메뉴 건너뛰기




Volumn 10, Issue 7, 2009, Pages 713-729

Insights into the structure, function, and regulation of human cytochrome P450 1A2

Author keywords

Aromatic hydrocarbon receptor; CYP1A2; Inducer; Inhibitor; Substrate

Indexed keywords

ALPHA NAPHTHOFLAVONE; APIGENIN; ARISTOLOCHIC ACID; AROMATIC HYDROCARBON RECEPTOR; CARCINOGEN; CELECOXIB; CIPROFLOXACIN; CLOZAPINE; COUMARIN; CYCLOBENZAPRINE; CYTOCHROME P450 1A1; CYTOCHROME P450 1A2; CYTOCHROME P450 2A6; CYTOCHROME P450 3A4; DIURON; ISOSAFROLE; LEFLUNOMIDE; LIDOCAINE; MELATONIN; OLTIPRAZ; PHENAZONE; POLYCYCLIC AROMATIC HYDROCARBON; PROPOFOL; RETINOID; RILUZOLE; ROFECOXIB; TACRINE; THEOPHYLLINE; UNINDEXED DRUG; VENLAFAXINE;

EID: 66449111462     PISSN: 13892002     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920009789895552     Document Type: Review
Times cited : (70)

References (295)
  • 1
    • 0028237729 scopus 로고
    • Interindividual variations in human liver cytochrome P450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals
    • Shimada, T.; Yamazaki, H.; Mimura, M.; Inui, Y.; Guengerich, F. P. Interindividual variations in human liver cytochrome P450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals. J. Pharmacol. Exp. Ther., 1994, 270(1), 414-423.
    • (1994) J. Pharmacol. Exp. Ther , vol.270 , Issue.1 , pp. 414-423
    • Shimada, T.1    Yamazaki, H.2    Mimura, M.3    Inui, Y.4    Guengerich, F.P.5
  • 3
    • 0032963857 scopus 로고    scopus 로고
    • Cytochrome P-450 1A1 expression in human small bowel: Interindividual variation and inhibition by ketoconazole
    • Paine, M. F.; Schmiedlin-Ren, P.; Watkins, P. B. Cytochrome P-450 1A1 expression in human small bowel: interindividual variation and inhibition by ketoconazole. Drug Metab. Dispos., 1999, 27(3), 360-364.
    • (1999) Drug Metab. Dispos , vol.27 , Issue.3 , pp. 360-364
    • Paine, M.F.1    Schmiedlin-Ren, P.2    Watkins, P.B.3
  • 4
    • 0029998275 scopus 로고    scopus 로고
    • Comparative studies of drug-metabolizing enzymes in dog, monkey, and human small intestines, and in Caco-2 cells
    • Prueksaritanont, T.; Gorham, L. M.; Hochman, J. H.; Tran, L. O.; Vyas, K. P. Comparative studies of drug-metabolizing enzymes in dog, monkey, and human small intestines, and in Caco-2 cells. Drug Metab. Dispos., 1996, 24(6), 634-642.
    • (1996) Drug Metab. Dispos , vol.24 , Issue.6 , pp. 634-642
    • Prueksaritanont, T.1    Gorham, L.M.2    Hochman, J.H.3    Tran, L.O.4    Vyas, K.P.5
  • 5
    • 0030006119 scopus 로고    scopus 로고
    • Characterization of microsomal cytochrome P450 enzymes involved in the oxidation of xenobiotic chemicals in human fetal liver and adult lungs
    • Shimada, T.; Yamazaki, H.; Mimura, M.; Wakamiya, N.; Ueng, Y. F.; Guengerich, F. P.; Inui, Y. Characterization of microsomal cytochrome P450 enzymes involved in the oxidation of xenobiotic chemicals in human fetal liver and adult lungs. Drug Metab. Dispos., 1996, 24(5), 515-522.
    • (1996) Drug Metab. Dispos , vol.24 , Issue.5 , pp. 515-522
    • Shimada, T.1    Yamazaki, H.2    Mimura, M.3    Wakamiya, N.4    Ueng, Y.F.5    Guengerich, F.P.6    Inui, Y.7
  • 8
    • 0027439096 scopus 로고
    • CYP1A1 mRNA levels as a human exposure biomarker: Use of quantitative polymerase chain reaction to measure CYP1A1 expression in human peripheral blood lymphocytes
    • Vanden Heuvel, J. P.; Clark, G. C.; Thompson, C. L.; McCoy, Z.; Miller, C. R.; Lucier, G. W.; Bell, D. A. CYP1A1 mRNA levels as a human exposure biomarker: use of quantitative polymerase chain reaction to measure CYP1A1 expression in human peripheral blood lymphocytes. Carcinogenesis, 1993, 14(10), 2003-2006.
    • (1993) Carcinogenesis , vol.14 , Issue.10 , pp. 2003-2006
    • Vanden Heuvel, J.P.1    Clark, G.C.2    Thompson, C.L.3    McCoy, Z.4    Miller, C.R.5    Lucier, G.W.6    Bell, D.A.7
  • 9
    • 0035876315 scopus 로고    scopus 로고
    • Cytochrome P450 1A1 (CYP1A1) in blood lymphocytes evidence for catalytic activity and mRNA expression
    • Dey, A.; Parmar, D.; Dayal, M.; Dhawan, A.; Seth, P. K. Cytochrome P450 1A1 (CYP1A1) in blood lymphocytes evidence for catalytic activity and mRNA expression. Life Sci., 2001, 69(4), 383-393.
    • (2001) Life Sci , vol.69 , Issue.4 , pp. 383-393
    • Dey, A.1    Parmar, D.2    Dayal, M.3    Dhawan, A.4    Seth, P.K.5
  • 10
    • 18144430252 scopus 로고    scopus 로고
    • Cytochrome P450 1A1 and 1B1 in human blood lymphocytes are not suitable as biomarkers of exposure to dioxin-like compounds: Polymorphisms and interindividual variation in expression and inducibility
    • van Duursen, M. B.; Sanderson, J. T.; van den Berg, M. Cytochrome P450 1A1 and 1B1 in human blood lymphocytes are not suitable as biomarkers of exposure to dioxin-like compounds: polymorphisms and interindividual variation in expression and inducibility. Toxicol. Sci., 2005, 85(1), 703-712.
    • (2005) Toxicol. Sci , vol.85 , Issue.1 , pp. 703-712
    • van Duursen, M.B.1    Sanderson, J.T.2    van den Berg, M.3
  • 11
    • 0034988335 scopus 로고    scopus 로고
    • Uncertainty factors for chemical risk assessment: Interspecies differences in the in vivo pharmacokinetics and metabolism of human CYP1A2 substrates
    • Walton, K.; Dorne, J. L.; Renwick, A. G. Uncertainty factors for chemical risk assessment: interspecies differences in the in vivo pharmacokinetics and metabolism of human CYP1A2 substrates. Food Chem. Toxicol., 2001, 39(7), 667-680.
    • (2001) Food Chem. Toxicol , vol.39 , Issue.7 , pp. 667-680
    • Walton, K.1    Dorne, J.L.2    Renwick, A.G.3
  • 12
    • 0031962621 scopus 로고    scopus 로고
    • Differential selectivity of cytochrome P450 inhibitors against probe substrates in human and rat liver microsomes
    • Eagling, V. A.; Tjia, J. F.; Back, D. J. Differential selectivity of cytochrome P450 inhibitors against probe substrates in human and rat liver microsomes. Br. J. Clin. Pharmacol., 1998, 45(2), 107-114.
    • (1998) Br. J. Clin. Pharmacol , vol.45 , Issue.2 , pp. 107-114
    • Eagling, V.A.1    Tjia, J.F.2    Back, D.J.3
  • 13
    • 44949222437 scopus 로고    scopus 로고
    • Variation in CYP1A2 activity and its clinical implications: Influence of environmental factors and genetic polymorphisms
    • Gunes, A.; Dahl, M. L. Variation in CYP1A2 activity and its clinical implications: influence of environmental factors and genetic polymorphisms. Pharmacogenomics, 2008, 9(5), 625-637.
    • (2008) Pharmacogenomics , vol.9 , Issue.5 , pp. 625-637
    • Gunes, A.1    Dahl, M.L.2
  • 14
    • 0024445437 scopus 로고
    • Human CYP1A2: Sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression
    • Ikeya, K.; Jaiswal, A. K.; Owens, R. A.; Jones, J. E.; Nebert, D. W.; Kimura, S. Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. Mol. Endocrinol., 1989, 3(9), 1399-1408.
    • (1989) Mol. Endocrinol , vol.3 , Issue.9 , pp. 1399-1408
    • Ikeya, K.1    Jaiswal, A.K.2    Owens, R.A.3    Jones, J.E.4    Nebert, D.W.5    Kimura, S.6
  • 15
    • 0036667961 scopus 로고    scopus 로고
    • The interindividual differences in the 3-demthylation of caffeine alias CYP1A2 is determined by both genetic and environmental factors
    • Rasmussen, B. B.; Brix, T. H.; Kyvik, K. O.; Brosen, K. The interindividual differences in the 3-demthylation of caffeine alias CYP1A2 is determined by both genetic and environmental factors. Pharmacogenetics, 2002, 12(6), 473-478.
    • (2002) Pharmacogenetics , vol.12 , Issue.6 , pp. 473-478
    • Rasmussen, B.B.1    Brix, T.H.2    Kyvik, K.O.3    Brosen, K.4
  • 16
    • 33745147237 scopus 로고    scopus 로고
    • Use of 7-ethoxycoumarin to monitor multiple enzymes in the human CYP1, CYP2, and CYP3 families
    • Waxman, D. J.; Chang, T. K. Use of 7-ethoxycoumarin to monitor multiple enzymes in the human CYP1, CYP2, and CYP3 families. Methods Mol. Biol., 2006, 320, 153-156.
    • (2006) Methods Mol. Biol , vol.320 , pp. 153-156
    • Waxman, D.J.1    Chang, T.K.2
  • 17
    • 0030064194 scopus 로고    scopus 로고
    • 7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes
    • Yamazaki, H.; Inoue, K.; Mimura, M.; Oda, Y.; Guengerich, F. P.; Shimada, T. 7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes. Biochem. Pharmacol., 1996, 51(3), 313-319.
    • (1996) Biochem. Pharmacol , vol.51 , Issue.3 , pp. 313-319
    • Yamazaki, H.1    Inoue, K.2    Mimura, M.3    Oda, Y.4    Guengerich, F.P.5    Shimada, T.6
  • 18
    • 33745172501 scopus 로고    scopus 로고
    • Enzymatic analysis of cDNAexpressed human CYP1A1, CYP1A2, and CYP1B1 with 7-ethoxyresorufin as substrate
    • Chang, T. K.; Waxman, D. J. Enzymatic analysis of cDNAexpressed human CYP1A1, CYP1A2, and CYP1B1 with 7-ethoxyresorufin as substrate. Methods Mol. Biol., 2006, 320, 85-90.
    • (2006) Methods Mol. Biol , vol.320 , pp. 85-90
    • Chang, T.K.1    Waxman, D.J.2
  • 19
    • 0029769679 scopus 로고    scopus 로고
    • The influence of ethnic factors and gender on CYP1A2-mediated drug disposition: A comparative study in Caucasian and Chinese subjects using phenacetin as a marker substrate
    • Bartoli, A.; Xiaodong, S.; Gatti, G.; Cipolla, G.; Marchiselli, R.; Perucca, E. The influence of ethnic factors and gender on CYP1A2-mediated drug disposition: a comparative study in Caucasian and Chinese subjects using phenacetin as a marker substrate. Ther. Drug Monit., 1996, 18(5), 586-591.
    • (1996) Ther. Drug Monit , vol.18 , Issue.5 , pp. 586-591
    • Bartoli, A.1    Xiaodong, S.2    Gatti, G.3    Cipolla, G.4    Marchiselli, R.5    Perucca, E.6
  • 20
    • 0025969276 scopus 로고
    • Caffeine as a metabolic probe: Exploration of the enzyme-inducing effect of cigarette smoking
    • Kalow, W.; Tang, B. K. Caffeine as a metabolic probe: exploration of the enzyme-inducing effect of cigarette smoking. Clin. Pharmacol. Ther., 1991, 49(1), 44-48.
    • (1991) Clin. Pharmacol. Ther , vol.49 , Issue.1 , pp. 44-48
    • Kalow, W.1    Tang, B.K.2
  • 22
    • 0033865134 scopus 로고    scopus 로고
    • Evaluation of caffeine as an in vivo probe for CYP1A2 using measurements in plasma, saliva, and urine
    • Carrillo, J. A.; Christensen, M.; Ramos, S. I.; Alm, C.; Dahl, M. L.; Benitez, J.; Bertilsson, L. Evaluation of caffeine as an in vivo probe for CYP1A2 using measurements in plasma, saliva, and urine. Ther. Drug Monit., 2000, 22(4), 409-417.
    • (2000) Ther. Drug Monit , vol.22 , Issue.4 , pp. 409-417
    • Carrillo, J.A.1    Christensen, M.2    Ramos, S.I.3    Alm, C.4    Dahl, M.L.5    Benitez, J.6    Bertilsson, L.7
  • 23
    • 35448974964 scopus 로고    scopus 로고
    • Development of the "Inje cocktail" for high-throughput evaluation of five human cytochrome P450 isoforms in vivo
    • Ryu, J. Y.; Song, I. S.; Sunwoo, Y. E.; Shon, J. H.; Liu, K. H.; Cha, I. J.; Shin, J. G. Development of the "Inje cocktail" for high-throughput evaluation of five human cytochrome P450 isoforms in vivo. Clin. Pharmacol. Ther., 2007, 82(5), 531-540.
    • (2007) Clin. Pharmacol. Ther , vol.82 , Issue.5 , pp. 531-540
    • Ryu, J.Y.1    Song, I.S.2    Sunwoo, Y.E.3    Shon, J.H.4    Liu, K.H.5    Cha, I.J.6    Shin, J.G.7
  • 25
    • 0028929645 scopus 로고
    • Metabolism of theophylline by cDNA-expressed human cytochromes P-450
    • Ha, H. R.; Chen, J.; Freiburghaus, A. U.; Follath, F. Metabolism of theophylline by cDNA-expressed human cytochromes P-450. Br. J. Clin. Pharmacol., 1995, 39(3), 321-326.
    • (1995) Br. J. Clin. Pharmacol , vol.39 , Issue.3 , pp. 321-326
    • Ha, H.R.1    Chen, J.2    Freiburghaus, A.U.3    Follath, F.4
  • 26
    • 0026508999 scopus 로고
    • Characterization of human liver cytochromes P450 involved in theophylline metabolism
    • Sarkar, M. A.; Hunt, C.; Guzelian, P. S.; Karnes, H. T. Characterization of human liver cytochromes P450 involved in theophylline metabolism. Drug Metab. Dispos., 1992, 20(1), 31-37.
    • (1992) Drug Metab. Dispos , vol.20 , Issue.1 , pp. 31-37
    • Sarkar, M.A.1    Hunt, C.2    Guzelian, P.S.3    Karnes, H.T.4
  • 27
    • 0029018483 scopus 로고
    • Characterization of human cytochromes P450 involved in theophylline 8-hydroxylation
    • Zhang, Z. Y.; Kaminsky, L. S. Characterization of human cytochromes P450 involved in theophylline 8-hydroxylation. Biochem. Pharmacol., 1995, 50(2), 205-211.
    • (1995) Biochem. Pharmacol , vol.50 , Issue.2 , pp. 205-211
    • Zhang, Z.Y.1    Kaminsky, L.S.2
  • 28
    • 0027973024 scopus 로고
    • Theophylline N-demethylations as probes for P4501A1 and P4501A2
    • Sarkar, M. A.; Jackson, B. J. Theophylline N-demethylations as probes for P4501A1 and P4501A2. Drug Metab. Dispos., 1994, 22(6), 827-834.
    • (1994) Drug Metab. Dispos , vol.22 , Issue.6 , pp. 827-834
    • Sarkar, M.A.1    Jackson, B.J.2
  • 29
    • 0030094638 scopus 로고    scopus 로고
    • Theophylline metabolism in human liver microsomes: Inhibition studies
    • Tjia, J. F.; Colbert, J.; Back, D. J. Theophylline metabolism in human liver microsomes: inhibition studies. J Pharmacol. Exp. Ther., 1996, 276(3), 912-917.
    • (1996) J Pharmacol. Exp. Ther , vol.276 , Issue.3 , pp. 912-917
    • Tjia, J.F.1    Colbert, J.2    Back, D.J.3
  • 30
    • 0026849441 scopus 로고
    • Biotransformation of caffeine, paraxanthine, theobromine and theophylline by cDNA-expressed human CYP1A2 and CYP2E1
    • Gu, L.; Gonzalez, F. J.; Kalow, W.; Tang, B. K. Biotransformation of caffeine, paraxanthine, theobromine and theophylline by cDNA-expressed human CYP1A2 and CYP2E1. Pharmacogenetics, 1992, 2(2), 73-77.
    • (1992) Pharmacogenetics , vol.2 , Issue.2 , pp. 73-77
    • Gu, L.1    Gonzalez, F.J.2    Kalow, W.3    Tang, B.K.4
  • 32
    • 0032934859 scopus 로고    scopus 로고
    • Contribution of human hepatic cytochrome P450s and steroidogenic CYP17 to the N-demethylation of aminopyrine
    • Niwa, T.; Sato, R.; Yabusaki, Y.; Ishibashi, F.; Katagiri, M. Contribution of human hepatic cytochrome P450s and steroidogenic CYP17 to the N-demethylation of aminopyrine. Xenobiotica, 1999, 29(2), 187-193.
    • (1999) Xenobiotica , vol.29 , Issue.2 , pp. 187-193
    • Niwa, T.1    Sato, R.2    Yabusaki, Y.3    Ishibashi, F.4    Katagiri, M.5
  • 34
    • 0033783019 scopus 로고    scopus 로고
    • A significant role of human cytochrome P4502C8 in amiodarone N-deethylation: An approach to predict the contribution with relative activity factor
    • Ohyama, K.; Nakajima, M.; Nakamura, S.; Shimada, N.; Yamazaki, H.; Yokoi, T. A significant role of human cytochrome P4502C8 in amiodarone N-deethylation: An approach to predict the contribution with relative activity factor. Drug Metab. Dispos., 2000, 28(11), 1303-1310.
