메뉴 건너뛰기




Volumn 57, Issue 14, 2014, Pages 6183-6196

Flavin monooxygenase metabolism: Why medicinal chemists should matter

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450 3A4; FLAVIN MONOOXYGENASE; QUERCETIN; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; XENOBIOTIC AGENT;

EID: 84904988793     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm5007098     Document Type: Article
Times cited : (40)

References (61)
  • 1
    • 0034280122 scopus 로고    scopus 로고
    • Human flavin-containing monooxygenase: Substrate specificity and role in drug metabolism
    • Cashman, J. R. Human flavin-containing monooxygenase: substrate specificity and role in drug metabolism Curr. Drug Metab. 2000, 1, 181-191
    • (2000) Curr. Drug Metab. , vol.1 , pp. 181-191
    • Cashman, J.R.1
  • 3
    • 0013943627 scopus 로고
    • Microsomal oxidases. I the isolation and dialkylarylamine oxygenase activity of pork liver microsomes
    • Ziegler, D. M.; Pettit, F. H. Microsomal oxidases. I. The isolation and dialkylarylamine oxygenase activity of pork liver microsomes Biochemistry 1966, 5, 2932-2938
    • (1966) Biochemistry , vol.5 , pp. 2932-2938
    • Ziegler, D.M.1    Pettit, F.H.2
  • 4
    • 84861646776 scopus 로고    scopus 로고
    • Reactions and enzymes in the metabolism of drugs and other xenobiotics
    • Testa, B.; Pedretti, A.; Vistoli, G. Reactions and enzymes in the metabolism of drugs and other xenobiotics Drug Discovery Today 2012, 17, 549-560
    • (2012) Drug Discovery Today , vol.17 , pp. 549-560
    • Testa, B.1    Pedretti, A.2    Vistoli, G.3
  • 5
    • 84875163069 scopus 로고    scopus 로고
    • Pharmacokinetics, metabolism, and excretion of the antiviral drug arbidol in humans
    • Deng, P.; Zhong, D.; Yu, K.; Zhang, Y.; Wang, T.; Chen, X. Pharmacokinetics, metabolism, and excretion of the antiviral drug arbidol in humans Antimicrob. Agents Chemother. 2013, 57, 1743-1755
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 1743-1755
    • Deng, P.1    Zhong, D.2    Yu, K.3    Zhang, Y.4    Wang, T.5    Chen, X.6
  • 6
    • 77954416525 scopus 로고    scopus 로고
    • Benzydamine as a useful substrate of hepatic flavin-containing monooxygenase activity in veterinary species
    • Capolongo, F.; Santi, A.; Anfossi, P.; Montesissa, C. Benzydamine as a useful substrate of hepatic flavin-containing monooxygenase activity in veterinary species J. Vet. Pharmacol. Ther. 2009, 33, 341-346
    • (2009) J. Vet. Pharmacol. Ther. , vol.33 , pp. 341-346
    • Capolongo, F.1    Santi, A.2    Anfossi, P.3    Montesissa, C.4
  • 7
    • 84861605139 scopus 로고    scopus 로고
    • Expression of recombinant human flavin monooxygenase and moclobemide- N -oxide synthesis on multi-mg scale
    • Hanlon, S. P.; Camattari, A.; Abad, S.; Glieder, A.; Kittelmann, M.; Lütz, S.; Wirz, B.; Winkler, M. Expression of recombinant human flavin monooxygenase and moclobemide- N -oxide synthesis on multi-mg scale Chem. Commun. 2012, 48, 6001-6003
    • (2012) Chem. Commun. , vol.48 , pp. 6001-6003
    • Hanlon, S.P.1    Camattari, A.2    Abad, S.3    Glieder, A.4    Kittelmann, M.5    Lütz, S.6    Wirz, B.7    Winkler, M.8
  • 8
