메뉴 건너뛰기




Volumn 12, Issue 2, 2011, Pages 104-123

Regulation of phase II biotransformation enzymes by steroid hormones

Author keywords

Androgens; Cancer; Estrogens; Genetic polymorphism; Glucocorticoids; GLYAT; Nuclear receptors

Indexed keywords

ARYLAMINE ACETYLTRANSFERASE; BICALUTAMIDE; CATECHOL METHYLTRANSFERASE; DEXAMETHASONE; DRUG METABOLIZING ENZYME; FLUTAMIDE; GLUCOCORTICOID; GLUCURONOSYLTRANSFERASE; GLUTATHIONE TRANSFERASE; METRIBOLONE; MIFEPRISTONE; PROGESTERONE; SEX HORMONE; STEROID HORMONE; SULFOTRANSFERASE; THIOPURINE METHYLTRANSFERASE; VITAMIN D; XENOBIOTIC AGENT;

EID: 79952796042     PISSN: 13892002     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920011795016872     Document Type: Article
Times cited : (18)

References (249)
  • 1
    • 0034534895 scopus 로고    scopus 로고
    • Roles of glucuronidation and UDP-glucuronosyltransferases in xenobiotic bioactivation reactions
    • DOI 10.1016/S0009-2797(00)00198-8, PII S0009279700001988
    • Ritter, J. K. Roles of glucuronidation and UDP-glucuronosyltransferases in xenobiotic bioactivation reactions. Chem. Biol. Interact., 2000, 129(1-2), 171-193. (Pubitemid 32061059)
    • (2000) Chemico-Biological Interactions , vol.129 , Issue.1-2 , pp. 171-193
    • Ritter, J.K.1
  • 2
    • 0034534841 scopus 로고    scopus 로고
    • Sulfotransferases in the bioactivation of xenobiotics
    • DOI 10.1016/S0009-2797(00)00202-7, PII S0009279700002027
    • Glatt, H. Sulfotransferases in the bioactivation of xenobiotics. Chem Biol Interact, 2000, 129(1-2), 141-170. (Pubitemid 32061058)
    • (2000) Chemico-Biological Interactions , vol.129 , Issue.1-2 , pp. 141-170
    • Glatt, H.1
  • 4
    • 27944453968 scopus 로고    scopus 로고
    • Glutathione transferases: New functions
    • DOI 10.1016/j.sbi.2005.10.005, PII S0959440X05001922, Catalysis and Regulation/Proteins
    • Oakley, A. J. Glutathione transferases: New functions. Curr. Opin. Struct. Biol., 2005, 15(6), 716-723. (Pubitemid 41668529)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.6 , pp. 716-723
    • Oakley, A.J.1
  • 5
    • 77954762075 scopus 로고    scopus 로고
    • Functions and transcriptional regulation of adult human hepatic UDP-glucuronosyl-transferases (UGTs): Mechanisms responsible for interindividual variation of UGT levels
    • Bock, K. W. Functions and transcriptional regulation of adult human hepatic UDP-glucuronosyl-transferases (UGTs): Mechanisms responsible for interindividual variation of UGT levels. Biochem Pharmacol, 80(6), 771-777.
    • Biochem Pharmacol , vol.80 , Issue.6 , pp. 771-777
    • Bock, K.W.1
  • 7
    • 77952662988 scopus 로고    scopus 로고
    • Modulation of UDPglucuronosyltransferase activity by endogenous compounds
    • Ishii, Y.; Nurrochmad, A.; Yamada, H. Modulation of UDPglucuronosyltransferase activity by endogenous compounds. Drug Metab. Pharmacokinet., 25(2), 134-148.
    • Drug Metab. Pharmacokinet. , vol.25 , Issue.2 , pp. 134-148
    • Ishii, Y.1    Nurrochmad, A.2    Yamada, H.3
  • 8
    • 74549174924 scopus 로고    scopus 로고
    • Regulation of endobiotics glucuronidation by ligand-activated transcription factors: Physiological function and therapeutic potential
    • Verreault, M.; Kaeding, J.; Caron, P.; Trottier, J.; Grosse, L.; Houssin, E.; Paquet, S.; Perreault, M.; Barbier, O. Regulation of endobiotics glucuronidation by ligand-activated transcription factors: Physiological function and therapeutic potential. Drug Metab. Rev, 42(1), 106-118.
    • Drug Metab. Rev , vol.42 , Issue.1 , pp. 106-118
    • Verreault, M.1    Kaeding, J.2    Caron, P.3    Trottier, J.4    Grosse, L.5    Houssin, E.6    Paquet, S.7    Perreault, M.8    Barbier, O.9
  • 11
    • 0037819284 scopus 로고    scopus 로고
    • Pharmacogenomics of human UDP-glucuronosyltransferase enzymes
    • DOI 10.1038/sj.tpj.6500171
    • Guillemette, C. Pharmacogenomics of human UDP-glucuronosyltransferase enzymes. Pharmacogenomics J., 2003, 3(3), 136-158. (Pubitemid 36850156)
    • (2003) Pharmacogenomics Journal , vol.3 , Issue.3 , pp. 136-158
    • Guillemette, C.1
  • 12
    • 0028136583 scopus 로고
    • Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13
    • DOI 10.1006/geno.1994.1531
    • Monaghan, G.; Clarke, D. J.; Povey, S.; See, C. G.; Boxer, M.; Burchell, B. Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13. Genomics, 1994, 23(2), 496-499. (Pubitemid 24308276)
    • (1994) Genomics , vol.23 , Issue.2 , pp. 496-499
    • Monaghan, G.1    Clarke, D.J.2    Povey, S.3    Chee Gee See4    Boxer, M.5    Burchell, B.6
  • 13
    • 0037508573 scopus 로고    scopus 로고
    • Human uridine diphosphate-glucuronosyltransferase UGT2B7 conjugates mineralocorticoid and glucocorticoid metabolites
    • DOI 10.1210/en.2002-0052
    • Girard, C.; Barbier, O.; Veilleux, G.; El-Alfy, M.; Belanger, A. Human uridine diphosphate-glucuronosyltransferase UGT2B7 conjugates mineralocorticoid and glucocorticoid metabolites. Endocrinology, 2003, 144(6), 2659-2668. (Pubitemid 36629919)
    • (2003) Endocrinology , vol.144 , Issue.6 , pp. 2659-2668
    • Girard, C.1    Barbier, O.2    Veilleux, G.3    El-Alfy, M.4    Belanger, A.5
  • 14
    • 1642579667 scopus 로고    scopus 로고
    • An assessment of UDP-glucuronosyltransferase induction using primary human hepatocytes
    • DOI 10.1124/dmd.32.1.140
    • Soars, M. G.; Petullo, D. M.; Eckstein, J. A.; Kasper, S. C.; Wrighton, S. A. An assessment of udp-glucuronosyltransferase induction using primary human hepatocytes. Drug Metab. Dispos., 2004, 32(1), 140-148. (Pubitemid 38112546)
    • (2004) Drug Metabolism and Disposition , vol.32 , Issue.1 , pp. 140-148
    • Soars, M.G.1    Petullo, D.M.2    Eckstein, J.A.3    Kasper, S.C.4    Wrighton, S.A.5
  • 16
    • 0037369546 scopus 로고    scopus 로고
    • Tissue mRNA expression of the rat UDP-glucuronosyltransferase gene family
    • DOI 10.1124/dmd.31.3.326
    • Shelby, M. K.; Cherrington, N. J.; Vansell, N. R.; Klaassen, C. D. Tissue mRNA expression of the rat UDP-glucuronosyltransferase gene family. Drug Metab. Dispos., 2003, 31(3), 326-333. (Pubitemid 36249688)
    • (2003) Drug Metabolism and Disposition , vol.31 , Issue.3 , pp. 326-333
    • Shelby, M.K.1    Cherrington, N.J.2    Vansell, N.R.3    Klaassen, C.D.4
  • 17
    • 0030800075 scopus 로고    scopus 로고
    • Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: Identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue
    • Strassburg, C. P.; Oldhafer, K.; Manns, M. P.; Tukey, R. H. Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: Identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue. Mol. Pharmacol., 1997, 52(2), 212-220. (Pubitemid 27349612)
    • (1997) Molecular Pharmacology , vol.52 , Issue.2 , pp. 212-220
    • Strassburg, C.P.1    Oldhafer, K.2    Manns, M.P.3    Tukey, R.H.4
  • 20
    • 0027521059 scopus 로고
    • Human bilirubin UDP-glucuronosyltransferase catalyzes the glucuronidation of ethinylestradiol
    • Ebner, T.; Remmel, R. P.; Burchell, B. Human bilirubin UDPglucuronosyltransferase catalyzes the glucuronidation of ethinylestradiol. Mol. Pharmacol., 1993, 43(4), 649-654. (Pubitemid 23112743)
    • (1993) Molecular Pharmacology , vol.43 , Issue.4 , pp. 649-654
    • Ebner, T.1    Remmel, R.P.2    Burchell, B.3
  • 21
    • 0028856209 scopus 로고
    • Induction of phase I and phase II drugmetabolizing enzyme mRNA, protein, and activity by BHA, ethoxyquin, and oltipraz
    • Buetler, T. M.; Gallagher, E. P.; Wang, C.; Stahl, D. L.; Hayes, J. D.; Eaton, D. L. Induction of phase I and phase II drugmetabolizing enzyme mRNA, protein, and activity by BHA, ethoxyquin, and oltipraz. Toxicol. Appl. Pharmacol., 1995, 135(1), 45-57.
    • (1995) Toxicol. Appl. Pharmacol. , vol.135 , Issue.1 , pp. 45-57
    • Buetler, T.M.1    Gallagher, E.P.2    Wang, C.3    Stahl, D.L.4    Hayes, J.D.5    Eaton, D.L.6
  • 22
    • 0032791711 scopus 로고    scopus 로고
    • Expression and inducibility of the human bilirubin UDP- glucuronosyltransferase UGT1A1 in liver and cultured primary hepatocytes: Evidence for both genetic and environmental influences
    • DOI 10.1002/hep.510300205
    • Ritter, J. K.; Kessler, F. K.; Thompson, M. T.; Grove, A. D.; Auyeung, D. J.; Fisher, R. A. Expression and inducibility of the human bilirubin UDP-glucuronosyltransferase UGT1A1 in liver and cultured primary hepatocytes: Evidence for both genetic and environmental influences. Hepatology, 1999, 30(2), 476-484. (Pubitemid 29357514)
    • (1999) Hepatology , vol.30 , Issue.2 , pp. 476-484
    • Ritter, J.K.1    Kessler, F.K.2    Thompson, M.T.3    Grove, A.D.4    Auyeung, D.J.5    Fisher, R.A.6
  • 23
    • 0023777834 scopus 로고
    • Regulatory mechanisms of monofunctional and bifunctional anticarcinogenic enzyme inducers in murine liver
    • Prochaska, H. J.; Talalay, P. Regulatory mechanisms of monofunctional and bifunctional anticarcinogenic enzyme inducers in murine liver. Cancer Res, 1988, 48(17), 4776-4782.
    • (1988) Cancer Res , vol.48 , Issue.17 , pp. 4776-4782
    • Prochaska, H.J.1    Talalay, P.2
  • 25
    • 0035029401 scopus 로고    scopus 로고
    • The phenobarbital response enhancer module in the human bilirubin UDP-glucuronosyltransferase UGT1A1 gene and regulation by the nuclear receptor CAR
    • DOI 10.1053/jhep.2001.24172
    • Sugatani, J.; Kojima, H.; Ueda, A.; Kakizaki, S.; Yoshinari, K.; Gong, Q. H.; Owens, I. S.; Negishi, M.; Sueyoshi, T. The phenobarbital response enhancer module in the human bilirubin UDP-glucuronosyltransferase UGT1A1 gene and regulation by the nuclear receptor CAR. Hepatology, 2001, 33(5), 1232-1238. (Pubitemid 32378224)
    • (2001) Hepatology , vol.33 , Issue.5 , pp. 1232-1238
    • Sugatani, J.1    Kojima, H.2    Ueda, A.3    Kakizaki, S.4    Yoshinari, K.5    Gong, Q.-H.6    Owens, I.S.7    Negishi, M.8    Sueyoshi, T.9
  • 26
    • 2442631680 scopus 로고    scopus 로고
    • Asp85Tyr polymorphism in the UDP-glucuronosyltransferase (UGT) 2B15 gene and the risk of prostate cancer
    • DOI 10.1097/01.ju.0000117748.44313.43
    • Park, J.; Chen, L.; Shade, K.; Lazarus, P.; Seigne, J.; Patterson, S.; Helal, M.; Pow-Sang, J. Asp85tyr polymorphism in the udpglucuronosyltransferase (UGT) 2B15 gene and the risk of prostate cancer. J. Urol., 2004, 171(6 Pt 1), 2484-2488. (Pubitemid 38625520)
    • (2004) Journal of Urology , vol.171 , Issue.6 I , pp. 2484-2488
    • Park, J.1    Chen, L.2    Shade, K.3    Lazarus, P.4    Seigne, J.5    Patterson, S.6    Helal, M.7    Pow-Sang, J.8
  • 28
    • 0027394069 scopus 로고
    • The expression of UDP-glucuronosyltransferases of the UGT1 family in human liver and kidney and in response to drugs
    • DOI 10.1016/0006-2952(93)90064-4
    • Sutherland, L.; Ebner, T.; Burchell, B. The expression of UDPglucuronosyltransferases of the UGT1 family in human liver and kidney and in response to drugs. Biochem. Pharmacol., 1993, 45(2), 295-301. (Pubitemid 23042627)
    • (1993) Biochemical Pharmacology , vol.45 , Issue.2 , pp. 295-301
    • Sutherland, L.1    Ebner, T.2    Burchell, B.3
  • 29
    • 0027160090 scopus 로고
    • Differential effects of human recombinant interleukin-1β and dexamethasone on hepatic drug-metabolizing enzymes in male and female rats
    • DOI 10.1016/0006-2952(93)90198-6
    • Ferrari, L.; Herber, R.; Batt, A. M.; Siest, G. Differential effects of human recombinant interleukin-1 beta and dexamethasone on hepatic drug-metabolizing enzymes in male and female rats. Biochem. Pharmacol., 1993, 45(11), 2269-2277. (Pubitemid 23171088)
    • (1993) Biochemical Pharmacology , vol.45 , Issue.11 , pp. 2269-2277
    • Ferrari, L.1    Herber, R.2    Batt, A.-M.3    Siest, G.4
  • 30
    • 0031950872 scopus 로고    scopus 로고
    • Regulation of uridine diphosphate glucuronosyltransferase during the acute-phase response
    • Strasser, S. I.; Mashford, M. L.; Desmond, P. V. Regulation of uridine diphosphate glucuronosyltransferase during the acute-phase response. J. Gastroenterol. Hepatol., 1998, 13(1), 88-94. (Pubitemid 28137765)
    • (1998) Journal of Gastroenterology and Hepatology , vol.13 , Issue.1 , pp. 88-94
    • Strasser, S.I.1    Mashford, M.L.2    Desmond, P.V.3
  • 31
    • 0032974429 scopus 로고    scopus 로고
    • The effect of hormones on the expression of five isoforms of UDP- glucuronosyltransferase in primary cultures of rat hepatocytes
    • Li, Y. Q.; Prentice, D. A.; Howard, M. L.; Mashford, M. L.; Desmond, P. V. The effect of hormones on the expression of five isoforms of UDP-glucuronosyltransferase in primary cultures of rat hepatocytes. Pharm. Res., 1999, 16(2), 191-197. (Pubitemid 29135121)
    • (1999) Pharmaceutical Research , vol.16 , Issue.2 , pp. 191-197
    • Li, Y.Q.1    Prentice, D.A.2    Howard, M.L.3    Mashford, M.L.4    Desmond, P.V.5
  • 32
    • 0033975748 scopus 로고    scopus 로고
    • Glucuronidation of thyroxine in primary monolayer cultures of rat hepatocytes: In vitro induction of UDP-glucuronosyltranferases by methylcholanthrene, clofibrate, and dexamethasone alone and in combination
    • Jemnitz, K.; Veres, Z.; Monostory, K.; Vereczkey, L. Glucuronidation of thyroxine in primary monolayer cultures of rat hepatocytes: In vitro induction of UDP-glucuronosyltranferases by methylcholanthrene, clofibrate, and dexamethasone alone and in combination. Drug Metab. Dispos., 2000, 28(1), 34-37. (Pubitemid 30027509)
    • (2000) Drug Metabolism and Disposition , vol.28 , Issue.1 , pp. 34-37
    • Jemnitz, K.1    Veres, Z.2    Monostory, K.3    Vereczkey, L.4
  • 33
    • 14944341677 scopus 로고    scopus 로고
    • Transcriptional regulation of human UGT1A1 gene expression: Activated glucocorticoid receptor enhances constitutive androstane receptor/ pregnane X receptor-mediated UDP-glucuronosyltransferase 1A1 regulation with glucocorticoid receptor-interacting protein 1
    • DOI 10.1124/mol.104.007161
    • Sugatani, J.; Nishitani, S.; Yamakawa, K.; Yoshinari, K.; Sueyoshi, T.; Negishi, M.; Miwa, M. Transcriptional regulation of human UGT1A1 gene expression: Activated glucocorticoid receptor enhances constitutive androstane receptor/pregnane X receptormediated UDP-glucuronosyltransferase 1A1 regulation with glucocorticoid receptor-interacting protein 1. Mol. Pharmacol., 2005, 67(3), 845-855. (Pubitemid 40365332)
    • (2005) Molecular Pharmacology , vol.67 , Issue.3 , pp. 845-855
