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Volumn , Issue , 2007, Pages 1973-2040

Analysis and characterization of enzymes and nucleic acids

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EID: 85083761724     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (10)

References (364)
  • 1
    • 0001818451 scopus 로고
    • Microsomal enzymes involved in toxicology: Analysis and separation
    • 1st ed., Hayes, A. W., Ed., Raven Press, New York
    • Guengerich, F. P., Microsomal enzymes involved in toxicology: analysis and separation, in Principles and Methods of Toxicology, 1st ed., Hayes, A. W., Ed., Raven Press, New York, 1982, pp. 609-634.
    • (1982) Principles and Methods of Toxicology , pp. 609-634
    • Guengerich, F.P.1
  • 2
    • 0002254766 scopus 로고
    • Analysis and characterization of enzymes
    • 2nd ed., Hayes, A. W., Ed., Raven Press, New York
    • Guengerich, F. P., Analysis and characterization of enzymes, in Principles and Methods of Toxicology, 2nd ed., Hayes, A. W., Ed., Raven Press, New York, 1989, pp. 777-814.
    • (1989) Principles and Methods of Toxicology , pp. 777-814
    • Guengerich, F.P.1
  • 3
    • 0002254766 scopus 로고
    • Analysis and characterization of enzymes
    • 3rd ed., Hayes, A. W., Ed., Raven Press, New York
    • Guengerich, F. P., Analysis and characterization of enzymes, in Principles and Methods of Toxicology, 3rd ed., Hayes, A. W., Ed., Raven Press, New York, 1994, pp. 1259-1313.
    • (1994) Principles and Methods of Toxicology , pp. 1259-1313
    • Guengerich, F.P.1
  • 4
    • 0001286370 scopus 로고    scopus 로고
    • Analysis and characterization of enzymes and nucleic acids
    • 4th ed., Hayes, A. W., Ed., Taylor & Francis, Philadelphia, PA
    • Guengerich, F. P., Analysis and characterization of enzymes and nucleic acids, in Principles and Methods of Toxicology, 4th ed., Hayes, A. W., Ed., Taylor & Francis, Philadelphia, PA, 2001, pp. 1625-1687.
    • (2001) Principles and Methods of Toxicology , pp. 1625-1687
    • Guengerich, F.P.1
  • 5
    • 84965819872 scopus 로고
    • The presence and significance of bound amino azodyes in the livers of rats fed p-dimethylaminoazobenzene
    • Miller, E. C. and Miller, J. A., The presence and significance of bound amino azodyes in the livers of rats fed p-dimethylaminoazobenzene, Cancer Res., 7, 468-480, 1947.
    • (1947) Cancer Res , vol.7 , pp. 468-480
    • Miller, E.C.1    Miller, J.A.2
  • 6
    • 0004946256 scopus 로고    scopus 로고
    • Introduction and historical perspective
    • Guengerich, F. P., Ed., in Comprehensive Toxicology, Vol. 3, Biotransformation, Guengerich, F. P., Ed., Elsevier Science, Oxford
    • Guengerich, F. P., Introduction and historical perspective, in Biotransformation, Vol. 3, Guengerich, F. P., Ed., in Comprehensive Toxicology, Vol. 3, Biotransformation, Guengerich, F. P., Ed., Elsevier Science, Oxford, 1997, pp. 1-6.
    • (1997) Biotransformation , vol.3 , pp. 1-6
    • Guengerich, F.P.1
  • 8
    • 1642281756 scopus 로고    scopus 로고
    • Drug-protein adducts: An industry perspective on minimizing the potential for drug bioactivation in drug discovery and development
    • Evans, D. C., Watt, A. P., Nicoll-Griffith, D. A., and Baillie, T. A., Drug-protein adducts: an industry perspective on minimizing the potential for drug bioactivation in drug discovery and development, Chem. Res. Toxicol., 17, 3-16, 2004.
    • (2004) Chem. Res. Toxicol , vol.17 , pp. 3-16
    • Evans, D.C.1    Watt, A.P.2    Nicoll-Griffith, D.A.3    Baillie, T.A.4
  • 9
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich, F. P., Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity, Chem. Res. Toxicol., 14, 611-650, 2001.
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 10
    • 9944265101 scopus 로고    scopus 로고
    • Principles of covalent binding of reactive metabolites and examples of activation of bis-electrophiles by conjugation
    • Guengerich, F. P., Principles of covalent binding of reactive metabolites and examples of activation of bis-electrophiles by conjugation, Arch. Biochem. Biophys., 433, 369-378, 2005.
