Yuk-Ching Tse-Dinh, Ph.D.
Professor of Biochemistry and Molecular Biology
Email:
Address:
Department of Biochemistry and Molecular Biology
New York Medical College
Valhalla, NY 10595
Professional Interests:
Research interests include topoisomerase structure, mechanism, function and regulation. Our current research is targeting bacterial DNA topoisomerase I to bring about a new class of novel antibacterial drugs.
Education Profile:
Post Graduate Studies
Graduate Degree: Ph.D.
Graduate Degree Institution: Harvard University
Undergraduate Institution: Hollins College
Selected Bibliography:
Tse-Dinh YC 2009. Bacterial topoisomerase I as a target for discovery of antibacterial compounds. Invited peer reviewed Survey and Summary for Nucl Acids Res 37, 731-737.
Sutherland JH, Tse-Dinh YC 2010. Analysis of RuvABC and RecG involvement in the Escherichia coli response to the covalent topoisomerase-DNA complex. J Bacteriol 192, 4445-51.
Narula G, Becker J, Cheng B, Dani N, Abrenica MV, Tse-Dinh YC 2010. The DNA relaxation activity and covalent complex accumulation of Mycobacterium tuberculosis topoisomerase I can be assayed in Escherichia coli: application for identification of potential FRET-dye labeling sites. BMC Biochemistry 11, 41.
Zhang Z, Cheng B, Tse-Dinh YC 2011. Crystal structure of a covalent intermediate in DNA cleavage and rejoining by Escherichia coli DNA topoisomerase I. Proc Natl Acad Sci USA 108, 6939-6944.
Narula G, Annamalai T, Aedo S, Cheng B, Sorokin E, Wong A, Tse-Dinh YC 2011. The strictly conserved Arg-321 residue in the active site of Escherichia coli topoisomerase I plays a critical role in DNA rejoining. J Biol Chem 286, 18673-18682.
Liu IF, Sutherland JH, Cheng B, Tse-Dinh YC 2011. Topoisomerase I function during Escherichia coli response to antibiotics and stress enhances cell killing from stabilization of its cleavage complex. J Antimicrob Chemother 66, 1518-1524.