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Volumn , Issue , 2005, Pages 1-689

Cytochrome P450: Structure, mechanism, and biochemistry: Third edition

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EID: 84892292579     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/b139087     Document Type: Book
Times cited : (304)

References (250)
  • 14
    • 8044248685 scopus 로고
    • Rat hepatic cytochrome P-450: Comparative study of multiple isozymic forms
    • PR. Ortiz de Montellano ed., Plenum Press, New York, NY
    • Waxman, D. J. (1986). Rat hepatic cytochrome P-450: Comparative study of multiple isozymic forms. In PR. Ortiz de Montellano (ed.), Cytochrome P-450. Structure, Mechanism, and Biochemistry. Plenum Press, New York, NY, pp. 525-538.
    • (1986) Cytochrome P-450. Structure, Mechanism, and Biochemistry. , pp. 525-538
    • Waxman, D.J.1
  • 15
    • 0024236331 scopus 로고
    • The molecular biology of cytochrome P450s
    • Gonzalez, F. J. (1989). The molecular biology of cytochrome P450s. Pharmacol. Rev. 40, 243-288.
    • (1989) Pharmacol. Rev. , vol.40 , pp. 243-288
    • Gonzalez, F.J.1
  • 16
    • 0036227791 scopus 로고    scopus 로고
    • Update information on human P450s
    • Guengerich, F. P. (2002). Update information on human P450s. Drug Metab. Rev. 34, 7-15.
    • (2002) Drug Metab. Rev. , vol.34 , pp. 7-15
    • Guengerich, F.P.1
  • 17
    • 0027756106 scopus 로고
    • In vitro methods for assessing human hepatic drug metabolism: Their use in drug development
    • Wrighton, S. A., M. Van Den Branden, J. C. Stevens, L. A. Shipley, and B. J. Ring (1993). In vitro methods for assessing human hepatic drug metabolism: Their use in drug development. Drug Metab. Rev. 25, 453-484.
    • (1993) Drug Metab. Rev. , vol.25 , pp. 453-484
    • Wrighton, S.A.1    Van Den Branden, M.2    Stevens, J.C.3    Shipley, L.A.4    Ring, B.J.5
  • 18
    • 0028858960 scopus 로고
    • Cytochrome P450 inhibitors. Evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes
    • Newton, D. J., R. W. Wang, and A. Y. Lu (1995). Cytochrome P450 inhibitors. Evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes, Drug Metab. Dispos. 23, 154-158.
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 154-158
    • Newton, D.J.1    Wang, R.W.2    Lu, A.Y.3
  • 20
    • 0002888510 scopus 로고
    • Human cytochrome P450 enzymes
    • P. R. Ortiz de Montellano ed., Plenum Press, New York, NY
    • Guengerich, F. P. (1995). Human cytochrome P450 enzymes. In P. R. Ortiz de Montellano (ed.), Cytochrome P450: Structure, Mechanism and Biochemistry. Plenum Press, New York, NY, pp. 473-574.
    • (1995) Cytochrome P450: Structure, Mechanism and Biochemistry. , pp. 473-574
    • Guengerich, F.P.1
  • 21
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • P. R. Ortiz de Montellano ed., Plenum Press, New York, NY
    • Guengerich, F. P. (2004). Human cytochrome P450 enzymes. In, P. R. Ortiz de Montellano (ed.), Cytochrome P450: Structure, Mechanism and Biochemistry. Plenum Press, New York, NY, pp. 370-530.
    • (2004) Cytochrome P450: Structure, Mechanism and Biochemistry. , pp. 370-530
    • Guengerich, F.P.1
  • 22
    • 0030834058 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes: A status report summarizing their reactions, substrates, inducers, and inhibitors
    • Rendic, S. and F. J. Di Carlo (1997). Human cytochrome P450 enzymes: A status report summarizing their reactions, substrates, inducers, and inhibitors. Drug Metab. Rev. 29, 413-580.
    • (1997) Drug Metab. Rev. , vol.29 , pp. 413-580
    • Rendic, S.1    Di Carlo, F.J.2
  • 23
    • 0036223831 scopus 로고    scopus 로고
    • Summary of information on human CYP enzymes: Human P450 metabolism data
    • Rendic, S. (2002). Summary of information on human CYP enzymes: Human P450 metabolism data. Drug Metab. Rev. 34, 83-448.
    • (2002) Drug Metab. Rev. , vol.34 , pp. 83-448
    • Rendic, S.1
  • 24
    • 0038312064 scopus 로고    scopus 로고
    • Selectivities of human cytochrome P450 inhibitors toward rat P450 isoforms: Study with cDNA-expressed systems of the rat
    • Kobayashi, K., K. Urashima, N. Shimada, and K. Chiba (2003). Selectivities of human cytochrome P450 inhibitors toward rat P450 isoforms: Study with cDNA-expressed systems of the rat. Drug Metab. Dispos. 31, 833-836.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 833-836
    • Kobayashi, K.1    Urashima, K.2    Shimada, N.3    Chiba, K.4
  • 25
    • 0036497073 scopus 로고    scopus 로고
    • Substrate specificity for rat cytochrome P450 (CYP) isoforms: Screening with cDNA-expressed systems of the rat
    • Kobayashi, K., K. Urashima, N. Shimada, and K. Chiba (2002). Substrate specificity for rat cytochrome P450 (CYP) isoforms: Screening with cDNA-expressed systems of the rat. Biochem. Pharmacol. 63, 889-896.
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 889-896
    • Kobayashi, K.1    Urashima, K.2    Shimada, N.3    Chiba, K.4
  • 26
    • 0036893593 scopus 로고    scopus 로고
    • Evaluation of cytochrome P450 probe substrates commonly used by the pharmaceutical industry to study in vitro drug interactions
    • Yuan, R., S. Madani, X. X. Wei, K. Reynolds, and S. M. Huang (2002). Evaluation of cytochrome P450 probe substrates commonly used by the pharmaceutical industry to study in vitro drug interactions. Drug Metab. Dispos. 30, 1311-1319.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 1311-1319
    • Yuan, R.1    Madani, S.2    Wei, X.X.3    Reynolds, K.4    Huang, S.M.5
  • 27
    • 0031962621 scopus 로고    scopus 로고
    • Differential selectivity of cytochrome P450 inhibitors against probe substrates in human and rat liver microsomes
    • Eagling, V. A., J. F. Tjia, and D. J. Back (1998). Differential selectivity of cytochrome P450 inhibitors against probe substrates in human and rat liver microsomes. Br. J. Clin. Pharmacol. 45, 107-114.
    • (1998) Br. J. Clin. Pharmacol. , vol.45 , pp. 107-114
    • Eagling, V.A.1    Tjia, J.F.2    Back, D.J.3
  • 28
    • 0026537062 scopus 로고
    • Biotransformation of caffeine and theophylline in mammalian cell lines genetically engineered for expression of single cytochrome P450 isoforms
    • Fuhr, U, J. Doehmer, N. Battula, C. Wolfel, C. Kudla, Y. Keita et al. (1992). Biotransformation of caffeine and theophylline in mammalian cell lines genetically engineered for expression of single cytochrome P450 isoforms. Biochem. Pharmacol. 43, 225-235.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 225-235
    • Fuhr, U.1    Doehmer, J.2    Battula, N.3    Wolfel, C.4    Kudla, C.5    Keita, Y.6
  • 29
    • 0026906604 scopus 로고
    • Caffeine as a probe for human cytochromes P450: Validation using cDNA expression, immunoinhibition and microsomal kinetic and inhibitor techniques
    • Tassaneeyakul, W., Z. Mohamed, D. J. Birkett, M. E. McManus, M. E. Verones, R. H. Tukey et al. (1992). Caffeine as a probe for human cytochromes P450: Validation using cDNA expression, immunoinhibition and microsomal kinetic and inhibitor techniques. Pharmacogenetics 2, 173-183.
    • (1992) Pharmacogenetics , vol.2 , pp. 173-183
    • Tassaneeyakul, W.1    Mohamed, Z.2    Birkett, D.J.3    McManus, M.E.4    Verones, M.E.5    Tukey, R.H.6
  • 32
    • 0027380074 scopus 로고
    • Isoformselective mechanism-based inhibition of human cytochrome P450 1A2 by furafylline
    • Kunze, K. L. and W. F. Trager (1993). Isoformselective mechanism-based inhibition of human cytochrome P450 1A2 by furafylline. Chem. Res. Toxicol. 6, 649-656.
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 649-656
    • Kunze, K.L.1    Trager, W.F.2
  • 33
    • 0028362263 scopus 로고
    • Characterization of the inhibition of P4501A2 by furafylline
    • Clarke, S. E., A. D. Ayrton, and R. J. Chenery (1994). Characterization of the inhibition of P4501A2 by furafylline. Xenobiotica 24, 517-526.
    • (1994) Xenobiotica , vol.24 , pp. 517-526
    • Clarke, S.E.1    Ayrton, A.D.2    Chenery, R.J.3
  • 34
    • 0030094638 scopus 로고    scopus 로고
    • Theophylline metabolism in human liver microsomes: Inhibition studies
    • Tjia, J. F., J. Colbert, and D. J. Back (1996). Theophylline metabolism in human liver microsomes: Inhibition studies. J. Pharmacol. Exp. Ther. 276, 912-917.
    • (1996) J. Pharmacol. Exp. Ther. , vol.276 , pp. 912-917
    • Tjia, J.F.1    Colbert, J.2    Back, D.J.3
  • 35
    • 0024343858 scopus 로고
    • Human cytochrome P-450PIA (P450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines, Proc
    • Butler, M. N., M. Iwasaki, F. P. Guengerich, and F. K. Kadlubar (1989). Human cytochrome P-450PIA (P450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines, Proc. Natl. Acad. Sci. USA, 86, 7696-7700.
    • (1989) Natl. Acad. Sci. USA , vol.86 , pp. 7696-7700
    • Butler, M.N.1    Iwasaki, M.2    Guengerich, F.P.3    Kadlubar, F.K.4
  • 36
    • 0034687092 scopus 로고    scopus 로고
    • Rate-determining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants
    • Yun, C. H., G. P. Miller, and F. P. Guengerich (2000). Rate-determining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants. Biochemistry 39, 11319-11329.
    • (2000) Biochemistry , vol.39 , pp. 11319-11329
    • Yun, C.H.1    Miller, G.P.2    Guengerich, F.P.3
  • 37
    • 0031717524 scopus 로고    scopus 로고
    • Inhibitory monoclonal antibodies to human cytochrome P450 1A2: Analysis of phenacetin O-deethylation in human liver
    • Yang, T. J., Y. Sai, K. W. Krausz, F. J. Gonzalez, and H. V. Gelboin (1998). Inhibitory monoclonal antibodies to human cytochrome P450 1A2: Analysis of phenacetin O-deethylation in human liver. Pharmacogenetics 8, 375-382.
    • (1998) Pharmacogenetics , vol.8 , pp. 375-382
    • Yang, T.J.1    Sai, Y.2    Krausz, K.W.3    Gonzalez, F.J.4    Gelboin, H.V.5
  • 38
    • 0031785065 scopus 로고    scopus 로고
    • Comparative inhibition of human cytochrome P450 1A1 and 1A2 by flavonoids
    • Zhai, S., R. Dai, F. K. Friedman, and R. E. Vestal (1998). Comparative inhibition of human cytochrome P450 1A1 and 1A2 by flavonoids. Drug Metab. Dispos. 26, 989-992.
    • (1998) Drug Metab. Dispos. , vol.26 , pp. 989-992
    • Zhai, S.1    Dai, R.2    Friedman, F.K.3    Vestal, R.E.4
  • 39
    • 0032499398 scopus 로고    scopus 로고
    • Structure-related inhibition of human hepatic caffeine N3-demethylation by naturally occurring flavonoids
    • Lee, H., H. Yeom, Y. G. Kim, C. N. Yoon, C. Jin, J. S. Choi et al. (1998). Structure-related inhibition of human hepatic caffeine N3-demethylation by naturally occurring flavonoids. Biochem. Pharmacol. 55, 1369-1375.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1369-1375
    • Lee, H.1    Yeom, H.2    Kim, Y.G.3    Yoon, C.N.4    Jin, C.5    Choi, J.S.6
  • 40
    • 0028106482 scopus 로고
    • Cytochrome P450 specificities of alkoxyresorufin O-dealkylation in human and rat liver
    • Burke, M. D., S. Thompson, R. J. Weaver, C. R. Wolf, and R. T. Mayer (1994). Cytochrome P450 specificities of alkoxyresorufin O-dealkylation in human and rat liver. Biochem. Pharmacol. 48, 923-936.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 923-936
    • Burke, M.D.1    Thompson, S.2    Weaver, R.J.3    Wolf, C.R.4    Mayer, R.T.5
  • 41
    • 84892287817 scopus 로고
    • Induction of cytochromes P450IA1 and P450IA2 and measurement of catalytic activities
    • Rodrigues, A. D. and R. A. Prough (1992). Induction of cytochromes P450IA1 and P450IA2 and measurement of catalytic activities. Meth. Enzymol. 206, 423431.
    • (1992) Meth. Enzymol. , vol.206 , pp. 423431
    • Rodrigues, A.D.1    Prough, R.A.2
  • 42
    • 0025841777 scopus 로고
    • Purification and characterization of human liver microsomal cytochrome P-450 2A6
    • Yun, C. H., T. Shimada, and F. P. Guengerich (1991). Purification and characterization of human liver microsomal cytochrome P-450 2A6. Mol. Pharmacol. 40, 679-685.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 679-685
    • Yun, C.H.1    Shimada, T.2    Guengerich, F.P.3
  • 43
    • 0025022689 scopus 로고
    • The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes
    • Yamano, S., J. Tatsuno, and F. J. Gonzalez (1990). The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes. Biochemistry 29, 1322-1329.
    • (1990) Biochemistry , vol.29 , pp. 1322-1329
    • Yamano, S.1    Tatsuno, J.2    Gonzalez, F.J.3
  • 44
    • 0032812611 scopus 로고    scopus 로고
    • An inhibitory monoclonal antibody to human cytochrome P450 2A6 defines its role in the metabolism of coumarin, 7-ethoxycoumarin and 4-nitroanisole in human liver
    • Sai, Y., T. J. Yang, K. W. Krausz, F. J. Gonzalez, and H. V. Gelboin (1999). An inhibitory monoclonal antibody to human cytochrome P450 2A6 defines its role in the metabolism of coumarin, 7-ethoxycoumarin and 4-nitroanisole in human liver. Pharmacogenetics 9, 229-237.
