For full publication by Prof. Min and the Min group, click below:

https://orcid.org/0000-0002-4221-9321

Here is a link to Google Scholar Citations:

https://scholar.google.com/citations?user=HuGhZm0AAAAJ

* indicate Min as a (co-)corresponding author.

• Tavakoli, A. & Min, J. H.*, Photochemical modifications for DNA/RNA oligonucleotides. RSC Adv 12, 6484-6507 (2022). doi:10.1039/d1ra05951c

• Paul, D., Mu, H., Tavakoli, A., Dai, Q., Chakraborty, S., He, C., Ansari, A., Broyde, S. & Min, J. H.* Impact of DNA sequences on DNA ‘opening’ by the Rad4/XPC nucleotide excision repair complex. DNA Repair (Amst) 107, 103194 (2021). doi:10.1016/j.dnarep.2021.103194
• Van Eeuwen, T., Shim, Y., Kim, H. J., Zhao, T., Basu, S., Garcia, B. A., Kaplan, C., Min, J. H.*; Murakami, K., Structure of TFIIH/Rad4-Rad23-Rad33 in damaged DNA opening in Nucleotide Excision Repair. Nature Communications 12, 3338 (2021)
  https://doi.org/10.1038/s41467-021-23684-x
• Tavakoli, A.; Paul, D.; Mu, H.; Kuchlyan, J.; Baral, S.; Ansari, A.; Broyde, S.; Min, J. H.*, Light-induced modulation of DNA recognition by the Rad4/XPC damage sensor protein. RSC Chemical Biology 2, 523-536 (2021) https://doi.org/10.1039/D0CB00192A
• Paul, D., Mu, H., Tavakoli, A., Dai, Q., Chen, X., Chakraborty, S., He, C., Ansari, A., Broyde, S. & Min, J. H.* Tethering-facilitated DNA ‘opening’ and complementary roles of beta-hairpin motifs in the Rad4/XPC DNA damage sensor protein. Nucleic Acids Research 48, 12348-12364, (2020)
  https://doi.org/10.1093/nar/gkaa909
• Feher, K. M., Kolbanovskiy, A., Durandin, A., Shim, Y., Min, J. H., Lee, Y. C., Shafirovich, V., Mu, H., Broyde, S. & Geacintov, N. E. The DNA damage-sensing NER repair factor XPC-RAD23B does not recognize bulky DNA lesions with a missing nucleotide opposite the lesion. DNA Repair (Amst) 96, 102985, (2020) doi:10.1016/j.dnarep.2020.102985
• Kolbanovskiy, M., Shim, Y., Min, J. H., Geacintov, N. E. & Shafirovich, V. Inhibition of Excision of Oxidatively Generated Hydantoin DNA Lesions by NEIL1 by the Competitive Binding of the Nucleotide Excision Repair Factor XPC-RAD23B. Biochemistry 59, 1728-1736, (2020)
  doi:10.1021/acs.biochem.0c00080
• 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)
  DOI: 10.1093/nar/gkz359
  – Noted as a Breakthrough paper and additionally featured in:
  • http://www.narbreakthrough.com/2019/05/21/structure-and-mechanism-of-pyrimidine-pyrimidone-6-4-photoproduct-recognition-by-the-rad4xpc-nucleotide-excision-repair-complex/
  • https://www.baylor.edu/mediacommunications/news.php?action=story&story=211125
  • https://www.news-medical.net/news/20190715/Research-sheds-light-on-sun-induced-DNA-damage-and-repair.aspx
  • https://bioengineer.org/study-gives-insight-into-sun-induced-dna-damage-and-cell-repair/
  • https://scienmag.com/study-gives-insight-into-sun-induced-dna-damage-and-cell-repair/
  • http://www.healthnewsdigest.com/news/Research_270/Better-Understanding-of-How-Sunlight-induced-DNA-Damage-Is-Initially-Recognized-for-Repair-in-Cells.shtml
  • https://www.sciencecodex.com/study-gives-insight-sun-induced-dna-damage-and-cell-repair-629480
  • https://www.sciencedaily.com/releases/2019/07/190714103138.htm
  • https://www.technologynetworks.com/genomics/news/gaining-insight-into-sun-induced-dna-damage-and-cell-repair-321716
  • https://phys.org/news/2019-07-insight-sun-induced-dna-cell.html
  • https://mp.weixin.qq.com/s/4_lHgidpV9jtRMeIl3tHeg
• 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).
  DOI: 10.1093/nar/gkx1216
• Liu, S. L., Wang, Z. G., Hu, Y., Xin, Y., Singaram, I., Gorai, S., Zhou, X., Shim, Y., Min, J. H., Gong, L. W., Hay, N., Zhang, J. & Cho, W. Quantitative Lipid Imaging Reveals a New Signaling Function of Phosphatidylinositol-3,4-Bisphophate: Isoform- and Site-Specific Activation of Akt. Mol. Cell 71, 1092-1104 e1095, (2018). DOI: 10.1016/j.molcel.2018.07.035
• 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).
  DOI: 10.1021/acs.chemrestox.7b00074
• 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).
  DOI: 10.1016/j.molcel.2016.09.005
• 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).
  DOI: 10.1073/pnas.1514666113
  – Recommended by F1000 http://f1000.com/prime/726259932?subscriptioncode=f6582524-7f78-4829-92fd-cfce44643643&utm_medium=email&utm_source=prime_ypp.
• 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).
  DOI: 10.1074/jbc.M115.693218
• 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).
  DOI: 10.1007/s00018-015-2075-z
• 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).
  DOI: 10.1038/ncomms6849
  – Science Daily (http://www.sciencedaily.com/releases/2015/01/150128141423.htm)
  – Phys.org (http://phys.org/news/2015-01-dna-stall-patrolling-molecule.html)
  – Biology News Net (http://www.biologynews.net/archives/2015/01/28/damaged_dna_may_stall_patrolling_molecule_to_initiate_repair.html)
  – SciGuru Science News (http://www.sciguru.org/newsitem/18318/damaged-dna-may-stall-patrolling-molecule-initiate-repair)
  – Chicago Biomedical Consortium’s Science Spotlight  (http://www.chicagobiomedicalconsortium.org/news/news_2015/news_2015_03.php)
  – UIC News (http://news.uic.edu/taking-a-closer-look-at-damaged-dna; http://news.uic.edu/damaged-dna-may-stall-patrolling-molecule-to-initiate-repair)
• 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).
  DOI: 10.1016/j.dnarep.2014.03.026
• 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).
  DOI: 10.1042/bj20140374 
• 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).
  DOI: 10.1038/ncomms2527
• 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). DOI: 10.1074/jbc.m112.444026 
• 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). DOI: 10.1002/jmr.2308
• 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).DOI: 10.1016/j.ab.2012.05.006
• 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).
  DOI: 10.1016/j.cell.2012.04.027
• Min, J. H. and Pavletich, N. P. Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature 449, 570-575 (2007).
  DOI: 10.1038/nature06155
  – Highlighted in News and Views: Sugasawa, K. and Hanaoka, F. Struct. Mol. Biol. 14, 887-888 (2007). DOI:10.1038/nsmb1007-887
  – Highlighted in Preview: Scharer, O. D. Mol. Cell 28, 184-186 (2007). DOI: 10.1016/j.molcel.2007.10.006
• 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).
  DOI: 10.1016/S0076-6879(04)81022-X
• 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).
  DOI: 10.1126/science.1073440
• 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).
  DOI: 10.1021/bi002600g
• 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).
  DOI: 10.1016/s1388-1981(00)00106-2 
• 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).
  DOI: 10.1021/bi991149u