    • (2000) Drug Metab. Dispos , vol.28 , Issue.11 , pp. 1303-1310
    • Ohyama, K.1    Nakajima, M.2    Nakamura, S.3    Shimada, N.4    Yamazaki, H.5    Yokoi, T.6
  • 35
    • 0141842760 scopus 로고    scopus 로고
    • Concentration dependent stereoselectivity of propafenone N-depropylation metabolism with human hepatic recombinant CYP1A2
    • Zhou, Q.; Yao, T. W.; Yu, Y. N.; Zeng, S. Concentration dependent stereoselectivity of propafenone N-depropylation metabolism with human hepatic recombinant CYP1A2. Pharmazie, 2003, 58(9), 651-653.
    • (2003) Pharmazie , vol.58 , Issue.9 , pp. 651-653
    • Zhou, Q.1    Yao, T.W.2    Yu, Y.N.3    Zeng, S.4
  • 36
    • 0027460033 scopus 로고
    • Identification and characterization of the cytochrome P450 enzymes involved in N-dealkylation of propafenone: Molecular base for interaction potential and variable disposition of active metabolites
    • Botsch, S.; Gautier, J. C.; Beaune, P.; Eichelbaum, M.; Kroemer, H. K. Identification and characterization of the cytochrome P450 enzymes involved in N-dealkylation of propafenone: molecular base for interaction potential and variable disposition of active metabolites. Mol. Pharmacol., 1993, 43(1), 120-126.
    • (1993) Mol. Pharmacol , vol.43 , Issue.1 , pp. 120-126
    • Botsch, S.1    Gautier, J.C.2    Beaune, P.3    Eichelbaum, M.4    Kroemer, H.K.5
  • 37
    • 0033739717 scopus 로고    scopus 로고
    • Bioactivation of tegafur to 5-fluorouracil is catalyzed by cytochrome P450 2A6 in human liver microsomes in vitro
    • Ikeda, K.; Yoshisue, K.; Matsushima, E.; Nagayama, S.; Kobayashi, K.; Tyson, C. A.; Chiba, K.; Kawaguchi, Y. Bioactivation of tegafur to 5-fluorouracil is catalyzed by cytochrome P450 2A6 in human liver microsomes in vitro. Clin. Cancer Res., 2000, 6(11), 4409-4415.
    • (2000) Clin. Cancer Res , vol.6 , Issue.11 , pp. 4409-4415
    • Ikeda, K.1    Yoshisue, K.2    Matsushima, E.3    Nagayama, S.4    Kobayashi, K.5    Tyson, C.A.6    Chiba, K.7    Kawaguchi, Y.8
  • 38
    • 0033664818 scopus 로고    scopus 로고
    • Roles of cytochromes P450 1A2, 2A6, and 2C8 in 5-fluorouracil formation from tegafur, an anticancer prodrug, in human liver microsomes
    • Komatsu, T.; Yamazaki, H.; Shimada, N.; Nakajima, M.; Yokoi, T. Roles of cytochromes P450 1A2, 2A6, and 2C8 in 5-fluorouracil formation from tegafur, an anticancer prodrug, in human liver microsomes. Drug Metab. Dispos., 2000, 28(12), 1457-1463.
    • (2000) Drug Metab. Dispos , vol.28 , Issue.12 , pp. 1457-1463
    • Komatsu, T.1    Yamazaki, H.2    Shimada, N.3    Nakajima, M.4    Yokoi, T.5
  • 39
    • 33645826544 scopus 로고    scopus 로고
    • Detection of a new N-oxidized metabolite of flutamide, N-[4-nitro-3-(trifluoromethyl) phenyl]hydroxylamine, in human liver microsomes and urine of prostate cancer patients
    • Goda, R.; Nagai, D.; Akiyama, Y.; Nishikawa, K.; Ikemoto, I.; Aizawa, Y.; Nagata, K.; Yamazoe, Y. Detection of a new N-oxidized metabolite of flutamide, N-[4-nitro-3-(trifluoromethyl) phenyl]hydroxylamine, in human liver microsomes and urine of prostate cancer patients. Drug Metab. Dispos., 2006, 34(5), 828-835.
    • (2006) Drug Metab. Dispos , vol.34 , Issue.5 , pp. 828-835
    • Goda, R.1    Nagai, D.2    Akiyama, Y.3    Nishikawa, K.4    Ikemoto, I.5    Aizawa, Y.6    Nagata, K.7    Yamazoe, Y.8
  • 41
    • 0037377922 scopus 로고    scopus 로고
    • Thalidomide-induced suppression of embryo fibroblast proliferation requires CYP1A1-mediated activation
    • Miyata, M.; Tamura, E.; Motoki, K.; Nagata, K.; Yamazoe, Y. Thalidomide-induced suppression of embryo fibroblast proliferation requires CYP1A1-mediated activation. Drug Metab. Dispos., 2003, 31(4), 469-475.
    • (2003) Drug Metab. Dispos , vol.31 , Issue.4 , pp. 469-475
    • Miyata, M.1    Tamura, E.2    Motoki, K.3    Nagata, K.4    Yamazoe, Y.5
  • 42
    • 27544462180 scopus 로고    scopus 로고
    • Relative contributions of the five major human cytochromes P450, 1A2, 2C9, 2C19, 2D6, and 3A4, to the hepatic metabolism of the proteasome inhibitor bortezomib
    • Uttamsingh, V.; Lu, C.; Miwa, G.; Gan, L. S. Relative contributions of the five major human cytochromes P450, 1A2, 2C9, 2C19, 2D6, and 3A4, to the hepatic metabolism of the proteasome inhibitor bortezomib. Drug Metab. Dispos., 2005, 33(11), 1723-1728.
    • (2005) Drug Metab. Dispos , vol.33 , Issue.11 , pp. 1723-1728
    • Uttamsingh, V.1    Lu, C.2    Miwa, G.3    Gan, L.S.4
  • 43
    • 0033673590 scopus 로고    scopus 로고
    • Identification of the human liver cytochrome P450 isoenzyme responsible for the 6-methylhydroxylation of the novel anticancer drug 5,6-dimethylxanthenone-4-acetic acid
    • Zhou, S.; Paxton, J. W.; Tingle, M. D.; Kestell, P. Identification of the human liver cytochrome P450 isoenzyme responsible for the 6-methylhydroxylation of the novel anticancer drug 5,6-dimethylxanthenone-4-acetic acid. Drug Metab. Dispos., 2000, 28(12), 1449-1456.
    • (2000) Drug Metab. Dispos , vol.28 , Issue.12 , pp. 1449-1456
    • Zhou, S.1    Paxton, J.W.2    Tingle, M.D.3    Kestell, P.4
  • 44
    • 1842853817 scopus 로고    scopus 로고
    • Predicting pharmacokinetics and drug interactions in patients from in vitro and in vivo models: The experience with 5,6-dimethylxanthenone-4-acetic acid (DMXAA), an anti-cancer drug eliminated mainly by conjugation
    • Zhou, S.; Kestell, P.; Paxton, J. W. Predicting pharmacokinetics and drug interactions in patients from in vitro and in vivo models: the experience with 5,6-dimethylxanthenone-4-acetic acid (DMXAA), an anti-cancer drug eliminated mainly by conjugation. Drug Metab. Rev., 2002, 34(4), 751-790.
    • (2002) Drug Metab. Rev , vol.34 , Issue.4 , pp. 751-790
    • Zhou, S.1    Kestell, P.2    Paxton, J.W.3
  • 45
    • 0033786365 scopus 로고    scopus 로고
    • Cytochrome P4502C9 is the principal catalyst of racemic acenocoumarol hydroxylation reactions in human liver microsomes
    • Thijssen, H. H.; Flinois, J. P.; Beaune, P. H. Cytochrome P4502C9 is the principal catalyst of racemic acenocoumarol hydroxylation reactions in human liver microsomes. Drug Metab. Dispos., 2000, 28(11), 1284-1290.
    • (2000) Drug Metab. Dispos , vol.28 , Issue.11 , pp. 1284-1290
    • Thijssen, H.H.1    Flinois, J.P.2    Beaune, P.H.3
  • 46
    • 0027267722 scopus 로고
    • Human liver microsomal metabolism of the enantiomers of warfarin and acenocoumarol: P450 isozyme diversity determines the differences in their pharmacokinetics
    • Hermans, J. J.; Thijssen, H. H. Human liver microsomal metabolism of the enantiomers of warfarin and acenocoumarol: P450 isozyme diversity determines the differences in their pharmacokinetics. Br. J. Pharmacol., 1993, 110(1), 482-490.
    • (1993) Br. J. Pharmacol , vol.110 , Issue.1 , pp. 482-490
    • Hermans, J.J.1    Thijssen, H.H.2
  • 47
    • 0031015345 scopus 로고    scopus 로고
    • Human P450 metabolism of warfarin
    • Kaminsky, L. S.; Zhang, Z. Y. Human P450 metabolism of warfarin. Pharmacol. Ther., 1997, 73(1), 67-74.
    • (1997) Pharmacol. Ther , vol.73 , Issue.1 , pp. 67-74
    • Kaminsky, L.S.1    Zhang, Z.Y.2
  • 48
    • 0030992855 scopus 로고    scopus 로고
    • Hydroxylation and demethylation of the tricyclic antidepressant nortriptyline by cDNA-expressed human cytochrome P450 isozymes
    • Olesen, O. V.; Linnet, K. Hydroxylation and demethylation of the tricyclic antidepressant nortriptyline by cDNA-expressed human cytochrome P450 isozymes. Drug Metab. Dispos., 1997, 25(6), 740-744.
    • (1997) Drug Metab. Dispos , vol.25 , Issue.6 , pp. 740-744
    • Olesen, O.V.1    Linnet, K.2
  • 49
    • 0019788132 scopus 로고
    • Demethylation and hydroxylation of amitriptyline, nortriptyline, and 10-hydroxyamitriptyline in human liver microsomes
    • Mellstrom, B.; von Bahr, C. Demethylation and hydroxylation of amitriptyline, nortriptyline, and 10-hydroxyamitriptyline in human liver microsomes. Drug Metab. Dispos., 1981, 9(6), 565-568.
    • (1981) Drug Metab. Dispos , vol.9 , Issue.6 , pp. 565-568
    • Mellstrom, B.1    von Bahr, C.2
  • 50
    • 0034109883 scopus 로고    scopus 로고
    • Microsomal binding of amitriptyline: Effect on estimation of enzyme kinetic parameters in vitro
    • Venkatakrishnan, K.; von Moltke, L. L.; Obach, R. S.; Greenblatt, D. J. Microsomal binding of amitriptyline: effect on estimation of enzyme kinetic parameters in vitro. J. Pharmacol. Exp. Ther., 2000, 293(2), 343-350.
    • (2000) J. Pharmacol. Exp. Ther , vol.293 , Issue.2 , pp. 343-350
    • Venkatakrishnan, K.1    von Moltke, L.L.2    Obach, R.S.3    Greenblatt, D.J.4
  • 52
    • 0030976985 scopus 로고    scopus 로고
    • Reappraisal of human CYP isoforms involved in imipramine N-demethylation and 2-hydroxylation: A study using microsomes obtained from putative extensive and poor metabolizers of S-mephenytoin and eleven recombinant human CYPs
    • Koyama, E.; Chiba, K.; Tani, M.; Ishizaki, T. Reappraisal of human CYP isoforms involved in imipramine N-demethylation and 2-hydroxylation: a study using microsomes obtained from putative extensive and poor metabolizers of S-mephenytoin and eleven recombinant human CYPs. J. Pharmacol. Exp. Ther., 1997, 281(3), 1199-1210.
    • (1997) J. Pharmacol. Exp. Ther , vol.281 , Issue.3 , pp. 1199-1210
    • Koyama, E.1    Chiba, K.2    Tani, M.3    Ishizaki, T.4
  • 54
    • 0030425332 scopus 로고    scopus 로고
    • The biotransformation of clomipramine in vitro, identification of the cytochrome P450s responsible for the separate metabolic pathways
    • Nielsen, K. K.; Flinois, J. P.; Beaune, P.; Brosen, K. The biotransformation of clomipramine in vitro, identification of the cytochrome P450s responsible for the separate metabolic pathways. J. Pharmacol. Exp. Ther., 1996, 277(3), 1659-1664.
    • (1996) J. Pharmacol. Exp. Ther , vol.277 , Issue.3 , pp. 1659-1664
    • Nielsen, K.K.1    Flinois, J.P.2    Beaune, P.3    Brosen, K.4
  • 56
    • 0036010090 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes contributing to demethylation of maprotiline in man
    • Brachtendorf, L.; Jetter, A.; Beckurts, K. T.; Holscher, A. H.; Fuhr, U. Cytochrome P450 enzymes contributing to demethylation of maprotiline in man. Pharmacol. Toxicol., 2002, 90(3), 144-149.
    • (2002) Pharmacol. Toxicol , vol.90 , Issue.3 , pp. 144-149
    • Brachtendorf, L.1    Jetter, A.2    Beckurts, K.T.3    Holscher, A.H.4    Fuhr, U.5
  • 57
    • 0033810675 scopus 로고    scopus 로고
    • Metabolism of the antidepressant mirtazapine in vitro: Contribution of cytochromes P450 1A2, 2D6, and 3A4
    • Stormer, E.; von Moltke, L. L.; Shader, R. I.; Greenblatt, D. J. Metabolism of the antidepressant mirtazapine in vitro: contribution of cytochromes P450 1A2, 2D6, and 3A4. Drug Metab. Dispos., 2000, 28(10), 1168-1175.
    • (2000) Drug Metab. Dispos , vol.28 , Issue.10 , pp. 1168-1175
    • Stormer, E.1    von Moltke, L.L.2    Shader, R.I.3    Greenblatt, D.J.4
  • 58
    • 0030434501 scopus 로고    scopus 로고
    • Identification of human cytochrome P450 isoforms involved in the stereoselective metabolism of mianserin enantiomers
    • Koyama, E.; Chiba, K.; Tani, M.; Ishizaki, T. Identification of human cytochrome P450 isoforms involved in the stereoselective metabolism of mianserin enantiomers. J. Pharmacol. Exp. Ther., 1996, 278(1), 21-30.
    • (1996) J. Pharmacol. Exp. Ther , vol.278 , Issue.1 , pp. 21-30
    • Koyama, E.1    Chiba, K.2    Tani, M.3    Ishizaki, T.4
  • 59
    • 0032701770 scopus 로고    scopus 로고
    • Azelastine N-demethylation by cytochrome P-450 (CYP)3A4, CYP2D6, and CYP1A2 in human liver microsomes: Evaluation of approach to predict the contribution of multiple CYPs
    • Nakajima, M.; Nakamura, S.; Tokudome, S.; Shimada, N.; Yamazaki, H.; Yokoi, T. Azelastine N-demethylation by cytochrome P-450 (CYP)3A4, CYP2D6, and CYP1A2 in human liver microsomes: evaluation of approach to predict the contribution of multiple CYPs. Drug Metab. Dispos., 1999, 27(12), 1381-1391.
    • (1999) Drug Metab. Dispos , vol.27 , Issue.12 , pp. 1381-1391
    • Nakajima, M.1    Nakamura, S.2    Tokudome, S.3    Shimada, N.4    Yamazaki, H.5    Yokoi, T.6
  • 60
    • 0029827090 scopus 로고    scopus 로고
    • Oxidative metabolism of flunarizine and cinnarizine by microsomes from B-lymphoblastoid cell lines expressing human cytochrome P450 enzymes
    • Kariya, S.; Isozaki, S.; Uchino, K.; Suzuki, T.; Narimatsu, S. Oxidative metabolism of flunarizine and cinnarizine by microsomes from B-lymphoblastoid cell lines expressing human cytochrome P450 enzymes. Biol. Pharm. Bull., 1996, 19(11), 1511-1514.
    • (1996) Biol. Pharm. Bull , vol.19 , Issue.11 , pp. 1511-1514
    • Kariya, S.1    Isozaki, S.2    Uchino, K.3    Suzuki, T.4    Narimatsu, S.5
  • 62
    • 33845929539 scopus 로고    scopus 로고
    • Identification of human cytochrome p450 isozymes involved in diphenhydramine N-demethylation
    • Akutsu, T.; Kobayashi, K.; Sakurada, K.; Ikegaya, H.; Furihata, T.; Chiba, K. Identification of human cytochrome p450 isozymes involved in diphenhydramine N-demethylation. Drug Metab. Dispos., 2007, 35(1), 72-78.
    • (2007) Drug Metab. Dispos , vol.35 , Issue.1 , pp. 72-78
    • Akutsu, T.1    Kobayashi, K.2    Sakurada, K.3    Ikegaya, H.4    Furihata, T.5    Chiba, K.6
  • 64
    • 0032913679 scopus 로고    scopus 로고
    • Cytochrome P-450 isoforms involved in carboxylic acid ester cleavage of Hantzsch pyridine ester of pranidipine
    • Kudo, S.; Okumura, H.; Miyamoto, G.; Ishizaki, T. Cytochrome P-450 isoforms involved in carboxylic acid ester cleavage of Hantzsch pyridine ester of pranidipine. Drug Metab. Dispos., 1999, 27(2), 303-308.
    • (1999) Drug Metab. Dispos , vol.27 , Issue.2 , pp. 303-308
    • Kudo, S.1    Okumura, H.2    Miyamoto, G.3    Ishizaki, T.4
  • 65
    • 0030726786 scopus 로고    scopus 로고
    • Formation of guanoxabenz from guanabenz in human liver. A new metabolic marker for CYP1A2
    • Clement, B.; Demesmaeker, M. Formation of guanoxabenz from guanabenz in human liver. A new metabolic marker for CYP1A2. Drug Metab. Dispos., 1997, 25(11), 1266-1271.
    • (1997) Drug Metab. Dispos , vol.25 , Issue.11 , pp. 1266-1271
    • Clement, B.1    Demesmaeker, M.2
  • 66
    • 16444386701 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of almotriptan, a serotonin 5-HT1B/1D receptor agonist for the treatment of migraine
    • McEnroe, J. D.; Fleishaker, J. C. Clinical pharmacokinetics of almotriptan, a serotonin 5-HT1B/1D receptor agonist for the treatment of migraine. Clin. Pharmacokinet., 2005, 44(3), 237-246.
