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Volumn 35, Issue 5, 1998, Pages 361-390

Inhibition and induction of cytochrome P450 and the clinical implications

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450;

EID: 0031794361     PISSN: 03125963     EISSN: None     Source Type: Journal    
DOI: 10.2165/00003088-199835050-00003     Document Type: Review
Times cited : (764)

References (192)
  • 1
    • 0025273823 scopus 로고
    • Enzymatic oxidation of xenobiotic chemicals
    • Guengerich FP. Enzymatic oxidation of xenobiotic chemicals. Crit Rev Biochem Mol Biol 1990; 25: 97-103
    • (1990) Crit Rev Biochem Mol Biol , vol.25 , pp. 97-103
    • Guengerich, F.P.1
  • 2
    • 0026651273 scopus 로고
    • Human cytochromes P450: Problems and prospects
    • Gonzalez FJ. Human cytochromes P450: problems and prospects. Trends Pharmacol Sci 1992; 13: 346-52
    • (1992) Trends Pharmacol Sci , vol.13 , pp. 346-352
    • Gonzalez, F.J.1
  • 3
    • 0002888510 scopus 로고
    • Human cytochrome P450 enzymes
    • Ortiz de Montellano PR, editor. [chapter 14]. 2nd ed. New York: Plenum Press
    • Guengerich FP. Human cytochrome P450 enzymes. In: Ortiz de Montellano PR, editor. Cytochrome P450: structure, mechanism, and biochemistry [chapter 14]. 2nd ed. New York: Plenum Press, 1995: 473-535
    • (1995) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 473-535
    • Guengerich, F.P.1
  • 4
    • 0030022629 scopus 로고    scopus 로고
    • An overview of current cytochrome P450 technology for assessing the safety and efficacy of new materials
    • Parkinson A. An overview of current cytochrome P450 technology for assessing the safety and efficacy of new materials. Toxicol Pathol 1996; 24: 45-57
    • (1996) Toxicol Pathol , vol.24 , pp. 45-57
    • Parkinson, A.1
  • 5
    • 0028832177 scopus 로고
    • Cytochrome P450 monooxygenases and interactions of psychotropic drugs: A five-year update
    • Shen WW. Cytochrome P450 monooxygenases and interactions of psychotropic drugs: a five-year update. Int J Psychiatry Med 1995; 25: 277-90
    • (1995) Int J Psychiatry Med , vol.25 , pp. 277-290
    • Shen, W.W.1
  • 6
    • 0028818646 scopus 로고
    • Antidepressant drug interactions and the cytochrome P450 system: A critical appraisal
    • Riesenman C. Antidepressant drug interactions and the cytochrome P450 system: a critical appraisal. Pharmacotherapy 1995; 15: 84S-99S
    • (1995) Pharmacotherapy , vol.15
    • Riesenman, C.1
  • 7
    • 0023248835 scopus 로고
    • Pharmacokinetic interactions of cimetidine 1987
    • Somogyi A, Muirhead M. Pharmacokinetic interactions of cimetidine 1987. Clin Pharmacokinet 1987; 12: 321-66
    • (1987) Clin Pharmacokinet , vol.12 , pp. 321-366
    • Somogyi, A.1    Muirhead, M.2
  • 8
    • 9044254525 scopus 로고    scopus 로고
    • P450 superfamily, update on new sequences, gene mapping, accession numbers and nomenclature
    • Nelson DR, Koymans L, Kamataki T, et al. P450 superfamily, update on new sequences, gene mapping, accession numbers and nomenclature. Pharmacogenetics 1996; 6: 1-42
    • (1996) Pharmacogenetics , vol.6 , pp. 1-42
    • Nelson, D.R.1    Koymans, L.2    Kamataki, T.3
  • 9
    • 0028237729 scopus 로고
    • Interindividual variations in human liver cytochrome P450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians
    • Shimada T, Yamazaki H, Mimura M, et al. Interindividual variations in human liver cytochrome P450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians. J Pharmacol Exp Ther 1994; 270: 414-23
    • (1994) J Pharmacol Exp Ther , vol.270 , pp. 414-423
    • Shimada, T.1    Yamazaki, H.2    Mimura, M.3
  • 10
    • 0025757011 scopus 로고
    • Comparison of levels of human microsomal cytochrome P450 enzymes and epoxide hydrolase in normal and disease states using immunochemical analysis of surgical samples
    • Guengerich FP, Turvy CG. Comparison of levels of human microsomal cytochrome P450 enzymes and epoxide hydrolase in normal and disease states using immunochemical analysis of surgical samples. J Pharmacol Exp Ther 1991; 256: 1189-94
    • (1991) J Pharmacol Exp Ther , vol.256 , pp. 1189-1194
    • Guengerich, F.P.1    Turvy, C.G.2
  • 11
    • 0023718998 scopus 로고
    • Characterization of cDNAs, mRNAs and proteins related to human liver microsomal cytochrome P450 (S)-mephenytoin 4′-hydroxylase
    • Ged C, Umbenhauer DR, Bellew TM, et al. Characterization of cDNAs, mRNAs and proteins related to human liver microsomal cytochrome P450 (S)-mephenytoin 4′-hydroxylase. Biochemistry 1988; 27: 6929-40
    • (1988) Biochemistry , vol.27 , pp. 6929-6940
    • Ged, C.1    Umbenhauer, D.R.2    Bellew, T.M.3
  • 12
    • 0025763625 scopus 로고
    • Cloning and expression of complementary DNAs for multiple numbers of the human cytochrome P450 II C subfamily
    • Romkes M, Faletto MB, Blaisdell JA, et al. Cloning and expression of complementary DNAs for multiple numbers of the human cytochrome P450 II C subfamily. Biochemistry 1991; 30: 3247-55
    • (1991) Biochemistry , vol.30 , pp. 3247-3255
    • Romkes, M.1    Faletto, M.B.2    Blaisdell, J.A.3
  • 13
    • 0002635197 scopus 로고
    • The genetic polymorphism of debrisoquine/sparteine metabolism: Molecular mechanisms
    • Kalow W, editor, New York: Pergamon Press
    • Meyer UA, Skoda RC, Zanger UM, et al. The genetic polymorphism of debrisoquine/sparteine metabolism: molecular mechanisms. In: Kalow W, editor, Pharmacogenetics of drug metabolism. New York: Pergamon Press, 1992: 609-23
    • (1992) Pharmacogenetics of Drug Metabolism , pp. 609-623
    • Meyer, U.A.1    Skoda, R.C.2    Zanger, U.M.3
  • 14
    • 0002100324 scopus 로고
    • Genetic polymorphism of S-mephenytoin hydroxylation
    • Kalow W, editor. New York: Pergamon Press
    • Wilkinson GR, Guengerich FP, Branch RA. Genetic polymorphism of S-mephenytoin hydroxylation. In: Kalow W, editor. Pharmacogenetics of drug metabolism. New York: Pergamon Press, 1992: 657-85
    • (1992) Pharmacogenetics of Drug Metabolism , pp. 657-685
    • Wilkinson, G.R.1    Guengerich, F.P.2    Branch, R.A.3
  • 15
    • 0028204887 scopus 로고
    • The molecular basis of genetic polymorphisms of drug metabolism
    • Meyer UA. The molecular basis of genetic polymorphisms of drug metabolism. J Pharm Pharmacol 1994; 46 Suppl, 1: 409-15
    • (1994) J Pharm Pharmacol , vol.46 , Issue.1 SUPPL. , pp. 409-415
    • Meyer, U.A.1
  • 16
    • 0025572192 scopus 로고
    • Hydroxylation polymorphisms of debrisoquine and mephenytoin in European populations
    • Alvan G, Bechtel P, Iselius L, et al. Hydroxylation polymorphisms of debrisoquine and mephenytoin in European populations. Eur J Clin Pharmacol 1990; 39: 533-7
    • (1990) Eur J Clin Pharmacol , vol.39 , pp. 533-537
    • Alvan, G.1    Bechtel, P.2    Iselius, L.3
  • 17
    • 0026506140 scopus 로고
    • Pronounced differences between native Chinese and Swedish populations in the polymorphic hydroxylations of debrisoquin and S-mephenytoin
    • Bertilsson L, Lou YQ, Du YL, et al. Pronounced differences between native Chinese and Swedish populations in the polymorphic hydroxylations of debrisoquin and S-mephenytoin. Clin Pharmacol Ther 1992; 51: 388-97
    • (1992) Clin Pharmacol Ther , vol.51 , pp. 388-397
    • Bertilsson, L.1    Lou, Y.Q.2    Du, Y.L.3
  • 18
    • 0027136288 scopus 로고
    • Inherited amplification of an active gene in the cytochrome P450 CYP2D locus as a cause of ultrarapid metabolism of debrisoquine
    • Johansson I, Lundqvist E, Bertilsson L, et al. Inherited amplification of an active gene in the cytochrome P450 CYP2D locus as a cause of ultrarapid metabolism of debrisoquine. Proc Natl Acad Sci USA 1993; 90: 11825-9
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11825-11829
    • Johansson, I.1    Lundqvist, E.2    Bertilsson, L.3
  • 19
    • 0029064096 scopus 로고
    • Ultrarapid hydroxylation of debrisoquine in a Swedish population: Analysis of the molecular genetic basis
    • Dahl M-L, Johansson I, Bertilsson L, et al. Ultrarapid hydroxylation of debrisoquine in a Swedish population: analysis of the molecular genetic basis. J Pharmacol Exp Ther 1995; 274: 516-20
    • (1995) J Pharmacol Exp Ther , vol.274 , pp. 516-520
    • Dahl, M.-L.1    Johansson, I.2    Bertilsson, L.3
  • 20
    • 0030432585 scopus 로고
    • Frequent distribution of ultrarapid metabolizers of debrisoquine in an Ethiopian population carrying duplicated and multiduplicated functional CYP2D6 alleles
    • Aklillu E, Persson I, Bertilsson L, et al. Frequent distribution of ultrarapid metabolizers of debrisoquine in an Ethiopian population carrying duplicated and multiduplicated functional CYP2D6 alleles. J Pharmacol Exp Ther 1995; 278: 441-6
    • (1995) J Pharmacol Exp Ther , vol.278 , pp. 441-446
    • Aklillu, E.1    Persson, I.2    Bertilsson, L.3
  • 21
    • 0028348860 scopus 로고
    • Interethnic factors affecting drug response
    • Testa B, Meyer UA, editors. New York: Academic Press
    • Kalow W, Bertilsson L. Interethnic factors affecting drug response. In: Testa B, Meyer UA, editors. Advantages in drug research. New York: Academic Press, 1994: 1-53
    • (1994) Advantages in Drug Research , pp. 1-53
    • Kalow, W.1    Bertilsson, L.2
  • 22
    • 0024442372 scopus 로고
    • Metoprolol and mephenytoin oxidation in far eastern oriental subjects. Japanese versus mainland Chinese