    • (1999) Pharmacogenetics , vol.9 , pp. 229-237
    • Sai, Y.1    Yang, T.J.2    Krausz, K.W.3    Gonzalez, F.J.4    Gelboin, H.V.5
  • 45
    • 0035024678 scopus 로고    scopus 로고
    • Evaluation of methoxsalen, tranylcypromine, and tryptamine as specific and selective CYP2A6 inhibitors in vitro
    • Zhang, W., T. Kilicarslan, R. F. Tyndale, and E. M. Sellers (2001). Evaluation of methoxsalen, tranylcypromine, and tryptamine as specific and selective CYP2A6 inhibitors in vitro. Drug Metab. Dispos. 29, 897-902
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 897-902
    • Zhang, W.1    Kilicarslan, T.2    Tyndale, R.F.3    Sellers, E.M.4
  • 46
    • 0035119491 scopus 로고    scopus 로고
    • In vitro inhibition of cytochrome P450 enzymes in human liver microsomes by a potent CYP2A6 inhibitor, trans-2-phenylcyclopropylamine (Tranylcypromine), and its nonamine analog, cyclopropylbenzene
    • Taavitsainen, P., R. Juvonen, and O. Pelkonen (2001). In vitro inhibition of cytochrome P450 enzymes in human liver microsomes by a potent CYP2A6 inhibitor, trans-2-phenylcyclopropylamine (Tranylcypromine), and its nonamine analog, cyclopropylbenzene. Drug Metab. Dispos. 29, 217-222.
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 217-222
    • Taavitsainen, P.1    Juvonen, R.2    Pelkonen, O.3
  • 47
    • 0031149716 scopus 로고    scopus 로고
    • Inhibition of coumarin 7-hydroxylase activity in human liver microsomes
    • Draper, A. J., A. Madan, and A. Parkinson (1997). Inhibition of coumarin 7-hydroxylase activity in human liver microsomes. Arch. Biochem. Biophys. 341, 47-61.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 47-61
    • Draper, A.J.1    Madan, A.2    Parkinson, A.3
  • 48
    • 0031848620 scopus 로고    scopus 로고
    • (R) - (+) - Menthofuran is a potent, mechanism-based inactivator of human liver cytochrome P450 2A6
    • Khojasteh-Bakht, S. C., L. L. Koenigs, R. M. Peter, W. F. Trager, and S. D. Nelson (1998). (R) - (+) - Menthofuran is a potent, mechanism-based inactivator of human liver cytochrome P450 2A6. Drug Metab. Dispos. 26, 701-704.
    • (1998) Drug Metab. Dispos. , vol.26 , pp. 701-704
    • Khojasteh-Bakht, S.C.1    Koenigs, L.L.2    Peter, R.M.3    Trager, W.F.4    Nelson, S.D.5
  • 49
    • 0032516469 scopus 로고    scopus 로고
    • Mechanismbased inactivation of P450 2A6 by furanocoumarins
    • Koenigs, L. L. and W. F. Trager (1998). Mechanismbased inactivation of P450 2A6 by furanocoumarins. Biochemistry 37, 10047-10061.
    • (1998) Biochemistry , vol.37 , pp. 10047-10061
    • Koenigs, L.L.1    Trager, W.F.2
  • 50
    • 0029833258 scopus 로고    scopus 로고
    • Catalytic role of cytochrome P450 2B6 in N-demethylation of S-mephenytion
    • Heyn, H., R. B. White, and J. C. Stevens (1996). Catalytic role of cytochrome P450 2B6 in N-demethylation of S-mephenytion. Drug Metab. Dispos. 24, 948-954.
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 948-954
    • Heyn, H.1    White, R.B.2    Stevens, J.C.3
  • 51
    • 0036647214 scopus 로고    scopus 로고
    • New selective inhibitors of cytochromes P450 2B and their application to antimutagenesis of tamoxifen
    • Stiborova, M., L. Borek-Dohalska, P. Hodek, J. Mraz, and E. Frei (2002). New selective inhibitors of cytochromes P450 2B and their application to antimutagenesis of tamoxifen. Arch. Biochem. Biophys. 403, 41-49.
    • (2002) Arch. Biochem. Biophys. , vol.403 , pp. 41-49
    • Stiborova, M.1    Borek-Dohalska, L.2    Hodek, P.3    Mraz, J.4    Frei, E.5
  • 53
    • 0032811460 scopus 로고    scopus 로고
    • The role of CYP2B6 in human xenobiotic metabolism
    • Ekins, S. and S. A. Wrighton (1999). The role of CYP2B6 in human xenobiotic metabolism. Drug Metab. Rev. 31, 719-754.
    • (1999) Drug Metab. Rev. , vol.31 , pp. 719-754
    • Ekins, S.1    Wrighton, S.A.2
  • 54
    • 0036237885 scopus 로고    scopus 로고
    • Triethylenethiophosphoramide is a specific inhibitor of cytochrome P450 2B6: Implications for cyclophosphamide metabolism
    • Rae, J. M., N. V. Soukhova, D. A. Flockhart, and Z. Desta (2002). Triethylenethiophosphoramide is a specific inhibitor of cytochrome P450 2B6: Implications for cyclophosphamide metabolism. Drug Metab. Dispos. 30, 525-530.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 525-530
    • Rae, J.M.1    Soukhova, N.V.2    Flockhart, D.A.3    Desta, Z.4
  • 55
    • 0033810079 scopus 로고    scopus 로고
    • Validation of bupropion hydroxylation as a selective marker of human cytochrome P450 2B6 catalytic activity
    • Faucette, S. R., R. L. Hawke, E. L. Lecluyse, S. S. Shord, B. Yan, R. M. Laethem et al. (2000). Validation of bupropion hydroxylation as a selective marker of human cytochrome P450 2B6 catalytic activity. Drug Metab. Dispos. 28, 1222-1230.
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 1222-1230
    • Faucette, S.R.1    Hawke, R.L.2    Lecluyse, E.L.3    Shord, S.S.4    Yan, B.5    Laethem, R.M.6
  • 57
    • 0034791777 scopus 로고    scopus 로고
    • Polymorphisms in human CYP2C8 decrease metabolism of the anticancer drug paclitaxel and arachidonic acid
    • Dai, D., D. C. Zeldin, J. A. Blaisdell, B. Chanas, S. J. Coulter, B. I. Ghanayem et al. (2001). Polymorphisms in human CYP2C8 decrease metabolism of the anticancer drug paclitaxel and arachidonic acid, Pharmacogenetics 11, 597-607.
    • (2001) Pharmacogenetics , vol.11 , pp. 597-607
    • Dai, D.1    Zeldin, D.C.2    Blaisdell, J.A.3    Chanas, B.4    Coulter, S.J.5    Ghanayem, B.I.6
  • 58
    • 0027957132 scopus 로고
    • Metabolism of taxol by human hepatic microsomes and human liver slices: Participation of cytochrome P450 3A4 and an unknown P450 enzyme
    • Harris, J. W., A. Rahman, B. R. Kim, F. P. Guengerich, and J. Collins (1994). Metabolism of taxol by human hepatic microsomes and human liver slices: Participation of cytochrome P450 3A4 and an unknown P450 enzyme. Cancer Res. 54, 4026-4035.
    • (1994) Cancer Res. , vol.54 , pp. 4026-4035
    • Harris, J.W.1    Rahman, A.2    Kim, B.R.3    Guengerich, F.P.4    Collins, J.5
  • 59
    • 0028036727 scopus 로고
    • Selective biotransformation of taxol to 6 alpha-hydroxytaxol by human cytochrome P450 2C8
    • Rahman, A., K. R. Korzekwa, J. Grogan, F. J. Gonzalez, and J. W. Harris (1994). Selective biotransformation of taxol to 6 alpha-hydroxytaxol by human cytochrome P450 2C8. Cancer Res. 54, 5543-5546.
    • (1994) Cancer Res. , vol.54 , pp. 5543-5546
    • Rahman, A.1    Korzekwa, K.R.2    Grogan, J.3    Gonzalez, F.J.4    Harris, J.W.5
  • 60
    • 0036266778 scopus 로고    scopus 로고
    • Trimethoprim and sulfamethoxazole are selective inhibitors of CYP2C8 and CYP2C9, respectively
    • Wen, X., J. S. Wang, J. T. Backman, J. Laitila, and P. J. Neuvonen (2002). Trimethoprim and sulfamethoxazole are selective inhibitors of CYP2C8 and CYP2C9, respectively. Drug Metab. Dispos. 30, 631-635.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 631-635
    • Wen, X.1    Wang, J.S.2    Backman, J.T.3    Laitila, J.4    Neuvonen, P.J.5
  • 61
    • 0038193696 scopus 로고    scopus 로고
    • Involvement of CYP3A4, CYP2C8, and CYP2D6 in the metabolism of (R)- and (S)-methadone in vitro
    • Wang, J. S. and C. L. De Vane (2003). Involvement of CYP3A4, CYP2C8, and CYP2D6 in the metabolism of (R) - and (S)-methadone in vitro. Drug Metab. Dispos. 31, 742-747.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 742-747
    • Wang, J.S.1    De Vane, C.L.2
  • 62
    • 0033048695 scopus 로고    scopus 로고
    • Roles of human cytochrome P450s 2C9 and 3A4 in the metabolic activation of diclofenac
    • Tang, W, R. A. Stearns, R. W. Wang, S. H. Chiu, and T. A. Baillie (1999). Roles of human cytochrome P450s 2C9 and 3A4 in the metabolic activation of diclofenac. Chem. Res. Toxicol. 12, 192-199.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 192-199
    • Tang, W.1    Stearns, R.A.2    Wang, R.W.3    Chiu, S.H.4    Baillie, T.A.5
  • 63
    • 0027264432 scopus 로고
    • Cytochrome P450TB (CYP2C): A major monooxygenase catalyzing diclofenac 4'-hydroxylation in human liver
    • Leemann, T, C. Transon, and P. Dayer (1993). Cytochrome P450TB (CYP2C): A major monooxygenase catalyzing diclofenac 4'-hydroxylation in human liver. Life Sci. 52, 29-34.
    • (1993) Life Sci. , vol.52 , pp. 29-34
    • Leemann, T.1    Transon, C.2    Dayer, P.3
  • 64
    • 0026519541 scopus 로고
    • Hydroxylation of warfarin by human cDNA-expressed cytochrome P-450: A role for P-4502C9 in the etiology of (S)-warfarin-drug interactions
    • Rettie, A. E., K. R. Korzekwa, K. L. Kunze, R. F. Lawrence, A. C. Eddy, T. Aoyama et al. (1992). Hydroxylation of warfarin by human cDNA-expressed cytochrome P-450: A role for P-4502C9 in the etiology of (S)-warfarin-drug interactions. Chem. Res. Toxicol. 5, 54-59.
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 54-59
    • Rettie, A.E.1    Korzekwa, K.R.2    Kunze, K.L.3    Lawrence, R.F.4    Eddy, A.C.5    Aoyama, T.6
  • 65
    • 0035028935 scopus 로고    scopus 로고
    • Relative contributions of CYP2C9 and 2C19 to phenytoin 4-hydroxylation in vitro: Inhibition by sulfaphenazole, omeprazole, and ticlopidine
    • Giancarlo, G. M., K. Venkatakrishnan, B. W. Granda, L. L. Von Moltke, and D. J. Greenblatt (2001). Relative contributions of CYP2C9 and 2C19 to phenytoin 4-hydroxylation in vitro: Inhibition by sulfaphenazole, omeprazole, and ticlopidine. Eur. J. Clin. Pharmacol. 57, 31-36.
    • (2001) Eur. J. Clin. Pharmacol. , vol.57 , pp. 31-36
    • Giancarlo, G.M.1    Venkatakrishnan, K.2    Granda, B.W.3    Von Moltke, L.L.4    Greenblatt, D.J.5
  • 66
    • 0025014594 scopus 로고
    • Tolbutamide and mephenytoin hydroxylation by human cytochrome P450s in the CYP2C subfamily
    • Relling, M. V, T. Aoyama, F. J. Gonzalez, and U. A. Meyer (1989). Tolbutamide and mephenytoin hydroxylation by human cytochrome P450s in the CYP2C subfamily. J. Pharmacol. Exp. Ther. 252, 442-447.
    • (1989) J. Pharmacol. Exp. Ther. , vol.252 , pp. 442-447
    • Relling, M.V.1    Aoyama, T.2    Gonzalez, F.J.3    Meyer, U.A.4
  • 67
    • 0024354143 scopus 로고
    • Expression of a human liver cytochrome P-450 protein with tolbutamide hydroxylase activity in Saccharomyces cerevisiae
    • Brian, W. R., P. K. Srivastava, D. R. Umbenhauer, R. S. Lloyd, and F. P. Guengerich (1989). Expression of a human liver cytochrome P-450 protein with tolbutamide hydroxylase activity in Saccharomyces cerevisiae. Biochemistry 28, 4993-4999.
    • (1989) Biochemistry , vol.28 , pp. 4993-4999
    • Brian, W.R.1    Srivastava, P.K.2    Umbenhauer, D.R.3    Lloyd, R.S.4    Guengerich, F.P.5
  • 68
    • 0025916087 scopus 로고
    • Separation of human liver tolbutamine hydroxylase and (S)-mephenytoin 4'-hydroxylase cytochrome P-450 enzymes
    • Srivastava, P. K., C. H. Yun, P. H. Beaune, C. Ged, and F. P. Guengerich (1991). Separation of human liver tolbutamine hydroxylase and (S)-mephenytoin 4'-hydroxylase cytochrome P-450 enzymes. Mol. Pharmacol. 40, 69-79.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 69-79
    • Srivastava, P.K.1    Yun, C.H.2    Beaune, P.H.3    Ged, C.4    Guengerich, F.P.5
  • 69
    • 0029737485 scopus 로고    scopus 로고
    • Use of tolbutamide as a substrate probe for human hepatic cytochrome P450 2C9
    • Miners, J. O. and D. J. Birkett (1996). Use of tolbutamide as a substrate probe for human hepatic cytochrome P450 2C9. Meth. Enzymol. 272, 139-145.
    • (1996) Meth. Enzymol. , vol.272 , pp. 139-145
    • Miners, J.O.1    Birkett, D.J.2
  • 70
    • 0031856787 scopus 로고    scopus 로고
    • Characterization of CYP2C19 and CYP2C9 from human liver: Respective roles in microsomal tolbutamide, S-mephenytoin, and omeprazole hydroxylation
    • Lasker, J. M., M. R. Wester, E. Aramsombatdee, and J. L. Raucy (1998). Characterization of CYP2C19 and CYP2C9 from human liver: Respective roles in microsomal tolbutamide, S-mephenytoin, and omeprazole hydroxylation. Arch. Biochem. Biophys. 353, 16-24.