    • Sugatani, J.1    Nishitani, S.2    Yamakawa, K.3    Yoshinari, K.4    Sueyoshi, T.5    Negishi, M.6    Miwa, M.7
  • 34
    • 33745615119 scopus 로고    scopus 로고
    • Induction of human UDP-glucuronosyltransferase 1A1 by cortisol-GR
    • DOI 10.1007/s11033-005-1750-9
    • Usui, T.; Kuno, T.; Mizutani, T. Induction of human UDPglucuronosyltransferase 1A1 by cortisol-GR. Mol. Biol. Rep., 2006, 33(2), 91-96. (Pubitemid 43992643)
    • (2006) Molecular Biology Reports , vol.33 , Issue.2 , pp. 91-96
    • Usui, T.1    Kuno, T.2    Mizutani, T.3
  • 35
    • 21644470890 scopus 로고    scopus 로고
    • Stimulation of transcriptional expression of human UDP- glucuronosyltransferase 1A1 by dexamethasone
    • DOI 10.1023/B:MOLE.0000043582.35335.ff
    • Kanou, M.; Usui, T.; Ueyama, H.; Sato, H.; Ohkubo, I.; Mizutani, T. Stimulation of transcriptional expression of human UDPglucuronosyltransferase 1A1 by dexamethasone. Mol. Biol.Rep., 2004, 31(3), 151-158. (Pubitemid 40941142)
    • (2004) Molecular Biology Reports , vol.31 , Issue.3 , pp. 151-158
    • Kanou, M.1    Usui, T.2    Ueyama, H.3    Sato, H.4    Ohkubo, I.5    Mizutani, T.6
  • 36
    • 31044440754 scopus 로고    scopus 로고
    • Proximal HNF1 element is essential for the induction of human UDP-glucuronosyltransferase 1A1 by glucocorticoid receptor
    • DOI 10.1016/j.bcp.2005.11.014, PII S0006295205007781
    • Usui, T.; Kuno, T.; Ueyama, H.; Ohkubo, I.; Mizutani, T. Proximal HNF1 element is essential for the induction of human UDPglucuronosyltransferase 1A1 by glucocorticoid receptor. Biochem. Pharmacol., 2006, 71(5), 693-701. (Pubitemid 43122002)
    • (2006) Biochemical Pharmacology , vol.71 , Issue.5 , pp. 693-701
    • Usui, T.1    Kuno, T.2    Ueyama, H.3    Ohkubo, I.4    Mizutani, T.5
  • 37
    • 38549087625 scopus 로고    scopus 로고
    • Dexamethasone-mediated up-regulation of human CYP2A6 involves the glucocorticoid receptor and increased binding of hepatic nuclear factor 4α to the proximal promoter
    • DOI 10.1124/mol.107.039354
    • Onica, T.; Nichols, K.; Larin, M.; Ng, L.; Maslen, A.; Dvorak, Z.; Pascussi, J. M.; Vilarem, M. J.; Maurel, P.; Kirby, G. M. Dexamethasone-mediated up-regulation of human CYP2A6 involves the glucocorticoid receptor and increased binding of hepatic nuclear factor 4 alpha to the proximal promoter. Mol. Pharmacol., 2008, 73(2), 451-460. (Pubitemid 351159215)
    • (2008) Molecular Pharmacology , vol.73 , Issue.2 , pp. 451-460
    • Onica, T.1    Nichols, K.2    Larin, M.3    Ng, L.4    Maslen, A.5    Dvorak, Z.6    Pascussi, J.-M.7    Vilarem, M.-J.8    Maurel, P.9    Kirby, G.M.10
  • 38
    • 33750885465 scopus 로고    scopus 로고
    • Expression of xenobiotic metabolizing enzymes in different lung compartments of smokers and nonsmokers
    • DOI 10.1289/ehp.8861
    • Thum, T.; Erpenbeck, V. J.; Moeller, J.; Hohlfeld, J. M.; Krug, N.; Borlak, J. Expression of xenobiotic metabolizing enzymes in different lung compartments of smokers and nonsmokers. Environ. Health Perspect., 2006, 114(11), 1655-1661. (Pubitemid 44718269)
    • (2006) Environmental Health Perspectives , vol.114 , Issue.11 , pp. 1655-1661
    • Thum, T.1    Erpenbeck, V.J.2    Moeller, J.3    Hohlfeld, J.M.4    Krug, N.5    Borlak, J.6
  • 39
    • 34249339752 scopus 로고    scopus 로고
    • Cigarette smoke as a trigger for the dioxin receptor-mediated signaling pathway
    • DOI 10.1016/j.canlet.2006.11.015, PII S0304383506006410
    • Kitamura, M.; Kasai, A. Cigarette smoke as a trigger for the dioxin receptor-mediated signaling pathway. Cancer Lett, 2007, 252(2), 184-194. (Pubitemid 46809788)
    • (2007) Cancer Letters , vol.252 , Issue.2 , pp. 184-194
    • Kitamura, M.1    Kasai, A.2
  • 40
    • 39749086304 scopus 로고    scopus 로고
    • 3) inhibits androgen glucuronidation in prostate cancer cells
    • DOI 10.1158/1535-7163.MCT-07-0455
    • Kaeding, J.; Belanger, J.; Caron, P.; Verreault, M.; Belanger, A.; Barbier, O. Calcitrol (1alpha,25-dihydroxyvitamin D3) inhibits androgen glucuronidation in prostate cancer cells. Mol. Cancer Ther., 2008, 7(2), 380-390. (Pubitemid 351302531)
    • (2008) Molecular Cancer Therapeutics , vol.7 , Issue.2 , pp. 380-390
    • Kaeding, J.1    Belanger, J.2    Caron, P.3    Verreault, M.4    Belanger, A.5    Barbier, O.6
  • 41
    • 77149128673 scopus 로고    scopus 로고
    • Vitamin D: Considerations in the continued development as an agent for cancer prevention and therapy
    • Trump, D. L.; Deeb, K. K.; Johnson, C. S. Vitamin D: Considerations in the continued development as an agent for cancer prevention and therapy. Cancer J, 16(1), 1-9.
    • Cancer J , vol.16 , Issue.1 , pp. 1-9
    • Trump, D.L.1    Deeb, K.K.2    Johnson, C.S.3
  • 42
    • 68549101673 scopus 로고    scopus 로고
    • A phase II trial of calcitriol and naproxen in recurrent prostate cancer
    • Srinivas, S.; Feldman, D. A phase II trial of calcitriol and naproxen in recurrent prostate cancer. Anticancer. Res., 2009, 29(9), 3605-3610.
    • (2009) Anticancer. Res. , vol.29 , Issue.9 , pp. 3605-3610
    • Srinivas, S.1    Feldman, D.2
  • 43
    • 0032524203 scopus 로고    scopus 로고
    • Characterization of the UDP-glucuronosyltransferase isoenzyme expressed in rat ovary and its regulation by gonadotropins
    • Becedas, L.; Lundgren, B.; De Pierre, J. W. Characterization of the UDP-glucuronosyltransferase isoenzyme expressed in rat ovary and its regulation by gonadotropins. Biochem. J., 1998, 332 (Pt 1), 51-55. (Pubitemid 28239317)
    • (1998) Biochemical Journal , vol.332 , Issue.1 , pp. 51-55
    • Becedas, L.1    Lundgren, B.2    De Pierre, J.W.3
  • 44
    • 37549060373 scopus 로고    scopus 로고
    • Regulation of UDP-glucuronosyltransferase (UGT) 1A1 by progesterone and its impact on labetalol elimination
    • Jeong, H.; Choi, S.; Song, J. W.; Chen, H.; Fischer, J. H. Regulation of UDP-glucuronosyltransferase (UGT) 1A1 by progesterone and its impact on labetalol elimination. Xenobiotica, 2008, 38(1), 62-75.
    • (2008) Xenobiotica , vol.38 , Issue.1 , pp. 62-75
    • Jeong, H.1    Choi, S.2    Song, J.W.3    Chen, H.4    Fischer, J.H.5
  • 46
    • 0034489130 scopus 로고    scopus 로고
    • Cellular localization of uridine diphosphoglucuronosyltransferase 2B enzymes in the human prostate by in situ hybridization and immunohistochemistry
    • DOI 10.1210/jc.85.12.4819
    • Barbier, O.; Lapointe, H.; El Alfy, M.; Hum, D. W.; Belanger, A. Cellular localization of uridine diphosphoglucuronosyltransferase 2B enzymes in the human prostate by in situ hybridization and immunohistochemistry. J. Clin. Endocrinol. Metab., 2000, 85(12), 4819-4826. (Pubitemid 32157673)
    • (2000) Journal of Clinical Endocrinology and Metabolism , vol.85 , Issue.12 , pp. 4819-4826
    • Barbier, O.1    Lapointe, H.2    El Alfy, M.3    Hum, D.W.4    Belanger, A.5
  • 47
    • 42949113073 scopus 로고    scopus 로고
    • Inactivation of androgens by UDP-glucuronosyltransferases in the human prostate
    • DOI 10.1016/j.beem.2008.01.001, PII S1521690X0800002X
    • Barbier, O.; Belanger, A. Inactivation of androgens by UDPglucuronosyltransferases in the human prostate. Best. Pract. Res. Clin. Endocrinol. Metab., 2008, 22(2), 259-270. (Pubitemid 351611947)
    • (2008) Best Practice and Research: Clinical Endocrinology and Metabolism , vol.22 , Issue.2 , pp. 259-270
    • Barbier, O.1    Belanger, A.2
  • 48
    • 0029953793 scopus 로고    scopus 로고
    • Regulation of steroid glucuronosyltransferase activities and transcripts by androgen in the human prostatic cancer LNCaP cell line
    • DOI 10.1210/en.137.7.2872
    • Guillemette, C.; Hum, D. W.; Belanger, A. Regulation of steroid glucuronosyltransferase activities and transcripts by androgen in the human prostatic cancer LNCaP cell line. Endocrinology, 1996, 137(7), 2872-2879. (Pubitemid 26192181)
    • (1996) Endocrinology , vol.137 , Issue.7 , pp. 2872-2879
    • Guillemette, C.1    Hum, D.W.2    Belanger, A.3
  • 49
    • 45349098272 scopus 로고    scopus 로고
    • Androgen receptor mediates the expression of UDP-glucuronosyltransferase 2 BI5 and BI7 genes
    • DOI 10.1002/pros.20749
    • Bao, B. Y.; Chuang, B. F.; Wang, Q.; Sartor, O.; Balk, S. P.; Brown, M.; Kantoff, P. W.; Lee, G. S. Androgen receptor mediates the expression of UDP-glucuronosyltransferase 2 B15 and B17 genes. Prostate, 2008, 68(8), 839-848. (Pubitemid 351845215)
    • (2008) Prostate , vol.68 , Issue.8 , pp. 839-848
    • Bao, B.-Y.1    Chuang, B.-F.2    Wang, Q.3    Sartor, O.4    Balk, S.P.5    Brown, M.6    Kantoff, P.W.7    Lee, G.-S.M.8
  • 50
    • 36348992078 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferase 2B15 (UGT2B15) and UGT2B17 enzymes are major determinants of the androgen response in prostate cancer LNCaP cells
    • DOI 10.1074/jbc.M703370200
    • Chouinard, S.; Barbier, O.; Belanger, A. UDP-glucuronosyltransferase 2B15 (UGT2B15) and UGT2B17 enzymes are major determinants of the androgen response in prostate cancer LNCaP cells. J. Biol. Chem., 2007, 282(46), 33466-33474. (Pubitemid 350159554)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33466-33474
    • Chouinard, S.1    Barbier, O.2    Belanger, A.3
  • 51
    • 0037359143 scopus 로고    scopus 로고
    • Androgen-independent growth in LNCaP cell lines and steroid uridine diphosphate-glucuronosyltransferase expression
    • Kanaya, J.; Takashima, M.; Koh, E.; Namiki, M. Androgenindependent growth in LNCaP cell lines and steroid uridine diphosphate-glucuronosyltransferase expression. Asian J. Androl., 2003, 5(1), 9-13. (Pubitemid 36417093)
    • (2003) Asian Journal of Andrology , vol.5 , Issue.1 , pp. 9-13
    • Kanaya, J.1    Takashima, M.2    Koh, E.3    Namiki, M.4
  • 52
    • 0030751368 scopus 로고    scopus 로고
    • Sex hormones differentially regulate isoforms of UDP- glucuronosyltransferase
    • DOI 10.1023/A:1012130118186
    • Strasser, S. I.; Smid, S. A.; Mashford, M. L.; Desmond, P. V. Sex hormones differentially regulate isoforms of UDPglucuronosyltransferase. Pharm. Res., 1997, 14(9), 1115-1121. (Pubitemid 27432530)
    • (1997) Pharmaceutical Research , vol.14 , Issue.9 , pp. 1115-1121
    • Strasser, S.I.1    Smid, S.A.2    Mashford, M.L.3    Desmond, P.V.4
  • 53
    • 0033737123 scopus 로고    scopus 로고
    • Follicle-stimulating hormone, testosterone, and hypoxia differentially regulate UDP-glucuronosyltransferase 1 isoforms expression in rat sertoli and peritubular myoid cells
    • Magnanti, M.; Giuliani, L.; Gandini, O.; Gazzaniga, P.; Santiemma, V.; Ciotti, M.; Saccani, G.; Frati, L.; Agliano, A. M. Follicle-stimulating hormone, testosterone, and hypoxia differentially regulate UDP-glucuronosyltransferase 1 isoforms expression in rat sertoli and peritubular myoid cells. J. Steroid Biochem. Mol. Biol., 2000, 74(3), 149-155.
    • (2000) J. Steroid Biochem. Mol. Biol. , vol.74 , Issue.3 , pp. 149-155
    • Magnanti, M.1    Giuliani, L.2    Gandini, O.3    Gazzaniga, P.4    Santiemma, V.5    Ciotti, M.6    Saccani, G.7    Frati, L.8    Agliano, A.M.9
  • 54
    • 50049094222 scopus 로고    scopus 로고
    • Androgen regulation of renal uridine diphosphoglucuronosyltransferase 1A1 in rats
    • Stern, S. T.; Tallman, M. N.; Miles, K. K.; Ritter, J. K.; Smith, P. C. Androgen regulation of renal uridine diphosphoglucuronosyltransferase 1A1 in rats. Drug Metab. Dispos., 2008, 36(9), 1737-1739.
    • (2008) Drug Metab. Dispos. , vol.36 , Issue.9 , pp. 1737-1739
    • Stern, S.T.1    Tallman, M.N.2    Miles, K.K.3    Ritter, J.K.4    Smith, P.C.5
  • 55
    • 33746043754 scopus 로고    scopus 로고
    • Estrogen regulation of the glucuronidation enzyme UGT2B15 in estrogen receptor-positive breast cancer cells
    • DOI 10.1210/en.2006-0358
    • Harrington, W. R.; Sengupta, S.; Katzenellenbogen, B. S. Estrogen regulation of the glucuronidation enzyme UGT2B15 in estrogen receptor-positive breast cancer cells. Endocrinology, 2006, 147(8), 3843-3850. (Pubitemid 44079389)
    • (2006) Endocrinology , vol.147 , Issue.8 , pp. 3843-3850
    • Harrington, W.R.1    Sengupta, S.2    Katzenellenbogen, B.S.3
  • 56
    • 67650828089 scopus 로고    scopus 로고
    • Estrogen receptor alpha, fos-related antigen-2, and c-Jun coordinately regulate human UDP glucuronosyltransferase 2B15 and 2B17 expression in response to 17beta-estradiol in MCF-7 cells
    • Hu, D. G.; Mackenzie, P. I. Estrogen receptor alpha, fos-related antigen-2, and c-Jun coordinately regulate human UDP glucuronosyltransferase 2B15 and 2B17 expression in response to 17beta-estradiol in MCF-7 cells. Mol. Pharmacol., 2009, 76(2), 425-439.
    • (2009) Mol. Pharmacol. , vol.76 , Issue.2 , pp. 425-439
    • Hu, D.G.1    Mackenzie, P.I.2
  • 57
    • 0033305436 scopus 로고    scopus 로고
    • Effect of estrogen agonists and antagonists on induction of progesterone receptor in a rat hypothalamic cell line
    • Fitzpatrick, S. L.; Berrodin, T. J.; Jenkins, S. F.; Sindoni, D. M.; Deecher, D. C.; Frail, D. E. Effect of estrogen agonists and antagonists on induction of progesterone receptor in a rat hypothalamic cell line. Endocrinology, 1999, 140(9), 3928-3937. (Pubitemid 30647086)
    • (1999) Endocrinology , vol.140 , Issue.9 , pp. 3928-3937
    • Fitzpatrick, S.L.1    Berrodin, T.J.2    Jenkins, S.F.3    Sindoni, D.M.4    Deecher, D.C.5    Frail, D.E.6
  • 59
    • 27944483765 scopus 로고    scopus 로고
    • Isoflavones modulate the glucuronidation of estradiol in human liver microsomes
    • DOI 10.1093/carcin/bgi197
    • Pfeiffer, E.; Treiling, C. R.; Hoehle, S. I.; Metzler, M. Isoflavones modulate the glucuronidation of estradiol in human liver microsomes. Carcinogenesis, 2005, 26(12), 2172-2178. (Pubitemid 41672205)
    • (2005) Carcinogenesis , vol.26 , Issue.12 , pp. 2172-2178
    • Pfeiffer, E.1    Treiling, C.R.2    Hoehle, S.I.3    Metzler, M.4
  • 61
    • 70349142306 scopus 로고    scopus 로고
    • Upregulation of UDP-glucuronosyltransferase (UGT) 1A4 by 17betaestradiol: A potential mechanism of increased lamotrigine elimination in pregnancy
    • Chen, H.; Yang, K.; Choi, S.; Fischer, J. H.; Jeong, H. Upregulation of UDP-glucuronosyltransferase (UGT) 1A4 by 17betaestradiol: A potential mechanism of increased lamotrigine elimination in pregnancy. Drug Metab. Dispos., 2009, 37(9), 1841-1847.
