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- aggregation classification "A1".
- aggregation creator B240473.
- aggregation creator B240474.
- aggregation creator person.
- aggregation date "2012".
- aggregation format "application/pdf".
- aggregation hasFormat 3059760.bibtex.
- aggregation hasFormat 3059760.csv.
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- aggregation isPartOf urn:issn:1568-0266.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Medicine and Health Sciences".
- aggregation title "Drug design and identification of potent leads against Mycobacterium tuberculosis thymidine monophosphate kinase".
- aggregation abstract "Antiviral chemotherapy often relies on nucleoside analogues, which, once phophorylated by intracellular kinases, target viral polymerases impeding DNA synthesis. In contrast, nucleoside analogues are much less explored as antibacterial drugs. Thymidine monophosphate kinase from Mycobacterium tuberculosis (TMPKmt), which is essential to DNA replication, was selected as a promising target for the design of new inhibitors. This review describes stepwise modifications of the TMPKmt substrate, guided by the feedback of enzyme assays and crystallographic analysis to afford potent enzyme inhibitors some of which also exhibited antitubercular activity. More importantly, several of the reported thymidine analogues provided a deeper understanding of the structure and catalytic mechanism of this intriguing enzyme.".
- aggregation authorList BK513440.
- aggregation endPage "705".
- aggregation issue "7".
- aggregation startPage "694".
- aggregation volume "12".
- aggregation aggregates 3059779.
- aggregation isDescribedBy 3059760.
- aggregation similarTo LU-3059760.