    • (2005) Clin. Pharmacokinet , vol.44 , Issue.3 , pp. 237-246
    • McEnroe, J.D.1    Fleishaker, J.C.2
  • 67
    • 0032878034 scopus 로고    scopus 로고
    • Determination of the human cytochrome P450 isoforms involved in the metabolism of zolmitriptan
    • Wild, M. J.; McKillop, D.; Butters, C. J. Determination of the human cytochrome P450 isoforms involved in the metabolism of zolmitriptan. Xenobiotica, 1999, 29(8), 847-857.
    • (1999) Xenobiotica , vol.29 , Issue.8 , pp. 847-857
    • Wild, M.J.1    McKillop, D.2    Butters, C.J.3
  • 69
    • 0035197059 scopus 로고    scopus 로고
    • In vitro characterization of the metabolism of haloperidol using recombinant cytochrome p450 enzymes and human liver microsomes
    • Fang, J.; McKay, G.; Song, J.; Remillrd, A.; Li, X.; Midha, K. In vitro characterization of the metabolism of haloperidol using recombinant cytochrome p450 enzymes and human liver microsomes. Drug Metab. Dispos., 2001, 29(12), 1638-1643.
    • (2001) Drug Metab. Dispos , vol.29 , Issue.12 , pp. 1638-1643
    • Fang, J.1    McKay, G.2    Song, J.3    Remillrd, A.4    Li, X.5    Midha, K.6
  • 70
    • 0038630452 scopus 로고    scopus 로고
    • Contribution of human cytochrome P450 isoforms to the metabolism of the simplest phenothiazine neuroleptic promazine
    • Wojcikowski, J.; Pichard-Garcia, L.; Maurel, P.; Daniel, W. A. Contribution of human cytochrome P450 isoforms to the metabolism of the simplest phenothiazine neuroleptic promazine. Br. J. Pharmacol., 2003, 138(8), 1465-1474.
    • (2003) Br. J. Pharmacol , vol.138 , Issue.8 , pp. 1465-1474
    • Wojcikowski, J.1    Pichard-Garcia, L.2    Maurel, P.3    Daniel, W.A.4
  • 71
    • 0030077735 scopus 로고    scopus 로고
    • Identification of the human cytochromes P450 responsible for the in vitro formation of the major oxidative metabolites of the antipsychotic agent olanzapine
    • Ring, B. J.; Catlow, J.; Lindsay, T. J.; Gillespie, T.; Roskos, L. K.; Cerimele, B. J.; Swanson, S. P.; Hamman, M. A.; Wrighton, S. A. Identification of the human cytochromes P450 responsible for the in vitro formation of the major oxidative metabolites of the antipsychotic agent olanzapine. J. Pharmacol. Exp. Ther., 1996, 276(2), 658-666.
    • (1996) J. Pharmacol. Exp. Ther , vol.276 , Issue.2 , pp. 658-666
    • Ring, B.J.1    Catlow, J.2    Lindsay, T.J.3    Gillespie, T.4    Roskos, L.K.5    Cerimele, B.J.6    Swanson, S.P.7    Hamman, M.A.8    Wrighton, S.A.9
  • 72
    • 0033066470 scopus 로고    scopus 로고
    • Identification of cytochrome P450 enzymes involved in the metabolism of zotepine, an antipsychotic drug, in human liver microsomes
    • Shiraga, T.; Kaneko, H.; Iwasaki, K.; Tozuka, Z.; Suzuki, A.; Hata, T. Identification of cytochrome P450 enzymes involved in the metabolism of zotepine, an antipsychotic drug, in human liver microsomes. Xenobiotica, 1999, 29(3), 217-229.
    • (1999) Xenobiotica , vol.29 , Issue.3 , pp. 217-229
    • Shiraga, T.1    Kaneko, H.2    Iwasaki, K.3    Tozuka, Z.4    Suzuki, A.5    Hata, T.6
  • 73
    • 33344460427 scopus 로고    scopus 로고
    • Characterization of human cytochrome P450 enzymes involved in the metabolism of the piperidine-type phenothiazine neuroleptic thioridazine
    • Wojcikowski, J.; Maurel, P.; Daniel, W. A. Characterization of human cytochrome P450 enzymes involved in the metabolism of the piperidine-type phenothiazine neuroleptic thioridazine. Drug Metab. Dispos., 2006, 34(3), 471-476.
    • (2006) Drug Metab. Dispos , vol.34 , Issue.3 , pp. 471-476
    • Wojcikowski, J.1    Maurel, P.2    Daniel, W.A.3
  • 74
    • 0028020099 scopus 로고
    • Cytochrome P450 isozymes involved in propranolol metabolism in human liver microsomes. The role of CYP2D6 as ring-hydroxylase and CYP1A2 as N-desisopropylase
    • Masubuchi, Y.; Hosokawa, S.; Horie, T.; Suzuki, T.; Ohmori, S.; Kitada, M.; Narimatsu, S. Cytochrome P450 isozymes involved in propranolol metabolism in human liver microsomes. The role of CYP2D6 as ring-hydroxylase and CYP1A2 as N-desisopropylase. Drug Metab. Dispos., 1994, 22(6), 909-915.
    • (1994) Drug Metab. Dispos , vol.22 , Issue.6 , pp. 909-915
    • Masubuchi, Y.1    Hosokawa, S.2    Horie, T.3    Suzuki, T.4    Ohmori, S.5    Kitada, M.6    Narimatsu, S.7
  • 75
    • 0030848298 scopus 로고    scopus 로고
    • In vitro identification of the human cytochrome P450 enzymes involved in the metabolism of R(+)- and S(-)-carvedilol
    • Oldham, H. G.; Clarke, S. E. In vitro identification of the human cytochrome P450 enzymes involved in the metabolism of R(+)- and S(-)-carvedilol. Drug Metab. Dispos., 1997, 25(8), 970-977.
    • (1997) Drug Metab. Dispos , vol.25 , Issue.8 , pp. 970-977
    • Oldham, H.G.1    Clarke, S.E.2
  • 78
    • 0028785979 scopus 로고
    • Identification of the human liver cytochrome P450 enzymes involved in the metabolism of zileuton (ABT-077) and its N-dehydroxylated metabolite, Abbott-66193
    • Machinist, J. M.; Mayer, M. D.; Shet, M. S.; Ferrero, J. L.; Rodrigues, A. D. Identification of the human liver cytochrome P450 enzymes involved in the metabolism of zileuton (ABT-077) and its N-dehydroxylated metabolite, Abbott-66193. Drug Metab. Dispos., 1995, 23(10), 1163-1174.
    • (1995) Drug Metab. Dispos , vol.23 , Issue.10 , pp. 1163-1174
    • Machinist, J.M.1    Mayer, M.D.2    Shet, M.S.3    Ferrero, J.L.4    Rodrigues, A.D.5
  • 79
    • 1642441389 scopus 로고    scopus 로고
    • Cytochrome P450 1A2 is a major determinant of lidocaine metabolism in vivo: Effects of liver function
    • Orlando, R.; Piccoli, P.; De Martin, S.; Padrini, R.; Floreani, M.; Palatini, P. Cytochrome P450 1A2 is a major determinant of lidocaine metabolism in vivo: effects of liver function. Clin. Pharmacol. Ther., 2004, 75(1), 80-88.
    • (2004) Clin. Pharmacol. Ther , vol.75 , Issue.1 , pp. 80-88
    • Orlando, R.1    Piccoli, P.2    De Martin, S.3    Padrini, R.4    Floreani, M.5    Palatini, P.6
  • 82
    • 0038002981 scopus 로고    scopus 로고
    • The cytochrome P450 2B6 (CYP2B6) is the main catalyst of efavirenz primary and secondary metabolism: Implication for HIV/AIDS therapy and utility of efavirenz as a substrate marker of CYP2B6 catalytic activity
    • Ward, B. A.; Gorski, J. C.; Jones, D. R.; Hall, S. D.; Flockhart, D. A.; Desta, Z. The cytochrome P450 2B6 (CYP2B6) is the main catalyst of efavirenz primary and secondary metabolism: implication for HIV/AIDS therapy and utility of efavirenz as a substrate marker of CYP2B6 catalytic activity. J. Pharmacol. Exp. Ther., 2003, 306(1), 287-300.
    • (2003) J. Pharmacol. Exp. Ther , vol.306 , Issue.1 , pp. 287-300
    • Ward, B.A.1    Gorski, J.C.2    Jones, D.R.3    Hall, S.D.4    Flockhart, D.A.5    Desta, Z.6
  • 83
    • 0029860967 scopus 로고    scopus 로고
    • Disposition of fluvoxamine in humans is determined by the polymorphic CYP2D6 and also by the CYP1A2 activity
    • Carrillo, J. A.; Dahl, M. L.; Svensson, J. O.; Alm, C.; Rodriguez, I.; Bertilsson, L. Disposition of fluvoxamine in humans is determined by the polymorphic CYP2D6 and also by the CYP1A2 activity. Clin. Pharmacol. Ther., 1996, 60(2), 183-190.
    • (1996) Clin. Pharmacol. Ther , vol.60 , Issue.2 , pp. 183-190
    • Carrillo, J.A.1    Dahl, M.L.2    Svensson, J.O.3    Alm, C.4    Rodriguez, I.5    Bertilsson, L.6
  • 85
    • 0028240611 scopus 로고
    • The effect of enzyme inhibition on the metabolism and activation of tacrine by human liver microsomes
    • Spaldin, V.; Madden, S.; Pool, W. F.; Woolf, T. F.; Park, B. K. The effect of enzyme inhibition on the metabolism and activation of tacrine by human liver microsomes. Br. J. Clin. Pharmacol., 1994, 38(1), 15-22.
    • (1994) Br. J. Clin. Pharmacol , vol.38 , Issue.1 , pp. 15-22
    • Spaldin, V.1    Madden, S.2    Pool, W.F.3    Woolf, T.F.4    Park, B.K.5
  • 86
    • 0029089652 scopus 로고
    • Determination of human hepatic cytochrome P4501A2 activity in vitro use of tacrine as an isoenzyme-specific probe
    • Spaldin, V.; Madden, S.; Adams, D. A.; Edwards, R. J.; Davies, D. S.; Park, B. K. Determination of human hepatic cytochrome P4501A2 activity in vitro use of tacrine as an isoenzyme-specific probe. Drug Metab. Dispos., 1995, 23(9), 929-934.
    • (1995) Drug Metab. Dispos , vol.23 , Issue.9 , pp. 929-934
    • Spaldin, V.1    Madden, S.2    Adams, D.A.3    Edwards, R.J.4    Davies, D.S.5    Park, B.K.6
  • 88
    • 0036841947 scopus 로고    scopus 로고
    • Pathways of carbamazepine bioactivation in vitro I. Characterization of human cytochromes P450 responsible for the formation of 2- and 3-hydroxylated metabolites
    • Pearce, R. E.; Vakkalagadda, G. R.; Leeder, J. S. Pathways of carbamazepine bioactivation in vitro I. Characterization of human cytochromes P450 responsible for the formation of 2- and 3-hydroxylated metabolites. Drug Metab. Dispos., 2002, 30(11), 1170-1179.
    • (2002) Drug Metab. Dispos , vol.30 , Issue.11 , pp. 1170-1179
    • Pearce, R.E.1    Vakkalagadda, G.R.2    Leeder, J.S.3
  • 92
    • 0032870308 scopus 로고    scopus 로고
    • Multiple cytochrome P-450s involved in the metabolism of terbinafine suggest a limited potential for drug-drug interactions
    • Vickers, A. E.; Sinclair, J. R.; Zollinger, M.; Heitz, F.; Glanzel, U.; Johanson, L.; Fischer, V. Multiple cytochrome P-450s involved in the metabolism of terbinafine suggest a limited potential for drug-drug interactions. Drug Metab. Dispos., 1999, 27(9), 1029-1038.
    • (1999) Drug Metab. Dispos , vol.27 , Issue.9 , pp. 1029-1038
    • Vickers, A.E.1    Sinclair, J.R.2    Zollinger, M.3    Heitz, F.4    Glanzel, U.5    Johanson, L.6    Fischer, V.7
  • 93
    • 33747584882 scopus 로고    scopus 로고
    • Urinary metabolite profiling reveals CYP1A2-mediated metabolism of NSC686288 (aminoflavone)
    • Chen, C.; Meng, L.; Ma, X.; Krausz, K. W.; Pommier, Y.; Idle, J. R.; Gonzalez, F. J. Urinary metabolite profiling reveals CYP1A2-mediated metabolism of NSC686288 (aminoflavone). J. Pharmacol. Exp. Ther., 2006, 318(3), 1330-1342.
    • (2006) J. Pharmacol. Exp. Ther , vol.318 , Issue.3 , pp. 1330-1342
    • Chen, C.1    Meng, L.2    Ma, X.3    Krausz, K.W.4    Pommier, Y.5    Idle, J.R.6    Gonzalez, F.J.7
  • 94
    • 0032567128 scopus 로고    scopus 로고
    • Cholinesterase inhibition for Alzheimer disease: A meta-analysis of the tacrine trials. Dementia Trialists' Collaboration
    • Qizilbash, N.; Whitehead, A.; Higgins, J.; Wilcock, G.; Schneider, L.; Farlow, M. Cholinesterase inhibition for Alzheimer disease: a meta-analysis of the tacrine trials. Dementia Trialists' Collaboration. Jama, 1998, 280(20), 1777-1782.
    • (1998) Jama , vol.280 , Issue.20 , pp. 1777-1782
    • Qizilbash, N.1    Whitehead, A.2    Higgins, J.3    Wilcock, G.4    Schneider, L.5    Farlow, M.6
  • 96
    • 0030936913 scopus 로고    scopus 로고
    • Wagstaff, A. J.; Bryson, H. M. Tizanidine. A review of its pharmacology, clinical efficacy and tolerability in the management of spasticity associated with cerebral and spinal disorders. Drugs, 1997, 53(3), 435-452.
    • Wagstaff, A. J.; Bryson, H. M. Tizanidine. A review of its pharmacology, clinical efficacy and tolerability in the management of spasticity associated with cerebral and spinal disorders. Drugs, 1997, 53(3), 435-452.
  • 97
    • 0029680102 scopus 로고    scopus 로고
    • Identification of human liver cytochrome P450 isoforms involved in the in vitro metabolism of cyclobenzaprine
    • Wang, R. W.; Liu, L.; Cheng, H. Identification of human liver cytochrome P450 isoforms involved in the in vitro metabolism of cyclobenzaprine. Drug Metab. Dispos., 1996, 24(7), 786-791.
    • (1996) Drug Metab. Dispos , vol.24 , Issue.7 , pp. 786-791
    • Wang, R.W.1    Liu, L.2    Cheng, H.3
  • 98
    • 0029916692 scopus 로고    scopus 로고
    • Cytochromes P450, 1A2, and 2C9 are responsible for the human hepatic O-demethylation of R- and S-naproxen
    • Miners, J. O.; Coulter, S.; Tukey, R. H.; Veronese, M. E.; Birkett, D. J. Cytochromes P450, 1A2, and 2C9 are responsible for the human hepatic O-demethylation of R- and S-naproxen. Biochem. Pharmacol., 1996, 51(8), 1003-1008.
    • (1996) Biochem. Pharmacol , vol.51 , Issue.8 , pp. 1003-1008
    • Miners, J.O.1    Coulter, S.2    Tukey, R.H.3    Veronese, M.E.4    Birkett, D.J.5
  • 99
    • 0141569613 scopus 로고    scopus 로고
    • In vitro metabolism studies on the isoxazole ring scission in the anti-inflammatory agent lefluonomide to its active alpha-cyanoenol metabolite A771726: Mechanistic similarities with the cytochrome P450-catalyzed dehydration of aldoximes
    • Kalgutkar, A. S.; Nguyen, H. T.; Vaz, A. D.; Doan, A.; Dalvie, D. K.; McLeod, D. G.; Murray, J. C. In vitro metabolism studies on the isoxazole ring scission in the anti-inflammatory agent lefluonomide to its active alpha-cyanoenol metabolite A771726: mechanistic similarities with the cytochrome P450-catalyzed dehydration of aldoximes. Drug Metab. Dispos., 2003, 31(10), 1240-1250.
    • (2003) Drug Metab. Dispos , vol.31 , Issue.10 , pp. 1240-1250
    • Kalgutkar, A.S.1    Nguyen, H.T.2    Vaz, A.D.3    Doan, A.4    Dalvie, D.K.5    McLeod, D.G.6    Murray, J.C.7
  • 101
    • 0031798917 scopus 로고    scopus 로고
    • Possible involvement of multiple human cytochrome P450 isoforms in the liver metabolism of propofol
    • Guitton, J.; Buronfosse, T.; Desage, M.; Flinois, J. P.; Perdrix, J. P.; Brazier, J. L.; Beaune, P. Possible involvement of multiple human cytochrome P450 isoforms in the liver metabolism of propofol. Br. J. Anaesth., 1998, 80(6), 788-795.
    • (1998) Br. J. Anaesth , vol.80 , Issue.6 , pp. 788-795
    • Guitton, J.1    Buronfosse, T.2    Desage, M.3    Flinois, J.P.4    Perdrix, J.P.5    Brazier, J.L.6    Beaune, P.7
  • 102
    • 34250208597 scopus 로고    scopus 로고
    • Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND)
    • CD001447
    • Miller, R. G.; Mitchell, J. D.; Lyon, M.; Moore, D. H. Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND). Cochrane Database Syst. Rev., 2007, 1, CD001447.
    • (2007) Cochrane Database Syst. Rev , vol.1
    • Miller, R.G.1    Mitchell, J.D.2    Lyon, M.3    Moore, D.H.4
  • 103
    • 34548777456 scopus 로고    scopus 로고
    • Clinical care of patients with amyotrophic lateral sclerosis
    • Radunovic, A.; Mitsumoto, H.; Leigh, P. N. Clinical care of patients with amyotrophic lateral sclerosis. Lancet Neurol., 2007, 6(10), 913-925.
    • (2007) Lancet Neurol , vol.6 , Issue.10 , pp. 913-925
    • Radunovic, A.1    Mitsumoto, H.2    Leigh, P.N.3
  • 104
    • 0030596899 scopus 로고    scopus 로고
    • Riluzole
    • Wokke, J. Riluzole. Lancet, 1996, 348(9030), 795-799.
    • (1996) Lancet , vol.348 , Issue.9030 , pp. 795-799
    • Wokke, J.1
  • 105
    • 0030255620 scopus 로고    scopus 로고
    • Riluzole. A review of its pharmacodynamic and pharmacokinetic properties and therapeutic potential in amyotrophic lateral sclerosis
    • Bryson, H. M.; Fulton, B.; Benfield, P. Riluzole. A review of its pharmacodynamic and pharmacokinetic properties and therapeutic potential in amyotrophic lateral sclerosis. Drugs, 1996, 52(4), 549-563.
