Publications

publications

28. Bokyung Kim, Young Ho Ko, Jinbeom Si, Jongbum Na, Gabriella Ortore*, Grazia Chiellini*, and Jin Hae Kim* (2023) Thyroxine metabolite-derived 3-iodothyronamine (T1AM) and synthetic analogs as efficient suppressors of transthyretin amyloidosis, Comput. Struct. Biotechnol. J. 21, 4717. https://doi.org/10.1016/j.csbj.2023.09.028 

27. Hong-Guen Lee, Jin Hae Kim, Tumpa Gorai, Young Ho Ko, Haw-Young Kwon, Wooseong Chung, Ilha Hwang, Sungsu Lim, Yun Kyung Kim, Kwanwoo Shin, Young-Tae Chang*, Kimoon Kim*, Kyeng Min Park* (2022) Contagious Aggregation: Transmittable Protein Aggregation in Cellular Communities Initiated by Synthetic Cells, J. Am. Chem. Soc. 144, 5067. https://doi.org/10.1021/jacs.1c13545 

26. Wonjin Yang, Beom Soo Kim, Srinivasan Muniyappan, Young-Ho Lee, Jin Hae Kim*, Wookyung Yu* (2021) Aggregation-prone structural ensembles of transthyretin collected with regression analysis for NMR chemical shift, Front. Mol. Biosci. 8, 766830 (*Co-correspondence). https://doi.org/10.3389/fmolb.2021.766830 

25. Jin Hae Kim*, Hyokeun Park, Tae-Gon Kim, Hyunmi Lee, Shinae Jun, Eunha Lee, Woo Sung Jeon, Jaegwan Chung & In-Sun Jung* (2021) Facile and versatile ligand analysis method of colloidal quantum dot, Sci. Rep. 11, 19889 (*Co-correspondence). https://doi.org/10.1038/s41598-021-99358-x 

24. Srinivasan Muniyappan, Yuxi Lin, Young Ho Lee, Jin Hae Kim (2021) 17O NMR Spectroscopy: A Novel Probe for Characterizing Protein Structure and Folding, Biology (Basel) 10, 453. https://doi.org/10.3390/biology10060453 

23. Jin-Beom Si, Bokyung Kim, Jin Hae Kim (2021) Transthyretin misfolding, a fatal structural pathogenesis mechanism, Int. J. Mol. Sci. 22, 4429. https://doi.org/10.3390/ijms22094429 

22. Bokyung Kim, Young Ho Ko, Massimiliano Runfola, Simona Rapposelli, Gabriella Ortore*, Grazia Chiellini*, Jin Hae Kim* (2021) Diphenyl-methane based thyromimetic inhibitors for transthyretin amyloidosis, Int. J. Mol. Sci. 22, 3488 (*Co-correspondence). https://doi.org/10.3390/ijms22073488 

21. Federica Saponaro, Jin Hae Kim, Grazia Chiellini (2020) Transthyretin Stabilization: An Emerging Strategy for the Treatment of Alzheimer’s Disease?, Int. J. Mol. Sci. 21, 8672. https://doi.org/10.3390/ijms21228672 

20. Hisham S Alhajala, John L Markley, Jin Hae Kim, Mona M Al-Gizawiy, Kathleen M Schmainda, John S Kuo, Christopher R Chitambar (2020) The cytotoxicity of gallium maltolate in glioblastoma cells is enhanced by metformin through combined action on mitochondrial complex 1, Oncotarget 11, 1531. https://doi.org/10.18632/oncotarget.27567 

19. Ken Ogata, Dong-Su Ko, Changhoon Jung, Jun-Ho Lee, Soohwan Sul, Hee-Goo Kim, Jinah Seo, Jihyun Jang, Meiten Koh, Kihong Kim, Jin Hae Kim, In-Sun Jung, Min Sik Park, Koichi Takei, Shunsuke Saito, Shinya Wakita, Kimihiko Ito, Yoshimi Kubo, Kohei Uosaki, Seokgwang Doo, SungSoo Han, Jai Kwang Shin, Seongho Jeon (2019) Spontaneous pseudo-topological silicon quantization for redesigned Si-based Li-ion batteries, Nano Energy 56, 875-883. https://doi.org/10.1016/j.nanoen.2018.11.092 

18. Ken Ogata, Seongho Jeon, Dong-Su Ko, In-Sun Jung, Jin Hae Kim, Kimihiko Ito, Yoshimi Kubo, Koichi Takei, Shunsuke Saito, Y.-H. Cho, H. Park, J. Jang, H.-G. Kim, J.-H. Kim, Y. S. Kim, W. Choi, Meiten Koh, Kohei Uosaki, Seokgwang Doo, Y. Hwang, SungSoo Han (2018) Evolving affinity between Coulombic reversibility and hysteretic phase transformations in nano-structured silicon-based lithium-ion batteries, Nat. Commun. 9, 479. https://doi.org/10.1038/s41467-018-02824-w 

