PUBLICATIONS

2021

1. Moiani, D., Link, T.M., Brosey, C.A., Katsonis, P., Lichtarge, O., Kim, Y., Joachimiak, A., Ma, Z., Kim, I.K., Ahmed, Z., Jones, D.E., Tsutakawa, S.E., and Tainer, J.A. (2021) An efficient chemical screening method for structure-based inhibitors to nucleic acid enzymes targeting the DNA repair-replication interface and SARS CoV-2. Methods in Enzymology. in press.

2. Kasson, S., Dharmapriya, N., and Kim, I.K. (2021) Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes. PLoS Onein press.

3. Yang, C.S., Jividen, K., Kamata, T., Dworak, N., Oostdyk, L., Remlein, B., Pourfarjam, Y., Kim, I.K., Du, K.P., Abbas, T., Sherman, N.E., Wotton, D., and Paschal, B.M. (2021) Androgen signaling uses a writer and a reader of ADP-ribosylation to regulate protein complex assembly. Nature Communications. In press (IF: 14.92).

4. Ma, Z., Pourfarjam, Y., and Kim, I.K. (2021). Reconstitution and functional characterization of SARS-CoV-2 proofreading complex. Protein Expression and Purification. In press.

5. Pourfarjam, Y., Ma, Z., Kurinov, I., Moss, J., and Kim, I.K. (2021) Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 (ARH3) reveals the basis of metal selectivity and different roles for the two Mg ions. Journal of Biological Chemistry. in press.

6. Hammel, M., Rashid, I., Sverzhinsky, A., Pourfarjam, Y., Tsai, M.S., Ellenberger, T., Pascal, J.M., Kim, I.K.#, Tainer, J.A.#, and Tomkinson, A.E.# (2021) An atypical BRCT-BRCT interaction with human DNA Ligase IIIa compacts the XRCC1 scaffold protein within a flexible DNA repair complex. Nucleic Acids Research. 49(1), 306-321, PMCID: PMC7797052 (IF: 16.97)

(#: Co-corresponding author)


2020

1. Pourfarjam, Y., Kasson, S., Tran, L., Ho, C. and Kim, I.K. (2020) PARG has a robust endo-glycohydrolase activity that releases protein-free poly(ADP-ribose) chains. Biochemical and Biophysical Research Communications. 527(3), 818-823, PMID: 32439163.


2019

1. Houl, J.H., Ye, Z., Brosey, C.A., Balapiti-Modarage, L.P.F., Namjoshi, S., Bacolla, A., Laverty, D., Walker, B.L., Pourfarjam, Y., Warden, L.S., Chinnam, N.B., Moiani, D., Stegeman, R.A., Chen, M.K., Hung, M.C., Nagel, Z.D., Ellenberger, T., Kim, I.K.#, Jones, D.E., Ahmed, Z.# and Tainer, J.A.# (2019) Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death. Nature Communications. 10(1), 5654, PMCID: PMC6906431. (IF: 14.92)

(#: Co-corresponding author)


2018

1. Pourfarjam, Y., Ventura, J., Kurinov, I., Cho, A., Moss, J., and Kim, I.K. (2018). Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. Journal of Biological Chemistry. 293, 12350-12359. 


2015

1. Kim, I.K.#, Stegeman, R.A., Brosey, C.A., and 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. Journal of Biological Chemistry. 290, 3775-3783 

(#: Co-corresponding author)

2. Cheruiyot, A*, Paudyal, S.C.*, Kim, I.K.*, Sparks, M., Ellenberger, T., Helen Piwnica-Worms, and You, Z.  (2015). Poly(ADP-ribose)-binding promotes Exo1 damage recruitment and suppresses its nuclease activities. DNA Repair (Amst)35, 106-115 (*: Co-first author)

3. Kukshal, V., Kim, I.K., Hura, G.L., Tomkinson, A., Tainer, J.A., and Ellenberger, T. (2015). Human DNA ligase III bridges two DNA ends to promote specific intermolecular end joining. Nucleic Acids Research43, 7021-7031.

4. Chen, X, Kim, I.K., Honaker, Y. Paudyal, S.C., Koh, W.K., Sparks, M., Li, S., Piwnica-Worms, H., Ellenberger, T., and You, Z. (2015). 14-3-3 Proteins restrain the Exo1 nuclease to prevent over-resection. Journal of Biological Chemistry. 290, 12300-12312.


2012

1. Kim, I.K., Kiefer, J.R., Ho, C.M.W., Stegeman, R.A., Classen, S., Tainer, J.A., and Ellenberger, T. (2012). Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element. Nature Structural & Molecular Biology. 19, 653-656.

W© In-Kwon Kim, Department of Chemistry, University of Cincinnati 2016