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Here is a link to Google Scholar Citations:

* indicate (co-)corresponding authorship.

  • Paul, D., Mu, H., Zhao, H., Ouerfelli, O., Jeffery, P.D., Broyde, S., Min, J. H*., Structure and mechanism of pyrimidine-pyrimidone (6-4) photoproduct recognition by the Rad4/XPC nucleotide excision repair complex. Nucleic Acids Research 47, 6015-6028 (2019), noted as a Breakthrough paper
  • Chakraborty, S., Steinbach, P.J., Paul, D., Mu, H., Broyde, S., Min, J.H.*, & Ansari, A., Enhanced spontaneous DNA twisting/bending fluctuations unveiled by fluorescence lifetime distributions promote mismatch recognition by the Rad4 nucleotide excision repair complex. Nucleic Acids Research 46 (3), 1240-1255 (2018).
  • Mu, H., Geacintov, N.E., Min, J.H., Zhang, Y., & Broyde, S., The nucleotide excision repair lesion-recognition protein Rad4 captures a pre-flipped partner base in a benzo[a]pyrene-derived DNA lesion: how structure impacts the binding pathway. Chemical Research in Toxicology (2017).
  • Kong, M., Liu, L., Chen, X., Driscoll, K.I., Mao, P., Bohm, S., Kad, N.M., Watkins, S.C., Bernstein, K.A., Wyrick, J.J., Min, J.H.*, & Van Houten, B., Single-Molecule Imaging Reveals that Rad4 Employs a Dynamic DNA Damage Recognition Process. Molecular Cell 64 (2), 376-387 (2016).
  • Velmurugu, Y., Chen, X., Slogoff Sevilla, P., Min, J.H.* & Ansari, A., Twist-open mechanism of DNA damage recognition by Rad4/XPC nucleotide excision repair complex, Proceedings of the National Academy of Sciences of the United States of America 113 (16), E2296-2305 (2016).
    – Recommended by F1000
  • Shafirovich, V., Kropachev, K., Anderson, T., Liu, Z., Kolbanovskiy, M., Martin, B.D., Sugden, K., Shim, Y., Chen, X., Min, J.H., & Geacintov, N.E., Base and Nucleotide Excision Repair of Oxidatively Generated Guanine Lesions in DNA. Journal of Biological Chemistry 291 (10), 5309-5319 (2016).
  • Puumalainen, M.R., Ruthemann, P., Min, J.H.*, & Naegeli, H., Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation. Cellular and Molecular Life Sciences 73 (3), 547-566 (2016).
  • Chen, X., Velmurugu, Y., Zheng, G., Park, B., Shim, Y., Kim, Y., Liu, L., Van Houten, B., He, C., Ansari, A., & Min, J.H.*, Kinetic gating mechanism of DNA damage recognition by Rad4/XPC. Nature Communications 6, 5849 (2015).
    – Highlighted in Science 360, the NSF News site (
    – Science Daily (
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    – Biology News Net (
    – SciGuru Science News (
    – Chicago Biomedical Consortium’s Science Spotlight (
    – UIC News (;
  • Lee, Y.C., Cai, Y., Mu, H., Broyde, S., Amin, S., Chen, X., Min, J.H., & Geacintov, N.E., The relationships between XPC binding to conformationally diverse DNA adducts and their excision by the human NER system: Is there a correlation? DNA Repair (Amst) 19, 55-63 (2014).
  • Koh-Stenta, X., Joy, J., Poulsen, A., Li, R., Tan, Y., Shim, Y., Min, J.H., Wu, L., Ngo, A., Peng, J., Seetoh, W.G., Cao, J., Wee, J.L., Kwek, P.Z., Hung, A., Lakshmanan, U., Flotow, H., Guccione, E., & Hill, J., Characterization of the histone methyltransferase PRDM9 utilising biochemical, biophysical and chemical biology techniques. Biochemical Journal 461 (2), 323-334 (2014).
  • Zhang, L., Szulwach, K.E., Hon, G.C., Song, C.X., Park, B., Yu, M., Lu, X., Dai, Q., Wang, X., Street, C.R., Tan, H., Min, J.H., Ren, B., Jin, P., & He, C., Tet-mediated covalent labelling of 5-methylcytosine for its genome-wide detection and sequencing. Nature Communications 4, 1517 (2013).
  • Krasikova, Y.S., Rechkunova, N.I., Maltseva, E.A., Pestryakov, P.E., Petruseva, I.O., Sugasawa, K., Chen, X., Min, J.H., & Lavrik, O.I., Comparative analysis of interaction of human and yeast DNA damage recognition complexes with damaged DNA in nucleotide excision repair. Journal of Biological Chemistry 288 (15), 10936-10947 (2013).
  • Krasikova, Y.S., Rechkunova, N.I., Maltseva, E.A., Anarbaev, R.O., Pestryakov, P.E., Sugasawa, K., Min, J.H., & Lavrik, O.I., Human and yeast DNA damage recognition complexes bind with high affinity DNA structures mimicking in size transcription bubble. Journal of Molecular Recognition 26 (12), 653-661 (2013).
  • Shim, Y., Duan, M.R., Chen, X., Smerdon, M.J., & Min, J.H.*, Polycistronic coexpression and nondenaturing purification of histone octamers. Analytical Biochemistry 427 (2), 190-192 (2012).
  • Yu, M., Hon, G.C., Szulwach, K.E., Song, C.X., Zhang, L., Kim, A., Li, X., Dai, Q., Shen, Y., Park, B., Min, J.H., Jin, P., Ren, B., & He, C., Base-Resolution Analysis of 5-Hydroxymethylcytosine in the Mammalian Genome. Cell 149 (6), 1368-1380 (2012).
  • Min, J. H. and Pavletich, N. P. Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature 449, 570-575 (2007).
    – Highlighted in News and Views: Sugasawa, K. and Hanaoka, F. Struct. Mol. Biol. 14, 887-888 (2007).
    – Highlighted in Preview: Scharer, O. D. Mol. Cell 28, 184-186 (2007).
  • Yang, H., Ivan, M., Min, J. H., Kim, W. Y., and Kaelin, W. G., Jr. Analysis of von Hippel-Lindau hereditary cancer syndrome: implications of oxygen sensing. Methods in Enzymology 381, 320-335 (2004).
  • Min, J. H., Yang, H., Ivan, M., Gertler, F., Kaelin, W. G., Jr., and Pavletich, N. P. Structure of an HIF-1a–pVHL complex: hydroxyproline recognition in signaling. Science 296, 1886-1889 (2002).
  • Min, J. H., Wilder, C., Aoki, J., Arai, H., Inoue, K., Paul, L., and Gelb, M. H. Platelet-activating factor acetylhydrolases: broad substrate specificity and lipoprotein binding does not modulate the catalytic properties of the plasma enzyme. Biochemistry 40, 4539-4549 (2001).
  • Gelb, M. H., Min, J. H., and Jain, M. K. Do membrane-bound enzymes access their substrates from the membrane or aqueous phase: interfacial versus non-interfacial enzymes. Biochimica Biophysica Acta 1488, 20-27 (2000).
  • Min, J. H., Jain, M. K., Wilder, C., Paul, L., Apitz-Castro, R., Aspleaf, D. C., and Gelb, M. H. Membrane-bound plasma platelet activating factor acetylhydrolase acts on substrate in the aqueous phase. Biochemistry 38, 12935-12942 (1999).