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Volumn 26, Issue 4, 2013, Pages 517-528

Binding of diverse environmental chemicals with human cytochromes P450 2A13, 2A6, and 1B1 and enzyme inhibition

Author keywords

[No Author keywords available]

Indexed keywords

1 HYDROXYPYRENE; 1 NITROPYRENE; 7 HYDROXYFLAVONE; ACENAPHTHYLENE; BIPHENYL; CHRYSIN; CYTOCHROME P450 1B1; CYTOCHROME P450 2A; CYTOCHROME P450 2A13; CYTOCHROME P450 2A6; FLAVONE; FLUORANTHENE; GALANGIN; NAPHTHALENE; PHENANTHRENE; PYRENE; TETRACHLOROBIPHENYL; UNCLASSIFIED DRUG;

EID: 84876255651     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx300492j     Document Type: Article
Times cited : (27)

References (69)
  • 1
    • 79955512616 scopus 로고    scopus 로고
    • Cytochrome P450-mediated pulmonary metabolism of carcinogens: Regulation and cross-talk in lung carcinogenesis
    • Anttila, S., Raunio, H., and Hakkola, J. (2011) Cytochrome P450-mediated pulmonary metabolism of carcinogens: regulation and cross-talk in lung carcinogenesis Am. J. Respir. Cell Mol. Biol. 44, 583-590
    • (2011) Am. J. Respir. Cell Mol. Biol. , vol.44 , pp. 583-590
    • Anttila, S.1    Raunio, H.2    Hakkola, J.3
  • 2
    • 67649577249 scopus 로고    scopus 로고
    • Chemoprevention of lung carcinogenesis in addicted smokers and ex-smokers
    • Hecht, S. S., Kassie, F., and Hatsukami, D. K. (2009) Chemoprevention of lung carcinogenesis in addicted smokers and ex-smokers Nat. Rev. Cancer 9, 476-488
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 476-488
    • Hecht, S.S.1    Kassie, F.2    Hatsukami, D.K.3
  • 4
    • 33748041085 scopus 로고    scopus 로고
    • Combined analysis of r -1, t -2,3, c -4-tetrahydroxy-1,2,3,4- tetrahydrophenanthrene and 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol in smokers' plasma
    • Carmella, S. G., Yoder, A., and Hecht, S. S. (2006) Combined analysis of r -1, t -2,3, c -4-tetrahydroxy-1,2,3,4-tetrahydrophenanthrene and 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol in smokers' plasma Cancer Epidemiol. Biomarkers Prev. 15, 1490-1494
    • (2006) Cancer Epidemiol. Biomarkers Prev. , vol.15 , pp. 1490-1494
    • Carmella, S.G.1    Yoder, A.2    Hecht, S.S.3
  • 5
    • 0035226983 scopus 로고    scopus 로고
    • Carcinogen biomarkers for lung or oral cancer chemoprevention trials
    • Hecht, S. S. (2001) Carcinogen biomarkers for lung or oral cancer chemoprevention trials IARC Sci. Publ. 154, 245-255
    • (2001) IARC Sci. Publ. , vol.154 , pp. 245-255
    • Hecht, S.S.1
  • 6
    • 84863920443 scopus 로고    scopus 로고
    • Contributions of human enzymes in carcinogen metabolism
    • Rendic, S. and Guengerich, F. P. (2012) Contributions of human enzymes in carcinogen metabolism Chem. Res. Toxicol. 25, 1316-1383
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 1316-1383
    • Rendic, S.1    Guengerich, F.P.2
  • 7
    • 80051723506 scopus 로고    scopus 로고
    • Metabolism and biomarkers of heterocyclic aromatic amines in molecular epidemiology studies: Lessons learned from aromatic amines
    • Turesky, R. J. and Le Marchand, L. (2011) Metabolism and biomarkers of heterocyclic aromatic amines in molecular epidemiology studies: lessons learned from aromatic amines Chem. Res. Toxicol. 24, 1169-1214
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1169-1214
    • Turesky, R.J.1    Le Marchand, L.2
  • 8
    • 20444412643 scopus 로고    scopus 로고
    • Metabolic activation of polycyclic and heterocyclic aromatic hydrocarbons and DNA damage: A review
    • Xue, W. and Warshawsky, D. (2005) Metabolic activation of polycyclic and heterocyclic aromatic hydrocarbons and DNA damage: a review Toxicol. Appl. Pharmacol. 206, 73-93
