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Volumn 10, Issue 1, 2008, Pages 200-207

Reaction phenotyping: Current industry efforts to identify enzymes responsible for metabolizing drug candidates

Author keywords

Cytochrome P450; Metabolism; Reaction phenotyping; UDP glucuronosyl transferase

Indexed keywords

BENZYLNIRVANOL; COMPLEMENTARY DNA; CYTOCHROME P450; CYTOCHROME P450 1A2; CYTOCHROME P450 2A6; CYTOCHROME P450 2B6; CYTOCHROME P450 2C19; CYTOCHROME P450 2C8; CYTOCHROME P450 2C9; CYTOCHROME P450 2D6; CYTOCHROME P450 2E1; CYTOCHROME P450 3A4; CYTOCHROME P450 INHIBITOR; DIMETHYLANILINE MONOOXYGENASE; DRUG METABOLIZING ENZYME; ENZYME INHIBITOR; FLAVIN CONTANING MONOOXYGENASE INHIBITOR; FURAFYLLINE; GLUCURONOSYLTRANSFERASE; KETOCONAZOLE; QUINIDINE; SULFAPHENAZOLE; TROLEANDOMYCIN;

EID: 51249114512     PISSN: 15507416     EISSN: None     Source Type: Journal    
DOI: 10.1208/s12248-008-9019-6     Document Type: Short Survey
Times cited : (48)

References (47)
  • 1
    • 0035987212 scopus 로고    scopus 로고
    • Cytochrome P450 pharmacogenetics in drug development: In vitro studies and clinical consequences
    • A. D. Rodrigues, and T. H. Rushmore. Cytochrome P450 pharmacogenetics in drug development: In vitro studies and clinical consequences. Curr. Drug Metab. 3:289-309 (2002).
    • (2002) Curr. Drug Metab. , vol.3 , pp. 289-309
    • Rodrigues, A.D.1    Rushmore, T.H.2
  • 2
    • 0022178173 scopus 로고
    • Interethnic differences in genetic polymorphism of debrisoquin and mephenytoin hydroxylation between Japanese and Caucasian populations
    • K. Nakamura, F. Goto, W. A. Ray, C. B. McAllister, E. Jacqz, G. R. Wilkinson, and R. A. Branch. Interethnic differences in genetic polymorphism of debrisoquin and mephenytoin hydroxylation between Japanese and Caucasian populations. Clin. Pharmacol. Ther. 38:402-408 (1985).
    • (1985) Clin. Pharmacol. Ther. , vol.38 , pp. 402-408
    • Nakamura, K.1    Goto, F.2    Ray, W.A.3    McAllister, C.B.4    Jacqz, E.5    Wilkinson, G.R.6    Branch, R.A.7
  • 3
    • 0031840217 scopus 로고    scopus 로고
    • Genetic polymorphism of cytochrome P450s, CYP2C19, and CYP2C9 in a Japanese population
    • M. Kimura, I. Ieiri, K. Mamiya, A. Urae, and S. Higuchi. Genetic polymorphism of cytochrome P450s, CYP2C19, and CYP2C9 in a Japanese population. Ther. Drug Monit. 20:243-247 (1998).
    • (1998) Ther. Drug Monit. , vol.20 , pp. 243-247
    • Kimura, M.1    Ieiri, I.2    Mamiya, K.3    Urae, A.4    Higuchi, S.5
  • 4
    • 34248347478 scopus 로고    scopus 로고
    • The pharmacogenetics of CYP2C9 and CYP2C19: Ethnic variation and clinical significance
    • R. Jose, and A. Chandrasekaran. The pharmacogenetics of CYP2C9 and CYP2C19: Ethnic variation and clinical significance. Curr. Clin. Pharm. 2(1):93-109 (2007).
    • (2007) Curr. Clin. Pharm. , vol.2 , Issue.1 , pp. 93-109
    • Jose, R.1    Chandrasekaran, A.2
  • 5
    • 33646205301 scopus 로고    scopus 로고
    • Interethnic and intraethnic variability of CYP2C8 and CYP2C9 polymorphisms in healthy individuals
    • E. Garcia-Martin, C. Martinez, J. M. Ladero, and J. A. G. Agundez. Interethnic and intraethnic variability of CYP2C8 and CYP2C9 polymorphisms in healthy individuals. Mol. Diagn. Ther. 10:29-40 (2006).