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 369-378
    • Guengerich, F.P.1
  • 12
    • 0033627608 scopus 로고    scopus 로고
    • Profiles in toxicology: Paracelsus, herald of modern toxicology
    • Borzelleca, J. F., Profiles in toxicology: Paracelsus, herald of modern toxicology, Toxicol. Sci., 53, 2-4, 2000.
    • (2000) Toxicol. Sci , vol.53 , pp. 2-4
    • Borzelleca, J.F.1
  • 13
    • 17044392310 scopus 로고    scopus 로고
    • Life and times in biochemical toxicology
    • Guengerich, F. P., Life and times in biochemical toxicology, Int. J. Toxicol., 24, 1-17, 2005.
    • (2005) Int. J. Toxicol , vol.24 , pp. 1-17
    • Guengerich, F.P.1
  • 14
    • 0023947818 scopus 로고
    • Cytochrome P-450 isozyme selectivity in the oxidation of acetaminophen
    • Harvison, P. J., Guengerich, F. P., Rashed, M. S., and Nelson, S. D., Cytochrome P-450 isozyme selectivity in the oxidation of acetaminophen, Chem. Res. Toxicol., 1, 47-52, 1988.
    • (1988) Chem. Res. Toxicol , vol.1 , pp. 47-52
    • Harvison, P.J.1    Guengerich, F.P.2    Rashed, M.S.3    Nelson, S.D.4
  • 15
    • 0027304762 scopus 로고
    • Cytochrome P450 enzymes involved in acetaminophen activation by rat and human liver microsomes and their kinetics
    • Patten, C. J., Thomas, P. E., Guy, R. L., Lee, M., Gonzalez, F. J., Guengerich, F. P., and Yang, C. S., Cytochrome P450 enzymes involved in acetaminophen activation by rat and human liver microsomes and their kinetics, Chem. Res. Toxicol., 6, 511-518, 1993.
    • (1993) Chem. Res. Toxicol , vol.6 , pp. 511-518
    • Patten, C.J.1    Thomas, P.E.2    Guy, R.L.3    Lee, M.4    Gonzalez, F.J.5    Guengerich, F.P.6    Yang, C.S.7
  • 18
    • 0021146055 scopus 로고
    • The microsomal metabolism and site of covalent binding to protein of 3'-hydroxyacetanilide, a nonhepatotoxic positional isomer of acetaminophen
    • Streeter, A. J., Bjorge, S. M., Axworthy, D. B., Nelson, S. D., and Baillie, T. A., The microsomal metabolism and site of covalent binding to protein of 3'-hydroxyacetanilide, a nonhepatotoxic positional isomer of acetaminophen, Drug Metab. Dispos., 12, 565-576, 1984.
    • (1984) Drug Metab. Dispos , vol.12 , pp. 565-576
    • Streeter, A.J.1    Bjorge, S.M.2    Axworthy, D.B.3    Nelson, S.D.4    Baillie, T.A.5
  • 19
    • 0025009272 scopus 로고
    • Acetaminophen structure-toxicity studies: In vivo covalent binding of a nonhepatotoxic analog, 3-hydroxyacetanilide
    • Roberts, S. A., Price, V. F., and Jollow, D. J., Acetaminophen structure-toxicity studies: in vivo covalent binding of a nonhepatotoxic analog, 3-hydroxyacetanilide, Toxicol. Appl. Pharmacol., 105, 195-208, 1990.
    • (1990) Toxicol. Appl. Pharmacol , vol.105 , pp. 195-208
    • Roberts, S.A.1    Price, V.F.2    Jollow, D.J.3
  • 20
    • 0032504193 scopus 로고    scopus 로고
    • Identification of the hepatic protein targets of reactive metabolites of acetaminophen in vivo in mice using two-dimensional gel electrophoresis and mass spectrometry
    • Qiu, Y., Benet, L. Z., and Burlingame, A. L., Identification of the hepatic protein targets of reactive metabolites of acetaminophen in vivo in mice using two-dimensional gel electrophoresis and mass spectrometry, J. Biol. Chem., 273, 17940-17953, 1998.