    • (2005) Toxicol. Appl. Pharmacol. , vol.206 , pp. 73-93
    • Xue, W.1    Warshawsky, D.2
  • 9
    • 33845267470 scopus 로고    scopus 로고
    • The role of cytochrome P450 enzymes in endogenous signalling pathways and environmental carcinogenesis
    • Nebert, D. W. and Dalton, T. P. (2006) The role of cytochrome P450 enzymes in endogenous signalling pathways and environmental carcinogenesis Nat. Rev. Cancer 6, 947-960
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 947-960
    • Nebert, D.W.1    Dalton, T.P.2
  • 11
    • 0032565569 scopus 로고    scopus 로고
    • Activation of procarcinogens by individual human cytochrome P450 enzymes
    • Guengerich, F. P. and Shimada, T. (1998) Activation of procarcinogens by individual human cytochrome P450 enzymes Mut. Res. 400, 201-213
    • (1998) Mut. Res. , vol.400 , pp. 201-213
    • Guengerich, F.P.1    Shimada, T.2
  • 12
    • 34047243800 scopus 로고    scopus 로고
    • Xenobiotic-metabolizing enzymes involved in activation and detoxification of carcinogenic polycyclic aromatic hydrocarbons
    • Shimada, T. (2006) Xenobiotic-metabolizing enzymes involved in activation and detoxification of carcinogenic polycyclic aromatic hydrocarbons Drug Metab. Pharmacokinet. 21, 257-276
    • (2006) Drug Metab. Pharmacokinet. , vol.21 , pp. 257-276
    • Shimada, T.1
  • 13
    • 0034665139 scopus 로고    scopus 로고
    • Human cytochrome P450 CYP2A13: Predominant exression in the respiratory tract and its high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
    • Su, T., Bao, Z., Zhang, Q.-Y., Smith, T. J., Hong, J.-Y., and Ding, X. (2000) Human cytochrome P450 CYP2A13: Predominant exression in the respiratory tract and its high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone Cancer Res. 60, 5074-5079
    • (2000) Cancer Res. , vol.60 , pp. 5074-5079
    • Su, T.1    Bao, Z.2    Zhang, Q.-Y.3    Smith, T.J.4    Hong, J.-Y.5    Ding, X.6
  • 14
    • 33847138652 scopus 로고    scopus 로고
    • Transcriptional regulation of human CYP2A13 expression in the respiratory tract by CCAAT/enhancer binding protein and epigenetic modulation
    • Ling, G., Wei, Y., and Ding, X. (2007) Transcriptional regulation of human CYP2A13 expression in the respiratory tract by CCAAT/enhancer binding protein and epigenetic modulation Mol. Pharmacol. 71, 807-816
    • (2007) Mol. Pharmacol. , vol.71 , pp. 807-816
    • Ling, G.1    Wei, Y.2    Ding, X.3
  • 15
    • 84867054081 scopus 로고    scopus 로고
    • Differential distribution of CYP2A6 and CYP2A13 in the human respiratory tract
    • Chiang, H.-C., Wang, C.-K., and Tsou, T.-C. (2012) Differential distribution of CYP2A6 and CYP2A13 in the human respiratory tract Respiration 84, 319-326
    • (2012) Respiration , vol.84 , pp. 319-326
    • Chiang, H.-C.1    Wang, C.-K.2    Tsou, T.-C.3
  • 16
    • 33748918311 scopus 로고    scopus 로고
    • CYP2A13 in human respiratory tissues and lung cancers: An immunohistochemical study with a new peptide-specific antibody
    • Zhu, L. R., Thomas, P. E., Lu, G., Reuhl, K. R., Yang, G. Y., Wang, L. D., Wang, S. L, Yang, C. S., He, X. Y., and Hong, J. Y. (2006) CYP2A13 in human respiratory tissues and lung cancers: an immunohistochemical study with a new peptide-specific antibody Drug Metab. Dispos. 34, 1672-1676
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 1672-1676
    • Zhu, L.R.1    Thomas, P.E.2    Lu, G.3    Reuhl, K.R.4    Yang, G.Y.5    Wang, L.D.6    Wang, S.L.7    Yang, C.S.8    He, X.Y.9    Hong, J.Y.10
  • 17
    • 21144437181 scopus 로고    scopus 로고