    • (1998) Arch. Biochem. Biophys. , vol.353 , pp. 16-24
    • Lasker, J.M.1    Wester, M.R.2    Aramsombatdee, E.3    Raucy, J.L.4
  • 71
    • 0028078626 scopus 로고
    • Thiophene derivatives as new mechanismbased inhibitors of cytochromes P450: Inactivation of yeast-expressed human liver P450 2C9 by tienilic acid
    • Lopez-Garcia, M. P., P. M. Dansette, and D. Mansuy (1993). Thiophene derivatives as new mechanismbased inhibitors of cytochromes P450: Inactivation of yeast-expressed human liver P450 2C9 by tienilic acid. Biochemistry 33, 166-175.
    • (1993) Biochemistry , vol.33 , pp. 166-175
    • Lopez-Garcia, M.P.1    Dansette, P.M.2    Mansuy, D.3
  • 72
    • 0027468338 scopus 로고
    • Human liver P450s expressed in yeast as tools for reactive metabolite formation studies: Oxidative activation of tienilic acid by P450 2C9 and P450 2C10
    • Lopez-Garcia, M. R, P. M. Dansette, P. Valadon, C. Amar, P. H. Beaune, F. P. Guengerich et al. (1993). Human liver P450s expressed in yeast as tools for reactive metabolite formation studies: Oxidative activation of tienilic acid by P450 2C9 and P450 2C10. Eur. J. Biochem. 213, 223-232.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 223-232
    • Lopez-Garcia, M.R.1    Dansette, P.M.2    Valadon, P.3    Amar, C.4    Beaune, P.H.5    Guengerich, F.P.6
  • 73
    • 0022574425 scopus 로고
    • Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction
    • Shimada, T., K. S. Misono, and F. P. Guengerich (1986). Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction. J. Biol. Chem. 261, 909-921.
    • (1986) J. Biol. Chem. , vol.261 , pp. 909-921
    • Shimada, T.1    Misono, K.S.2    Guengerich, F.P.3
  • 74
    • 0024439393 scopus 로고
    • Warfarin as a probe of cytochromes P450 function
    • Kaminsky, L. S. (1989). Warfarin as a probe of cytochromes P450 function. Drug Metab. Rev. 20, 479-487.
    • (1989) Drug Metab. Rev. , vol.20 , pp. 479-487
    • Kaminsky, L.S.1
  • 75
    • 0019741894 scopus 로고
    • Production and application of antibodies to rat liver cytochrome P-450
    • Kaminsky, L. S., M. J. Fasco, and F. P. Guengerich (1981). Production and application of antibodies to rat liver cytochrome P-450. Meth. Enzymol. 74, 262-272.
    • (1981) Meth. Enzymol. , vol.74 , pp. 262-272
    • Kaminsky, L.S.1    Fasco, M.J.2    Guengerich, F.P.3
  • 76
    • 0028858604 scopus 로고
    • Highly sensitive and specific high-performance liquid chromatographic analysis of 7-hydroxywarfarin, a marker for human cytochrome P-4502C9 activity
    • Lang, D. and R. Bocker (1995). Highly sensitive and specific high-performance liquid chromatographic analysis of 7-hydroxywarfarin, a marker for human cytochrome P-4502C9 activity. J. Chromatogr. Biomed. Appl. 672, 305-309.
    • (1995) J. Chromatogr. Biomed. Appl. , vol.672 , pp. 305-309
    • Lang, D.1    Bocker, R.2
  • 77
    • 0033564329 scopus 로고    scopus 로고
    • Comparison of the substrate specificities of human liver cytochrome P450s 2C9 and 2C18: Application to the design of a specific substrate of CYP 2C18
    • Minoletti, C., S. Dijols, P. M. Dansette, and D. Mansuy (1999). Comparison of the substrate specificities of human liver cytochrome P450s 2C9 and 2C18: Application to the design of a specific substrate of CYP 2C18. Biochemistry 38, 7828-7836.
    • (1999) Biochemistry , vol.38 , pp. 7828-7836
    • Minoletti, C.1    Dijols, S.2    Dansette, P.M.3    Mansuy, D.4
  • 78
    • 0035887069 scopus 로고    scopus 로고
    • Interaction of new sulfaphenazole derivatives with human liver cytochrome P450 2Cs: Structural determinants required for selective recognition by CYP 2C9 and for inhibition of human CYP 2Cs
    • Ha-Duong, N. T., C. Marques-Soares, S. Dijols, M. A. Sari, P. M. Dansette, and D. Mansuy Interaction of new sulfaphenazole derivatives with human liver cytochrome P450 2Cs: Structural determinants required for selective recognition by CYP 2C9 and for inhibition of human CYP 2Cs. Arch. Biochem. Biophys. 394, 189-200.
    • Arch. Biochem. Biophys. , vol.394 , pp. 189-200
    • Ha-Duong, N.T.1    Marques-Soares, C.2    Dijols, S.3    Sari, M.A.4    Dansette, P.M.5    Mansuy, D.6
  • 79
    • 0027445449 scopus 로고
    • Isolation and characterization of human liver cytochrome P450 2C19: Correlation between 2C19 and S-mephenytoin 4'-hydroxylation
    • Wrighton, S. A., J. C. Stevens, G. W. Becker, and M. Van Den Branden (1993). Isolation and characterization of human liver cytochrome P450 2C19: Correlation between 2C19 and S-mephenytoin 4'-hydroxylation. Arch. Biochem. Biophys. 306, 240-245.
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 240-245
    • Wrighton, S.A.1    Stevens, J.C.2    Becker, G.W.3    Van Den Branden, M.4
  • 81
    • 0036179579 scopus 로고    scopus 로고
    • (+)-N-3-Benzylnirvanol and (-)-N-3-benzyl-phenobarbital: New potent and selective in vitro inhibitors of CYP2C19
    • Suzuki, H., M. B. Kneller, R. L. Haining, and W. F. Trager, A. E. Rettie (2002). (+)-N-3-Benzylnirvanol and (-)-N-3-benzyl-phenobarbital: New potent and selective in vitro inhibitors of CYP2C19. Drug Metab. Dispos. 30, 235-239.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 235-239
    • Suzuki, H.1    Kneller, M.B.2    Haining, R.L.3    Trager, W.F.4    Rettie, A.E.5
  • 82
    • 0037369493 scopus 로고    scopus 로고
    • Verification of the selectivity of (+) N-3-benzylnirvanol as a CYP2C19 inhibitor
    • Walsky, R. L. and R. S. Obach (2003). Verification of the selectivity of (+) N-3-benzylnirvanol as a CYP2C19 inhibitor. Drug Metab. Dispos. 31, 343.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 343
    • Walsky, R.L.1    Obach, R.S.2
  • 84
    • 0035699870 scopus 로고    scopus 로고
    • Inhibition by ticlopidine and its derivatives of human liver cytochrome P450. Mechanism-based inactivation of CYP 2C19 by ticlopidine
    • Ha-Duong, N. T., S. Dijols, A. C. Macherey, P. M. Dansette, and D. Mansuy (2001). Inhibition by ticlopidine and its derivatives of human liver cytochrome P450. Mechanism-based inactivation of CYP 2C19 by ticlopidine. Adv. Exp. Med. Biol. 500, 145-148.
    • (2001) Adv. Exp. Med. Biol. , vol.500 , pp. 145-148
    • Ha-Duong, N.T.1    Dijols, S.2    Macherey, A.C.3    Dansette, P.M.4    Mansuy, D.5
  • 85
    • 0023154962 scopus 로고
    • Debrisoquine 4-hydroxylase: Characterization of a new P450 gene subfamily, regulation, chromosomal mapping, and molecular analysis of the DA rat polymorphism
    • Gonzalez, F. J., T. Matsunaga, K. Nagata, U. A. Meyer, D. W. Nebert, J. Pastewka et al. (1987). Debrisoquine 4-hydroxylase: Characterization of a new P450 gene subfamily, regulation, chromosomal mapping, and molecular analysis of the DA rat polymorphism. DNA 6, 149-161.
    • (1987) DNA , vol.6 , pp. 149-161
    • Gonzalez, F.J.1    Matsunaga, T.2    Nagata, K.3    Meyer, U.A.4    Nebert, D.W.5    Pastewka, J.6
  • 86
    • 0022980052 scopus 로고
    • Debrisoquine/sparteinetype polymorphism of drug oxidation. Purification and characterization of two functionally different human liver cytochrome P-450 isozymes involved in impaired hydroxylation of the prototype substrate bufuralol
    • Gut, J., T. Catin, P. Dayer, T. Kronbach, U. Zanger, and U. A. Meyer (1986). Debrisoquine/sparteinetype polymorphism of drug oxidation. Purification and characterization of two functionally different human liver cytochrome P-450 isozymes involved in impaired hydroxylation of the prototype substrate bufuralol. J. Biol. Chem. 261, 11734-11743.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11734-11743
    • Gut, J.1    Catin, T.2    Dayer, P.3    Kronbach, T.4    Zanger, U.5    Meyer, U.A.6
  • 87
    • 0026324040 scopus 로고
    • Bufuralol, dextromethorphan, and debrisoquine as prototype substrates for human P450IID6
    • Kronbach, T. (1991). Bufuralol, dextromethorphan, and debrisoquine as prototype substrates for human P450IID6. Meth. Enzymol. 206, 509-517.
    • (1991) Meth. Enzymol. , vol.206 , pp. 509-517
    • Kronbach, T.1
  • 88
    • 0021345446 scopus 로고
    • Competitive inhibition of sparteine oxidation in human liver by beta-adrenoceptor antagonists and other cardiovascular drugs
    • Otton, S. V., T. Inaba, and W. Kalow (1984). Competitive inhibition of sparteine oxidation in human liver by beta-adrenoceptor antagonists and other cardiovascular drugs. Life Sci. 34, 73-80.
    • (1984) Life Sci. , vol.34 , pp. 73-80
    • Otton, S.V.1    Inaba, T.2    Kalow, W.3
  • 89
    • 0037369622 scopus 로고    scopus 로고
    • Apparent mechanism-based inhibition of human CYP2D6 in vitro by paroxetine: Comparison with fluoxetine and quinidine
    • Bertelsen, K. M., K. Venkatakrishnan, L. L. Von Moltke, R. S. Obach, and D. J. Greenblatt (2003). Apparent mechanism-based inhibition of human CYP2D6 in vitro by paroxetine: Comparison with fluoxetine and quinidine. Drug Metab. Dispos. 31, 289-293.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 289-293
    • Bertelsen, K.M.1    Venkatakrishnan, K.2    Von Moltke, L.L.3    Obach, R.S.4    Greenblatt, D.J.5
  • 90
    • 0026568846 scopus 로고
    • The role of cytochrome P4502D6 in the metabolism of paroxetine by human liver microsomes
    • Bloomer, J. C., F. R. Woods, R. E. Haddock, M. S. Lennard, and G. T. Tucker (1992). The role of cytochrome P4502D6 in the metabolism of paroxetine by human liver microsomes. Br. J. Clin. Pharmacol. 33, 521-523.
    • (1992) Br. J. Clin. Pharmacol. , vol.33 , pp. 521-523
    • Bloomer, J.C.1    Woods, F.R.2    Haddock, R.E.3    Lennard, M.S.4    Tucker, G.T.5
  • 91
    • 0026576928 scopus 로고
    • Pharmacokinetics of the selective serotonin reuptake inhibitor paroxetine: Nonlinearity and relation to the sparteine oxidation polymorphism
    • Sindrup, S. H., K. Brosen, and L. F. Gram (1992). Pharmacokinetics of the selective serotonin reuptake inhibitor paroxetine: Nonlinearity and relation to the sparteine oxidation polymorphism. Clin. Pharmacol. Ther. 51, 288-295.
    • (1992) Clin. Pharmacol. Ther. , vol.51 , pp. 288-295
    • Sindrup, S.H.1    Brosen, K.2    Gram, L.F.3
  • 93
    • 0024557660 scopus 로고
    • Dextromethorphan O-demethylation in liver microsomes as a prototype reaction to monitor cytochrome P-450 dbl activity
    • Dayer, P., T. Leemann, and R. Striberni (1989). Dextromethorphan O-demethylation in liver microsomes as a prototype reaction to monitor cytochrome P-450 dbl activity. Clin. Pharmacol. Ther. 45, 34-40.
    • (1989) Clin. Pharmacol. Ther. , vol.45 , pp. 34-40
    • Dayer, P.1    Leemann, T.2    Striberni, R.3
  • 94
    • 0029774120 scopus 로고    scopus 로고
    • 14C]dextromethorphan as substrate
    • 14C]dextromethorphan as substrate. Meth. Enzymol. 272, 186-195.
    • (1996) Meth. Enzymol. , vol.272 , pp. 186-195
    • Rodrigues, A.D.1
  • 95
    • 0034998765 scopus 로고    scopus 로고
    • Mechanism-based inactivation of CYP2D6 by 5-fluoro-2-[4-[(2-phenyl-1 H-imidazol-5-yl) methyl]-l-piperazinyl]pyrimidine
    • Palamanda, J. R., C. N. Casciano, L. A. Norton, R. P. Clement, L. V. Favreau, C. Lin et al. (2001). Mechanism-based inactivation of CYP2D6 by 5-fluoro-2-[4-[(2-phenyl-1 H-imidazol-5-yl) methyl]-l-piperazinyl]pyrimidine. Drug Metab. Dispos. 29, 863-867.
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 863-867
    • Palamanda, J.R.1    Casciano, C.N.2    Norton, L.A.3    Clement, R.P.4    Favreau, L.V.5    Lin, C.6
  • 96
    • 0028918999 scopus 로고
    • Selectivity of cytochrome P4502E1 in chlorzoxazone 6-hydroxylation
    • Yamazaki, H., Z. Guo, and F. P. Guengerich (1995). Selectivity of cytochrome P4502E1 in chlorzoxazone 6-hydroxylation. Drug Metab. Dispos. 23, 438-440.
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 438-440
    • Yamazaki, H.1    Guo, Z.2    Guengerich, F.P.3
  • 98
    • 0025857783 scopus 로고
    • Erratum
    • Erratum in: Chem. Res. Toxicol. 4, 389, 1991.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 389
  • 99
    • 0022852729 scopus 로고
    • Inhibition of microsomal oxidation of ethanol by pyrazole and 4-methylpyrazole in vitro. Increased effectiveness after induction by pyrazole and 4-methylpyrazole
    • Feierman, D. E. and A. I. Cederbaum (1986). Inhibition of microsomal oxidation of ethanol by pyrazole and 4-methylpyrazole in vitro. Increased effectiveness after induction by pyrazole and 4-methylpyrazole. Biochem. J. 239, 671-677.
    • (1986) Biochem. J. , vol.239 , pp. 671-677
    • Feierman, D.E.1    Cederbaum, A.I.2
  • 100
    • 0026319304 scopus 로고
    • Induction, purification, and characterization of cytochrome P450IIE1
    • Yang, C. S., C. J. Patten, H. Ishizaki, and J. S. H. Yoo (1992). Induction, purification, and characterization of cytochrome P450IIE1. Meth. Enzymol. 206, 595-603.