    • (1998) J. Biol. Chem , vol.273 , pp. 17940-17953
    • Qiu, Y.1    Benet, L.Z.2    Burlingame, A.L.3
  • 21
    • 0003137106 scopus 로고
    • The isolation of a cancer-producing hydrocarbon from coal tar, Parts I, II, and III
    • Cook, J. W., Hewett, C. L., and Hieger, I., The isolation of a cancer-producing hydrocarbon from coal tar, Parts I, II, and III, J. Chem. Soc., 394-405, 1933.
    • (1933) J. Chem. Soc , pp. 394-405
    • Cook, J.W.1    Hewett, C.L.2    Hieger, I.3
  • 22
    • 0033010256 scopus 로고    scopus 로고
    • 1 exo-8,9-epoxide and relevance to toxicity and detoxication
    • 1 exo-8,9-epoxide and relevance to toxicity and detoxication, Drug Metab. Rev., 31, 141-158, 1999.
    • (1999) Drug Metab. Rev , vol.31 , pp. 141-158
    • Guengerich, F.P.1    Johnson, W.W.2
  • 24
    • 0037293066 scopus 로고    scopus 로고
    • Chemoprevention with chlorophyllin in individuals exposed to dietary anatoxin
    • Egner, P. A., Munoz, A., and Kensler, T. W., Chemoprevention with chlorophyllin in individuals exposed to dietary anatoxin, Mutat. Res., 523-524, 209-216, 2003.
    • (2003) Mutat. Res , Issue.523-524 , pp. 209-216
    • Egner, P.A.1    Munoz, A.2    Kensler, T.W.3
  • 26
    • 0037424262 scopus 로고    scopus 로고
    • Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway: Identification of novel gene clusters for cell survival
    • Kwak, M. K., Wakabayashi, N., Itoh, K., Motohashi, H., Yamamoto, M., and Kensler, T. W., Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway: identification of novel gene clusters for cell survival, J. Biol. Chem., 278, 8135-8145, 2003.
    • (2003) J. Biol. Chem , vol.278 , pp. 8135-8145
    • Kwak, M.K.1    Wakabayashi, N.2    Itoh, K.3    Motohashi, H.4    Yamamoto, M.5    Kensler, T.W.6
  • 27
    • 33845469510 scopus 로고
    • Chemical mechanisms of catalysis by cytochromes P-450: A unified view
    • Guengerich, F. P. and Macdonald, T. L., Chemical mechanisms of catalysis by cytochromes P-450: a unified view, Acct. Chem. Res., 17, 9-16, 1984.
    • (1984) Acct. Chem. Res , vol.17 , pp. 9-16
    • Guengerich, F.P.1    Macdonald, T.L.2
  • 29
    • 0020533983 scopus 로고
    • Suicidal destruction of cytochrome P-450 during oxidative drug metabolism
    • Ortiz de Montellano, P. R. and Correia, M. A., Suicidal destruction of cytochrome P-450 during oxidative drug metabolism, Annu. Rev. Pharmacol. Toxicol., 23, 481-503, 1983.
    • (1983) Annu. Rev. Pharmacol. Toxicol , vol.23 , pp. 481-503
    • Ortiz de Montellano, P.R.1    Correia, M.A.2
  • 30
    • 84892244187 scopus 로고    scopus 로고
    • Inhibition of cytochrome P450 enzymes
    • Ortiz de Montellano, P. R., Ed., Kluwer Academic/Plenum Publishers, New York
    • Correia, M. A. and Ortiz de Montellano, P. R., Inhibition of cytochrome P450 enzymes, in Cytochrome P450: Structure, Mechanism, and Biochemistry, Ortiz de Montellano, P. R., Ed., Kluwer Academic/Plenum Publishers, New York, 2005, pp. 247-322.
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 247-322
    • Correia, M.A.1    Ortiz de Montellano, P.R.2
  • 31
    • 0000126071 scopus 로고
    • Reactions catalyzed by the cytochrome P-450 system
    • Vol. 1, Jakoby, W. B., Ed., Academic Press, New York
    • Wislocki, P. G., Miwa, G. T., and Lu, A. Y. H., Reactions catalyzed by the cytochrome P-450 system, in Enzymatic Basis of Detoxication, Vol. 1, Jakoby, W. B., Ed., Academic Press, New York, 1980, pp. 135-182.