    • Horai Y, Nakano M, Ishizaki T, et al. Metoprolol and mephenytoin oxidation in far eastern oriental subjects. Japanese versus mainland Chinese. Clin Pharmacol Ther 1989; 46: 198-207
    • (1989) Clin Pharmacol Ther , vol.46 , pp. 198-207
    • Horai, Y.1    Nakano, M.2    Ishizaki, T.3
  • 23
    • 0027954308 scopus 로고
    • Catalytic selectivity of human cytochrome P450 enzymes: Relevance to drug metabolism and toxicity
    • Guengerich FP. Catalytic selectivity of human cytochrome P450 enzymes: relevance to drug metabolism and toxicity. Toxicol Lett 1994; 70: 133-8
    • (1994) Toxicol Lett , vol.70 , pp. 133-138
    • Guengerich, F.P.1
  • 24
    • 0343772220 scopus 로고
    • Human cytochrome P450 enzymes and chemical carcinogenesis
    • Jeffery EH, editor. Boca Rato (FL): CRC Press
    • Guengerich FP, Shimada T. Human cytochrome P450 enzymes and chemical carcinogenesis. In: Jeffery EH, editor. Human drug metabolism: from molecular biology to man. Boca Rato (FL): CRC Press, 1992: 5-12
    • (1992) Human Drug Metabolism: From Molecular Biology to Man , pp. 5-12
    • Guengerich, F.P.1    Shimada, T.2
  • 25
    • 0006423804 scopus 로고    scopus 로고
    • Cytochrome P450: From a single protein to a family of proteins - With some personal reflections
    • Ioannides CI, editor. Boca Raton: CRC Press
    • Estabrook RW. Cytochrome P450: from a single protein to a family of proteins - with some personal reflections. In: Ioannides CI, editor. Cytochromes P450: metabolic and toxicologixal aspects. Boca Raton: CRC Press, 1996: 3-28
    • (1996) Cytochromes P450: Metabolic and Toxicologixal Aspects , pp. 3-28
    • Estabrook, R.W.1
  • 26
    • 0342834498 scopus 로고
    • Inhibitors of cytochrome P450 and possibilities for their therapeutic application
    • Ruckpauland K, Rein H, editors. [chapter 3]. Berlin: Akademie Verlag
    • Correia MA, Oritz de Montellano PR. Inhibitors of cytochrome P450 and possibilities for their therapeutic application. In: Ruckpauland K, Rein H, editors. Medicinal implications in cytochrome P450 catalyzed biotransformations [chapter 3]. Berlin: Akademie Verlag, 1993: 74-146
    • (1993) Medicinal Implications in Cytochrome P450 Catalyzed Biotransformations , pp. 74-146
    • Correia, M.A.1    Oritz De Montellano, P.R.2
  • 28
    • 0028989491 scopus 로고
    • Structural basis of selective cytochrome P450 inhibition
    • Halpert JR. Structural basis of selective cytochrome P450 inhibition. Ann Pharmacol Toxicol 1995; 35: 29-53
    • (1995) Ann Pharmacol Toxicol , vol.35 , pp. 29-53
    • Halpert, J.R.1
  • 29
    • 0016169576 scopus 로고
    • Structure-activity relationships in the effects of 1-alkylimidazoles on microsomal oxidation in vitro and in vivo
    • Wilkinson CF, Hetnarski K, Cantwell GP, et al. Structure-activity relationships in the effects of 1-alkylimidazoles on microsomal oxidation in vitro and in vivo. Biochem Pharmacol 1974; 23: 2377-86
    • (1974) Biochem Pharmacol , vol.23 , pp. 2377-2386
    • Wilkinson, C.F.1    Hetnarski, K.2    Cantwell, G.P.3
  • 30
    • 0017687255 scopus 로고
    • Steric factors in the inhibitory interactions of imidazoles with microsomal enzymes
    • Rogerson TD, Wilkinson CF, Hetnarski K. Steric factors in the inhibitory interactions of imidazoles with microsomal enzymes. Biochem Pharmacol 1977; 26: 1039-42
    • (1977) Biochem Pharmacol , vol.26 , pp. 1039-1042
    • Rogerson, T.D.1    Wilkinson, C.F.2    Hetnarski, K.3
  • 31
    • 0018949006 scopus 로고
    • The effect of cimetidine on in vitro and in vivo microsomal drug metabolism in the rat
    • Pelkonen O, Puurunen J. The effect of cimetidine on in vitro and in vivo microsomal drug metabolism in the rat. Biochem Pharmacol 1980; 29: 3075-80
    • (1980) Biochem Pharmacol , vol.29 , pp. 3075-3080
    • Pelkonen, O.1    Puurunen, J.2
  • 32
    • 0000148048 scopus 로고
    • Comparative effects of imidazole antifungals on liver monooxygenases
    • Gascon MP, Oestreicher-Kondo M, Dayer P. Comparative effects of imidazole antifungals on liver monooxygenases [abstract]. Clin Pharmacol Ther 1991; 49: 158
    • (1991) Clin Pharmacol Ther , vol.49 , pp. 158
    • Gascon, M.P.1    Oestreicher-Kondo, M.2    Dayer, P.3
  • 33
    • 0027317764 scopus 로고
    • The discovery of fluconazole
    • Richardson K. The discovery of fluconazole. Drug News Perspect 1993; 6: 299-303
    • (1993) Drug News Perspect , vol.6 , pp. 299-303
    • Richardson, K.1
  • 34
    • 0015953888 scopus 로고
    • Influence of pyridine and some pyridine derivatives on spectral properties of reduced microsomes and on microsomal drug metabolizing activity
    • Jonen HG, Hüthwohl B, Kahl R, et al. Influence of pyridine and some pyridine derivatives on spectral properties of reduced microsomes and on microsomal drug metabolizing activity. Biochem Pharmacol 1974; 23: 1319-29
    • (1974) Biochem Pharmacol , vol.23 , pp. 1319-1329
    • Jonen, H.G.1    Hüthwohl, B.2    Kahl, R.3
  • 35
    • 0342399214 scopus 로고
    • Mechanism of inhibition of adrenal steroid 11-beta-hydroxylase by metyrapone (metopirone)
    • Dominguez OV, Samuels LT. Mechanism of inhibition of adrenal steroid 11-beta-hydroxylase by metyrapone (metopirone). Endocrinology 1963; 73: 304-9
    • (1963) Endocrinology , vol.73 , pp. 304-309
    • Dominguez, O.V.1    Samuels, L.T.2
  • 36
    • 0014722772 scopus 로고
    • Inhibitors of adrenal steroid biosynthesis
    • Temple TE, Liddle GW. Inhibitors of adrenal steroid biosynthesis. Annu Rev Pharmacol 1970; 10: 199-218
    • (1970) Annu Rev Pharmacol , vol.10 , pp. 199-218
    • Temple, T.E.1    Liddle, G.W.2
  • 37
    • 0343940711 scopus 로고    scopus 로고
    • Study of potential pharmacokinetic interaction between indinavir and clarithromycin
    • Winchell GA, McCrea JB, Tomasko L, et al. Study of potential pharmacokinetic interaction between indinavir and clarithromycin. Pharm Res 1996; 13 Suppl.: S434
    • (1996) Pharm Res , vol.13 , Issue.SUPPL.
    • Winchell, G.A.1    McCrea, J.B.2    Tomasko, L.3
  • 38
    • 0018769008 scopus 로고
    • A class of strong inhibitors of microsomal monooxygenases; the ellipticines
    • Lesca P, Rafidinarivo P, Lecointe P, et al. A class of strong inhibitors of microsomal monooxygenases; the ellipticines. Chem Biol Interact 1979; 24: 189-98
    • (1979) Chem Biol Interact , vol.24 , pp. 189-198
    • Lesca, P.1    Rafidinarivo, P.2    Lecointe, P.3
  • 39
    • 0025606337 scopus 로고
    • Species variation in the response of cytochrome P450-dependent monooxygenase system to inducers and inhibitors
    • Boobis AR, Sesardic D, Murray BP, et al. Species variation in the response of cytochrome P450-dependent monooxygenase system to inducers and inhibitors. Xenobiotics 1990; 20: 1139-61
    • (1990) Xenobiotics , vol.20 , pp. 1139-1161
    • Boobis, A.R.1    Sesardic, D.2    Murray, B.P.3
  • 40
    • 0021131521 scopus 로고
    • In vitro effects of quinoline derivatives on cytochrome P450 and aminopyrine N-demethylase activity in rat hepatic microsomes
    • Murray M. In vitro effects of quinoline derivatives on cytochrome P450 and aminopyrine N-demethylase activity in rat hepatic microsomes. Biochem Pharmacol 1984; 33: 3277-81
    • (1984) Biochem Pharmacol , vol.33 , pp. 3277-3281
    • Murray, M.1
  • 41
    • 0022515427 scopus 로고
    • Mechanistic aspects of the inhibition of microsomal drug oxidation by primaquine
    • Murray M, Farrell GC. Mechanistic aspects of the inhibition of microsomal drug oxidation by primaquine. Biochem Pharmacol 1986; 35: 2149-55
    • (1986) Biochem Pharmacol , vol.35 , pp. 2149-2155
    • Murray, M.1    Farrell, G.C.2
  • 42
    • 0021962359 scopus 로고
    • Effect of mefloquine on hepatic drug metabolism in the rat: Comparative study with primaquine
    • Riviere JH, Back DJ. Effect of mefloquine on hepatic drug metabolism in the rat: comparative study with primaquine. Biochem Pharmacol 1985; 34: 567-71
    • (1985) Biochem Pharmacol , vol.34 , pp. 567-571
    • Riviere, J.H.1    Back, D.J.2
  • 43
    • 0016766586 scopus 로고
    • Studies on the interaction of safrole with rat hepatic microsomes
    • Elcombe CR, Bridges JW, Gray TJB, et al. Studies on the interaction of safrole with rat hepatic microsomes. Biochem Pharmacol 1975; 24: 1427-33
    • (1975) Biochem Pharmacol , vol.24 , pp. 1427-1433
    • Elcombe, C.R.1    Bridges, J.W.2    Gray, T.J.B.3
  • 44
    • 0018415353 scopus 로고
    • Further studies on the dissociation of the isosafrole metabolite-cytochrome P450 complex
    • Dickins M, Elcombe CR, Moloney SJ, et al. Further studies on the dissociation of the isosafrole metabolite-cytochrome P450 complex. Biochem Pharmacol 1979; 28: 231-8
    • (1979) Biochem Pharmacol , vol.28 , pp. 231-238
    • Dickins, M.1    Elcombe, C.R.2    Moloney, S.J.3
  • 45
    • 0015568634 scopus 로고
    • Formation and binding of carbanions by cytochrome P450 of liver microsomes
    • Ullrich V, Schnabel KH. Formation and binding of carbanions by cytochrome P450 of liver microsomes. Drug Metab Dispos 1973; 1: 176-83
    • (1973) Drug Metab Dispos , vol.1 , pp. 176-183
    • Ullrich, V.1    Schnabel, K.H.2
  • 46
    • 0021850255 scopus 로고
    • Selective inhibitory interactions of alkoxymethylenedioxybenzenes towards monooxygenase activity in rat hepatic microsomes
    • Murray M, Hetnarski K, Wilkinson CF. Selective inhibitory interactions of alkoxymethylenedioxybenzenes towards monooxygenase activity in rat hepatic microsomes. Xenobiotics 1985; 15: 369-7