    • Metabolic activation of the tobacco carcinogen 4-(methylnitrosamino)-(3- pyridyl)-1-butanone by cytochrome P450 2A13 in human fetal nasal microsomes
    • Wong, H. L., Zhang, X., Zhang, Q. Y., Gu, J., Ding, X., Hecht, S. S., and Murphy, S. E. (2005) Metabolic activation of the tobacco carcinogen 4-(methylnitrosamino)-(3-pyridyl)-1-butanone by cytochrome P450 2A13 in human fetal nasal microsomes Chem. Res. Toxicol. 18, 913-918
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 913-918
    • Wong, H.L.1    Zhang, X.2    Zhang, Q.Y.3    Gu, J.4    Ding, X.5    Hecht, S.S.6    Murphy, S.E.7
  • 18
    • 84863848211 scopus 로고    scopus 로고
    • Cytochrome P450-catalyzed degradation of nicotine: Fundamental parameters determining hydroxylation by cytochrome P450 2A6 at the 5′-carbon or the N -methyl carbon
    • Kwiecien, R. A., Le Questel, J. Y., Lebreton, J., Delaforge, M., Andre, F., Pihan, E., Roussel, A., Fournial, A., Paneth, P., and Robins, R. J. (2012) Cytochrome P450-catalyzed degradation of nicotine: Fundamental parameters determining hydroxylation by cytochrome P450 2A6 at the 5′-carbon or the N -methyl carbon J. Phys. Chem. B 116, 7827-7840
    • (2012) J. Phys. Chem. B , vol.116 , pp. 7827-7840
    • Kwiecien, R.A.1    Le Questel, J.Y.2    Lebreton, J.3    Delaforge, M.4    Andre, F.5    Pihan, E.6    Roussel, A.7    Fournial, A.8    Paneth, P.9    Robins, R.J.10
  • 19
    • 72949119129 scopus 로고    scopus 로고
    • Structure, function, regulation and polymorphism of human cytochrome P450 2A6
    • Di, Y. M., Chow, V. D., Yang, L. P., and Zhou, S. F. (2009) Structure, function, regulation and polymorphism of human cytochrome P450 2A6 Curr. Drug Metab. 10, 754-780
    • (2009) Curr. Drug Metab. , vol.10 , pp. 754-780
    • Di, Y.M.1    Chow, V.D.2    Yang, L.P.3    Zhou, S.F.4
  • 23
    • 21244461430 scopus 로고    scopus 로고
    • Metabolism and bioactivation of toxicants in the lung. the in vitro cellular approach
    • Castell, J. V., Donato, M. T., and Gomez-Lechon, M. J. (2005) Metabolism and bioactivation of toxicants in the lung. The in vitro cellular approach Exp. Toxicol. Pathol. 57 (Suppl. 1) 189-204
    • (2005) Exp. Toxicol. Pathol. , vol.57 , Issue.SUPPL. 1 , pp. 189-204
    • Castell, J.V.1    Donato, M.T.2    Gomez-Lechon, M.J.3
  • 25
    • 41849093006 scopus 로고    scopus 로고
    • Human cytochrome P450 2A13 efficiently metabolizes chemicals in air pollutants: Naphthalene, styrene, and toluene
    • Fukami, T., Katoh, M., Yamazaki, H., Yokoi, T., and Nakajima, M. (2008) Human cytochrome P450 2A13 efficiently metabolizes chemicals in air pollutants: naphthalene, styrene, and toluene Chem. Res. Toxicol. 21, 720-725
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 720-725
    • Fukami, T.1    Katoh, M.2    Yamazaki, H.3    Yokoi, T.4    Nakajima, M.5
  • 26
    • 2642510760 scopus 로고    scopus 로고
    • Role of aryl hydrocarbon receptor-mediated induction of the CYP1 enzymes in environmental toxicity and cancer
    • Nebert, D. W., Dalton, T. P., Okey, A. B., and Gonzalez, F. J. (2004) Role of aryl hydrocarbon receptor-mediated induction of the CYP1 enzymes in environmental toxicity and cancer J. Biol. Chem. 279, 23847-23850
    • (2004) J. Biol. Chem. , vol.279 , pp. 23847-23850
    • Nebert, D.W.1    Dalton, T.P.2    Okey, A.B.3    Gonzalez, F.J.4
  • 27
    • 34047253007 scopus 로고    scopus 로고
    • Different mechanisms for inhibition of human cytochromes P450 1A1, 1A2 and 1B1 by polycyclic aromatic inhibitors
    • Shimada, T., Murayama, N., Okada, K., Funae, Y., Yamazaki, H., and Guengerich, F. P. (2007) Different mechanisms for inhibition of human cytochromes P450 1A1, 1A2 and 1B1 by polycyclic aromatic inhibitors Chem. Res. Toxicol. 20, 489-496
