Kostyantyn D. Bobyk, Ph.D. - Publications

Affiliations: 
2010 Department of Chemistry and Biochemistry University of Oklahoma, Norman, OK, United States 
Area:
Biochemistry

6 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
2015 Bobyk KD, Ballou DP, Rokita SE. Rapid kinetics of dehalogenation promoted by iodotyrosine deiodinase from human thyroid. Biochemistry. 54: 4487-94. PMID 26151430 DOI: 10.1021/Acs.Biochem.5B00410  0.445
2012 Kumar VP, Thomas LM, Bobyk KD, Andi B, Cook PF, West AH. Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 51: 857-66. PMID 22243403 DOI: 10.1021/Bi201808U  0.649
2011 Karsten WE, Reyes ZL, Bobyk KD, Cook PF, Chooback L. Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics. 516: 67-74. PMID 21982920 DOI: 10.1016/J.Abb.2011.09.008  0.625
2011 Bobyk KD, Kim SG, Kumar VP, Kim SK, West AH, Cook PF. The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH. Archives of Biochemistry and Biophysics. 513: 71-80. PMID 21798231 DOI: 10.1016/J.Abb.2011.07.009  0.738
2010 Ekanayake DK, Andi B, Bobyk KD, West AH, Cook PF. Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts. The Journal of Biological Chemistry. 285: 20756-68. PMID 20427272 DOI: 10.1074/Jbc.M110.119826  0.388
2006 Mikolosko J, Bobyk K, Zgurskaya HI, Ghosh P. Conformational flexibility in the multidrug efflux system protein AcrA. Structure (London, England : 1993). 14: 577-87. PMID 16531241 DOI: 10.1016/J.Str.2005.11.015  0.311
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