Moonsung Choi, Ph.D. - Publications

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

16 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
2021 Han T, Ko E, Kim M, Choi M, Lee C, Kim IH, Shin S, Um MY. Mori Ramulus Inhibits Pancreatic β-Cell Apoptosis and Prevents Insulin Resistance by Restoring Hepatic Mitochondrial Function. Antioxidants (Basel, Switzerland). 10. PMID 34204891 DOI: 10.3390/antiox10060901  0.6
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  0.6
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  0.6
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  0.6
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  0.6
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  0.6
2019 Jeoung S, Shin S, Choi M. Copper-binding energetics of amicyanin in different folding states. Metallomics : Integrated Biometal Science. PMID 31830170 DOI: 10.1039/C9Mt00261H  0.6
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 Dow BA, Sukumar N, Matos JO, Choi M, Schulte A, Tatulian SA, Davidson VL. The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site. Archives of Biochemistry and Biophysics. 550: 20-7. PMID 24704124 DOI: 10.1016/J.Abb.2014.03.010  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
2011 Sukumar N, Choi M, Davidson VL. Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper. Journal of Inorganic Biochemistry. 105: 1638-44. PMID 22071089 DOI: 10.1016/J.Jinorgbio.2011.08.002  0.52
2011 Choi M, Sukumar N, Mathews FS, Liu A, Davidson VL. Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface. Biochemistry. 50: 1265-73. PMID 21268585 DOI: 10.1021/Bi101794Y  0.52
2011 Choi M, Davidson VL. Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes. Metallomics : Integrated Biometal Science. 3: 140-51. PMID 21258692 DOI: 10.1039/C0Mt00061B  0.52
2009 Choi M, Sukumar N, Liu A, Davidson VL. Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine. Biochemistry. 48: 9174-84. PMID 19715303 DOI: 10.1021/Bi900836H  0.52
2008 Ma JK, Lee S, Choi M, Bishop GR, Hosler JP, Davidson VL. The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyanin. Journal of Inorganic Biochemistry. 102: 342-6. PMID 17986390 DOI: 10.1016/J.Jinorgbio.2007.09.007  0.52
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