    • (2009) Drug Metab. Dispos. , vol.37 , Issue.9 , pp. 1841-1847
    • Chen, H.1    Yang, K.2    Choi, S.3    Fischer, J.H.4    Jeong, H.5
  • 62
    • 0031037573 scopus 로고    scopus 로고
    • Induction of two UDP-glucuronosyltransferase isoforms sensitive to phenobarbital that are involved in morphine glucuronidation: Production of isoform-selective antipeptide antibodies toward UGT1.1r and UGT2B1
    • Ishii, Y.; Takami, A.; Tsuruda, K.; Kurogi, A.; Yamada, H.; Oguri, K. Induction of two UDP-glucuronosyltransferase isoforms sensitive to phenobarbital that are involved in morphine glucuronidation: Production of isoform-selective antipeptide antibodies toward UGT1.1r and UGT2B1. Drug Metab. Dispos., 1997, 25(2), 163-167. (Pubitemid 27086116)
    • (1997) Drug Metabolism and Disposition , vol.25 , Issue.2 , pp. 163-167
    • Ishii, Y.1    Takami, A.2    Tsuruda, K.3    Kurogi, A.4    Yamada, H.5    Oguri, K.6
  • 63
    • 0029783146 scopus 로고    scopus 로고
    • Phase II enzyme expression in rat liver in response to the antiestrogen tamoxifen
    • Nuwaysir, E. F.; Daggett, D. A.; Jordan, V. C.; Pitot, H. C. Phase II enzyme expression in rat liver in response to the antiestrogen tamoxifen. Cancer Res., 1996, 56(16), 3704-3710. (Pubitemid 26272016)
    • (1996) Cancer Research , vol.56 , Issue.16 , pp. 3704-3710
    • Nuwaysir, E.F.1    Daggett, D.A.2    Jordan, V.C.3    Pitot, H.C.4
  • 64
    • 0030934879 scopus 로고    scopus 로고
    • Bioactivation of mutagens via sulfation
    • Glatt, H. Sulfation and sulfotransferases 4: Bioactivation of mutagens via sulfation. Faseb J., 1997, 11(5), 314-321. (Pubitemid 27193935)
    • (1997) FASEB Journal , vol.11 , Issue.5 , pp. 314-321
    • Glatt, H.1
  • 65
    • 0031670051 scopus 로고    scopus 로고
    • Rat, but not human, sulfotransferase activates a tamoxifen metabolite to produce DNA adducts and gene mutations in bacteria and mammalian cells in culture
    • DOI 10.1093/carcin/19.10.1709
    • Glatt, H.; Davis, W.; Meinl, W.; Hermersdorfer, H.; Venitt, S.; Phillips, D. H. Rat, but not human, sulfotransferase activates a tamoxifen metabolite to produce DNA adducts and gene mutations in bacteria and mammalian cells in culture. Carcinogenesis, 1998, 19(10), 1709-1713. (Pubitemid 28474633)
    • (1998) Carcinogenesis , vol.19 , Issue.10 , pp. 1709-1713
    • Glatt, H.1    Davis, W.2    Meinl, W.3    Hermersdorfer, H.4    Venitt, S.5    Phillips, D.H.6
  • 66
    • 0035666996 scopus 로고    scopus 로고
    • Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3′,5-triiodothyronine as the substrate
    • DOI 10.1677/joe.0.1710525
    • Li, X.; Clemens, D. L.; Cole, J. R.; Anderson, R. J. Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3',5-triiodothyronine as the substrate. J. Endocrinol., 2001, 171(3), 525-532. (Pubitemid 34026367)
    • (2001) Journal of Endocrinology , vol.171 , Issue.3 , pp. 525-532
    • Li, X.1    Clemens, D.L.2    Cole, J.R.3    Anderson, R.J.4
  • 67
    • 0027051110 scopus 로고
    • Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenal
    • Comer, K. A.; Falany, C. N. Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenal. Mol. Pharmacol., 1992, 41(4), 645-651. (Pubitemid 23021450)
    • (1992) Molecular Pharmacology , vol.41 , Issue.4 , pp. 645-651
    • Comer, K.A.1    Falany, C.N.2
  • 68
    • 70349280717 scopus 로고    scopus 로고
    • 24-hydroxycholesterol sulfation by human cytosolic sulfotransferases: Formation of monosulfates and disulfates, molecular modeling, sulfatase sensitivity, and inhibition of liver x receptor activation
    • Cook, I. T.; Duniec-Dmuchowski, Z.; Kocarek, T. A.; Runge- Morris, M.; Falany, C. N. 24-hydroxycholesterol sulfation by human cytosolic sulfotransferases: Formation of monosulfates and disulfates, molecular modeling, sulfatase sensitivity, and inhibition of liver x receptor activation. Drug Metab. Dispos., 2009, 37(10), 2069-2078.
    • (2009) Drug Metab. Dispos. , vol.37 , Issue.10 , pp. 2069-2078
    • Cook, I.T.1    Duniec-Dmuchowski, Z.2    Kocarek, T.A.3    Runge- Morris, M.4    Falany, C.N.5
  • 69
    • 0032549065 scopus 로고    scopus 로고
    • Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases
    • DOI 10.1016/S0009-2797(97)00117-8, PII S0009279797001178
    • Coughtrie, M. W.; Sharp, S.; Maxwell, K.; Innes, N. P. Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases. Chem. Biol. Interact., 1998, 109(1-3), 3-27. (Pubitemid 28161098)
    • (1998) Chemico-Biological Interactions , vol.109 , Issue.1-3 , pp. 3-27
    • Coughtrie, M.W.H.1    Sharp, S.2    Maxwell, K.3    Innes, N.P.4
  • 70
    • 1642268315 scopus 로고    scopus 로고
    • A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily
    • DOI 10.1097/00008571-200403000-00009
    • Blanchard, R. L.; Freimuth, R. R.; Buck, J.; Weinshilboum, R. M.; Coughtrie, M. W. A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics, 2004, 14(3), 199-211. (Pubitemid 38373115)
    • (2004) Pharmacogenetics , vol.14 , Issue.3 , pp. 199-211
    • Blanchard, R.L.1    Freimuth, R.R.2    Buck, J.3    Weinshilboum, R.M.4    Coughtrie, M.W.H.5
  • 71
    • 0032213662 scopus 로고    scopus 로고
    • Human hydroxysteroid sulfotransferase SULT2B1: Two enzymes encoded by a single chromosome 19 gene
    • DOI 10.1006/geno.1998.5518
    • Her, C.; Wood, T. C.; Eichler, E. E.; Mohrenweiser, H. W.; Ramagli, L. S.; Siciliano, M. J.; Weinshilboum, R. M. Human hydroxysteroid sulfotransferase SULT2B1: Two enzymes encoded by a single chromosome 19 gene. Genomics, 1998, 53(3), 284-295. (Pubitemid 28527630)
    • (1998) Genomics , vol.53 , Issue.3 , pp. 284-295
    • Her, C.1    Wood, T.C.2    Eichler, E.E.3    Mohrenweiser, H.W.4    Ramagli, L.S.5    Siciliano, M.J.6    Weinshilboum, R.M.7
  • 74
    • 0029549968 scopus 로고
    • Human dehydroepiandrosterone sulfotransferase. Purification, molecular cloning, and characterization
    • DOI 10.1111/j.1749-6632.1995.tb17372.x
    • Falany, C. N.; Comer, K. A.; Dooley, T. P.; Glatt, H. Human dehydroepiandrosterone sulfotransferase. Purification, molecular cloning, and characterization. Ann. N. Y. Acad. Sci., 1995, 774, 59-72. (Pubitemid 26140360)
    • (1995) Annals of the New York Academy of Sciences , vol.774 , pp. 59-72
    • Falany, C.N.1    Comer, K.A.2    Dooley, T.P.3    Glatt, H.4
  • 75
    • 0025230526 scopus 로고
    • Purification and characterization of human liver phenol-sulfating phenol sulfotransferase
    • DOI 10.1016/0003-9861(90)90265-Z
    • Falany, C. N.; Vazquez, M. E.; Heroux, J. A.; Roth, J. A. Purification and characterization of human liver phenol-sulfating phenol sulfotransferase. Arch. Biochem. Biophys., 1990, 278(2), 312-318. (Pubitemid 20126057)
    • (1990) Archives of Biochemistry and Biophysics , vol.278 , Issue.2 , pp. 312-318
    • Falany, C.N.1    Vazquez, M.E.2    Heroux, J.A.3    Roth, J.A.4
  • 76
    • 0034649125 scopus 로고    scopus 로고
    • Expression profiling of human sulfotransferase and sulfatase gene superfamilies in epithelial tissues and cultured cells
    • Dooley, T. P.; Haldeman-Cahill, R.; Joiner, J.; Wilborn, T. W. Expression profiling of human sulfotransferase and sulfatase gene superfamilies in epithelial tissues and cultured cells. Biochem. Biophys. Res. Commun., 2000, 277(1), 236-245.
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , Issue.1 , pp. 236-245
    • Dooley, T.P.1    Haldeman-Cahill, R.2    Joiner, J.3    Wilborn, T.W.4
  • 77
    • 38749090899 scopus 로고    scopus 로고
    • Regulation of sulfotransferase enzymes by prototypical microsomal enzyme inducers in mice
    • DOI 10.1124/jpet.107.129650
    • Alnouti, Y.; Klaassen, C. D. Regulation of sulfotransferase enzymes by prototypical microsomal enzyme inducers in mice. J.Pharmacol. Exp. Ther., 2008, 324(2), 612-621. (Pubitemid 351185863)
    • (2008) Journal of Pharmacology and Experimental Therapeutics , vol.324 , Issue.2 , pp. 612-621
    • Alnouti, Y.1    Klaassen, C.D.2
  • 78
    • 33847153493 scopus 로고    scopus 로고
    • Human constitutive androstane receptor mediated methotrexate induction of human dehydroepiandrosterone sulfotransferase (hSULT2A1)
    • DOI 10.1016/j.tox.2006.12.019, PII S0300483X06007402, Includes Special Issue Section: Proceedings of the Joint Meeting of the British Toxicology Society and The In Vitro Toxicology Society and The UK NC3 Rs, University of York, UK, 14-15 Sept 2006
    • Chen, X.; Zhang, J.; Baker, S. M.; Chen, G. Human constitutive androstane receptor mediated methotrexate induction of human dehydroepiandrosterone sulfotransferase (hSULT2A1). Toxicology, 2007, 231(2-3), 224-233. (Pubitemid 46283167)
    • (2007) Toxicology , vol.231 , Issue.2-3 , pp. 224-233
    • Chen, X.1    Zhang, J.2    Baker, S.M.3    Chen, G.4
  • 79
    • 33845910657 scopus 로고    scopus 로고
    • Nuclear receptor interactions in methotrexate induction of human dehydroepiandrosterone sulfotransferase (hSULT2A1)
    • DOI 10.1002/jbt.20149
    • Chen, X.; Maiti, S.; Zhang, J.; Chen, G. Nuclear receptor interactions in methotrexate induction of human dehydroepiandrosterone sulfotransferase (hSULT2A1). J. Biochem. Mol. Toxicol., 2006, 20(6), 309-317. (Pubitemid 46025671)
    • (2006) Journal of Biochemical and Molecular Toxicology , vol.20 , Issue.6 , pp. 309-317
    • Chen, X.1    Maiti, S.2    Zhang, J.3    Chen, G.4
  • 80
    • 0035206998 scopus 로고    scopus 로고
    • Targeted disruption of the mouse estrogen sulfotransferase gene reveals a role of estrogen metabolism in intracrine and paracrine estrogen regulation
    • DOI 10.1210/en.142.12.5342
    • Qian, Y. M.; Sun, X. J.; Tong, M. H.; Li, X. P.; Richa, J.; Song, W. C. Targeted disruption of the mouse estrogen sulfotransferase gene reveals a role of estrogen metabolism in intracrine and paracrine estrogen regulation. Endocrinology, 2001, 142(12), 5342-5350. (Pubitemid 33131967)
    • (2001) Endocrinology , vol.142 , Issue.12 , pp. 5342-5350
    • Qian, Y.M.1    Sun, X.J.2    Tong, M.H.3    Li, X.P.4    Richa, J.5    Song, W.-C.6
  • 81
    • 14644389506 scopus 로고    scopus 로고
    • Spontaneous fetal loss caused by placental thrombosis in estrogen sulfotransferase-deficient mice
    • DOI 10.1038/nm1184
    • Tong, M. H.; Jiang, H.; Liu, P.; Lawson, J. A.; Brass, L. F.; Song, W. C. Spontaneous fetal loss caused by placental thrombosis in estrogen sulfotransferase-deficient mice. Nat. Med., 2005, 11(2), 153-159. (Pubitemid 40321350)
    • (2005) Nature Medicine , vol.11 , Issue.2 , pp. 153-159
    • Tong, M.H.1    Jiang, H.2    Liu, P.3    Lawson, J.A.4    Brass, L.F.5    Song, W.-C.6
  • 83
    • 33644877840 scopus 로고    scopus 로고
    • Epigenetic silencing of the sulfotransferase 1A1 gene by hypermethylation in breast tissue
    • Kwon, M. S.; Kim, S. J.; Lee, S. Y.; Jeong, J. H.; Lee, E. S.; Kang, H. S. Epigenetic silencing of the sulfotransferase 1A1 gene by hypermethylation in breast tissue. Oncol. Rep., 2006, 15(1), 27-32.
    • (2006) Oncol. Rep. , vol.15 , Issue.1 , pp. 27-32
    • Kwon, M.S.1    Kim, S.J.2    Lee, S.Y.3    Jeong, J.H.4    Lee, E.S.5    Kang, H.S.6
  • 84
    • 0029100907 scopus 로고
    • Characterization of bovine tracheobronchial phenol sulphotransferase cDNA and detection of mRNA regulation by cortisol
    • Schauss, S. J.; Henry, T.; Palmatier, R.; Halvorson, L.; Dannenbring, R.; Beckmann, J. D. Characterization of bovine tracheobronchial phenol sulphotransferase cDNA and detection of mRNA regulation by cortisol. Biochem. J., 1995, 311 (Pt 1), 209-217.
    • (1995) Biochem. J. , vol.311 , Issue.PART 1 , pp. 209-217
    • Schauss, S.J.1    Henry, T.2    Palmatier, R.3    Halvorson, L.4    Dannenbring, R.5    Beckmann, J.D.6
  • 85
    • 0028145932 scopus 로고
    • Regulation of phenol sulfotransferase expression in cultured bovine bronchial epithelial cells by hydrocortisone
    • Beckmann, J. D.; Illig, M.; Bartzatt, R. Regulation of phenol sulfotransferase expression in cultured bovine bronchial epithelial cells by hydrocortisone. J.Cell Physiol., 1994, 160(3), 603-610. (Pubitemid 24288919)
    • (1994) Journal of Cellular Physiology , vol.160 , Issue.3 , pp. 603-610
    • Beckmann, J.D.1    Illig, M.2    Bartzatt, R.3
  • 86
    • 0029858259 scopus 로고    scopus 로고
    • Regulation of rat hepatic sulfotransferase gene expression by glucocorticoid hormones
    • Runge-Morris, M.; Rose, K.; Kocarek, T. A. Regulation of rat hepatic sulfotransferase gene expression by glucocorticoid hormones. Drug Metab Dispos, 1996, 24(10), 1095-1101. (Pubitemid 26346222)
    • (1996) Drug Metabolism and Disposition , vol.24 , Issue.10 , pp. 1095-1101
    • Runge-Morris, M.1    Rose, K.2    Kocarek, T.A.3
  • 87
    • 0034937430 scopus 로고    scopus 로고
    • Transcriptional regulation of rat hepatic aryl sulfotransferase (SULT1A1) gene expression by glucocorticoids
    • Duanmu, Z.; Kocarek, T. A.; Runge-Morris, M. Transcriptional regulation of rat hepatic aryl sulfotransferase (SULT1A1) gene expression by glucocorticoids. Drug Metab. Dispos., 2001, 29(8), 1130-1135. (Pubitemid 32660532)
    • (2001) Drug Metabolism and Disposition , vol.29 , Issue.8 , pp. 1130-1135
    • Duanmu, Z.1    Kocarek, T.A.2    Runge-Morris, M.3
  • 88
    • 0142243105 scopus 로고    scopus 로고
    • Transactivation of glucocorticoid-inducible rat aryl sulfotransferase (SULT1A1) gene transcription
    • DOI 10.1124/dmd.31.11.1378
    • Fang, H. L.; Shenoy, S.; Duanmu, Z.; Kocarek, T. A.; Runge- Morris, M. Transactivation of glucocorticoid-inducible rat aryl sulfotransferase (SULT1A1) gene transcription. Drug Metab. Dispos., 2003, 31(11), 1378-1381. (Pubitemid 37310327)
    • (2003) Drug Metabolism and Disposition , vol.31 , Issue.11 , pp. 1378-1381
    • Fang, H.-L.1    Shenoy, S.2    Duanmu, Z.3    Kocarek, T.A.4    Runge-Morris, M.5
  • 89
    • 0036707624 scopus 로고    scopus 로고
    • Effects of dexamethasone on aryl (SULT1A1)- and hydroxysteroid (SULT2A1)-sulfotransferase gene expression in primary cultured human hepatocytes
    • Duanmu, Z.; Locke, D.; Smigelski, J.; Wu, W.; Dahn, M. S.; Falany, C. N.; Kocarek, T. A.; Runge-Morris, M. Effects of dexamethasone on aryl (SULT1A1)- and hydroxysteroid (SULT2A1)-sulfotransferase gene expression in primary cultured human hepatocytes. Drug Metab. Dispos., 2002, 30(9), 997-1004.