    • (2006) Mol. Diagn. Ther. , vol.10 , pp. 29-40
    • Garcia-Martin, E.1    Martinez, C.2    Ladero, J.M.3    Agundez, J.A.G.4
  • 6
    • 0032456884 scopus 로고    scopus 로고
    • Clinically important pharmacokinetic drug-drug interactions: Role of cytochrome P450 enzymes
    • E. Tanaka. Clinically important pharmacokinetic drug-drug interactions: role of cytochrome P450 enzymes. J. Clin. Pharm. Ther. 23:403-416 (1998).
    • (1998) J. Clin. Pharm. Ther. , vol.23 , pp. 403-416
    • Tanaka, E.1
  • 7
    • 0033972441 scopus 로고    scopus 로고
    • Pharmacokinetic-pharmacodynamic consequences and clinical relevance of cytochrome P450 3A4 inhibition
    • G. K. Dresser, J. D. Spence, and D. G. Bailey. Pharmacokinetic-pharmacodynamic consequences and clinical relevance of cytochrome P450 3A4 inhibition. Clin. Pharm. 38:41-57 (2000).
    • (2000) Clin. Pharm. , vol.38 , pp. 41-57
    • Dresser, G.K.1    Spence, J.D.2    Bailey, D.G.3
  • 8
    • 0031751330 scopus 로고    scopus 로고
    • Ritonavir: Clinical pharmacokinetics and interactions with other anti-HIV agents
    • A. Hsu, G. R. Granneman, and J. Bertz. Ritonavir: Clinical pharmacokinetics and interactions with other anti-HIV agents. Clin. Pharm. 35:275-291 (1998).
    • (1998) Clin. Pharm. , vol.35 , pp. 275-291
    • Hsu, A.1    Granneman, G.R.2    Bertz, J.3
  • 10
    • 0036157094 scopus 로고    scopus 로고
    • Human hepatic flavin-containing monooxygenases 1 (FMO1) and 3 (FMO3) developmental expression
    • S. B. Koukouritaki, P. Simpson, C. K. Yeung, A. E. Rettie, and R. N. Hines. Human hepatic flavin-containing monooxygenases 1 (FMO1) and 3 (FMO3) developmental expression. Pediatr. Res. 51:236-243 (2002).
    • (2002) Pediatr. Res. , vol.51 , pp. 236-243
    • Koukouritaki, S.B.1    Simpson, P.2    Yeung, C.K.3    Rettie, A.E.4    Hines, R.N.5
  • 11
    • 0029836098 scopus 로고    scopus 로고
    • Dietary indole-3-carbinol inhibits FMO activity and the expression of flavin-containing monooxygenase form 1 in rat liver and intestine
    • S. Larsen-Su, and D. E. Williams. Dietary indole-3-carbinol inhibits FMO activity and the expression of flavin-containing monooxygenase form 1 in rat liver and intestine. Drug Metab. Dispos. 24:927-931 (1996).
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 927-931
    • Larsen-Su, S.1    Williams, D.E.2
  • 12
    • 0037819284 scopus 로고    scopus 로고
    • Pharmacogenomics of human UDP-glucuronosyltransferase enzymes
    • C. Guillemette. Pharmacogenomics of human UDP-glucuronosyltransferase enzymes. Pharmacogenomics J. 3:136-158 (2003).
    • (2003) Pharmacogenomics J. , vol.3 , pp. 136-158
    • Guillemette, C.1
  • 13
    • 33847659653 scopus 로고    scopus 로고
    • The impact of UGT1A8, UGT1A9, and UGT2B7 genetic polymorphisms on the pharmacokinetic profile of mycophenolic acid after a single oral dose in healthy volunteers
    • E. Levesque, R. Delage, M.-O. Benoit-Biancamano, P. Caron, O. Bernard, F. Couture, and C. Guillemette. The impact of UGT1A8, UGT1A9, and UGT2B7 genetic polymorphisms on the pharmacokinetic profile of mycophenolic acid after a single oral dose in healthy volunteers. Clin. Pharm. Ther. 81:392-400 (2007).
