|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
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pubmed:dateCreated |
2008-1-28
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|
pubmed:abstractText |
The emergence of drug resistant strains of important human pathogens has made urgent the necessity of finding new targets and novel antimicrobial agents. One of the most promising targets is FabH. In this review we summarize the progress made in the design of FabH inhibitors and the role played by the 3D-structure of the enzyme in the drug design process.
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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 |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
1389-5575
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
8
|
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pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
36-45
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|
pubmed:dateRevised |
2010-10-7
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|
pubmed:meshHeading |
|
|
pubmed:year |
2008
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|
pubmed:articleTitle |
Bacterial beta-ketoacyl-acyl carrier protein synthase III (FabH): an attractive target for the design of new broad-spectrum antimicrobial agents.
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|
pubmed:affiliation |
Central University of Las Villas, Santa Clara, 54830, Villa Clara, Cuba.
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|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|