17. Dong Young Kim, Hosang Park, Woon Ih Choi, Basab Roy, Jinah Seo, Insun Park, Jin Hae Kim, Jong Hwan Park, Yoon-Sok Kang, Meiten Koh (2017) Ab initio study of the operating mechanisms of tris(trimethylsilyl)phosphite as a multifunctional additive for Li-ion batteries, J. Power Sources 355, 154-163. https://doi.org/10.1016/j.jpowsour.2017.04.062 

16. Javier Oroz*, Jin Hae Kim*, Bliss J. Chang, Markus Zweckstetter (2017) Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90, Nat. Struct. Mol. Biol. 24, 407-413 (*equal contribution). https://doi.org/10.1038/nsmb.3380 

15. Jin Hae Kim, Javier Oroz, Markus Zweckstetter (2016) Structure of monomeric transthyretin carrying the clinically important T119M mutation, Angew. Chem. Int. Ed. 55, 16168-16171. https://doi.org/10.1002/anie.201608516 

14. T. Reid Alderson, Jin Hae Kim, John L. Markley (2016) Dynamical structures of Hsp70 and Hsp70-Hsp40 complexes, Structure 24, 1014-1030. https://doi.org/10.1016/j.str.2016.05.011 

13. Jin Hae Kim, Jameson R. Bothe, T. Reid Alderson, and John L. Markley (2015) Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies, Biochim. Biophys. Acta 1853, 1416-1428. https://doi.org/10.1016/j.bbamcr.2014.11.020 

12. T. Reid Alderson, Jin Hae Kim, Kai Cai, Ronnie O. Frederick, Marco Tonelli, and John L. Markley (2014) The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations, Biochemistry 53, 7148-7159. https://doi.org/10.1021/bi5010552 

11. Jin Hae Kim, T. Reid Alderson, Ronnie O. Frederick, and John L. Markley (2014) Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe–S cluster biogenesis, J. Am. Chem. Soc. 136, 11586–11589. https://doi.org/10.1021/ja5055252 

10. Ziqi Dai, Jin Hae Kim, Marco Tonelli, Ibrahim K. Ali, and John L. Markley (2014) pH-induced conformational change of IscU at low pH correlates with protonation/deprotonation of two conserved histidine residues, Biochemistry 53, 5290–5297. https://doi.org/10.1021/bi500313t 

9. Jin Hae Kim*, Jameson R. Bothe*, Ronnie O. Frederick, Johneisa C. Holder, and John L. Markley (2014) Role of IscX in iron-sulfur cluster biogenesis in Escherichia coli, J. Am. Chem. Soc. 136, 7933-7942 (*equal contribution). https://doi.org/10.1021/ja501260h 

8. Jin Hae Kim, Ronnie O. Frederick, Nichole M. Reinen, Andrew T. Troupis, and John L. Markley (2013) [2Fe-2S]-ferredoxin binds directly to cysteine desulfurase and supplies electrons for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin, J. Am. Chem. Soc. 135, 8117-8120. https://doi.org/10.1021/ja401950a 

7. Kai Cai, Ronnie O. Frederick, Jin Hae Kim, Nichole M. Reinen, Marco Tonelli, and John L. Markley (2013) Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU), J. Biol. Chem. 288, 28755-28770. https://doi.org/10.1074/jbc.M113.482042 

6. John L. Markley, Jin Hae Kim, Ziqi Dai, Jameson R. Bothe, Kai Cai, Ronnie O. Frederick, and Marco Tonelli (2013) Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery, FEBS Lett. 587, 1172-1179. https://doi.org/10.1016/j.febslet.2013.01.003 

5. Jin Hae Kim, Marco Tonelli, Ronnie O. Frederick, Darius C.-F. Chow, and John L. Markley (2012) Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU), J. Biol. Chem. 287, 31406-31413. https://doi.org/10.1074/jbc.M112.352617   

4. Jin Hae Kim, Marco Tonelli, Taewook Kim, and John L. Markley (2012) Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli, Biochemistry 51, 5557-5563. https://doi.org/10.1021/bi300579p 

3. Jin Hae Kim, Marco Tonelli, and John L. Markley (2012) Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase, Proc. Natl. Acad. Sci. U.S.A. 109, 454-459. https://doi.org/10.1073/pnas.1114372109 

2. Woonghee Lee, Jin Hae Kim, W. Milo Westler, and John L. Markley (2011) PONDEROSA, an automated 3D-NOESY peak picking program, enables automated protein structure determination, Bioinformatics 27, 1727-1728. https://doi.org/10.1093/bioinformatics/btr200 

1. Jin Hae Kim, Anna K. Fuzery, Marco Tonelli, Dennis T. Ta, W. Milo Westler, Larry E. Vickery, and John L. Markley (2009) Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB, Biochemistry 48, 6062-6071. https://doi.org/10.1021/bi9002277