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 489-496
    • Shimada, T.1    Murayama, N.2    Okada, K.3    Funae, Y.4    Yamazaki, H.5    Guengerich, F.P.6
  • 28
    • 58149085978 scopus 로고    scopus 로고
    • Interaction of polycyclic aromatic hydrocarbons with human cytochrome P450 1B1 in inhibiting catalytic activity
    • Shimada, T., Murayama, N., Tanaka, K., Takenaka, S., Yamazaki, H., Guengerich, F. P., and Komori, M. (2008) Interaction of polycyclic aromatic hydrocarbons with human cytochrome P450 1B1 in inhibiting catalytic activity Chem. Res. Toxicol. 21, 2313-2323
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 2313-2323
    • Shimada, T.1    Murayama, N.2    Tanaka, K.3    Takenaka, S.4    Yamazaki, H.5    Guengerich, F.P.6    Komori, M.7
  • 29
    • 67651002558 scopus 로고    scopus 로고
    • Reverse type i binding spectra of human cytochrome P450 1B1 induced by derivatives of flavonoids, stilbenes, pyrenes, naphthalenes, phenanthrenes, and biphenyls that Inhibit catalytic activity: Structure-function relationships
    • Shimada, T., Tanaka, K., Takenaka, S., Foroozesh, M. K., Murayama, N., Yamazaki, H., Guengerich, F. P., and Komori, M. (2009) Reverse type I binding spectra of human cytochrome P450 1B1 induced by derivatives of flavonoids, stilbenes, pyrenes, naphthalenes, phenanthrenes, and biphenyls that Inhibit catalytic activity: structure-function relationships Chem. Res. Toxicol. 22, 1325-1333
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1325-1333
    • Shimada, T.1    Tanaka, K.2    Takenaka, S.3    Foroozesh, M.K.4    Murayama, N.5    Yamazaki, H.6    Guengerich, F.P.7    Komori, M.8
  • 31
    • 0031021458 scopus 로고    scopus 로고
    • Propynylaryl acetylenes as mechanism-based inhibitors of cytochrome P450 1A1, 1A2, and 2B1 enzymes
    • Foroozesh, M., Primrose, G., Guo, Z., Bell, L. C., Guengerich, F. P., and Alworth, W. L. (1997) Propynylaryl acetylenes as mechanism-based inhibitors of cytochrome P450 1A1, 1A2, and 2B1 enzymes Chem. Res. Toxicol. 10, 91-102
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 91-102
    • Foroozesh, M.1    Primrose, G.2    Guo, Z.3    Bell, L.C.4    Guengerich, F.P.5    Alworth, W.L.6
  • 34
    • 84855770436 scopus 로고    scopus 로고
    • QSAR models of cytochrome P450 enzyme 1A2 inhibitors using CoMFA, CoMSIA and HQSAR
    • Sridhar, J., Foroozesh, M., and Stevens, C. L. (2011) QSAR models of cytochrome P450 enzyme 1A2 inhibitors using CoMFA, CoMSIA and HQSAR SAR QSAR Environ. Res. 22, 681-697
    • (2011) SAR QSAR Environ. Res. , vol.22 , pp. 681-697
    • Sridhar, J.1    Foroozesh, M.2    Stevens, C.L.3
  • 35
    • 28844479959 scopus 로고    scopus 로고
    • Analysis of coumarin 7-hydroxylation activity of cytochrome P450 2A6 using random mutagenesis
    • Kim, D., Wu, Z.-L., and Guengerich, F. P. (2005) Analysis of coumarin 7-hydroxylation activity of cytochrome P450 2A6 using random mutagenesis J. Biol. Chem. 280, 40319-40327
    • (2005) J. Biol. Chem. , vol.280 , pp. 40319-40327
    • Kim, D.1    Wu, Z.-L.2    Guengerich, F.P.3
  • 36
    • 84876267453 scopus 로고    scopus 로고
    • Metabolic activation of polycyclic aromatic hydrocarbons and aryl and heterocyclic amines by human cytochromes P450 2A13 and 2A6
    • DOI: 10.1021/tx3004906
    • Shimada, T., Murayama, N., Yamazaki, H., Tanaka, K., Takenaka, S., Komori, M., Kim, D., and Guengerich, F. P. (2013) Metabolic activation of polycyclic aromatic hydrocarbons and aryl and heterocyclic amines by human cytochromes P450 2A13 and 2A6. Chem. Res. Toxicol. 26, DOI: 10.1021/tx3004906.