    • (1985) Xenobiotics , vol.15 , pp. 369-377
    • Murray, M.1    Hetnarski, K.2    Wilkinson, C.F.3
  • 47
    • 0017717638 scopus 로고
    • Inhibition of mixed-function oxidations by substrates forming reduced cytochrome P450 metabolic-intermediate-complexes
    • Franklin MR. Inhibition of mixed-function oxidations by substrates forming reduced cytochrome P450 metabolic-intermediate-complexes. Pharmacol Ther 1977; 2: 227-45
    • (1977) Pharmacol Ther , vol.2 , pp. 227-245
    • Franklin, M.R.1
  • 48
    • 0016729058 scopus 로고
    • Cumene hydroperoxide-mediated formation of inhibited complexes of methylenedioxyphenyl compounds with cytochrome P450
    • Elcombe CR, Bridges JW, Nimmo-Smith RH, et al. Cumene hydroperoxide-mediated formation of inhibited complexes of methylenedioxyphenyl compounds with cytochrome P450. Biochem Soc Trans 1975; 3: 967-70
    • (1975) Biochem Soc Trans , vol.3 , pp. 967-970
    • Elcombe, C.R.1    Bridges, J.W.2    Nimmo-Smith, R.H.3
  • 49
    • 0018864384 scopus 로고
    • Generation of carbon monoxide during the microsomal metabolism of methylene-dioxyphenyl compounds
    • Yu LS, Wilkinson CF, Anders MW. Generation of carbon monoxide during the microsomal metabolism of methylene-dioxyphenyl compounds. Biochem Pharmacol 1980; 29: 1113-22
    • (1980) Biochem Pharmacol , vol.29 , pp. 1113-1122
    • Yu, L.S.1    Wilkinson, C.F.2    Anders, M.W.3
  • 50
    • 0016238393 scopus 로고
    • Interaction of methylenedioxyphenyl (1,3-benzodixole) compounds with enzymes and their effects on mammals
    • Hodgson E, Philpot RM. Interaction of methylenedioxyphenyl (1,3-benzodixole) compounds with enzymes and their effects on mammals. Drug Metab Rev 1974; 3: 231-301
    • (1974) Drug Metab Rev , vol.3 , pp. 231-301
    • Hodgson, E.1    Philpot, R.M.2
  • 51
    • 0020055161 scopus 로고
    • Self-induction by oleandomycin of its own transformation into a metabolite forming an inactive complex with reduced cytochrome P450: Comparison with troleandomycin
    • Pessayre D, Descatoire V, Tinel M, et al. Self-induction by oleandomycin of its own transformation into a metabolite forming an inactive complex with reduced cytochrome P450: comparison with troleandomycin. J Pharmacol Exp Ther 1982; 221: 215-21
    • (1982) J Pharmacol Exp Ther , vol.221 , pp. 215-221
    • Pessayre, D.1    Descatoire, V.2    Tinel, M.3
  • 52
    • 0020554553 scopus 로고
    • Dual effects of macrolide antibiotics on rat liver cytochrome P450 induction and formation of metabolic complexes: A structure activity relationship
    • Delaforge M, Jaouen M, Mansuy D. Dual effects of macrolide antibiotics on rat liver cytochrome P450 induction and formation of metabolic complexes: a structure activity relationship. Biochem Pharmacol 1983; 32: 2309-18
    • (1983) Biochem Pharmacol , vol.32 , pp. 2309-2318
    • Delaforge, M.1    Jaouen, M.2    Mansuy, D.3
  • 53
    • 0023024338 scopus 로고
    • Macrolide antibiotics inhibit the degradation of the glucocorticoid-responsive cytochrome P450P in rat hepatocytes in vivo and in primary monolayer culture
    • Watkins PB, Wrighton SA, Schuetz EG, et al. Macrolide antibiotics inhibit the degradation of the glucocorticoid-responsive cytochrome P450P in rat hepatocytes in vivo and in primary monolayer culture. J Biol Chem Chem 1986; 261: 6264-71
    • (1986) J Biol Chem Chem , vol.261 , pp. 6264-6271
    • Watkins, P.B.1    Wrighton, S.A.2    Schuetz, E.G.3
  • 54
    • 0020079949 scopus 로고
    • Formation of an inactive cytochrome P450 Fe (II)-metabolite complex after administration of troleandomycin in humans
    • Pessayre D, Larrey D, Vitaux J, et al. Formation of an inactive cytochrome P450 Fe (II)-metabolite complex after administration of troleandomycin in humans. Biochem Pharmacol 1982; 31: 1699-704
    • (1982) Biochem Pharmacol , vol.31 , pp. 1699-1704
    • Pessayre, D.1    Larrey, D.2    Vitaux, J.3
  • 55
    • 0019415838 scopus 로고
    • Self-induction by erythromycin of its own transformation into a metabolite forming an inactive complex with reduced cytochrome P450
    • Danan G, Descatoire V, Pessayre D. Self-induction by erythromycin of its own transformation into a metabolite forming an inactive complex with reduced cytochrome P450. J Pharmacol Exp Ther 1981; 218: 509-14
    • (1981) J Pharmacol Exp Ther , vol.218 , pp. 509-514
    • Danan, G.1    Descatoire, V.2    Pessayre, D.3
  • 56
    • 0020575075 scopus 로고
    • Effects of erythromycin on hepatic drug metabolizing enzymes in humans
    • Larrey D, Funck-Brentano C, Breil P, et al. Effects of erythromycin on hepatic drug metabolizing enzymes in humans. Biochem Pharmacol 1983; 32: 1063-8
    • (1983) Biochem Pharmacol , vol.32 , pp. 1063-1068
    • Larrey, D.1    Funck-Brentano, C.2    Breil, P.3
  • 57
    • 0024319135 scopus 로고
    • Inhibition of oxidative drug metabolism by orphenadrine: In vitro and in vivo evidence for isozyme-specific complexation of cytochrome P450 and inhibition kinetics
    • Reidy GF, Mahta I, Murray M. Inhibition of oxidative drug metabolism by orphenadrine: in vitro and in vivo evidence for isozyme-specific complexation of cytochrome P450 and inhibition kinetics. Mol Pharmacol 1989; 35: 736-43
    • (1989) Mol Pharmacol , vol.35 , pp. 736-743
    • Reidy, G.F.1    Mahta, I.2    Murray, M.3
  • 58
    • 0017158099 scopus 로고
    • SKF-525A inhibition, induction and 452-nm complex formation
    • Buening MK, Franklin MR. SKF-525A inhibition, induction and 452-nm complex formation. Drug Metab Dispos 1976; 4: 244-55
    • (1976) Drug Metab Dispos , vol.4 , pp. 244-255
    • Buening, M.K.1    Franklin, M.R.2
  • 59
    • 0023943088 scopus 로고
    • Isozyme-selective complexation of cytochrome P450 in hepatic microsomes from SKF-525A-induced rats
    • Murray M. Isozyme-selective complexation of cytochrome P450 in hepatic microsomes from SKF-525A-induced rats. Arch Biochem Biophys 1988; 262: 381-8
    • (1988) Arch Biochem Biophys , vol.262 , pp. 381-388
    • Murray, M.1
  • 60
    • 0000792692 scopus 로고
    • Iron porphyrin-nitrene complexes: Preparation from 1,1-dialkylhydrazines: electronic structure from NMR, Mössbauer, and the magnetic susceptibility studies and crystal structure of the [tetrakis(p-chlorophenyl)porphyrinato-(2,2,6.6,-tetramethyl-1-piperidyl)nitrene] iron complex
    • Mahy JP, Battioni P, Mansuy D, et al. Iron porphyrin-nitrene complexes: preparation from 1,1-dialkylhydrazines: electronic structure from NMR, Mössbauer, and the magnetic susceptibility studies and crystal structure of the [tetrakis(p-chlorophenyl)porphyrinato-(2,2,6.6,-tetramethyl-1-piperidyl)nitrene] iron complex. J Am Chem Soc 1984; 106: 1699-706
    • (1984) J Am Chem Soc , vol.106 , pp. 1699-1706
    • Mahy, J.P.1    Battioni, P.2    Mansuy, D.3
  • 61
    • 0019488808 scopus 로고
    • Mechanism of the inhibitory action of isoniazid on microsomal drug metabolism
    • Muakkasah SF, Bidlack WR, Yang WCT. Mechanism of the inhibitory action of isoniazid on microsomal drug metabolism. Biochem Pharmacol 1981; 30: 1651-8
    • (1981) Biochem Pharmacol , vol.30 , pp. 1651-1658
    • Muakkasah, S.F.1    Bidlack, W.R.2    Yang, W.C.T.3
  • 62
    • 0014747936 scopus 로고
    • Diphenylhydantoin intoxication: A complication of isoniazid therapy
    • Kutt H, Brennan R, Dehajia H, et al. Diphenylhydantoin intoxication: a complication of isoniazid therapy. Am Rev Respir Dis 1970; 101: 377-84
    • (1970) Am Rev Respir Dis , vol.101 , pp. 377-384
    • Kutt, H.1    Brennan, R.2    Dehajia, H.3
  • 63
    • 0017606451 scopus 로고
    • Interaction of isoniazid and warfarin
    • Rosenthal AR, Self TH, Baker HD, et al. Interaction of isoniazid and warfarin. JAMA 1977; 238: 2177
    • (1977) JAMA , vol.238 , pp. 2177
    • Rosenthal, A.R.1    Self, T.H.2    Baker, H.D.3
  • 65
    • 0003729243 scopus 로고
    • Suicide substrate for drug metabolizing enzymes: Mechanisms and biological consequences
    • Gibson GG, editor. New York: Taylor & Francis
    • Ortiz de Montellano PR. Suicide substrate for drug metabolizing enzymes: mechanisms and biological consequences. In: Gibson GG, editor. Progress in drug metabolism. Vol. II. New York: Taylor & Francis, 1988: 99-148
    • (1988) Progress in Drug Metabolism , vol.2 , pp. 99-148
    • Ortiz De Montellano, P.R.1
  • 66
    • 0023552178 scopus 로고
    • Inactivation of multiple hepatic cytochrome P450 isozymes in rats by allyliso-propylacetamide: Mechanistic implications
    • Bornheim LM, Underwood MC, Caldera P, et al. Inactivation of multiple hepatic cytochrome P450 isozymes in rats by allyliso-propylacetamide: mechanistic implications. Mol Pharmacol 1987; 32: 299-308
    • (1987) Mol Pharmacol , vol.32 , pp. 299-308
    • Bornheim, L.M.1    Underwood, M.C.2    Caldera, P.3
  • 67
    • 0021865483 scopus 로고
    • Differential haemin-mediated restoration of cytochromc P450 N-demethylases after inactivation by allisopropylacetamide
    • Bornheim LM, Kotaka AN, Correia MA. Differential haemin-mediated restoration of cytochromc P450 N-demethylases after inactivation by allisopropylacetamide. Biochem J 1985; 227: 277-86
    • (1985) Biochem J , vol.227 , pp. 277-286
    • Bornheim, L.M.1    Kotaka, A.N.2    Correia, M.A.3
  • 68
    • 0023883363 scopus 로고
    • Oxidation of 17α-ethynylestradiol by human liver cytochrome P450
    • Guengerich FP. Oxidation of 17α-ethynylestradiol by human liver cytochrome P450. Mol Pharmacol 1988; 33: 500-8