    • (1996) Drugs , vol.52 , Issue.4 , pp. 549-563
    • Bryson, H.M.1    Fulton, B.2    Benfield, P.3
  • 106
    • 42349092390 scopus 로고    scopus 로고
    • An association study of riluzole serum concentration and survival and disease progression in patients with ALS
    • Groeneveld, G. J.; van Kan, H. J.; Lie, A. H. L.; Guchelaar, H. J.; van den Berg, L. H. An association study of riluzole serum concentration and survival and disease progression in patients with ALS. Clin. Pharmacol. Ther., 2008, 83(5), 718-722.
    • (2008) Clin. Pharmacol. Ther , vol.83 , Issue.5 , pp. 718-722
    • Groeneveld, G.J.1    van Kan, H.J.2    Lie, A.H.L.3    Guchelaar, H.J.4    van den Berg, L.H.5
  • 107
    • 0030924553 scopus 로고    scopus 로고
    • Involvement of human CYP1A isoenzymes in the metabolism and drug interactions of riluzole in vitro
    • Sanderink, G. J.; Bournique, B.; Stevens, J.; Petry, M.; Martinet, M. Involvement of human CYP1A isoenzymes in the metabolism and drug interactions of riluzole in vitro. J. Pharmacol. Exp. Ther., 1997, 282(3), 1465-1472.
    • (1997) J. Pharmacol. Exp. Ther , vol.282 , Issue.3 , pp. 1465-1472
    • Sanderink, G.J.1    Bournique, B.2    Stevens, J.3    Petry, M.4    Martinet, M.5
  • 108
    • 0036136927 scopus 로고    scopus 로고
    • CYP1A-mediated metabolism of the Janus kinase-3 inhibitor 4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazoline: Structural basis for inactivation by regioselective O-demethylation
    • Uckun, F. M.; Thoen, J.; Chen, H.; Sudbeck, E.; Mao, C.; Malaviya, R.; Liu, X. P.; Chen, C. L. CYP1A-mediated metabolism of the Janus kinase-3 inhibitor 4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazoline: structural basis for inactivation by regioselective O-demethylation. Drug Metab. Dispos., 2002, 30(1), 74-85.
    • (2002) Drug Metab. Dispos , vol.30 , Issue.1 , pp. 74-85
    • Uckun, F.M.1    Thoen, J.2    Chen, H.3    Sudbeck, E.4    Mao, C.5    Malaviya, R.6    Liu, X.P.7    Chen, C.L.8
  • 109
    • 0032565569 scopus 로고    scopus 로고
    • Activation of procarcinogens by human cytochrome P450 enzymes
    • Guengerich, F. P.; Shimada, T. Activation of procarcinogens by human cytochrome P450 enzymes. Mutat. Res., 1998, 400(1-2), 201-213.
    • (1998) Mutat. Res , vol.400 , Issue.1-2 , pp. 201-213
    • Guengerich, F.P.1    Shimada, T.2
  • 110
    • 0035978747 scopus 로고    scopus 로고
    • Metabolic activation of heterocyclic amines and other procarcinogens in Salmonella typhimurium umu tester strains expressing human cytochrome P4501A1, 1A2, 1B1, 2C9, 2D6, 2E1, and 3A4 and human NADPH-P450 reductase and bacterial O-acetyltransferase
    • Oda, Y.; Aryal, P.; Terashita, T.; Gillam, E. M.; Guengerich, F. P.; Shimada, T. Metabolic activation of heterocyclic amines and other procarcinogens in Salmonella typhimurium umu tester strains expressing human cytochrome P4501A1, 1A2, 1B1, 2C9, 2D6, 2E1, and 3A4 and human NADPH-P450 reductase and bacterial O-acetyltransferase. Mutat. Res., 2001, 492(1-2), 81-90.
    • (2001) Mutat. Res , vol.492 , Issue.1-2 , pp. 81-90
    • Oda, Y.1    Aryal, P.2    Terashita, T.3    Gillam, E.M.4    Guengerich, F.P.5    Shimada, T.6
  • 111
    • 0029010216 scopus 로고
    • cDNA-directed expression of human cytochrome P450 CYP1A1 using baculovirus. Purification, dependency on NADPH-P450 oxidoreductase, and reconstitution of catalytic properties without purification
    • Buters, J. T.; Shou, M.; Hardwick, J. P.; Korzekwa, K. R.; Gonzalez, F. J. cDNA-directed expression of human cytochrome P450 CYP1A1 using baculovirus. Purification, dependency on NADPH-P450 oxidoreductase, and reconstitution of catalytic properties without purification. Drug Metab. Dispos., 1995, 23(7), 696-701.
    • (1995) Drug Metab. Dispos , vol.23 , Issue.7 , pp. 696-701
    • Buters, J.T.1    Shou, M.2    Hardwick, J.P.3    Korzekwa, K.R.4    Gonzalez, F.J.5
  • 112
    • 0029758268 scopus 로고    scopus 로고
    • Stereoselective epoxidation and hydration at the K-region of polycyclic aromatic hydrocarbons by cDNA-expressed cytochromes P450 1A1, 1A2, and epoxide hydrolase
    • Shou, M.; Gonzalez, F. J.; Gelboin, H. V. Stereoselective epoxidation and hydration at the K-region of polycyclic aromatic hydrocarbons by cDNA-expressed cytochromes P450 1A1, 1A2, and epoxide hydrolase. Biochemistry, 1996, 35(49), 15807-15813.
    • (1996) Biochemistry , vol.35 , Issue.49 , pp. 15807-15813
    • Shou, M.1    Gonzalez, F.J.2    Gelboin, H.V.3
  • 113
    • 34250708477 scopus 로고    scopus 로고
    • CYP1A induction and human risk assessment: An evolving tale of in vitro and in vivo studies
    • Ma, Q.; Lu, A. Y. CYP1A induction and human risk assessment: an evolving tale of in vitro and in vivo studies. Drug Metab. Dispos., 2007, 35(7), 1009-1016.
    • (2007) Drug Metab. Dispos , vol.35 , Issue.7 , pp. 1009-1016
    • Ma, Q.1    Lu, A.Y.2
  • 114
    • 0032838774 scopus 로고    scopus 로고
    • Metabolism of benzo[a]pyrene to trans-7,8-dihydroxy-7, 8-dihydrobenzo[a]pyrene by recombinant human cytochrome P450 1B1 and purified liver epoxide hydrolase
    • Shimada, T.; Gillam, E. M.; Oda, Y.; Tsumura, F.; Sutter, T. R.; Guengerich, F. P.; Inoue, K. Metabolism of benzo[a]pyrene to trans-7,8-dihydroxy-7, 8-dihydrobenzo[a]pyrene by recombinant human cytochrome P450 1B1 and purified liver epoxide hydrolase. Chem. Res. Toxicol., 1999, 12(7), 623-629.
    • (1999) Chem. Res. Toxicol , vol.12 , Issue.7 , pp. 623-629
    • Shimada, T.1    Gillam, E.M.2    Oda, Y.3    Tsumura, F.4    Sutter, T.R.5    Guengerich, F.P.6    Inoue, K.7
  • 116
    • 0028986147 scopus 로고
    • Oxidation of aflatoxin B1 by bacterial recombinant human cytochrome P450 enzymes
    • Ueng, Y. F.; Shimada, T.; Yamazaki, H.; Guengerich, F. P. Oxidation of aflatoxin B1 by bacterial recombinant human cytochrome P450 enzymes. Chem. Res. Toxicol., 1995, 8(2), 218-225.
    • (1995) Chem. Res. Toxicol , vol.8 , Issue.2 , pp. 218-225
    • Ueng, Y.F.1    Shimada, T.2    Yamazaki, H.3    Guengerich, F.P.4
  • 117
    • 0028179768 scopus 로고
    • High promutagen activating capacity of yeast microsomes containing human cytochrome P-450 1A and human NADPH-cytochrome P-450 reductase
    • Sengstag, C.; Eugster, H. P.; Wurgler, F. E. High promutagen activating capacity of yeast microsomes containing human cytochrome P-450 1A and human NADPH-cytochrome P-450 reductase. Carcinogenesis, 1994, 15(5), 837-843.
    • (1994) Carcinogenesis , vol.15 , Issue.5 , pp. 837-843
    • Sengstag, C.1    Eugster, H.P.2    Wurgler, F.E.3
  • 118
    • 0028064672 scopus 로고
    • Development of a human lymphoblastoid cell line constitutively expressing human CYP1A1 cDNA: Substrate specificity with model substrates and promutagens
    • Penman, B. W.; Chen, L.; Gelboin, H. V.; Gonzalez, F. J.; Crespi, C. L. Development of a human lymphoblastoid cell line constitutively expressing human CYP1A1 cDNA: substrate specificity with model substrates and promutagens. Carcinogenesis, 1994, 15(9), 1931-1937.
    • (1994) Carcinogenesis , vol.15 , Issue.9 , pp. 1931-1937
    • Penman, B.W.1    Chen, L.2    Gelboin, H.V.3    Gonzalez, F.J.4    Crespi, C.L.5
  • 119
    • 0030904085 scopus 로고    scopus 로고
    • Development of a human lymphoblastoid cell line constitutively expressing human CYP1B1 cDNA: Substrate specificity with model substrates and promutagens
    • Crespi, C. L.; Penman, B. W.; Steimel, D. T.; Smith, T.; Yang, C. S.; Sutter, T. R. Development of a human lymphoblastoid cell line constitutively expressing human CYP1B1 cDNA: substrate specificity with model substrates and promutagens. Mutagenesis, 1997, 12(2), 83-89.
    • (1997) Mutagenesis , vol.12 , Issue.2 , pp. 83-89
    • Crespi, C.L.1    Penman, B.W.2    Steimel, D.T.3    Smith, T.4    Yang, C.S.5    Sutter, T.R.6
  • 120
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillam, E. M.; Baba, T.; Kim, B. R.; Ohmori, S.; Guengerich, F. P. Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys., 1993, 305(1), 123-131.
    • (1993) Arch. Biochem. Biophys , vol.305 , Issue.1 , pp. 123-131
    • Gillam, E.M.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5
  • 121
    • 34548088206 scopus 로고    scopus 로고
    • Characterization of diuron N-demethylation by mammalian hepatic microsomes and cDNA-expressed human cytochrome P450 enzymes
    • Abass, K.; Reponen, P.; Turpeinen, M.; Jalonen, J.; Pelkonen, O. Characterization of diuron N-demethylation by mammalian hepatic microsomes and cDNA-expressed human cytochrome P450 enzymes. Drug Metab. Dispos., 2007, 35(9), 1634-1641.
    • (2007) Drug Metab. Dispos , vol.35 , Issue.9 , pp. 1634-1641
    • Abass, K.1    Reponen, P.2    Turpeinen, M.3    Jalonen, J.4    Pelkonen, O.5
  • 122
    • 0031657035 scopus 로고    scopus 로고
    • Human cytochrome P450-catalyzed conversion of the proestrogenic pesticide methoxychlor into an estrogen. Role of CYP2C19 and CYP1A2 in O-demethylation
    • Stresser, D. M.; Kupfer, D. Human cytochrome P450-catalyzed conversion of the proestrogenic pesticide methoxychlor into an estrogen. Role of CYP2C19 and CYP1A2 in O-demethylation. Drug Metab. Dispos., 1998, 26(9), 868-874.
    • (1998) Drug Metab. Dispos , vol.26 , Issue.9 , pp. 868-874
    • Stresser, D.M.1    Kupfer, D.2
  • 123
    • 0018078757 scopus 로고
    • Studies on the in vivo and in vitro estrogenic activities of methoxychlor and its metabolites. Role of hepatic mono-oxygenase in methoxychlor activation
    • Bulger, W. H.; Muccitelli, R. M.; Kupfer, D. Studies on the in vivo and in vitro estrogenic activities of methoxychlor and its metabolites. Role of hepatic mono-oxygenase in methoxychlor activation. Biochem. Pharmacol., 1978, 27(20), 2417-2423.
    • (1978) Biochem. Pharmacol , vol.27 , Issue.20 , pp. 2417-2423
    • Bulger, W.H.1    Muccitelli, R.M.2    Kupfer, D.3
  • 124
    • 0017029682 scopus 로고
    • Hepatocarcinogenicity of estragole (1-allyl-4-methoxybenzene) and 1′-hydroxyestragole in the mouse and mutagenicity of 1′- acetoxyestragole in bacteria
    • Drinkwater, N. R.; Miller, E. C.; Miller, J. A.; Pitot, H. C. Hepatocarcinogenicity of estragole (1-allyl-4-methoxybenzene) and 1′-hydroxyestragole in the mouse and mutagenicity of 1′- acetoxyestragole in bacteria. J. Natl. Cancer Inst., 1976, 57(6), 1323-1331.
    • (1976) J. Natl. Cancer Inst , vol.57 , Issue.6 , pp. 1323-1331
    • Drinkwater, N.R.1    Miller, E.C.2    Miller, J.A.3    Pitot, H.C.4
  • 125
    • 0023543566 scopus 로고
    • Metabolism of estragole in rat and mouse and influence of dose size on excretion of the proximate carcinogen 1'-hydroxyestragole
    • Anthony, A.; Caldwell, J.; Hutt, A. J.; Smith, R. L. Metabolism of estragole in rat and mouse and influence of dose size on excretion of the proximate carcinogen 1'-hydroxyestragole. Food Chem. Toxicol., 1987, 25(11), 799-806.
    • (1987) Food Chem. Toxicol , vol.25 , Issue.11 , pp. 799-806
    • Anthony, A.1    Caldwell, J.2    Hutt, A.J.3    Smith, R.L.4
  • 127
    • 0015593170 scopus 로고
    • The metabolism of the naturally occurring hepatocarcinogen safrole to 1′-hydroxysafrole and the electrophilic reactivity of 1'-acetoxysafrole
    • Borchert, P.; Wislocki, P. G.; Miller, J. A.; Miller, E. C. The metabolism of the naturally occurring hepatocarcinogen safrole to 1′-hydroxysafrole and the electrophilic reactivity of 1'-acetoxysafrole. Cancer Res., 1973, 33(3), 575-589.
    • (1973) Cancer Res , vol.33 , Issue.3 , pp. 575-589
    • Borchert, P.1    Wislocki, P.G.2    Miller, J.A.3    Miller, E.C.4
  • 129
    • 4243125326 scopus 로고    scopus 로고
    • Identification of the main human cytochrome P450 enzymes involved in safrole 1′-hydroxylation
    • Ueng, Y. F.; Hsieh, C. H.; Don, M. J.; Chi, C. W.; Ho, L. K. Identification of the main human cytochrome P450 enzymes involved in safrole 1′-hydroxylation. Chem. Res. Toxicol., 2004, 17(8), 1151-1156.
    • (2004) Chem. Res. Toxicol , vol.17 , Issue.8 , pp. 1151-1156
    • Ueng, Y.F.1    Hsieh, C.H.2    Don, M.J.3    Chi, C.W.4    Ho, L.K.5
  • 131
    • 0031410088 scopus 로고    scopus 로고
    • Cytochrome P450 mediated bioactivation of methyleugenol to 1'-hydroxymethyleugenol in Fischer 344 rat and human liver microsomes
    • Gardner, I.; Wakazono, H.; Bergin, P.; de Waziers, I.; Beaune, P.; Kenna, J. G.; Caldwell, J. Cytochrome P450 mediated bioactivation of methyleugenol to 1'-hydroxymethyleugenol in Fischer 344 rat and human liver microsomes. Carcinogenesis, 1997, 18(9), 1775-1783.
    • (1997) Carcinogenesis , vol.18 , Issue.9 , pp. 1775-1783
    • Gardner, I.1    Wakazono, H.2    Bergin, P.3    de Waziers, I.4    Beaune, P.5    Kenna, J.G.6    Caldwell, J.7
  • 132
    • 13844319935 scopus 로고    scopus 로고
    • Drug bioactivation and covalent binding to target proteins and toxicity relevance
    • Zhou, S. F. Drug bioactivation and covalent binding to target proteins and toxicity relevance. Drug Metab. Rev., 2005, 37(1): 41-213.
    • (2005) Drug Metab. Rev , vol.37 , Issue.1 , pp. 41-213
    • Zhou, S.F.1
  • 133
    • 34547677792 scopus 로고    scopus 로고
    • Metabolic activation of herbal and dietary constituents and its clinical and toxicological implications: An update
    • Zhou, S. F.; Xue, C. C.; Yu, X. Q.; Wang, G. Metabolic activation of herbal and dietary constituents and its clinical and toxicological implications: an update. Curr. Drug Metab., 2007, 8(6), 526-553.
    • (2007) Curr. Drug Metab , vol.8 , Issue.6 , pp. 526-553
    • Zhou, S.F.1    Xue, C.C.2    Yu, X.Q.3    Wang, G.4
  • 134
    • 0034861029 scopus 로고    scopus 로고
    • Human enzymes involved in the metabolic activation of carcinogenic aris tolochic acids: Evidence for reductive activation by cytochromes P450 1A1 and 1A2
    • Stiborova, M.; Frei, E.; Wiessler, M.; Schmeiser, H. H. Human enzymes involved in the metabolic activation of carcinogenic aris tolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2. Chem. Res. Toxicol., 2001, 14(8), 1128-1137.
    • (2001) Chem. Res. Toxicol , vol.14 , Issue.8 , pp. 1128-1137
    • Stiborova, M.1    Frei, E.2    Wiessler, M.3    Schmeiser, H.H.4
  • 135
    • 0036257348 scopus 로고    scopus 로고
    • Carcinogenic aristolochic acids upon activation by DT-diaphorase form adducts found in DNA of patients with Chinese herbs nephropathy
    • Stiborova, M.; Frei, E.; Sopko, B.; Wiessler, M.; Schmeiser, H. H. Carcinogenic aristolochic acids upon activation by DT-diaphorase form adducts found in DNA of patients with Chinese herbs nephropathy. Carcinogenesis, 2002, 23(4), 617-625.