    • (2013) Chem. Res. Toxicol. , vol.26
    • Shimada, T.1    Murayama, N.2    Yamazaki, H.3    Tanaka, K.4    Takenaka, S.5    Komori, M.6    Kim, D.7    Guengerich, F.P.8
  • 37
    • 0030843652 scopus 로고    scopus 로고
    • Drug metabolism by Escherichia coli expressing human cytochromes P450
    • Parikh, A., Gillam, E. M. J., and Guengerich, F. P. (1997) Drug metabolism by Escherichia coli expressing human cytochromes P450 Nat. Biotechnol. 15, 784-788
    • (1997) Nat. Biotechnol. , vol.15 , pp. 784-788
    • Parikh, A.1    Gillam, E.M.J.2    Guengerich, F.P.3
  • 38
    • 33644542728 scopus 로고    scopus 로고
    • Inhibition of human cytochrome P450 1A1, 1A2, and 1B1-mediated activation of procarcinogens to genotoxic metabolites by polycyclic aromatic hydrocarbons
    • Shimada, T. and Guengerich, F. P. (2006) Inhibition of human cytochrome P450 1A1, 1A2, and 1B1-mediated activation of procarcinogens to genotoxic metabolites by polycyclic aromatic hydrocarbons Chem. Res. Toxicol. 19, 288-294
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 288-294
    • Shimada, T.1    Guengerich, F.P.2
  • 39
    • 0028075688 scopus 로고
    • Catalytic roles of rat and human cytochrome P450 2A enzymes in testosterone 7α- and coumarin 7-hydroxylations
    • Yamazaki, H., Mimura, M., Sugahara, C., and Shimada, T. (1994) Catalytic roles of rat and human cytochrome P450 2A enzymes in testosterone 7α- and coumarin 7-hydroxylations Biochem. Pharmacol. 48, 1524-1527
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1524-1527
    • Yamazaki, H.1    Mimura, M.2    Sugahara, C.3    Shimada, T.4
  • 40
    • 0030959377 scopus 로고    scopus 로고
    • Cytochrome P450-dependent drug oxidation activities in liver microsomes of various animal species including rats, guinea pigs, dogs, monkeys, and humans
    • Shimada, T., Mimura, M., Inoue, K., Nakamura, S., Oda, H., Ohmori, S., and Yamazaki, H. (1997) Cytochrome P450-dependent drug oxidation activities in liver microsomes of various animal species including rats, guinea pigs, dogs, monkeys, and humans Arch. Toxicol. 71, 401-408
    • (1997) Arch. Toxicol. , vol.71 , pp. 401-408
    • Shimada, T.1    Mimura, M.2    Inoue, K.3    Nakamura, S.4    Oda, H.5    Ohmori, S.6    Yamazaki, H.7
  • 41
    • 41849149011 scopus 로고    scopus 로고
    • Analysis and Characterization of Enzymes and Nucleic Acids
    • (Hayes, A. W. Ed.) 5 th ed. pp, CRC Press, Boca Raton, FL.
    • Guengerich, F. P. and Bartleson, C. J. (2007) Analysis and Characterization of Enzymes and Nucleic Acids, in Principles and Methods of Toxicology (Hayes, A. W., Ed.) 5 th ed., pp 1981-2048, CRC Press, Boca Raton, FL.
    • (2007) Principles and Methods of Toxicology , pp. 1981-2048
    • Guengerich, F.P.1    Bartleson, C.J.2
  • 42
    • 0032908959 scopus 로고    scopus 로고
    • Highly sensitive high-performance liquid chromatographic assay for coumarin 7-hydroxylation and 7-ethoxycoumarin O-deethylation by human liver cytochrome P450 enzymes
    • Yamazaki, H., Tanaka, M., and Shimada, T. (1999) Highly sensitive high-performance liquid chromatographic assay for coumarin 7-hydroxylation and 7-ethoxycoumarin O-deethylation by human liver cytochrome P450 enzymes J. Chromatogr. B 721, 13-19
    • (1999) J. Chromatogr. B , vol.721 , pp. 13-19
    • Yamazaki, H.1    Tanaka, M.2    Shimada, T.3
  • 43
    • 0014024732 scopus 로고
    • Substrate interaction with hydroxylase system in liver microsomes
    • Imai, Y. and Sato, R. (1966) Substrate interaction with hydroxylase system in liver microsomes Biochem. Biophys. Res. Commun. 22, 620-626
    • (1966) Biochem. Biophys. Res. Commun. , vol.22 , pp. 620-626
    • Imai, Y.1    Sato, R.2
  • 44
    • 0014059179 scopus 로고
