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Corey M Johnson - Publications

Affiliations: 
University of Texas at Austin, Austin, Texas, U.S.A. 
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7 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
2022 Johnson CM, Fast W. On the kinetic mechanism of dimethylarginine dimethylaminohydrolase. Bioorganic & Medicinal Chemistry. 66: 116816. PMID 35598478 DOI: 10.1016/j.bmc.2022.116816  0.628
2011 Johnson CM, Monzingo AF, Ke Z, Yoon DW, Linsky TW, Guo H, Robertus JD, Fast W. On the mechanism of dimethylarginine dimethylaminohydrolase inactivation by 4-halopyridines. Journal of the American Chemical Society. 133: 10951-9. PMID 21630706 DOI: 10.1021/Ja2033684  0.53
2011 Johnson CM, Linsky TW, Yoon DW, Person MD, Fast W. Discovery of halopyridines as quiescent affinity labels: inactivation of dimethylarginine dimethylaminohydrolase. Journal of the American Chemical Society. 133: 1553-62. PMID 21222447 DOI: 10.1021/Ja109207M  0.528
2005 Johnson CM, Roderick SL, Cook PF. The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol. Archives of Biochemistry and Biophysics. 433: 85-95. PMID 15581568 DOI: 10.1016/J.Abb.2004.08.014  0.496
2004 Johnson CM, Huang B, Roderick SL, Cook PF. Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae. Biochemistry. 43: 15534-9. PMID 15581365 DOI: 10.1021/Bi048450H  0.399
2004 Johnson CM, Huang B, Roderick SL, Cook PF. Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae. Archives of Biochemistry and Biophysics. 429: 115-22. PMID 15313214 DOI: 10.1016/J.Abb.2004.06.006  0.389
2001 Tai CH, Burkhard P, Gani D, Jenn T, Johnson C, Cook PF. Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase. Biochemistry. 40: 7446-52. PMID 11412097 DOI: 10.1021/Bi015511S  0.464
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