    • (2002) Carcinogenesis , vol.23 , Issue.4 , pp. 617-625
    • Stiborova, M.1    Frei, E.2    Sopko, B.3    Wiessler, M.4    Schmeiser, H.H.5
  • 136
    • 0034861029 scopus 로고    scopus 로고
    • Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: Evidence for reductive activation by cytochromes P450 1A1 and 1A2
    • Stiborova, M.; Frei, E.; Wiessler, M.; Schmeiser, H. H. Human enzymes involved in the metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2. Chem. Res. Toxicol., 2001, 14(8), 1128-1137.
    • (2001) Chem. Res. Toxicol , vol.14 , Issue.8 , pp. 1128-1137
    • Stiborova, M.1    Frei, E.2    Wiessler, M.3    Schmeiser, H.H.4
  • 139
    • 0036236050 scopus 로고    scopus 로고
    • Identification of the cytochromes P450 that catalyze coumarin 3,4-epoxidation and 3-hydroxylation
    • Born, S. L.; Caudill, D.; Fliter, K. L.; Purdon, M. P. Identification of the cytochromes P450 that catalyze coumarin 3,4-epoxidation and 3-hydroxylation. Drug Metab. Dispos., 2002, 30(5), 483-487.
    • (2002) Drug Metab. Dispos , vol.30 , Issue.5 , pp. 483-487
    • Born, S.L.1    Caudill, D.2    Fliter, K.L.3    Purdon, M.P.4
  • 140
    • 0025841777 scopus 로고
    • Purification and characterization of human liver microsomal cytochrome P450 2A6
    • Yun, C. H.; Shimada, T.; Guengerich, F. P. Purification and characterization of human liver microsomal cytochrome P450 2A6. Mol. Pharmacol., 1991, 40(5), 679-685.
    • (1991) Mol. Pharmacol , vol.40 , Issue.5 , pp. 679-685
    • Yun, C.H.1    Shimada, T.2    Guengerich, F.P.3
  • 141
    • 0031424015 scopus 로고    scopus 로고
    • Comparison of CYP2A6 catalytic activity on coumarin 7-hydroxylation in human and monkey liver microsomes
    • Li, Y.; Li, N. Y.; Sellers, E. M. Comparison of CYP2A6 catalytic activity on coumarin 7-hydroxylation in human and monkey liver microsomes. Eur. J. Drug Metab. Pharmacokinet., 1997, 22(4), 295-304.
    • (1997) Eur. J. Drug Metab. Pharmacokinet , vol.22 , Issue.4 , pp. 295-304
    • Li, Y.1    Li, N.Y.2    Sellers, E.M.3
  • 142
    • 0344069675 scopus 로고    scopus 로고
    • Expression of cytochrome P450 2A6 in Escherichia coli: Purification, spectral and catalytic characterization, and preparation of polyclonal antibodies
    • Soucek, P. Expression of cytochrome P450 2A6 in Escherichia coli: purification, spectral and catalytic characterization, and preparation of polyclonal antibodies. Arch. Biochem. Biophys., 1999, 370(2), 190-200.
    • (1999) Arch. Biochem. Biophys , vol.370 , Issue.2 , pp. 190-200
    • Soucek, P.1
  • 143
    • 0025214234 scopus 로고
    • Identification of the human liver cytochrome P450 responsible for coumarin 7-hydroxylase activity
    • Miles, J. S.; McLaren, A. W.; Forrester, L. M.; Glancey, M. J.; Lang, M. A.; Wolf, C. R. Identification of the human liver cytochrome P450 responsible for coumarin 7-hydroxylase activity. Biochem. J., 1990, 267(2), 365-371.
    • (1990) Biochem. J , vol.267 , Issue.2 , pp. 365-371
    • Miles, J.S.1    McLaren, A.W.2    Forrester, L.M.3    Glancey, M.J.4    Lang, M.A.5    Wolf, C.R.6
  • 144
    • 0024407169 scopus 로고
    • The effects of 5,6 benzo-[a]-pyrone (coumarin) and DEC on filaritic lymphoedema and elephantiasis in India. Preliminary results
    • Jamal, S.; Casley-Smith, J. R.; Casley-Smith, J. R. The effects of 5,6 benzo-[a]-pyrone (coumarin) and DEC on filaritic lymphoedema and elephantiasis in India. Preliminary results. Ann. Trop. Med. Parasitol., 1989, 83(3), 287-290.
    • (1989) Ann. Trop. Med. Parasitol , vol.83 , Issue.3 , pp. 287-290
    • Jamal, S.1    Casley-Smith, J.R.2    Casley-Smith, J.R.3
  • 147
    • 0037636423 scopus 로고    scopus 로고
    • Identification of CYP1A2 as the main isoform for the phase I hydroxylated metabolism of genistein and a prodrug converting enzyme of methylated isoflavones
    • Hu, M.; Krausz, K.; Chen, J.; Ge, X.; Li, J.; Gelboin, H. L.; Gonzalez, F. J. Identification of CYP1A2 as the main isoform for the phase I hydroxylated metabolism of genistein and a prodrug converting enzyme of methylated isoflavones. Drug Metab. Dispos., 2003, 31(7), 924-931.
    • (2003) Drug Metab. Dispos , vol.31 , Issue.7 , pp. 924-931
    • Hu, M.1    Krausz, K.2    Chen, J.3    Ge, X.4    Li, J.5    Gelboin, H.L.6    Gonzalez, F.J.7
  • 149
    • 0038683676 scopus 로고    scopus 로고
    • In vitro metabolism of genistein and tangeretin by human and murine cytochrome P450s
    • Breinholt, V. M.; Rasmussen, S. E.; Brosen, K.; Friedberg, T. H. In vitro metabolism of genistein and tangeretin by human and murine cytochrome P450s. Pharmacol. Toxicol., 2003, 93(1), 14-22.
    • (2003) Pharmacol. Toxicol , vol.93 , Issue.1 , pp. 14-22
    • Breinholt, V.M.1    Rasmussen, S.E.2    Brosen, K.3    Friedberg, T.H.4
  • 150
    • 0036146585 scopus 로고    scopus 로고
    • Oxidation of the flavonoids galangin and kaempferide by human liver microsomes and CYP1A1, CYP1A2, and CYP2C9
    • Otake, Y.; Walle, T. Oxidation of the flavonoids galangin and kaempferide by human liver microsomes and CYP1A1, CYP1A2, and CYP2C9. Drug Metab. Dispos., 2002, 30(2), 103-105.
    • (2002) Drug Metab. Dispos , vol.30 , Issue.2 , pp. 103-105
    • Otake, Y.1    Walle, T.2
  • 151
    • 0032931833 scopus 로고    scopus 로고
    • Roles of CYP2A6 and CYP2B6 in nicotine C-oxidation by human liver microsomes
    • Yamazaki, H.; Inoue, K.; Hashimoto, M.; Shimada, T. Roles of CYP2A6 and CYP2B6 in nicotine C-oxidation by human liver microsomes. Arch. Toxicol., 1999, 73(2), 65-70.
    • (1999) Arch. Toxicol , vol.73 , Issue.2 , pp. 65-70
    • Yamazaki, H.1    Inoue, K.2    Hashimoto, M.3    Shimada, T.4
  • 152
    • 22944440387 scopus 로고    scopus 로고
    • Nicotine 5′-oxidation and methyl oxidation by P450 2A enzymes
    • Murphy, S. E.; Raulinaitis, V.; Brown, K. M. Nicotine 5′-oxidation and methyl oxidation by P450 2A enzymes. Drug Metab. Dispos., 2005, 33(8), 1166-1173.
    • (2005) Drug Metab. Dispos , vol.33 , Issue.8 , pp. 1166-1173
    • Murphy, S.E.1    Raulinaitis, V.2    Brown, K.M.3
  • 153
    • 0033749374 scopus 로고    scopus 로고
    • 2′-Hydroxylation of nicotine by cytochrome P450 2A6 and human liver microsomes: Formation of a lung carcinogen precursor
    • Hecht, S. S.; Hochalter, J. B.; Villalta, P. W.; Murphy, S. E. 2′-Hydroxylation of nicotine by cytochrome P450 2A6 and human liver microsomes: formation of a lung carcinogen precursor. Proc. Natl. Acad. Sci. USA, 2000, 97(23), 12493-12497.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.23 , pp. 12493-12497
    • Hecht, S.S.1    Hochalter, J.B.2    Villalta, P.W.3    Murphy, S.E.4
  • 154
    • 0030885491 scopus 로고    scopus 로고
    • A major role for CYP2A6 in nicotine C-oxidation by human liver microsomes
    • Messina, E. S.; Tyndale, R. F.; Sellers, E. M. A major role for CYP2A6 in nicotine C-oxidation by human liver microsomes. J. Pharmacol. Exp. Ther., 1997, 282(3), 1608-1614.
    • (1997) J. Pharmacol. Exp. Ther , vol.282 , Issue.3 , pp. 1608-1614
    • Messina, E.S.1    Tyndale, R.F.2    Sellers, E.M.3
  • 155
    • 0029113117 scopus 로고
    • In vitro-in vivo correlations of human S-nicotine metabolism
    • Berkman, C. E.; Park, S. B.; Wrighton, S. A.; Cashman, J. R. In vitro-in vivo correlations of human S-nicotine metabolism. Biochem. Pharmacol., 1995, 50(4), 565-570.
    • (1995) Biochem. Pharmacol , vol.50 , Issue.4 , pp. 565-570
    • Berkman, C.E.1    Park, S.B.2    Wrighton, S.A.3    Cashman, J.R.4
  • 157
    • 0034764793 scopus 로고    scopus 로고
    • Contribution of CYP1A2 in the hepatic metabolism of melatonin: Studies with isolated microsomal preparations and liver slices
    • Skene, D. J.; Papagiannidou, E.; Hashemi, E.; Snelling, J.; Lewis, D. F.; Fernandez, M.; Ioannides, C. Contribution of CYP1A2 in the hepatic metabolism of melatonin: studies with isolated microsomal preparations and liver slices. J. Pineal Res., 2001, 31(4), 333-342.
    • (2001) J. Pineal Res , vol.31 , Issue.4 , pp. 333-342
    • Skene, D.J.1    Papagiannidou, E.2    Hashemi, E.3    Snelling, J.4    Lewis, D.F.5    Fernandez, M.6    Ioannides, C.7
  • 159
    • 0026750059 scopus 로고
    • Uroporphyrinogen oxidation catalyzed by reconstituted cytochrome P450IA2
    • Lambrecht, R. W.; Sinclair, P. R.; Gorman, N.; Sinclair, J. F. Uroporphyrinogen oxidation catalyzed by reconstituted cytochrome P450IA2. Arch. Biochem. Biophys., 1992, 294(2), 504-510.
    • (1992) Arch. Biochem. Biophys , vol.294 , Issue.2 , pp. 504-510
    • Lambrecht, R.W.1    Sinclair, P.R.2    Gorman, N.3    Sinclair, J.F.4
  • 160
    • 0031830896 scopus 로고    scopus 로고
    • Roles of cytochromes P450 1A2 and 3A4 in the oxidation of estradiol and estrone in human liver microsomes
    • Yamazaki, H.; Shaw, P. M.; Guengerich, F. P.; Shimada, T. Roles of cytochromes P450 1A2 and 3A4 in the oxidation of estradiol and estrone in human liver microsomes. Chem. Res. Toxicol., 1998, 11(6), 659-665.
    • (1998) Chem. Res. Toxicol , vol.11 , Issue.6 , pp. 659-665
    • Yamazaki, H.1    Shaw, P.M.2    Guengerich, F.P.3    Shimada, T.4
  • 161
    • 0042315387 scopus 로고    scopus 로고
    • Characterization of the oxidative metabolites of 17β-estradiol and estrone formed by 15 selectively expressed human cytochrome P450 isoforms
    • Lee, A. J.; Cai, M. X.; Thomas, P. E.; Conney, A. H.; Zhu, B. T. Characterization of the oxidative metabolites of 17β-estradiol and estrone formed by 15 selectively expressed human cytochrome P450 isoforms. Endocrinology, 2003, 144(8), 3382-3398.
    • (2003) Endocrinology , vol.144 , Issue.8 , pp. 3382-3398
    • Lee, A.J.1    Cai, M.X.2    Thomas, P.E.3    Conney, A.H.4    Zhu, B.T.5
  • 162
    • 0034911153 scopus 로고    scopus 로고
    • Characterization of the NADPH-dependent metabolism of 17β-estradiol to multiple metabolites by human liver microsomes and selectively expressed human cytochrome P450 3A4 and 3A5
    • Lee, A. J.; Kosh, J. W.; Conney, A. H.; Zhu, B. T. Characterization of the NADPH-dependent metabolism of 17β-estradiol to multiple metabolites by human liver microsomes and selectively expressed human cytochrome P450 3A4 and 3A5. J. Pharmacol. Exp. Ther., 2001, 298(2), 420-432.
    • (2001) J. Pharmacol. Exp. Ther , vol.298 , Issue.2 , pp. 420-432
    • Lee, A.J.1    Kosh, J.W.2    Conney, A.H.3    Zhu, B.T.4
  • 163
    • 15344344226 scopus 로고    scopus 로고
    • Metabolism of melatonin by human cytochromes P450
    • Ma, X.; Idle, J. R.; Krausz, K. W.; Gonzalez, F. J. Metabolism of melatonin by human cytochromes P450. Drug Metab. Dispos., 2005, 33(4), 489-494.
    • (2005) Drug Metab. Dispos , vol.33 , Issue.4 , pp. 489-494
    • Ma, X.1    Idle, J.R.2    Krausz, K.W.3    Gonzalez, F.J.4
  • 164
  • 166
    • 0034057188 scopus 로고    scopus 로고
    • Biosynthesis of all-transretinoic acid from all-trans-retinol: Catalysis of all-trans-retinol oxidation by human P450 cytochromes
    • Chen, H.; Howald, W. N.; Juchau, M. R. Biosynthesis of all-transretinoic acid from all-trans-retinol: catalysis of all-trans-retinol oxidation by human P450 cytochromes. Drug Metab. Dispos., 2000, 28(3), 315-322.
    • (2000) Drug Metab. Dispos , vol.28 , Issue.3 , pp. 315-322
    • Chen, H.1    Howald, W.N.2    Juchau, M.R.3
  • 167
    • 0034090984 scopus 로고    scopus 로고
    • Human cytochrome P450 metabolism of retinals to retinoic acids
    • Zhang, Q. Y.; Dunbar, D.; Kaminsky, L. Human cytochrome P450 metabolism of retinals to retinoic acids. Drug Metab. Dispos., 2000, 28(3), 292-297.
    • (2000) Drug Metab. Dispos , vol.28 , Issue.3 , pp. 292-297
    • Zhang, Q.Y.1    Dunbar, D.2    Kaminsky, L.3
  • 168
    • 3242682298 scopus 로고    scopus 로고
    • Metabolism of retinoids and arachidonic acid by human and mouse cytochrome P450 1b1
    • Choudhary, D.; Jansson, I.; Stoilov, I.; Sarfarazi, M.; Schenkman, J. B. Metabolism of retinoids and arachidonic acid by human and mouse cytochrome P450 1b1. Drug Metab. Dispos., 2004, 32(8), 840-847.
    • (2004) Drug Metab. Dispos , vol.32 , Issue.8 , pp. 840-847
    • Choudhary, D.1    Jansson, I.2    Stoilov, I.3    Sarfarazi, M.4    Schenkman, J.B.5
  • 169
    • 0029039791 scopus 로고
    • Arachidonic acid metabolism by human cytochrome P450s 2C8, 2C9, 2E1, and 1A2: Regioselective oxygenation and evidence for a role for CYP2C enzymes in arachidonic acid epoxygenation in human liver microsomes
    • Rifkind, A. B.; Lee, C.; Chang, T. K.; Waxman, D. J. Arachidonic acid metabolism by human cytochrome P450s 2C8, 2C9, 2E1, and 1A2: regioselective oxygenation and evidence for a role for CYP2C enzymes in arachidonic acid epoxygenation in human liver microsomes. Arch. Biochem. Biophys., 1995, 320(2), 380-389.
    • (1995) Arch. Biochem. Biophys , vol.320 , Issue.2 , pp. 380-389
    • Rifkind, A.B.1    Lee, C.2    Chang, T.K.3    Waxman, D.J.4
  • 170
    • 0031951506 scopus 로고    scopus 로고
    • Cytochromes P450 with bisallylic hydroxylation activity on arachidonic and linoleic acids studied with human recombinant enzymes and with human and rat liver microsomes
    • Bylund, J.; Kunz, T.; Valmsen, K.; Oliw, E. H. Cytochromes P450 with bisallylic hydroxylation activity on arachidonic and linoleic acids studied with human recombinant enzymes and with human and rat liver microsomes. J. Pharmacol. Exp. Ther., 1998, 284(1), 51-60.
    • (1998) J. Pharmacol. Exp. Ther , vol.284 , Issue.1 , pp. 51-60
    • Bylund, J.1    Kunz, T.2    Valmsen, K.3    Oliw, E.H.4
  • 171
    • 0034756188 scopus 로고    scopus 로고
    • Differential selectivity in carbamazepine-induced inactivation of cytochrome P450 enzymes in rat and human liver
    • Masubuchi, Y.; Nakano, T.; Ose, A.; Horie, T. Differential selectivity in carbamazepine-induced inactivation of cytochrome P450 enzymes in rat and human liver. Arch. Toxicol., 2001, 75(9), 538-543.
    • (2001) Arch. Toxicol , vol.75 , Issue.9 , pp. 538-543
    • Masubuchi, Y.1    Nakano, T.2    Ose, A.3    Horie, T.4
  • 172
    • 0031944859 scopus 로고    scopus 로고
    • Dihydralazine-induced inactivation of cytochrome P450 enzymes in rat liver microsomes
    • Masubuchi, Y.; Horie, T. Dihydralazine-induced inactivation of cytochrome P450 enzymes in rat liver microsomes. Drug Metab. Dispos., 1998, 26(4), 338-342.
    • (1998) Drug Metab. Dispos , vol.26 , Issue.4 , pp. 338-342
    • Masubuchi, Y.1    Horie, T.2
  • 173
    • 0027380074 scopus 로고
    • Isoform-selective mechanism-based inhibition of human cytochrome P450 1A2 by furafylline
    • Kunze, K. L.; Trager, W. F. Isoform-selective mechanism-based inhibition of human cytochrome P450 1A2 by furafylline. Chem. Res. Toxicol., 1993, 6(5), 649-656.
