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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
2005-8-18
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pubmed:abstractText |
We report that N(6)-(1-naphthyl)-ADP inhibits the Escherichia coli RecA protein in vitro. A novel rapid screen identified it as a potent inhibitor of RecA nucleoprotein filament formation, and further characterization established it as an ATP-competitive inhibitor of RecA-catalyzed ATP hydrolysis. This and other inhibitors of RecA activities represent a new approach for understanding the molecular targets and pathways involved in the evolution of antibiotic resistance in bacteria.
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pubmed:grant |
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-2623
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5408-11
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16107138-1-Naphthylamine,
pubmed-meshheading:16107138-Adenosine Diphosphate,
pubmed-meshheading:16107138-Adenosine Triphosphate,
pubmed-meshheading:16107138-DNA, Single-Stranded,
pubmed-meshheading:16107138-Drug Resistance, Bacterial,
pubmed-meshheading:16107138-Escherichia coli Proteins,
pubmed-meshheading:16107138-Hydrolysis,
pubmed-meshheading:16107138-Kinetics,
pubmed-meshheading:16107138-Models, Molecular,
pubmed-meshheading:16107138-Protein Binding,
pubmed-meshheading:16107138-Rec A Recombinases,
pubmed-meshheading:16107138-Structure-Activity Relationship
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pubmed:year |
2005
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pubmed:articleTitle |
A molecular target for suppression of the evolution of antibiotic resistance: inhibition of the Escherichia coli RecA protein by N(6)-(1-naphthyl)-ADP.
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pubmed:affiliation |
School of Pharmacy, Division of Medicinal Chemistry and Natural Products, University of North Carolina at Chapel Hill, CB 7360, Chapel Hill, North Carolina 27599-7360, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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