    • (2002) Drug Metab. Dispos. , vol.30 , Issue.9 , pp. 997-1004
    • Duanmu, Z.1    Locke, D.2    Smigelski, J.3    Wu, W.4    Dahn, M.S.5    Falany, C.N.6    Kocarek, T.A.7    Runge-Morris, M.8
  • 90
    • 0032555487 scopus 로고    scopus 로고
    • Tissue-specific and androgen-repressible regulation of the rat dehydroepiandrosterone sulfotransferase gene promoter
    • DOI 10.1074/jbc.273.34.21856
    • Song, C. S.; Jung, M. H.; Kim, S. C.; Hassan, T.; Roy, A. K.; Chatterjee, B. Tissue-specific and androgen-repressible regulation of the rat dehydroepiandrosterone sulfotransferase gene promoter. J. Biol. Chem., 1998, 273(34), 21856-21866. (Pubitemid 28405363)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.34 , pp. 21856-21866
    • Song, C.S.1    Jung, M.H.2    Kim, S.C.3    Hassan, T.4    Roy, A.K.5    Chatterjee, B.6
  • 91
    • 11144281346 scopus 로고    scopus 로고
    • Regulation of glucocorticoid-inducible hydroxysteroid sulfotransferase (SULT2A-40/41) gene transcription in primary cultured rat hepatocytes: Role of CCAAT/enhancer-binding protein liver-enriched transcription factors
    • DOI 10.1124/dmd.104.000281
    • Fang, H. L.; Abdolalipour, M.; Duanmu, Z.; Smigelski, J. R.; Weckle, A.; Kocarek, T. A.; Runge-Morris, M. Regulation of glucocorticoid-inducible hydroxysteroid sulfotransferase (SULT2A-40/41) gene transcription in primary cultured rat hepatocytes: Role of CCAAT/enhancer-binding protein liverenriched transcription factors. Drug Metab. Dispos., 2005, 33(1), 147-156. (Pubitemid 40023526)
    • (2005) Drug Metabolism and Disposition , vol.33 , Issue.1 , pp. 147-156
    • Fang, H.-L.1    Abdolalipour, M.2    Duanmu, Z.3    Smigelski, J.R.4    Weckle, A.5    Kocarek, T.A.6    Runge-Morris, M.7
  • 92
    • 36348961429 scopus 로고    scopus 로고
    • Induction of human sulfotransferase 1A3 (SULT1A3) by glucocorticoids
    • DOI 10.1016/j.lfs.2007.09.029, PII S0024320507007412
    • Bian, H. S.; Ngo, S. Y.; Tan, W.; Wong, C. H.; Boelsterli, U. A.; Tan, T. M. Induction of human sulfotransferase 1A3 (SULT1A3) by glucocorticoids. Life Sci., 2007, 81(25-26), 1659-1667. (Pubitemid 350151445)
    • (2007) Life Sciences , vol.81 , Issue.25-26 , pp. 1659-1667
    • Bian, H.S.1    Ngo, S.Y.Y.2    Tan, W.3    Wong, C.H.4    Boelsterli, U.A.5    Tan, T.M.C.6
  • 93
    • 0032080151 scopus 로고    scopus 로고
    • Sulfuryl transfer: The catalytic mechanism of human estrogen sulfotransferase
    • DOI 10.1074/jbc.273.18.10888
    • Zhang, H.; Varlamova, O.; Vargas, F. M.; Falany, C. N.; Leyh, T. S. Sulfuryl transfer: The catalytic mechanism of human estrogen sulfotransferase. J. Biol. Chem., 1998, 273(18), 10888-10892. (Pubitemid 28204925)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 10888-10892
    • Zhang, H.1    Varmalova, O.2    Vargas, F.M.3    Falany, C.N.4    Leyh, T.S.5
  • 95
    • 73649147746 scopus 로고    scopus 로고
    • Glucocorticoids stimulate hepatic and renal catecholamine inactivation by direct rapid induction of the dopamine sulfotransferase Sult1d1
    • Wong, S.; Tan, K.; Carey, K. T.; Fukushima, A.; Tiganis, T.; Cole, T. J. Glucocorticoids stimulate hepatic and renal catecholamine inactivation by direct rapid induction of the dopamine sulfotransferase Sult1d1. Endocrinology, 151(1), 185-194.
    • Endocrinology , vol.151 , Issue.1 , pp. 185-194
    • Wong, S.1    Tan, K.2    Carey, K.T.3    Fukushima, A.4    Tiganis, T.5    Cole, T.J.6
  • 98
    • 0032548975 scopus 로고    scopus 로고
    • Regulation of sulfotransferase mRNA expression in male and female rats of various ages
    • DOI 10.1016/S0009-2797(97)00141-5
    • Klaassen, C. D.; Liu, L.; Dunn, R. T., 2nd. Regulation of sulfotransferase mRNA expression in male and female rats of various ages. Chem. Biol. Interact., 1998, 109(1-3), 299-313. (Pubitemid 28161122)
    • (1998) Chemico-Biological Interactions , vol.109 , Issue.1-3 , pp. 299-313
    • Klaassen, C.D.1    Liu, L.2    Dunn II, R.T.3
  • 99
    • 0032748919 scopus 로고    scopus 로고
    • Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy
    • DOI 10.1093/molehr/5.11.995
    • Rubin, G. L.; Harrold, A. J.; Mills, J. A.; Falany, C. N.; Coughtrie, M. W. Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy. Mol. Hum. Reprod., 1999, 5(11), 995-1002. (Pubitemid 29518902)
    • (1999) Molecular Human Reproduction , vol.5 , Issue.11 , pp. 995-1002
    • Rubin, G.L.1    Harrold, A.J.2    Mills, J.A.3    Falany, C.N.4    Coughtrie, M.W.H.5
  • 100
    • 0242441514 scopus 로고    scopus 로고
    • Estrogen sulfotransferase and sulfatase: Roles in the regulation of estrogen activity in human uterine endometrial carcinomas
    • DOI 10.1111/j.1349-7006.2003.tb01369.x
    • Tanaka, K.; Kubushiro, K.; Iwamori, Y.; Okairi, Y.; Kiguchi, K.; Ishiwata, I.; Tsukazaki, K.; Nozawa, S.; Iwamori, M. Estrogen sulfotransferase and sulfatase: Roles in the regulation of estrogen activity in human uterine endometrial carcinomas. Cancer Sci., 2003, 94(10), 871-876. (Pubitemid 37406969)
    • (2003) Cancer Science , vol.94 , Issue.10 , pp. 871-876
    • Tanaka, K.1    Kubushiro, K.2    Iwamori, Y.3    Okairi, Y.4    Kiguchi, K.5    Ishiwata, I.6    Tsukuzaki, K.7    Nozawa, S.8    Iwamori, M.9
  • 101
    • 33748585937 scopus 로고    scopus 로고
    • Regulation of SULT1E1 expression in Ishikawa adenocarcinoma cells by tibolone
    • DOI 10.1016/j.steroids.2006.05.018, PII S0039128X06001346
    • Falany, J. L.; Falany, C. N. Regulation of SULT1E1 expression in Ishikawa adenocarcinoma cells by tibolone. Steroids, 2006, 71(10), 880-885. (Pubitemid 44376404)
    • (2006) Steroids , vol.71 , Issue.10 , pp. 880-885
    • Falany, J.L.1    Falany, C.N.2
  • 102
    • 2142828438 scopus 로고    scopus 로고
    • Expression of estrogen sulfotransferase in breast tissues and the regulation of ESTmRNA by estrogen]
    • Deng, W. H.; Wu, Y. Y.; Luo, L. H.; Wang, S.; Tang, W. Q.; Zhang, Y. F. [Expression of estrogen sulfotransferase in breast tissues and the regulation of ESTmRNA by estrogen]. Zhonghua Yi Xue Za Zhi, 2003, 83(21), 1891-1894.
    • (2003) Zhonghua Yi Xue Za Zhi , vol.83 , Issue.21 , pp. 1891-1894
    • Deng, W.H.1    Wu, Y.Y.2    Luo, L.H.3    Wang, S.4    Tang, W.Q.5    Zhang, Y.F.6
  • 104
    • 56049114437 scopus 로고    scopus 로고
    • Genistein induction of human sulfotransferases in HepG2 and Caco-2 cells
    • Chen, Y.; Huang, C.; Zhou, T.; Chen, G. Genistein induction of human sulfotransferases in HepG2 and Caco-2 cells. Basic Clin. Pharmacol. Toxicol., 2008, 103(6), 553-559.
    • (2008) Basic Clin. Pharmacol. Toxicol. , vol.103 , Issue.6 , pp. 553-559
    • Chen, Y.1    Huang, C.2    Zhou, T.3    Chen, G.4
  • 105
    • 9144251959 scopus 로고    scopus 로고
    • Inhibition of rat liver sulfotransferases SULT1A1 and SULT2A1 and glucuronosyltransferase by dietary flavonoids
    • DOI 10.1080/00498250310001615762
    • Mesia-Vela, S.; Kauffman, F. C. Inhibition of rat liver sulfotransferases SULT1A1 and SULT2A1 and glucuronosyltransferase by dietary flavonoids. Xenobiotica, 2003, 33(12), 1211-1220. (Pubitemid 38122243)
    • (2003) Xenobiotica , vol.33 , Issue.12 , pp. 1211-1220
    • Mesia-Vela, S.1    Kauffman, F.C.2
  • 106
    • 33746661669 scopus 로고    scopus 로고
    • Phase II antioxidant enzyme activities in brain of male and female ACI rats treated chronically with estradiol
    • DOI 10.1016/j.brainres.2006.05.093, PII S0006899306015502
    • Stakhiv, T. M.; Mesia-Vela, S.; Kauffman, F. C. Phase II antioxidant enzyme activities in brain of male and female ACI rats treated chronically with estradiol. Brain Res., 2006, 1104(1), 80-91. (Pubitemid 44164435)
    • (2006) Brain Research , vol.1104 , Issue.1 , pp. 80-91
    • Stakhiv, T.M.1    Mesia-Vela, S.2    Kauffman, F.C.3
  • 107
    • 0026717501 scopus 로고
    • Estrogen sulfotransferase of the rat liver: Complementary DNA cloning and age- and sex-specific regulation of messenger RNA
    • Demyan, W. F.; Song, C. S.; Kim, D. S.; Her, S.; Gallwitz, W.; Rao, T. R.; Slomczynska, M.; Chatterjee, B.; Roy, A. K. Estrogen sulfotransferase of the rat liver: Complementary DNA cloning and age- and sex-specific regulation of messenger RNA. Mol. Endocrinol., 1992, 6(4), 589-597.
    • (1992) Mol. Endocrinol. , vol.6 , Issue.4 , pp. 589-597
    • Demyan, W.F.1    Song, C.S.2    Kim, D.S.3    Her, S.4    Gallwitz, W.5    Rao, T.R.6    Slomczynska, M.7    Chatterjee, B.8    Roy, A.K.9
  • 108
    • 67651121941 scopus 로고    scopus 로고
    • Effect of insulin and testosterone on androgen production and transcription of SULT2A1 in the NCI-H295R adrenocortical cell line
    • Kumar, A.; Magoffin, D.; Munir, I.; Azziz, R. Effect of insulin and testosterone on androgen production and transcription of SULT2A1 in the NCI-H295R adrenocortical cell line. Fertil. Steril., 2009, 92(2), 793-797.
    • (2009) Fertil. Steril. , vol.92 , Issue.2 , pp. 793-797
    • Kumar, A.1    Magoffin, D.2    Munir, I.3    Azziz, R.4
  • 109
    • 54349083290 scopus 로고    scopus 로고
    • Gender-specific expression and mechanism of regulation of estrogen sulfotransferase in adipose tissues of the mouse
    • Khor, V. K.; Tong, M. H.; Qian, Y.; Song, W. C. Gender-specific expression and mechanism of regulation of estrogen sulfotransferase in adipose tissues of the mouse. Endocrinology, 2008, 149(11), 5440-5448.
    • (2008) Endocrinology , vol.149 , Issue.11 , pp. 5440-5448
    • Khor, V.K.1    Tong, M.H.2    Qian, Y.3    Song, W.C.4
  • 111
    • 1342265781 scopus 로고    scopus 로고
    • Dehydroepiandrosterone Sulfotransferase Is a Target for Transcriptional Induction by the Vitamin D Receptor
    • DOI 10.1124/mol.65.3.720
    • Echchgadda, I.; Song, C. S.; Roy, A. K.; Chatterjee, B. Dehydroepiandrosterone sulfotransferase is a target for transcriptional induction by the vitamin D receptor. Mol. Pharmacol., 2004, 65(3), 720-729. (Pubitemid 38264040)
    • (2004) Molecular Pharmacology , vol.65 , Issue.3 , pp. 720-729
    • Echchgadda, I.1    Song, C.S.2    Roy, A.K.3    Chatterjee, B.4
  • 112
    • 33645401882 scopus 로고    scopus 로고
    • An essential role of the CAAT/enhancer binding protein-alpha in the vitamin D-induced expression of the human steroid/bile acid-sulfotransferase (SULT2A1)
    • Song, C. S.; Echchgadda, I.; Seo, Y. K.; Oh, T.; Kim, S.; Kim, S. A.; Cho, S.; Shi, L.; Chatterjee, B. An essential role of the CAAT/enhancer binding protein-alpha in the vitamin D-induced expression of the human steroid/bile acid-sulfotransferase (SULT2A1). Mol. Endocrinol., 2006, 20(4), 795-808.
    • (2006) Mol. Endocrinol. , vol.20 , Issue.4 , pp. 795-808
    • Song, C.S.1    Echchgadda, I.2    Seo, Y.K.3    Oh, T.4    Kim, S.5    Kim, S.A.6    Cho, S.7    Shi, L.8    Chatterjee, B.9
  • 113
    • 0024265036 scopus 로고
    • Intracellular binding and transport of hormones and xenobiotics by glutathione-S-transferases
    • Listowsky, I.; Abramovitz, M.; Homma, H.; Niitsu, Y. Intracellular binding and transport of hormones and xenobiotics by glutathione- S-transferases. Drug Metab. Rev., 1988, 19(3-4), 305-318. (Pubitemid 19043739)
    • (1988) Drug Metabolism Reviews , vol.19 , Issue.3-4 , pp. 305-318
    • Listowsky, I.1    Abramovitz, M.2    Homma, H.3    Niitsu, Y.4
  • 114
    • 0024473664 scopus 로고
    • Glutathione-S-transferase are major cytosolic thyroid hormone binding proteins
    • Ishigaki, S.; Abramovitz, M.; Listowsky, I. Glutathione-Stransferases are major cytosolic thyroid hormone binding proteins. Arch. Biochem. Biophys., 1989, 273(2), 265-272. (Pubitemid 19221980)
    • (1989) Archives of Biochemistry and Biophysics , vol.273 , Issue.2 , pp. 265-272
    • Ishigaki, S.1    Abramovitz, M.2    Listowsky, I.3
  • 115
    • 0345832239 scopus 로고    scopus 로고
    • Parallel Evolutionary Pathways for Glutathione Transferases: Structure and Mechanism of the Mitochondrial Class Kappa Enzyme rGSTK1-1
    • DOI 10.1021/bi035832z
    • Ladner, J. E.; Parsons, J. F.; Rife, C. L.; Gilliland, G. L.; Armstrong, R. N. Parallel evolutionary pathways for glutathione transferases: Structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1. Biochemistry, 2004, 43(2), 352-361. (Pubitemid 38082557)
    • (2004) Biochemistry , vol.43 , Issue.2 , pp. 352-361
    • Ladner, J.E.1    Parsons, J.F.2    Rife, C.L.3    Gilliland, G.L.4    Armstrong, R.N.5
  • 116
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • DOI 10.1042/0264-6021:3600001
    • Sheehan, D.; Meade, G.; Foley, V. M.; Dowd, C. A. Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J., 2001, 360(Pt 1), 1-16. (Pubitemid 33081943)
    • (2001) Biochemical Journal , vol.360 , Issue.1 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 117
    • 0033011878 scopus 로고    scopus 로고
    • Common structural features of MAPEG - A widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism
    • Jakobsson, P. J.; Morgenstern, R.; Mancini, J.; Ford-Hutchinson, A.; Persson, B. Common structural features of MAPEG-a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci., 1999, 8(3), 689-692. (Pubitemid 29117984)
    • (1999) Protein Science , vol.8 , Issue.3 , pp. 689-692
    • Jakobsson, P.-J.1    Morgenstern, R.2    Mancini, J.3    Ford-Hutchinson, A.4    Persson, B.5
  • 118
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes, J. D.; Pulford, D. J. The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol., 1995, 30(6), 445-600.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , Issue.6 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 119
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • DOI 10.1021/tx960072x
    • Armstrong, R. N. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol., 1997, 10(1), 2-18. (Pubitemid 27044902)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.1 , pp. 2-18
    • Armstrong, R.N.1
  • 120
    • 0346025630 scopus 로고    scopus 로고
    • Garlic attenuates chrysotile-mediated pulmonary toxicity in rats by altering the phase I and phase II drug metabolizing enzyme system
    • DOI 10.1002/jbt.10100
    • Ameen, M.; Musthapa, M. S.; Abidi, P.; Ahmad, I.; Rahman, Q. Garlic attenuates chrysotile-mediated pulmonary toxicity in rats by altering the phase I and phase II drug metabolizing enzyme system. J. Biochem. Mol. Toxicol., 2003, 17(6), 366-371. (Pubitemid 38072285)
    • (2003) Journal of Biochemical and Molecular Toxicology , vol.17 , Issue.6 , pp. 366-371
    • Ameen, M.1    Musthapa, M.S.2    Abidi, P.3    Ahmad, I.4    Rahman, Q.5
  • 121
    • 4043083497 scopus 로고    scopus 로고
    • Modulation of 3-methylcholanthrene-induced rat hepatic and renal cytochrome P450 and phase II enzymes by plant phenols: Protocatechuic and tannic acids
    • DOI 10.1016/j.toxlet.2004.04.016, PII S0378427404002322
    • Krajka-Kuzniak, V.; Szaefer, H.; Baer-Dubowska, W. Modulation of 3-methylcholanthrene-induced rat hepatic and renal cytochrome P450 and phase II enzymes by plant phenols: Protocatechuic and tannic acids. Toxicol. Lett., 2004, 152(2), 117-126. (Pubitemid 39061763)
    • (2004) Toxicology Letters , vol.152 , Issue.2 , pp. 117-126
    • Krajka-Kuzniak, V.1    Szaefer, H.2    Baer-Dubowska, W.3
  • 122
    • 0035201366 scopus 로고    scopus 로고
    • Rifampin is a selective, pleiotropic inducer of drug metabolism genes in human hepatocytes: Studies with cDNA and oligonucleotide expression arrays
    • Rae, J. M.; Johnson, M. D.; Lippman, M. E.; Flockhart, D. A. Rifampin is a selective, pleiotropic inducer of drug metabolism genes in human hepatocytes: Studies with cDNA and oligonucleotide expression arrays. J. Pharmacol. Exp. Ther., 2001, 299(3), 849-857. (Pubitemid 33104951)
    • (2001) Journal of Pharmacology and Experimental Therapeutics , vol.299 , Issue.3 , pp. 849-857
    • Rae, J.M.1    Johnson, M.D.2    Lippman, M.E.3    Flockhart, D.A.4
  • 123
    • 0032730016 scopus 로고    scopus 로고
    • Effects of sulindac, sulindac metabolites, and aspirin on the activity of detoxification enzymes in HT-29 human colon adenocarcinoma cells
    • Patten, E. J.; DeLong, M. J. Effects of sulindac, sulindac metabolites, and aspirin on the activity of detoxification enzymes in HT-29 human colon adenocarcinoma cells. Cancer Lett., 1999, 147(1-2), 95-100.
