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Structural heterogeneity of Caucasian N-acetyltransferase at the NAT1 gene locus.
Vatsis KP, Weber WW. Vatsis KP, et al. Arch Biochem Biophys. 1993 Feb 15;301(1):71-6. doi: 10.1006/abbi.1993.1116. Arch Biochem Biophys. 1993. PMID: 8442668
Abolition of oxygenase function, retention of NADPH oxidase activity, and emergence of peroxidase activity upon replacement of the axial cysteine-436 ligand by histidine in cytochrome P450 2B4.
Vatsis KP, Peng HM, Coon MJ. Vatsis KP, et al. Arch Biochem Biophys. 2005 Feb 1;434(1):128-38. doi: 10.1016/ Arch Biochem Biophys. 2005. PMID: 15629116
Ipso-substitution by cytochrome P450 with conversion of p-hydroxybenzene derivatives to hydroquinone: evidence for hydroperoxo-iron as the active oxygen species.
Vatsis KP, Coon MJ. Vatsis KP, et al. Arch Biochem Biophys. 2002 Jan 1;397(1):119-29. doi: 10.1006/abbi.2001.2665. Arch Biochem Biophys. 2002. PMID: 11747318
Replacement of active-site cysteine-436 by serine converts cytochrome P450 2B4 into an NADPH oxidase with negligible monooxygenase activity.
Vatsis KP, Peng HM, Coon MJ. Vatsis KP, et al. J Inorg Biochem. 2002 Sep 20;91(4):542-53. doi: 10.1016/s0162-0134(02)00438-5. J Inorg Biochem. 2002. PMID: 12237221
Individual variability in p-aminobenzoic acid N-acetylation by human N-acetyltransferase (NAT1) of peripheral blood.
Weber WW, Vatsis KP. Weber WW, et al. Among authors: vatsis kp. Pharmacogenetics. 1993 Aug;3(4):209-12. doi: 10.1097/00008571-199308000-00006. Pharmacogenetics. 1993. PMID: 8220441 No abstract available.
Nomenclature for N-acetyltransferases.
Vatsis KP, Weber WW, Bell DA, Dupret JM, Evans DA, Grant DM, Hein DW, Lin HJ, Meyer UA, Relling MV, et al. Vatsis KP, et al. Pharmacogenetics. 1995 Feb;5(1):1-17. doi: 10.1097/00008571-199502000-00001. Pharmacogenetics. 1995. PMID: 7773298 Review.
Structure of the gene for human butyrylcholinesterase. Evidence for a single copy.
Arpagaus M, Kott M, Vatsis KP, Bartels CF, La Du BN, Lockridge O. Arpagaus M, et al. Among authors: vatsis kp. Biochemistry. 1990 Jan 9;29(1):124-31. doi: 10.1021/bi00453a015. Biochemistry. 1990. PMID: 2322535
Molecular genetic basis of rapid and slow acetylation in mice.
Martell KJ, Vatsis KP, Weber WW. Martell KJ, et al. Among authors: vatsis kp. Mol Pharmacol. 1991 Aug;40(2):218-27. Mol Pharmacol. 1991. PMID: 1875909
Diverse point mutations in the human gene for polymorphic N-acetyltransferase.
Vatsis KP, Martell KJ, Weber WW. Vatsis KP, et al. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6333-7. doi: 10.1073/pnas.88.14.6333. Proc Natl Acad Sci U S A. 1991. PMID: 2068113 Free PMC article.
Slow acetylation in mice is caused by a labile and catalytically impaired mutant N-acetyltransferase (NAT2 9).
De Leon JH, Martell KJ, Vatsis KP, Weber WW. De Leon JH, et al. Among authors: vatsis kp. Drug Metab Dispos. 1995 Dec;23(12):1354-61. Drug Metab Dispos. 1995. PMID: 8689943
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