메뉴 건너뛰기




Volumn 39, Issue 4, 2011, Pages 644-652

Characterization of niflumic acid as a selective inhibitor of human liver microsomal UDP-glucuronosyltransferase 1A9: Application to the reaction phenotyping of acetaminophen glucuronidation

Author keywords

[No Author keywords available]

Indexed keywords

GLUCURONOSYLTRANSFERASE 1A1; GLUCURONOSYLTRANSFERASE 1A3; GLUCURONOSYLTRANSFERASE 1A4; GLUCURONOSYLTRANSFERASE 1A6; GLUCURONOSYLTRANSFERASE 1A9; GLUCURONOSYLTRANSFERASE 2B15; GLUCURONOSYLTRANSFERASE 2B17; GLUCURONOSYLTRANSFERASE 2B4; GLUCURONOSYLTRANSFERASE 2B7; HYMECROMONE; NIFLUMIC ACID; PARACETAMOL; PROPOFOL; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 79952819517     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.110.037036     Document Type: Article
Times cited : (97)

References (42)
  • 2
    • 0036435763 scopus 로고    scopus 로고
    • In vitro-in vivo correlations for drugs eliminated by glucuronidation: Investigations with the model substrate zidovudine
    • DOI 10.1046/j.1365-2125.2002.01669.x
    • Boase S and Miners JO (2002) In vitro-in vivo correlations for drugs eliminated by glucuronidation: investigations with the model substrate zidovudine. Br J Clin Pharmacol 54:493-503. (Pubitemid 35356875)
    • (2002) British Journal of Clinical Pharmacology , vol.54 , Issue.5 , pp. 493-503
    • Boase, S.1    Miners, J.O.2
  • 4
    • 33847383675 scopus 로고    scopus 로고
    • 4-3-keto C19- And C21-hydroxysteroids by human liver microsomal and recombinant UDP-glucuronosyltransferases (UGTs): 6α- and 21-hydroxyprogesterone are selective substrates for UGT2B7
    • DOI 10.1124/dmd.106.013052
    • Bowalgaha K, Elliot DJ, Mackenzie PI, Knights KM, and Miners JO (2007) The glucuronidation of Δ4-3-keto C19- and C21-hydroxysteroids by human liver microsomal and recombinant UDP-glucuronosyltransferases (UGTs): 6α- and 21-hydroxyprogesterone are selective substrates for UGT2B7. Drug Metab Dispos 35:363-370. (Pubitemid 46333898)
    • (2007) Drug Metabolism and Disposition , vol.35 , Issue.3 , pp. 363-370
    • Bowalgaha, K.1    Elliot, D.J.2    Mackenzie, P.I.3    Knights, K.M.4    Miners, J.O.5
  • 5
    • 26444551640 scopus 로고    scopus 로고
    • S-naproxen and desmethylnaproxen glucuronidation by human liver microsomes and recombinant human UDP-glucuronosyltransferases (UGT): Role of UGT2B7 in the elimination of naproxen
    • DOI 10.1111/j.1365-2125.2005.02446.x
    • Bowalgaha K, Elliot DJ, Mackenzie PI, Knights KM, Swedmark S, and Miners JO (2005) S-Naproxen and desmethylnaproxen glucuronidation by human liver microsomes and recombinant human UDP-glucuronosyltransferases (UGT): role of UGT2B7 in the elimination of naproxen. Br J Clin Pharmacol 60:423-433. (Pubitemid 41428474)
    • (2005) British Journal of Clinical Pharmacology , vol.60 , Issue.4 , pp. 423-433
    • Bowalgaha, K.1    Elliot, D.J.2    Mackenzie, P.I.3    Knights, K.M.4    Swedmark, S.5    Miners, J.O.6
  • 6
    • 30144436526 scopus 로고    scopus 로고
    • Isoform-selective probe substrates for in vitro studies of human UDP-glucuronosyltransferases
    • Court MH (2005) Isoform-selective probe substrates for in vitro studies of human UDP-glucuronosyltransferases. Methods Enzymol 400:104-116.