    • (2007) Clin. Pharm. Ther. , vol.81 , pp. 392-400
    • Levesque, E.1    Delage, R.2    Benoit-Biancamano, M.-O.3    Caron, P.4    Bernard, O.5    Couture, F.6    Guillemette, C.7
  • 14
    • 15244342411 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferases and clinical drug-drug interactions
    • T. K. L. Kiang, M. H. H. Ensom, and T. K. H. Chang. UDP-glucuronosyltransferases and clinical drug-drug interactions. Pharmacol. Ther. 106:97-132 (2005).
    • (2005) Pharmacol. Ther. , vol.106 , pp. 97-132
    • Kiang, T.K.L.1    Ensom, M.H.H.2    Chang, T.K.H.3
  • 15
    • 0033105118 scopus 로고    scopus 로고
    • Integrated cytochrome P450 reaction phenotyping: Attempting to bridge the gap between cDNA-expressed cytochromes P450 and native human liver microsomes
    • A. D. Rodrigues. Integrated cytochrome P450 reaction phenotyping: attempting to bridge the gap between cDNA-expressed cytochromes P450 and native human liver microsomes. Biochem. Pharmacol. 57:465-480 (1999).
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 465-480
    • Rodrigues, A.D.1
  • 16
    • 0030022629 scopus 로고    scopus 로고
    • An overview of current cytochrome P450 technology for assessing the safety and efficacy of new materials
    • A. Parkinson. An overview of current cytochrome P450 technology for assessing the safety and efficacy of new materials. Toxicol. Pathol. 24:48-57 (1996).
    • (1996) Toxicol. Pathol. , vol.24 , pp. 48-57
    • Parkinson, A.1
  • 17
    • 0028114740 scopus 로고
    • Use of in vitro human metabolism studies in drug development. An industrial perspective
    • A. D. Rodrigues. Use of in vitro human metabolism studies in drug development. An industrial perspective. Biochem. Pharmacol. 48:2147-2156 (1994).
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 2147-2156
    • Rodrigues, A.D.1
  • 18
    • 33746899674 scopus 로고    scopus 로고
    • Approach to the prediction of the contribution of major cytochrome P450 enzymes to drug metabolism in the early drug-discovery stage
    • C. Emoto, S. Murase, and K. Iwasaki. Approach to the prediction of the contribution of major cytochrome P450 enzymes to drug metabolism in the early drug-discovery stage. Xenobiotica. 36:671-683 (2006).
    • (2006) Xenobiotica. , vol.36 , pp. 671-683
    • Emoto, C.1    Murase, S.2    Iwasaki, K.3
  • 19
    • 0028342648 scopus 로고
    • Utility of in vitro drug metabolism data in predicting in vivo metabolic clearance
    • J. B. Houston. Utility of in vitro drug metabolism data in predicting in vivo metabolic clearance. Biochem. Pharm. 47:1469-1479 (1994).
    • (1994) Biochem. Pharm. , vol.47 , pp. 1469-1479
    • Houston, J.B.1
  • 22
    • 1542344547 scopus 로고    scopus 로고
    • Predicting drug clearance from recombinantly expressed CYPs: Intersystem extrapolation factors
    • N. J. Proctor, G. T. Tucker, and A. Rostami-Hodjegan. Predicting drug clearance from recombinantly expressed CYPs: Intersystem extrapolation factors. Xenobiotica. 34:151-178 (2004).
    • (2004) Xenobiotica. , vol.34 , pp. 151-178
    • Proctor, N.J.1    Tucker, G.T.2    Rostami-Hodjegan, A.3
  • 23
    • 33645995117 scopus 로고    scopus 로고
    • Monospecific antipeptide antibodies against human hepatic UDP-glucuronosyltransferase 1A subfamily (UGT1A) isoforms
    • S.-I. Ikushiro, E. Yoshikazu, K. Yoshihisa, S. Yamada, and T. Sakaki. Monospecific antipeptide antibodies against human hepatic UDP-glucuronosyltransferase 1A subfamily (UGT1A) isoforms. Drug Metab. Pharmacokinet. 21:70-74 (2006).
    • (2006) Drug Metab. Pharmacokinet. , vol.21 , pp. 70-74
    • Ikushiro, S.-I.1    Yoshikazu, E.2    Yoshihisa, K.3    Yamada, S.4    Sakaki, T.5
  • 24
    • 0036890353 scopus 로고    scopus 로고
    • Complexities of glucuronidation affecting in vitro - In vivo extrapolation
    • J. H. Lin, and B. K. Wong. Complexities of glucuronidation affecting in vitro - in vivo extrapolation. Curr. Drug Metab. 3:623-646 (2002).