    • (1992) Meth. Enzymol. , vol.206 , pp. 595-603
    • Yang, C.S.1    Patten, C.J.2    Ishizaki, H.3    Yoo, J.S.H.4
  • 101
    • 0027487006 scopus 로고
    • Validation of 4-nitrophenol as an in vitro substrate probe for human liver CYP2E1 using cDNA expression and microsomal kinetic techniques
    • Tassaneeyakul, W., M. E. Veronese, D. J. Birkett, F. J. Gonzalez, and J. O. Miners (1993). Validation of 4-nitrophenol as an in vitro substrate probe for human liver CYP2E1 using cDNA expression and microsomal kinetic techniques. Biochem. Pharmacol. 46, 1975-1981.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1975-1981
    • Tassaneeyakul, W.1    Veronese, M.E.2    Birkett, D.J.3    Gonzalez, F.J.4    Miners, J.O.5
  • 102
    • 0026035519 scopus 로고
    • Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects
    • Guengerich, F. P., D. H. Kim, and M. Iwasaki (1991). Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects. Chem. Res. Toxicol. 4, 168-179.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 168-179
    • Guengerich, F.P.1    Kim, D.H.2    Iwasaki, M.3
  • 103
    • 0032977948 scopus 로고    scopus 로고
    • Lack of singledose disulfiram effects on cytochrome P-450 2C 9, 2C 19, 2D6, and 3A4 activities: Evidence for specificity toward P-450 2E1
    • Kharasch, E. D., D. C. Hankins, C. Jubert, K. E. Thummel, and J. K. Taraday (1999). Lack of singledose disulfiram effects on cytochrome P-450 2C 9, 2C 19, 2D6, and 3A4 activities: Evidence for specificity toward P-450 2E1. Drug Metab. Dispos. 27, 717-723.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 717-723
    • Kharasch, E.D.1    Hankins, D.C.2    Jubert, C.3    Thummel, K.E.4    Taraday, J.K.5
  • 104
    • 0028174881 scopus 로고
    • Evaluation of triacetyloleandomycin, α-naphthoflavone and diethyldithiocarbamate as selective chemical probes for inhibition of human cytochromes P450
    • Chang, T. K. H., F. J. Gonzalez, and D. J. Waxman (1994). Evaluation of triacetyloleandomycin, α-naphthoflavone and diethyldithiocarbamate as selective chemical probes for inhibition of human cytochromes P450. Arch. Biochem. Biophys. 311, 437-442.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 437-442
    • Chang, T.K.H.1    Gonzalez, F.J.2    Waxman, D.J.3
  • 105
    • 0022975115 scopus 로고
    • Characterization of ethanol-inducible human liver N-nitrosodimethylamine demethylase
    • Wrighton, S. A., P. E. Thomas, D. T. Molowa, M. Haniu, J. E. Shively, S. L. Maines et al. (1986). Characterization of ethanol-inducible human liver N-nitrosodimethylamine demethylase. Biochemistry 25, 6731-6735.
    • (1986) Biochemistry , vol.25 , pp. 6731-6735
    • Wrighton, S.A.1    Thomas, P.E.2    Molowa, D.T.3    Haniu, M.4    Shively, J.E.5    Maines, S.L.6
  • 106
    • 0023877321 scopus 로고
    • Metabolism of N-nitrosodialkylamines by human liver microsomes
    • Yoo, J. S., F. P. Guengerich, and C. S. Yang (1988). Metabolism of N-nitrosodialkylamines by human liver microsomes. Cancer Res. 48, 1499-1504.
    • (1988) Cancer Res. , vol.48 , pp. 1499-1504
    • Yoo, J.S.1    Guengerich, F.P.2    Yang, C.S.3
  • 107
    • 0026744568 scopus 로고
    • Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N-nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes
    • Yamazaki, H., Y. Inui, C. H. Yun, M. Mimura, F. R. Guengerich, and T. Shimada (1992). Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N-nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes. Carcinogenesis 13, 1789-1794.
    • (1992) Carcinogenesis , vol.13 , pp. 1789-1794
    • Yamazaki, H.1    Inui, Y.2    Yun, C.H.3    Mimura, M.4    Guengerich, F.R.5    Shimada, T.6
  • 108
    • 0026691523 scopus 로고
    • Participation of rat liver cytochrome P450 2E1 in the activation of N-nitrosodimethylamine and N-nitrosodiethylamine to products genotoxic in an acetyltransferase-overexpressing Salmonella typhimurium strain (NM2009)
    • Yamazaki, H., Y. Oda, Y. Funae, S. Imaoka, Y. Inui, F. P. Guengerich et al. (1992). Participation of rat liver cytochrome P450 2E1 in the activation of N-nitrosodimethylamine and N-nitrosodiethylamine to products genotoxic in an acetyltransferase-overexpressing Salmonella typhimurium strain (NM2009). Carcinogenesis 13, 979-985.
    • (1992) Carcinogenesis , vol.13 , pp. 979-985
    • Yamazaki, H.1    Oda, Y.Y.F.2    Imaoka, S.3    Inui, Y.4    Guengerich, F.P.5
  • 109
    • 0023929834 scopus 로고
    • Human liver microsomal steroid metabolism: Identification of the major microsomal steroid hormone 6 beta-hydroxylase cytochrome P-450 enzyme
    • Waxman, D. J., C. Attisano, F. P. Guengerich, and D. P. Lapenson (1988). Human liver microsomal steroid metabolism: Identification of the major microsomal steroid hormone 6 beta-hydroxylase cytochrome P-450 enzyme. Arch. Biochem. Biophys. 263, 424-436.
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 424-436
    • Waxman, D.J.1    Attisano, C.2    Guengerich, F.P.3    Lapenson, D.P.4
  • 110
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillam, E. M., T. Baba, B. R. Kim, S. Ohmori, and F. P. Guengerich (1993). Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys. 305, 123-131.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 123-131
    • Gillam, E.M.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5
  • 111
    • 0025184340 scopus 로고
    • Mechanism-based inactivation of human liver cytochrome P-450 IIIA4 by gestodene
    • Guengerich, F. P. (1990). Mechanism-based inactivation of human liver cytochrome P-450 IIIA4 by gestodene. Chem. Res. Toxicol. 3, 363-371.
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 363-371
    • Guengerich, F.P.1
  • 112
    • 0022998708 scopus 로고
    • Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism
    • Guengerich, F. P., M. V. Martin, P. H. Beaune, P. Kremers, T. Wolff, and D. J. Waxman (1986). Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism. J. Biol. Chem. 261, 5051-5060.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5051-5060
    • Guengerich, F.P.1    Martin, M.V.2    Beaune, P.H.3    Kremers, P.4    Wolff, T.5    Waxman, D.J.6
  • 113
    • 0023858226 scopus 로고
    • Human P450PCN1: Sequence, chromosome localization, and direct evidence through cDNA expression that P450PCN1 is nifedipine oxidase
    • Gonzalez, F. J., B. J. Schmid, M. Umeno, O. W. Mcbride, J. P. Hardwick, U. A. Meyer et al. (1988). Human P450PCN1: Sequence, chromosome localization, and direct evidence through cDNA expression that P450PCN1 is nifedipine oxidase. DNA 7, 79-86.
    • (1988) DNA , vol.7 , pp. 79-86
    • Gonzalez, F.J.1    Schmid, B.J.2    Umeno, M.3    Mcbride, O.W.4    Hardwick, J.P.5    Meyer, U.A.6
  • 114
    • 0025860978 scopus 로고
    • Oxidation of dihydropyridine calcium channel blockers and analogues by human liver cytochrome P-450 II1A4
    • Guengerich, F. P, W. R. Brian, M. Iwasaki, M. A. Sari, C. Bäärnhielm, and P. Berntsson (1991). Oxidation of dihydropyridine calcium channel blockers and analogues by human liver cytochrome P-450 II1A4. J. Med. Chem. 34, 1838-1844.
    • (1991) J. Med. Chem. , vol.34 , pp. 1838-1844
    • Guengerich, F.P.1    Brian, W.R.2    Iwasaki, M.3    Sari, M.A.4    Bäärnhielm, C.5    Berntsson, P.6
  • 115
    • 0028568243 scopus 로고
    • Oral triazolam is potentially hazardous to patients receiving systemic antimycotics
    • Varhe, A., M. B. Klaus, T. Olkkola, and P. J. Neuvonen (1994). Oral triazolam is potentially hazardous to patients receiving systemic antimycotics. Clin. Pharmacol. Then 56, 601-607.
    • (1994) Clin. Pharmacol. Then , vol.56 , pp. 601-607
    • Varhe, A.1    Klaus, M.B.2    Olkkola, T.3    Neuvonen, P.J.4
  • 118
    • 0027253615 scopus 로고
    • Oxidation of acetaminophen to N-acetyl-p-aminobenzoquinone imine by human CYP3A4
    • Thummel, K. E., C. A. Lee, K. L. Kunze, S. D. Nelson, and J. T. Slattery (1993). Oxidation of acetaminophen to N-acetyl-p-aminobenzoquinone imine by human CYP3A4. Biochem. Pharmacol. 45, 1563-1569.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 1563-1569
    • Thummel, K.E.1    Lee, C.A.2    Kunze, K.L.3    Nelson, S.D.4    Slattery, J.T.5
  • 119
    • 0025670512 scopus 로고
    • Expression of human liver cytochrome P450 IIIA4 in yeast. A functional model for the hepatic enzyme
    • Renaud, J. P., C. Cullin, D. Pompon, P. Beaune, and D. Mansuy (1990). Expression of human liver cytochrome P450 IIIA4 in yeast. A functional model for the hepatic enzyme. Eur. J. Biochem. 194:889-896.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 889-896
    • Renaud, J.P.1    Cullin, C.2    Pompon, D.3    Beaune, P.4    Mansuy, D.5
  • 120
    • 0024373348 scopus 로고
    • Oxidation of midazolam and triazolam by human liver cytochrome P450IIIA4
    • Kronbach, T., D. Mathys, M. Umeno, F. J. Gonzalez, and U. A. Meyer (1989). Oxidation of midazolam and triazolam by human liver cytochrome P450IIIA4. Mol. Pharmacol. 36, 89-96.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 89-96
    • Kronbach, T.1    Mathys, D.2    Umeno, M.3    Gonzalez, F.J.4    Meyer, U.A.5
  • 121
    • 0028114619 scopus 로고
    • Use of midazolam as a human cytochrome P450 3A probe: I. In vitro-in vivo correlations in liver transplant patients
    • Thummel, K. E., D. D. Shen, T. D. Podoll, K. L. Kunze, W. F. Trager, P. S. Hartwell et al. (1994). Use of midazolam as a human cytochrome P450 3A probe: I. In vitro-in vivo correlations in liver transplant patients. J. Pharmacol. Exp. Ther. 271, 549-556.
    • (1994) J. Pharmacol. Exp. Ther. , vol.271 , pp. 549-556
    • Thummel, K.E.1    Shen, D.D.2    Podoll, T.D.3    Kunze, K.L.4    Trager, W.F.5    Hartwell, P.S.6
  • 122
    • 84892227407 scopus 로고    scopus 로고
    • Azamulin is superior to ketoconazole as a selective CYP3A inhibitor probe
    • Abstracts from the 11th North American 1SSX Meeting, Orlando, FL, USA, Oct. 27-Oct. 31, Abs. 355
    • Stresser, M. D., M. I. Broudy, S. S. Dehal, C. J. Patten, and C. L. Crespi (2002). Azamulin is superior to ketoconazole as a selective CYP3A inhibitor probe. Drug Metab. Rev. Abstracts from the 11th North American 1SSX Meeting, Orlando, FL, USA, Oct. 27-Oct. 31, Vol. 34, Abs. 355, p. 178.
    • (2002) Drug Metab. Rev. , vol.34 , pp. 178
    • Stresser, M.D.1    Broudy, M.I.2    Dehal, S.S.3    Patten, C.J.4    Crespi, C.L.5
  • 123
    • 0030582402 scopus 로고    scopus 로고
    • Identification of CYP3A4 as the principal enzyme catalyzing mifepristone (RU 486) oxidation in human liver microsomes
    • Jang, G. R., S. A. Wrighton, and L. Z. Benet (1996). Identification of CYP3A4 as the principal enzyme catalyzing mifepristone (RU 486) oxidation in human liver microsomes. Biochem. Pharmacol. 52, 753-761.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 753-761
    • Jang, G.R.1    Wrighton, S.A.2    Benet, L.Z.3
  • 124
    • 0033061072 scopus 로고    scopus 로고
    • Mechanism-based inactivation of cytochrome P-450-3A4 by mifepristone (RU486)
    • He, K., T. F. Woolf, and P. F. Hollenberg (1999). Mechanism-based inactivation of cytochrome P-450-3A4 by mifepristone (RU486). J. Pharmacol. Exp. Ther. 288, 791-797.
    • (1999) J. Pharmacol. Exp. Ther. , vol.288 , pp. 791-797
    • He, K.1    Woolf, T.F.2    Hollenberg, P.F.3
  • 125
    • 0036707616 scopus 로고    scopus 로고
    • Differential oxidation of mifepristone by cytochromes P450 3A4 and 3A5: Selective inactivation of P450 3A4
    • Khan, K. K., Y. Q. He, M. A. Correia, and J. R. Halpert (2002). Differential oxidation of mifepristone by cytochromes P450 3A4 and 3A5: Selective inactivation of P450 3A4. Drug Metab. Dispos. 30, 985-990.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 985-990
    • Khan, K.K.1    He, Y.Q.2    Correia, M.A.3    Halpert, J.R.4
  • 126
    • 0032773854 scopus 로고    scopus 로고
    • Diltiazem inhibition of cytochrome P-450 3A activity is due to metabolite intermediate complex formation
    • Jones, D. R., J. C. Gorski, M. A. Hamman, B. S. Mayhew, S. Rider, and S. D. Hall (1999). Diltiazem inhibition of cytochrome P-450 3A activity is due to metabolite intermediate complex formation. J. Pharmacol. Exp. Ther. 290, 1116-1125.
    • (1999) J. Pharmacol. Exp. Ther. , vol.290 , pp. 1116-1125
    • Jones, D.R.1    Gorski, J.C.2    Hamman, M.A.3    Mayhew, B.S.4    Rider, S.5    Hall, S.D.6
  • 127
    • 0025161416 scopus 로고
    • Studies on the expression and metabolic capabilities of human liver cytochrome P450IIIA5 (HLp3)
    • Wrighton, S. A., W. R. Brian, M. A. Sari, M. Iwasaki, F. P. Guengerich, J. L. Raucy et al. (1990). Studies on the expression and metabolic capabilities of human liver cytochrome P450IIIA5 (HLp3). Mol. Pharmacol. 38, 207-213.
