Vatsis KP[au] - Search Results

Year	Number of Results
1972	1
1973	1
1974	1
1975	1
1977	1
1978	2
1979	3
1980	1
1982	2
1989	1
1990	1
1991	2
1993	2
1994	1
1995	2
2000	1
2002	2
2004	1
2005	2
2022	0

1

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.

2

Hydroxylation by the hydroperoxy-iron species in cytochrome P450 enzymes.

Chandrasena RE, Vatsis KP, Coon MJ, Hollenberg PF, Newcomb M. Chandrasena RE, et al. Among authors: vatsis kp. J Am Chem Soc. 2004 Jan 14;126(1):115-26. doi: 10.1021/ja038237t. J Am Chem Soc. 2004. PMID: 14709076

3

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.

4

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 Free article.

5

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/j.abb.2004.10.015. Arch Biochem Biophys. 2005. PMID: 15629116

6

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

7

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

8

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

9

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

10

Oxidative aldehyde deformylation catalyzed by NADPH-cytochrome P450 reductase and the flavoprotein domain of neuronal nitric oxide synthase.

Vatsis KP, Coon MJ. Vatsis KP, et al. Biochem Biophys Res Commun. 2005 Dec 2;337(4):1107-11. doi: 10.1016/j.bbrc.2005.09.167. Epub 2005 Oct 5. Biochem Biophys Res Commun. 2005. PMID: 16226717

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