Publications

Google Scholar for Min-Sung Kim

  • I Chun, HJ Kim, S Hong, YG Kim, MS Kim (2023) Structural basis of DNA binding by the NAC transcription factor ORE1, a master regulator of plant senescence. Plant Communications 4 (3)
  • J Kim, JY Lee, SY Park, YJ Lee, MS Kim (2020) Crystal structure of human interleukin-2 in complex with TCB2, a new antibody-drug candidate with antitumor activity. Oncoimmunology 10 (1)
  • Notarangelo, L. D., Kim, M. S., Walter, J. E., and Lee, Y. N. (2016) Human RAG mutations: biochemistry and clinical implications. Nat Rev Immunol 16, 234-246 
  • Lapkouski, M., Chuenchor, W., Kim, M. S., Gellert, M., and Yang, W. (2015) Assembly Pathway and Characterization of the RAG1/2-DNA Paired and Signal-end Complexes. The Journal of biological chemistry 290, 14618-14625
  • Kim, M. S., Lapkouski, M., Yang, W., and Gellert, M. (2015) Crystal structure of the V(D)J recombinase RAG1-RAG2. Nature 518, 507-511
  • Lee, C. H., Kim, M. S., Chung, B. M. Leahy, D. J. & Coulombe, P. A. (2012) Structural basis for heteromeric assembly and perinuclear organization of keratin filaments, Nat Struct Mol Biol. 19, 707-715 
  • Kim, M. S., Saunders, A. M., Hamaoka, B. Y., Beachy, P. A., & Leahy, D. J. (2011) Structure of the protein core of the glypican Dally-like and localization of a region important for hedgehog signaling, Proc Natl Acad Sci U S A. 108, 13112-13117.
  • Williams, E. H., Pappano, W. N., Saunders, A. M., Kim, M. S., Leahy, D. J. & Beachy, P. A. (2010) Dally-like core protein and its mammalian homologues mediate stimulatory and inhibitory effects on Hedgehog signal response, Proc Natl Acad Sci U S A. 107, 5869-74.
  • Zaidman-Remy, A., Herve, M., Poidevin, M., Pili-Floury, S., Kim, M. S., Blanot, D., Oh, B. H., Ueda, R., Mengin-Lecreulx, D., and Lemaitre, B. (2006) The Drosophila amidase PGRP-LB modulates the immune response to bacterial infection. Immunity 24, 463-473.
  • Lim, J. H., Kim, M. S., Kim, H. E., Yano, T., Oshima, Y., Aggarwal, K., Goldman, W. E., Silverman, N., Kurata, S. & Oh, B. H. (2006) Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins, J Biol Chem. 281, 8286-95.
  • Kim, M. S., Yi, M. J., Lee, K. H., Wagner, J., Munger, C., Kim, Y. G., Whiteway, M., Cygler, M., Oh, B. H. & Sacher, M. (2005) Biochemical and crystallographic studies reveal a specific interaction between TRAPP subunits Trs33p and Bet3p, Traffic. 6, 1183-95.
  • Woo, E. J., Kim, Y. G., Kim, M. S., Han, W. D., Shin, S., Robinson, H., Park, S. Y. & Oh, B. H. (2004) Structural mechanism for inactivation and activation of CAD/DFF40 in the apoptotic pathway, Mol Cell. 14, 531-9.
  • Kim, M. S., Shin, J., Lee, W., Lee, H. S. & Oh, B. H. (2003) Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture, J Biol Chem. 278, 28173-80.
  • Kim, M. S., Byun, M. & Oh, B. H. (2003) Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster, Nat Immunol. 4, 787-93.
  • Lee, H. S.*, Kim, M. S.*, Cho, H. S., Kim, J. I., Kim, T. J., Choi, J. H., Park, C., Lee, H. S., Oh, B. H. & Park, K. H. (2002) Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other, J Biol Chem. 277, 21891-7. *Equal contribution
  • Kim, M. S., Oh, H., Park, C. & Oh, B. H. (2001) Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli RbsD, a component of the ribose-transport system with unknown biochemical function, Acta Crystallogr D Biol Crystallogr. 57, 728-30.
  • Choi, G., Ha, N. C., Kim, M. S., Hong, B. H., Oh, B. H. & Choi, K. Y. (2001) Pseudoreversion of the catalytic activity of Y14F by the additional substitution(s) of tyrosine with phenylalanine in the hydrogen bond network of delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B, Biochemistry. 40, 6828-35.
  • Ha, N. C., Kim, M. S., Lee, W., Choi, K. Y. & Oh, B. H. (2000) Detection of large pKa perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes, J Biol Chem. 275, 41100-6.
  • Cha, S. S., Kim, M. S., Choi, Y. H., Sung, B. J., Shin, N. K., Shin, H. C., Sung, Y. C. & Oh, B. H. (1999) 2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity, Immunity. 11, 253-61.

 

Methods

  • Longo, P. A., Kavran, J. M., Kim, M. S., and Leahy, D. J. (2014) Single cell cloning of a stable mammalian cell line. Methods in enzymology 536, 165-172
  • P, A. L., Kavran, J. M., Kim, M. S., and Leahy, D. J. (2013) Generating mammalian stable cell lines by electroporation. Methods in enzymology 529, 209-226
  • Longo, P. A., Kavran, J. M., Kim, M. S., and Leahy, D. J. (2013) Transient mammaliancell transfection with polyethylenimine (PEI). Methods in enzymology 529, 227-240
  • Kim, M. S., and Leahy, D. (2013) Enzymatic deglycosylation of glycoproteins. Methods in enzymology 533, 259-263