    • (1999) Cancer Lett. , vol.147 , Issue.1-2 , pp. 95-100
    • Patten, E.J.1    DeLong, M.J.2
  • 124
    • 0021142412 scopus 로고
    • Induction of cytosolic glutathione transferase and microsomal epoxide hydrolase activities in extrahepatic organs of the rat by phenobarbital, 3-methylcholanthrene and trans-stilbene oxide
    • DePierre, J. W.; Seidegard, J.; Morgenstern, R.; Balk, L.; Meijer, J.; Astrom, A.; Norelius, I.; Ernster, L. Induction of cytosolic glutathione transferase and microsomal epoxide hydrolase activities in extrahepatic organs of the rat by phenobarbital, 3-methylcholanthrene and trans-stilbene oxide. Xenobiotica, 1984, 14(4), 295-301. (Pubitemid 14108121)
    • (1984) Xenobiotica , vol.14 , Issue.4 , pp. 295-301
    • Depierre, J.W.1    Seidegard, J.2    Morgenstern, R.3
  • 126
    • 56649105360 scopus 로고    scopus 로고
    • Induction of hepatic glutathione S-transferases in male mice by prototypes of various classes of microsomal enzyme inducers
    • Knight, T. R.; Choudhuri, S.; Klaassen, C. D. Induction of hepatic glutathione S-transferases in male mice by prototypes of various classes of microsomal enzyme inducers. Toxicol. Sci., 2008, 106(2), 329-338.
    • (2008) Toxicol. Sci. , vol.106 , Issue.2 , pp. 329-338
    • Knight, T.R.1    Choudhuri, S.2    Klaassen, C.D.3
  • 127
    • 84924280938 scopus 로고    scopus 로고
    • Effect of GSTM1 and GSTT1 double deletions in the development of oxidative stress in diabetic nephropathy patients
    • Datta, S. K.; Kumar, V.; Ahmed, R. S.; Tripathi, A. K.; Kalra, O. P.; Banerjee, B. D. Effect of GSTM1 and GSTT1 double deletions in the development of oxidative stress in diabetic nephropathy patients. Indian J. Biochem. Biophys., 47(2), 100-103.
    • Indian J. Biochem. Biophys. , vol.47 , Issue.2 , pp. 100-103
    • Datta, S.K.1    Kumar, V.2    Ahmed, R.S.3    Tripathi, A.K.4    Kalra, O.P.5    Banerjee, B.D.6
  • 128
    • 77957292572 scopus 로고    scopus 로고
    • The association of glutathione-S-transferase gene polymorphisms (GSTM1, GSTT1, GSTP1) with idiopathic male infertility
    • Safarinejad, M. R.; Shafiei, N.; Safarinejad, S. The association of glutathione-S-transferase gene polymorphisms (GSTM1, GSTT1, GSTP1) with idiopathic male infertility. J. Hum. Genet., 2010, 55, 565-570.
    • (2010) J. Hum. Genet. , Issue.55 , pp. 565-570
    • Safarinejad, M.R.1    Shafiei, N.2    Safarinejad, S.3
  • 129
    • 0025138731 scopus 로고
    • Glucocorticoid regulation of polycyclic aromatic hydrocarbon induction of cytochrome P450IA1, glutathione S-transferases, and NAD(P)H:quinone oxidoreductase in cultured fetal rat hepatocytes
    • Sherratt, A. J.; Banet, D. E.; Prough, R. A. Glucocorticoid regulation of polycyclic aromatic hydrocarbon induction of cytochrome P450IA1, glutathione S-transferases, and NAD(P) H:quinone oxidoreductase in cultured fetal rat hepatocytes. Mol. Pharmacol., 1990, 37(2), 198-205. (Pubitemid 20082983)
    • (1990) Molecular Pharmacology , vol.37 , Issue.2 , pp. 198-205
    • Sherratt, A.J.1    Banet, D.E.2    Prough, R.A.3
  • 130
    • 0025679098 scopus 로고
    • Influence of hormones and drugs on glutathione-S-transferase levels in primary culture of adult rat hepatocytes
    • Gebhardt, R.; Fitzke, H.; Fausel, M.; Eisenmann-Tappe, I.; Mecke, D. Influence of hormones and drugs on glutathione-S-transferase levels in primary culture of adult rat hepatocytes. Cell Biol. Toxicol., 1990, 6(4), 365-378.
    • (1990) Cell Biol. Toxicol. , vol.6 , Issue.4 , pp. 365-378
    • Gebhardt, R.1    Fitzke, H.2    Fausel, M.3    Eisenmann-Tappe, I.4    Mecke, D.5
  • 131
    • 0026817134 scopus 로고
    • Effects of ethanol, dexamethasone and RU 486 on expression of cytochromes P450 2B, 2E, 3A and glutathione transferase pi in a rat hepatoma cell line (Fao)
    • de Waziers, I.; Bouguet, J.; Beaune, P. H.; Gonzalez, F. J.; Ketterer, B.; Barouki, R. Effects of ethanol, dexamethasone and RU 486 on expression of cytochromes P450 2B, 2E, 3A and glutathione transferase pi in a rat hepatoma cell line (Fao). Pharmacogenetics, 1992, 2(1), 12-18.
    • (1992) Pharmacogenetics , vol.2 , Issue.1 , pp. 12-18
    • De Waziers, I.1    Bouguet, J.2    Beaune, P.H.3    Gonzalez, F.J.4    Ketterer, B.5    Barouki, R.6
  • 132
    • 0026718795 scopus 로고
    • Glucocorticoid androgen, and retinoic acid regulation of glutathione S-transferase gene expression in hamster smooth muscle tumor cells
    • Schwartz, D. A.; Norris, J. S. Glucocorticoid, androgen, and retinoic acid regulation of glutathione S-transferase gene expression in hamster smooth muscle tumor cells. Biochem. Biophys. Res. Commun., 1992, 184(2), 1108-1113.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , Issue.2 , pp. 1108-1113
    • Schwartz, D.A.1    Norris, J.S.2
  • 133
    • 0026780911 scopus 로고
    • Cloning of a muclass glutathione S-transferase gene and identification of the glucocorticoid regulatory domains in its 5' flanking sequence
    • Fan, W.; Trifiletti, R.; Cooper, T.; Norris, J. S. Cloning of a muclass glutathione S-transferase gene and identification of the glucocorticoid
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , Issue.13 , pp. 6104-6108
    • Fan, W.1    Trifiletti, R.2    Cooper, T.3    Norris, J.S.4
  • 134
    • 0026786828 scopus 로고
    • Suppression of glutathione transferase P expression by glucocorticoid
    • Sakai, M.; Muramatsu, M.; Nishi, S. Suppression of glutathione transferase P expression by glucocorticoid. Biochem. Biophys. Res. Commun., 1992, 187(2), 976-983.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , Issue.2 , pp. 976-983
    • Sakai, M.1    Muramatsu, M.2    Nishi, S.3
  • 135
    • 0027436837 scopus 로고
    • Expression of glutathione S-transferase P-form in primary cultured rat liver parenchymal cells by coplanar polychlorinated biphenyl congeners is suppressed by protein kinase inhibitors and dexamethasone
    • DOI 10.1016/0014-5793(93)80386-9
    • Aoki, Y.; Matsumoto, M.; Suzuki, K. T. Expression of glutathione S-transferase P-form in primary cultured rat liver parenchymal cells by coplanar polychlorinated biphenyl congeners is suppressed by protein kinase inhibitors and dexamethasone. FEBS Lett., 1993, 333(1-2), 114-118. (Pubitemid 23306950)
    • (1993) FEBS Letters , vol.333 , Issue.1-2 , pp. 114-118
    • Aoki, Y.1    Matsumoto, M.2    Suzuki, K.T.3
  • 136
    • 0030016238 scopus 로고    scopus 로고
    • Role of interleukin 6 and corticosteroids in the regulation of expression of glutathione S-transferases in primary cultures of rat hepatocytes
    • Voss, S. H.; Park, Y.; Kwon, S. O.; Whalen, R.; Boyer, T. D. Role of interleukin 6 and corticosteroids in the regulation of expression of glutathione S-transferases in primary cultures of rat hepatocytes. Biochem. J., 1996, 317 (Pt 2), 627-632. (Pubitemid 26254005)
    • (1996) Biochemical Journal , vol.317 , Issue.2 , pp. 627-632
    • Voss, S.H.1    Park, Y.2    Kwon, S.-O.3    Whalen, R.4    Boyer, T.D.5
  • 137
    • 0029859993 scopus 로고    scopus 로고
    • Hormonal regulation of hepatic enzymes involved in foreign compound metabolism
    • Prough, R. A.; Linder, M. W.; Pinaire, J. A.; Xiao, G. H.; Falkner, K. C. Hormonal regulation of hepatic enzymes involved in foreign compound metabolism. Faseb J., 1996, 10(12), 1369-1377. (Pubitemid 26347871)
    • (1996) FASEB Journal , vol.10 , Issue.12 , pp. 1369-1377
    • Prough, R.A.1    Linder, M.W.2    Pinaire, J.A.3    Xiao, G.-H.4    Falkner, K.C.5
  • 138
    • 0031865753 scopus 로고    scopus 로고
    • Negative regulation of the rat glutathione S-transferase A2 gene by glucocorticoids involves a canonical glucocorticoid consensus sequence
    • Falkner, K. C.; Rushmore, T. H.; Linder, M. W.; Prough, R. A. Negative regulation of the rat glutathione S-transferase A2 gene by glucocorticoids involves a canonical glucocorticoid consensus sequence. Mol. Pharmacol., 1998, 53(6), 1016-1026. (Pubitemid 28280443)
    • (1998) Molecular Pharmacology , vol.53 , Issue.6 , pp. 1016-1026
    • Falkner, K.C.1    Rushmore, T.H.2    Linder, M.W.3    Prough, R.A.4
  • 139
    • 0034866270 scopus 로고    scopus 로고
    • Regulation of the rat glutathione S-transferase A2 gene by glucocorticoids: Involvement of both the glucocorticoid and pregnane X receptors
    • Falkner, K. C.; Pinaire, J. A.; Xiao, G. H.; Geoghegan, T. E.; Prough, R. A. Regulation of the rat glutathione S-transferase A2 gene by glucocorticoids: Involvement of both the glucocorticoid and pregnane X receptors. Mol. Pharmacol., 2001, 60(3), 611-619. (Pubitemid 32781569)
    • (2001) Molecular Pharmacology , vol.60 , Issue.3 , pp. 611-619
    • Falkner, K.C.1    Pinaire, J.A.2    Xiao, G.-H.3    Geoghegan, T.E.4    Prough, R.A.5
  • 140
    • 18144417838 scopus 로고    scopus 로고
    • Glucocorticoid receptor (GR)-associated SMRT binding to C/EBPbeta TAD and Nrf2 Neh4/5: Role of SMRT recruited to GR in GSTA2 gene repression
    • Ki, S. H.; Cho, I. J.; Choi, D. W.; Kim, S. G. Glucocorticoid receptor (GR)-associated SMRT binding to C/EBPbeta TAD and Nrf2 Neh4/5: Role of SMRT recruited to GR in GSTA2 gene repression. Mol. Cell Biol., 2005, 25(10), 4150-4165.
    • (2005) Mol. Cell Biol. , vol.25 , Issue.10 , pp. 4150-4165
    • Ki, S.H.1    Cho, I.J.2    Choi, D.W.3    Kim, S.G.4
  • 141
    • 34548453027 scopus 로고    scopus 로고
    • Regulation of the rat glutathione S-transferase A2 gene by glucocorticoids: Crosstalk through C/EBPs
    • DOI 10.1080/03602530701511216, PII 781828749
    • Falkner, K. C.; Prough, R. A. Regulation of the rat glutathione Stransferase A2 gene by glucocorticoids: Crosstalk through C/EBPs. Drug Metab. Rev., 2007, 39(2-3), 401-418. (Pubitemid 47355729)
    • (2007) Drug Metabolism Reviews , vol.39 , Issue.2-3 , pp. 401-418
    • Falkner, K.C.1    Prough, R.A.2
  • 142
    • 77949612842 scopus 로고    scopus 로고
    • Glutathione S-transferase M1 inhibits dexamethasone-induced apoptosis in association with the suppression of Bim through dual mechanisms in a lymphoblastic leukemia cell line
    • Hosono, N.; Kishi, S.; Iho, S.; Urasaki, Y.; Yoshida, A.; Kurooka, H.; Yokota, Y.; Ueda, T. Glutathione S-transferase M1 inhibits dexamethasone-induced apoptosis in association with the suppression of Bim through dual mechanisms in a lymphoblastic leukemia cell line. Cancer Sci., 101(3), 767-773.
    • Cancer Sci. , vol.101 , Issue.3 , pp. 767-773
    • Hosono, N.1    Kishi, S.2    Iho, S.3    Urasaki, Y.4    Yoshida, A.5    Kurooka, H.6    Yokota, Y.7    Ueda, T.8
  • 143
    • 0031730369 scopus 로고    scopus 로고
    • Correlation of increased mortality with the suppression of radiation-inducible microsomal epoxide hydrolase and glutathione S-transferase gene expression by dexamethasone: Effects on vitamin C and E-induced radioprotection
    • DOI 10.1016/S0006-2952(98)00203-2, PII S0006295298002032
    • Nam, S. Y.; Cho, C. K.; Kim, S. G. Correlation of increased mortality with the suppression of radiation-inducible microsomal epoxide hydrolase and glutathione S-transferase gene expression by dexamethasone: Effects on vitamin C and E-induced radioprotection. Biochem. Pharmacol., 1998, 56(10), 1295-1304. (Pubitemid 28512677)
    • (1998) Biochemical Pharmacology , vol.56 , Issue.10 , pp. 1295-1304
    • Nam, S.Y.1    Cho, C.K.2    Kim, S.G.3
  • 144
    • 0029666445 scopus 로고    scopus 로고
    • 3 on the activity patterns of hepatic drug metabolizing enzymes in transplantable murine lymphoma
    • Sardar, S.; Chatterjee, M.; Ghosh, S.; Roy, K. Role of vitamin D3 on the activity patterns of hepatic drug metabolizing enzymes in transplantable murine lymphoma. Cancer Invest., 1996, 14(4), 328-334. (Pubitemid 26249170)
    • (1996) Cancer Investigation , vol.14 , Issue.4 , pp. 328-334
    • Sardar, S.1    Chatterjee, M.2    Ghosh, S.3    Roy, K.4
  • 145
    • 4444273792 scopus 로고    scopus 로고
    • 3 prevents DNA damage and restores antioxidant enzymes in rat hepatocarcinogenesis induced by diethylnitrosamine and promoted by phenobarbital
    • Banakar, M. C.; Paramasivan, S. K.; Chattopadhyay, M. B.; Datta, S.; Chakraborty, P.; Chatterjee, M.; Kannan, K.; Thygarajan, E. 1alpha, 25-dihydroxyvitamin D3 prevents DNA damage and restores antioxidant enzymes in rat hepatocarcinogenesis induced by diethylnitrosamine and promoted by phenobarbital. World J. Gastroenterol., 2004, 10(9), 1268-1275. (Pubitemid 39162429)
    • (2004) World Journal of Gastroenterology , vol.10 , Issue.9 , pp. 1268-1275
    • Banakar, M.C.1    Paramasivan, S.K.2    Chattopadhyay, M.B.3    Datta, S.4    Chakraborty, P.5    Chatterjee, M.6    Kannan, K.7    Thygarajan, E.8
  • 146
    • 0029022656 scopus 로고
    • Effect of ovariectomy and sex hormone replacement on glutathione and glutathione-related enzymes in rat hepatocarcinogenesis
    • Hambali, Z.; Ngah, W. Z.; Wahid, S. A.; Kadir, K. A. Effect of ovariectomy and sex hormone replacement on glutathione and glutathione-related enzymes in rat hepatocarcinogenesis. Pathology, 1995, 27(1), 30-35.
    • (1995) Pathology , vol.27 , Issue.1 , pp. 30-35
    • Hambali, Z.1    Ngah, W.Z.2    Wahid, S.A.3    Kadir, K.A.4
  • 147
    • 0032912877 scopus 로고    scopus 로고
    • Effects of progesterone and estradiol benzoate on glutathione dependent antioxidant enzyme activities in the brain of female rats
    • Pajovic, S. B.; Saicic, Z. S.; Spasic, M. B.; Petrovic, V. M.; Martinovic, J. V. Effects of progesterone and estradiol benzoate on glutathione dependent antioxidant enzyme activities in the brain of female rats. Gen. Physiol. Biophys., 1999, 18(1), 35-44. (Pubitemid 29238792)
    • (1999) General Physiology and Biophysics , vol.18 , Issue.1 , pp. 35-44
    • Pajovic, S.B.1    Saicic, Z.S.2    Spasic, M.B.3    Petrovic, V.M.4    Martinovic, J.V.5
  • 148
    • 33746928315 scopus 로고    scopus 로고
    • Alterations in hepatic metabolism of adult male rats following exposure to hydroxyprogesterone during embryonic development
    • DOI 10.1111/j.1745-7262.2006.00081.x
    • Pushpalatha, T.; Reddy, P. R.; Reddy, P. S. Alterations in hepatic metabolism of adult male rats following exposure to hydroxyprogesterone during embryonic development. Asian J. Androl., 2006, 8(4), 463-467. (Pubitemid 44304492)
    • (2006) Asian Journal of Andrology , vol.8 , Issue.4 , pp. 463-467
    • Pushpalatha, T.1    Reddy, P.R.2    Reddy, P.S.3
  • 149
    • 65049085551 scopus 로고    scopus 로고
    • Progesterone regulation of glutathione S-transferase Mu2 expression in mouse uterine luminal epithelium during preimplantation period
    • Ni, H.; Yu, X. J.; Liu, H. J.; Lei, W.; Rengaraj, D.; Li, X. J.; Yang, Z. M. Progesterone regulation of glutathione S-transferase Mu2 expression in mouse uterine luminal epithelium during preimplantation period. Fertil. Steril., 2009, 91(5 Suppl), 2123-2130.