    • (1988) Mol Pharmacol , vol.33 , pp. 500-508
    • Guengerich, F.P.1
  • 69
    • 0019906370 scopus 로고
    • Inactivation of cytochrome P450 and production of N-alkylated porphyrins caused in hepatocytes by substituted dihydropyridines: Structural requirements for loss haem and alkylation of the pyrrole nitrogen atom
    • De Matteis F, Hollands C, Gibbs AH, et al. Inactivation of cytochrome P450 and production of N-alkylated porphyrins caused in hepatocytes by substituted dihydropyridines: structural requirements for loss haem and alkylation of the pyrrole nitrogen atom. FEBS Lett 1982; 145: 87-92
    • (1982) FEBS Lett , vol.145 , pp. 87-92
    • De Matteis, F.1    Hollands, C.2    Gibbs, A.H.3
  • 70
    • 0019509069 scopus 로고
    • Covalent modification of lysine during the suicide inactivation of rat liver cylochrome P450 by chloramphenicol
    • Halpert JR. Covalent modification of lysine during the suicide inactivation of rat liver cylochrome P450 by chloramphenicol. Biochem Pharmacol 1981; 30: 875-81
    • (1981) Biochem Pharmacol , vol.30 , pp. 875-881
    • Halpert, J.R.1
  • 71
    • 0022253108 scopus 로고
    • On the mechanism of the inactivation of the major phenobarbital-inducible isozymes of rat liver cytochrome P450 by chloramphenicol
    • Halpert JR, Miller NE, Gorsky LD. On the mechanism of the inactivation of the major phenobarbital-inducible isozymes of rat liver cytochrome P450 by chloramphenicol. J Biol Chem 1985; 260: 8397-403
    • (1985) J Biol Chem , vol.260 , pp. 8397-8403
    • Halpert, J.R.1    Miller, N.E.2    Gorsky, L.D.3
  • 72
    • 0021970342 scopus 로고
    • Isozyme selectivity of the inhibition of rat liver cytochromes P450 by chloramphenicol in vivo
    • Halpert JR, Balfour C, Miller NE, et al. Isozyme selectivity of the inhibition of rat liver cytochromes P450 by chloramphenicol in vivo. Mol Pharmacol 1985; 28: 290-6
    • (1985) Mol Pharmacol , vol.28 , pp. 290-296
    • Halpert, J.R.1    Balfour, C.2    Miller, N.E.3
  • 73
    • 0027275796 scopus 로고
    • Mechanism-based inactivation of cytochrome P450 2B1 by 2-ethynylnaphthalene: Identification of an active-site peptide
    • Roberts ES, Hopkins NE, Alworth WL, et al. Mechanism-based inactivation of cytochrome P450 2B1 by 2-ethynylnaphthalene: identification of an active-site peptide. Chem Res Toxicol 1993; 6: 470-9
    • (1993) Chem Res Toxicol , vol.6 , pp. 470-479
    • Roberts, E.S.1    Hopkins, N.E.2    Alworth, W.L.3
  • 74
    • 0028078626 scopus 로고
    • Thiophene derivatives as new mechanism-based inhibitors ot cytochromes P450: Inactivation of yeast-expressed human liver P450 2C9 by tienilic acid
    • Lopez-Garcia MP, Dansette PM, Mansuy D. Thiophene derivatives as new mechanism-based inhibitors ot cytochromes P450: inactivation of yeast-expressed human liver P450 2C9 by tienilic acid. Biochemistry 1993; 33: 166-75
    • (1993) Biochemistry , vol.33 , pp. 166-175
    • Lopez-Garcia, M.P.1    Dansette, P.M.2    Mansuy, D.3
  • 75
    • 0030992920 scopus 로고    scopus 로고
    • Metabolism of chemoprotective agent diallyl sulfide to glutathione conjugates in rats
    • Jin L, Baillie TA. Metabolism of chemoprotective agent diallyl sulfide to glutathione conjugates in rats. Chem Res Toxicol 1997; 10: 318-27
    • (1997) Chem Res Toxicol , vol.10 , pp. 318-327
    • Jin, L.1    Baillie, T.A.2
  • 76
    • 0024507387 scopus 로고
    • Oxidation of cycloalkylamine by cytochrome P450
    • Bondon A, McDonald T, Harris TM, et al. Oxidation of cycloalkylamine by cytochrome P450. J Biol Chem 1989; 264: 1985-97
    • (1989) J Biol Chem , vol.264 , pp. 1985-1997
    • Bondon, A.1    McDonald, T.2    Harris, T.M.3
  • 77
    • 0024397272 scopus 로고
    • Oxidative metabolism of spironolactone: Evidence for involvement of electrophilic thiosteroid species in drug-mediated destruction of rat hepatic cytochrome P450
    • Decker CJ, Rashed MS, Baillie TA, et al. Oxidative metabolism of spironolactone: evidence for involvement of electrophilic thiosteroid species in drug-mediated destruction of rat hepatic cytochrome P450. Biochemistry 1989; 28: 5128-36
    • (1989) Biochemistry , vol.28 , pp. 5128-5136
    • Decker, C.J.1    Rashed, M.S.2    Baillie, T.A.3
  • 78
    • 84930288145 scopus 로고
    • The metabolism of methylated aminoazo dyes: V. Evidence for induction of enzyme systems in the rat by 3-methyl-cholanthrene
    • Conney AH, Miller EC, Miller JA. The metabolism of methylated aminoazo dyes: V. Evidence for induction of enzyme systems in the rat by 3-methyl-cholanthrene. Cancer Res 1956; 16: 450-9
    • (1956) Cancer Res , vol.16 , pp. 450-459
    • Conney, A.H.1    Miller, E.C.2    Miller, J.A.3
  • 79
    • 34250972453 scopus 로고
    • Die Beschleunigung des Evipanabbaues unter der Wirkung von Barbituraten
    • Remmer H. Die Beschleunigung des Evipanabbaues unter der Wirkung von Barbituraten. Naturwissenschaften 1958; 8: 189-91
    • (1958) Naturwissenschaften , vol.8 , pp. 189-191
    • Remmer, H.1
  • 80
    • 0001018633 scopus 로고
    • Induction of cytochrome P450 enzymes that metabolize xenobiotics
    • Ortiz de Montellano PR, editor. [chapter 10]. 2nd ed. New York: Plenum Press
    • Whitlock JP, Denison MS. Induction of cytochrome P450 enzymes that metabolize xenobiotics. In: Ortiz de Montellano PR, editor. Cytochrome P450: structure, mechanism and biochemistry [chapter 10]. 2nd ed. New York: Plenum Press, 1995: 367-90
    • (1995) Cytochrome P450: Structure, Mechanism and Biochemistry , pp. 367-390
    • Whitlock, J.P.1    Denison, M.S.2
  • 81
    • 0002030427 scopus 로고
    • Enzyme induction in the cytochrome P450 system
    • Kalow W, editor. [chapter 19]. New York: Pergamon Press
    • Okey AB. Enzyme induction in the cytochrome P450 system. In: Kalow W, editor. Pharmacogenetics of drug metabolism [chapter 19]. New York: Pergamon Press, 1992; 549-608
    • (1992) Pharmacogenetics of Drug Metabolism , pp. 549-608
    • Okey, A.B.1
  • 82
    • 0021806780 scopus 로고
    • Immunochemical evidence for induction of alcohol-oxidizing cytochrome P450 of rabbit liver microsomes by diverse agents: Ethanol, imidazole, trichloroethylene, acetone, pyrazole and isoniazid
    • U S A
    • Koop DR, Crump BC, Nordblom GD, et al. Immunochemical evidence for induction of alcohol-oxidizing cytochrome P450 of rabbit liver microsomes by diverse agents: ethanol, imidazole, trichloroethylene, acetone, pyrazole and isoniazid. Proc Natl Acad Sci USA 1985; U S A 82: 4065-9
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4065-4069
    • Koop, D.R.1    Crump, B.C.2    Nordblom, G.D.3
  • 83
    • 0024521525 scopus 로고
    • Induction of rat hepatic N-nitrosodimethylamine demethylase by acetone is due to protein stabilization
    • Song BJ, Veech RL, Park SS, et al. Induction of rat hepatic N-nitrosodimethylamine demethylase by acetone is due to protein stabilization. J Biol Chem 1989; 264: 3568-72
    • (1989) J Biol Chem , vol.264 , pp. 3568-3572
    • Song, B.J.1    Veech, R.L.2    Park, S.S.3
  • 84
    • 0023386817 scopus 로고
    • Stabilization of cytochrome P450j messenger ribonucleic acid in the diabetic rat
    • Song BJ, Matsunaga T, Hardwick JP, et al. Stabilization of cytochrome P450j messenger ribonucleic acid in the diabetic rat. Mol Endocrinol 1987; 1: 542-7
    • (1987) Mol Endocrinol , vol.1 , pp. 542-547
    • Song, B.J.1    Matsunaga, T.2    Hardwick, J.P.3
  • 85
    • 0023914486 scopus 로고
    • Mechanism of induction of cytochrome P450ac (P450j) in chemically induced and spontaneously diabetic rats
    • Dong Z, Hong J, Ma Q, et al. Mechanism of induction of cytochrome P450ac (P450j) in chemically induced and spontaneously diabetic rats. Arch Biochem Biophs 1988; 263: 29-35
    • (1988) Arch Biochem Biophs , vol.263 , pp. 29-35
    • Dong, Z.1    Hong, J.2    Ma, Q.3
  • 86
    • 0001303308 scopus 로고
    • Inhibition of the carcinogenic action of 7,12-dimethylbenz(a)anthracene by β-naphthoflavone
    • Wattenberg LW, Leong JL. Inhibition of the carcinogenic action of 7,12-dimethylbenz(a)anthracene by β-naphthoflavone. Proc Soc Exp Biol Med 1968; 128: 940-3
    • (1968) Proc Soc Exp Biol Med , vol.128 , pp. 940-943
    • Wattenberg, L.W.1    Leong, J.L.2
  • 87
    • 0018348547 scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin: Potent anticarcinogenic activity in CD-1 mice
    • DiGiovanna J, Berry DL, Juchau MR, et al. 2,3,7,8-Tetrachlorodibenzo-p-dioxin: potent anticarcinogenic activity in CD-1 mice. Biochem Biophys Res Commun 1979; 86: 577-84
    • (1979) Biochem Biophys Res Commun , vol.86 , pp. 577-584
    • DiGiovanna, J.1    Berry, D.L.2    Juchau, M.R.3
  • 88
    • 0019074870 scopus 로고
    • Benzo(a)pyrene metabolism, activation and carcinogenesis: Role of mixed function oxidases and related enzymes
    • Gelboin HV. Benzo(a)pyrene metabolism, activation and carcinogenesis: role of mixed function oxidases and related enzymes. Pharmacol Rev 1980; 60: 1107-66
    • (1980) Pharmacol Rev , vol.60 , pp. 1107-1166
    • Gelboin, H.V.1
  • 89
    • 0027751340 scopus 로고
    • Induction of cytochrome P4501 as an indicator of potential chemical carcinogenesis
    • Ioannides C, Parke DV. Induction of cytochrome P4501 as an indicator of potential chemical carcinogenesis. Drug Metab Rev 1993; 25: 485-501
    • (1993) Drug Metab Rev , vol.25 , pp. 485-501
    • Ioannides, C.1    Parke, D.V.2
  • 90
    • 0027763199 scopus 로고
    • CYP1A1: Friend or foe?
