Sooim Shin, Ph.D. - Publications

Affiliations: 
2011 The University of Mississippi Medical Center, Jackson, MS, United States 
Area:
Biochemistry, General Biophysics

20 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
2020 Lee H, Ko E, Shin S, Choi M, Kim KT. Differential mitochondrial dysregulation by exposure to individual organochlorine pesticides (OCPs) and their mixture in zebrafish embryos. Environmental Pollution (Barking, Essex : 1987). 277: 115904. PMID 33714130 DOI: 10.1016/j.envpol.2020.115904  0.52
2020 Ko E, Um MY, Choi M, Han T, Kim IH, Shin S. Seed Improves Pancreatic Mitochondrial Function Leading to Recovery of Glucose Metabolism. The American Journal of Chinese Medicine. 1-15. PMID 32329641 DOI: 10.1142/S0192415X20500317  0.52
2020 Ko E, Choi M, Shin S. Bottom-line mechanism of organochlorine pesticides on mitochondria dysfunction linked with type 2 diabetes. Journal of Hazardous Materials. 393: 122400. PMID 32135367 DOI: 10.1016/J.Jhazmat.2020.122400  0.52
2020 Nam H, Hwang BJ, Choi DY, Shin S, Choi M. Tobacco Etch Virus (TEV) protease with multiple mutations to improve solubility and reduce self-cleavage exhibits enhanced enzymatic activity. Febs Open Bio. PMID 32129006 DOI: 10.1002/2211-5463.12828  0.52
2020 Ko E, Kim D, Kim K, Choi M, Shin S. The action of low-doses of persistent organic pollutants (POPs) on mitochondrial function in zebrafish eyes and comparison with hyperglycemia to identify a link between POPs and diabetes. Toxicology Mechanisms and Methods. 1-29. PMID 31948334 DOI: 10.1080/15376516.2020.1717704  0.52
2015 Shin S, Feng M, Li C, Williamson HR, Choi M, Wilmot CM, Davidson VL. A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent Fe(II)/Fe(III) state and enhances charge resonance stabilization of the bis-Fe(IV) state. Biochimica Et Biophysica Acta. 1847: 709-16. PMID 25896561 DOI: 10.1016/J.Bbabio.2015.04.008  0.52
2014 Shin S, Choi M, Williamson HR, Davidson VL. A simple method to engineer a protein-derived redox cofactor for catalysis. Biochimica Et Biophysica Acta. 1837: 1595-601. PMID 24858537 DOI: 10.1016/J.Bbabio.2014.05.354  0.52
2014 Shin S, Yukl ET, Sehanobish E, Wilmot CM, Davidson VL. Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG. Biochemistry. 53: 1342-9. PMID 24517455 DOI: 10.1021/Bi5000349  0.52
2014 Sehanobish E, Shin S, Sanchez-Amat A, Davidson VL. Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase. Febs Letters. 588: 752-6. PMID 24462691 DOI: 10.1016/J.Febslet.2014.01.021  0.52
2014 Shin S, Davidson VL. MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis. Archives of Biochemistry and Biophysics. 544: 112-8. PMID 24144526 DOI: 10.1016/J.Abb.2013.10.004  0.52
2013 Shin S, Feng M, Davidson VL. Mutation of Trp(93) of MauG to tyrosine causes loss of bound Ca(2+) and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis. The Biochemical Journal. 456: 129-37. PMID 24024544 DOI: 10.1042/Bj20130981  0.52
2013 Abu Tarboush N, Yukl ET, Shin S, Feng M, Wilmot CM, Davidson VL. Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG. Biochemistry. 52: 6358-67. PMID 23952537 DOI: 10.1021/Bi400905S  0.52
2013 Yukl ET, Liu F, Krzystek J, Shin S, Jensen LM, Davidson VL, Wilmot CM, Liu A. Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 110: 4569-73. PMID 23487750 DOI: 10.1073/Pnas.1215011110  0.52
2012 Abu Tarboush N, Shin S, Geng J, Liu A, Davidson VL. Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity. Febs Letters. 586: 4339-43. PMID 23127557 DOI: 10.1016/J.Febslet.2012.10.044  0.52
2012 Choi M, Shin S, Davidson VL. Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex. Biochemistry. 51: 6942-9. PMID 22897160 DOI: 10.1021/Bi300817D  0.52
2012 Chen Y, Naik SG, Krzystek J, Shin S, Nelson WH, Xue S, Yang JJ, Davidson VL, Liu A. Role of calcium in metalloenzymes: effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG. Biochemistry. 51: 1586-97. PMID 22320333 DOI: 10.1021/Bi201575F  0.52
2011 Shin S, Feng M, Chen Y, Jensen LM, Tachikawa H, Wilmot CM, Liu A, Davidson VL. The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis. Biochemistry. 50: 144-50. PMID 21128656 DOI: 10.1021/Bi101819M  0.52
2010 Shin S, Abu Tarboush N, Davidson VL. Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase. Biochemistry. 49: 5810-6. PMID 20540536 DOI: 10.1021/Bi1004969  0.52
2009 Shin S, Lee S, Davidson VL. Suicide inactivation of MauG during reaction with O(2) or H(2)O(2) in the absence of its natural protein substrate. Biochemistry. 48: 10106-12. PMID 19788236 DOI: 10.1021/Bi901284E  0.52
2009 Lee S, Shin S, Li X, Davidson VL. Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry. 48: 2442-7. PMID 19196017 DOI: 10.1021/Bi802166C  0.52
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