    • (2005) Methods Enzymol , vol.400 , pp. 104-116
    • Court, M.H.1
  • 7
    • 74549132748 scopus 로고    scopus 로고
    • Interindividual variability in hepatic drug glucuronidation: Studies into the role of age, sex, enzyme inducers, and genetic polymorphism using the human liver bank as a model system
    • Court MH (2010) Interindividual variability in hepatic drug glucuronidation: studies into the role of age, sex, enzyme inducers, and genetic polymorphism using the human liver bank as a model system. Drug Metab Rev 42:209-224.
    • (2010) Drug Metab Rev , vol.42 , pp. 209-224
    • Court, M.H.1
  • 9
    • 34047141016 scopus 로고    scopus 로고
    • Glucuronidation of fenamates: Kinetic studies using human kidney cortical microsomes and recombinant UDP-glucuronosyltransferase (UGT) 1A9 and 2B7
    • DOI 10.1016/j.bcp.2007.01.030, PII S0006295207000627
    • Gaganis P, Miners JO, and Knights KM (2007) Glucuronidation of fenamates: kinetic studies using human kidney cortical microsomes and recombinant UDP-glucuronosyltransferase (UGT) 1A9 and 2B7. Biochem Pharmacol 73:1683-1691. (Pubitemid 46527548)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.10 , pp. 1683-1691
    • Gaganis, P.1    Miners, J.O.2    Knights, K.M.3
  • 10
    • 0037819284 scopus 로고    scopus 로고
    • Pharmacogenomics of human UDP-glucuronosyltransferase enzymes
    • Guillemette C (2003) Pharmacogenomics of human UDP- glucuronosyltransferase enzymes. Pharmacogenomics J 3:136-158.
    • (2003) Pharmacogenomics J , vol.3 , pp. 136-158
    • Guillemette, C.1
  • 11
    • 54349124543 scopus 로고    scopus 로고
    • The configuration of the 17-hydroxy group variably influences the glucuronidation of β-estradiol and epiestradiol by human UDP-glucuronosyltransferases
    • Itäaho K, Mackenzie PI, Ikushiro S, Miners JO, and Finel M (2008) The configuration of the 17-hydroxy group variably influences the glucuronidation of β-estradiol and epiestradiol by human UDP-glucuronosyltransferases. Drug Metab Dispos 36:2307-2315.
    • (2008) Drug Metab Dispos , vol.36 , pp. 2307-2315
    • Itäaho, K.1    Mackenzie, P.I.2    Ikushiro, S.3    Miners, J.O.4    Finel, M.5
  • 12
    • 15244342411 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferases and clinical drug-drug interactions
    • DOI 10.1016/j.pharmthera.2004.10.013
    • Kiang TK, Ensom MH, and Chang TK (2005) UDP-glucuronosyltransferases and clinical drug-drug interactions. Pharmacol Ther 106:97-132. (Pubitemid 40386722)
    • (2005) Pharmacology and Therapeutics , vol.106 , Issue.1 , pp. 97-132
    • Kiang, T.K.L.1    Ensom, M.H.H.2    Chang, T.K.H.3
  • 13
    • 34748850636 scopus 로고    scopus 로고
    • Critical roles of residues 36 and 40 in the phenol and tertiary amine aglycone substrate selectivities of UDP-glucuronosyltransferases 1A3 and 1A4
    • DOI 10.1124/mol.107.037952
    • Kubota T, Lewis BC, Elliot DJ, Mackenzie PI, and Miners JO (2007) Critical roles of residues 36 and 40 in the phenol and tertiary amine aglycone substrate selectivities of UDP-glucuronosyltransferases 1A3 and 1A4. Mol Pharmacol 72:1054-1062. (Pubitemid 47481428)
    • (2007) Molecular Pharmacology , vol.72 , Issue.4 , pp. 1054-1062
    • Kubota, T.1    Lewis, B.C.2    Elliot, D.J.3    Mackenzie, P.I.4    Miners, J.O.5
  • 14
    • 6344248683 scopus 로고    scopus 로고
    • Specificity and regioselectivity of the conjugation of estradiol, estrone, and their catecholestrogen and methoxyestrogen metabolites by human uridine diphospho-glucuronosyltransferases expressed in endometrium
