| pubmed-article:15743201 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15743201 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:15743201 | lifeskim:mentions | umls-concept:C0007292 | lld:lifeskim |
| pubmed-article:15743201 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:15743201 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:15743201 | lifeskim:mentions | umls-concept:C1136254 | lld:lifeskim |
| pubmed-article:15743201 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:15743201 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
| pubmed-article:15743201 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:15743201 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:15743201 | pubmed:dateCreated | 2005-3-3 | lld:pubmed |
| pubmed-article:15743201 | pubmed:abstractText | Fatty acid biosynthesis is essential for bacterial survival. Components of this biosynthetic pathway have been identified as attractive targets for the development of new antibacterial agents. FabH, beta-ketoacyl-ACP synthase III, is a particularly attractive target, since it is central to the initiation of fatty acid biosynthesis and is highly conserved among Gram-positive and -negative bacteria. Small molecules that inhibit FabH enzymatic activity have the potential to be candidates within a novel class of selective, nontoxic, broad-spectrum antibacterials. Using crystallographic structural information on these highly conserved active sites and structure based drug design principles, a benzoylaminobenzoic acid series of compounds was developed as potent inhibitors of FabH. This inhibitor class demonstrates strong antibacterial activity against Gram-positive and selected Gram-negative organisms. | lld:pubmed |
| pubmed-article:15743201 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15743201 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15743201 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15743201 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15743201 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15743201 | pubmed:issn | 0022-2623 | lld:pubmed |
| pubmed-article:15743201 | pubmed:author | pubmed-author:SuYingY | lld:pubmed |
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| pubmed-article:15743201 | pubmed:author | pubmed-author:NieZheZ | lld:pubmed |
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| pubmed-article:15743201 | pubmed:author | pubmed-author:LuJiaJ | lld:pubmed |
| pubmed-article:15743201 | pubmed:author | pubmed-author:MargosiakStep... | lld:pubmed |
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| pubmed-article:15743201 | pubmed:author | pubmed-author:ChuShaosongS | lld:pubmed |
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| pubmed-article:15743201 | pubmed:author | pubmed-author:CortezJosephJ | lld:pubmed |
| pubmed-article:15743201 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15743201 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:15743201 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:15743201 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15743201 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15743201 | pubmed:pagination | 1596-609 | lld:pubmed |
| pubmed-article:15743201 | pubmed:dateRevised | 2010-10-7 | lld:pubmed |
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| pubmed-article:15743201 | pubmed:meshHeading | pubmed-meshheading:15743201... | lld:pubmed |
| pubmed-article:15743201 | pubmed:meshHeading | pubmed-meshheading:15743201... | lld:pubmed |
| pubmed-article:15743201 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15743201 | pubmed:articleTitle | Structure-based design, synthesis, and study of potent inhibitors of beta-ketoacyl-acyl carrier protein synthase III as potential antimicrobial agents. | lld:pubmed |
| pubmed-article:15743201 | pubmed:affiliation | Departments of Medicinal Chemistry, Protein Biochemistry and Structural Biology, Quorex Pharmaceuticals Inc., 1890 Rutherford Road, Suite 200, Carlsbad, CA 92008, USA. zhenie@phoenixpharmaco.com | lld:pubmed |
| pubmed-article:15743201 | pubmed:publicationType | Journal Article | lld:pubmed |
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