    • (1993) Chem. Res. Toxicol , vol.6 , Issue.5 , pp. 649-656
    • Kunze, K.L.1    Trager, W.F.2
  • 174
    • 0035712266 scopus 로고    scopus 로고
    • Isoniazid is a mechanism-based inhibitor of cytochrome P450 1A2, 2A6, 2C19 and 3A4 isoforms in human liver microsomes
    • Wen, X.; Wang, J. S.; Neuvonen, P. J.; Backman, J. T. Isoniazid is a mechanism-based inhibitor of cytochrome P450 1A2, 2A6, 2C19 and 3A4 isoforms in human liver microsomes. Eur. J. Clin. Pharmacol., 2002, 57(11), 799-804.
    • (2002) Eur. J. Clin. Pharmacol , vol.57 , Issue.11 , pp. 799-804
    • Wen, X.1    Wang, J.S.2    Neuvonen, P.J.3    Backman, J.T.4
  • 175
    • 33751558274 scopus 로고    scopus 로고
    • Rofecoxib is a potent, metabolism-dependent inhibitor of CYP1A2: Implications for in vitro prediction of drug interactions
    • Karjalainen, M. J.; Neuvonen, P. J.; Backman, J. T. Rofecoxib is a potent, metabolism-dependent inhibitor of CYP1A2: implications for in vitro prediction of drug interactions. Drug Metab. Dispos., 2006, 34(12), 2091-2096.
    • (2006) Drug Metab. Dispos , vol.34 , Issue.12 , pp. 2091-2096
    • Karjalainen, M.J.1    Neuvonen, P.J.2    Backman, J.T.3
  • 176
    • 0142243111 scopus 로고    scopus 로고
    • Mechanism-based inhibition of human liver microsomal cytochrome P450 1A2 by zileuton, a 5-lipoxygenase inhibitor
    • Lu, P.; Schrag, M. L.; Slaughter, D. E.; Raab, C. E.; Shou, M.; Rodrigues, A. D. Mechanism-based inhibition of human liver microsomal cytochrome P450 1A2 by zileuton, a 5-lipoxygenase inhibitor. Drug Metab. Dispos., 2003, 31(11), 1352-1360.
    • (2003) Drug Metab. Dispos , vol.31 , Issue.11 , pp. 1352-1360
    • Lu, P.1    Schrag, M.L.2    Slaughter, D.E.3    Raab, C.E.4    Shou, M.5    Rodrigues, A.D.6
  • 177
    • 0034015751 scopus 로고    scopus 로고
    • Inhibitory effects of amiodarone and its Ndeethylated metabolite on human cytochrome P450 activities: Prediction of in vivo drug interactions
    • Ohyama, K.; Nakajima, M.; Suzuki, M.; Shimada, N.; Yamazaki, H.; Yokoi, T. Inhibitory effects of amiodarone and its Ndeethylated metabolite on human cytochrome P450 activities: prediction of in vivo drug interactions. Br. J. Clin. Pharmacol., 2000, 49(3), 244-253.
    • (2000) Br. J. Clin. Pharmacol , vol.49 , Issue.3 , pp. 244-253
    • Ohyama, K.1    Nakajima, M.2    Suzuki, M.3    Shimada, N.4    Yamazaki, H.5    Yokoi, T.6
  • 178
    • 0034014663 scopus 로고    scopus 로고
    • Inhibition of human cytochrome P450 enzymes by 1,2-dithiole-3-thione, oltipraz and its derivatives, and sulforaphane
    • Langouet, S.; Furge, L. L.; Kerriguy, N.; Nakamura, K.; Guillouzo, A.; Guengerich, F. P. Inhibition of human cytochrome P450 enzymes by 1,2-dithiole-3-thione, oltipraz and its derivatives, and sulforaphane. Chem. Res. Toxicol., 2000, 13(4), 245-252.
    • (2000) Chem. Res. Toxicol , vol.13 , Issue.4 , pp. 245-252
    • Langouet, S.1    Furge, L.L.2    Kerriguy, N.3    Nakamura, K.4    Guillouzo, A.5    Guengerich, F.P.6
  • 179
    • 0035192944 scopus 로고    scopus 로고
    • Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: Evidence for mechanism-based inactivation of CYP1A2
    • Chang, T. K.; Chen, J.; Lee, W. B. Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: evidence for mechanism-based inactivation of CYP1A2. J. Pharmacol. Exp. Ther., 2001, 299(3), 874-882.
    • (2001) J. Pharmacol. Exp. Ther , vol.299 , Issue.3 , pp. 874-882
    • Chang, T.K.1    Chen, J.2    Lee, W.B.3
  • 180
    • 34047253007 scopus 로고    scopus 로고
    • Different mechanisms for inhibition of human cytochromes P450 1A1, 1A2, and 1B1 by polycyclic aromatic inhibitors
    • Shimada, T.; Murayama, N.; Okada, K.; Funae, Y.; Yamazaki, H.; Guengerich, F. P. Different mechanisms for inhibition of human cytochromes P450 1A1, 1A2, and 1B1 by polycyclic aromatic inhibitors. Chem. Res. Toxicol., 2007, 20(3), 489-496.
    • (2007) Chem. Res. Toxicol , vol.20 , Issue.3 , pp. 489-496
    • Shimada, T.1    Murayama, N.2    Okada, K.3    Funae, Y.4    Yamazaki, H.5    Guengerich, F.P.6
  • 181
    • 19444374624 scopus 로고    scopus 로고
    • Organophosphorothionate pesticides inhibit the bioactivation of imipramine by human hepatic cytochrome P450s
    • Di Consiglio, E.; Meneguz, A.; Testai, E. Organophosphorothionate pesticides inhibit the bioactivation of imipramine by human hepatic cytochrome P450s. Toxicol. Appl. Pharmacol., 2005, 205(3), 237-246.
    • (2005) Toxicol. Appl. Pharmacol , vol.205 , Issue.3 , pp. 237-246
    • Di Consiglio, E.1    Meneguz, A.2    Testai, E.3
  • 183
    • 85030294813 scopus 로고    scopus 로고
    • Drug interactions with zileuton
    • Lau, R. Drug interactions with zileuton. Lancet, 1997, 349(9063), 1479-1480.
    • (1997) Lancet , vol.349 , Issue.9063 , pp. 1479-1480
    • Lau, R.1
  • 184
    • 0028856906 scopus 로고
    • Pharmacodynamic and stereoselective pharmacokinetic interactions between zileuton and warfarin in humans
    • Awni, W. M.; Hussein, Z.; Granneman, G. R.; Patterson, K. J.; Dube, L. M.; Cavanaugh, J. H. Pharmacodynamic and stereoselective pharmacokinetic interactions between zileuton and warfarin in humans. Clin. Pharmacokinet., 1995, 29(Suppl 2), 67-76.
    • (1995) Clin. Pharmacokinet , vol.29 , Issue.SUPPL. 2 , pp. 67-76
    • Awni, W.M.1    Hussein, Z.2    Granneman, G.R.3    Patterson, K.J.4    Dube, L.M.5    Cavanaugh, J.H.6
  • 186
    • 0028802939 scopus 로고
    • Lack of pharmacokinetic interaction between zileuton and phenytoin in humans
    • Samara, E.; Cavanaugh, J. H.; Mukherjee, D.; Granneman, G. R. Lack of pharmacokinetic interaction between zileuton and phenytoin in humans. Clin. Pharmacokinet., 1995, 29(Suppl 2), 84-91.
    • (1995) Clin. Pharmacokinet , vol.29 , Issue.SUPPL. 2 , pp. 84-91
    • Samara, E.1    Cavanaugh, J.H.2    Mukherjee, D.3    Granneman, G.R.4
  • 187
    • 0028885993 scopus 로고
    • Assessment of the pharmacokinetic interaction between zileuton and digoxin in humans
    • Awni, W. M.; Hussein, Z.; Cavanaugh, J. H.; Granneman, G. R.; Dube, L. M. Assessment of the pharmacokinetic interaction between zileuton and digoxin in humans. Clin. Pharmacokinet., 1995, 29(Suppl 2), 92-97.
    • (1995) Clin. Pharmacokinet , vol.29 , Issue.SUPPL. 2 , pp. 92-97
    • Awni, W.M.1    Hussein, Z.2    Cavanaugh, J.H.3    Granneman, G.R.4    Dube, L.M.5
  • 188
    • 0028828041 scopus 로고
    • The pharmacokinetic and pharmacodynamic interactions between the 5-lipoxygenase inhibitor zileuton and the cyclooxygenase inhibitor naproxen in human volunteers
    • Awni, W. M.; Braeckman, R. A.; Cavanaugh, J. H.; Locke, C. S.; Linnen, P. J.; Granneman, G. R.; Dube, L. M. The pharmacokinetic and pharmacodynamic interactions between the 5-lipoxygenase inhibitor zileuton and the cyclooxygenase inhibitor naproxen in human volunteers. Clin. Pharmacokinet., 1995, 29(Suppl 2), 112-124.
    • (1995) Clin. Pharmacokinet , vol.29 , Issue.SUPPL. 2 , pp. 112-124
    • Awni, W.M.1    Braeckman, R.A.2    Cavanaugh, J.H.3    Locke, C.S.4    Linnen, P.J.5    Granneman, G.R.6    Dube, L.M.7
  • 190
    • 0028875885 scopus 로고
    • The influence of multiple oral doses of zileuton on the steady-state pharmacokinetics of sulfasalazine and its metabolites, sulfapyridine and N-acetylsulfapyridine
    • Awni, W. M.; Braeckman, R. A.; Locke, C. S.; Dube, L. M.; Granneman, G. R. The influence of multiple oral doses of zileuton on the steady-state pharmacokinetics of sulfasalazine and its metabolites, sulfapyridine and N-acetylsulfapyridine. Clin. Pharmacokinet., 1995, 29(Suppl 2), 98-104.
    • (1995) Clin. Pharmacokinet , vol.29 , Issue.SUPPL. 2 , pp. 98-104
    • Awni, W.M.1    Braeckman, R.A.2    Locke, C.S.3    Dube, L.M.4    Granneman, G.R.5
  • 194
    • 33747072651 scopus 로고    scopus 로고
    • Rofecoxib is a potent inhibitor of cytochrome P450 1A2: Studies with tizanidine and caffeine in healthy subjects
    • Backman, J. T.; Karjalainen, M. J.; Neuvonen, M.; Laitila, J.; Neuvonen, P. J. Rofecoxib is a potent inhibitor of cytochrome P450 1A2: studies with tizanidine and caffeine in healthy subjects. Br. J. Clin. Pharmacol., 2006, 62(3), 345-357.
    • (2006) Br. J. Clin. Pharmacol , vol.62 , Issue.3 , pp. 345-357
    • Backman, J.T.1    Karjalainen, M.J.2    Neuvonen, M.3    Laitila, J.4    Neuvonen, P.J.5
  • 197
  • 198
    • 0028898044 scopus 로고
    • Selective serotonin reuptake inhibitors and theophylline metabolism in human liver microsomes: Potent inhibition by fluvoxamine
    • Rasmussen, B. B.; Maenpaa, J.; Pelkonen, O.; Loft, S.; Poulsen, H. E.; Lykkesfeldt, J.; Brosen, K. Selective serotonin reuptake inhibitors and theophylline metabolism in human liver microsomes: potent inhibition by fluvoxamine. Br. J. Clin. Pharmacol., 1995, 39(2), 151-159.
    • (1995) Br. J. Clin. Pharmacol , vol.39 , Issue.2 , pp. 151-159
    • Rasmussen, B.B.1    Maenpaa, J.2    Pelkonen, O.3    Loft, S.4    Poulsen, H.E.5    Lykkesfeldt, J.6    Brosen, K.7
  • 199
    • 0031581817 scopus 로고    scopus 로고
    • Distinction of CYP1A1 and CYP1A2 activity by selective inhibition using fluvoxamine and isosafrole
    • Pastrakuljic, A.; Tang, B. K.; Roberts, E. A.; Kalow, W. Distinction of CYP1A1 and CYP1A2 activity by selective inhibition using fluvoxamine and isosafrole. Biochem. Pharmacol., 1997, 53(4), 531-538.
    • (1997) Biochem. Pharmacol , vol.53 , Issue.4 , pp. 531-538
    • Pastrakuljic, A.1    Tang, B.K.2    Roberts, E.A.3    Kalow, W.4
  • 200
    • 0021824615 scopus 로고
    • Impairment of caffeine clearance by chronic use of low-dose oestrogen-containing oral contraceptives
    • Abernethy, D. R.; Todd, E. L. Impairment of caffeine clearance by chronic use of low-dose oestrogen-containing oral contraceptives. Eur. J. Clin. Pharmacol., 1985, 28(4), 425-428.
    • (1985) Eur. J. Clin. Pharmacol , vol.28 , Issue.4 , pp. 425-428
    • Abernethy, D.R.1    Todd, E.L.2
  • 201
    • 0027999366 scopus 로고
    • Inhibition of caffeine metabolism by ciprofloxacin in children with cystic fibrosis as measured by the caffeine breath test
    • Parker, A. C.; Preston, T.; Heaf, D.; Kitteringham, N. R.; Choonara, I. Inhibition of caffeine metabolism by ciprofloxacin in children with cystic fibrosis as measured by the caffeine breath test. Br. J. Clin. Pharmacol., 1994, 38(6), 573-576.
    • (1994) Br. J. Clin. Pharmacol , vol.38 , Issue.6 , pp. 573-576
    • Parker, A.C.1    Preston, T.2    Heaf, D.3    Kitteringham, N.R.4    Choonara, I.5
  • 202
    • 10044260714 scopus 로고    scopus 로고
    • Ciprofloxacin greatly increases concentrations and hypotensive effect of tizanidine by inhibiting its cytochrome P450 1A2-mediated presystemic metabolism
    • Granfors, M. T.; Backman, J. T.; Neuvonen, M.; Neuvonen, P. J. Ciprofloxacin greatly increases concentrations and hypotensive effect of tizanidine by inhibiting its cytochrome P450 1A2-mediated presystemic metabolism. Clin. Pharmacol. Ther., 2004, 76(6), 598-606.
    • (2004) Clin. Pharmacol. Ther , vol.76 , Issue.6 , pp. 598-606
    • Granfors, M.T.1    Backman, J.T.2    Neuvonen, M.3    Neuvonen, P.J.4
  • 203
  • 204
    • 24944458055 scopus 로고    scopus 로고
    • Effect of antifungal drugs on cytochrome P450 (CYP) 1A2, CYP2D6, and CYP2E1 activities in human liver microsomes
    • Niwa, T.; Inoue-Yamamoto, S.; Shiraga, T.; Takagi, A. Effect of antifungal drugs on cytochrome P450 (CYP) 1A2, CYP2D6, and CYP2E1 activities in human liver microsomes. Biol. Pharm. Bull., 2005, 28(9), 1813-1816.
    • (2005) Biol. Pharm. Bull , vol.28 , Issue.9 , pp. 1813-1816
    • Niwa, T.1    Inoue-Yamamoto, S.2    Shiraga, T.3    Takagi, A.4
  • 205
  • 206
  • 207
    • 0030834105 scopus 로고    scopus 로고
    • Venlafaxine: In vitro inhibition of CYP2D6 dependent imipramine and desipramine metabolism; comparative studies with selected SSRIs, and effects on human hepatic CYP3A4, CYP2C9 and CYP1A2
    • Ball, S. E.; Ahern, D.; Scatina, J.; Kao, J. Venlafaxine: in vitro inhibition of CYP2D6 dependent imipramine and desipramine metabolism; comparative studies with selected SSRIs, and effects on human hepatic CYP3A4, CYP2C9 and CYP1A2. Br. J. Clin. Pharmacol., 1997, 43(6), 619-626.
    • (1997) Br. J. Clin. Pharmacol , vol.43 , Issue.6 , pp. 619-626
    • Ball, S.E.1    Ahern, D.2    Scatina, J.3    Kao, J.4
  • 208
    • 0031785065 scopus 로고    scopus 로고
    • Comparative inhibition of human cytochromes P450 1A1 and 1A2 by flavonoids
    • Zhai, S.; Dai, R.; Friedman, F. K.; Vestal, R. E. Comparative inhibition of human cytochromes P450 1A1 and 1A2 by flavonoids. Drug Metab. Dispos., 1998, 26(10), 989-992.
    • (1998) Drug Metab. Dispos , vol.26 , Issue.10 , pp. 989-992
    • Zhai, S.1    Dai, R.2    Friedman, F.K.3    Vestal, R.E.4
  • 209
    • 0036181017 scopus 로고    scopus 로고
    • The alkaloid rutaecarpine is a selective inhibitor of cy tochrome P450 1A in mouse and human liver microsomes
    • Ueng, Y. F.; Jan, W. C.; Lin, L. C.; Chen, T. L.; Guengerich, F. P.; Chen, C. F. The alkaloid rutaecarpine is a selective inhibitor of cy tochrome P450 1A in mouse and human liver microsomes. Drug Metab. Dispos., 2002, 30(3), 349-353.
    • (2002) Drug Metab. Dispos , vol.30 , Issue.3 , pp. 349-353
    • Ueng, Y.F.1    Jan, W.C.2    Lin, L.C.3    Chen, T.L.4    Guengerich, F.P.5    Chen, C.F.6
  • 210
    • 0033584453 scopus 로고    scopus 로고
    • Resveratrol is a selective human cytochrome P450 1A1 inhibitor
    • Chun, Y. J.; Kim, M. Y.; Guengerich, F. P. Resveratrol is a selective human cytochrome P450 1A1 inhibitor. Biochem. Biophys. Res. Commun., 1999, 262(1), 20-24.
    • (1999) Biochem. Biophys. Res. Commun , vol.262 , Issue.1 , pp. 20-24
    • Chun, Y.J.1    Kim, M.Y.2    Guengerich, F.P.3
  • 211
    • 0037666303 scopus 로고    scopus 로고
    • Differential inhibition of human cytochrome P450 enzymes by ε-viniferin, the dimer of resveratrol: Comparison with resveratrol and polyphenols from alcoholized beverages
    • Piver, B.; Berthou, F.; Dreano, Y.; Lucas, D. Differential inhibition of human cytochrome P450 enzymes by ε-viniferin, the dimer of resveratrol: comparison with resveratrol and polyphenols from alcoholized beverages. Life Sci., 2003, 73(9), 1199-1213.