    • 0033820669 scopus 로고    scopus 로고
    • The involvement of flavin-containing monooxygenase but not CYP3A4 in metabolism of itopride hydrochloride, a gastroprokinetic agent: Comparison with cisapride and mosapride citrate
    • Mushiroda, T.; Douya, R.; Takahara, E.; Nagata, O. The involvement of flavin-containing monooxygenase but not CYP3A4 in metabolism of itopride hydrochloride, a gastroprokinetic agent: comparison with cisapride and mosapride citrate Drug Metab. Dispos. 2000, 28, 1231-1237
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 1231-1237
    • Mushiroda, T.1    Douya, R.2    Takahara, E.3    Nagata, O.4
  • 9
    • 0033763393 scopus 로고    scopus 로고
    • Oxidation of ranitidine by isozymes of flavin-containing monooxygenase and cytochrome P450
    • Chung, W. G.; Park, C. S.; Roh, H. K.; Lee, W. K.; Cha, Y. N. Oxidation of ranitidine by isozymes of flavin-containing monooxygenase and cytochrome P450 Jpn. J. Pharmacol. 2000, 84, 213-220
    • (2000) Jpn. J. Pharmacol. , vol.84 , pp. 213-220
    • Chung, W.G.1    Park, C.S.2    Roh, H.K.3    Lee, W.K.4    Cha, Y.N.5
  • 10
    • 84882240094 scopus 로고    scopus 로고
    • Pharmacogenetics of olanzapine metabolism
    • Söderberg, M. M.; Dahl, M. L. Pharmacogenetics of olanzapine metabolism Pharmacogenomics 2013, 14, 1319-1336
    • (2013) Pharmacogenomics , vol.14 , pp. 1319-1336
    • Söderberg, M.M.1    Dahl, M.L.2
  • 12
    • 0032874277 scopus 로고    scopus 로고
    • Flavin-containing monooxygenase-mediated N-oxidation of the M(1)-muscarinic agonist xanomeline
    • Ring, B. J.; Wrighton, S. A.; Aldridge, S. L.; Hansen, K.; Haehner, B.; Shipley, L. A. Flavin-containing monooxygenase-mediated N-oxidation of the M(1)-muscarinic agonist xanomeline Drug Metab. Dispos. 1999, 27, 1099-1103
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 1099-1103
    • Ring, B.J.1    Wrighton, S.A.2    Aldridge, S.L.3    Hansen, K.4    Haehner, B.5    Shipley, L.A.6
  • 13
    • 0027160817 scopus 로고
    • Tertiary amines related to brompheniramine: Preferred conformations for N-oxygenation by the hog liver flavin-containing monooxygenase
    • Cashman, J. R.; Celestial, J. R.; Leach, A.; Newdoll, J.; Park, S. B. Tertiary amines related to brompheniramine: preferred conformations for N-oxygenation by the hog liver flavin-containing monooxygenase Pharm. Res. 1993, 10, 1097-1105
    • (1993) Pharm. Res. , vol.10 , pp. 1097-1105
    • Cashman, J.R.1    Celestial, J.R.2    Leach, A.3    Newdoll, J.4    Park, S.B.5
  • 15
    • 0032188794 scopus 로고    scopus 로고
    • Modulation of human flavin-containing monooxygenase 3 activity by tricyclic antidepressants and other agents: Importance of residue 428
    • Adali, O.; Carver, G. C.; Philpot, R. M. Modulation of human flavin-containing monooxygenase 3 activity by tricyclic antidepressants and other agents: importance of residue 428 Arch. Biochem. Biophys. 1998, 358, 92-97
    • (1998) Arch. Biochem. Biophys. , vol.358 , pp. 92-97
    • Adali, O.1    Carver, G.C.2    Philpot, R.M.3
  • 16
    • 33845929539 scopus 로고    scopus 로고
    • Identification of human cytochrome p450 isozymes involved in diphenhydramine N-demethylation