    • DOI 10.1210/jc.2004-0331
    • Lépine J, Bernard O, Plante M, Têtu B, Pelletier G, Labrie F, Bélanger A, and Guillemette C (2004) Specificity and regioselectivity of the conjugation of estradiol, estrone, and their catecholestrogen and methoxyestrogen metabolites by human uridine diphosphoglucuronosyltransferases expressed in endometrium. J Clin Endocrinol Metab 89:5222-5232. (Pubitemid 39391472)
    • (2004) Journal of Clinical Endocrinology and Metabolism , vol.89 , Issue.10 , pp. 5222-5232
    • Lepine, J.1    Bernard, O.2    Plante, M.3    Tetu, B.4    Pelletier, G.5    Labrie, F.6    Belanger, A.7    Guillemette, C.8
  • 15
    • 33947429721 scopus 로고    scopus 로고
    • Amino terminal domains of human UDP-glucuronosyltransferases (UGT) 2B7 and 2B15 associated with substrate selectivity and autoactivation
    • DOI 10.1016/j.bcp.2006.12.021, PII S0006295206008549
    • Lewis BC, Mackenzie PI, Elliot DJ, Burchell B, Bhasker CR, and Miners JO (2007) Amino terminal domains of human UDP-glucuronosyltransferases (UGT) 2B7 and 2B15 associated with substrate selectivity and autoactivation. Biochem Pharmacol 73:1463-1473. (Pubitemid 46452582)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.9 , pp. 1463-1473
    • Lewis, B.C.1    Mackenzie, P.I.2    Elliot, D.J.3    Burchell, B.4    Bhasker, C.R.5    Miners, J.O.6
  • 17
    • 33745595327 scopus 로고    scopus 로고
    • Identification of human UDP-glucuronosyltransferase responsible for the glucuronidation of niflumic acid in human liver
    • DOI 10.1007/s11095-006-0250-5
    • Mano Y, Usui T, and Kamimura H (2006a) Identification of human UDP-glucuronosyltransferase responsible for the glucuronidation of niflumic acid in human liver. Pharm Res 23:1502-1508. (Pubitemid 43993813)
    • (2006) Pharmaceutical Research , vol.23 , Issue.7 , pp. 1502-1508
    • Mano, Y.1    Usui, T.2    Kamimura, H.3
  • 18
    • 31744443743 scopus 로고    scopus 로고
    • In vitro inhibitory effects of non-steroidal anti-inflammatory drugs on 4-methylumbelliferone glucuronidation in recombinant human UDP- glucuronosyltransferase 1A9 - Potent inhibition by niflumic acid
    • DOI 10.1002/bdd.475
    • Mano Y, Usui T, and Kamimura H (2006b) In vitro inhibitory effects of non-steroidal anti-inflammatory drugs on 4-methylumbelliferone glucuronidation in recombinant human UDP-glucuronosyltransferase 1A9 - potent inhibition by niflumic acid. Biopharm Drug Dispos 27:1-6. (Pubitemid 43173968)
    • (2006) Biopharmaceutics and Drug Disposition , vol.27 , Issue.1 , pp. 1-6
    • Mano, Y.1    Usui, T.2    Kamimura, H.3
  • 19
    • 0021269529 scopus 로고
    • Determinants of acetaminophen metabolism: Effect of inducers and inhibitors of drug metabolism on acetaminophen's metabolic pathways
    • Miners JO, Attwood J, and Birkett DJ (1984) Determinants of acetaminophen metabolism: effect of inducers and inhibitors of drug metabolism on acetaminophen's metabolic pathways. Clin Pharmacol Ther 35:480-486. (Pubitemid 14133487)
    • (1984) Clinical Pharmacology and Therapeutics , vol.35 , Issue.4 , pp. 480-486
    • Miners, J.O.1    Attwood, J.2    Birkett, D.J.3
  • 20
    • 33646077674 scopus 로고    scopus 로고
    • In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: Pitfalls and promises
    • Miners JO, Knights KM, Houston JB, and Mackenzie PI (2006) In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: pitfalls and promises. Biochem Pharmacol 71:1531-1539.