    • Spectral studies of drug interaction with hepatic microsomal cytochrome P-450
    • Schenkman, J. B., Remmer, H., and Estabrook, R. W. (1967) Spectral studies of drug interaction with hepatic microsomal cytochrome P-450 Mol. Pharmacol. 3, 113-123
    • (1967) Mol. Pharmacol. , vol.3 , pp. 113-123
    • Schenkman, J.B.1    Remmer, H.2    Estabrook, R.W.3
  • 45
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 46
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: Elimination of interfering substances
    • Brown, R. E., Jarvis, K. L., and Hyland, K. J. (1989) Protein measurement using bicinchoninic acid: elimination of interfering substances Anal. Biochem. 180, 136-139
    • (1989) Anal. Biochem. , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvis, K.L.2    Hyland, K.J.3
  • 47
    • 79953126762 scopus 로고    scopus 로고
    • Structural characterization of the complex between α-naphthoflavone and human cytochrome P450 1B1
    • Wang, A., Savas, U., Stout, C. D., and Johnson, E. F. (2011) Structural characterization of the complex between α-naphthoflavone and human cytochrome P450 1B1 J. Biol. Chem. 286, 5736-5743
    • (2011) J. Biol. Chem. , vol.286 , pp. 5736-5743
    • Wang, A.1    Savas, U.2    Stout, C.D.3    Johnson, E.F.4
  • 48
    • 26944462419 scopus 로고    scopus 로고
    • Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen
    • Yano, J. K., Hsu, M. H., Griffin, K. J., Stout, C. D., and Johnson, E. F. (2005) Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen Nat. Struct. Biol. 11, 822-823
    • (2005) Nat. Struct. Biol. , vol.11 , pp. 822-823
    • Yano, J.K.1    Hsu, M.H.2    Griffin, K.J.3    Stout, C.D.4    Johnson, E.F.5
  • 49
    • 84864531088 scopus 로고    scopus 로고
    • Nicotine and 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone binding and access channel in human cytochrome P450 2A6 and 2A13 enzymes
    • Devore, N. M. and Scott, E. E. (2012) Nicotine and 4-(methylnitrosamino)- 1-(3-pyridyl)-1-butanone binding and access channel in human cytochrome P450 2A6 and 2A13 enzymes J. Biol. Chem. 287, 26576-26585
    • (2012) J. Biol. Chem. , vol.287 , pp. 26576-26585
    • Devore, N.M.1    Scott, E.E.2
  • 51
    • 80051739998 scopus 로고    scopus 로고
    • Spectral modification and catalytic inhibition of human cytochromes P450 1A1, 1A2, 1B1, 2A6, and 2A13 by four chemopreventive organoselenium compounds
    • Shimada, T., Murayama, N., Tanaka, K., Takenaka, S., Guengerich, F. P., Yamazaki, H., and Komori, M. (2011) Spectral modification and catalytic inhibition of human cytochromes P450 1A1, 1A2, 1B1, 2A6, and 2A13 by four chemopreventive organoselenium compounds Chem. Res. Toxicol. 24, 1327-1337
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1327-1337
    • Shimada, T.1    Murayama, N.2    Tanaka, K.3    Takenaka, S.4    Guengerich, F.P.5    Yamazaki, H.6    Komori, M.7
  • 54
    • 0016709169 scopus 로고
    • Studies on the substrate-induced spectral change of cytochrome P-450 in liver microsomes
    • Yoshida, Y. and Kumaoka, H. (1975) Studies on the substrate-induced spectral change of cytochrome P-450 in liver microsomes J. Biochem. (Tokyo, Jpn.) 78, 55-68
    • (1975) J. Biochem. (Tokyo, Jpn.) , vol.78 , pp. 55-68
    • Yoshida, Y.1    Kumaoka, H.2
  • 55
    • 84860217008 scopus 로고    scopus 로고
    • Structural comparison of cytochromes P450 2A6, 2A13, and 2E1 with pilocarpine
    • DeVore, N. M., Meneely, K. M., Bart, A. G., Stephens, E. S., Battaile, K. P., and Scott, E. E. (2012) Structural comparison of cytochromes P450 2A6, 2A13, and 2E1 with pilocarpine FEBS J. 279, 1621-1631
    • (2012) FEBS J. , vol.279 , pp. 1621-1631
