In-kwon Kim
Assistant Professor
Department of Chemistry
University of Cincinnati
United States of America
Biography
In-Kwon Kim is an Assistant Professor at the University of Cincinnati. He is a structural biochemist with research interests in poly(ADP-ribose) metabolism and signaling, DNA damage response, nucleic acid enzymology, and cancer drug discovery. After completing a B.S. degree from Seoul National University in 1998, he obtained his M.Sc (2000; Microbiology) and Ph.D. (2005; Biophysics and Structural Biology) degree under the direction of Prof. Sa-Ouk Kang from Seoul National University. In 2006, he joined the research group of Prof. Tom Ellenberger at Washington University School of Medicine as a post-doc and was promoted into (Research) Assistant Professor in 2012.
Research Interest
His research was focused on the structure, mechanism, and drug discovery of key enzymes in poly(ADP-ribose) metabolism and DNA repair. He also worked in the Washington University Drug Discovery Program, led by Prof. Michael Holtzman. He joined the faculty at University of Cincinnati in 2016 as part of the Cancer Cluster Hiring Initiative and continues his research. Mechanism and pharmacological control of Poly(ADP-ribose) turnover and signaling Nucleic acid enzymology in DNA damage response Cancer drug discovery through high-throughput screening
Publications
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Cheruiyot, A*, Paudyal, S.C.*, Kim, I.K.*, Sparks, M., Ellenberger, T., Helen Piwnica-Worms, & You, Z. (2015). Poly(ADP-ribose)-binding promotes Exo1 damage recruitment and suppresses its nuclease activities. DNA repair (Amst), 35, 106-115.
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Kukshal, V., Kim, I.K., Hura, G.L., Tomkinson, A., Tainer, J.A., & Ellenberger, T. (2015). Human DNA ligase III bridges two DNA ends to promote specific intermolecular end joining. Nucleic Acid Res., 43, 7021-7031.
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Kim, I.K.**, Stegeman, R.A., Brosey, C.A., & Ellenberger, T.** (2015). A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase. J. Biol. Chem., 290, 3775-3783.