    • (1980) Enzymatic Basis of Detoxication , pp. 135-182
    • Wislocki, P.G.1    Miwa, G.T.2    Lu, A.Y.H.3
  • 32
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • Ortiz de Montellano, P. R., Ed., Kluwer Academic/Plenum Publishers, New York
    • Guengerich, F. P., Human cytochrome P450 enzymes, in Cytochrome P450: Structure, Mechanism, and Biochemistry, Ortiz de Montellano, P. R., Ed., Kluwer Academic/Plenum Publishers, New York, 2005, pp. 377-531.
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 377-531
    • Guengerich, F.P.1
  • 33
    • 0036223831 scopus 로고    scopus 로고
    • Summary of information on human CYP enzymes: Human P450 metabolism data
    • Rendic, S., Summary of information on human CYP enzymes: human P450 metabolism data, Drug Metab. Rev., 34, 83-448, 2002.
    • (2002) Drug Metab. Rev , vol.34 , pp. 83-448
    • Rendic, S.1
  • 34
    • 0002211689 scopus 로고
    • Detoxication enzymes
    • 1, Jakoby, W. B., Ed., Academic Press, New York
    • Jakoby, W. B., Detoxication enzymes, in Enzymatic Basis of Detoxication, Vol. 1, Jakoby, W. B., Ed., Academic Press, New York, 1980, pp. 1-6.
    • (1980) Enzymatic Basis of Detoxication, Vol , pp. 1-6
    • Jakoby, W.B.1
  • 35
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • Ortiz de Montellano, P. R., Ed., Kluwer Academic/Plenum Publishers, New York
    • Guengerich, F. P., Human cytochrome P450 enzymes, in Cytochrome P450: Structure, Mechanism, and Biochemistry, Ortiz de Montellano, P. R., Ed., Kluwer Academic/Plenum Publishers, New York, 2005, pp. 377-531.
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 377-531
    • Guengerich, F.P.1
  • 36
    • 0021880336 scopus 로고
    • Enzymatic activation of chemicals to toxic metabolites
    • Guengerich, F. P. and Liebler, D. C., Enzymatic activation of chemicals to toxic metabolites, CRC Crit. Rev. Toxicol., 14, 259-307, 1985.
    • (1985) CRC Crit. Rev. Toxicol , vol.14 , pp. 259-307
    • Guengerich, F.P.1    Liebler, D.C.2
  • 38
    • 0024976419 scopus 로고
    • coh substrate specificity by mutation of a single amino-acid residue
    • coh substrate specificity by mutation of a single amino-acid residue, Nature, 339, 632-634, 1989.
    • (1989) Nature , vol.339 , pp. 632-634
    • Lindberg, R.L.P.1    Negishi, M.2
  • 39
    • 0001786847 scopus 로고
    • Enzymology of human liver cytochromes P-450
    • Vol. 1, Guengerich, F. P., Ed., CRC Press, Boca Raton, FL
    • Distlerath, L. M. and Guengerich, F. P., Enzymology of human liver cytochromes P-450, in Mammalian Cytochromes P-450, Vol. 1, Guengerich, F. P., Ed., CRC Press, Boca Raton, FL, 1987, pp. 133-198.
    • (1987) Mammalian Cytochromes P-450 , pp. 133-198
    • Distlerath, L.M.1    Guengerich, F.P.2
  • 40
    • 0021156192 scopus 로고
    • Effects of nutritive factors on metabolic processes involving bioactivation and detoxication of chemicals
    • Guengerich, F. P., Effects of nutritive factors on metabolic processes involving bioactivation and detoxication of chemicals, Annu. Rev. Nutr., 4, 207-231, 1984.
    • (1984) Annu. Rev. Nutr , vol.4 , pp. 207-231
    • Guengerich, F.P.1
  • 41
    • 0032924934 scopus 로고    scopus 로고
    • Human cytochrome P-450 3A4: Regulation and role in drug metabolism
    • Guengerich, F. P., Human cytochrome P-450 3A4: regulation and role in drug metabolism, Annu. Rev. Pharmacol. Toxicol., 39, 1-17, 1999.
    • (1999) Annu. Rev. Pharmacol. Toxicol , vol.39 , pp. 1-17
    • Guengerich, F.P.1
  • 42
    • 0021254565 scopus 로고
    • Interaction of liver microsomal cytochrome P-450 and NADPH-cytochrome P-450 reductase in the presence and absence of lipid
    • Müller-Enoch, D., Churchill, P., Fleischer, S., and Guengerich, F. P., Interaction of liver microsomal cytochrome P-450 and NADPH-cytochrome P-450 reductase in the presence and absence of lipid, J. Biol. Chem., 259, 8174-8182, 1984.
