Miyeon Kim, Ph.D. - Publications

Affiliations: 
2007 University of Virginia, Charlottesville, VA 
Area:
magnetic resonance, membrane proteins

14 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2014 Chen Q, Zhuo Y, Kim M, Hanson SM, Francis DJ, Vishnivetskiy SA, Altenbach C, Klug CS, Hubbell WL, Gurevich VV. Self-association of arrestin family members. Handbook of Experimental Pharmacology. 219: 205-23. PMID 24292832 DOI: 10.1007/978-3-642-41199-1_11  0.92
2013 Song X, Seo J, Baameur F, Vishnivetskiy SA, Chen Q, Kook S, Kim M, Brooks EK, Altenbach C, Hong Y, Hanson SM, Palazzo MC, Chen J, Hubbell WL, Gurevich EV, et al. Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant. Cellular Signalling. 25: 2613-24. PMID 24012956 DOI: 10.1016/J.Cellsig.2013.08.022  0.92
2012 Kim M, Vishnivetskiy SA, Van Eps N, Alexander NS, Cleghorn WM, Zhan X, Hanson SM, Morizumi T, Ernst OP, Meiler J, Gurevich VV, Hubbell WL. Conformation of receptor-bound visual arrestin. Proceedings of the National Academy of Sciences of the United States of America. 109: 18407-12. PMID 23091036 DOI: 10.1073/Pnas.1216304109  0.92
2012 Mokdad A, Herrick DZ, Kahn AK, Andrews E, Kim M, Cafiso DS. Ligand-induced structural changes in the Escherichia coli ferric citrate transporter reveal modes for regulating protein-protein interactions. Journal of Molecular Biology. 423: 818-30. PMID 22982293 DOI: 10.1016/J.Jmb.2012.09.003  0.92
2011 Kim M, Hanson SM, Vishnivetskiy SA, Song X, Cleghorn WM, Hubbell WL, Gurevich VV. Robust self-association is a common feature of mammalian visual arrestin-1. Biochemistry. 50: 2235-42. PMID 21288033 DOI: 10.1021/Bi1018607  0.92
2010 Flores Jiménez RH, Do Cao MA, Kim M, Cafiso DS. Osmolytes modulate conformational exchange in solvent-exposed regions of membrane proteins. Protein Science : a Publication of the Protein Society. 19: 269-78. PMID 20014029 DOI: 10.1002/Pro.305  0.92
2010 Vishnivetskiy SA, Francis D, Van Eps N, Kim M, Hanson SM, Klug CS, Hubbell WL, Gurevich VV. The role of arrestin alpha-helix I in receptor binding. Journal of Molecular Biology. 395: 42-54. PMID 19883657 DOI: 10.1016/J.Jmb.2009.10.058  0.92
2009 Do Cao MA, Crouzy S, Kim M, Becchi M, Cafiso DS, Di Pietro A, Jault JM. Probing the conformation of the resting state of a bacterial multidrug ABC transporter, BmrA, by a site-directed spin labeling approach. Protein Science : a Publication of the Protein Society. 18: 1507-20. PMID 19479721 DOI: 10.1002/Pro.141  0.92
2008 Xu Q, Kim M, Ho KW, Lachowicz P, Fanucci GE, Cafiso DS. Membrane hydrocarbon thickness modulates the dynamics of a membrane transport protein. Biophysical Journal. 95: 2849-58. PMID 18586842 DOI: 10.1529/Biophysj.108.133629  0.92
2008 Kim M, Xu Q, Murray D, Cafiso DS. Solutes alter the conformation of the ligand binding loops in outer membrane transporters. Biochemistry. 47: 670-9. PMID 18092811 DOI: 10.1021/Bi7016415  0.92
2007 Kim M, Fanucci GE, Cafiso DS. Substrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved. Proceedings of the National Academy of Sciences of the United States of America. 104: 11975-80. PMID 17606918 DOI: 10.1073/Pnas.0702172104  0.92
2006 Xu Q, Ellena JF, Kim M, Cafiso DS. Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance. Biochemistry. 45: 10847-54. PMID 16953570 DOI: 10.1021/Bi061051X  0.92
2006 Kim M, Xu Q, Fanucci GE, Cafiso DS. Solutes modify a conformational transition in a membrane transport protein. Biophysical Journal. 90: 2922-9. PMID 16443663 DOI: 10.1529/Biophysj.105.078246  0.92
2003 Fanucci GE, Coggshall KA, Cadieux N, Kim M, Kadner RJ, Cafiso DS. Substrate-induced conformational changes of the periplasmic N-terminus of an outer-membrane transporter by site-directed spin labeling. Biochemistry. 42: 1391-400. PMID 12578351 DOI: 10.1021/Bi027120Z  0.92
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