    • Akutsu, T.; Kobayashi, K.; Sakurada, K.; Ikegaya, H.; Furihata, T.; Chiba, K. Identification of human cytochrome p450 isozymes involved in diphenhydramine N-demethylation Drug Metab. Dispos. 2007, 35, 72-78
    • (2007) Drug Metab. Dispos. , vol.35 , pp. 72-78
    • Akutsu, T.1    Kobayashi, K.2    Sakurada, K.3    Ikegaya, H.4    Furihata, T.5    Chiba, K.6
  • 17
    • 0023894686 scopus 로고
    • Flavin-containing monooxygenases: Catalytic mechanism and substrate specificities
    • Ziegler, D. M. Flavin-containing monooxygenases: catalytic mechanism and substrate specificities Drug Metab. Rev. 1988, 19, 1-32
    • (1988) Drug Metab. Rev. , vol.19 , pp. 1-32
    • Ziegler, D.M.1
  • 18
    • 19444375492 scopus 로고    scopus 로고
    • Mammalian flavin-containing monooxygenases: Structure/function, genetic polymorphisms and role in drug metabolism
    • Krueger, S. K.; Williams, D. E. Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism Pharmacol. Ther. 2005, 106, 357-387
    • (2005) Pharmacol. Ther. , vol.106 , pp. 357-387
    • Krueger, S.K.1    Williams, D.E.2
  • 20
    • 84867493875 scopus 로고    scopus 로고
    • Construction and consensus performance of (Q)SAR models for predicting phospholipidosis using a dataset of 743 compounds
    • Orogo, A. M.; Choi, S. S.; Minnier, B. L.; Kruhlak, N. L. Construction and consensus performance of (Q)SAR models for predicting phospholipidosis using a dataset of 743 compounds Mol. Inf. 2012, 31, 725-739
    • (2012) Mol. Inf. , vol.31 , pp. 725-739
    • Orogo, A.M.1    Choi, S.S.2    Minnier, B.L.3    Kruhlak, N.L.4
  • 21
    • 80052810835 scopus 로고    scopus 로고
    • Predicting phospholipidosis: A fluorescence non cell based in vitro assay for the determination of drug phospholipid complex formation in early drug discovery
    • Zhou, L.; Geraci, G.; Hess, S.; Yang, L.; Wang, J.; Argikar, U. Predicting phospholipidosis: a fluorescence non cell based in vitro assay for the determination of drug phospholipid complex formation in early drug discovery Anal. Chem. 2011, 83, 6980-6987
    • (2011) Anal. Chem. , vol.83 , pp. 6980-6987
    • Zhou, L.1    Geraci, G.2    Hess, S.3    Yang, L.4    Wang, J.5    Argikar, U.6
  • 23
    • 0033066470 scopus 로고    scopus 로고
    • Identification of cytochrome P450 enzymes involved in the metabolism of zotepine, an antipsychotic drug, in human liver microsomes
    • Shiraga, T.; Kaneko, H.; Iwasaki, K.; Tozuka, Z.; Suzuki, A.; Hata, T. Identification of cytochrome P450 enzymes involved in the metabolism of zotepine, an antipsychotic drug, in human liver microsomes Xenobiotica 1999, 29, 217-229
    • (1999) Xenobiotica , vol.29 , pp. 217-229
    • Shiraga, T.1    Kaneko, H.2    Iwasaki, K.3    Tozuka, Z.4    Suzuki, A.5    Hata, T.6
  • 24
    • 33845925755 scopus 로고    scopus 로고
    • The metabolomics of (+/-)-arecoline 1-oxide in the mouse and its formation by human flavin-containing monooxygenases
    • Giri, S.; Krausz, K. W.; Idle, J. R.; Gonzalez, F. J. The metabolomics of (+/-)-arecoline 1-oxide in the mouse and its formation by human flavin-containing monooxygenases Biochem. Pharmacol. 2007, 73, 561-573