    • Beresford AP. CYP1A1: friend or foe? Drug Metab Rev 1993; 25: 503-17
    • (1993) Drug Metab Rev , vol.25 , pp. 503-517
    • Beresford, A.P.1
  • 91
    • 0025602894 scopus 로고
    • Induction of drug-metabolizing enzymes by xenobiotics
    • Bock KW, Lipp H-P, Bock-Hennig BS. Induction of drug-metabolizing enzymes by xenobiotics. Xenobiotica 1990; 20: 1101-11
    • (1990) Xenobiotica , vol.20 , pp. 1101-1111
    • Bock, K.W.1    Lipp, H.-P.2    Bock-Hennig, B.S.3
  • 92
    • 0026782943 scopus 로고
    • Induction of cytochrome P450 1A genes (CYP1A) by omeprazole in the human alimentary tract
    • McDonnell WM, Scheiman JM, Traber PG. Induction of cytochrome P450 1A genes (CYP1A) by omeprazole in the human alimentary tract. Gastroenterology 1993; 103: 1500-16
    • (1993) Gastroenterology , vol.103 , pp. 1500-1516
    • McDonnell, W.M.1    Scheiman, J.M.2    Traber, P.G.3
  • 93
    • 0025368026 scopus 로고
    • Omeprazole is an aryl hydrocarbon-like inducer of human hepatic cytochrome P450
    • Diaz D, Fabre I, Daujat M, et al. Omeprazole is an aryl hydrocarbon-like inducer of human hepatic cytochrome P450. Gastroenterology 1990; 99: 737-47
    • (1990) Gastroenterology , vol.99 , pp. 737-747
    • Diaz, D.1    Fabre, I.2    Daujat, M.3
  • 94
    • 0026444552 scopus 로고
    • Phenobarbital and related compounds: Approaches to interspecies extrapolation
    • Rice JM, Diwan BA, Ward JM, et al. Phenobarbital and related compounds: approaches to interspecies extrapolation. Prog Clin Biol Res 1992; 374: 231-49
    • (1992) Prog Clin Biol Res , vol.374 , pp. 231-249
    • Rice, J.M.1    Diwan, B.A.2    Ward, J.M.3
  • 95
    • 0028567499 scopus 로고
    • Induction and autoinduction properties of rifamycin derivatives: A review of animal and human studies
    • Strolin Benedetti M, Dostert P. Induction and autoinduction properties of rifamycin derivatives: a review of animal and human studies. Environ Health Perspect 1994; 102 Suppl. 9: 101-5
    • (1994) Environ Health Perspect , vol.102 , Issue.9 SUPPL. , pp. 101-105
    • Strolin Benedetti, M.1    Dostert, P.2
  • 97
    • 0027462638 scopus 로고
    • Understanding consequences of concurrent therapies
    • Peck CC, Temple R, Collins JM. Understanding consequences of concurrent therapies. JAMA 1993; 269: 1550-2
    • (1993) JAMA , vol.269 , pp. 1550-1552
    • Peck, C.C.1    Temple, R.2    Collins, J.M.3
  • 98
    • 0028361593 scopus 로고
    • Inhibition of human CYP3A catalyzed 1′-hydroxy midazolam formation by ketoconazole, nifedipine, erythromycin, cimetidine and nizatidine
    • Wrington S, Ring BJ. Inhibition of human CYP3A catalyzed 1′-hydroxy midazolam formation by ketoconazole, nifedipine, erythromycin, cimetidine and nizatidine. Pharm Res 1994; 11: 921-4
    • (1994) Pharm Res , vol.11 , pp. 921-924
    • Wrington, S.1    Ring, B.J.2
  • 99
    • 0001131495 scopus 로고
    • Simple inhibition systems
    • Segel IH, editor. [chapter 3]. Wiley-Interscience. New York: John Wiley & Sons
    • Segel RH. Simple inhibition systems. In: Segel IH, editor. Enzyme kinetics [chapter 3]. Wiley-Interscience. New York: John Wiley & Sons, 1975: 100-60
    • (1975) Enzyme Kinetics , pp. 100-160
    • Segel, R.H.1
  • 100
    • 0018710974 scopus 로고
    • Time-dependent kinetics: V. Time course of drug levels during enzyme induction (one-compartment model)
    • Levy RH, Dumain MS, Cook JL. Time-dependent kinetics: V. Time course of drug levels during enzyme induction (one-compartment model). J Pharmacokinet Biopharm 1979; 7: 557-78
    • (1979) J Pharmacokinet Biopharm , vol.7 , pp. 557-578
    • Levy, R.H.1    Dumain, M.S.2    Cook, J.L.3
  • 101
    • 0018350179 scopus 로고
    • Time-dependent kinetics: VI. Direct relationship between equations from drug levels during induction and those involving constant clearance
    • Levy RH, Dumain MS. Time-dependent kinetics: VI. Direct relationship between equations from drug levels during induction and those involving constant clearance. J Pharm Sci 1979; 68: 934-6
    • (1979) J Pharm Sci , vol.68 , pp. 934-936
    • Levy, R.H.1    Dumain, M.S.2
  • 102
    • 0018348734 scopus 로고
    • Time-dependent kinetics: IV. Pharmacokinetic theory of enzyme induction
    • Levy RH, Lai AA, Dumain MS. Time-dependent kinetics: IV. Pharmacokinetic theory of enzyme induction. J Pharm Sci 1979; 68: 398-9
    • (1979) J Pharm Sci , vol.68 , pp. 398-399
    • Levy, R.H.1    Lai, A.A.2    Dumain, M.S.3
  • 103
    • 0029872126 scopus 로고    scopus 로고
    • Role of cytochrome P450 3A4 in human metabolism of MK-639, a potent human immunodeficiency virus protease inhibitor
    • Chiba M, Hensleigh M, Nishime JA, et al. Role of cytochrome P450 3A4 in human metabolism of MK-639, a potent human immunodeficiency virus protease inhibitor. Drug Metab Dispos 1996; 24: 307-14
    • (1996) Drug Metab Dispos , vol.24 , pp. 307-314
    • Chiba, M.1    Hensleigh, M.2    Nishime, J.A.3
  • 104
    • 0027154768 scopus 로고
    • Stereo- and regio-selective N- and S-oxidation of tertiary amines and sulfides in the presence of adult human liver microsomes
    • Cashman JR, Young Z, Yang L, et al. Stereo- and regio-selective N- and S-oxidation of tertiary amines and sulfides in the presence of adult human liver microsomes. Drug Metab Dispos 1993; 21: 492-501
    • (1993) Drug Metab Dispos , vol.21 , pp. 492-501
    • Cashman, J.R.1    Young, Z.2    Yang, L.3
  • 105
    • 0023711819 scopus 로고
    • Metabolism of diazepam in vitro by human liver microsomes: Independent variability of N-demethylation and C3-hydroxylation
    • Inaba T, Tait A, Nakano M, et al. Metabolism of diazepam in vitro by human liver microsomes: independent variability of N-demethylation and C3-hydroxylation. Drug Metab Dispos 1988; 16: 605-8
    • (1988) Drug Metab Dispos , vol.16 , pp. 605-608
    • Inaba, T.1    Tait, A.2    Nakano, M.3
  • 106
    • 0027744044 scopus 로고
    • Cytochronie P450 mediated metabolism of diazepam in human and rat: Involvement of human CYP 2C in N-demethylation in the substrate concentration-dependent manner
    • Yasumori T, Nagata K, Yang SK, et al. Cytochronie P450 mediated metabolism of diazepam in human and rat: involvement of human CYP 2C in N-demethylation in the substrate concentration-dependent manner. Pharmacogenetics 1993; 3: 291-301
    • (1993) Pharmacogenetics , vol.3 , pp. 291-301
    • Yasumori, T.1    Nagata, K.2    Yang, S.K.3
  • 107
    • 0029560982 scopus 로고
    • Metabolism of the immunosuppressant tacrolimus in the small intestine: Cytochrome P450, drug interactions, and interindividual variability
    • Lampen A, Christians U, Guengerich FP, et al. Metabolism of the immunosuppressant tacrolimus in the small intestine: cytochrome P450, drug interactions, and interindividual variability. Drug Metab Dispos 1995; 23: 1315-24
    • (1995) Drug Metab Dispos , vol.23 , pp. 1315-1324
    • Lampen, A.1    Christians, U.2    Guengerich, F.P.3
  • 108
    • 0030430033 scopus 로고    scopus 로고
    • Cytochrome P450 isoform inhibitors as a tool for the investigation of metabolic reactions catalyzed by human liver microsomes
    • Bourrié M, Meunier V, Berger Y, et al. Cytochrome P450 isoform inhibitors as a tool for the investigation of metabolic reactions catalyzed by human liver microsomes. J Pharmacol Exp Ther 1996; 277: 321-32
    • (1996) J Pharmacol Exp Ther , vol.277 , pp. 321-332
    • Bourrié, M.1    Meunier, V.2    Berger, Y.3
  • 109
    • 0030009690 scopus 로고    scopus 로고
    • Inhibition of terfenadine metabolism in vitro by azole antifungal agents and by selective serotonin reuptake inhibitor antidepressants: Relation to pharmacokinetic interactions in vivo
    • Von Moltke LL, Greenblatt DJ, Duan SX, et al. Inhibition of terfenadine metabolism in vitro by azole antifungal agents and by selective serotonin reuptake inhibitor antidepressants: relation to pharmacokinetic interactions in vivo. J Clin Psychopharmacol 1996; 16: 104-12
    • (1996) J Clin Psychopharmacol , vol.16 , pp. 104-112
    • Von Moltke, L.L.1    Greenblatt, D.J.2    Duan, S.X.3
  • 110
    • 0030430035 scopus 로고    scopus 로고
    • Cytochrome P450-mediated metabolism of the HIV-1 protease inhibitor ritonavir (ABT-538) in human liver microsomes
    • Kumar GN, Rodrigues AD, Buko AM, et al. Cytochrome P450-mediated metabolism of the HIV-1 protease inhibitor ritonavir (ABT-538) in human liver microsomes. J Pharmacol Exp Ther 1996; 277: 423-31
    • (1996) J Pharmacol Exp Ther , vol.277 , pp. 423-431
    • Kumar, G.N.1    Rodrigues, A.D.2    Buko, A.M.3
  • 111
    • 0030024225 scopus 로고    scopus 로고
    • Kinetics of drug metabolism in rat liver slices: II. Comparison of clearance by liver slices and freshly isolated hepatocytes
    • Worboys PD, Bradbury A, Houston B. Kinetics of drug metabolism in rat liver slices: II. Comparison of clearance by liver slices and freshly isolated hepatocytes. Drug Metab Dispos 1996; 24: 676-81
    • (1996) Drug Metab Dispos , vol.24 , pp. 676-681
    • Worboys, P.D.1    Bradbury, A.2    Houston, B.3
  • 113
    • 0026443864 scopus 로고
    • Cyclosporin A metabolism in human liver, kidney, and intestine slices: Comparison to rat and dog slices and human cell lines
    • Vickers AEM, Fischer V, Connors S, et al. Cyclosporin A metabolism in human liver, kidney, and intestine slices: comparison to rat and dog slices and human cell lines. Drug Metab Dispos 1992; 20: 802-9
    • (1992) Drug Metab Dispos , vol.20 , pp. 802-809
    • Vickers, A.E.M.1    Fischer, V.2    Connors, S.3
  • 114
    • 0027168407 scopus 로고
    • The biotransformation of the ergot derivative CQA 206-291 in human, dog and rat liver slice cultures and prediction of in vivo plasma clearance
    • Vickers AEM, Connors S, Zollinger M, et al. The biotransformation of the ergot derivative CQA 206-291 in human, dog and rat liver slice cultures and prediction of in vivo plasma clearance. Drud Metab Dispos 1993; 21: 454-9
    • (1993) Drud Metab Dispos , vol.21 , pp. 454-459
    • Vickers, A.E.M.1    Connors, S.2    Zollinger, M.3
  • 115
    • 0027327501 scopus 로고
    • Development of a simple incubation system for metabolism studies with precision-cut liver slices
    • Dogterom P. Development of a simple incubation system for metabolism studies with precision-cut liver slices. Drug Metab Dispos 1993; 21: 699-704
    • (1993) Drug Metab Dispos , vol.21 , pp. 699-704
    • Dogterom, P.1
  • 116
    • 0001714139 scopus 로고
    • Primary hepatocyte culture as in vitro toxicological system
    • Gad S, editor. New York: Raven Press
    • Li AP. Primary hepatocyte culture as in vitro toxicological system. In: Gad S, editor. In vitro toxicology. New York: Raven Press, 1994: 195-220
    • (1994) In Vitro Toxicology , pp. 195-220
    • Li, A.P.1
  • 117
    • 0029021932 scopus 로고
    • Rifampicin induction of lidocaine metabolism in cultured human hepatocytes
    • Li AP, Rasmussen A, Xu L, et al. Rifampicin induction of lidocaine metabolism in cultured human hepatocytes. J Pharmacol Exp Ther 1995; 274: 673-7
    • (1995) J Pharmacol Exp Ther , vol.274 , pp. 673-677
    • Li, A.P.1    Rasmussen, A.2    Xu, L.3
  • 118
    • 0027239514 scopus 로고
    • Influence of extracellular matrix overlay on phenobarbital-mediated induction of CYP2B1, 2B2 and 3A1 genes in primary adult rat hepatocyte culture
    • Sidhu JS, Farin FM, Omiecinski CJ. Influence of extracellular matrix overlay on phenobarbital-mediated induction of CYP2B1, 2B2 and 3A1 genes in primary adult rat hepatocyte culture. Arch Biochem Biophys 1993; 301: 103-13
    • (1993) Arch Biochem Biophys , vol.301 , pp. 103-113
    • Sidhu, J.S.1    Farin, F.M.2    Omiecinski, C.J.3
  • 119
    • 0023132476 scopus 로고
    • Clearance approaches in pharmacology
    • Wilkinson GR. Clearance approaches in pharmacology. Pharmacol Rev 1987; 39: 1-47
    • (1987) Pharmacol Rev , vol.39 , pp. 1-47
    • Wilkinson, G.R.1
  • 120
    • 0016566218 scopus 로고
    • A physiological approach to hepatic drug clearance
    • Wilkinson GR, Shand DG. A physiological approach to hepatic drug clearance. Clin Pharmacol Ther 1975; 18: 377-90
    • (1975) Clin Pharmacol Ther , vol.18 , pp. 377-390
    • Wilkinson, G.R.1    Shand, D.G.2
  • 121
    • 0342940805 scopus 로고    scopus 로고
    • HIV protease inhibitors: From drug design to clinical studies
    • Lin JH. HIV protease inhibitors: from drug design to clinical studies. Adv Drug Deliv Rev 1997; 27: 215-33
    • (1997) Adv Drug Deliv Rev , vol.27 , pp. 215-233
    • Lin, J.H.1
  • 122
    • 0029974065 scopus 로고    scopus 로고
    • Species differences in the pharmacokinetics and metabolism of indinavir, a potent human immunodeficiency virus protease inhibitor
    • Lin JH, Chiba M, Balani SK, et al. Species differences in the pharmacokinetics and metabolism of indinavir, a potent human immunodeficiency virus protease inhibitor. Drug Metab Dispos 1996; 24: 1111-20
    • (1996) Drug Metab Dispos , vol.24 , pp. 1111-1120
    • Lin, J.H.1    Chiba, M.2    Balani, S.K.3
  • 124
    • 0012481814 scopus 로고    scopus 로고
    • Effects of ketoconazole and other P450 inhibitors on the pharmacokinetics of indinavir
    • McCrea J, Woolf E, Sterret A, et al. Effects of ketoconazole and other P450 inhibitors on the pharmacokinetics of indinavir. Pharm Res 1996; 13 Suppl.: S485
    • (1996) Pharm Res , vol.13 , Issue.SUPPL.