    • Devore, N.M.1    Meneely, K.M.2    Bart, A.G.3    Stephens, E.S.4    Battaile, K.P.5    Scott, E.E.6
  • 56
    • 66649122018 scopus 로고    scopus 로고
    • Key residues controlling binding of diverse ligands to human cytochrome P450 2A enzymes
    • DeVore, N. M., Smith, B. D., Wang, J. L., Lushington, G. H., and Scott, E. E. (2009) Key residues controlling binding of diverse ligands to human cytochrome P450 2A enzymes Drug Metab. Dispos. 37, 1319-1327
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1319-1327
    • Devore, N.M.1    Smith, B.D.2    Wang, J.L.3    Lushington, G.H.4    Scott, E.E.5
  • 57
    • 3242761322 scopus 로고    scopus 로고
    • Levels of PAHs in soil and vegetation samples from Tarragona County, Spain
    • Nadal, M., Schuhmacher, M., and Domingo, J. L. (2004) Levels of PAHs in soil and vegetation samples from Tarragona County, Spain Environ. Pollut. 132, 1-11
    • (2004) Environ. Pollut. , vol.132 , pp. 1-11
    • Nadal, M.1    Schuhmacher, M.2    Domingo, J.L.3
  • 58
    • 0037205639 scopus 로고    scopus 로고
    • Detection of polycyclic aromatic hydrocarbon levels in milk collected near potential contamination sources
    • Grova, N., Feidt, C., Crepineau, C., Laurent, C., Lafargue, P. E., Hachimi, A., and Rychen, G. (2002) Detection of polycyclic aromatic hydrocarbon levels in milk collected near potential contamination sources J. Agric. Food Chem. 50, 4640-4642
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4640-4642
    • Grova, N.1    Feidt, C.2    Crepineau, C.3    Laurent, C.4    Lafargue, P.E.5    Hachimi, A.6    Rychen, G.7
  • 59
    • 0020431144 scopus 로고
    • Induction of microsomal enzymes by foreign chemicals and carcinogenesis by polycyclic aromatic hydrocarbons: G. H. A. Clowes Memorial Lecture
    • Conney, A. H. (1982) Induction of microsomal enzymes by foreign chemicals and carcinogenesis by polycyclic aromatic hydrocarbons: G. H. A. Clowes Memorial Lecture Cancer Res. 42, 4875-4917
    • (1982) Cancer Res. , vol.42 , pp. 4875-4917
    • Conney, A.H.1
  • 60
    • 0021287601 scopus 로고
    • Mutagenicity of the enantiomers of the diastereomeric bay-region benzo(c)phenanthrene 3,4-diol-1,2-epoxides in bacterial and mammalian cells
    • Wood, A. W., Chang, R. L., Levin, W., Thakker, D. R., Yagi, H., Sayer, J. M., Jerina, D. M., and Conney, A. H. (1984) Mutagenicity of the enantiomers of the diastereomeric bay-region benzo(c)phenanthrene 3,4-diol-1,2-epoxides in bacterial and mammalian cells Cancer Res. 44, 2320-2324
    • (1984) Cancer Res. , vol.44 , pp. 2320-2324
    • Wood, A.W.1    Chang, R.L.2    Levin, W.3    Thakker, D.R.4    Yagi, H.5    Sayer, J.M.6    Jerina, D.M.7    Conney, A.H.8
  • 61
    • 0022607674 scopus 로고
    • Tumorigenicity of optical isomers of the diastereomeric bay-region 3,4-diol-1,2-epoxides of benzo(c)phenanthrene in murine tumor models
    • Levin, W., Chang, R. L., Wood, A. W., Thakker, D. R., Yagi, H., Jerina, D. M., and Conney, A. H. (1986) Tumorigenicity of optical isomers of the diastereomeric bay-region 3,4-diol-1,2-epoxides of benzo(c)phenanthrene in murine tumor models Cancer Res. 46, 2257-2261
    • (1986) Cancer Res. , vol.46 , pp. 2257-2261
    • Levin, W.1    Chang, R.L.2    Wood, A.W.3    Thakker, D.R.4    Yagi, H.5    Jerina, D.M.6    Conney, A.H.7
  • 62
    • 33845358503 scopus 로고    scopus 로고
    • Synthetic inhibitors of cytochrome P-450 2A6: Inhibitory activity, difference spectra, mechanism of inhibition, and protein cocrystallization
    • Yano, J. K., Denton, T. T., Cerny, M. A., Zhang, X., Johnson, E. F., and Cashman, J. R. (2006) Synthetic inhibitors of cytochrome P-450 2A6: inhibitory activity, difference spectra, mechanism of inhibition, and protein cocrystallization J. Med. Chem. 49, 6987-7001