    • (1990) Mol. Pharmacol. , vol.38 , pp. 207-213
    • Wrighton, S.A.1    Brian, W.R.2    Sari, M.A.3    Iwasaki, M.4    Guengerich, F.P.5    Raucy, J.L.6
  • 128
    • 0028912205 scopus 로고
    • Expression of cytochrome P450 3A5 in Escherichia coli: Effects of 5' modification, purification, spectral characterization, reconstitution conditions, and catalytic activities
    • Gillam, E. M., Z. Guo, Y. F. Ueng, H. Yamazaki, I. Cock, P. E. Reilly et al. (1995). Expression of cytochrome P450 3A5 in Escherichia coli: Effects of 5' modification, purification, spectral characterization, reconstitution conditions, and catalytic activities. Arch. Biochem. Biophys. 317, 374-384.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 374-384
    • Gillam, E.M.1    Guo, Z.2    Ueng, Y.F.3    Yamazaki, H.4    Cock, I.5    Reilly, P.E.6
  • 129
    • 85030134509 scopus 로고
    • Erratum
    • Erratum in: Arch. Biochem. Biophys. 318, 498, 1995.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 498
  • 130
    • 0028234586 scopus 로고
    • Regioselective biotransformation of midazolam by members of the human cytochrome P450 3A (CYP3A) subfamily
    • Gorski, J. C., S. D. Hall, D. R. Jones, M. Van Den Branden, and S. A. Wrighton (1994). Regioselective biotransformation of midazolam by members of the human cytochrome P450 3A (CYP3A) subfamily. Biochem. Pharmacol. 47, 1643-1653.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 1643-1653
    • Gorski, J.C.1    Hall, S.D.2    Jones, D.R.3    Vanden Branden, M.4    Wrighton, S.A.5
  • 131
    • 0032829243 scopus 로고    scopus 로고
    • Biotransformation of alprazolam by members of the human cytochrome P4503A subfamily
    • Gorski, J. C, D. R. Jones, M. A. Hamman, S. A. Wrighton, and S. D. Hall (1999). Biotransformation of alprazolam by members of the human cytochrome P4503A subfamily. Xenobiotica 29, 931-944.
    • (1999) Xenobiotica , vol.29 , pp. 931-944
    • Gorski, J.C.1    Jones, D.R.2    Hamman, M.A.3    Wrighton, S.A.4    Hall, S.D.5
  • 133
    • 0038101411 scopus 로고    scopus 로고
    • Identification of epitopes on cytochrome P450 3A4/5 recognized by monoclonal antibodies
    • Parimoo, B., V. M. Mishin, C. M. Busch, and P. E. Thomas (2003). Identification of epitopes on cytochrome P450 3A4/5 recognized by monoclonal antibodies. Arch. Biochem. Biophys. 414, 244-254.
    • (2003) Arch. Biochem. Biophys. , vol.414 , pp. 244-254
    • Parimoo, B.1    Mishin, V.M.2    Busch, C.M.3    Thomas, P.E.4
  • 134
    • 0023200455 scopus 로고
    • P-450 HFLa, a form of cytochrome P-450 purified from human fetal livers, is the 16 alpha-hydroxylase of dehydroepiandrosterone 3-sulfate
    • Kitada, M., T. Kamataki, K. Itahashi, T. Rikihisa, and Y. Kanakubo (1987). P-450 HFLa, a form of cytochrome P-450 purified from human fetal livers, is the 16 alpha-hydroxylase of dehydroepiandrosterone 3-sulfate. J. Biol. Chem. 262, 13534-13537.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13534-13537
    • Kitada, M.1    Kamataki, T.2    Itahashi, K.3    Rikihisa, T.4    Kanakubo, Y.5
  • 135
    • 0242276321 scopus 로고    scopus 로고
    • CYP3A4 and CYP3A7-mediated carbamazepine 10, 11-epoxidation are activated by differential endogenous steroids
    • Nakamura, H., N. Torimoto, I. Ishii, N. Ariyoshi, H. Nakasa, S. Ohmori et al. (2003). CYP3A4 and CYP3A7-mediated carbamazepine 10, 11-epoxidation are activated by differential endogenous steroids. Drug Metab. Dispos. 31, 432-438.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 432-438
    • Nakamura, H.1    Torimoto, N.2    Ishii, I.3    Ariyoshi, N.4    Nakasa, H.5    Ohmori, S.6
  • 136
    • 0031259757 scopus 로고    scopus 로고
    • Expression of cytochrome P450 3A7 in Escherichia coll. Effects of 5' modification and catalytic characterization of recombinant enzyme expressed in bicistronic format with NADPH-cytochrome P450 reductase
    • Gillam, E. M., R. M. Wunsch, Y. F. Ueng, T. Shimada, P. E. Reilly, T. Kamataki et al. (1997). Expression of cytochrome P450 3A7 in Escherichia coll. Effects of 5' modification and catalytic characterization of recombinant enzyme expressed in bicistronic format with NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 346, 81-90.
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 81-90
    • Gillam, E.M.1    Wunsch, R.M.2    Ueng, Y.F.3    Shimada, T.4    Reilly, P.E.5    Kamataki, T.6
  • 138
    • 0030297422 scopus 로고    scopus 로고
    • Identification of CYP4A11 as the major lauric acid omega-hydroxylase in human liver microsomes
    • Powell, P. K., I. Wolf, and J. M. Lasker (1996). Identification of CYP4A11 as the major lauric acid omega-hydroxylase in human liver microsomes. Arch. Biochem. Biophys. 335, 219-226.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 219-226
    • Powell, P.K.1    Wolf, I.2    Lasker, J.M.3
  • 139
    • 0028151666 scopus 로고
    • Lauric acid as a model substrate for the simultaneous determination of cytochrome P450 2E1 and 4A in hepatic microsomes
    • Clarke, S. E., S. J. Baldwin, J. C. Bloomer, A. D. Ayrton, R. S. Sozio, and R. J. Chenery (1994). Lauric acid as a model substrate for the simultaneous determination of cytochrome P450 2E1 and 4A in hepatic microsomes. Chem. Res. Toxicol. 7, 836-842.
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 836-842
    • Clarke, S.E.1    Baldwin, S.J.2    Bloomer, J.C.3    Ayrton, A.D.4    Sozio, R.S.5    Chenery, R.J.6
  • 140
    • 0029568002 scopus 로고
    • Validation of the (omega-1)-hydroxylation of lauric acid as an in vitro substrate probe for human liver CYP2E1
    • Amet, Y, F. Berthou, S. Baird, Y. Dreano, J. P. Bail, and J. F. Menez (1995). Validation of the (omega-1) - hydroxylation of lauric acid as an in vitro substrate probe for human liver CYP2E1. Biochem. Pharmacol. 50, 1775-1782.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 1775-1782
    • Amet, Y.1    Berthou, F.2    Baird, S.3    Dreano, Y.4    Bail, J.P.5    Menez, J.F.6
  • 141
    • 0037228554 scopus 로고    scopus 로고
    • Differential regulation of human CYP4A genes by peroxisome proliferators and dexamethasone
    • Savas, U., M. H. Hsu, and E. F. Johnson (2003). Differential regulation of human CYP4A genes by peroxisome proliferators and dexamethasone. Arch. Biochem. Biophys. 409, 212-220.
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 212-220
    • Savas, U.1    Hsu, M.H.2    Johnson, E.F.3
  • 142
    • 0008834287 scopus 로고    scopus 로고
    • 10-(imidazolyl)-decanoic acid (10-IDA) is a selective and potent inhibitor of CYP4A9/11
    • Abstracts from the 10th North American ISSX Meeting, Indianapolis, IN, USA, Vol. 32 Suppl. 2, Abs. 188
    • Oglivie, B. W., S. M. Otradovec, B. L. Paris, J. A. Scheinkoenig, P. W. Carrott, S. P. Loecker et al. (2000). 10-(imidazolyl)-decanoic acid (10-IDA) is a selective and potent inhibitor of CYP4A9/11. Drug. Metab. Rev. Abstracts from the 10th North American ISSX Meeting, Indianapolis, IN, USA, Vol. 32(Suppl. 2), Abs. 188, p. 230.
    • (2000) Drug. Metab. Rev. , pp. 230
    • Oglivie, B.W.1    Otradovec, S.M.2    Paris, B.L.3    Scheinkoenig, J.A.4    Carrott, P.W.5    Loecker, S.P.6
  • 144
    • 0031808169 scopus 로고    scopus 로고
    • Metabolism of arachidonic acid to 20-hydroxy-5, 8, 11, 14-eicosatetraenoic acid by P450 enzymes in human liver: Involvement of CYP4F2 and CYP4A11
    • Powell, P. K., I. Wolf, R. Jin, and J. M. Lasker (1998). Metabolism of arachidonic acid to 20-hydroxy-5, 8, 11, 14-eicosatetraenoic acid by P450 enzymes in human liver: Involvement of CYP4F2 and CYP4A11. J. Pharmacol. Exp. Ther. 285, 1327-1336.
    • (1998) J. Pharmacol. Exp. Ther. , vol.285 , pp. 1327-1336
    • Powell, P.K.1    Wolf, I.2    Jin, R.3    Lasker, J.M.4
  • 145
    • 0032213301 scopus 로고    scopus 로고
    • Role of human CYP4F2 in hepatic catabolism of the proinflammatory agent leukotriene B4
    • Jin, R., D. R. Koop, J. L. Raucy, and J. M. Asker (1998). Role of human CYP4F2 in hepatic catabolism of the proinflammatory agent leukotriene B4. Arch. Biochem. Biophys. 359, 89-98.
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 89-98
    • Jin, R.1    Koop, D.R.2    Raucy, J.L.3    Asker, J.M.4
  • 146
    • 0034660506 scopus 로고    scopus 로고
    • Promoter activity and regulation of the CYP4F2 leukotrieneB (4) omega-hydroxylase gene by peroxisomal proliferators and retinoic acid in HepG2 cells
    • Zhang, X., L. Chen, and J. P. Hardwick (2000). Promoter activity and regulation of the CYP4F2 leukotrieneB (4) omega-hydroxylase gene by peroxisomal proliferators and retinoic acid in HepG2 cells. Arch. Biochem. Biophys. 378, 364-376.
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 364-376
    • Zhang, X.1    Chen, L.2    Hardwick, J.P.3
  • 147
    • 0021150830 scopus 로고
    • Omega-oxidation is the major pathway for the catabolism of leukotriene B4 in human polymorphonuclear leukocytes
    • Shak, S. and I. Goldstein (1984). Omega-oxidation is the major pathway for the catabolism of leukotriene B4 in human polymorphonuclear leukocytes. J. Biol. Chem. 259, 10181-10187.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10181-10187
    • Shak, S.1    Goldstein, I.2
  • 148
    • 0034809149 scopus 로고    scopus 로고
    • CDNA cloning and expression of CYP4F12, a novel human cytochrome P450
    • Bylund, J., M. Bylund, and E. H. Oliw (2001). cDNA cloning and expression of CYP4F12, a novel human cytochrome P450. Biochem. Biophys. Res. Commun. 280, 892-897.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 892-897
    • Bylund, J.1    Bylund, M.2    Oliw, E.H.3
  • 150
    • 0033106423 scopus 로고    scopus 로고
    • Structure and chromosomal assignment of the sterol 12alpha-hydroxylase gene (CYP8B1) in human and mouse: Eukaryotic cytochrome P-450 gene devoid of introns
    • Gafvels, M., M. Olin, B. P. Chowdhary, T. Raudsepp, U. Andersson, B. Persson et al. (1999). Structure and chromosomal assignment of the sterol 12alpha-hydroxylase gene (CYP8B1) in human and mouse: Eukaryotic cytochrome P-450 gene devoid of introns. Genomics 56, 184-196.
    • (1999) Genomics , vol.56 , pp. 184-196
    • Gafvels, M.1    Olin, M.2    Chowdhary, B.P.3    Raudsepp, T.4    Andersson, U.5    Persson, B.6
  • 151
    • 0035064593 scopus 로고    scopus 로고
    • Mechanism-based inhibition of human cytochrome P450 1A1 by rhapontigenin
    • Chun, Y. J., S. Y. Ryu, T. C. Jeong, and M. Y. Kim (2001). Mechanism-based inhibition of human cytochrome P450 1A1 by rhapontigenin. Drug. Metab. Dispos. 29, 389-393.
    • (2001) Drug. Metab. Dispos. , vol.29 , pp. 389-393
    • Chun, Y.J.1    Ryu, S.Y.2    Jeong, T.C.3    Kim, M.Y.4
  • 152
    • 0020434524 scopus 로고
    • Purification and characterization of liver microsomal cytochromes P-450: Electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or beta-naphthoflavone
    • Guengerich, F. P., G. A. Dannan, S. T. Wright, M. V. Martin, and L. S. Kaminsky (1982). Purification and characterization of liver microsomal cytochromes P-450: Electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or beta-naphthoflavone. Biochemistry 21, 6019-6030.
    • (1982) Biochemistry , vol.21 , pp. 6019-6030
    • Guengerich, F.P.1    Dannan, G.A.2    Wright, S.T.3    Martin, M.V.4    Kaminsky, L.S.5
  • 153
    • 0025194581 scopus 로고
    • High affinity phenacetin O-deethylase is catalysed specifically by cytochrome P450d (P450IA2) in the liver of the rat
    • Sesardic, D., R. J. Edwards, D. S. Davies, R. E. Thomas, W. Levin, and A. R. Boobis (1990). High affinity phenacetin O-deethylase is catalysed specifically by cytochrome P450d (P450IA2) in the liver of the rat. Biochem. Pharmacol. 39, 489-498.
    • (1990) Biochem. Pharmacol. , vol.39 , pp. 489-498
    • Sesardic, D.1    Edwards, R.J.2    Davies, D.S.3    Thomas, R.E.4    Levin, W.5    Boobis, A.R.6
  • 154
    • 0027973024 scopus 로고
    • Theophylline N-demethylations as probes for P4501A1 and P4501A2
    • Sarkar, M. A. and B. J. Jackson (1994). Theophylline N-demethylations as probes for P4501A1 and P4501A2. Drug Metab. Dispos. 22, 827-834.
    • (1994) Drug Metab. Dispos. , vol.22 , pp. 827-834
    • Sarkar, M.A.1    Jackson, B.J.2
  • 155
    • 0035890772 scopus 로고    scopus 로고
    • A new selective and potent inhibitor of human cytochrome P450 1B1 and its application to antimutagenesis
    • Chun, Y. J., S. Kim, D. Kim, S. K. Lee, and F. P. Guengerich (2001). A new selective and potent inhibitor of human cytochrome P450 1B1 and its application to antimutagenesis. Cancer Res. 61, 8164-8170.