    • (2009) Fertil. Steril. , vol.91 , Issue.5 SUPPL. , pp. 2123-2130
    • Ni, H.1    Yu, X.J.2    Liu, H.J.3    Lei, W.4    Rengaraj, D.5    Li, X.J.6    Yang, Z.M.7
  • 150
    • 0023011646 scopus 로고
    • Developmental and hormonal regulation of the major form of hepatic glutathione S-transferase in male mice
    • DOI 10.1016/0006-291X(86)90771-0
    • Hatayama, I.; Satoh, K.; Sato, K. Developmental and hormonal regulation of the major form of hepatic glutathione S-transferase in male mice. Biochem. Biophys. Res. Commun., 1986, 140(2), 581-588. (Pubitemid 17190101)
    • (1986) Biochemical and Biophysical Research Communications , vol.140 , Issue.2 , pp. 581-588
    • Hatayama, I.1    Satoh, K.2    Sato, K.3
  • 151
    • 0023645561 scopus 로고
    • Identification of glutathione S-transferase Yb1 mRNA as the androgen-repressed mRNA by cDNA cloning and sequence analysis
    • Chang, C. S.; Saltzman, A. G.; Sorensen, N. S.; Hiipakka, R. A.; Liao, S. S. Identification of glutathione S-transferase Yb1 mRNA as the androgen-repressed mRNA by cDNA cloning and sequence analysis. J. Biol. Chem., 1987, 262(25), 11901-11903.
    • (1987) J. Biol. Chem. , vol.262 , Issue.25 , pp. 11901-11903
    • Chang, C.S.1    Saltzman, A.G.2    Sorensen, N.S.3    Hiipakka, R.A.4    Liao, S.S.5
  • 152
    • 0032525802 scopus 로고    scopus 로고
    • Growth hormone- and testosterone-dependent regulation of glutathione transferase subunit A5 in rat liver
    • Staffas, L.; Ellis, E. M.; Hayes, J. D.; Lundgren, B.; Depierre, J. W.; Mankowitz, L. Growth hormone- and testosterone-dependent regulation of glutathione transferase subunit A5 in rat liver. Biochem. J., 1998, 332 (Pt 3), 763-768. (Pubitemid 28306703)
    • (1998) Biochemical Journal , vol.332 , Issue.3 , pp. 763-768
    • Staffas, L.1    Ellis, E.M.2    Hayes, J.D.3    Lundgren, B.4    DePierre, J.W.5    Mankowitz, L.6
  • 154
    • 0034671784 scopus 로고    scopus 로고
    • Quantitative and qualitative gender-related differences in jejunal glutathione S-transferase in the rat: Effect of testosterone administration
    • DOI 10.1016/S0024-3205(00)00948-6, PII S0024320500009486
    • Catania, V. A.; Luquita, M. G.; Sanchez Pozzi, E. J.; Mottino, A. D. Quantitative and qualitative gender-related differences in jejunal glutathione S-transferase in the rat effect of testosterone administration. Life Sci., 2000, 68(4), 467-474. (Pubitemid 32011898)
    • (2000) Life Sciences , vol.68 , Issue.4 , pp. 467-474
    • Catania, V.A.1    Luquita, M.G.2    Pozzi E.J.Sanchez3    Mottino, A.D.4
  • 155
    • 0035988214 scopus 로고    scopus 로고
    • Glutathione S-transferase alpha expressed in porcine Sertoli cells is under the control of follicle-stimulating hormone and testosterone
    • Benbrahim-Tallaa, L.; Tabone, E.; Tosser-Klopp, G.; Hatey, F.; Benahmed, M. Glutathione S-transferase alpha expressed in porcine Sertoli cells is under the control of follicle-stimulating hormone and testosterone. Biol. Reprod., 2002, 66(6), 1734-1742. (Pubitemid 34547270)
    • (2002) Biology of Reproduction , vol.66 , Issue.6 , pp. 1734-1742
    • Benbrahim-Tallaa, L.1    Tabone, E.2    Tosser-Klopp, G.3    Hatey, F.4    Benahmed, M.5
  • 156
    • 0025999721 scopus 로고
    • Selenium-dependent glutathione peroxidase expression is inversely related to estrogen receptor content of human breast cancer cells
    • Townsend, A. J.; Morrow, C. S.; Sinha, B. K.; Cowan, K. H. Selenium-dependent glutathione peroxidase expression is inversely related to estrogen receptor content of human breast cancer cells. Cancer Commun., 1991, 3(8), 265-270.
    • (1991) Cancer Commun. , vol.3 , Issue.8 , pp. 265-270
    • Townsend, A.J.1    Morrow, C.S.2    Sinha, B.K.3    Cowan, K.H.4
  • 158
    • 0026745056 scopus 로고
    • Posttranscriptional control of glutathione S-transferase pi gene expression in human breast cancer cells
    • Morrow, C. S.; Chiu, J.; Cowan, K. H. Posttranscriptional control of glutathione S-transferase pi gene expression in human breast cancer cells. J. Biol. Chem., 1992, 267(15), 10544-10550.
    • (1992) J. Biol. Chem. , vol.267 , Issue.15 , pp. 10544-10550
    • Morrow, C.S.1    Chiu, J.2    Cowan, K.H.3
  • 159
    • 0031589544 scopus 로고    scopus 로고
    • Role of posttranscriptional processes in the regulation of glutathione S-Transferase p1 gene expression in human breast cancer cells
    • DOI 10.1006/bbrc.1997.7109
    • Jhaveri, M. S.; Stephens, T. E.; Morrow, C. S. Role of posttranscriptional processes in the regulation of glutathione Stransferase P1 gene expression in human breast cancer cells. Biochem. Biophys. Res. Commun., 1997, 237(3), 729-734. (Pubitemid 27434756)
    • (1997) Biochemical and Biophysical Research Communications , vol.237 , Issue.3 , pp. 729-734
    • Jhaveri, M.S.1    Stephens, T.E.2    Morrow, C.S.3
  • 160
    • 0032498885 scopus 로고    scopus 로고
    • Contribution of proximal promoter elements to the regulation of basal and differential glutathione S-transferase P1 gene expression in human breast cancer cells
    • DOI 10.1016/S0167-4781(97)00187-5, PII S0167478197001875
    • Jhaveri, M. S.; Morrow, C. S. Contribution of proximal promoter elements to the regulation of basal and differential glutathione Stransferase P1 gene expression in human breast cancer cells. Biochim. Biophys. Acta, 1998, 1396(2), 179-190. (Pubitemid 28150180)
    • (1998) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1396 , Issue.2 , pp. 179-190
    • Jhaveri, M.S.1    Morrow, C.S.2
  • 161
    • 0032571585 scopus 로고    scopus 로고
    • Methylation-mediated regulation of the glutathione S-transferase P1 gene in human breast cancer cells
    • DOI 10.1016/S0378-1119(98)00021-3, PII S0378111998000213
    • Jhaveri, M. S.; Morrow, C. S. Methylation-mediated regulation of the glutathione S-transferase P1 gene in human breast cancer cells. Gene, 1998, 210(1), 1-7. (Pubitemid 28156380)
    • (1998) Gene , vol.210 , Issue.1 , pp. 1-7
    • Jhaveri, M.S.1    Morrow, C.S.2
  • 162
    • 0029806029 scopus 로고    scopus 로고
    • Glutathione-S-transferase in rat ovary: Its changes during estrous cycle and increase in its activity by estradiol-17 beta
    • Singh, D.; Pandey, R. S. Glutathione-S-transferase in rat ovary: Its changes during estrous cycle and increase in its activity by estradiol-17 beta. Indian J. Exp. Biol., 1996, 34(11), 1158-1160.
    • (1996) Indian J. Exp. Biol. , vol.34 , Issue.11 , pp. 1158-1160
    • Singh, D.1    Pandey, R.S.2
  • 163
    • 0347480514 scopus 로고    scopus 로고
    • Induction of NAD(P)H quinone oxidoreductase and glutathione S-transferase activities in livers of female August-Copenhagen Irish rats treated chronically with estradiol: Comparison with the Sprague-Dawley rat
    • DOI 10.1016/j.jsbmb.2003.08.007
    • Sanchez, R. I.; Mesia-Vela, S.; Kauffman, F. C. Induction of NAD(P)H quinone oxidoreductase and glutathione S-transferase activities in livers of female August-Copenhagen Irish rats treated chronically with estradiol: Comparison with the Sprague-Dawley rat. J. Steroid Biochem. Mol. Biol., 2003, 87(2-3), 199-206. (Pubitemid 37532527)
    • (2003) Journal of Steroid Biochemistry and Molecular Biology , vol.87 , Issue.2-3 , pp. 199-206
    • Sanchez, R.I.1    Mesia-Vela, S.2    Kauffman, F.C.3
  • 164
    • 1942436892 scopus 로고    scopus 로고
    • Transcriptional regulation by the estrogen receptor of antioxidative stress enzymes and its functional implications
    • DOI 10.1038/sj.onc.1207358
    • Montano, M. M.; Deng, H.; Liu, M.; Sun, X.; Singal, R. Transcriptional regulation by the estrogen receptor of antioxidative stress enzymes and its functional implications. Oncogene, 2004, 23(14), 2442-2453. (Pubitemid 38520742)
    • (2004) Oncogene , vol.23 , Issue.14 , pp. 2442-2453
    • Montano, M.M.1    Deng, H.2    Liu, M.3    Sun, X.4    Singal, R.5
  • 165
    • 27644506546 scopus 로고    scopus 로고
    • Estrogen receptor α increases basal and cigarette smoke extract-induced expression of CYP1A1 and CYP1B1, but not GSTP1, in normal human bronchial epithelial cells
    • DOI 10.1002/mc.20128
    • Han, W.; Pentecost, B. T.; Pietropaolo, R. L.; Fasco, M. J.; Spivack, S. D. Estrogen receptor alpha increases basal and cigarette smoke extract-induced expression of CYP1A1 and CYP1B1, but not GSTP1, in normal human bronchial epithelial cells. Mol. Carcinog., 2005, 44(3), 202-211. (Pubitemid 41552753)
    • (2005) Molecular Carcinogenesis , vol.44 , Issue.3 , pp. 202-211
    • Han, W.1    Pentecost, B.T.2    Pietropaolo, R.L.3    Fasco, M.J.4    Spivack, S.D.5
  • 166
    • 0025344002 scopus 로고
    • Human arylamine N-acetyltransferase genes: Isolation, chromosomal localization, and functional expression
    • Blum, M.; Grant, D. M.; McBride, W.; Heim, M.; Meyer, U. A. Human arylamine N-acetyltransferase genes: Isolation, chromosomal localization, and functional expression. DNA Cell Biol., 1990, 9(3), 193-203.
    • (1990) DNA Cell Biol. , vol.9 , Issue.3 , pp. 193-203
    • Blum, M.1    Grant, D.M.2    McBride, W.3    Heim, M.4    Meyer, U.A.5
  • 167
    • 47649088476 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferases: From structure to function
    • DOI 10.1080/03602530802186603, PII 795101507
    • Sim, E.; Walters, K.; Boukouvala, S. Arylamine N-acetyltransferases: From structure to function. Drug Metab. Rev., 2008, 40(3), 479-510. (Pubitemid 352019961)
    • (2008) Drug Metabolism Reviews , vol.40 , Issue.3 , pp. 479-510
    • Sim, E.1    Walters, K.2    Boukouvala, S.3
  • 169
    • 0028043708 scopus 로고
    • Structure-function studies of human arylamine N-acetyltransferases NAT1 and NAT2. Functional analysis of recombinant NAT1/NAT2 chimeras expressed in Escherichia coli
    • Dupret, J. M.; Goodfellow, G. H.; Janezic, S. A.; Grant, D. M. Structure-function studies of human arylamine N-acetyltransferases NAT1 and NAT2. Functional analysis of recombinant NAT1/NAT2 chimeras expressed in Escherichia coli. J. Biol. Chem., 1994, 269(43), 26830-26835.
    • (1994) J. Biol. Chem. , vol.269 , Issue.43 , pp. 26830-26835
    • Dupret, J.M.1    Goodfellow, G.H.2    Janezic, S.A.3    Grant, D.M.4
  • 170
    • 0036850037 scopus 로고    scopus 로고
    • Metabolic activation of the environmental contaminant 3-nitrobenzanthrone by human acetyltransferases and sulfotransferase
    • Arlt, V. M.; Glatt, H.; Muckel, E.; Pabel, U.; Sorg, B. L.; Schmeiser, H. H.; Phillips, D. H. Metabolic activation of the environmental contaminant 3-nitrobenzanthrone by human acetyltransferases and sulfotransferase. Carcinogenesis, 2002, 23(11), 1937-1945. (Pubitemid 35355944)
    • (2002) Carcinogenesis , vol.23 , Issue.11 , pp. 1937-1945
    • Arlt, V.M.1    Glatt, H.2    Muckel, E.3    Pabel, U.4    Sorg, B.L.5    Schmeiser, H.H.6    Phillips, D.H.7
  • 171
    • 44249120547 scopus 로고    scopus 로고
    • Identification of the xenobiotic-metabolizing enzyme arylamine N-acetyltransferase 1 as a new target of cisplatin in breast cancer cells: Molecular and cellular mechanisms of inhibition
    • DOI 10.1124/mol.108.045328
    • Ragunathan, N.; Dairou, J.; Pluvinage, B.; Martins, M.; Petit, E.; Janel, N.; Dupret, J. M.; Rodrigues-Lima, F. Identification of the xenobiotic-metabolizing enzyme arylamine N-acetyltransferase 1 as a new target of cisplatin in breast cancer cells: Molecular and cellular mechanisms of inhibition. Mol. Pharmacol., 2008, 73(6), 1761-1768. (Pubitemid 351724363)
    • (2008) Molecular Pharmacology , vol.73 , Issue.6 , pp. 1761-1768
    • Ragunathan, N.1    Dairou, J.2    Pluvinage, B.3    Martins, M.4    Petit, E.5    Janel, N.6    Dupret, J.-M.7    Rodrigues-Lima, F.8
  • 172
    • 77953489818 scopus 로고    scopus 로고
    • Human arylamine N-acetyltransferase 1: A drug-metabolizing enzyme and a drug target?
    • Rodrigues-Lima, F.; Dairou, J.; Busi, F.; Dupret, J. M. Human arylamine N-acetyltransferase 1: A drug-metabolizing enzyme and a drug target? Curr. Drug Targets, 11(6), 759-766.
    • Curr. Drug Targets , vol.11 , Issue.6 , pp. 759-766
    • Rodrigues-Lima, F.1    Dairou, J.2    Busi, F.3    Dupret, J.M.4
  • 173
    • 0037201542 scopus 로고    scopus 로고
    • Molecular genetics and function of NAT1 and NAT2: Role in aromatic amine metabolism and carcinogenesis
    • DOI 10.1016/S0027-5107(02)00153-7, PII S0027510702001537
    • Hein, D. W. Molecular genetics and function of NAT1 and NAT2: Role in aromatic amine metabolism and carcinogenesis. Mutat. Res., 2002, 506-507, 65-77. (Pubitemid 35286541)
    • (2002) Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis , vol.506-507 , pp. 65-77
    • Hein, D.W.1
  • 174
    • 0037917384 scopus 로고
    • Clinical implications of isoniazid blood levels in pulmonary tuberculosis
    • Mitchell, R. S.; Bell, J. C. Clinical implications of isoniazid blood levels in pulmonary tuberculosis. N. Engl. J. Med., 1957, 257(22), 1066-1070.
    • (1957) N. Engl. J. Med. , vol.257 , Issue.22 , pp. 1066-1070
    • Mitchell, R.S.1    Bell, J.C.2
  • 175
    • 0001120978 scopus 로고
    • A study of the renal clearances, metabolic inactivation rates, and serum fall-off interaction of isoniazid and paraminosalicylic acid in man
    • Jenne, J. W.; Macdonald, F. M.; Mendoza, E. A study of the renal clearances, metabolic inactivation rates, and serum fall-off interaction of isoniazid and paraminosalicylic acid in man. Am. Rev. Respir. Dis., 1961, 84, 371-378.
    • (1961) Am. Rev. Respir. Dis. , vol.84 , pp. 371-378
    • Jenne, J.W.1    Macdonald, F.M.2    Mendoza, E.3
  • 176
    • 0009758636 scopus 로고
    • Human acetylation polymorphism
    • Evans, D. A.; White, T. A. Human Acetylation Polymorphism. J. Lab Clin. Med., 1964, 63, 394-403.
    • (1964) J. Lab Clin. Med. , vol.63 , pp. 394-403
    • Evans, D.A.1    White, T.A.2
  • 177
    • 0033675835 scopus 로고    scopus 로고
    • Pharmacogenetics of the arylamine N-acetyltransferases: A symposium in honor of Wendell W. Weber
    • Hein, D. W.; McQueen, C. A.; Grant, D. M.; Goodfellow, G. H.; Kadlubar, F. F.; Weber, W. W. Pharmacogenetics of the arylamine N-acetyltransferases: A symposium in honor of Wendell W. Weber. Drug Metab. Dispos., 2000, 28(12), 1425-1432.