    • (2006) Biochem Pharmacol , vol.71 , pp. 1531-1539
    • Miners, J.O.1    Knights, K.M.2    Houston, J.B.3    Mackenzie, P.I.4
  • 21
  • 22
    • 74549222703 scopus 로고    scopus 로고
    • The prediction of drug-glucuronidation parameters in humans: UDP-glucuronosyltransferase enzyme-selective substrate and inhibitor probes for reaction phenotyping and in vitro-in vivo extrapolation of drug clearance and drug-drug interaction potential
    • Miners JO, Mackenzie PI, and Knights KM (2010a) The prediction of drug-glucuronidation parameters in humans: UDP-glucuronosyltransferase enzyme-selective substrate and inhibitor probes for reaction phenotyping and in vitro-in vivo extrapolation of drug clearance and drug-drug interaction potential. Drug Metab Rev 42:196-208.
    • (2010) Drug Metab Rev , vol.42 , pp. 196-208
    • Miners, J.O.1    Mackenzie, P.I.2    Knights, K.M.3
  • 23
    • 0037184841 scopus 로고    scopus 로고
    • Genetic polymorphisms of UDP-glucuronosyltransferases and their functional significance
    • DOI 10.1016/S0300-483X(02)00449-3, PII S0300483X02004493
    • Miners JO, McKinnon RA, and Mackenzie PI (2002) Genetic polymorphisms of UDP-glucuronosyltransferases and their functional significance. Toxicology 181-182:453-456. (Pubitemid 36015736)
    • (2002) Toxicology , vol.181-182 , pp. 453-456
    • Miners, J.O.1    McKinnon, R.A.2    Mackenzie, P.I.3
  • 24
    • 79952831126 scopus 로고    scopus 로고
    • The in vitro characterization of inhibitory drug-drug interactions involving UDP-glucuronosyltransferase
    • Pang KS, Rodrigues AD, and Peter R eds Springer, New York
    • Miners JO, Polasek TM, Mackenzie PI, and Knights KM (2010b) The in vitro characterization of inhibitory drug-drug interactions involving UDP-glucuronosyltransferase, in Enzyme and Transporter Based Drug-Drug Interactions (Pang KS, Rodrigues AD, and Peter R eds), pp 217-236, Springer, New York.
    • (2010) Enzyme and Transporter Based Drug-Drug Interactions , pp. 217-236
    • Miners, J.O.1    Polasek, T.M.2    Mackenzie, P.I.3    Knights, K.M.4
  • 25
  • 26
    • 33744500475 scopus 로고    scopus 로고
    • Kinetics of acetaminophen glucuronidation by UDP-glucuronosyltransferases 1A1, 1A6, 1A9 and 2B15. Potential implications in acetaminophen-induced hepatotoxicity
    • DOI 10.1021/tx050317i
    • Mutlib AE, Goosen TC, Bauman JN, Williams JA, Kulkarni S, and Kostrubsky S (2006) Kinetics of acetaminophen glucuronidation by UDP- glucuronosyltransferases 1A1, 1A6, 1A9 and 2B15. Potential implications in acetaminophen-induced hepatotoxicity. Chem Res Toxicol 19:701-709. (Pubitemid 43800987)
    • (2006) Chemical Research in Toxicology , vol.19 , Issue.5 , pp. 701-709
    • Mutlib, A.E.1    Goosen, T.C.2    Bauman, J.N.3    Williams, J.A.4    Kulkarni, S.5    Kostrubsky, S.6
  • 27
    • 58149467072 scopus 로고    scopus 로고
    • Determination of mRNA expression of human UDP-glucuronosyltransferases and application for localization in various human tissues by real-time reverse transcriptase-polymerase chain reaction
    • Ohno S and Nakajin S (2009) Determination of mRNA expression of human UDP-glucuronosyltransferases and application for localization in various human tissues by real-time reverse transcriptase-polymerase chain reaction. Drug Metab Dispos 37:32-40.