    • (2001) Cancer Res. , vol.61 , pp. 8164-8170
    • Chun, Y.J.1    Kim, S.2    Kim, D.3    Lee, S.K.4    Guengerich, F.P.5
  • 156
    • 0036172417 scopus 로고    scopus 로고
    • Erratum
    • Erratum in: Cancer Res. 62, 1232, 2002.
    • (2002) Cancer Res. , vol.62 , pp. 1232
  • 158
    • 0033815520 scopus 로고    scopus 로고
    • Roles of NADPH-P450 reductase in the O-deethylation of 7-ethoxycoumarin by recombinant human cytochrome P4501B1 variants in Escherichia coli
    • Shimada, X, F. Tsumura, E. M. Gillam, F. P. Guengerich, and K. Inoue (2000). Roles of NADPH-P450 reductase in the O-deethylation of 7-ethoxycoumarin by recombinant human cytochrome P4501B1 variants in Escherichia coli. Protein Expr. Purif. 20, 73-80.
    • (2000) Protein Expr. Purif. , vol.20 , pp. 73-80
    • Shimada, X.1    Tsumura, F.2    Gillam, E.M.3    Guengerich, F.P.4    Inoue, K.5
  • 159
    • 0033858044 scopus 로고    scopus 로고
    • Effect of chlorinated hydrocarbons on expression of cytochrome P450 1A 1, 1A2 and 1B1 and 2- and 4-hydroxylation of 17beta-estradiol in female Sprague-Dawley rats
    • Badawi, A. F., E. L. Cavalieri, and E. G. Rogan (2000). Effect of chlorinated hydrocarbons on expression of cytochrome P450 1A 1, 1A2 and 1B1 and 2- and 4-hydroxylation of 17beta-estradiol in female Sprague-Dawley rats. Carcinogenesis 21, 1593-1599.
    • (2000) Carcinogenesis , vol.21 , pp. 1593-1599
    • Badawi, A.F.1    Cavalieri, E.L.2    Rogan, E.G.3
  • 161
    • 0023442649 scopus 로고
    • Isozyme specificity of testosterone 7α-hydroxylation in rat hepatic microsomes: Is cytochrome P-450a the sole catalyst?
    • Levin, W., P. E. Thomas, D. E. Ryan, and A. W. Wood (1987). Isozyme specificity of testosterone 7α-hydroxylation in rat hepatic microsomes: Is cytochrome P-450a the sole catalyst? Arch. Biochem. Biophys. 258, 630-635.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 630-635
    • Levin, W.1    Thomas, P.E.2    Ryan, D.E.3    Wood, A.W.4
  • 162
    • 0020624336 scopus 로고
    • Regioselectivity and stereoselectivity of androgen hydroxylations catalyzed by cytochrome P-450 isozymes purified from phenobarbital-induced rat liver
    • Waxman, D. J., A. Ko, and C. Walsh (1983). Regioselectivity and stereoselectivity of androgen hydroxylations catalyzed by cytochrome P-450 isozymes purified from phenobarbital-induced rat liver. J. Biol. Chem. 258, 11937-11947.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11937-11947
    • Waxman, D.J.1    Ko, A.2    Walsh, C.3
  • 163
    • 0023837746 scopus 로고
    • Interactions of hepatic cytochromes P-450 with steroid hormones. Regioselectivity and stereoselectivity of steroid metabolism and hormonal regulation of rat P-450 enzyme expression
    • Waxman, D. J. (1988). Interactions of hepatic cytochromes P-450 with steroid hormones. Regioselectivity and stereoselectivity of steroid metabolism and hormonal regulation of rat P-450 enzyme expression. Biochem. Pharmacol. 37, 71-84.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 71-84
    • Waxman, D.J.1
  • 164
    • 0021112308 scopus 로고
    • 19 steroids by five highly purified and reconstituted rat hepatic cytochrome P450 isozymes
    • 19 steroids by five highly purified and reconstituted rat hepatic cytochrome P450 isozymes. J. Biol. Chem. 258, 8839-8847.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8839-8847
    • Wood, A.W.1    Ryan, D.R.2    Thomas, P.E.3    Levin, W.4
  • 165
    • 0026324283 scopus 로고
    • Measurement of steroid hydroxylation reactions by high-performance liquid chromatography as indicator of P450 identity and function
    • Arlotto, M. P., J. M. Trant, and R. W. Estabrook (1992). Measurement of steroid hydroxylation reactions by high-performance liquid chromatography as indicator of P450 identity and function. Meth. Enzymol. 206, 454-462.
    • (1992) Meth. Enzymol. , vol.206 , pp. 454-462
    • Arlotto, M.P.1    Trant, J.M.2    Estabrook, R.W.3
  • 166
    • 0026717011 scopus 로고
    • 12 alpha-hydroxytestosterone. A hitherto unidentified testosterone metabolite produced by cytochrome P-450 2A2
    • Smith, S. J., K. R. Korzekwa, T. Aoyama, F. J. Gonzalez, J. F. Darbyshire, K. Sugiyama et al. (1992). 12 alpha-hydroxytestosterone. A hitherto unidentified testosterone metabolite produced by cytochrome P-450 2A2. Drug Metab. Dispos. 20, 566-571.
    • (1992) Drug Metab. Dispos. , vol.20 , pp. 566-571
    • Smith, S.J.1    Korzekwa, K.R.2    Aoyama, T.3    Gonzalez, F.J.4    Darbyshire, J.F.5    Sugiyama, K.6
  • 167
    • 0024532593 scopus 로고
    • Secobarbital-mediated inactivation of rat liver cytochrome P-450b: A mechanistic reappraisal
    • Lunetta, J. M., K. Sugiyama, and M. A. Correia (1989). Secobarbital-mediated inactivation of rat liver cytochrome P-450b: A mechanistic reappraisal. Mol. Pharmacol. 35, 10-17.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 10-17
    • Lunetta, J.M.1    Sugiyama, K.2    Correia, M.A.3
  • 168
    • 0029862643 scopus 로고    scopus 로고
    • Identification of the heme adduct and an active site peptide modified during mechanism-based inactivation of rat liver cytochrome P450 2B1 by secobarbital
    • He, K., A. M. Falick, B. Chen, F. Nilsson, and M. A. Correia (1996). Identification of the heme adduct and an active site peptide modified during mechanism-based inactivation of rat liver cytochrome P450 2B1 by secobarbital. Chem. Res. Toxicol. 9, 614-622.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 614-622
    • He, K.1    Falick, A.M.2    Chen, B.3    Nilsson, F.4    Correia, M.A.5
  • 169
    • 0022350885 scopus 로고
    • Dealkylation of pentoxyresorufin: A rapid and sensitive assay for measuring induction of cytochrome (s) P-450 by phenobarbital and other xenobiotics in the rat
    • Lubet, R. A., R. T. Mayer, J. W. Cameron, R. W. Nims, M. D. Burke, T. Wolff et al. (1985). Dealkylation of pentoxyresorufin: A rapid and sensitive assay for measuring induction of cytochrome (s) P-450 by phenobarbital and other xenobiotics in the rat. Arch. Biochem. Biophys. 238, 43-48.
    • (1985) Arch. Biochem. Biophys. , vol.238 , pp. 43-48
    • Lubet, R.A.1    Mayer, R.T.2    Cameron, J.W.3    Nims, R.W.4    Burke, M.D.5    Wolff, T.6
  • 170
    • 0025214645 scopus 로고
    • Selective inactivation by chlorofluoroacetamides of the major phenobarbital-inducible form (s) of rat liver cytochrome P-450
    • Halpert, J., J. Y. Jaw, C. Balfour, and L. S. Kaminsky (1990). Selective inactivation by chlorofluoroacetamides of the major phenobarbital-inducible form (s) of rat liver cytochrome P-450. Drug Metab. Dispos. 18, 168-174.
    • (1990) Drug Metab. Dispos. , vol.18 , pp. 168-174
    • Halpert, J.1    Jaw, J.Y.2    Balfour, C.3    Kaminsky, L.S.4
  • 171
    • 0026726554 scopus 로고
    • Suicide inhibitors of cytochrome P450 1A1 and P450 2B1
    • Hopkins, N. E., M. K. Foroozesh, and W. L. Alworth (1992). Suicide inhibitors of cytochrome P450 1A1 and P450 2B1. Biochem. Pharmacol. 44, 787-796.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 787-796
    • Hopkins, N.E.1    Foroozesh, M.K.2    Alworth, W.L.3
  • 173
    • 0023643411 scopus 로고
    • Regioselective progesterone hydroxylation catalyzed by eleven rat hepatic cytochrome P-450 isozymes
    • Swinney, D. C., D. E. Ryan, P. E. Thomas, and W. Levin (1987). Regioselective progesterone hydroxylation catalyzed by eleven rat hepatic cytochrome P-450 isozymes. Biochemistry 26, 7073-7083.
    • (1987) Biochemistry , vol.26 , pp. 7073-7083
    • Swinney, D.C.1    Ryan, D.E.2    Thomas, P.E.3    Levin, W.4
  • 174
    • 0024548434 scopus 로고
    • Specific inactivation by 17β-substituted steroids of rabbit and rat liver cytochromes P-450 responsible for progesterone 21-hydroxylation
    • Halpert, J., J. Y. Jaw, and C. Balfour (1989). Specific inactivation by 17β-substituted steroids of rabbit and rat liver cytochromes P-450 responsible for progesterone 21-hydroxylation. Mol. Pharmacol. 34, 148-156.
    • (1989) Mol. Pharmacol. , vol.34 , pp. 148-156
    • Halpert, J.1    Jaw, J.Y.2    Balfour, C.3
  • 175
    • 0038312064 scopus 로고    scopus 로고
    • Selectivities of human cytochrome P450 inhibitors toward rat P450 isoforms: Study with cDNA-expressed systems of the rat
    • Kobayashi, K., K. Urashima, N. Shimada, and K. Chiba (2003). Selectivities of human cytochrome P450 inhibitors toward rat P450 isoforms: Study with cDNA-expressed systems of the rat. Drug Metab. Dispos. 31, 833-836.
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 833-836
    • Kobayashi, K.1    Urashima, K.2    Shimada, N.3    Chiba, K.4
  • 176
    • 0034869012 scopus 로고    scopus 로고
    • Mechanism-based inactivation of CYP2C11 by diclofenac
    • Masubuchi, Y., A. Ose, and T. Horie (2001). Mechanism-based inactivation of CYP2C11 by diclofenac. Drug Metab. Dispos. 29, 1190-1195.
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 1190-1195
    • Masubuchi, Y.1    Ose, A.2    Horie, T.3
  • 177
    • 0030992926 scopus 로고    scopus 로고
    • Cytochrome P4502C11 is a target of diclofenac covalent binding in rats
    • Shen, S., S. J. Hargus, B. M. Martin, and L. R. Pohl (1997). Cytochrome P4502C11 is a target of diclofenac covalent binding in rats. Chem. Res. Toxicol. 10, 420-423.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 420-423
    • Shen, S.1    Hargus, S.J.2    Martin, B.M.3    Pohl, L.R.4
  • 178
    • 0021719860 scopus 로고
    • Purification, characterization, and pituitary regulation of the sex-specific cytochrome P-450 15 beta-hydroxylase from liver microsomes of untreated female rats
    • MacGeoch, C., E. T. Morgan, J. Halpert, and J. A. Gustafsson (1984). Purification, characterization, and pituitary regulation of the sex-specific cytochrome P-450 15 beta-hydroxylase from liver microsomes of untreated female rats. J. Biol. Chem. 259, 15433-15439.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15433-15439
    • MacGeoch, C.1    Morgan, E.T.2    Halpert, J.3    Gustafsson, J.A.4
  • 179
    • 0031574143 scopus 로고    scopus 로고
    • Expression of four rat CYP2D isoforms in Saccharomyces cerevisiae and their catalytic specificity
    • Wan, J., S. Imaoka, T. Chow, T. Hiroi, Y. Yabusaki, and Y. Funae (1997). Expression of four rat CYP2D isoforms in Saccharomyces cerevisiae and their catalytic specificity. Arch. Biochem. Biophys. 348, 383-390.
    • (1997) Arch. Biochem. Biophys. , vol.348 , pp. 383-390
    • Wan, J.1    Imaoka, S.2    Chow, T.3    Hiroi, T.4    Yabusaki, Y.5    Funae, Y.6
  • 180
    • 0032911164 scopus 로고    scopus 로고
    • Developmental changes in the catalytic activity and expression of CYP2D isoforms in the rat liver
    • Chow, T., S. Imaoka, T. Hiroi, and Y. Funae (1999). Developmental changes in the catalytic activity and expression of CYP2D isoforms in the rat liver. Drug Metab. Dispos. 27, 188-192.
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 188-192
    • Chow, T.1    Imaoka, S.2    Hiroi, T.3    Funae, Y.4
  • 182
    • 0021236705 scopus 로고
    • Purification and characterization of the rat liver microsomal cytochrome P-450 involved in the 4-hydroxylation of debrisoquine, a prototype for genetic variation in oxidative drug metabolism
    • Larrey, D., L. M. Distlerath, G. A. Dannan, G. R. Wilkinson, and F. P. Guengerich (1984). Purification and characterization of the rat liver microsomal cytochrome P-450 involved in the 4-hydroxylation of debrisoquine, a prototype for genetic variation in oxidative drug metabolism. Biochemistry 23, 2787-2795.
    • (1984) Biochemistry , vol.23 , pp. 2787-2795
    • Larrey, D.1    Distlerath, L.M.2    Dannan, G.A.3    Wilkinson, G.R.4    Guengerich, F.P.5
  • 183
    • 0035165936 scopus 로고    scopus 로고
    • Chlorzoxazone: A probe drug the metabolism of which can be used to monitor one-point blood sampling in the carbon tetrachlorideintoxicated rat
    • Tanaka, E. (2001). Chlorzoxazone: A probe drug the metabolism of which can be used to monitor one-point blood sampling in the carbon tetrachlorideintoxicated rat. Hum. Exp. Toxicol. 20, 381-385.
    • (2001) Hum. Exp. Toxicol. , vol.20 , pp. 381-385
    • Tanaka, E.1
  • 184
    • 0034085366 scopus 로고    scopus 로고
    • Chlorzoxazone: A probe drug whose metabolism can be used to monitor toluene exposure in rats
    • Mizuno, D., E. Tanaka, K. Tanno, and S. Misawa (2000). Chlorzoxazone: A probe drug whose metabolism can be used to monitor toluene exposure in rats. Arch. Toxicol. 74, 139-144.
