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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2000-1-11
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pubmed:abstractText |
To understand the chemical basis of action for the PDR5-encoded multidrug resistance transporter of Saccharomyces cerevisiae, we compared the relative hypersensitivities of the wild-type (RW2802) and null mutant strains toward a series of tri-n-alkyltin compounds. These compounds differ from each other in a systematic fashion-either by hydrocarbon chain length or by anion composition. Using zone-of-inhibition and fixed-concentration assays, we found that the ethyl, propyl, and butyl compounds are strong PDR5 substrates, whereas the methyl and pentyl compounds are weak. We conclude that hydrophobicity and anion makeup are relatively unimportant factors in determining whether a tri-n-alkyltin compound is a good PDR5 substrate but that the dissociation of the compound and the molecular size are significant.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-10029991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-1130791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-1319843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-141273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-1678520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-3162758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-7635278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-7840595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-8094081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-8102521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-8294477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-8437567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-8940170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10602734-9450972
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/P-Glycoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/PDR5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trialkyltin Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Triethyltin Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Trimethyltin Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/tributyltin,
http://linkedlifedata.com/resource/pubmed/chemical/triethyltin,
http://linkedlifedata.com/resource/pubmed/chemical/trimethyltin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0066-4804
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
134-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10602734-ATP-Binding Cassette Transporters,
pubmed-meshheading:10602734-Drug Resistance, Multiple,
pubmed-meshheading:10602734-Fungal Proteins,
pubmed-meshheading:10602734-Membrane Proteins,
pubmed-meshheading:10602734-P-Glycoprotein,
pubmed-meshheading:10602734-Saccharomyces cerevisiae,
pubmed-meshheading:10602734-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10602734-Solubility,
pubmed-meshheading:10602734-Structure-Activity Relationship,
pubmed-meshheading:10602734-Substrate Specificity,
pubmed-meshheading:10602734-Trialkyltin Compounds,
pubmed-meshheading:10602734-Triethyltin Compounds,
pubmed-meshheading:10602734-Trimethyltin Compounds
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pubmed:year |
2000
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pubmed:articleTitle |
Chemical specificity of the PDR5 multidrug resistance gene product of Saccharomyces cerevisiae based on studies with tri-n-alkyltin chlorides.
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pubmed:affiliation |
Departments of Biology, The Catholic University of America, Washington, D.C. 20064, USA. Golin@cua.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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