Yuk-Ching Tse-Dinh, Ph.D.
Professor of Biochemistry and Molecular Biology
Department of Biochemistry and Molecular Biology
New York Medical College
Valhalla, NY 10595
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.
Post Graduate Studies
Graduate Degree: Ph.D.
Graduate Degree Institution: Harvard University
Undergraduate Institution: Hollins College
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.