    • (2009) Drug Metab Dispos , vol.37 , pp. 32-40
    • Ohno, S.1    Nakajin, S.2
  • 28
    • 77954896503 scopus 로고    scopus 로고
    • In vitro-in vivo extrapolation predicts drug-drug interactions arising from inhibition of codeine glucuronidation by dextropropoxyphene, fluconazole, ketoconazole, and methadone in humans
    • Raungrut P, Uchaipichat V, Elliot DJ, Janchawee B, Somogyi AA, and Miners JO (2010) In vitro-in vivo extrapolation predicts drug-drug interactions arising from inhibition of codeine glucuronidation by dextropropoxyphene, fluconazole, ketoconazole, and methadone in humans. J Pharmacol Exp Ther 334:609-618.
    • (2010) J Pharmacol Exp Ther , vol.334 , pp. 609-618
    • Raungrut, P.1    Uchaipichat, V.2    Elliot, D.J.3    Janchawee, B.4    Somogyi, A.A.5    Miners, J.O.6
  • 30
    • 33947398317 scopus 로고    scopus 로고
    • Binding of inhibitory fatty acids is responsible for the enhancement of UDP-glucuronosyltransferase 2B7 activity by albumin: Implications for in vitro-in vivo extrapolation
    • DOI 10.1124/jpet.106.118216
    • Rowland A, Gaganis P, Elliot DJ, Mackenzie PI, Knights KM, and Miners JO (2007) Binding of inhibitory fatty acids is responsible for the enhancement of UDP-glucuronosyltransferase 2B7 activity by albumin: implications for in vitro-in vivo extrapolation. J Pharmacol Exp Ther 321:137-147. (Pubitemid 46456976)
    • (2007) Journal of Pharmacology and Experimental Therapeutics , vol.321 , Issue.1 , pp. 137-147
    • Rowland, A.1    Gaganis, P.2    Elliot, D.J.3    Mackenzie, P.I.4    Knights, K.M.5    Miners, J.O.6
  • 31
    • 44149117018 scopus 로고    scopus 로고
    • The "albumin effect" and drug glucuronidation: Bovine serum albumin and fatty acid-free human serum albumin enhance the glucuronidation of UDP-glucuronosyltransferase (UGT) 1A9 substrates but not UGT1A1 and UGT1A6 activities
    • DOI 10.1124/dmd.108.021105
    • Rowland A, Knights KM, Mackenzie PI, and Miners JO (2008) The "albumin effect" and drug glucuronidation: bovine serum albumin and fatty acid-free human serum albumin enhance the glucuronidation of UDP-glucuronosyltransferase (UGT) 1A9 substrates but not UGT1A1 and UGT1A6 activities. Drug Metab Dispos 36:1056-1062. (Pubitemid 351717462)
    • (2008) Drug Metabolism and Disposition , vol.36 , Issue.6 , pp. 1056-1062
    • Rowland, A.1    Knights, K.M.2    Mackenzie, P.I.3    Miners, J.O.4
  • 33
    • 0038532316 scopus 로고    scopus 로고
    • The effect of incubation conditions on the enzyme kinetics of UDP-glucuronosyltransferases
    • Soars MG, Ring BJ, and Wrighton SA (2003) The effect of incubation conditions on the enzyme kinetics of UDP-glucuronosyltransferases. Drug Metab Dispos 31:762-767. (Pubitemid 36617665)
    • (2003) Drug Metabolism and Disposition , vol.31 , Issue.6 , pp. 762-767
    • Soars, M.G.1    Ring, B.J.2    Wrighton, S.A.3
  • 34
    • 0042679455 scopus 로고    scopus 로고
    • Isoform selectivity and kinetics of morphine 3- And 6-glucuronidation by human UDP-glucuronosyltransferases: Evidence for atypical glucuronidation kinetics by UGT2B7