    • (2003) Life Sci , vol.73 , Issue.9 , pp. 1199-1213
    • Piver, B.1    Berthou, F.2    Dreano, Y.3    Lucas, D.4
  • 212
    • 0035064593 scopus 로고    scopus 로고
    • Mechanism-based inhibition of human cytochrome P450 1A1 by rhapontigenin
    • Chun, Y. J.; Ryu, S. Y.; Jeong, T. C.; Kim, M. Y. Mechanism-based inhibition of human cytochrome P450 1A1 by rhapontigenin. Drug Metab. Dispos., 2001, 29(4 Pt 1), 389-393.
    • (2001) Drug Metab. Dispos , vol.29 , Issue.4 PART 1 , pp. 389-393
    • Chun, Y.J.1    Ryu, S.Y.2    Jeong, T.C.3    Kim, M.Y.4
  • 213
    • 34347235844 scopus 로고    scopus 로고
    • Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2
    • Sansen, S.; Yano, J. K.; Reynald, R. L.; Schoch, G. A.; Griffin, K. J.; Stout, C. D.; Johnson, E. F. Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. J. Biol. Chem., 2007, 282(19), 14348-14355.
    • (2007) J. Biol. Chem , vol.282 , Issue.19 , pp. 14348-14355
    • Sansen, S.1    Yano, J.K.2    Reynald, R.L.3    Schoch, G.A.4    Griffin, K.J.5    Stout, C.D.6    Johnson, E.F.7
  • 214
    • 1542364450 scopus 로고    scopus 로고
    • Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site
    • Schoch, G. A.; Yano, J. K.; Wester, M. R.; Griffin, K. J.; Stout, C. D.; Johnson, E. F. Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site. J. Biol. Chem., 2004, 279(10), 9497-9503.
    • (2004) J. Biol. Chem , vol.279 , Issue.10 , pp. 9497-9503
    • Schoch, G.A.1    Yano, J.K.2    Wester, M.R.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 215
    • 26944462419 scopus 로고    scopus 로고
    • Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen
    • Yano, J. K.; Hsu, M. H.; Griffin, K. J.; Stout, C. D.; Johnson, E. F. Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. Nat. Struct. Mol. Biol., 2005, 12(9), 822-823.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , Issue.9 , pp. 822-823
    • Yano, J.K.1    Hsu, M.H.2    Griffin, K.J.3    Stout, C.D.4    Johnson, E.F.5
  • 216
    • 0042573727 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 A resolution: Evidence for an induced fit model of substrate binding
    • Wester, M. R.; Johnson, E. F.; Marques-Soares, C.; Dijols, S.; Dansette, P. M.; Mansuy, D.; Stout, C. D. Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 A resolution: evidence for an induced fit model of substrate binding. Biochemistry, 2003, 42(31), 9335-9345.
    • (2003) Biochemistry , vol.42 , Issue.31 , pp. 9335-9345
    • Wester, M.R.1    Johnson, E.F.2    Marques-Soares, C.3    Dijols, S.4    Dansette, P.M.5    Mansuy, D.6    Stout, C.D.7
  • 217
    • 0036028701 scopus 로고    scopus 로고
    • Purification and crystallization of N-terminally truncated forms of microsomal cytochrome P450 2C5
    • Wester, M. R.; Stout, C. D.; Johnson, E. F. Purification and crystallization of N-terminally truncated forms of microsomal cytochrome P450 2C5. Methods Enzymol., 2002, 357, 73-79.
    • (2002) Methods Enzymol , vol.357 , pp. 73-79
    • Wester, M.R.1    Stout, C.D.2    Johnson, E.F.3
  • 218
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • Williams, P. A.; Cosme, J.; Sridhar, V.; Johnson, E. F.; McRee, D. E. Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell, 2000, 5(1), 121-131.
    • (2000) Mol. Cell , vol.5 , Issue.1 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 219
    • 33645673185 scopus 로고    scopus 로고
    • Identification of membrane-contacting loops of the catalytic domain of cytochrome P450 2C2 by tryptophan fluorescence scanning
    • Ozalp, C.; Szczesna-Skorupa, E.; Kemper, B. Identification of membrane-contacting loops of the catalytic domain of cytochrome P450 2C2 by tryptophan fluorescence scanning. Biochemistry, 2006, 45(14), 4629-4637.
    • (2006) Biochemistry , vol.45 , Issue.14 , pp. 4629-4637
    • Ozalp, C.1    Szczesna-Skorupa, E.2    Kemper, B.3
  • 220
    • 0042265520 scopus 로고    scopus 로고
    • Crystal structure of human cytochrome P450 2C9 with bound warfarin
    • Williams, P. A.; Cosme, J.; Ward, A.; Angove, H. C.; Matak Vinkovic, D.; Jhoti, H. Crystal structure of human cytochrome P450 2C9 with bound warfarin. Nature, 2003, 424(6947), 464-468.
    • (2003) Nature , vol.424 , Issue.6947 , pp. 464-468
    • Williams, P.A.1    Cosme, J.2    Ward, A.3    Angove, H.C.4    Matak Vinkovic, D.5    Jhoti, H.6
  • 221
    • 4143143372 scopus 로고    scopus 로고
    • The structure of human cytochrome P450 2C9 complexed with flurbiprofen at 2.0-Å resolution
    • Wester, M. R.; Yano, J. K.; Schoch, G. A.; Yang, C.; Griffin, K. J.; Stout, C. D.; Johnson, E. F. The structure of human cytochrome P450 2C9 complexed with flurbiprofen at 2.0-Å resolution. J. Biol. Chem., 2004, 279(34), 35630-35637.
    • (2004) J. Biol. Chem , vol.279 , Issue.34 , pp. 35630-35637
    • Wester, M.R.1    Yano, J.K.2    Schoch, G.A.3    Yang, C.4    Griffin, K.J.5    Stout, C.D.6    Johnson, E.F.7
  • 223
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: Insight into the range of P450 conformations and the coordination of redox partner binding
    • Scott, E. E.; White, M. A.; He, Y. A.; Johnson, E. F.; Stout, C. D.; Halpert, J. R. Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: insight into the range of P450 conformations and the coordination of redox partner binding. J. Biol. Chem., 2004, 279(26), 27294-27301.
    • (2004) J. Biol. Chem , vol.279 , Issue.26 , pp. 27294-27301
    • Scott, E.E.1    White, M.A.2    He, Y.A.3    Johnson, E.F.4    Stout, C.D.5    Halpert, J.R.6
  • 225
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-Å resolution
    • Yano, J. K.; Wester, M. R.; Schoch, G. A.; Griffin, K. J.; Stout, C. D.; Johnson, E. F. The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-Å resolution. J. Biol. Chem., 2004, 279(37), 38091-38094.
    • (2004) J. Biol. Chem , vol.279 , Issue.37 , pp. 38091-38094
    • Yano, J.K.1    Wester, M.R.2    Schoch, G.A.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 227
    • 1242318619 scopus 로고    scopus 로고
    • Tight-binding inhibition by α-naphthoflavone of human cytochrome P450 1A2
    • Cho, U. S.; Park, E. Y.; Dong, M. S.; Park, B. S.; Kim, K.; Kim, K. H. Tight-binding inhibition by α-naphthoflavone of human cytochrome P450 1A2. Biochim. Biophys. Acta, 2003, 1648(1-2), 195-202.
    • (2003) Biochim. Biophys. Acta , vol.1648 , Issue.1-2 , pp. 195-202
    • Cho, U.S.1    Park, E.Y.2    Dong, M.S.3    Park, B.S.4    Kim, K.5    Kim, K.H.6
  • 228
    • 1542328873 scopus 로고    scopus 로고
    • The effect of reciprocal active site mutations in human cytochromes P450 1A1 and 1A2 on alkoxyresorufin metabolism
    • Liu, J.; Ericksen, S. S.; Sivaneri, M.; Besspiata, D.; Fisher, C. W.; Szklarz, G. D. The effect of reciprocal active site mutations in human cytochromes P450 1A1 and 1A2 on alkoxyresorufin metabolism. Arch. Biochem. Biophys., 2004, 424(1), 33-43.
    • (2004) Arch. Biochem. Biophys , vol.424 , Issue.1 , pp. 33-43
    • Liu, J.1    Ericksen, S.S.2    Sivaneri, M.3    Besspiata, D.4    Fisher, C.W.5    Szklarz, G.D.6
  • 229
    • 33745048978 scopus 로고    scopus 로고
    • Rifampicin is only a weak inducer of CYP1A2-mediated presystemic and systemic metabolism: Studies with tizanidine and caffeine
    • Backman, J. T.; Granfors, M. T.; Neuvonen, P. J. Rifampicin is only a weak inducer of CYP1A2-mediated presystemic and systemic metabolism: studies with tizanidine and caffeine. Eur. J. Clin. Pharmacol., 2006, 62(6), 451-461.
    • (2006) Eur. J. Clin. Pharmacol , vol.62 , Issue.6 , pp. 451-461
    • Backman, J.T.1    Granfors, M.T.2    Neuvonen, P.J.3
  • 231
    • 0019845496 scopus 로고
    • Assessment of the cytochrome P448 dependent liver enzyme system by a caffeine breath test
    • Wietholtz, H.; Voegelin, M.; Arnaud, M. J.; Bircher, J.; Preisig, R. Assessment of the cytochrome P448 dependent liver enzyme system by a caffeine breath test. Eur. J. Clin. Pharmacol., 1981, 21(1), 53-59.
    • (1981) Eur. J. Clin. Pharmacol , vol.21 , Issue.1 , pp. 53-59
    • Wietholtz, H.1    Voegelin, M.2    Arnaud, M.J.3    Bircher, J.4    Preisig, R.5
  • 232
    • 0033055995 scopus 로고    scopus 로고
    • Drug interactions with tobacco smoking. An update
    • Zevin, S.; Benowitz, N. L. Drug interactions with tobacco smoking. An update. Clin. Pharmacokinet., 1999, 36(6), 425-438.
    • (1999) Clin. Pharmacokinet , vol.36 , Issue.6 , pp. 425-438
    • Zevin, S.1    Benowitz, N.L.2
  • 233
    • 0019625841 scopus 로고
    • Cigarette smoking and theophylline clearance and metabolism
    • Grygiel, J. J.; Birkett, D. J. Cigarette smoking and theophylline clearance and metabolism. Clin. Pharmacol. Ther., 1981, 30(4), 491-496.
    • (1981) Clin. Pharmacol. Ther , vol.30 , Issue.4 , pp. 491-496
    • Grygiel, J.J.1    Birkett, D.J.2
  • 234
    • 0036433001 scopus 로고    scopus 로고
    • Inducibility of CYP1A2 by omeprazole in vivo related to the genetic polymorphism of CYP1A2
    • Han, X. M.; Ouyang, D. S.; Chen, X. P.; Shu, Y.; Jiang, C. H.; Tan, Z. R.; Zhou, H. H. Inducibility of CYP1A2 by omeprazole in vivo related to the genetic polymorphism of CYP1A2. Br. J. Clin. Pharmacol., 2002, 54(5), 540-543.
    • (2002) Br. J. Clin. Pharmacol , vol.54 , Issue.5 , pp. 540-543
    • Han, X.M.1    Ouyang, D.S.2    Chen, X.P.3    Shu, Y.4    Jiang, C.H.5    Tan, Z.R.6    Zhou, H.H.7
  • 235
    • 45049083306 scopus 로고    scopus 로고
    • Omeprazole transactivates human CYP1A1 and CYP1A2 expression through the common regulatory region containing multiple xenobiotic-responsive elements
    • Yoshinari, K.; Ueda, R.; Kusano, K.; Yoshimura, T.; Nagata, K.; Yamazoe, Y. Omeprazole transactivates human CYP1A1 and CYP1A2 expression through the common regulatory region containing multiple xenobiotic-responsive elements. Biochem. Pharmacol., 2008, 76(1), 139-145.
    • (2008) Biochem. Pharmacol , vol.76 , Issue.1 , pp. 139-145
    • Yoshinari, K.1    Ueda, R.2    Kusano, K.3    Yoshimura, T.4    Nagata, K.5    Yamazoe, Y.6
  • 237
    • 0032479408 scopus 로고    scopus 로고
    • An evaluation of the cytochrome P450 induction potential of pantoprazole in primary human hepatocytes
    • Masubuchi, N.; Li, A. P.; Okazaki, O. An evaluation of the cytochrome P450 induction potential of pantoprazole in primary human hepatocytes. Chem. Biol. Interact., 1998, 114(1-2), 1-13.
    • (1998) Chem. Biol. Interact , vol.114 , Issue.1-2 , pp. 1-13
    • Masubuchi, N.1    Li, A.P.2    Okazaki, O.3
  • 238
    • 0026699994 scopus 로고
    • Increase of cytochrome P450IA2 activity by omeprazole: Evidence by the 13C-[N-3-methyl]-caffeine breath test in poor and extensive metabolizers of '-mephenytoin
    • Rost, K. L.; Brosicke, H.; Brockmoller, J.; Scheffler, M.; Helge, H.; Roots, I. Increase of cytochrome P450IA2 activity by omeprazole: evidence by the 13C-[N-3-methyl]-caffeine breath test in poor and extensive metabolizers of '-mephenytoin. Clin. Pharmacol. Ther., 1992, 52(2), 170-180.
    • (1992) Clin. Pharmacol. Ther , vol.52 , Issue.2 , pp. 170-180
    • Rost, K.L.1    Brosicke, H.2    Brockmoller, J.3    Scheffler, M.4    Helge, H.5    Roots, I.6
  • 240
    • 0028051743 scopus 로고
    • Specific and dose-dependent enzyme induction by omeprazole in human beings
    • Rost, K. L.; Brosicke, H.; Heinemeyer, G.; Roots, I. Specific and dose-dependent enzyme induction by omeprazole in human beings. Hepatology, 1994, 20(5), 1204-1212.
    • (1994) Hepatology , vol.20 , Issue.5 , pp. 1204-1212
    • Rost, K.L.1    Brosicke, H.2    Heinemeyer, G.3    Roots, I.4
  • 243
    • 0029986312 scopus 로고    scopus 로고
    • Omeprazole and lansoprazole are not inducers of cytochrome P4501A2 under conventional therapeutic conditions
    • Rizzo, N.; Padoin, C.; Palombo, S.; Scherrmann, J. M.; Girre, C. Omeprazole and lansoprazole are not inducers of cytochrome P4501A2 under conventional therapeutic conditions. Eur. J. Clin. Pharmacol., 1996, 49(6), 491-495.
    • (1996) Eur. J. Clin. Pharmacol , vol.49 , Issue.6 , pp. 491-495
    • Rizzo, N.1    Padoin, C.2    Palombo, S.3    Scherrmann, J.M.4    Girre, C.5
  • 244
    • 2642510760 scopus 로고    scopus 로고
    • Role of aryl hydrocarbon receptor-mediated induction of the CYP1 enzymes in environmental toxicity and cancer
    • Nebert, D. W.; Dalton, T. P.; Okey, A. B.; Gonzalez, F. J. Role of aryl hydrocarbon receptor-mediated induction of the CYP1 enzymes in environmental toxicity and cancer. J. Biol. Chem., 2004, 279(23), 23847-23850.
    • (2004) J. Biol. Chem , vol.279 , Issue.23 , pp. 23847-23850
    • Nebert, D.W.1    Dalton, T.P.2    Okey, A.B.3    Gonzalez, F.J.4
  • 245
    • 0034969560 scopus 로고    scopus 로고
    • Induction of CYP1A1. The AhR/DRE paradigm: Transcription, receptor regulation, and expanding biological roles
    • Ma, Q. Induction of CYP1A1. The AhR/DRE paradigm: transcription, receptor regulation, and expanding biological roles. Curr. Drug Metab., 2001, 2(2), 149-164.
    • (2001) Curr. Drug Metab , vol.2 , Issue.2 , pp. 149-164
    • Ma, Q.1
  • 246
    • 0026725943 scopus 로고
    • Cloning of the Ahreceptor cDNA reveals a distinctive ligand-activated transcription factor
    • Burbach, K. M.; Poland, A.; Bradfield, C. A. Cloning of the Ahreceptor cDNA reveals a distinctive ligand-activated transcription factor. Proc. Natl. Acad. Sci. U. S. A., 1992, 89(17), 8185-8189.
    • (1992) Proc. Natl. Acad. Sci. U. S. A , vol.89 , Issue.17 , pp. 8185-8189
    • Burbach, K.M.1    Poland, A.2    Bradfield, C.A.3
  • 248
    • 0035834750 scopus 로고    scopus 로고
    • The Q-rich subdomain of the human Ah receptor transactivation domain is required for dioxin-mediated transcriptional activity
    • Kumar, M. B.; Ramadoss, P.; Reen, R. K.; Vanden Heuvel, J. P.; Perdew, G. H. The Q-rich subdomain of the human Ah receptor transactivation domain is required for dioxin-mediated transcriptional activity. J. Biol. Chem., 2001, 276(45), 42302-42310.
    • (2001) J. Biol. Chem , vol.276 , Issue.45 , pp. 42302-42310
    • Kumar, M.B.1    Ramadoss, P.2    Reen, R.K.3    Vanden Heuvel, J.P.4    Perdew, G.H.5
  • 251
    • 0037462747 scopus 로고    scopus 로고
    • The hsp90 Co-chaperone XAP2 alters importin-β recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activity
    • Petrulis, J. R.; Kusnadi, A.; Ramadoss, P.; Hollingshead, B.; Perdew, G. H. The hsp90 Co-chaperone XAP2 alters importin-β recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activity. J. Biol. Chem., 2003, 278(4), 2677-2685.
    • (2003) J. Biol. Chem , vol.278 , Issue.4 , pp. 2677-2685
    • Petrulis, J.R.1    Kusnadi, A.2    Ramadoss, P.3    Hollingshead, B.4    Perdew, G.H.5
  • 252
    • 0034532301 scopus 로고    scopus 로고
    • Subcellular localization of the aryl hydrocarbon receptor is modulated by the immunophilin homolog hepatitis B virus X-associated protein 2
    • Petrulis, J. R.; Hord, N. G.; Perdew, G. H. Subcellular localization of the aryl hydrocarbon receptor is modulated by the immunophilin homolog hepatitis B virus X-associated protein 2. J. Biol. Chem., 2000, 275(48), 37448-37453.
    • (2000) J. Biol. Chem , vol.275 , Issue.48 , pp. 37448-37453
    • Petrulis, J.R.1    Hord, N.G.2    Perdew, G.H.3
  • 253
    • 33751088551 scopus 로고    scopus 로고
    • Endogenous hepatic expression of the hepatitis B virus X-associated protein 2 is adequate for maximal association with aryl hydrocarbon receptor-90-kDa heat shock protein complexes
    • Hollingshead, B. D.; Patel, R. D.; Perdew, G. H. Endogenous hepatic expression of the hepatitis B virus X-associated protein 2 is adequate for maximal association with aryl hydrocarbon receptor-90-kDa heat shock protein complexes. Mol. Pharmacol., 2006, 70(6), 2096-2107.