    • (2002) Curr. Drug Metab. , vol.3 , pp. 623-646
    • Lin, J.H.1    Wong, B.K.2
  • 25
    • 0035197725 scopus 로고    scopus 로고
    • Interindividual variability in acetaminophen glucuronidation by human liver microsomes: Identification of relevant acetaminophen UDP-glucuronosyltransferase isoforms
    • M. H. Court, S. X. Duan, L. L. Von Moltke, D. J. Greenblatt, C. J. Patten, J. O. Miners, and P. I. MacKenzie. Interindividual variability in acetaminophen glucuronidation by human liver microsomes: identification of relevant acetaminophen UDP-glucuronosyltransferase isoforms. J. Pharmacol. Exp. Ther. 299:998-1006 (2001).
    • (2001) J. Pharmacol. Exp. Ther. , vol.299 , pp. 998-1006
    • Court, M.H.1    Duan, S.X.2    Von Moltke, L.L.3    Greenblatt, D.J.4    Patten, C.J.5    Miners, J.O.6    MacKenzie, P.I.7
  • 26
    • 4744368269 scopus 로고    scopus 로고
    • Abundance of cytochromes P450 in human liver: A meta-analysis
    • K. R. Yeo, A. Rostami-Hodjegan, and G. T. Tucker. Abundance of cytochromes P450 in human liver: A meta-analysis. Br. J. Clin. Pharmacol. 57:687-688 (2004).
    • (2004) Br. J. Clin. Pharmacol. , vol.57 , pp. 687-688
    • Yeo, K.R.1    Rostami-Hodjegan, A.2    Tucker, G.T.3
  • 27
    • 0038685671 scopus 로고    scopus 로고
    • Validation of serotonin (5-hydrosytryptamine) as an in vitro substrate probe for human UDP-glucuronosyltransferase (UGT) 1A6
    • S. Krishnaswamy, S. X. Duan, L. L. Von Moltke, D. J. Greenblatt, and M. H. Court. Validation of serotonin (5-hydrosytryptamine) as an in vitro substrate probe for human UDP-glucuronosyltransferase (UGT) 1A6. Drug Metab. Disp. 31:133-139 (2003).
    • (2003) Drug Metab. Disp. , vol.31 , pp. 133-139
    • Krishnaswamy, S.1    Duan, S.X.2    Von Moltke, L.L.3    Greenblatt, D.J.4    Court, M.H.5
  • 28
    • 0033661491 scopus 로고    scopus 로고
    • Tissue distribution and interindividual variation in human UDP-glucuronosyltransferase activity: Relationship between UGT1A1 promoter genotype and variability in a liver bank
    • M. B. Fisher, M. Vandenbranden, K. Findlay, B. Burchell, K. E. Thummel, S. D. Hall, and S. A. Wrighton. Tissue distribution and interindividual variation in human UDP-glucuronosyltransferase activity: Relationship between UGT1A1 promoter genotype and variability in a liver bank. Pharmacogenetics. 10:727-739 (2000).
    • (2000) Pharmacogenetics. , vol.10 , pp. 727-739
    • Fisher, M.B.1    Vandenbranden, M.2    Findlay, K.3    Burchell, B.4    Thummel, K.E.5    Hall, S.D.6    Wrighton, S.A.7
  • 29
    • 0034680792 scopus 로고    scopus 로고
    • Polymorphic gene regulation and interindividual variation of UDP-glucuronosyltransferase activity in human small intestine
    • C. P. Strassburg, S. Kneip, J. Topp, P. Obermayer-Straub, A. Barutt, R. H. Turkey, and M. P. Manns. Polymorphic gene regulation and interindividual variation of UDP-glucuronosyltransferase activity in human small intestine. J. Biol. Chem. 46a:36164-36171 (2000).