    • (2000) Drug Metab. Dispos. , vol.28 , Issue.12 , pp. 1425-1432
    • Hein, D.W.1    McQueen, C.A.2    Grant, D.M.3    Goodfellow, G.H.4    Kadlubar, F.F.5    Weber, W.W.6
  • 178
    • 0013830743 scopus 로고
    • Partial purification and properties of the isoniazid transacetylase in human liver. Its relationship to the acetylation of p-aminosalicylic acid
    • Jennne, J. W. Partial purification and properties of the isoniazid transacetylase in human liver. Its relationship to the acetylation of p-aminosalicylic acid. J. Clin. Invest., 1965, 44(12), 1992-2002.
    • (1965) J. Clin. Invest. , vol.44 , Issue.12 , pp. 1992-2002
    • Jennne, J.W.1
  • 180
    • 0027182143 scopus 로고
    • Structural heterogeneity of Caucasian N-acetyltransferase at the NAT1 gene locus
    • DOI 10.1006/abbi.1993.1116
    • Vatsis, K. P.; Weber, W. W. Structural heterogeneity of Caucasian N-acetyltransferase at the NAT1 gene locus. Arch. Biochem. Biophys., 1993, 301(1), 71-76. (Pubitemid 23227178)
    • (1993) Archives of Biochemistry and Biophysics , vol.301 , Issue.1 , pp. 71-76
    • Vatsis, K.P.1    Weber, W.W.2
  • 181
    • 38049061726 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferase 1 expression in breast cancer cell lines: A potential marker in estrogen receptorpositive tumors
    • Wakefield, L.; Robinson, J.; Long, H.; Ibbitt, J. C.; Cooke, S.; Hurst, H. C.; Sim, E. Arylamine N-acetyltransferase 1 expression in breast cancer cell lines: A potential marker in estrogen receptorpositive tumors. Genes Chromosomes Cancer, 2008, 47(2), 118-126.
    • (2008) Genes Chromosomes Cancer , vol.47 , Issue.2 , pp. 118-126
    • Wakefield, L.1    Robinson, J.2    Long, H.3    Ibbitt, J.C.4    Cooke, S.5    Hurst, H.C.6    Sim, E.7
  • 182
    • 0026586827 scopus 로고
    • Androgen receptors in operable breast cancer: Relation to other steroid hormone receptors, correlations to prognostic factors and predictive value for effect of adjuvant tamoxifen treatment
    • Soreide, J. A.; Lea, O. A.; Varhaug, J. E.; Skarstein, A.; Kvinnsland, S. Androgen receptors in operable breast cancer: Relation to other steroid hormone receptors, correlations to prognostic factors and predictive value for effect of adjuvant tamoxifen treatment. Eur. J. Surg. Oncol., 1992, 18(2), 112-118.
    • (1992) Eur. J. Surg. Oncol. , vol.18 , Issue.2 , pp. 112-118
    • Soreide, J.A.1    Lea, O.A.2    Varhaug, J.E.3    Skarstein, A.4    Kvinnsland, S.5
  • 183
    • 0036391671 scopus 로고    scopus 로고
    • Association of prostate cancer with rapid N-acetyltransferase 1 (NAT110) in combination with slow N-acetyltransferase 2 acetylator genotypes in a pilot case-control study
    • Hein, D. W.; Leff, M. A.; Ishibe, N.; Sinha, R.; Frazier, H. A.; Doll, M. A.; Xiao, G. H.; Weinrich, M. C.; Caporaso, N. E. Association of prostate cancer with rapid N-acetyltransferase 1 (NAT110) in combination with slow N-acetyltransferase 2 acetylator genotypes in a pilot case-control study. Environ. Mol. Mutagen, 2002, 40(3), 161-167.
    • (2002) Environ. Mol. Mutagen , vol.40 , Issue.3 , pp. 161-167
    • Hein, D.W.1    Leff, M.A.2    Ishibe, N.3    Sinha, R.4    Frazier, H.A.5    Doll, M.A.6    Xiao, G.H.7    Weinrich, M.C.8    Caporaso, N.E.9
  • 184
    • 47749111711 scopus 로고    scopus 로고
    • Regulation of arylamine N-acetyltransferases
    • DOI 10.2174/138920008784892128
    • Butcher, N. J.; Tiang, J.; Minchin, R. F. Regulation of arylamine N-acetyltransferases. Curr. Drug Metab., 2008, 9(6), 498-504. (Pubitemid 352025180)
    • (2008) Current Drug Metabolism , vol.9 , Issue.6 , pp. 498-504
    • Butcher, N.J.1    Tiang, J.2    Minchin, R.F.3
  • 185
    • 3242880312 scopus 로고    scopus 로고
    • Regulation of the activity of the human drug metabolizing enzyme arylamine N-acetyltransferase 1: Role of genetic and non genetic factors
    • DOI 10.2174/1381612043383845
    • Rodrigues-Lima, F.; Dupret, J. M. Regulation of the activity of the human drug metabolizing enzyme arylamine N-acetyltransferase 1: Role of genetic and non genetic factors. Curr. Pharm Des., 2004, 10(20), 2519-2524. (Pubitemid 38997431)
    • (2004) Current Pharmaceutical Design , vol.10 , Issue.20 , pp. 2519-2524
    • Rodrigues-Lima, F.1    Dupret, J.-M.2
  • 186
    • 17144376746 scopus 로고    scopus 로고
    • Genomic organization of human arylamine N-acetyltransferase Type I reveals alternative promoters that generate different 5′-UTR splice variants with altered translational activities
    • DOI 10.1042/BJ20040903
    • Butcher, N. J.; Arulpragasam, A.; Goh, H. L.; Davey, T.; Minchin, R. F. Genomic organization of human arylamine Nacetyltransferase Type I reveals alternative promoters that generate different 5'-UTR splice variants with altered translational activities. Biochem. J., 2005, 387(Pt 1), 119-127. (Pubitemid 40524081)
    • (2005) Biochemical Journal , vol.387 , Issue.1 , pp. 119-127
    • Butcher, N.J.1    Arulpragasam, A.2    Goh, H.L.3    Davey, T.4    Minchin, R.F.5
  • 187
    • 0025880699 scopus 로고
    • Structure and restriction fragment length polymorphism of genes for human liver arylamine Nacetyltransferases
    • Ebisawa, T.; Deguchi, T. Structure and restriction fragment length polymorphism of genes for human liver arylamine Nacetyltransferases. Biochem. Biophys. Res. Commun., 1991, 177(3), 1252-1257.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , Issue.3 , pp. 1252-1257
    • Ebisawa, T.1    Deguchi, T.2
  • 188
    • 0141444660 scopus 로고    scopus 로고
    • Structure and transcriptional regulation of the Nat2 gene encoding for the drug-metabolizing enzyme arylamine N-acetyltransferase type 2 in mice
    • DOI 10.1042/BJ20030812
    • Boukouvala, S.; Price, N.; Plant, K. E.; Sim, E. Structure and transcriptional regulation of the Nat2 gene encoding for the drugmetabolizing enzyme arylamine N-acetyltransferase type 2 in mice. Biochem J, 2003, 375(Pt 3), 593-602. (Pubitemid 37433507)
    • (2003) Biochemical Journal , vol.375 , Issue.3 , pp. 593-602
    • Boukouvala, S.1    Price, N.2    Plant, K.E.3    Sim, E.4
  • 189
    • 3242787887 scopus 로고    scopus 로고
    • Identification of the major promoter and non-coding exons of the human arylamine N-acetyltransferase 1 gene (NAT1)
    • DOI 10.1097/01.fpc.0000114755.08559.6e
    • Husain, A.; Barker, D. F.; States, J. C.; Doll, M. A.; Hein, D. W. Identification of the major promoter and non-coding exons of the human arylamine N-acetyltransferase 1 gene (NAT1). Pharmacogenetics, 2004, 14(7), 397-406. (Pubitemid 38971230)
    • (2004) Pharmacogenetics , vol.14 , Issue.7 , pp. 397-406
    • Husain, A.1    Barker, D.F.2    States, J.C.3    Doll, M.A.4    Hein, D.W.5
  • 190
    • 0032818433 scopus 로고    scopus 로고
    • N-acetyltransferase expression and DNA binding of N-hydroxyheterocyclic amines in human prostate epithelium
    • DOI 10.1093/carcin/20.8.1591
    • Wang, C. Y.; Debiec-Rychter, M.; Schut, H. A.; Morse, P.; Jones, R. F.; Archer, C.; King, C. M.; Haas, G. P. N-Acetyltransferase expression and DNA binding of N-hydroxyheterocyclic amines in human prostate epithelium. Carcinogenesis, 1999, 20(8), 1591-1595. (Pubitemid 29385450)
    • (1999) Carcinogenesis , vol.20 , Issue.8 , pp. 1591-1595
    • Wang, C.Y.1    Debiec-Rychter, M.2    Schut, H.A.J.3    Morse, P.4    Jones, R.F.5    Archer, C.6    King, C.M.7    Haas, G.P.8
  • 191
    • 33744485815 scopus 로고    scopus 로고
    • N-Acetyltransferase and sulfotransferase activity in human prostate: Potential for carcinogen activation
    • DOI 10.1097/01.fpc.0000204998.22301.09, PII 0121301120060600000002
    • Al-Buheissi, S. Z.; Patel, H. R.; Meinl, W.; Hewer, A.; Bryan, R. L.; Glatt, H.; Miller, R. A.; Phillips, D. H. N-Acetyltransferase and sulfotransferase activity in human prostate: Potential for carcinogen activation. Pharmacogenet. Genomics, 2006, 16(6), 391-399. (Pubitemid 43804797)
    • (2006) Pharmacogenetics and Genomics , vol.16 , Issue.6 , pp. 391-399
    • Al-Buheissi, S.Z.1    Patel, H.R.2    Meinl, W.3    Hewer, A.4    Bryan, R.L.5    Glatt, H.6    Miller, R.A.7    Phillips, D.H.8
  • 194
    • 33846403754 scopus 로고    scopus 로고
    • Induction of human arylamine N-acetyltransferase type I by androgens in human prostate cancer cells
    • DOI 10.1158/0008-5472.CAN-06-2635
    • Butcher, N. J.; Tetlow, N. L.; Cheung, C.; Broadhurst, G. M.; Minchin, R. F. Induction of human arylamine N-acetyltransferase type I by androgens in human prostate cancer cells. Cancer Res., 2007, 67(1), 85-92. (Pubitemid 46142762)
    • (2007) Cancer Research , vol.67 , Issue.1 , pp. 85-92
    • Butcher, N.J.1    Tetlow, N.L.2    Cheung, C.3    Broadhurst, G.M.4    Minchin, R.F.5
  • 195
    • 18844441459 scopus 로고    scopus 로고
    • Steroid hormones regulate gene expression posttranscriptionally by altering the stabilities of messenger RNAs
    • DOI 10.1095/biolreprod.105.040014
    • Ing, N. H. Steroid hormones regulate gene expression posttranscriptionally by altering the stabilities of messenger RNAs. Biol. Reprod., 2005, 72(6), 1290-1296. (Pubitemid 40696071)
    • (2005) Biology of Reproduction , vol.72 , Issue.6 , pp. 1290-1296
    • Ing, N.H.1
  • 196
    • 77952305207 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferase 1 gene regulation by androgens requires a conserved heat shock element for heat shock factor-1
    • Butcher, N. J.; Minchin, R. F. Arylamine N-acetyltransferase 1 gene regulation by androgens requires a conserved heat shock element for heat shock factor-1. Carcinogenesis, 31(5), 820-826.
    • Carcinogenesis , vol.31 , Issue.5 , pp. 820-826
    • Butcher, N.J.1    Minchin, R.F.2
  • 197
    • 0028918413 scopus 로고
    • Kinetics of human soluble and membrane-bound catechol O-methyltransferase: A revised mechanism and description of the thermolabile variant of the enzyme
    • Lotta, T.; Vidgren, J.; Tilgmann, C.; Ulmanen, I.; Melen, K.; Julkunen, I.; Taskinen, J. Kinetics of human soluble and membrane-bound catechol O-methyltransferase: A revised mechanism and description of the thermolabile variant of the enzyme. Biochemistry, 1995, 34(13), 4202-4210.
    • (1995) Biochemistry , vol.34 , Issue.13 , pp. 4202-4210
    • Lotta, T.1    Vidgren, J.2    Tilgmann, C.3    Ulmanen, I.4    Melen, K.5    Julkunen, I.6    Taskinen, J.7
  • 198
    • 0021341783 scopus 로고
    • Characterization of membrane-bound and soluble catechol-O- methyltransferase from human frontal cortex
    • Jeffery, D. R.; Roth, J. A. Characterization of membrane-bound and soluble catechol-O-methyltransferase from human frontal cortex. J. Neurochem., 1984, 42(3), 826-832. (Pubitemid 14198969)
    • (1984) Journal of Neurochemistry , vol.42 , Issue.3 , pp. 826-832
    • Jeffery, D.R.1    Roth, J.A.2
  • 199
    • 0020637004 scopus 로고
    • Localization of membranebound catechol-O-methyltransferase
    • Rivett, A. J.; Francis, A.; Roth, J. A. Localization of membranebound catechol-O-methyltransferase. J. Neurochem., 1983, 40(5), 1494-1496.
    • (1983) J. Neurochem. , vol.40 , Issue.5 , pp. 1494-1496
    • Rivett, A.J.1    Francis, A.2    Roth, J.A.3
  • 200
    • 0027416777 scopus 로고
    • Dynamics of melanogenesis intermediates
    • Pavel, S. Dynamics of melanogenesis intermediates. J. Invest. Dermatol., 1993, 100(2 Suppl), 162S-165S. (Pubitemid 23051692)
    • (1993) Journal of Investigative Dermatology , vol.100 , Issue.2 SUPPL.
    • Pavel, S.1
  • 202
    • 0015083327 scopus 로고
    • Enzymic methylation of L-ascorbic acid by catechol O-methyltransferase
    • Blaschke, E.; Hertting, G. Enzymic methylation of L-ascorbic acid by catechol O-methyltransferase. Biochem. Pharmacol., 1971, 20(7), 1363-1370.
    • (1971) Biochem. Pharmacol. , vol.20 , Issue.7 , pp. 1363-1370
    • Blaschke, E.1    Hertting, G.2
  • 205
    • 0025099288 scopus 로고
    • The O-methylation of 4-hydroxyestradiol is inhibited by 2-hydroxyestradiol: Implications for estrogen-induced carcinogenesis
    • Roy, D.; Weisz, J.; Liehr, J. G. The O-methylation of 4- hydroxyestradiol is inhibited by 2-hydroxyestradiol: Implications for estrogen-induced carcinogenesis. Carcinogenesis, 1990, 11(3), 459-462. (Pubitemid 20079400)
    • (1990) Carcinogenesis , vol.11 , Issue.3 , pp. 459-462
    • Roy, D.1    Weisz, J.2    Liehr, J.G.3
  • 206
    • 0017672676 scopus 로고
    • Catechol-O-methyltransferase in human breast cancers
    • Assicot, M.; Contesso, G.; Bohuon, C. Catechol-O-methyltransferase in human breast cancers. Eur. J. Cancer, 1977, 13(9), 961-966.
    • (1977) Eur. J. Cancer , vol.13 , Issue.9 , pp. 961-966
    • Assicot, M.1    Contesso, G.2    Bohuon, C.3
  • 207
    • 0018627984 scopus 로고
    • Catecholestrogen synthesis and metabolism by human breast tumors in vitro
    • Hoffman, A. R.; Paul, S. M.; Axelrod, J. Catecholestrogen synthesis and metabolism by human breast tumors in vitro. Cancer Res, 1979, 39(11), 4584-4587. (Pubitemid 10198635)
    • (1979) Cancer Research , vol.39 , Issue.11 , pp. 4584-4587
    • Hoffman, A.R.1    Paul, S.V.2    Axelrod, J.3
  • 208
    • 0038643355 scopus 로고
    • Merriam GR and Lipsett MB Ed.; Raven Press: New York
    • Longcope, C. In: Catechol estrogens; Merriam GR and Lipsett MB, Ed.; Raven Press: New York, 1983; Vol., pp.
    • (1983) Catechol Estrogens
    • Longcope, C.1
  • 209
    • 0027964721 scopus 로고
    • Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters
    • DOI 10.1111/j.1432-1033.1994.tb19083.x
    • Tenhunen, J.; Salminen, M.; Lundstrom, K.; Kiviluoto, T.; Savolainen, R.; Ulmanen, I. Genomic organization of the human catechol O-methyltransferase gene and its expression from two distinct promoters. Eur. J. Biochem., 1994, 223(3), 1049-1059. (Pubitemid 24263190)
    • (1994) European Journal of Biochemistry , vol.223 , Issue.3 , pp. 1049-1059
    • Tenhunen, J.1    Salminen, M.2    Lundstrom, K.3    Savolainen, R.4    Ulmanen, I.5
  • 210
    • 0026316817 scopus 로고
    • Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro
    • Ulmanen, I.; Lundstrom, K. Cell-free synthesis of rat and human catechol O-methyltransferase. Insertion of the membrane-bound form into microsomal membranes in vitro. Eur. J. Biochem., 1991, 202(3), 1013-1020.