    • DOI 10.1124/dmd.31.9.1086
    • Stone AN, Mackenzie PI, Galetin A, Houston JB, and Miners JO (2003) Isoform selectivity and kinetics of morphine 3- and 6-glucuronidation by human UDP-glucuronosyltransferases: evidence for atypical glucuronidation kinetics by UGT2B7. Drug Metab Dispos 31:1086-1089. (Pubitemid 37048278)
    • (2003) Drug Metabolism and Disposition , vol.31 , Issue.9 , pp. 1086-1089
    • Stone, A.N.1    Mackenzie, P.I.2    Galetin, A.3    Houston, J.B.4    Miners, J.O.5
  • 35
    • 52949103260 scopus 로고    scopus 로고
    • Kinetic modeling of the interactions between 4-methylumbelliferone, 1-naphthol, and zidovudine glucuronidation by UDP-glucuronosyltransferase 2B7 (UGT2B7) provides evidence for multiple substrate binding and effector sites
    • Uchaipichat V, Galetin A, Houston JB, Mackenzie PI, Williams JA, and Miners JO (2008) Kinetic modeling of the interactions between 4-methylumbelliferone, 1-naphthol, and zidovudine glucuronidation by UDP-glucuronosyltransferase 2B7 (UGT2B7) provides evidence for multiple substrate binding and effector sites. Mol Pharmacol 74:1152-1162.
    • (2008) Mol Pharmacol , vol.74 , pp. 1152-1162
    • Uchaipichat, V.1    Galetin, A.2    Houston, J.B.3    Mackenzie, P.I.4    Williams, J.A.5    Miners, J.O.6
  • 36
    • 33344473930 scopus 로고    scopus 로고
    • Selectivity of substrate (trifluoperazine) and inhibitor (amitriptyline, androsterone, canrenoic acid, hecogenin, phenylbutazone, quinidine, quinine, and sulfinpyrazone) "probes" for human UDP-glucuronosyltransferases
    • Uchaipichat V, Mackenzie PI, Elliot DJ, and Miners JO (2006a) Selectivity of substrate (trifluoperazine) and inhibitor (amitriptyline, androsterone, canrenoic acid, hecogenin, phenylbutazone, quinidine, quinine, and sulfinpyrazone) "probes" for human UDP-glucuronosyltransferases. Drug Metab Dispos 34:449-456.
    • (2006) Drug Metab Dispos , vol.34 , pp. 449-456
    • Uchaipichat, V.1    Mackenzie, P.I.2    Elliot, D.J.3    Miners, J.O.4
  • 37
    • 1842536833 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid
    • DOI 10.1124/dmd.32.4.413
    • Uchaipichat V, Mackenzie PI, Guo XH, Gardner-Stephen D, Galetin A, Houston JB, and Miners JO (2004) Human UDP-glucuronosyltransferases: isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid. Drug Metab Dispos 32:413-423. (Pubitemid 38420275)
    • (2004) Drug Metabolism and Disposition , vol.32 , Issue.4 , pp. 413-423
    • Uchaipichat, V.1    Mackenzie, P.I.2    Guo, X.-H.3    Gardner-Stephen, D.4    Galetin, A.5    Houston, J.B.6    Miners, J.O.7
  • 38
    • 33344478229 scopus 로고    scopus 로고
    • Quantitative prediction of in vivo inhibitory interactions involving glucuronidated drugs from in vitro data: The effect of fluconazole on zidovudine glucuronidation
    • Uchaipichat V, Winner LK, Mackenzie PI, Elliot DJ, Williams JA, and Miners JO (2006b) Quantitative prediction of in vivo inhibitory interactions involving glucuronidated drugs from in vitro data: the effect of fluconazole on zidovudine glucuronidation. Br J Clin Pharmacol 61:427-439.
