| pubmed-article:17967002 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C0003448 | lld:lifeskim |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C1157266 | lld:lifeskim |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:17967002 | lifeskim:mentions | umls-concept:C0950382 | lld:lifeskim |
| pubmed-article:17967002 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:17967002 | pubmed:dateCreated | 2007-11-26 | lld:pubmed |
| pubmed-article:17967002 | pubmed:abstractText | A study of the structure-activity relationships of 5'-O-[N-(salicyl)sulfamoyl]adenosine (6), a potent inhibitor of the bifunctional enzyme salicyl-AMP ligase (MbtA, encoded by the gene Rv2384) in Mycobacterium tuberculosis, is described, targeting the salicyl moiety. A systematic series of analogues was prepared exploring the importance of substitution at the C-2 position revealing that a hydroxy group is required for optimal activity. Examination of a series of substituted salicyl derivatives indicated that substitution at C-4 was tolerated. Consequently, a series of analogues at this position provided 4-fluoro derivative, which displayed an impressive MIC99 of 0.098 microM against whole-cell M. tuberculosis under iron-limiting conditions. Examination of other heterocyclic, cycloalkyl, alkyl, and aminoacyl replacements of the salicyl moiety demonstrated that these nonconservative modifications were poorly tolerated, a result consistent with the fairly strict substrate specificities of related non-ribosomal peptide synthetase adenylation enzymes. | lld:pubmed |
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| pubmed-article:17967002 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17967002 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17967002 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17967002 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17967002 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:17967002 | pubmed:issn | 0022-2623 | lld:pubmed |
| pubmed-article:17967002 | pubmed:author | pubmed-author:BennettEric... | lld:pubmed |
| pubmed-article:17967002 | pubmed:author | pubmed-author:WilsonDaniel... | lld:pubmed |
| pubmed-article:17967002 | pubmed:author | pubmed-author:BoshoffHelena... | lld:pubmed |
| pubmed-article:17967002 | pubmed:author | pubmed-author:BarryClifton... | lld:pubmed |
| pubmed-article:17967002 | pubmed:author | pubmed-author:AldrichCourtn... | lld:pubmed |
| pubmed-article:17967002 | pubmed:author | pubmed-author:QiaoChunhuaC | lld:pubmed |
| pubmed-article:17967002 | pubmed:author | pubmed-author:GupteAmolA | lld:pubmed |
| pubmed-article:17967002 | pubmed:author | pubmed-author:SomuRavindran... | lld:pubmed |
| pubmed-article:17967002 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17967002 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:17967002 | pubmed:volume | 50 | lld:pubmed |
| pubmed-article:17967002 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17967002 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17967002 | pubmed:pagination | 6080-94 | lld:pubmed |
| pubmed-article:17967002 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17967002 | pubmed:meshHeading | pubmed-meshheading:17967002... | lld:pubmed |
| pubmed-article:17967002 | pubmed:meshHeading | pubmed-meshheading:17967002... | lld:pubmed |
| pubmed-article:17967002 | pubmed:meshHeading | pubmed-meshheading:17967002... | lld:pubmed |
| pubmed-article:17967002 | pubmed:meshHeading | pubmed-meshheading:17967002... | lld:pubmed |
| pubmed-article:17967002 | pubmed:meshHeading | pubmed-meshheading:17967002... | lld:pubmed |
| pubmed-article:17967002 | pubmed:meshHeading | pubmed-meshheading:17967002... | lld:pubmed |
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| pubmed-article:17967002 | pubmed:meshHeading | pubmed-meshheading:17967002... | lld:pubmed |
| pubmed-article:17967002 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17967002 | pubmed:articleTitle | 5'-O-[(N-acyl)sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: an adenylation enzyme required for siderophore biosynthesis of the mycobactins. | lld:pubmed |
| pubmed-article:17967002 | pubmed:affiliation | Center for Drug Design, Academic Health Center, University of Minnesota, Minneapolis, MN 55455, USA. | lld:pubmed |
| pubmed-article:17967002 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17967002 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17967002 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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