    • (1984) J. Biol. Chem , vol.259 , pp. 8174-8182
    • Müller-Enoch, D.1    Churchill, P.2    Fleischer, S.3    Guengerich, F.P.4
  • 44
    • 0026654417 scopus 로고
    • Role of phospholipids in reconstituted cytochrome P450 3A forms and mechanism of their activation of catalytic activity
    • Imaoka, S., Imai, Y., Shimada, T., and Funae, Y., Role of phospholipids in reconstituted cytochrome P450 3A forms and mechanism of their activation of catalytic activity, Biochemistry, 31, 6063-6069, 1992.
    • (1992) Biochemistry , vol.31 , pp. 6063-6069
    • Imaoka, S.1    Imai, Y.2    Shimada, T.3    Funae, Y.4
  • 46
    • 0001786846 scopus 로고
    • Cytochrome P-450 enzymes and drug metabolism
    • Vol. 10, Bridges, J. W., Chasseaud, L. F., and Gibson, G. G., Eds., Taylor & Francis, London
    • Guengerich, F. P., Cytochrome P-450 enzymes and drug metabolism, in Progress in Drug Metabolism, Vol. 10, Bridges, J. W., Chasseaud, L. F., and Gibson, G. G., Eds., Taylor & Francis, London, 1987, pp. 1-54.
    • (1987) Progress in Drug Metabolism , pp. 1-54
    • Guengerich, F.P.1
  • 47
    • 0020700718 scopus 로고
    • Regulation of cytochrome P-450: Immunochemical quantitation of eight isozymes in liver microsomes of rats treated with polybrominated biphenyl congeners
    • Dannan, G. A., Guengerich, F. P., Kaminsky, L. S., and Aust, S. D., Regulation of cytochrome P-450: immunochemical quantitation of eight isozymes in liver microsomes of rats treated with polybrominated biphenyl congeners, J. Biol. Chem., 258, 1282-1288, 1983.
    • (1983) J. Biol. Chem , vol.258 , pp. 1282-1288
    • Dannan, G.A.1    Guengerich, F.P.2    Kaminsky, L.S.3    Aust, S.D.4
  • 48
    • 0020434524 scopus 로고
    • Purification and characterization of liver microsomal cytochromes P-450: Electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or ß-naphthoflavone
    • Guengerich, F. P. et al., Purification and characterization of liver microsomal cytochromes P-450: electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or ß-naphthoflavone, Biochemistry 21, 6019-6030, 1982.
    • (1982) Biochemistry , vol.21 , pp. 6019-6030
    • Guengerich, F.P.1
  • 49
    • 0022975388 scopus 로고
    • 4-steroid 5a-reductase, flavin-containing monooxygenase, and sex-specific cytochromes P-450
    • 4-steroid 5a-reductase, flavin-containing monooxygenase, and sex-specific cytochromes P-450, J. Biol. Chem., 261, 10728-10735, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 10728-10735
    • Dannan, G.A.1    Waxman, D.J.2    Guengerich, F.P.3
  • 50
    • 0021947032 scopus 로고
    • Regulation of rat hepatic cytochrome P-450: Age-dependent expression, hormonal imprinting, and xenobiotic inducibility of sex-specific isoenzymes
    • Waxman, D. J., Dannan, G. A., and Guengerich, F. P., Regulation of rat hepatic cytochrome P-450: age-dependent expression, hormonal imprinting, and xenobiotic inducibility of sex-specific isoenzymes, Biochemistry, 24, 4409-4417, 1985.
    • (1985) Biochemistry , vol.24 , pp. 4409-4417
    • Waxman, D.J.1    Dannan, G.A.2    Guengerich, F.P.3
  • 51
    • 85049459956 scopus 로고    scopus 로고
    • Enzyme regulation, in Comprehensive Toxicology, Vol. 3
    • Guengerich, F. P., Ed., Elsevier Science, Oxford
    • Waterman, M. R. and Guengerich, F. P., Enzyme regulation, in Comprehensive Toxicology, Vol. 3, Biotransformation, Guengerich, F. P., Ed., Elsevier Science, Oxford, 1997, pp. 7-14.