    • (2006) Br J Clin Pharmacol , vol.61 , pp. 427-439
    • Uchaipichat, V.1    Winner, L.K.2    Mackenzie, P.I.3    Elliot, D.J.4    Williams, J.A.5    Miners, J.O.6
  • 39
    • 34748822655 scopus 로고    scopus 로고
    • Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of bilirubin and other UDP-glucuronosyltransferase 1A substrates
    • DOI 10.1097/FPC.0b013e328256b1b6, PII 0121301120071200000002
    • Udomuksorn W, Elliot DJ, Lewis BC, Mackenzie PI, Yoovathaworn K, and Miners JO (2007) Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of bilirubin and other UDP-glucuronosyltransferase 1A substrates. Pharmacogenet Genomics 17:1017-1029. (Pubitemid 351339486)
    • (2007) Pharmacogenetics and Genomics , vol.17 , Issue.12 , pp. 1017-1029
    • Udomuksorn, W.1    Elliot, D.J.2    Lewis, B.C.3    Mackenzie, P.I.4    Yoovathaworn, K.5    Miners, J.O.6
  • 40
    • 0036249921 scopus 로고    scopus 로고
    • Inhibition of mycophenolic acid glucuronidation by niflumic acid in human liver microsomes
    • Vietri M, Pietrabissa A, Mosca F, and Pacifici GM (2002) Inhibition of mycophenolic acid glucuronidation by niflumic acid in human liver microsomes. Eur J Clin Pharmacol 58:93-97.
    • (2002) Eur J Clin Pharmacol , vol.58 , pp. 93-97
    • Vietri, M.1    Pietrabissa, A.2    Mosca, F.3    Pacifici, G.M.4
  • 41
    • 0036843701 scopus 로고    scopus 로고
    • Differential modulation of UDP-glucuronosyltransferase 1A1 (UGT1A1)-catalyzed estradiol-3-glucuronidation by the addition of UGT1A1 substrates and other compounds to human liver microsomes
    • DOI 10.1124/dmd.30.11.1266
    • Williams JA, Ring BJ, Cantrell VE, Campanale K, Jones DR, Hall SD, and Wrighton SA (2002) Differential modulation of UDP-glucuronosyltransferase 1A1 (UGT1A1)-catalyzed estradiol-3-glucuronidation by the addition of UGT1A1 substrates and other compounds to human liver microsomes. Drug Metab Dispos 30:1266-1273. (Pubitemid 35265835)
    • (2002) Drug Metabolism and Disposition , vol.30 , Issue.11 , pp. 1266-1273
    • Andrew, W.J.1    Ring, B.J.2    Cantrell, V.E.3    Campanale, K.4    Jones, D.R.5    Hall, S.D.6    Wrighton, S.A.7
  • 42
    • 76749137214 scopus 로고    scopus 로고
    • Glucuronidation of dihydrotestosterone and transandrosterone by recombinant UDP-glucuronosyltransferase (UGT) 1A4: Evidence for multiple UGT1A4 aglycone binding sites
    • Zhou J, Tracy TS, and Remmel RP (2010) Glucuronidation of dihydrotestosterone and transandrosterone by recombinant UDP- glucuronosyltransferase (UGT) 1A4: evidence for multiple UGT1A4 aglycone binding sites. Drug Metab Dispos 38:431-440.
    • (2010) Drug Metab Dispos , vol.38 , pp. 431-440
    • Zhou, J.1    Tracy, T.S.2    Remmel, R.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.