Source:http://linkedlifedata.com/resource/pubmed/id/15225721
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
2004-6-30
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pubmed:abstractText |
QSAR studies of a series of blockers of the SK(Ca) channel in guinea-pig hepatocytes suggests that the polarizability of the blocker is an important factor controlling the binding to the channel. It is suggested that, upon binding, an ion-pair is formed, a process that is promoted by the reorganization of the water molecules. The polarizability is not adequate to describe the potency of the most potent blockers with a good stereochemical fit to the channel, presumably due to more specific interactions taking place.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4031-5
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pubmed:meshHeading |
pubmed-meshheading:15225721-Animals,
pubmed-meshheading:15225721-Apamin,
pubmed-meshheading:15225721-Guinea Pigs,
pubmed-meshheading:15225721-Hepatocytes,
pubmed-meshheading:15225721-Kinetics,
pubmed-meshheading:15225721-Molecular Conformation,
pubmed-meshheading:15225721-Potassium Channels, Calcium-Activated
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pubmed:year |
2004
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pubmed:articleTitle |
Defining determinant molecular properties for the blockade of the apamin-sensitive SKCa channel in guinea-pig hepatocytes: the influence of polarizability and molecular geometry.
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pubmed:affiliation |
Department of Pharmaceutical Chemistry, School of Pharmacy, Aristotelian University of Thessaloniki, 541 24 Thessaloniki, Greece. dgalana@pharm.auth.gr
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pubmed:publicationType |
Journal Article
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