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 561-573
    • Giri, S.1    Krausz, K.W.2    Idle, J.R.3    Gonzalez, F.J.4
  • 25
    • 0033047284 scopus 로고    scopus 로고
    • In vitro metabolism of the m1-muscarinic agonist 5-(2-ethyl-2 H -tetrazol-5-yl)-1-methyl-1,2,3,6-tetrahydropyridine by human hepatic cytochromes p-450 determined at pH 7.4 and 8.5
    • Jensen, K. G.; Dalgaard, L. In vitro metabolism of the m1-muscarinic agonist 5-(2-ethyl-2 H -tetrazol-5-yl)-1-methyl-1,2,3,6-tetrahydropyridine by human hepatic cytochromes p-450 determined at pH 7.4 and 8.5 Drug Metab. Dispos. 1999, 27, 125-132
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 125-132
    • Jensen, K.G.1    Dalgaard, L.2
  • 26
    • 0030886020 scopus 로고    scopus 로고
    • N-oxygenation of phenethylamine to the trans -oxime by adult human liver flavin-containing monooxygenase and retroreduction of phenethylamine hydroxylamine by human liver microsomes
    • Lin, J.; Cashman, J. R. N-oxygenation of phenethylamine to the trans -oxime by adult human liver flavin-containing monooxygenase and retroreduction of phenethylamine hydroxylamine by human liver microsomes J. Pharmacol. Exp. Ther. 1997, 282, 1269-1279
    • (1997) J. Pharmacol. Exp. Ther. , vol.282 , pp. 1269-1279
    • Lin, J.1    Cashman, J.R.2
  • 27
    • 4744373354 scopus 로고    scopus 로고
    • Hydrogen bonding interactions of covalently bonded fluorine atoms: From crystallographic data to a new angular function in the GRID force field
    • Carosati, E.; Sciabola, S.; Cruciani, G. Hydrogen bonding interactions of covalently bonded fluorine atoms: from crystallographic data to a new angular function in the GRID force field J. Med. Chem. 2004, 47, 5114-5125
    • (2004) J. Med. Chem. , vol.47 , pp. 5114-5125
    • Carosati, E.1    Sciabola, S.2    Cruciani, G.3
  • 29
    • 84863294154 scopus 로고    scopus 로고
    • Identification of enzymes responsible for the N-oxidation of darexaban glucuronide, the pharmacologically active metabolite of darexaban, and the glucuronidation of darexaban N-oxides in human liver microsomes
    • Shiraga, T.; Yajima, K.; Teragaki, T.; Suzuki, K.; Hashimoto, T.; Iwatsubo, T.; Miyashita, A.; Usui, T. Identification of enzymes responsible for the N-oxidation of darexaban glucuronide, the pharmacologically active metabolite of darexaban, and the glucuronidation of darexaban N-oxides in human liver microsomes Biol. Pharm. Bull. 2012, 35, 413-421
    • (2012) Biol. Pharm. Bull. , vol.35 , pp. 413-421
    • Shiraga, T.1    Yajima, K.2    Teragaki, T.3    Suzuki, K.4    Hashimoto, T.5    Iwatsubo, T.6    Miyashita, A.7    Usui, T.8
  • 30
    • 0033791657 scopus 로고    scopus 로고
    • In vitro evaluation of the disposition of A novel cysteine protease inhibitor
    • Jacobsen, W.; Christians, U.; Benet, L. Z. In vitro evaluation of the disposition of A novel cysteine protease inhibitor Drug Metab. Dispos. 2000, 28, 1343-1351
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 1343-1351
    • Jacobsen, W.1    Christians, U.2    Benet, L.Z.3
  • 31
    • 1642498339 scopus 로고    scopus 로고
    • S-oxidation of S-methyl-esonarimod by flavin-containing monooxygenases in human liver microsomes