    • McCrea, J.1    Woolf, E.2    Sterret, A.3
  • 125
    • 0021248927 scopus 로고
    • Effect of product inhibition on elimination kinetics of ethoxybenzamide in rabbits
    • Lin JH, Sugiyama Y, Hanano M, et al. Effect of product inhibition on elimination kinetics of ethoxybenzamide in rabbits. Drug Metab Dispos 1984; 12: 253-6
    • (1984) Drug Metab Dispos , vol.12 , pp. 253-256
    • Lin, J.H.1    Sugiyama, Y.2    Hanano, M.3
  • 126
    • 0018126170 scopus 로고
    • Correlation between in vitro and in vivo drug metabolism rate: Oxidation of ethoxybenzamide in rat
    • Lin JH, Hayashi M, Awazu S, et al. Correlation between in vitro and in vivo drug metabolism rate: oxidation of ethoxybenzamide in rat. J Pharmacokinet Biopharm 1978; 6: 327-37
    • (1978) J Pharmacokinet Biopharm , vol.6 , pp. 327-337
    • Lin, J.H.1    Hayashi, M.2    Awazu, S.3
  • 127
    • 0020279521 scopus 로고
    • Physiological pharmacokinetics of ethoxybenzamide based on biochemical data obtained in vitro as well as on physiological data
    • Lin JH, Sugiyama Y, Awazu S, et al. Physiological pharmacokinetics of ethoxybenzamide based on biochemical data obtained in vitro as well as on physiological data. J Pharmacokinet Biopharm 1982; 10: 649-61
    • (1982) J Pharmacokinet Biopharm , vol.10 , pp. 649-661
    • Lin, J.H.1    Sugiyama, Y.2    Awazu, S.3
  • 128
    • 0029027857 scopus 로고
    • Prediction of in vivo disposition from in vitro systems: Clearance of phenytoin and tolbutamide using rat hepatic microsomal and hepatocyte data
    • Ashforth EIL, Carlile DJ, Chenery R, et al. Prediction of in vivo disposition from in vitro systems: clearance of phenytoin and tolbutamide using rat hepatic microsomal and hepatocyte data. J Pharmacol Exp Ther 1995; 274: 761-6
    • (1995) J Pharmacol Exp Ther , vol.274 , pp. 761-766
    • Ashforth, E.I.L.1    Carlile, D.J.2    Chenery, R.3
  • 129
    • 0028342648 scopus 로고
    • Utility of in vitro drug metabolism data in predicting in vivo metabolic clearance
    • Houston JB. Utility of in vitro drug metabolism data in predicting in vivo metabolic clearance. Biochem Pharmacol 1994; 47: 1469-74
    • (1994) Biochem Pharmacol , vol.47 , pp. 1469-1474
    • Houston, J.B.1
  • 130
    • 0028568568 scopus 로고
    • In vitro prediction of the terfenadine ketoconazole pharmacokinetic interaction
    • Von Moltke LL, Greenblatt DJ, Duan SX, et al. In vitro prediction of the terfenadine ketoconazole pharmacokinetic interaction. J Clin Pharmacol 1994; 34: 1222-7
    • (1994) J Clin Pharmacol , vol.34 , pp. 1222-1227
    • Von Moltke, L.L.1    Greenblatt, D.J.2    Duan, S.X.3
  • 131
    • 13144302846 scopus 로고
    • Influence of stiripentol on cytochrome P450-mediated metabolic pathways in humans: In vitro and in vivo comparison and calculation of in vivo inhibition constants
    • Tran A, Rey E, Pons G, et al. Influence of stiripentol on cytochrome P450-mediated metabolic pathways in humans: in vitro and in vivo comparison and calculation of in vivo inhibition constants. Clin Pharmacol Ther 1947; 62: 490-504
    • (1947) Clin Pharmacol Ther , vol.62 , pp. 490-504
    • Tran, A.1    Rey, E.2    Pons, G.3
  • 132
    • 0028194864 scopus 로고
    • Inhibition of desipramine hydroxylation in vitro by serotonin-reuptake-inhibitor antidepressants, and by quinidine and ketoconazole: A model system to predict drug interactions in vivo
    • Von Moltke LL, Greenblatt DJ, Cotreau-Bibbo MM, et al. Inhibition of desipramine hydroxylation in vitro by serotonin-reuptake-inhibitor antidepressants, and by quinidine and ketoconazole: a model system to predict drug interactions in vivo. J Pharmacol Exp Ther 1994; 268: 1278-83
    • (1994) J Pharmacol Exp Ther , vol.268 , pp. 1278-1283
    • Von Moltke, L.L.1    Greenblatt, D.J.2    Cotreau-Bibbo, M.M.3
  • 133
    • 0031974059 scopus 로고    scopus 로고
    • In vitro approaches to predicting drug interactions in vivo
    • Von Moltke LL, Greenblatt DJ, Schmider J, et al. In vitro approaches to predicting drug interactions in vivo. Biochem Pharmacol 1998; 55: 113-22
    • (1998) Biochem Pharmacol , vol.55 , pp. 113-122
    • Von Moltke, L.L.1    Greenblatt, D.J.2    Schmider, J.3
  • 134
    • 0030935086 scopus 로고    scopus 로고
    • Use of in vitro and in vivo data to estimate the likelihood of metabolic pharmacokinetic interactions
    • Bertz RJ, Granneman GR. Use of in vitro and in vivo data to estimate the likelihood of metabolic pharmacokinetic interactions. Clin Pharmacokinet 1997; 32: 210-58
    • (1997) Clin Pharmacokinet , vol.32 , pp. 210-258
    • Bertz, R.J.1    Granneman, G.R.2
  • 135
    • 0026099796 scopus 로고
    • 2-receptor antagonists: Relationship between intrinsic potency and effective plasma concentrations
    • 2-receptor antagonists: relationship between intrinsic potency and effective plasma concentrations. Clin Pharmacokinet 1991; 20: 218-36
    • (1991) Clin Pharmacokinet , vol.20 , pp. 218-236
    • Lin, J.H.1
  • 136
    • 0025985781 scopus 로고
    • Differential inhibition of individual human liver cytochromes P450 by cimetidine
    • Knodell RG, Browne DG, Gwozdz GP, et al. Differential inhibition of individual human liver cytochromes P450 by cimetidine. Gastroenterology 1991; 101: 1680-91
    • (1991) Gastroenterology , vol.101 , pp. 1680-1691
    • Knodell, R.G.1    Browne, D.G.2    Gwozdz, G.P.3
  • 137
    • 0026719245 scopus 로고
    • Selective inhibition of rat hepatic microsomal cytochrome P450: II. Effect of the in vitro administration
    • Chang T, Levine M, Bellward GD. Selective inhibition of rat hepatic microsomal cytochrome P450: II. Effect of the in vitro administration. J Pharmacol Exp Ther 1991; 260: 1450-5
    • (1991) J Pharmacol Exp Ther , vol.260 , pp. 1450-1455
    • Chang, T.1    Levine, M.2    Bellward, G.D.3
  • 138
    • 0026668190 scopus 로고
    • Selective inhibition of rat hepatic mierosomal cytochrome P450: I. Effect of the in vivo administration of cimetidine
    • Chang T, Levine M, Bandiera SM, et al. Selective inhibition of rat hepatic mierosomal cytochrome P450: I. Effect of the in vivo administration of cimetidine. J Pharmacol Exp Ther 1991; 260: 1441-9
    • (1991) J Pharmacol Exp Ther , vol.260 , pp. 1441-1449
    • Chang, T.1    Levine, M.2    Bandiera, S.M.3
  • 139
    • 0025168996 scopus 로고
    • Identification of the rabbit and human cytochromes P450 IIIA as the major enzymes involved m the N-demethylation of diltiazem
    • Pichard L, Gillet G, Fabre I, et al. Identification of the rabbit and human cytochromes P450 IIIA as the major enzymes involved m the N-demethylation of diltiazem. Drug Metab Dispos 1990; 18: 711-9
    • (1990) Drug Metab Dispos , vol.18 , pp. 711-719
    • Pichard, L.1    Gillet, G.2    Fabre, I.3
  • 140
    • 0025944905 scopus 로고
    • Biotransformation of lovastatin: IV. Identification of cytochrome P450 3A proteins as the major enzymes responsible for the oxidative metabolism of lovastatin in rat and human liver microsomes
    • Wang RW, Kari PH, Lu AYH, et al. Biotransformation of lovastatin: IV. Identification of cytochrome P450 3A proteins as the major enzymes responsible for the oxidative metabolism of lovastatin in rat and human liver microsomes. Arch Biochem Biophys 1991; 290: 355-61
    • (1991) Arch Biochem Biophys , vol.290 , pp. 355-361
    • Wang, R.W.1    Kari, P.H.2    Lu, A.Y.H.3
  • 141
    • 0009467090 scopus 로고    scopus 로고
    • Interaction of diltiazem with lovastatin and pravastatin
    • Agbim NE, Brater DC, Hall SD. Interaction of diltiazem with lovastatin and pravastatin [abstract]. Clin Pharmacol Ther 1997; 61: 201
    • (1997) Clin Pharmacol Ther , vol.61 , pp. 201
    • Agbim, N.E.1    Brater, D.C.2    Hall, S.D.3
  • 142
    • 0028916159 scopus 로고
    • Particular ability of cytochromes P450 3A to form inhibitory P450-iron-metabolite complexes upon metabolic oxidation of amino drugs
    • Bensoussan C, Delaforge M, Mansuy D. Particular ability of cytochromes P450 3A to form inhibitory P450-iron-metabolite complexes upon metabolic oxidation of amino drugs. Biochem Pharmacol 1995; 49: 591-602
    • (1995) Biochem Pharmacol , vol.49 , pp. 591-602
    • Bensoussan, C.1    Delaforge, M.2    Mansuy, D.3
  • 143
    • 0029925714 scopus 로고    scopus 로고
    • Diltiazem enhances the effects of triazolam by inhibiting its metabolism
    • Varhe A, Olkkola KT, Neuvonen PJ. Diltiazem enhances the effects of triazolam by inhibiting its metabolism. Clin Pharmacol Ther 1996; 59: 369-75
    • (1996) Clin Pharmacol Ther , vol.59 , pp. 369-375
    • Varhe, A.1    Olkkola, K.T.2    Neuvonen, P.J.3
  • 144
    • 0028359701 scopus 로고
    • Dose of midazolam should be reduced during diltiazem and verapamil treatments
