BerjukowSS | lld:pubmed |
| pubmed-article:9199780 | pubmed:author | pubmed-author:AczélSS | lld:pubmed |
| pubmed-article:9199780 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9199780 | pubmed:volume | 73 | lld:pubmed |
| pubmed-article:9199780 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9199780 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9199780 | pubmed:pagination | 157-67 | lld:pubmed |
| pubmed-article:9199780 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9199780 | pubmed:meshHeading | pubmed-meshheading:9199780-... | lld:pubmed |
| pubmed-article:9199780 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9199780 | pubmed:articleTitle | Calcium channel block by (-)devapamil is affected by the sequence environment and composition of the phenylalkylamine receptor site. | lld:pubmed |
| pubmed-article:9199780 | pubmed:affiliation | Institut für Biochemische Pharmakologie, Innsbruck, Austria. | lld:pubmed |
| pubmed-article:9199780 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9199780 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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