    • Ohmi, N.; Yoshida, H.; Endo, H.; Hasegawa, M.; Akimoto, M.; Higuchi, S. S-oxidation of S-methyl-esonarimod by flavin-containing monooxygenases in human liver microsomes Xenobiotica 2003, 33, 1221-1231
    • (2003) Xenobiotica , vol.33 , pp. 1221-1231
    • Ohmi, N.1    Yoshida, H.2    Endo, H.3    Hasegawa, M.4    Akimoto, M.5    Higuchi, S.6
  • 32
    • 84864713877 scopus 로고    scopus 로고
    • Regioselective oxidation of phospho-NSAIDs by human cytochrome P450 and flavin monooxygenase isoforms: Implications for their pharmacokinetic properties and safety
    • Xie, G.; Wong, C. C.; Cheng, K. W.; Huang, L.; Constantinides, P. P.; Rigas, B. Regioselective oxidation of phospho-NSAIDs by human cytochrome P450 and flavin monooxygenase isoforms: implications for their pharmacokinetic properties and safety Br. J. Pharmacol. 2012, 16, 222-232
    • (2012) Br. J. Pharmacol. , vol.16 , pp. 222-232
    • Xie, G.1    Wong, C.C.2    Cheng, K.W.3    Huang, L.4    Constantinides, P.P.5    Rigas, B.6
  • 33
    • 0037378805 scopus 로고    scopus 로고
    • Cytochrome P450 2C8 and flavin-containing monooxygenases are involved in the metabolism of tazarotenic acid in humans
    • Attar, M.; Dong, D.; Ling, K. H.; Tang-Liu, D. D. Cytochrome P450 2C8 and flavin-containing monooxygenases are involved in the metabolism of tazarotenic acid in humans Drug Metab. Dispos. 2003, 31, 476-481
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 476-481
    • Attar, M.1    Dong, D.2    Ling, K.H.3    Tang-Liu, D.D.4
  • 34
    • 0036893417 scopus 로고    scopus 로고
    • Effects of olopatadine, a new antiallergic agent, on human liver microsomal cytochrome P450 activities
    • Kajita, J.; Inano, K.; Fuse, E.; Kuwabara, T.; Kobayashi, H. Effects of olopatadine, a new antiallergic agent, on human liver microsomal cytochrome P450 activities Drug Metab. Dispos. 2002, 30, 1504-1511
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 1504-1511
    • Kajita, J.1    Inano, K.2    Fuse, E.3    Kuwabara, T.4    Kobayashi, H.5
  • 35
    • 0030893969 scopus 로고    scopus 로고
    • Oxidation of cysteine S-conjugates by rabbit liver microsomes and cDNA-expressed flavin-containing mono-oxygenases: Studies with S-(1,2-dichlorovinyl)-L-cysteine, S-(1,2,2-trichlorovinyl)-L-cysteine, S-allyl-L-cysteine, and S-benzyl-L-cysteine
    • Ripp, S. L.; Overby, L. H.; Philpot, R. M.; Elfarra, A. A. Oxidation of cysteine S-conjugates by rabbit liver microsomes and cDNA-expressed flavin-containing mono-oxygenases: studies with S-(1,2-dichlorovinyl)-L- cysteine, S-(1,2,2-trichlorovinyl)-L-cysteine, S-allyl-L-cysteine, and S-benzyl-L-cysteine Mol. Pharmacol. 1997, 51, 507-515
    • (1997) Mol. Pharmacol. , vol.51 , pp. 507-515
    • Ripp, S.L.1    Overby, L.H.2    Philpot, R.M.3    Elfarra, A.A.4
  • 36
    • 33751544803 scopus 로고    scopus 로고
    • In vivo metabolism of L-methionine in mice: Evidence for stereoselective formation of methionine-d-sulfoxide and quantitation of other major metabolites
    • Dever, J. T.; Elfarra, A. A. In vivo metabolism of L-methionine in mice: evidence for stereoselective formation of methionine-d-sulfoxide and quantitation of other major metabolites Drug Metab. Dispos. 2006, 34, 2036-2043