    • (1991) Eur. J. Biochem. , vol.202 , Issue.3 , pp. 1013-1020
    • Ulmanen, I.1    Lundstrom, K.2
  • 211
    • 0027717355 scopus 로고
    • Production of rat soluble and membrane-bound catechol O-methyltransferase forms from bifunctional mRNAs
    • Tenhunen, J.; Ulmanen, I. Production of rat soluble and membranebound catechol O-methyltransferase forms from bifunctional mRNAs. Biochem. J., 1993, 296 (Pt 3), 595-600. (Pubitemid 24008173)
    • (1993) Biochemical Journal , vol.296 , Issue.3 , pp. 595-600
    • Tenhunen, J.1    Ulmanen, I.2
  • 212
    • 0027483404 scopus 로고
    • Structure of the rat catechol-O-methyltransferase gene: Separate promoters are used to produce mRNAs for soluble and membrane-bound forms of the enzyme
    • Tenhunen, J.; Salminen, M.; Jalanko, A.; Ukkonen, S.; Ulmanen, I. Structure of the rat catechol-O-methyltransferase gene: Separate promoters are used to produce mRNAs for soluble and membranebound forms of the enzyme. DNA Cell Biol., 1993, 12(3), 253-263. (Pubitemid 23121007)
    • (1993) DNA and Cell Biology , vol.12 , Issue.3 , pp. 253-263
    • Tenhunen, J.1    Salminen, M.2    Jalanko, A.3    Ukkonen, S.4    Ulmanen, I.5
  • 214
    • 0030004521 scopus 로고    scopus 로고
    • Human catechol-O-methyltransferase pharmacogenetics: Description of a functional polymorphism and its potential application to neuropsychiatric disorders
    • DOI 10.1097/00008571-199606000-00007
    • Lachman, H. M.; Papolos, D. F.; Saito, T.; Yu, Y. M.; Szumlanski, C. L.; Weinshilboum, R. M. Human catechol-O-methyltransferase pharmacogenetics: Description of a functional polymorphism and its potential application to neuropsychiatric disorders. Pharmacogenetics, 1996, 6(3), 243-250. (Pubitemid 26226317)
    • (1996) Pharmacogenetics , vol.6 , Issue.3 , pp. 243-250
    • Lachman, H.M.1    Papolos, D.F.2    Saito, T.3    Yu, Y.-M.4    Szumlanski, C.L.5    Weinshilboum, R.M.6
  • 215
    • 0016630402 scopus 로고
    • Variation in activity of monoamine metabolizing enzymes in rat liver during pregnancy
    • Parvez, S.; Parvez, S. H.; Youdim, M. B. Variation in activity of monoamine metabolizing enzymes in rat liver during pregnancy. Br. J. Pharmacol., 1975, 53(2), 241-246.
    • (1975) Br. J. Pharmacol. , vol.53 , Issue.2 , pp. 241-246
    • Parvez, S.1    Parvez, S.H.2    Youdim, M.B.3
  • 216
    • 0017165699 scopus 로고
    • Decreased phenylethanolamine- N-methyltransferase and catechol-O-methyltransferase activity in rabbit adrenal glands during pregnancy
    • Parvez, H.; Parvez, S.; Raza-Bukhari, A. Decreased phenylethanolamine- N-methyltransferase and catechol-O-methyltransferase activity in rabbit adrenal glands during pregnancy. Br. J. Pharmacol., 1976, 57(3), 413-416.
    • (1976) Br. J. Pharmacol. , vol.57 , Issue.3 , pp. 413-416
    • Parvez, H.1    Parvez, S.2    Raza-Bukhari, A.3
  • 217
    • 0025819502 scopus 로고
    • Induction of catechol-Omethyltransferase in the luminal epithelium of rat uterus by progesterone
    • Inoue, K.; Creveling, C. R. Induction of catechol-Omethyltransferase in the luminal epithelium of rat uterus by progesterone. J. Histochem. Cytochem., 1991, 39(6), 823-828.
    • (1991) J. Histochem. Cytochem. , vol.39 , Issue.6 , pp. 823-828
    • Inoue, K.1    Creveling, C.R.2
  • 218
    • 0018872193 scopus 로고
    • Erythrocyte COMT-activity in patients with affective disorders
    • Fahndrich, E.; Coper, H.; Christ, W.; Helmchen, H.; Muller- Oerlinghausen, B.; Pietzcker, A. Erythrocyte COMT-activity in patients with affective disorders. Acta Psychiatr. Scand., 1980, 61(5), 427-437. (Pubitemid 10076766)
    • (1980) Acta Psychiatrica Scandinavica , vol.61 , Issue.5 , pp. 427-437
    • Faehndrich, E.1    Coper, H.2    Christ, W.3
  • 219
    • 0019567627 scopus 로고
    • Erythrocyte catechol-Omethyltransferase activity in a Swedish population
    • Floderus, Y.; Ross, S. B.; Wetterberg, L. Erythrocyte catechol-Omethyltransferase activity in a Swedish population. Clin. Genet., 1981, 19(5), 389-392.
    • (1981) Clin. Genet. , vol.19 , Issue.5 , pp. 389-392
    • Floderus, Y.1    Ross, S.B.2    Wetterberg, L.3
  • 221
    • 0033060947 scopus 로고    scopus 로고
    • Characterization and implications of estrogenic down-regulation of human catechol-O-methyltransferase gene transcription
    • Xie, T.; Ho, S. L.; Ramsden, D. Characterization and implications of estrogenic down-regulation of human catechol-O-methyltransferase gene transcription. Mol. Pharmacol., 1999, 56(1), 31-38. (Pubitemid 29309809)
    • (1999) Molecular Pharmacology , vol.56 , Issue.1 , pp. 31-38
    • Xie, T.1    Ho, S.-L.2    Ramsden, D.3
  • 222
    • 0029147741 scopus 로고
    • Repression of the interleukin-6 promoter by estrogen receptor is mediated by NF-kappa B and C/EBP beta
    • Stein, B.; Yang, M. X. Repression of the interleukin-6 promoter by estrogen receptor is mediated by NF-kappa B and C/EBP beta. Mol. Cell Biol., 1995, 15(9), 4971-4979.
    • (1995) Mol. Cell Biol. , vol.15 , Issue.9 , pp. 4971-4979
    • Stein, B.1    Yang, M.X.2
  • 223
    • 0029889675 scopus 로고    scopus 로고
    • Involvement of CCAAT/enhancer-binding protein and nuclear factor-κB binding sites in interleukin-6 promoter inhibition by estrogens
    • DOI 10.1210/me.10.6.713
    • Galien, R.; Evans, H. F.; Garcia, T. Involvement of CCAAT/enhancer- binding protein and nuclear factor-kappa B binding sites in interleukin-6 promoter inhibition by estrogens. Mol.Endocrinol., 1996, 10(6), 713-722. (Pubitemid 26176279)
    • (1996) Molecular Endocrinology , vol.10 , Issue.6 , pp. 713-722
    • Galien, R.1    Evans, H.F.2    Garcia, T.3
  • 224
    • 0142027141 scopus 로고    scopus 로고
    • Human catechol-Omethyltransferase down-regulation by estradiol
    • Jiang, H.; Xie, T.; Ramsden, D. B.; Ho, S. L. Human catechol- Omethyltransferase down-regulation by estradiol. Neuropharmacology, 2003, 45(7), 1011-1018.
    • (2003) Neuropharmacology , vol.45 , Issue.7 , pp. 1011-1018
    • Jiang, H.1    Xie, T.2    Ramsden, D.B.3    Ho, S.L.4
  • 225
    • 50249104076 scopus 로고    scopus 로고
    • Catechol-O-methyltransferase (COMT): A gene contributing to sex differences in brain function, and to sexual dimorphism in the predisposition to psychiatric disorders
    • Harrison, P. J.; Tunbridge, E. M. Catechol-O-methyltransferase (COMT): A gene contributing to sex differences in brain function, and to sexual dimorphism in the predisposition to psychiatric disorders. Neuropsychopharmacology, 2008, 33(13), 3037-3045.
    • (2008) Neuropsychopharmacology , vol.33 , Issue.13 , pp. 3037-3045
    • Harrison, P.J.1    Tunbridge, E.M.2
  • 226
    • 0000609893 scopus 로고
    • Metabolism of thiopyrimidines and thiopurines. SMethylation with S-adenosylmethionine transmethylase and catabolism in mammalian tissues
    • Remy, C. N. Metabolism of thiopyrimidines and thiopurines. SMethylation with S-adenosylmethionine transmethylase and catabolism in mammalian tissues. J. Biol. Chem, 1963, 238, 1078-1084.
    • (1963) J. Biol. Chem , vol.238 , pp. 1078-1084
    • Remy, C.N.1
  • 227
    • 0020640116 scopus 로고
    • Human kidney thiopurine methyltransferase. Purification and biochemical properties
    • DOI 10.1016/0006-2952(83)90582-8
    • Woodson, L. C.; Weinshilboum, R. M. Human kidney thiopurine methyltransferase. Purification and biochemical properties. Biochem. Pharmacol., 1983, 32(5), 819-826. (Pubitemid 13128727)
    • (1983) Biochemical Pharmacology , vol.32 , Issue.5 , pp. 819-826
    • Woodson, L.C.1    Weinshilboum, R.M.2
  • 230
    • 0017890059 scopus 로고
    • Purification and characterization of rat liver microsomal thiol methyltransferase
    • Borchardt, R. T.; Cheng, C. F. Purification and characterization of rat liver microsomal thiol methyltransferase. Biochim. Biophys. Acta, 1978, 522(2), 340-353. (Pubitemid 8274348)
    • (1978) Biochimica et Biophysica Acta , vol.522 , Issue.2 , pp. 340-353
    • Borchardt, R.T.1    Cheng, C.F.2
  • 231
    • 0018668378 scopus 로고
    • Thiol S-methyltransferase from rat liver
    • DOI 10.1016/0003-9861(79)90317-5
    • Weisiger, R. A.; Jakoby, W. B. Thiol S-methyltransferase from rat liver. Arch Biochem. Biophys., 1979, 196(2), 631-637. (Pubitemid 10230171)
    • (1979) Archives of Biochemistry and Biophysics , vol.196 , Issue.2 , pp. 631-637
    • Weisiger, R.A.1    Jakoby, W.B.2
  • 233
    • 53549094372 scopus 로고    scopus 로고
    • Functional characterization of 23 allelic variants of thiopurine Smethyltransferase gene (TPMT*2-*24)
    • Ujiie, S.; Sasaki, T.; Mizugaki, M.; Ishikawa, M.; Hiratsuka, M. Functional characterization of 23 allelic variants of thiopurine Smethyltransferase gene (TPMT*2-*24). Pharmacogenet. Genomics, 2008, 18(10), 887-893.
    • (2008) Pharmacogenet. Genomics , vol.18 , Issue.10 , pp. 887-893
    • Ujiie, S.1    Sasaki, T.2    Mizugaki, M.3    Ishikawa, M.4    Hiratsuka, M.5
  • 235
    • 0018822866 scopus 로고
    • Mercaptopurine pharmacogenetics: Monogenic inheritance of erythrocyte thiopurine methyltransferase activity
    • Weinshilboum, R. M.; Sladek, S. L. Mercaptopurine pharmacogenetics: Monogenic inheritance of erythrocyte thiopurine methyltransferase activity. Am. J. Hum. Genet., 1980, 32(5), 651-662. (Pubitemid 10061685)
    • (1980) American Journal of Human Genetics , vol.32 , Issue.5 , pp. 651-662
    • Weinshilboum, R.M.1    Sladek, S.L.2
  • 236
    • 79952790933 scopus 로고    scopus 로고
    • Accessed August 11, 2010
    • Topic, E., Pharmacogenetic and tumour drugs-2005 http:// www.ifcc.org/ejifcc/vol16no2/160206200512.html (Accessed August 11, 2010).
    • (2005) Pharmacogenetic and Tumour Drugs
    • Topic, E.1
  • 238
    • 0029919807 scopus 로고    scopus 로고
    • Thiopurine S-methyltransferase deficiency: Two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians
    • Tai, H. L.; Krynetski, E. Y.; Yates, C. R.; Loennechen, T.; Fessing, M. Y.; Krynetskaia, N. F.; Evans, W. E. Thiopurine Smethyltransferase deficiency: Two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians. Am. J. Hum. Genet., 1996, 58(4), 694-702. (Pubitemid 26086658)
    • (1996) American Journal of Human Genetics , vol.58 , Issue.4 , pp. 694-702
    • Tai, H.-L.1    Krynetski, E.Y.2    Yates, C.R.3    Loennechen, T.4    Fessing, M.Y.5    Krynetskaia, N.F.6    Evans, W.E.7
  • 239
    • 77954360099 scopus 로고    scopus 로고
    • Thiopurine S-methyltransferase polymorphisms and thiopurine toxicity in treatment of inflammatory bowel disease
    • Dong, X. W.; Zheng, Q.; Zhu, M. M.; Tong, J. L.; Ran, Z. H. Thiopurine S-methyltransferase polymorphisms and thiopurine toxicity in treatment of inflammatory bowel disease. World J. Gastroenterol., 16(25), 3187-3195.
    • World J. Gastroenterol. , vol.16 , Issue.25 , pp. 3187-3195
    • Dong, X.W.1    Zheng, Q.2    Zhu, M.M.3    Tong, J.L.4    Ran, Z.H.5
  • 240
    • 0023119219 scopus 로고
    • Thiopurine pharmacogenetics in leukemia: Correlation of erythrocyte thiopurine methyltransferase activity and 6-thioguanine nucleotide concentrations
    • Lennard, L.; Van Loon, J. A.; Lilleyman, J. S.; Weinshilboum, R. M. Thiopurine pharmacogenetics in leukemia: Correlation of erythrocyte thiopurine methyltransferase activity and 6-thioguanine nucleotide concentrations. Clin. Pharmacol. Ther., 1987, 41(1), 18-25. (Pubitemid 17008125)
    • (1987) Clinical Pharmacology and Therapeutics , vol.41 , Issue.1 , pp. 18-25
    • Lennard, L.1    Van Loon, J.A.2    Lilleyman, J.S.3    Weinshilboum, R.M.4
  • 241
    • 0026907122 scopus 로고
    • Human liver thiopurine methyltransferase pharmacogenetics: Biochemical properties, liver-erythrocyte correlation and presence of isozymes
    • Szumlanski, C. L.; Honchel, R.; Scott, M. C.; Weinshilboum, R. M. Human liver thiopurine methyltransferase pharmacogenetics: Biochemical properties, liver-erythrocyte correlation and presence of isozymes. Pharmacogenetics, 1992, 2(4), 148-159.
    • (1992) Pharmacogenetics , vol.2 , Issue.4 , pp. 148-159
    • Szumlanski, C.L.1    Honchel, R.2    Scott, M.C.3    Weinshilboum, R.M.4
  • 242
    • 0017880983 scopus 로고
    • Human erythrocyte thiopurine methyltransferase: radiochemical microassay and biochemical properties
    • DOI 10.1016/0009-8981(78)90311-X
    • Weinshilboum, R. M.; Raymond, F. A.; Pazmino, P. A. Human erythrocyte thiopurine methyltransferase: Radiochemical microassay and biochemical properties. Clin. Chim. Acta, 1978, 85(3), 323-333. (Pubitemid 8333694)
    • (1978) Clinica Chimica Acta , vol.85 , Issue.3 , pp. 323-333
    • Weinshilboum, R.M.1    Raymond, F.A.2    Pazmino, P.A.3
  • 243
    • 0032530636 scopus 로고    scopus 로고
    • Functional characterization of the human thiopurine S-methyltransferase (TPMT) gene promoter
    • Fessing, M. Y.; Krynetski, E. Y.; Zambetti, G. P.; Evans, W. E. Functional characterization of the human thiopurine Smethyltransferase (TPMT) gene promoter. Eur. J. Biochem., 1998, 256(3), 510-517. (Pubitemid 28440416)
    • (1998) European Journal of Biochemistry , vol.256 , Issue.3 , pp. 510-517
    • Fessing, M.Y.1    Krynetski, E.Y.2    Zambetti, G.P.3    Evans, W.E.4
  • 244
    • 0031423467 scopus 로고    scopus 로고
    • Promoter and intronic sequences of the human thiopurine S- methyltransferase (TPMT) gene isolated from a human Pac1 genomic library
    • DOI 10.1023/A:1012111325397
    • Krynetski, E. Y.; Fessing, M. Y.; Yates, C. R.; Sun, D.; Schuetz, J. D.; Evans, W. E. Promoter and intronic sequences of the human thiopurine S-methyltransferase (TPMT) gene isolated from a human PAC1 genomic library. Pharm. Res., 1997, 14(12), 1672-1678. (Pubitemid 28062909)
    • (1997) Pharmaceutical Research , vol.14 , Issue.12 , pp. 1672-1678
    • Krynetski, E.Y.1    Fessing, M.Y.2    Yates, C.R.3    Sun, D.4    Schuetz, J.D.5    Evans, W.E.6
  • 246
    • 42149127136 scopus 로고    scopus 로고
    • Human drug metabolism genes in parathionand estrogen-treated breast cells
    • Calaf, G. M.; Roy, D. Human drug metabolism genes in parathionand estrogen-treated breast cells. Int. J. Mol. Med., 2007, 20(6), 875-881.
    • (2007) Int. J. Mol. Med. , vol.20 , Issue.6 , pp. 875-881
    • Calaf, G.M.1    Roy, D.2
  • 247
    • 34547154782 scopus 로고    scopus 로고
    • Amino acid conjugation: Contribution to the metabolism and toxicity of xenobiotic carboxylic acids
    • DOI 10.1517/17425255.3.2.159
    • Knights, K. M.; Sykes, M. J.; Miners, J. O. Amino acid conjugation: Contribution to the metabolism and toxicity of xenobiotic carboxylic acids. Expert Opin. Drug Metab. Toxicol., 2007, 3(2), 159-168. (Pubitemid 47316038)
    • (2007) Expert Opinion on Drug Metabolism and Toxicology , vol.3 , Issue.2 , pp. 159-168
    • Knights, K.M.1    Sykes, M.J.2    Miners, J.O.3
  • 248
    • 0013788916 scopus 로고
    • Pharmacokinetics of salicylate elimination in man
    • Levy, G. Pharmacokinetics of salicylate elimination in man. J. Pharm. Sci., 1965, 54(7), 959-967.
    • (1965) J. Pharm. Sci. , vol.54 , Issue.7 , pp. 959-967
    • Levy, G.1
  • 249
    • 0030657045 scopus 로고    scopus 로고
    • Developmental profile of mitochondrial glycine N-acyltransferase in human liver
    • DOI 10.1016/S0022-3476(97)70293-2
    • Mawal, Y.; Paradis, K.; Qureshi, I. A. Developmental profile of mitochondrial glycine N-acyltransferase in human liver. J. Pediatr., 1997, 130(6), 1003-1007. (Pubitemid 27495135)
    • (1997) Journal of Pediatrics , vol.130 , Issue.6 , pp. 1003-1007
    • Mawal, Y.1    Paradis, K.2    Qureshi, I.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.