| pubmed-article:18493582 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18493582 | lifeskim:mentions | umls-concept:C0026926 | lld:lifeskim |
| pubmed-article:18493582 | lifeskim:mentions | umls-concept:C0040085 | lld:lifeskim |
| pubmed-article:18493582 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
| pubmed-article:18493582 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:18493582 | lifeskim:mentions | umls-concept:C1041438 | lld:lifeskim |
| pubmed-article:18493582 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:18493582 | pubmed:dateCreated | 2008-5-21 | lld:pubmed |
| pubmed-article:18493582 | pubmed:abstractText | Mycobacterium tuberculosis kills approximately 2 million people each year and presents an urgent need to identify new targets and new antitubercular drugs. Thymidylate synthase (TS) enzymes from other species offer good targets for drug development and the M. tuberculosis genome contains two putative TS enzymes, a conventional ThyA and a flavin-based ThyX. In M. tuberculosis, both TS enzymes have been implicated as essential for growth, either based on drug-resistance studies or genome-wide mutagenesis screens. To facilitate future small molecule inhibitors against these proteins, a detailed enzymatic characterization was necessary. | lld:pubmed |
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| pubmed-article:18493582 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18493582 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18493582 | pubmed:issn | 1932-6203 | lld:pubmed |
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| pubmed-article:18493582 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18493582 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:18493582 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18493582 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18493582 | pubmed:pagination | e2237 | lld:pubmed |
| pubmed-article:18493582 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:18493582 | pubmed:meshHeading | pubmed-meshheading:18493582... | lld:pubmed |
| pubmed-article:18493582 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18493582 | pubmed:articleTitle | Kinetics and ligand-binding preferences of Mycobacterium tuberculosis thymidylate synthases, ThyA and ThyX. | lld:pubmed |
| pubmed-article:18493582 | pubmed:affiliation | Department of Chemistry, University of Washington, Seattle, Washington, United States of America. | lld:pubmed |
| pubmed-article:18493582 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18493582 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18493582 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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