    • (1997) Biotransformation , pp. 7-14
    • Waterman, M.R.1    Guengerich, F.P.2
  • 52
    • 84892268812 scopus 로고    scopus 로고
    • Induction of P450 enzymes: Receptors
    • Ortiz De Montellano, P. R., Ed., Kluwer Academic/Plenum Publishers, New York
    • Williams, S. N., Dunham, E., and Bradfield, C. A., Induction of P450 enzymes: receptors, in Cytochrome P450: Structure, Mechanism, and Biochemistry, Ortiz De Montellano, P. R., Ed., Kluwer Academic/Plenum Publishers, New York, 2005, pp. 323-346.
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 323-346
    • Williams, S.N.1    Dunham, E.2    Bradfield, C.A.3
  • 53
    • 3142610292 scopus 로고
    • HLA-linked congenital adrenal hyperplasia results from a defective gene encoding a cytochrome P-450 specific for steroid 21-hydroxylation
    • White, P. C., New, M. I., and Dupont, B., HLA-linked congenital adrenal hyperplasia results from a defective gene encoding a cytochrome P-450 specific for steroid 21-hydroxylation, Proc. Natl. Acad. Sci. U.SA., 81, 7505-7509, 1984.
    • (1984) Proc. Natl. Acad. Sci. U.SA , vol.81 , pp. 7505-7509
    • White, P.C.1    New, M.I.2    Dupont, B.3
  • 54
    • 0027306807 scopus 로고
    • Regulation of steroid hydroxylase gene expression: Importance to physiology and disease
    • Keeney, D. S. and Waterman, M. R., Regulation of steroid hydroxylase gene expression: importance to physiology and disease, Pharmacol. Ther., 58, 301-317, 1993.
    • (1993) Pharmacol. Ther , vol.58 , pp. 301-317
    • Keeney, D.S.1    Waterman, M.R.2
  • 56
    • 0028858960 scopus 로고
    • Cytochrome P450 inhibitors: Evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes
    • Newton, D. J., Wang, R. W., and Lu, A. Y. H., Cytochrome P450 inhibitors: evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes, Drug Metab. Dispos., 23, 154-158, 1994.
    • (1994) Drug Metab. Dispos , vol.23 , pp. 154-158
    • Newton, D.J.1    Wang, R.W.2    Lu, A.Y.H.3
  • 57
    • 0025296345 scopus 로고
    • Metabolism of 2-acetylaminofluorene and benzo(a)pyrene and activation of food-derived heterocyclic amine mutagens by human cytochromes P-450
    • McManus, M. E., Burgess, W. M., Veronese, M. E., Huggett, A., Quattrochi, L. C., and Tukey, R. H., Metabolism of 2-acetylaminofluorene and benzo(a)pyrene and activation of food-derived heterocyclic amine mutagens by human cytochromes P-450, Cancer Res, 50, 3367-3376, 1990.
    • (1990) Cancer Res , vol.50 , pp. 3367-3376
    • McManus, M.E.1    Burgess, W.M.2    Veronese, M.E.3    Huggett, A.4    Quattrochi, L.C.5    Tukey, R.H.6
  • 58
    • 0026744568 scopus 로고
    • Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N-nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes
    • Yamazaki, H., Inui, Y., Yun, C.-H., Mimura, M., Guengerich, F. P., and Shimada, T., Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N-nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes, Carcinogenesis, 13, 1789-1794, 1992.
    • (1992) Carcinogenesis , vol.13 , pp. 1789-1794
    • Yamazaki, H.1    Inui, Y.2    Yun, C.-H.3    Mimura, M.4    Guengerich, F.P.5    Shimada, T.6
  • 59
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong, R. N., Structure, catalytic mechanism, and evolution of the glutathione transferases, Chem. Res. Toxicol., 10, 2-18,1997.
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 61
    • 0001643397 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferases, in Comprehensive Toxicology, Vol. 3
    • Guengerich, F. P., Ed., Oxford
    • Burchell, B., McGurk, K., Brierly, C. H., and Clarke, D. J., UDP-glucuronosyltransferases, in Comprehensive Toxicology, Vol. 3, Biotransformation, Guengerich, F. P., Ed., Oxford, 1997, pp. 401-135.