    • (2000) Arch. Toxicol. , vol.74 , pp. 139-144
    • Mizuno, D.1    Tanaka, E.2    Tanno, K.3    Misawa, S.4
  • 186
    • 0026652491 scopus 로고
    • Modulation of the levels of cytochromes P450 in rat liver and lung by dietary lipid
    • Yoo, J. S., T. J. Smith, S. M. Ning, M. J. Lee, R. E. Thomas, and C. S. Yang (1992). Modulation of the levels of cytochromes P450 in rat liver and lung by dietary lipid. Biochem. Pharmacol. 43, 2535-2542.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 2535-2542
    • Yoo, J.S.1    Smith, T.J.2    Ning, S.M.3    Lee, M.J.4    Thomas, R.E.5    Yang, C.S.6
  • 187
    • 0026691523 scopus 로고
    • Participation of rat liver cytochrome P450 2E1 in the activation of N-nitrosodimethylamine and N-nitrosodiethylamine to products genotoxic in an acetyltransferase-overexpressing Salmonella typhimurium strain (NM2009)
    • Yamazaki, H., Y. Oda, Y. Funae, S. Imaoka, Y. Inui, F. P. Guengerich et al. (1992). Participation of rat liver cytochrome P450 2E1 in the activation of N-nitrosodimethylamine and N-nitrosodiethylamine to products genotoxic in an acetyltransferase-overexpressing Salmonella typhimurium strain (NM2009). Carcinogenesis 13, 979-985.
    • (1992) Carcinogenesis , vol.13 , pp. 979-985
    • Yamazaki, H.1    Oda, Y.2    Funae, Y.3    Imaoka, S.4    Inui, Y.5    Guengerich, F.P.6
  • 189
    • 0030992920 scopus 로고    scopus 로고
    • Metabolism of the chemoprotective agent diallyl sulfide to glutathione conjugates in rats
    • Jin, L. and T. A. Baillie (1997). Metabolism of the chemoprotective agent diallyl sulfide to glutathione conjugates in rats. Chem. Res. Toxicol. 10, 318-327.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 318-327
    • Jin, L.1    Baillie, T.A.2
  • 190
    • 0034089655 scopus 로고    scopus 로고
    • Inactivation of hepatic CYP2E1 by an epoxide of diallyl sulfone
    • Premdas, P. D., R. J. Bowers, and P. G. Forkert (2000). Inactivation of hepatic CYP2E1 by an epoxide of diallyl sulfone. J. Pharmacol. Exp. Then 293, 1112-1120.
    • (2000) J. Pharmacol. Exp. Then , vol.293 , pp. 1112-1120
    • Premdas, P.D.1    Bowers, R.J.2    Forkert, P.G.3
  • 191
    • 0025209985 scopus 로고
    • Effect of phenethyl isothiocyanate on microsomal N-nitrosodimethylamine metabolism and other monooxygenase activities
    • Ishizaki, H., J. F. Brady, S. M. Ning, and C. S. Yang (1990). Effect of phenethyl isothiocyanate on microsomal N-nitrosodimethylamine metabolism and other monooxygenase activities. Xenobiotica 20, 255-264.
    • (1990) Xenobiotica , vol.20 , pp. 255-264
    • Ishizaki, H.1    Brady, J.F.2    Ning, S.M.3    Yang, C.S.4
  • 193
    • 0026577117 scopus 로고
    • Specifically designed thiosteroids as active site-directed probes for functional dissection of cytochrome P-450 3A isozymes
    • Underwood, M. C., J. R. Cashman, and M. A. Correia (1992). Specifically designed thiosteroids as active site-directed probes for functional dissection of cytochrome P-450 3A isozymes. Chem. Res. Toxicol. 5, 42-53.
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 42-53
    • Underwood, M.C.1    Cashman, J.R.2    Correia, M.A.3
  • 194
    • 0021800943 scopus 로고
    • Identification of the cytochrome P-450 induced by macrolide antibiotics in rat liver as the glucocorticoid responsive cytochrome P-450p
    • Wrighton, S. A., P. Maurel, E. G. Schuetz, P. B. Watkins, B. Young, and P. S. Guzelian (1985). Identification of the cytochrome P-450 induced by macrolide antibiotics in rat liver as the glucocorticoid responsive cytochrome P-450p. Biochemistry 24, 2171-2178.
    • (1985) Biochemistry , vol.24 , pp. 2171-2178
    • Wrighton, S.A.1    Maurel, P.2    Schuetz, E.G.3    Watkins, P.B.4    Young, B.5    Guzelian, P.S.6
  • 195
    • 0023024338 scopus 로고
    • Macrolide antibiotics inhibit the degradation of the glucocorticoid- responsive cytochrome P-450p in rat hepatocytes in vivo and in primary monolayer culture
    • Watkins, P. B., S. A. Wrighton, E. G. Schuetz, P. Maurel, and P. S. Guzelian (1986). Macrolide antibiotics inhibit the degradation of the glucocorticoid-responsive cytochrome P-450p in rat hepatocytes in vivo and in primary monolayer culture. J. Biol. Chem. 261, 6264-6271.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6264-6271
    • Watkins, P.B.1    Wrighton, S.A.2    Schuetz, E.G.3    Maurel, P.4    Guzelian, P.S.5
  • 196
    • 0033656861 scopus 로고    scopus 로고
    • Cytochrome P450 3A9 catalyzes the metabolism of progesterone and other steroid hormones
    • Wang, H., K. L. Napoli, and H. W. Strobel (2000). Cytochrome P450 3A9 catalyzes the metabolism of progesterone and other steroid hormones. Mol. Cell. Biochem. 213, 127-135.
    • (2000) Mol. Cell. Biochem. , vol.213 , pp. 127-135
    • Wang, H.1    Napoli, K.L.2    Strobel, H.W.3
  • 197
    • 0037229516 scopus 로고    scopus 로고
    • Rat liver CYP3A9: Structure-function relationships to its human liver orthologs: Site-directed mutagenesis to an efficient progesterone dihydroxylase
    • Xue, L., V. G. Zgoda, B. Arison, and M. A. Correia (2003). Rat liver CYP3A9: Structure-function relationships to its human liver orthologs: Site-directed mutagenesis to an efficient progesterone dihydroxylase. Arch. Biochem. Biophys. 409, 113-126.
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 113-126
    • Xue, L.1    Zgoda, V.G.2    Arison, B.3    Correia, M.A.4
  • 198
    • 0019949059 scopus 로고
    • Cytochrome P-450 induction by clofibrate: Purification and properties of a hepatic cytochrome P-450 relatively specific for the 12- and 11-hydroxylation of dodecanoic acid (lauric acid)
    • Gibson, G. G., T. C. Orton, and P. P. Tamburini (1982). Cytochrome P-450 induction by clofibrate: Purification and properties of a hepatic cytochrome P-450 relatively specific for the 12- and 11-hydroxylation of dodecanoic acid (lauric acid). Biochem. J. 203, 161-168.
    • (1982) Biochem. J. , vol.203 , pp. 161-168
    • Gibson, G.G.1    Orton, T.C.2    Tamburini, P.P.3
  • 199
    • 0024241108 scopus 로고
    • The catalytic site of rat hepatic lauric acid omega-hydroxylase. Protein versus prosthetic heme alkylation in the omega-hydroxylation of acetylenic fatty acids
    • CaJacob, C. A., W. K. Chan, E. Shepard, and P. R. Ortiz De Montellano (1988). The catalytic site of rat hepatic lauric acid omega-hydroxylase. Protein versus prosthetic heme alkylation in the omega-hydroxylation of acetylenic fatty acids. J. Biol. Chem. 263, 18640-18649.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18640-18649
    • Ca Jacob, C.A.1    Chan, W.K.2    Shepard, E.3    Ortiz De Montellano, P.R.4
  • 200
    • 0021345344 scopus 로고
    • Specific inactivation of hepatic fatty acid hydroxylases by acetylenic fatty acids
    • Ortiz De Montellano, P. R. and N. O. Reich (1984). Specific inactivation of hepatic fatty acid hydroxylases by acetylenic fatty acids. J. Biol. Chem. 259, 4136-1141.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4136-1141
    • Ortiz De Montellano, P.R.1    Reich, N.O.2
  • 201
    • 0026326790 scopus 로고
    • Reversed-phase highperformance liquid chromatography assay of cholesterol 7 alpha-hydroxylase
    • Chiang, J. Y (1991). Reversed-phase highperformance liquid chromatography assay of cholesterol 7 alpha-hydroxylase. Meth. Enzymol. 206, 483-491.
    • (1991) Meth. Enzymol. , vol.206 , pp. 483-491
    • Chiang, J.Y.1
  • 202
    • 0024401849 scopus 로고
    • Acetaminophen activation by human liver cytochromes P450IIE1 and P4501A2
    • Raucy, J. L., J. M. Lasker, C. S. Lieber, and M. Black (1989). Acetaminophen activation by human liver cytochromes P450IIE1 and P4501A2. Arch. Biochem. Biophys. 271, 270-283.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 270-283
    • Raucy, J.L.1    Lasker, J.M.2    Lieber, C.S.3    Black, M.4
  • 204
    • 0023706607 scopus 로고
    • Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: Simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography
    • Imaoka, S., K. Inoue, and Y. Funae (1988). Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: Simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography. Arch. Biochem. Biophys. 265, 159-170.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 159-170
    • Imaoka, S.1    Inoue, K.2    Funae, Y.3
  • 205
    • 0023552178 scopus 로고
    • Inactivation of multiple hepatic cytochrome P-450 isozymes in rats by allylisopropylacetamide: Mechanistic implications
    • Bornheim, L. M., M. C. Underwood, P. Caldera, A. E. Rettie, W. F. Trager, S. A. Wrighton et al. (1987). Inactivation of multiple hepatic cytochrome P-450 isozymes in rats by allylisopropylacetamide: Mechanistic implications. Mol. Pharmacol. 32, 299-308.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 299-308
    • Bornheim, L.M.1    Underwood, M.C.2    Caldera, P.3    Rettie, A.E.4    Trager, W.F.5    Wrighton, S.A.6
  • 206
    • 0011321904 scopus 로고
    • Genetic differences in the induction of monooxygenase activities by polycyclic aromatic compounds
    • J. B. Schenkman and D. Kupfer eds, Pergamon Press, New York, NY
    • Nebert, D. W (1982). Genetic differences in the induction of monooxygenase activities by polycyclic aromatic compounds. In J. B. Schenkman and D. Kupfer (eds), Hepatic Cytochrome P-450 Monooxygenase System. Pergamon Press, New York, NY, pp. 269-291.
    • (1982) Hepatic Cytochrome P-450 Monooxygenase System. , pp. 269-291
    • Nebert, D.W.1
  • 207
    • 0017831699 scopus 로고
    • Direct fluorometric methods for measuring mixedfunction oxidase activity
    • Prough, R. A., M. D. Burke, and R. T. Mayer (1978). Direct fluorometric methods for measuring mixedfunction oxidase activity. Meth. Enzymol. 52, 372-377.
    • (1978) Meth. Enzymol. , vol.52 , pp. 372-377
    • Prough, R.A.1    Burke, M.D.2    Mayer, R.T.3
  • 208
    • 0015838231 scopus 로고
    • Reduced diphosphopyridine nucleotide synergism of the reduced triphosphopyridine nucleotide dependent mixed function oxidase of hepatic microsomes. Role of the Type I drug binding site of cytochrome P-450
    • Correia, M. A. and G. J. Mannering (1973). Reduced diphosphopyridine nucleotide synergism of the reduced triphosphopyridine nucleotide dependent mixed function oxidase of hepatic microsomes. Role of the Type I drug binding site of cytochrome P-450. Mol. Pharmacol. 9, 470-485.
    • (1973) Mol. Pharmacol. , vol.9 , pp. 470-485
    • Correia, M.A.1    Mannering, G.J.2
  • 209
    • 0022913310 scopus 로고
    • Dissociation of cytochrome P-450 inactivation and induction
    • Ortiz De Montellano, P. R. and A. K. Costa (1986). Dissociation of cytochrome P-450 inactivation and induction. Arch. Biochem. Biophys. 251, 514-524.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 514-524
    • Ortiz De Montellano, P.R.1    Costa, A.K.2
  • 210
    • 0023898529 scopus 로고
    • In vivo inhibition of oxidative drug metabolism by, and acute toxicity of 1-aminobenzotriazole (ABT)
    • Mico, B. A., D. A. Federowicz, M. G. Ripple, and W. Kerns (1988). In vivo inhibition of oxidative drug metabolism by, and acute toxicity of 1-aminobenzotriazole (ABT). Biochem. Pharmacol. 37, 2515-2519.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 2515-2519
    • Mico, B.A.1    Federowicz, D.A.2    Ripple, M.G.3    Kerns, W.4
  • 211
    • 77957186623 scopus 로고
    • 1-Aminobenzotriazole-induced destruction of hepatic and renal cytochromes P450 in male Sprague-Dawley rats
    • Mugford, C. A., M. Mortillo, B. A. Mico, and J. B. Tarloff (1992). 1-Aminobenzotriazole-induced destruction of hepatic and renal cytochromes P450 in male Sprague-Dawley rats. Fundam. Appl. Toxicol. 19, 43-49.
    • (1992) Fundam. Appl. Toxicol. , vol.19 , pp. 43-49
    • Mugford, C.A.1    Mortillo, M.2    Mico, B.A.3    Tarloff, J.B.4
  • 212
    • 0029562838 scopus 로고
    • Effect of cimetidine on hepatic cytochrome P450: Evidence for formation of a metabolite-intermediate complex
    • Levine, M. and G. D. Bellward (1995). Effect of cimetidine on hepatic cytochrome P450: Evidence for formation of a metabolite-intermediate complex. Drug Metab. Dispos. 23, 1407-1411.
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 1407-1411
    • Levine, M.1    Bellward, G.D.2
  • 213
    • 0031885475 scopus 로고    scopus 로고
    • In vivo cimetidine inhibits hepatic CYP2C6 and CYP2C11 but not CYP1A1 in adult male rats
    • Levine, M., E. Y. Law, S. M. Bandiera, T. K. Chang, and G. D. Bellward (1998). In vivo cimetidine inhibits hepatic CYP2C6 and CYP2C11 but not CYP1A1 in adult male rats. J. Pharmacol. Exp. Ther. 284, 493-199.
    • (1998) J. Pharmacol. Exp. Ther. , vol.284 , pp. 493-199
    • Levine, M.1    Law, E.Y.2    Bandiera, S.M.3    Chang, T.K.4    Bellward, G.D.5
  • 215
    • 0023815132 scopus 로고
    • Ranitidine versus cimetidine. A comparison of their potential to cause clinically important drug interactions
    • Smith, S. R. and M. J. Kendall (1988). Ranitidine versus cimetidine. A comparison of their potential to cause clinically important drug interactions. Clin. Pharmacokinet. 15, 44-56.
