Department of Chemistry, Seoul National University
Publications
Equal contributors indicated with asterisk*
Corresponding Author indicated with bold
J. S. An*, H. Lee*, H. Kim, S. Woo, H. Nam, J. Lee, J. Y. Lee, S.-J. Nam, S. K. Lee, K.-B. Oh, S. Kim, D.-C. Oh "Discovery and Biosynthesis of Cihunamides, Macrocyclic Antibacterial RiPPs with a Unique C-N Linkage Formed by CYP450 Catalysis" Angew Chem Int Ed (2023) e202300998.
D. Seo, B. Koh, G.-e. Eom, H. W. Kim, S. Kim, "A dual gene-specific mutator system installs all transition mutations at similar frequencies in vivo" Nucleic Acids Res (2023) gkad266.
[DOI: doi.org/10.1093/nar/gkad266]
2023
H. Cho*, H. Lee*, K. T. Hong, H. Chung, I. Song, J.-S. Lee, S. Kim, "Bioinformatic expansion of borosins uncovers trans-acting peptide backbone N-methyltransferases in bacteria" Biochemistry (2022) 61(3), 183-194. [DOI: doi.org/10.1021/acs.biochem.1c00764]
G.-e. Eom, H. Lee, S. Kim, "Development of a genome-targeting mutator for the adaptive evolution of microbial cells" Nucleic Acids Res (2022) gkab1244 [DOI: 10.1093/nar/gkab1244]
2022
I. Song, Y. Kim, J. Yu, S. Y. Go, H. G. Lee, W. J. Song, S. Kim, "Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB" Nat Chem Biol (2021)[DOI: doi.org/10.1038/s41589-021-00855-x]
H. Park, S. Kim, "Gene-specific mutagenesis enables rapid continuous evolution of enzymes in vivo" Nucleic Acids Res (2021) gkaa1231 [DOI: 10.1093/nar/gkaa1231]
2021
H. Cho, Y. Choi, K. Min, J.B. Son, H. Park, H.H. Lee, S. Kim, "Over-activation of a Nonessential Bacterial Protease DegP as an Antibiotic Strategy" Commun Biol (2020) 3, 547[DOI: 10.1038/s42003-020-01266-9]
H. Lee, M. Choi, J.-U. Park, H. Roh, S. Kim, "Genome Mining Reveals High Topological Diversity of ω-Ester Containing Peptides and Divergent Evolution of ATP-Grasp Macrocyclases" J Am Chem Soc (2020) 142(6), 3013-3023 [DOI: 10.1021/jacs.9b12076]
C. Lee, H. Lee, J.-U. Park, S. Kim, "Introduction of Bifunctionality into the Multidomain Architecture of the ω-Ester-Containing Peptide Plesiocin" Biochemistry (2020) 59(3), 285-289 [DOI: 10.1021/acs.biochem.9b00803]
2020
H. Roh, Y. Han, H. Lee, S. Kim, "A topologically distinct modified peptide with multiple bicyclic core motifs expands the diversity of microviridin‐like peptides." Chembiochem (2019) 20(8), 1051-1059 [DOI: 10.1002/cbic.201800678]
2019
G.-e. Eom, S. Kim, "Identification of Nucleophilic Probes for Protease-Mediated Transpeptidation." Molecules (2018) 23, 2109 [DOI: 10.3390/molecules23092109]
S. Kim*, I. Song*, G. Eom, S. Kim, "A small periplasmic protein with a hydrophobic C-terminal residue enhances DegP proteolysis as a suicide activator." J Bacteriol (2018) 200, e00519-17 *These authors contributed equally [DOI: 10.1128/JB.00519-17]
2018
H. Park*, Y. Kim*, C. Choi, S. Kim, "Tripodal lipoprotein variants with C-terminal hydrophobic residues allosterically modulate activity of the DegP protease." J Mol Biol (2017) 429, 3090-3101 [DOI: 10.1016/j.jmb.2017.09.011]
H. Lee, Y. Park, S. Kim, "Enzymatic Cross-Linking of Side Chains Generates a Modified Peptide with Four Hairpin-like Bicyclic Repeats." Biochemistry (2017) 56, 4927-4930 [DOI: 10.1021/acs.biochem.7b00808]
2017
S. Kim, R.T. Sauer, “Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress.” Genes Dev (2014) 28, 902-911
[DOI: 10.1101/gad.238394.114]
S. Kim, R.T. Sauer, “Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival.” Proc Natl Acad Sci USA (2012) 109, 7263-8 [DOI: 10.1073/pnas.1204791109]
S. Kim, R.A. Grant, R.T. Sauer, “Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages.” Cell (2011) 145, 67-78 [DOI: 10.1016/j.cell.2011.02.024]
C.L. Hagan*, S. Kim*, D. Kahne, “Reconstitution of outer membrane protein assembly from purified components.” Science (2010) 328, 890-892 [DOI: 10.1126/science.1188919]
S. Kim, J.C. Malinverni, P. Sliz, T.J. Silhavy, S.C. Harrison, D. Kahne, “Structure and function of an essential component of the outer membrane protein assembly machine.” Science (2007) 317, 961-964 [DOI: 10.1126/science.1143993]