    • (2006) Mol. Pharmacol , vol.70 , Issue.6 , pp. 2096-2107
    • Hollingshead, B.D.1    Patel, R.D.2    Perdew, G.H.3
  • 254
    • 0032509519 scopus 로고    scopus 로고
    • Characterization of the Ah receptor-associated protein, ARA9
    • Carver, L. A.; LaPres, J. J.; Jain, S.; Dunham, E. E.; Bradfield, C. A. Characterization of the Ah receptor-associated protein, ARA9. J. Biol. Chem., 1998, 273(50), 33580-33587.
    • (1998) J. Biol. Chem , vol.273 , Issue.50 , pp. 33580-33587
    • Carver, L.A.1    LaPres, J.J.2    Jain, S.3    Dunham, E.E.4    Bradfield, C.A.5
  • 255
    • 0028077887 scopus 로고
    • The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system
    • Carver, L. A.; Jackiw, V.; Bradfield, C. A. The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system. J. Biol. Chem., 1994, 269(48), 30109-30112.
    • (1994) J. Biol. Chem , vol.269 , Issue.48 , pp. 30109-30112
    • Carver, L.A.1    Jackiw, V.2    Bradfield, C.A.3
  • 256
    • 0038768712 scopus 로고    scopus 로고
    • Activation of the aryl hydrocarbon receptor by structurally diverse exogenous and endogenous chemicals
    • 309-334
    • Denison, M. S.; Nagy, S. R. Activation of the aryl hydrocarbon receptor by structurally diverse exogenous and endogenous chemicals. Annu. Rev. Pharmacol. Toxicol., 2003, 43(309-334.
    • (2003) Annu. Rev. Pharmacol. Toxicol , vol.43
    • Denison, M.S.1    Nagy, S.R.2
  • 258
    • 0023665615 scopus 로고
    • Characterization of xenobiotic responsive elements upstream from the drug-metabolizing cytochrome P-450c gene: A similarity to glucocorticoid regulatory elements
    • Fujisawa-Sehara, A.; Sogawa, K.; Yamane, M.; Fujii-Kuriyama, Y. Characterization of xenobiotic responsive elements upstream from the drug-metabolizing cytochrome P-450c gene: a similarity to glucocorticoid regulatory elements. Nucleic Acids Res., 1987, 15(10), 4179-4191.
    • (1987) Nucleic Acids Res , vol.15 , Issue.10 , pp. 4179-4191
    • Fujisawa-Sehara, A.1    Sogawa, K.2    Yamane, M.3    Fujii-Kuriyama, Y.4
  • 259
    • 0141459483 scopus 로고    scopus 로고
    • Ah receptor regulation of mouse Cyp1B1 is additionally modulated by a second novel complex that forms at two AhR response elements
    • Zhang, L.; Zheng, W.; Jefcoate, C. R. Ah receptor regulation of mouse Cyp1B1 is additionally modulated by a second novel complex that forms at two AhR response elements. Toxicol. Appl. Pharmacol., 2003, 192(2), 174-190.
    • (2003) Toxicol. Appl. Pharmacol , vol.192 , Issue.2 , pp. 174-190
    • Zhang, L.1    Zheng, W.2    Jefcoate, C.R.3
  • 260
    • 0032570685 scopus 로고    scopus 로고
    • Characterization of the mouse Cyp1B1 gene. Identification of an enhancer region that directs aryl hydrocarbon receptor-mediated constitutive and induced expression
    • Zhang, L.; Savas, U.; Alexander, D. L.; Jefcoate, C. R. Characterization of the mouse Cyp1B1 gene. Identification of an enhancer region that directs aryl hydrocarbon receptor-mediated constitutive and induced expression. J. Biol. Chem., 1998, 273(9), 5174-5183.
    • (1998) J. Biol. Chem , vol.273 , Issue.9 , pp. 5174-5183
    • Zhang, L.1    Savas, U.2    Alexander, D.L.3    Jefcoate, C.R.4
  • 261
    • 0038236664 scopus 로고    scopus 로고
    • Involvement of the xenobiotic response element (XRE) in Ah receptor-mediated induction of human UDP-glucuronosyltransferase 1A1
    • Yueh, M. F.; Huang, Y. H.; Hiller, A.; Chen, S.; Nguyen, N.; Tukey, R. H. Involvement of the xenobiotic response element (XRE) in Ah receptor-mediated induction of human UDP-glucuronosyltransferase 1A1. J. Biol. Chem., 2003, 278(17), 15001-15006.
    • (2003) J. Biol. Chem , vol.278 , Issue.17 , pp. 15001-15006
    • Yueh, M.F.1    Huang, Y.H.2    Hiller, A.3    Chen, S.4    Nguyen, N.5    Tukey, R.H.6
  • 262
    • 0032899367 scopus 로고    scopus 로고
    • Identification of a novel mechanism of regulation of Ah (dioxin) receptor function
    • Mimura, J.; Ema, M.; Sogawa, K.; Fujii-Kuriyama, Y. Identification of a novel mechanism of regulation of Ah (dioxin) receptor function. Genes Dev., 1999, 13(1), 20-25.
    • (1999) Genes Dev , vol.13 , Issue.1 , pp. 20-25
    • Mimura, J.1    Ema, M.2    Sogawa, K.3    Fujii-Kuriyama, Y.4
  • 263
    • 0034987564 scopus 로고    scopus 로고
    • Human arylhydrocarbon receptor repressor (AHRR) gene: Genomic structure and analysis of polymorphism in endometriosis
    • Watanabe, T.; Imoto, I.; Kosugi, Y.; Fukuda, Y.; Mimura, J.; Fujii, Y.; Isaka, K.; Takayama, M.; Sato, A.; Inazawa, J. Human arylhydrocarbon receptor repressor (AHRR) gene: genomic structure and analysis of polymorphism in endometriosis. J. Hum. Genet., 2001, 46(6), 342-346.
    • (2001) J. Hum. Genet , vol.46 , Issue.6 , pp. 342-346
    • Watanabe, T.1    Imoto, I.2    Kosugi, Y.3    Fukuda, Y.4    Mimura, J.5    Fujii, Y.6    Isaka, K.7    Takayama, M.8    Sato, A.9    Inazawa, J.10
  • 265
    • 38549153970 scopus 로고    scopus 로고
    • Repression of aryl hydrocarbon receptor (AHR) signaling by AHR repressor: Role of DNA binding and competition for AHR nuclear translocator
    • Evans, B. R.; Karchner, S. I.; Allan, L. L.; Pollenz, R. S.; Tanguay, R. L.; Jenny, M. J.; Sherr, D. H.; Hahn, M. E. Repression of aryl hydrocarbon receptor (AHR) signaling by AHR repressor: role of DNA binding and competition for AHR nuclear translocator. Mol. Pharmacol., 2008, 73(2), 387-398.
    • (2008) Mol. Pharmacol , vol.73 , Issue.2 , pp. 387-398
    • Evans, B.R.1    Karchner, S.I.2    Allan, L.L.3    Pollenz, R.S.4    Tanguay, R.L.5    Jenny, M.J.6    Sherr, D.H.7    Hahn, M.E.8
  • 266
    • 36348985011 scopus 로고    scopus 로고
    • Analysis of the transcriptional regulation and molecular function of the aryl hydrocarbon receptor repressor in human cell lines
    • Haarmann-Stemmann, T.; Bothe, H.; Kohli, A.; Sydlik, U.; Abel, J.; Fritsche, E. Analysis of the transcriptional regulation and molecular function of the aryl hydrocarbon receptor repressor in human cell lines. Drug Metab Dispos, 2007, 35(12), 2262-2269.
    • (2007) Drug Metab Dispos , vol.35 , Issue.12 , pp. 2262-2269
    • Haarmann-Stemmann, T.1    Bothe, H.2    Kohli, A.3    Sydlik, U.4    Abel, J.5    Fritsche, E.6
  • 267
    • 33748750533 scopus 로고    scopus 로고
    • The arylhydrocarbon receptor repressor (AhRR): Structure, expression, and function
    • Haarmann-Stemmann, T.; Abel, J. The arylhydrocarbon receptor repressor (AhRR): structure, expression, and function. Biol. Chem., 2006, 387(9), 1195-1199.
    • (2006) Biol. Chem , vol.387 , Issue.9 , pp. 1195-1199
    • Haarmann-Stemmann, T.1    Abel, J.2
  • 268
    • 0030245635 scopus 로고    scopus 로고
    • Fernandez-Salguero, P. M.; Hilbert, D. M.; Rudikoff, S.; Ward, J. M.; Gonzalez, F. J. Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity. Toxicol. Appl. Pharmacol., 1996, 140(1), 173-179.
    • Fernandez-Salguero, P. M.; Hilbert, D. M.; Rudikoff, S.; Ward, J. M.; Gonzalez, F. J. Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity. Toxicol. Appl. Pharmacol., 1996, 140(1), 173-179.
  • 272
    • 33645808261 scopus 로고    scopus 로고
    • Liver deformation in Ahr-null mice: Evidence for aberrant hepatic perfusion in early development
    • Harstad, E. B.; Guite, C. A.; Thomae, T. L.; Bradfield, C. A. Liver deformation in Ahr-null mice: evidence for aberrant hepatic perfusion in early development. Mol. Pharmacol., 2006, 69(5), 1534-1541.
    • (2006) Mol. Pharmacol , vol.69 , Issue.5 , pp. 1534-1541
    • Harstad, E.B.1    Guite, C.A.2    Thomae, T.L.3    Bradfield, C.A.4
  • 273
    • 17544384815 scopus 로고    scopus 로고
    • ARNT-deficient mice and placental differentiation
    • Kozak, K. R.; Abbott, B.; Hankinson, O. ARNT-deficient mice and placental differentiation. Dev. Biol., 1997, 191(2), 297-305.
    • (1997) Dev. Biol , vol.191 , Issue.2 , pp. 297-305
    • Kozak, K.R.1    Abbott, B.2    Hankinson, O.3
  • 274
    • 37249016342 scopus 로고    scopus 로고
    • Deletion of the aryl hydrocarbon receptor-associated protein 9 leads to cardiac malformation and embryonic lethality
    • Lin, B. C.; Sullivan, R.; Lee, Y.; Moran, S.; Glover, E.; Bradfield, C. A. Deletion of the aryl hydrocarbon receptor-associated protein 9 leads to cardiac malformation and embryonic lethality. J. Biol. Chem., 2007, 282(49), 35924-35932.
    • (2007) J. Biol. Chem , vol.282 , Issue.49 , pp. 35924-35932
    • Lin, B.C.1    Sullivan, R.2    Lee, Y.3    Moran, S.4    Glover, E.5    Bradfield, C.A.6
  • 276
    • 0028034621 scopus 로고
    • Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors
    • Ema, M.; Ohe, N.; Suzuki, M.; Mimura, J.; Sogawa, K.; Ikawa, S.; Fujii-Kuriyama, Y. Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors. J. Biol. Chem., 1994, 269(44), 27337-27343.
    • (1994) J. Biol. Chem , vol.269 , Issue.44 , pp. 27337-27343
    • Ema, M.1    Ohe, N.2    Suzuki, M.3    Mimura, J.4    Sogawa, K.5    Ikawa, S.6    Fujii-Kuriyama, Y.7
  • 277
    • 0024337946 scopus 로고
    • Detection and characterization of a low affinity form of cytosolic Ah receptor in livers of mice nonresponsive to induction of cytochrome P1-450 by 3-methylcholanthrene
    • Okey, A. B.; Vella, L. M.; Harper, P. A. Detection and characterization of a low affinity form of cytosolic Ah receptor in livers of mice nonresponsive to induction of cytochrome P1-450 by 3-methylcholanthrene. Mol. Pharmacol., 1989, 35(6), 823-830.
    • (1989) Mol. Pharmacol , vol.35 , Issue.6 , pp. 823-830
    • Okey, A.B.1    Vella, L.M.2    Harper, P.A.3
  • 279
    • 0031438078 scopus 로고    scopus 로고
    • Signal transduction-mediated activation of the aryl hydrocarbon receptor in rat hepatoma H4IIE cells
    • Backlund, M.; Johansson, I.; Mkrtchian, S.; Ingelman-Sundberg, M. Signal transduction-mediated activation of the aryl hydrocarbon receptor in rat hepatoma H4IIE cells. J. Biol. Chem., 1997, 272(50), 31755-31763.
    • (1997) J. Biol. Chem , vol.272 , Issue.50 , pp. 31755-31763
    • Backlund, M.1    Johansson, I.2    Mkrtchian, S.3    Ingelman-Sundberg, M.4
  • 281
    • 17844385047 scopus 로고    scopus 로고
    • Metabolism-based drug-drug interactions: What determines individual variability in cytochrome P450 induction?
    • Tang, C.; Lin, J. H.; Lu, A. Y. Metabolism-based drug-drug interactions: what determines individual variability in cytochrome P450 induction? Drug Metab. Dispos., 2005, 33(5), 603-613.
    • (2005) Drug Metab. Dispos , vol.33 , Issue.5 , pp. 603-613
    • Tang, C.1    Lin, J.H.2    Lu, A.Y.3
  • 282
    • 2142695286 scopus 로고    scopus 로고
    • Oral exposure to benzo[a]pyrene in the mouse: Detoxication by inducible cytochrome P450 is more important than metabolic activation
    • Uno, S.; Dalton, T. P.; Derkenne, S.; Curran, C. P.; Miller, M. L.; Shertzer, H. G.; Nebert, D. W. Oral exposure to benzo[a]pyrene in the mouse: detoxication by inducible cytochrome P450 is more important than metabolic activation. Mol. Pharmacol., 2004, 65(5), 1225-1237.
    • (2004) Mol. Pharmacol , vol.65 , Issue.5 , pp. 1225-1237
    • Uno, S.1    Dalton, T.P.2    Derkenne, S.3    Curran, C.P.4    Miller, M.L.5    Shertzer, H.G.6    Nebert, D.W.7
  • 286
    • 0036775873 scopus 로고    scopus 로고
    • Effect of CYP1A2 deficiency on heterocyclic amine DNA adduct levels in mice
    • Snyderwine, E. G.; Yu, M.; Schut, H. A.; Knight-Jones, L.; Kimura, S. Effect of CYP1A2 deficiency on heterocyclic amine DNA adduct levels in mice. Food Chem. Toxicol., 2002, 40(10), 1529-1533.
    • (2002) Food Chem. Toxicol , vol.40 , Issue.10 , pp. 1529-1533
    • Snyderwine, E.G.1    Yu, M.2    Schut, H.A.3    Knight-Jones, L.4    Kimura, S.5
  • 288
    • 33745810900 scopus 로고    scopus 로고
    • For dioxin-induced birth defects, mouse or human CYP1A2 in maternal liver protects whereas mouse CYP1A1 and CYP1B1 are inconsequential
    • Dragin, N.; Dalton, T. P.; Miller, M. L.; Shertzer, H. G.; Nebert, D. W. For dioxin-induced birth defects, mouse or human CYP1A2 in maternal liver protects whereas mouse CYP1A1 and CYP1B1 are inconsequential. J. Biol. Chem., 2006, 281(27), 18591-18600.
    • (2006) J. Biol. Chem , vol.281 , Issue.27 , pp. 18591-18600
    • Dragin, N.1    Dalton, T.P.2    Miller, M.L.3    Shertzer, H.G.4    Nebert, D.W.5
  • 290
    • 0029758198 scopus 로고    scopus 로고
    • Role of CYP1A2 in caffeine pharmacokinetics and metabolism: Studies using mice deficient in CYP1A2
    • Buters, J. T.; Tang, B. K.; Pineau, T.; Gelboin, H. V.; Kimura, S.; Gonzalez, F. J. Role of CYP1A2 in caffeine pharmacokinetics and metabolism: studies using mice deficient in CYP1A2. Pharmacogenetics, 1996, 6(4), 291-296.
    • (1996) Pharmacogenetics , vol.6 , Issue.4 , pp. 291-296
    • Buters, J.T.1    Tang, B.K.2    Pineau, T.3    Gelboin, H.V.4    Kimura, S.5    Gonzalez, F.J.6
  • 291
    • 33645838033 scopus 로고    scopus 로고
    • Metabolism and hepatic toxicity of flutamide in cytochrome P450 1A2 knockout SV129 mice
    • Matsuzaki, Y.; Nagai, D.; Ichimura, E.; Goda, R.; Tomura, A.; Doi, M.; Nishikawa, K. Metabolism and hepatic toxicity of flutamide in cytochrome P450 1A2 knockout SV129 mice. J. Gastroenterol., 2006, 41(3), 231-239.
    • (2006) J. Gastroenterol , vol.41 , Issue.3 , pp. 231-239
    • Matsuzaki, Y.1    Nagai, D.2    Ichimura, E.3    Goda, R.4    Tomura, A.5    Doi, M.6    Nishikawa, K.7
  • 292
    • 0019955123 scopus 로고
    • In vivo activation of zoxazolamine metabolism by flavone
    • Lasker, J. M.; Huang, M. T.; Conney, A. H. In vivo activation of zoxazolamine metabolism by flavone. Science, 1982, 216(4553), 1419-1421.
    • (1982) Science , vol.216 , Issue.4553 , pp. 1419-1421
    • Lasker, J.M.1    Huang, M.T.2    Conney, A.H.3
  • 294
    • 0037838823 scopus 로고    scopus 로고
    • Intrinsic hepatic phenotype associated with the Cyp1a2 gene as shown by cDNA expression microarray analysis of the knockout mouse
    • Smith, A. G.; Davies, R.; Dalton, T. P.; Miller, M. L.; Judah, D.; Riley, J.; Gant, T.; Nebert, D. W. Intrinsic hepatic phenotype associated with the Cyp1a2 gene as shown by cDNA expression microarray analysis of the knockout mouse. EHP Toxicogenomics, 2003, 111(1T), 45-51.
    • (2003) EHP Toxicogenomics , vol.111 , Issue.1 T , pp. 45-51
    • Smith, A.G.1    Davies, R.2    Dalton, T.P.3    Miller, M.L.4    Judah, D.5    Riley, J.6    Gant, T.7    Nebert, D.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.