    • (2000) J. Biol. Chem. , vol.46 a , pp. 36164-36171
    • Strassburg, C.P.1    Kneip, S.2    Topp, J.3    Obermayer-Straub, P.4    Barutt, A.5    Turkey, R.H.6    Manns, M.P.7
  • 30
    • 0028223564 scopus 로고
    • Evidence for the intraluminal positioning of p-nitrol UDP-glucuronosyltransferase activity in rat liver microsomes
    • R. Fulceri, G. Banhegyi, A. Gamberucci, R. Giunti, J. Mandl, and A. Benedetti. Evidence for the intraluminal positioning of p-nitrol UDP-glucuronosyltransferase activity in rat liver microsomes. Arch. Biochem. Biophys. 309:43-46 (1994).
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 43-46
    • Fulceri, R.1    Banhegyi, G.2    Gamberucci, A.3    Giunti, R.4    Mandl, J.5    Benedetti, A.6
  • 31
    • 0034009448 scopus 로고    scopus 로고
    • In vitro glucuronidation using human liver microsomes and the pore-forming peptide alamethicin
    • M. B. Fisher, K. Campanale, B. L. Ackermann, M. Banderbranden, and S. A. Wrighton. In vitro glucuronidation using human liver microsomes and the pore-forming peptide alamethicin. Drug Metab. Disp. 25:560-566 (2000).
    • (2000) Drug Metab. Disp. , vol.25 , pp. 560-566
    • Fisher, M.B.1    Campanale, K.2    Ackermann, B.L.3    Banderbranden, M.4    Wrighton, S.A.5
  • 33
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • K. He, S. J. Ludtke, W. T. Heller, and H. W. Huang. Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71:2669-2679 (1996).
    • (1996) Biophys. J. , vol.71 , pp. 2669-2679
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 34
    • 0026602510 scopus 로고
    • Optimal detergent activation of rat liver microsomal UDP-glucuronosyltransferases toward morphine and 1-naphthol: Contribution to induction and latency studies
    • E. Lett, W. Kriszt, V. de Sandro, G. Ducrotoy, and L. Richert. Optimal detergent activation of rat liver microsomal UDP-glucuronosyltransferases toward morphine and 1-naphthol: contribution to induction and latency studies. Biochem. Pharmacol. 43:1649-1653 (1992).
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1649-1653
    • Lett, E.1    Kriszt, W.2    de Sandro, V.3    Ducrotoy, G.4    Richert, L.5
  • 35
    • 0031808472 scopus 로고    scopus 로고
    • Glucuronidation of 3¢-azido-3¢-deoxythymidine (zidovudine) by human liver microsomes-relevance to clinical pharmacokinetic interactions with atovaquone, fluconazole, methadone and valproic acid
    • C. B. Trapnell, R. W. Klecker, C. Jamis-Dow, and J. M. Colling. Glucuronidation of 3¢-azido-3¢-deoxythymidine (zidovudine) by human liver microsomes-relevance to clinical pharmacokinetic interactions with atovaquone, fluconazole, methadone and valproic acid. Antimicrob. Agents Chemother. 42:1592-1596 (1998).
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1592-1596
    • Trapnell, C.B.1    Klecker, R.W.2    Jamis-Dow, C.3    Colling, J.M.4
  • 36
    • 32944455130 scopus 로고    scopus 로고
    • Monoclonal Antibodies and Multifunctional Cytochrome P450: Drug Metabolism as Paradigm
    • H. V. Gelboin, and K. Krausz. Monoclonal Antibodies and Multifunctional Cytochrome P450: Drug Metabolism as Paradigm. J. Clin. Pharmacol. 46:353-372 (2006).
    • (2006) J. Clin. Pharmacol. , vol.46 , pp. 353-372
    • Gelboin, H.V.1    Krausz, K.2
  • 39
    • 0028362263 scopus 로고
    • Characterization of the inhibition of P4501A2 by furafylline
    • S. E. Clarke, A. D. Ayrton, and R. J. Chenery. Characterization of the inhibition of P4501A2 by furafylline. Xenobiotica. 24:517-526 (1994).
    • (1994) Xenobiotica. , vol.24 , pp. 517-526
    • Clarke, S.E.1    Ayrton, A.D.2    Chenery, R.J.3
  • 40
    • 0030430033 scopus 로고    scopus 로고
    • Cytochrome P450 isoform inhibitors as a tool for the investigation of metabolic reactions catalyzed by human liver microsomes
    • M. Bourrie, V. Meunier, Y. Berger, and G. Fabre. Cytochrome P450 isoform inhibitors as a tool for the investigation of metabolic reactions catalyzed by human liver microsomes. J. Pharmacol. Exp. Ther. 277:321-332 (1996).