    • (1988) Clin. Pharmacokinet. , vol.15 , pp. 44-56
    • Smith, S.R.1    Kendall, M.J.2
  • 216
    • 0023447289 scopus 로고
    • Degradation of rat hepatic cytochrome P-450 heme by 3, 5-dicarbethoxy-2, 6-dimethyl-4-ethyl-l, 4-dihydropyridine to irreversibly bound protein adducts
    • Correia, M. A., C. Decker, K. Sugiyama, P. Caldera, L. Bornheim, S. A. Wrighton et al. (1987). Degradation of rat hepatic cytochrome P-450 heme by 3, 5-dicarbethoxy-2, 6-dimethyl-4-ethyl-l, 4-dihydropyridine to irreversibly bound protein adducts. Arch. Biochem. Biophys. 258, 436-451.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 436-451
    • Correia, M.A.1    Decker, C.2    Sugiyama, K.3    Caldera, P.4    Bornheim, L.5    Wrighton, S.A.6
  • 217
    • 0018769008 scopus 로고
    • A class of strong inhibitors of microsomal monooxygenases: The ellipticines
    • Lesca, P., E. Rafidinarivo, P. Le Cointe, and D. Mansuy (1979). A class of strong inhibitors of microsomal monooxygenases: The ellipticines. Chem. Biol. Interact. 24, 189-198.
    • (1979) Chem. Biol. Interact. , vol.24 , pp. 189-198
    • Lesca, P.1    Rafidinarivo, E.2    Le Cointe, P.3    Mansuy, D.4
  • 219
    • 0036219021 scopus 로고    scopus 로고
    • Selective serotonin reuptake inhibitors and cytochrome P-450 mediated drug-drug interactions: An update
    • Hemeryck, A. and F. M. Belpaire (2002). Selective serotonin reuptake inhibitors and cytochrome P-450 mediated drug-drug interactions: An update. Curr. Drug. Metab. 3, 13-37.
    • (2002) Curr. Drug. Metab. , vol.3 , pp. 13-37
    • Hemeryck, A.1    Belpaire, F.M.2
  • 220
    • 0030867948 scopus 로고    scopus 로고
    • Pharmacokinetic drug interactions of new antidepressants: A review of the effects on the metabolism of other drugs
    • Richelson, E. (1997). Pharmacokinetic drug interactions of new antidepressants: A review of the effects on the metabolism of other drugs. Mayo Clin. Proc. 72, 835-847.
    • (1997) Mayo Clin. Proc. , vol.72 , pp. 835-847
    • Richelson, E.1
  • 222
    • 0032558386 scopus 로고    scopus 로고
    • Mechanismbased inactivation of cytochrome P450 2B1 by 8-methoxypsoralen and several other furanocoumarins
    • Koenigs, L. L. and W. F. Trager (1998). Mechanismbased inactivation of cytochrome P450 2B1 by 8-methoxypsoralen and several other furanocoumarins. Biochemistry 37, 13184-13193.
    • (1998) Biochemistry , vol.37 , pp. 13184-13193
    • Koenigs, L.L.1    Trager, W.F.2
  • 223
    • 0019835546 scopus 로고
    • Inhibitors of cytochrome P-450s and their mechanism of action
    • Testa, B. and P. Jenner (1981). Inhibitors of cytochrome P-450s and their mechanism of action. Drug Metab. Rev. 12, 1-117.
    • (1981) Drug Metab. Rev. , vol.12 , pp. 1-117
    • Testa, B.1    Jenner, P.2
  • 224
    • 0020530615 scopus 로고
    • Cytochrome P-450 isozyme 1 from phenobarbital-induced rat liver: Purification, characterization, and interactions with metyrapone and cytochrome b5
    • Waxman, D. J. and C. Walsh (1983). Cytochrome P-450 isozyme 1 from phenobarbital-induced rat liver: Purification, characterization, and interactions with metyrapone and cytochrome b5. Biochemistry 22, 4846-4855.
    • (1983) Biochemistry , vol.22 , pp. 4846-4855
    • Waxman, D.J.1    Walsh, C.2
  • 225
    • 0015511655 scopus 로고
    • Inhibition of hepatic oxidative xenobiotic metabolism by piperonyl butoxide
    • Franklin, M. R. (1972). Inhibition of hepatic oxidative xenobiotic metabolism by piperonyl butoxide. Biochem. Pharmacol. 21, 3287-3299.
    • (1972) Biochem. Pharmacol. , vol.21 , pp. 3287-3299
    • Franklin, M.R.1
  • 226
    • 0016238393 scopus 로고
    • Interaction of methylenedioxyphenyl (1, 3-benzodioxole) compounds with enzymes and their effects on mammals
    • Hodgson, E. and R. M. Philpot (1974). Interaction of methylenedioxyphenyl (1, 3-benzodioxole) compounds with enzymes and their effects on mammals. Drug. Metab. Rev. 3, 231-301.
    • (1974) Drug. Metab. Rev. , vol.3 , pp. 231-301
    • Hodgson, E.1    Philpot, R.M.2
  • 227
    • 0016325433 scopus 로고
    • The formation of complexes absorbing at 455 nm from cytochrome P-450 and metabolites of compounds related to SKF 525-A
    • Buening, M. K. and Franklin, M. R. (1974). The formation of complexes absorbing at 455 nm from cytochrome P-450 and metabolites of compounds related to SKF 525-A. Drug Metab. Dispos. 2, 386-390.
    • (1974) Drug Metab. Dispos. , vol.2 , pp. 386-390
    • Buening, M.K.1    Franklin, M.R.2
  • 228
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T. and R. Sato (1964). The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239, 2370-2378.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 229
    • 0000921783 scopus 로고
    • The spectrophotometric measurement of turbid suspensions of cytochromes associated with drug metabolism
    • C. F. Chignell ed., Appleton-Century-Crofts, New York, NY
    • Estabrook, R. W., J. A. Peterson, J. Baron, and A. G. Hildebrandt (1972). The spectrophotometric measurement of turbid suspensions of cytochromes associated with drug metabolism. In C. F. Chignell (ed.), Methods in Pharmacology, Vol. 2. Appleton-Century-Crofts, New York, NY, pp. 303-350.
    • (1972) Methods in Pharmacology , vol.2 , pp. 303-350
    • Estabrook, R.W.1    Peterson, J.A.2    Baron, J.3    Hildebrandt, A.G.4
  • 230
    • 0017168412 scopus 로고
    • Quantitative determination of cytochrome P-450 in rat liver homogenate
    • Matsubara, T., M. Koike, A. Touchi, Y. Tochino, and K. Sugeno (1976). Quantitative determination of cytochrome P-450 in rat liver homogenate, Anal. Biochem. 75, 596-603.
    • (1976) Anal. Biochem. , vol.75 , pp. 596-603
    • Matsubara, T.1    Koike, M.2    Touchi, A.3    Tochino, Y.4    Sugeno, K.5
  • 231
    • 0018405140 scopus 로고
    • Separation and characterization of highly purified forms of liver microsomal cytochrome P-450 from rats treated with polychlorinated biphenyls, phenobarbital, and 3-methylcholanthrene
    • Ryan, D. E., P. E. Thomas, D. Korzeniowski, and W. Levin (1979). Separation and characterization of highly purified forms of liver microsomal cytochrome P-450 from rats treated with polychlorinated biphenyls, phenobarbital, and 3-methylcholanthrene. J. Biol. Chem. 254, 1365-1374.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1365-1374
    • Ryan, D.E.1    Thomas, P.E.2    Korzeniowski, D.3    Levin, W.4
  • 232
    • 0021333633 scopus 로고
    • Characterization of three highly purified cytochromes P-450 from hepatic microsomes of adult male rats
    • Ryan, D. E., S. Iida, A. W. Wood, P. E. Thomas, C. S. Lieber, and W. Levin (1984). Characterization of three highly purified cytochromes P-450 from hepatic microsomes of adult male rats. J. Biol. Chem. 259, 1239-1250.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1239-1250
    • Ryan, D.E.1    Iida, S.2    Wood, A.W.3    Thomas, P.E.4    Lieber, C.S.5    Levin, W.6
  • 233
    • 0019161825 scopus 로고
    • Hepatic microsomal cytochrome P-450 from rats treated with isosafrole. Purification and characterization of four enzymic forms
    • Ryan, D. E., P. E. Thomas, and W. Levin (1980). Hepatic microsomal cytochrome P-450 from rats treated with isosafrole. Purification and characterization of four enzymic forms. J. Biol. Chem. 255, 7941-7955.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7941-7955
    • Ryan, D.E.1    Thomas, P.E.2    Levin, W.3
  • 234
    • 0017794351 scopus 로고
    • Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy
    • Jefcoate, C. R. (1978). Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy. Meth. Enzymol. 52, 258-279.
    • (1978) Meth. Enzymol. , vol.52 , pp. 258-279
    • Jefcoate, C.R.1
  • 235
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties
    • Omura, T. and R. Sato (1964). The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J. Biol. Chem. 239, 2379-2385.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 236
    • 0016729058 scopus 로고
    • Cumene hydroperoxidemediated formation of inhibited complexes of methylenedioxyphenyl compounds with cytochrome P450
    • Elcombe, C. R., J. Bridges, R. H. Nimmo-Smith, and J. Werringloer (1975). Cumene hydroperoxidemediated formation of inhibited complexes of methylenedioxyphenyl compounds with cytochrome P450. Biochem. Soc. Trans. 3, 967-970.
    • (1975) Biochem. Soc. Trans. , vol.3 , pp. 967-970
    • Elcombe, C.R.1    Bridges, J.2    Nimmo-Smith, R.H.3    Werringloer, J.4
  • 237
    • 0015310991 scopus 로고
    • The effect of piperonyl butoxide concentration on the formation of cytochrome P-450 difference spectra in hepatic microsomes from mice
    • Philpot, R. M. and E. Hodgson (1972). The effect of piperonyl butoxide concentration on the formation of cytochrome P-450 difference spectra in hepatic microsomes from mice. Mol. Pharmacol. 8, 204-214.
    • (1972) Mol. Pharmacol. , vol.8 , pp. 204-214
    • Philpot, R.M.1    Hodgson, E.2
  • 238
    • 0017717638 scopus 로고
    • Inhibition of mixed-function oxidations by substrates forming reduced cytochrome P-450 metabolic-intermediate complexes
    • Franklin, M. R. (1977). Inhibition of mixed-function oxidations by substrates forming reduced cytochrome P-450 metabolic-intermediate complexes. Pharmacol. Ther. A. 2, 227-245.
    • (1977) Pharmacol. Ther. A. , vol.2 , pp. 227-245
    • Franklin, M.R.1
  • 239
    • 0026346377 scopus 로고
    • Cytochrome P450 metabolic intermediate complexes from macrolide antibiotics and related compounds
    • Franklin, M. R. (1991). Cytochrome P450 metabolic intermediate complexes from macrolide antibiotics and related compounds. Meth. Enzymol. 206, 559-573.
    • (1991) Meth. Enzymol. , vol.206 , pp. 559-573
    • Franklin, M.R.1
  • 240
    • 0020632391 scopus 로고
    • Formation of inactive cytochrome P-450 Fe (II)-metabolite complexes with several erythromycin derivatives but not with josamycin and midecamycin in rats
    • Larrey, D., M. Tinel, and D. Pessayre (1983). Formation of inactive cytochrome P-450 Fe (II)-metabolite complexes with several erythromycin derivatives but not with josamycin and midecamycin in rats. Biochem. Pharmacol. 32, 1487-1493.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 1487-1493
    • Larrey, D.1    Tinel, M.2    Pessayre, D.3
  • 241
    • 0024271473 scopus 로고
    • In vivo and in vitro effects of a new macrolide antibiotic roxithromycin on rat liver cytochrome P-450: Comparison with troleandomycin and erythromycin
    • Delaforge, M., E. Sartori, and D. Mansuy (1988). In vivo and in vitro effects of a new macrolide antibiotic roxithromycin on rat liver cytochrome P-450: Comparison with troleandomycin and erythromycin. Chem. Biol. Interact. 68, 179-188.
    • (1988) Chem. Biol. Interact. , vol.68 , pp. 179-188
    • Delaforge, M.1    Sartori, E.2    Mansuy, D.3
  • 242
    • 0000756628 scopus 로고
    • The molar light absorption of pyridine ferroprotoporphyrin (Pyridine Haemochromogen)
    • Paul, K. G., H. Theorell, and A. Akeson (1953). The molar light absorption of pyridine ferroprotoporphyrin (Pyridine Haemochromogen). Acta. Chem. Scand. 7, 1284-1287.
    • (1953) Acta. Chem. Scand. , vol.7 , pp. 1284-1287
    • Paul, K.G.1    Theorell, H.2    Akeson, A.3
  • 243
    • 0017868128 scopus 로고
    • Spectral characterization of human hemoglobin and its derivatives
    • Waterman, M. R. (1978). Spectral characterization of human hemoglobin and its derivatives. Meth. Enzymol. 52, 456-463.
    • (1978) Meth. Enzymol. , vol.52 , pp. 456-463
    • Waterman, M.R.1
  • 244
    • 0001202995 scopus 로고
    • Pigments of rat liver microsomes
    • Klingenberg, M. (1958). Pigments of rat liver microsomes. Arch. Biochem. Biophys. 75, 376-386.
    • (1958) Arch. Biochem. Biophys. , vol.75 , pp. 376-386
    • Klingenberg, M.1
  • 247
    • 0002254766 scopus 로고
    • Analysis and characterization of enzymes
    • A. W. Hayes ed., Raven Press, Ltd., New York, NY
    • Guengerich, F. P. (1994). Analysis and characterization of enzymes. In A. W. Hayes (ed.), Principles and Methods of Toxicology. Raven Press, Ltd., New York, NY. pp. 1259-1313.
    • (1994) Principles and Methods of Toxicology. , pp. 1259-1313
    • Guengerich, F.P.1
  • 248
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterization, and kinetic studies
    • Phillips, A. H. and R. G. Langdon (1962). Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterization, and kinetic studies. J. Biol. Chem. 237, 2652-2660.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 249
    • 0017795019 scopus 로고
    • Purification and properties of NADPH-cytochrome P-450 reductase
    • Strobel, H. W and J. D. Dignam (1978). Purification and properties of NADPH-cytochrome P-450 reductase. Meth. Enzymol. 52, 89-96.
    • (1978) Meth. Enzymol. , vol.52 , pp. 89-96
    • Strobel, H.W.1    Dignam, J.D.2
  • 250
    • 0032497361 scopus 로고    scopus 로고
    • Structure-function relationships of human liver cytochromes P450 3A: Aflatoxin B1 metabolism as a probe
    • Wang, H., R. Dick, H. Yin, E. Licad-Coles, D. Kroetz, G. Szklarz et al. (1998). Structure-function relationships of human liver cytochromes P450 3A: Aflatoxin B1 metabolism as a probe. Biochemistry 37, 12536-12545.
    • (1998) Biochemistry , vol.37 , pp. 12536-12545
    • Wang, H.1    Dick, R.2    Yin, H.3    Licad-Coles, E.4    Kroetz, D.5    Szklarz, G.6


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