Source:http://linkedlifedata.com/resource/pubmed/id/11321570
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2001-4-25
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pubmed:abstractText |
The resistance of cells to many drugs simultaneously (multidrug resistance) often involves the expression of membrane transporters (Mdrs); each can recognize and expel a broad spectrum of chemically unrelated drugs from the cell. Despite extensive research for many years, the actual mechanism of multidrug transport is still largely unknown. In addition to general questions dealing with energy coupling, the molecular view of substrate recognition by Mdrs is generally obscure. This mini-review describes structural and functional properties of the Escherichia coli Mdr, MdfA, and discusses the possibility that this transporter may serve as a model for studying the multidrug recognition phenomenon and the mechanism of multidrug transport.
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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 |
Apr
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pubmed:issn |
1464-1801
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
171-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11321570-Amino Acid Sequence,
pubmed-meshheading:11321570-Bacterial Proteins,
pubmed-meshheading:11321570-Cell Membrane,
pubmed-meshheading:11321570-Drug Resistance, Microbial,
pubmed-meshheading:11321570-Drug Resistance, Multiple,
pubmed-meshheading:11321570-Escherichia coli,
pubmed-meshheading:11321570-Escherichia coli Proteins,
pubmed-meshheading:11321570-Membrane Transport Proteins,
pubmed-meshheading:11321570-Models, Biological,
pubmed-meshheading:11321570-Models, Molecular,
pubmed-meshheading:11321570-Molecular Sequence Data,
pubmed-meshheading:11321570-Protein Structure, Secondary,
pubmed-meshheading:11321570-Substrate Specificity
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pubmed:year |
2001
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pubmed:articleTitle |
MdfA, an interesting model protein for studying multidrug transport.
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pubmed:affiliation |
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel. bcbibi@wicc.weizmann.ac.il
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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