    • Backman TJ, Olkkola KT, Neuvonen PJ. Dose of midazolam should be reduced during diltiazem and verapamil treatments. Br J Clin Pharmacol 1994; 37: 221-5
    • (1994) Br J Clin Pharmacol , vol.37 , pp. 221-225
    • Backman, T.J.1    Olkkola, K.T.2    Neuvonen, P.J.3
  • 146
    • 0027468346 scopus 로고
    • Terfenadine-ketoconazole interaction: Pharmacokinetic and electrocardiographic consequences
    • Honig PK, Wortham DC, Zamani K, et al. Terfenadine-ketoconazole interaction: pharmacokinetic and electrocardiographic consequences. JAMA 1993; 269: 1535-9
    • (1993) JAMA , vol.269 , pp. 1535-1539
    • Honig, P.K.1    Wortham, D.C.2    Zamani, K.3
  • 147
    • 0027168405 scopus 로고
    • Oxidation of the antihistamine drug terfenadine in human liver microsomes: Role of cytochrome P450 3A(4) in N-dealkylation and C-hydroxylation
    • Yun C, Okerholm RA, Guengerich FP. Oxidation of the antihistamine drug terfenadine in human liver microsomes: role of cytochrome P450 3A(4) in N-dealkylation and C-hydroxylation. Drug Metab Dispos 1993; 21: 403-9
    • (1993) Drug Metab Dispos , vol.21 , pp. 403-409
    • Yun, C.1    Okerholm, R.A.2    Guengerich, F.P.3
  • 148
    • 0027474601 scopus 로고
    • Mechanism of the cardiotoxic action of terfenadine
    • Woosley RL, Chen Y, Freiman JP, et al. Mechanism of the cardiotoxic action of terfenadine. JAMA 1993; 269: 1532-6
    • (1993) JAMA , vol.269 , pp. 1532-1536
    • Woosley, R.L.1    Chen, Y.2    Freiman, J.P.3
  • 149
    • 0025222965 scopus 로고
    • Torsade de pointes occurring in association with terfenadine use
    • Monahan BP, Ferguson CL, Killeary ES, et al. Torsade de pointes occurring in association with terfenadine use. JAMA 1990; 264: 2788-90
    • (1990) JAMA , vol.264 , pp. 2788-2790
    • Monahan, B.P.1    Ferguson, C.L.2    Killeary, E.S.3
  • 150
    • 0027385194 scopus 로고
    • Syncope and cardiac arrhythmia due to an interaction between itraconazeole and terfenadine
    • Crane JK, Shih, H-T. Syncope and cardiac arrhythmia due to an interaction between itraconazeole and terfenadine. Am J Med 1993; 95: 445-6
    • (1993) Am J Med , vol.95 , pp. 445-446
    • Crane, J.K.1    Shih, H.-T.2
  • 151
    • 0026671408 scopus 로고
    • Changes in pharmacokinetics and electrocardiographic pharmacodynamics of terfenadine with concomitant administration of erythromycin
    • Honig PK, Woosley RL, Zamani K, et al. Changes in pharmacokinetics and electrocardiographic pharmacodynamics of terfenadine with concomitant administration of erythromycin. Clin Pharmacol Ther 1992; 52: 231-8
    • (1992) Clin Pharmacol Ther , vol.52 , pp. 231-238
    • Honig, P.K.1    Woosley, R.L.2    Zamani, K.3
  • 152
    • 0016137377 scopus 로고
    • Warfarin: Stereochemical aspects of its metabolism and the interaction with phenylbutazone
    • Lewis RJ, Trager WF, Chan KK, et al. Warfarin: stereochemical aspects of its metabolism and the interaction with phenylbutazone. J Clin Invest 1974; 53: 1607-17
    • (1974) J Clin Invest , vol.53 , pp. 1607-1617
    • Lewis, R.J.1    Trager, W.F.2    Chan, K.K.3
  • 153
    • 0029877219 scopus 로고    scopus 로고
    • Warfarin-fluconazole: Inhibition of the human cytochrome P450-dependent metabolism of warfarin by fluconazole - In vivo studies
    • Kunze KL, Wienkers LC, Thummel KE, et al. Warfarin-fluconazole: inhibition of the human cytochrome P450-dependent metabolism of warfarin by fluconazole - in vivo studies. Drug Metab Dispos 1996; 24: 414-21
    • (1996) Drug Metab Dispos , vol.24 , pp. 414-421
    • Kunze, K.L.1    Wienkers, L.C.2    Thummel, K.E.3
  • 154
    • 0023219309 scopus 로고
    • Enoxacin-warfarin interactions: Pharmacokinetics and stereochemical aspects
    • Toon S, Hopkins KJ, Garstang FM, et al. Enoxacin-warfarin interactions: pharmacokinetics and stereochemical aspects. Clin Pharmacol Ther 1987; 44: 32-41
    • (1987) Clin Pharmacol Ther , vol.44 , pp. 32-41
    • Toon, S.1    Hopkins, K.J.2    Garstang, F.M.3
  • 155
    • 0020055560 scopus 로고
    • Drug interactions with cimetidine
    • Somogyi A, Gugler R. Drug interactions with cimetidine. Clin Pharmacokinet 1982; 7: 23-41
    • (1982) Clin Pharmacokinet , vol.7 , pp. 23-41
    • Somogyi, A.1    Gugler, R.2
  • 156
    • 0026048337 scopus 로고
    • Further insight into the stereoselective interaction between warfarin and cimetidine in man
    • Niopas I, Toon S, Rowland M. Further insight into the stereoselective interaction between warfarin and cimetidine in man. Br J Clin Pharmacol 1991; 32: 508-11
    • (1991) Br J Clin Pharmacol , vol.32 , pp. 508-511
    • Niopas, I.1    Toon, S.2    Rowland, M.3
  • 157
    • 0020029076 scopus 로고
    • Potentiation of warfarin anticoagulation by amiodarone
    • Hamer A, Peter T, Mandel WJ, et al. Potentiation of warfarin anticoagulation by amiodarone. Circulation 1982; 65: 1025-9
    • (1982) Circulation , vol.65 , pp. 1025-1029
    • Hamer, A.1    Peter, T.2    Mandel, W.J.3
  • 158
    • 0026575955 scopus 로고
    • The mechanism of the interaction between amiodarone and warfarin in humans
    • Heimark LD, Wienkers L, Kunze K, et al. The mechanism of the interaction between amiodarone and warfarin in humans. Clin Pharmacol Ther 1992; 51: 398-407
    • (1992) Clin Pharmacol Ther , vol.51 , pp. 398-407
    • Heimark, L.D.1    Wienkers, L.2    Kunze, K.3
  • 159
    • 0023795013 scopus 로고
    • Polymorphic O-demethylation of codeine
    • Chen ZR, Somogyi AA, Bochner F. Polymorphic O-demethylation of codeine. Lancet 1988; II: 914-5
    • (1988) Lancet , vol.2 , pp. 914-915
    • Chen, Z.R.1    Somogyi, A.A.2    Bochner, F.3
  • 160
    • 0025735576 scopus 로고
    • The activation of biguanide antimalarial proguanil co-segregates with the mephenytoin oxidation polymorphism: A panel study
    • Ward SA, Helsby NA, Kjelbo E, et al. The activation of biguanide antimalarial proguanil co-segregates with the mephenytoin oxidation polymorphism: a panel study. Br J Clin Pharmacol 1991; 31: 689-92
    • (1991) Br J Clin Pharmacol , vol.31 , pp. 689-692
    • Ward, S.A.1    Helsby, N.A.2    Kjelbo, E.3
  • 161
    • 0025064349 scopus 로고
    • Effect of omeprazole treatment on diazepam plasma levels in slow versus normal rapid metabolizers of omeprazole
    • Andersson T, Cederberg C, Edvardsson G, et al. Effect of omeprazole treatment on diazepam plasma levels in slow versus normal rapid metabolizers of omeprazole. Clin Pharmacol Ther 1990; 47: 79-85
    • (1990) Clin Pharmacol Ther , vol.47 , pp. 79-85
    • Andersson, T.1    Cederberg, C.2    Edvardsson, G.3
  • 162
    • 0025241657 scopus 로고
    • Genetically determined steady-stale interaction between encainide and quinidine in patients with arrhythmias
    • Turgeon J, Pavlou HN, Wong W, et al. Genetically determined steady-stale interaction between encainide and quinidine in patients with arrhythmias. J Pharmacol Exp Ther 1990; 255: 642-9
    • (1990) J Pharmacol Exp Ther , vol.255 , pp. 642-649
    • Turgeon, J.1    Pavlou, H.N.2    Wong, W.3
  • 163
    • 0029859728 scopus 로고    scopus 로고
    • Differences between white subjects and Chinese subjects in the in vivo inhibition of cytochrome P450s 2C19, 2D6 and 3A by omeprazole
    • Caraco Y, Wilkinson GR, Wood AJJ. Differences between white subjects and Chinese subjects in the in vivo inhibition of cytochrome P450s 2C19, 2D6 and 3A by omeprazole. Clin Pharmacol Ther 1996; 60: 396-404
    • (1996) Clin Pharmacol Ther , vol.60 , pp. 396-404
    • Caraco, Y.1    Wilkinson, G.R.2    Wood, A.J.J.3
  • 164
    • 0029127629 scopus 로고
    • Interethnic difference in omeprazole's inhibition of diazepam metabolism
    • Caraco Y, Tateishi T, Wood AJJ. Interethnic difference in omeprazole's inhibition of diazepam metabolism. Clin Pharmacol Ther 1995; 58: 62-72
    • (1995) Clin Pharmacol Ther , vol.58 , pp. 62-72
    • Caraco, Y.1    Tateishi, T.2    Wood, A.J.J.3
  • 165
    • 0029023852 scopus 로고
    • Time- and dose-dependent pharmacokinetics of L-754,394, an HIV protease inhibitor, in rats, dogs and monkeys
    • Lin JH, Chiba M, Chen I-W, et al. Time- and dose-dependent pharmacokinetics of L-754,394, an HIV protease inhibitor, in rats, dogs and monkeys. J Pharmacol Exp Ther 1995; 274: 264-9
    • (1995) J Pharmacol Exp Ther , vol.274 , pp. 264-269
    • Lin, J.H.1    Chiba, M.2    Chen, I.-W.3
  • 166
    • 0025091419 scopus 로고
    • Pharmacokinetic drug interaction with cyclosporin: I
    • Yee GC, McGuire TR. Pharmacokinetic drug interaction with cyclosporin: I. Clin Pharmacokinet 1990; 19: 312-32
    • (1990) Clin Pharmacokinet , vol.19 , pp. 312-332
    • Yee, G.C.1    McGuire, T.R.2
  • 167
    • 0029089702 scopus 로고
