Source:http://linkedlifedata.com/resource/pubmed/id/15493921
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
42
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pubmed:dateCreated |
2004-10-20
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pubmed:abstractText |
A key factor in the potential clinical utility of membrane-active antibiotics is their cell selectivity (i.e., prokaryote over eukaryote). Cationic steroid antibiotics were developed to mimic the lipid A binding character of polymyxin B and are shown to bind lipid A derivatives with affinity greater than that of polymyxin B. The outer membranes of Gram-negative bacteria are comprised primarily of lipid A, and a fluorophore-appended cationic steroid antibiotic displays very high selectivity for Gram-negative bacterial membranes over Gram-positive bacteria and eukaryotic cell membranes. This cell selectivity of cationic steroid antibiotics may be due, in part, to the affinity of these compounds for lipid A.
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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 |
Oct
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pubmed:issn |
0002-7863
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2004 American Chemical Society
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
126
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13642-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15493921-Anti-Bacterial Agents,
pubmed-meshheading:15493921-Biomimetic Materials,
pubmed-meshheading:15493921-Cations,
pubmed-meshheading:15493921-Escherichia coli,
pubmed-meshheading:15493921-Lipid A,
pubmed-meshheading:15493921-Microbial Sensitivity Tests,
pubmed-meshheading:15493921-Pseudomonas aeruginosa,
pubmed-meshheading:15493921-Spectrometry, Fluorescence,
pubmed-meshheading:15493921-Staphylococcus aureus,
pubmed-meshheading:15493921-Steroids,
pubmed-meshheading:15493921-Structure-Activity Relationship,
pubmed-meshheading:15493921-Substrate Specificity
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pubmed:year |
2004
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pubmed:articleTitle |
Origins of cell selectivity of cationic steroid antibiotics.
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pubmed:affiliation |
Contribution from the Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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