    • (2006) J. Med. Chem. , vol.49 , pp. 6987-7001
    • Yano, J.K.1    Denton, T.T.2    Cerny, M.A.3    Zhang, X.4    Johnson, E.F.5    Cashman, J.R.6
  • 63
    • 2942605963 scopus 로고    scopus 로고
    • Identification of Val117 and Arg372 as critical amino acid residues for the activity difference between human CYP2A6 and CYP2A13 in coumarin 7-hydroxylation
    • He, X. Y., Shen, J., Hu, W. Y., Ding, X., Lu, A. Y., and Hong, J. Y. (2004) Identification of Val117 and Arg372 as critical amino acid residues for the activity difference between human CYP2A6 and CYP2A13 in coumarin 7-hydroxylation Arch. Biochem. Biophys. 427, 143-153
    • (2004) Arch. Biochem. Biophys. , vol.427 , pp. 143-153
    • He, X.Y.1    Shen, J.2    Hu, W.Y.3    Ding, X.4    Lu, A.Y.5    Hong, J.Y.6
  • 64
    • 28844494791 scopus 로고    scopus 로고
    • Expansion of substrate specificity of cytochrome P450 2A6 by mutagenesis
    • Wu, Z., Podust, L. M., and Guengerich, F. P. (2005) Expansion of substrate specificity of cytochrome P450 2A6 by mutagenesis J. Biol. Chem. 280, 41090-41100
    • (2005) J. Biol. Chem. , vol.280 , pp. 41090-41100
    • Wu, Z.1    Podust, L.M.2    Guengerich, F.P.3
  • 65
    • 61449158840 scopus 로고    scopus 로고
    • Effect of CYP2A13 active site mutation N297A on metabolism of coumarin and tobacco-specific nitrosamines
    • Schlicht, K. E., Berg, J. Z., and Murphy, S. E. (2009) Effect of CYP2A13 active site mutation N297A on metabolism of coumarin and tobacco-specific nitrosamines Drug Metab. Dispos. 37, 665-671
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 665-671
    • Schlicht, K.E.1    Berg, J.Z.2    Murphy, S.E.3
  • 66
    • 35148815019 scopus 로고    scopus 로고
    • Effects of eleven isothiocyanates on P450 2A6- and 2A13-catalyzed coumarin 7-hydroxylation
    • von Weymarn, L. B., Chun, J. A., Knudsen, G. A., and Hollenberg, P. F. (2007) Effects of eleven isothiocyanates on P450 2A6- and 2A13-catalyzed coumarin 7-hydroxylation Chem. Res. Toxicol. 20, 1252-1259
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 1252-1259
    • Von Weymarn, L.B.1    Chun, J.A.2    Knudsen, G.A.3    Hollenberg, P.F.4
  • 67
    • 70349546336 scopus 로고    scopus 로고
    • Synthesis and in vitro activity of heterocyclic inhibitors of CYP2A6 and CYP2A13, two cytochrome P450 enzymes present in the respiratory tract
    • Chougnet, A., Woggon, W.-D., Locher, E., and Schilling, B. (2009) Synthesis and in vitro activity of heterocyclic inhibitors of CYP2A6 and CYP2A13, two cytochrome P450 enzymes present in the respiratory tract ChemBioChem 10, 1562-1567
    • (2009) ChemBioChem , vol.10 , pp. 1562-1567
    • Chougnet, A.1    Woggon, W.-D.2    Locher, E.3    Schilling, B.4
  • 68
    • 84864545260 scopus 로고    scopus 로고
    • Evaluation of inhibition selectivity for human cytochrome P450 2A enzymes
    • Stephens, E. S., Walsh, A. A., and Scott, E. E. (2012) Evaluation of inhibition selectivity for human cytochrome P450 2A enzymes Drug Metab. Dispos. 40, 1797-1802
    • (2012) Drug Metab. Dispos. , vol.40 , pp. 1797-1802
    • Stephens, E.S.1    Walsh, A.A.2    Scott, E.E.3
  • 69
    • 84860216857 scopus 로고    scopus 로고
    • Inhibition and inactivation of cytochrome P450 2A6 and cytochrome P450 2A13 by methofuran, β-nicotyrine and menthol
    • Kramlinger, V. M., von Weymarn, L. B., and Murphy, S. E. (2012) Inhibition and inactivation of cytochrome P450 2A6 and cytochrome P450 2A13 by methofuran, β-nicotyrine and menthol Chem.-Biol. Interact. 197, 87-92
    • (2012) Chem.-Biol. Interact. , vol.197 , pp. 87-92
    • Kramlinger, V.M.1    Von Weymarn, L.B.2    Murphy, S.E.3


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