    • Ketoconazole to reduce the need for cyclosporine after cardiac transplantation
    • Keogh A, Spratt P, McCosker C, et al. Ketoconazole to reduce the need for cyclosporine after cardiac transplantation. N Engl J Med 1995; 333: 628-33
    • (1995) N Engl J Med , vol.333 , pp. 628-633
    • Keogh, A.1    Spratt, P.2    McCosker, C.3
  • 168
    • 0031006546 scopus 로고    scopus 로고
    • The use of other drugs to allow a lower dosage of cyclosporin to be used: Therapeutic and pharmacoeconomic considerations
    • Jones TE. The use of other drugs to allow a lower dosage of cyclosporin to be used: therapeutic and pharmacoeconomic considerations. Clin Pharmacokinet 1997; 32: 357-67
    • (1997) Clin Pharmacokinet , vol.32 , pp. 357-367
    • Jones, T.E.1
  • 169
    • 0031035968 scopus 로고    scopus 로고
    • Pharmacokinetic enhancement of inhibitors of the human immunodeficiency virus protease by coadministration with ritonavir
    • Kempf DJ, Marsh KC, Kumar G, et al. Pharmacokinetic enhancement of inhibitors of the human immunodeficiency virus protease by coadministration with ritonavir. Antimicrob Agents Chemother 1997; 41: 654-60
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 654-660
    • Kempf, D.J.1    Marsh, K.C.2    Kumar, G.3
  • 170
    • 0025005022 scopus 로고
    • Induction of polymorphic 4′-hydroxylation of S-mephenytoin by rifampicin
    • Zhou HH, Anthony LB, Wood AJJ, et al. Induction of polymorphic 4′-hydroxylation of S-mephenytoin by rifampicin. Br J Clin Pharmacol 1990; 30: 471-5
    • (1990) Br J Clin Pharmacol , vol.30 , pp. 471-475
    • Zhou, H.H.1    Anthony, L.B.2    Wood, A.J.J.3
  • 171
    • 0024603850 scopus 로고
    • Metabolism of cyclosporin A: IV. Purification and identification of the rifampicin-inducible human liver cytochrome P450 (cyclosporin A oxidase) as a product of P450 3A gene subfamily
    • Combalbert J, Fabre I, Fabre G, et al. Metabolism of cyclosporin A: IV. Purification and identification of the rifampicin-inducible human liver cytochrome P450 (cyclosporin A oxidase) as a product of P450 3A gene subfamily. Drug Metab Dispos 1984; 17: 197-207
    • (1984) Drug Metab Dispos , vol.17 , pp. 197-207
    • Combalbert, J.1    Fabre, I.2    Fabre, G.3
  • 172
    • 0016245363 scopus 로고
    • Interactions of sodium warfarin and rifampicin studies in man
    • O'Reilly RA. Interactions of sodium warfarin and rifampicin studies in man. Ann Intern Med 1974; 81: 337-40
    • (1974) Ann Intern Med , vol.81 , pp. 337-340
    • O'Reilly, R.A.1
  • 173
    • 0023619704 scopus 로고
    • The mechanism of warfarin-rifampicin drug interaction in humans
    • Heimark LD, Gibaldi M, Trager WF, et al. The mechanism of warfarin-rifampicin drug interaction in humans. Clin Pharmacol Ther 1987; 423: 385-94
    • (1987) Clin Pharmacol Ther , vol.423 , pp. 385-394
    • Heimark, L.D.1    Gibaldi, M.2    Trager, W.F.3
  • 175
    • 0016832118 scopus 로고
    • Effect of rifampicin treatment on the metabolism of estradiol and 17α-ethinylestradiol by human liver microsomes
    • Bolt HM, Kappus H, Bolt M. Effect of rifampicin treatment on the metabolism of estradiol and 17α-ethinylestradiol by human liver microsomes. Eur J Clin Pharmacol 1975; 8: 301-7
    • (1975) Eur J Clin Pharmacol , vol.8 , pp. 301-307
    • Bolt, H.M.1    Kappus, H.2    Bolt, M.3
  • 176
    • 0021592460 scopus 로고
    • Interaction between cyclosporin and rifampicin
    • Daniels NJ, Hunnisett AG, Morris PJ. Interaction between cyclosporin and rifampicin. Lancet 1984; II: 639
    • (1984) Lancet , vol.2 , pp. 639
    • Daniels, N.J.1    Hunnisett, A.G.2    Morris, P.J.3
  • 177
    • 0021941863 scopus 로고
    • Acute rejection and massive cyclosporine requirements in heart transplant recipients treated with rifampicin
    • Modry DL, Stinson EB, Oyer PE. Acute rejection and massive cyclosporine requirements in heart transplant recipients treated with rifampicin. Transplantation 1985; 39: 313-4
    • (1985) Transplantation , vol.39 , pp. 313-314
    • Modry, D.L.1    Stinson, E.B.2    Oyer, P.E.3
  • 178
    • 0030042485 scopus 로고    scopus 로고
    • Clinically significant drug interactions with cyclosporin: An update
    • Campana C, Regazzi MB, Buggia I, et al. Clinically significant drug interactions with cyclosporin: an update. Clin Pharmacokinet 1996; 30: 141-79
    • (1996) Clin Pharmacokinet , vol.30 , pp. 141-179
    • Campana, C.1    Regazzi, M.B.2    Buggia, I.3
  • 179
    • 0029841727 scopus 로고    scopus 로고
    • Pharmacokinetic interactions between antiepileptic drugs: Clinical considerations
    • Riva R, Albani F, Contin M, et al. Pharmacokinetic interactions between antiepileptic drugs: clinical considerations. Clin Pharmacokinet 1996; 31: 470-93
    • (1996) Clin Pharmacokinet , vol.31 , pp. 470-493
    • Riva, R.1    Albani, F.2    Contin, M.3
  • 180
    • 0015212910 scopus 로고
    • Clinical implications of enzyme induction
    • Breckenridge AM, Orme MLE. Clinical implications of enzyme induction. Ann N Y Acad Sci 1971; 179: 421-31
    • (1971) Ann N Y Acad Sci , vol.179 , pp. 421-431
    • Breckenridge, A.M.1    Orme, M.L.E.2
  • 181
    • 0022377740 scopus 로고
    • Antipyrine metabolite kinetics in healthy human volunteers during multiple dosing of phenytoin and carbamazepine
    • Shaw PN, Houston JB, Rowland M, et al. Antipyrine metabolite kinetics in healthy human volunteers during multiple dosing of phenytoin and carbamazepine. Br J Clin Pharmacol 1985; 20: 611-8
    • (1985) Br J Clin Pharmacol , vol.20 , pp. 611-618
    • Shaw, P.N.1    Houston, J.B.2    Rowland, M.3
  • 182
    • 0025005022 scopus 로고
    • Induction of polymorphic 4′-hydroxylation of S-mephenytoin by rifampicin
    • Zhou HH, Anthony LB, Wood JJ, et al. Induction of polymorphic 4′-hydroxylation of S-mephenytoin by rifampicin. Br J Clin Pharmacol 1990; 30: 471-5
    • (1990) Br J Clin Pharmacol , vol.30 , pp. 471-475
    • Zhou, H.H.1    Anthony, L.B.2    Wood, J.J.3
  • 183
    • 0026699994 scopus 로고
    • Increase of P450 IA2 activity by omeprazole: Evidence by the 13C-[N3-methyl]-caffeine breath test in poor and extensive metabolizers of S-mephenytoin
    • Rost KL, Brösicke H, Brockmöller J, et al. Increase of P450 IA2 activity by omeprazole: evidence by the 13C-[N3-methyl]-caffeine breath test in poor and extensive metabolizers of S-mephenytoin. Clin Pharmacol Ther 1992; 52: 170-80
    • (1992) Clin Pharmacol Ther , vol.52 , pp. 170-180
    • Rost, K.L.1    Brösicke, H.2    Brockmöller, J.3
  • 184
    • 0028051743 scopus 로고
    • Specific and dose-dependent enzyme induction by omeprazole in human beings
    • Rost KL, Brösicke H, Heinemeyer G, et al. Specific and dose-dependent enzyme induction by omeprazole in human beings. Hepatology 1994; 20: 1204-12
    • (1994) Hepatology , vol.20 , pp. 1204-1212
    • Rost, K.L.1    Brösicke, H.2    Heinemeyer, G.3
  • 185
    • 0025786589 scopus 로고
    • Age-dependent stereoselective increase in the oral clearance of hexobarbitone isomers caused by rifampicin
    • Smith DA, Chandler MHH, Shedlofsky SI, et al. Age-dependent stereoselective increase in the oral clearance of hexobarbitone isomers caused by rifampicin. Br J Clin Pharmacol 1991; 32: 735-9
    • (1991) Br J Clin Pharmacol , vol.32 , pp. 735-739
    • Smith, D.A.1    Chandler, M.H.H.2    Shedlofsky, S.I.3
  • 186
    • 0021148485 scopus 로고
    • Enzyme induction and β-adrenergic receptor blocking drugs
    • Branch RA, Herman RJ. Enzyme induction and β-adrenergic receptor blocking drugs. Br J Clin Pharmacol 1984; 17: 775-845
    • (1984) Br J Clin Pharmacol , vol.17 , pp. 775-845
    • Branch, R.A.1    Herman, R.J.2
  • 187
  • 188
    • 0018731154 scopus 로고
    • The effects of age and cigarette smoking on propranolol disposition
    • Vestal RE, Wood AJJ, Branch RA, et al. The effects of age and cigarette smoking on propranolol disposition. Clin Pharmacol Ther 1979; 26: 8-15
    • (1979) Clin Pharmacol Ther , vol.26 , pp. 8-15
    • Vestal, R.E.1    Wood, A.J.J.2    Branch, R.A.3
  • 189
    • 0017968392 scopus 로고
    • Reduced induction of drug metabolism in the elderly
    • Salem SAM. Reduced induction of drug metabolism in the elderly. Age Ageing 1978; 7: 68-73
    • (1978) Age Ageing , vol.7 , pp. 68-73
    • Salem, S.A.M.1
  • 190
    • 0018419356 scopus 로고
    • Influence of pentobarbital on effect and plasma levels of alprenolol and 4-hydroxyalprenolol
    • Collste P, Seideman P, Borg KO, et al. Influence of pentobarbital on effect and plasma levels of alprenolol and 4-hydroxyalprenolol. Clin Pharmacol Ther 1979; 25: 423-7
    • (1979) Clin Pharmacol Ther , vol.25 , pp. 423-427
    • Collste, P.1    Seideman, P.2    Borg, K.O.3
  • 192


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