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 2036-2043
    • Dever, J.T.1    Elfarra, A.A.2
  • 37
    • 0023616725 scopus 로고
    • Sulphoxidation of albendazole by the FAD-containing and cytochrome P-450 dependent mono-oxygenases from pig liver microsomes
    • el Amri, H. S.; Fargetton, X.; Delatour, P.; Batt, A. M. Sulphoxidation of albendazole by the FAD-containing and cytochrome P-450 dependent mono-oxygenases from pig liver microsomes Xenobiotica 1987, 17, 1159-1168
    • (1987) Xenobiotica , vol.17 , pp. 1159-1168
    • El Amri, H.S.1    Fargetton, X.2    Delatour, P.3    Batt, A.M.4
  • 38
    • 13444292819 scopus 로고    scopus 로고
    • Extrahepatic metabolism of carbamate and organophosphate thioether compounds by the flavin-containing monooxygenase and cytochrome P450 systems
    • Furnes, B.; Schlenk, D. Extrahepatic metabolism of carbamate and organophosphate thioether compounds by the flavin-containing monooxygenase and cytochrome P450 systems Drug Metab. Dispos. 2005, 33, 214-218
    • (2005) Drug Metab. Dispos. , vol.33 , pp. 214-218
    • Furnes, B.1    Schlenk, D.2
  • 41
    • 44349089600 scopus 로고    scopus 로고
    • Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase
    • Alfieri, A.; Malito, E.; Orru, R.; Fraaije, M. W.; Mattevi, A. Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 6572-6577
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6572-6577
    • Alfieri, A.1    Malito, E.2    Orru, R.3    Fraaije, M.W.4    Mattevi, A.5
  • 43
    • 34247263219 scopus 로고    scopus 로고
    • A common reference framework for analyzing/comparing proteins and ligands. Fingerprints for ligands and proteins (FLAP): Theory and application
    • Baroni, M.; Cruciani, G.; Sciabola, S.; Perruccio, F.; Mason, J. S. A common reference framework for analyzing/comparing proteins and ligands. Fingerprints for ligands and proteins (FLAP): theory and application J. Chem. Inf. Model. 2007, 47, 279-294
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 279-294
    • Baroni, M.1    Cruciani, G.2    Sciabola, S.3    Perruccio, F.4    Mason, J.S.5
  • 44
    • 84877651696 scopus 로고    scopus 로고
    • Ligand-, structure- and pharmacophore-based molecular fingerprints: A case study on adenosine A(1), A (2A), A (2B), and A (3) receptor antagonists
    • Sirci, F.; Goracci, L.; Rodríguez, D.; van Muijlwijk-Koezen, J.; Gutiérrez-de-Terán, H.; Mannhold, R. Ligand-, structure- and pharmacophore-based molecular fingerprints: a case study on adenosine A(1), A (2A), A (2B), and A (3) receptor antagonists J. Comput.-Aided Mol. Des. 2012, 26, 1247-1266
    • (2012) J. Comput.-Aided Mol. Des. , vol.26 , pp. 1247-1266
    • Sirci, F.1    Goracci, L.2    Rodríguez, D.3    Van Muijlwijk-Koezen, J.4    Gutiérrez-De-Terán, H.5    Mannhold, R.6
  • 46
    • 84905008654 scopus 로고    scopus 로고
    • Mayr's Database of Reactivity Parameters. (accessed February 1).
    • Mayr's Database of Reactivity Parameters. http://www.cup.lmu.de/oc/mayr/ reaktionsdatenbank/fe/showclass/40 (accessed February 1, 2014).