    • (1996) J. Pharmacol. Exp. Ther. , vol.277 , pp. 321-332
    • Bourrie, M.1    Meunier, V.2    Berger, Y.3    Fabre, G.4
  • 41
    • 0030456054 scopus 로고    scopus 로고
    • Interaction of sulfaphenazole derivatives with human liver cytochromes P4502C: Molecular origin of the specific inhibitory effects of sulfaphenazole on CYP2C9 and consequences for the substrate binding site topology of CYP2C9
    • A. Mancy, S. Dijols, S. Poli, F. P. Guengerich, and D. Mansuy. Interaction of sulfaphenazole derivatives with human liver cytochromes P4502C: Molecular origin of the specific inhibitory effects of sulfaphenazole on CYP2C9 and consequences for the substrate binding site topology of CYP2C9. Biochemistry. 35:16205-16212 (1996).
    • (1996) Biochemistry , vol.35 , pp. 16205-16212
    • Mancy, A.1    Dijols, S.2    Poli, S.3    Guengerich, F.P.4    Mansuy, D.5
  • 42
    • 0036179579 scopus 로고    scopus 로고
    • (+)-N-3-benzyl-nirvanol and (-)-N-3-benzylphenobarbital: New potent and selective in vitro inhibitors of CYP2C19
    • H. Suzuki, M. B. Kneller, R. L. Haining, W. F. Trager, and A. E. Rettie. (+)-N-3-benzyl-nirvanol and (-)-N-3-benzylphenobarbital: New potent and selective in vitro inhibitors of CYP2C19. Drug Metab. Dispos. 30: 235-239 (2002).
    • (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
  • 43
    • 0037369493 scopus 로고    scopus 로고
    • Verification of the selectivity of (+)N-3-benzylnirvanol as a CYP2C19 inhibitor
    • R. L. Walsky, and R. S. Obach. Verification of the selectivity of (+)N-3-benzylnirvanol as a CYP2C19 inhibitor. Drug Metab. Dispos. 31:343 (2003).
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 343
    • Walsky, R.L.1    Obach, R.S.2
  • 44
    • 0028858960 scopus 로고
    • Cytochrome P450 inhibitors. Evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes
    • D. J. Newton, R. W. Wang, and A. Y. Lu. 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).
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 154-158
    • Newton, D.J.1    Wang, R.W.2    Lu, A.Y.3
  • 45
    • 0030996094 scopus 로고    scopus 로고
    • The in vitro interaction of dexmedetomidine with human liver microsomal cytochrome P4502D6 (CYP2D6)
    • A. D. Rodrigues, and E. M. Roberts. The in vitro interaction of dexmedetomidine with human liver microsomal cytochrome P4502D6 (CYP2D6). Drug Metab. Dispos. 25:651-655 (1997).
    • (1997) Drug Metab. Dispos. , vol.25 , pp. 651-655
    • Rodrigues, A.D.1    Roberts, E.M.2
  • 46
    • 0031769798 scopus 로고    scopus 로고
    • Comparative studies of in vitro inhibition of cytochrome P450 3A4-dependent testosterone 6beta-hydroxylation by roxithromycin and its metabolites, troleandomycin, and erythromycin
    • H. Yamazaki, and T. Shimada. Comparative studies of in vitro inhibition of cytochrome P450 3A4-dependent testosterone 6beta-hydroxylation by roxithromycin and its metabolites, troleandomycin, and erythromycin. Drug Metab. Dispos. 26:1053-1057 (1998).
    • (1998) Drug Metab. Dispos. , vol.26 , pp. 1053-1057
    • Yamazaki, H.1    Shimada, T.2
  • 47
    • 0027475692 scopus 로고
    • In vitro interaction between cyclosporin A and macrolide antibiotics
    • F. Marre, G. de Sousa, A. M. Orloff, and R. Rahmani. In vitro interaction between cyclosporin A and macrolide antibiotics. Br. J. Clin. Pharm. 35:447-448 (1993).
    • (1993) Br. J. Clin. Pharm. , vol.35 , pp. 447-448
    • Marre, F.1    de Sousa, G.2    Orloff, A.M.3    Rahmani, R.4


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