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Search: authors:"Thirunavukkarasu Annamalai"

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Mechanism and resistance for antimycobacterial activity of a fluoroquinophenoxazine compound

: Pamela K. Garcia, Thirunavukkarasu Annamalai, Wenjie Wang, Raven S. Bell, Duc Le, Paula Martin Pancorbo, Sabah Sikandar, Ahmed Seddek, Purushottam B. Tiwari, Methodology: Thirunavukkarasu Annamalai ... . Project administration: Thirunavukkarasu Annamalai, Yuk-Ching Tse-Dinh. Resources: Xufen Yu, Dianqing Sun, Anne-Catrin Uhlemann. Supervision: Thirunavukkarasu Annamalai, Dianqing Sun, Fenfei Leng, Yuk

Inhibition of Zn(II) Binding Type IA Topoisomerases by Organomercury Compounds and Hg(II)

Type IA topoisomerase activities are essential for resolving DNA topological barriers via an enzyme-mediated transient single strand DNA break. Accumulation of topoisomerase DNA cleavage product can lead to cell death or genomic rearrangement. Many antibacterial and anticancer drugs act as topoisomerase poison inhibitors that form stabilized ternary complexes with the...

Identification of Anziaic Acid, a Lichen Depside from Hypotrachyna sp., as a New Topoisomerase Poison Inhibitor

Topoisomerase inhibitors are effective for antibacterial and anticancer therapy because they can lead to the accumulation of the intermediate DNA cleavage complex formed by the topoisomerase enzymes, which trigger cell death. Here we report the application of a novel enzyme-based high-throughput screening assay to identify natural product extracts that can lead to increased...

Analysis of DNA relaxation and cleavage activities of recombinant Mycobacterium tuberculosis DNA topoisomerase I from a new expression and purification protocol

Background Mycobacterium tuberculosis DNA topoisomerase I is an attractive target for discovery of novel TB drugs that act by enhancing the accumulation of the topoisomerase-DNA cleavage product. It shares a common transesterification domain with other type IA DNA topoisomerases. There is, however, no homology between the C-terminal DNA binding domains of Escherichia coli and M...