    • (2014)
  • 49
    • 73149102760 scopus 로고    scopus 로고
    • In vitro hepatic metabolism explains higher clearance of voriconazole in children versus adults: Role of CYP2C19 and flavin-containing monooxygenase 3
    • Yanni, S. B.; Annaert, P. P.; Augustijns, P.; Ibrahim, J. G.; Benjamin, D. K., Jr.; Thakker, D. R. In vitro hepatic metabolism explains higher clearance of voriconazole in children versus adults: role of CYP2C19 and flavin-containing monooxygenase 3 Drug Metab. Dispos. 2010, 38, 25-31
    • (2010) Drug Metab. Dispos. , vol.38 , pp. 25-31
    • Yanni, S.B.1    Annaert, P.P.2    Augustijns, P.3    Ibrahim, J.G.4    Benjamin, Jr.D.K.5    Thakker, D.R.6
  • 50
    • 33749010103 scopus 로고    scopus 로고
    • Enzyme-mediated protein haptenation of dapsone and sulfamethoxazole in human keratinocytes: II. Expression and role of flavin-containing monooxygenases and peroxidases
    • Vyas, P. M.; Roychowdhury, S.; Koukouritaki, S. B.; Hines, R. N.; Krueger, S. K.; Williams, D. E.; Nauseef, W. M.; Svensson, C. K. Enzyme-mediated protein haptenation of dapsone and sulfamethoxazole in human keratinocytes: II. Expression and role of flavin-containing monooxygenases and peroxidases J. Pharmacol. Exp. Ther. 2006, 319, 497-505
    • (2006) J. Pharmacol. Exp. Ther. , vol.319 , pp. 497-505
    • Vyas, P.M.1    Roychowdhury, S.2    Koukouritaki, S.B.3    Hines, R.N.4    Krueger, S.K.5    Williams, D.E.6    Nauseef, W.M.7    Svensson, C.K.8
  • 51
    • 77749258432 scopus 로고    scopus 로고
    • One-pot reductive amination of carbonyl compounds using sodium borohydride-amberlist 15
    • Alinezhad, H.; Tajbakhsh, M.; Mahdavi, N. One-pot reductive amination of carbonyl compounds using sodium borohydride-amberlist 15 Synth. Commun. 2010, 40, 951-956
    • (2010) Synth. Commun. , vol.40 , pp. 951-956
    • Alinezhad, H.1    Tajbakhsh, M.2    Mahdavi, N.3
  • 53
    • 78649402523 scopus 로고    scopus 로고
    • Enhanced metabolite identification with MS(E) and a semi-automated software for structural elucidation
    • Bonn, B.; Leandersson, C.; Fontaine, F.; Zamora, I. Enhanced metabolite identification with MS(E) and a semi-automated software for structural elucidation Rapid Commun. Mass Spectrom. 2010, 24, 3127-3138
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 3127-3138
    • Bonn, B.1    Leandersson, C.2    Fontaine, F.3    Zamora, I.4
  • 54
    • 84875709453 scopus 로고    scopus 로고
    • High-throughput, fully automated, specific MetID. A revolution for drug discovery
    • Zamora, I.; Fontaine, F.; Serra, B.; Plasencia, G. High-throughput, fully automated, specific MetID. A revolution for drug discovery Drug Discovery Today: Technol. 2013, 10, e199-205
    • (2013) Drug Discovery Today: Technol. , vol.10 , pp. 199-205
    • Zamora, I.1    Fontaine, F.2    Serra, B.3    Plasencia, G.4
  • 55
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. I-TASSER server for protein 3D structure prediction BMC Bioinf. 2008, 9, 40
    • (2008) BMC Bioinf. , vol.9 , pp. 40
    • Zhang, Y.1
  • 56
    • 84905034204 scopus 로고    scopus 로고
    • I-TASSER Online. (accessed February 12).
    • I-TASSER Online. http://zhanglab.ccmb.med.umich.edu/I-TASSER/ (accessed February 12, 2014).
    • (2014)
  • 59
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 2008, 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.