    • (1997) Biotransformation , pp. 401-135
    • Burchell, B.1    McGurk, K.2    Brierly, C.H.3    Clarke, D.J.4
  • 62
    • 0001564040 scopus 로고    scopus 로고
    • Epoxide hydrolases, in Comprehensive Toxicology, Vol. 3
    • Guengerich, F. P., Ed., Oxford
    • Hammock, B. D., Grant, D. F., and Storms, D. H., Epoxide hydrolases, in Comprehensive Toxicology, Vol. 3, Biotransformation, Guengerich, F. P., Ed., Oxford, 1997, pp. 283-305.
    • (1997) Biotransformation , pp. 283-305
    • Hammock, B.D.1    Grant, D.F.2    Storms, D.H.3
  • 63
    • 0022360477 scopus 로고
    • Rabbit lung flavin-containing monooxygenase: Purification, characterization, and induction during pregnancy
    • Williams, D. E., Hale, S. E., Muerhoff, A. S., and Masters, B. S. S., Rabbit lung flavin-containing monooxygenase: purification, characterization, and induction during pregnancy, Mol. Pharmacol, 28, 381-390, 1985.
    • (1985) Mol. Pharmacol , vol.28 , pp. 381-390
    • Williams, D.E.1    Hale, S.E.2    Muerhoff, A.S.3    Masters, B.S.S.4
  • 64
    • 0003085358 scopus 로고    scopus 로고
    • Monoamine oxidase and flavin-containing monooxygenases, in Comprehensive Toxicology, Vol. 3
    • Guengerich, F. P., Ed., Oxford
    • Cashman, J. R., Monoamine oxidase and flavin-containing monooxygenases, in Comprehensive Toxicology, Vol. 3, Biotransformation, Guengerich, F. P., Ed., Oxford, 1997, pp. 69-96.
    • (1997) Biotransformation , pp. 69-96
    • Cashman, J.R.1
  • 65
    • 0013569329 scopus 로고
    • Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains
    • Porter, T. D. and Kasper, C. B., Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains, Proc. Natl. Acad. Sci. USA., 82, 973-977, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 973-977
    • Porter, T.D.1    Kasper, C.B.2
  • 67
    • 30344448851 scopus 로고    scopus 로고
    • Phase 1 and phase 2 drug metabolism: Terminology that we should phase out
    • Josephy, P. D., Guengerich, F. P., and Miners, J. O., Phase 1 and phase 2 drug metabolism: terminology that we should phase out, Drug Metab. Rev., 37, 579-584, 2005.
    • (2005) Drug Metab. Rev , vol.37 , pp. 579-584
    • Josephy, P.D.1    Guengerich, F.P.2    Miners, J.O.3
  • 68
    • 0020585252 scopus 로고
    • Metabolism of acrylonitrile by isolated rat hepatocytes
    • Geiger, L. E., Hogy, L. L., and Guengerich, F. P., Metabolism of acrylonitrile by isolated rat hepatocytes, Cancer Res., 43, 3080-3087, 1983.
    • (1983) Cancer Res , vol.43 , pp. 3080-3087
    • Geiger, L.E.1    Hogy, L.L.2    Guengerich, F.P.3
  • 69
    • 0019825946 scopus 로고
    • In vitro metabolism of acrylonitrile to 2-cyanoethylene oxide, reaction with glutathione, and irreversible binding to proteins and nucleic acids
    • Guengerich, F. P., Geiger, L. E., Hogy, L. L., and Wright, P. L., In vitro metabolism of acrylonitrile to 2-cyanoethylene oxide, reaction with glutathione, and irreversible binding to proteins and nucleic acids, Cancer Res., 41, 4925-4933, 1981.
    • (1981) Cancer Res , vol.41 , pp. 4925-4933
    • Guengerich, F.P.1    Geiger, L.E.2    Hogy, L.L.3    Wright, P.L.4
  • 70
    • 0022497049 scopus 로고
    • In vivo interaction of acrylonitrile and 2-cyanoethylene oxide with DNA in rats
    • Hogy, L. L. and Guengerich, F. P., In vivo interaction of acrylonitrile and 2-cyanoethylene oxide with DNA in rats, Cancer Res., 46, 3932-3938, 1986.
    • (1986) Cancer Res , vol.46 , pp. 3932-3938
    • Hogy, L.L.1    Guengerich, F.P.2
  • 71
    • 0030614916 scopus 로고    scopus 로고
    • 2-ethenoguanine and 5,6,7,9-tetrahydro-7-hydroxy-9-oxoimidazo[1,2-a]purine in DNA treated with 2-chlorooxirane by high-performance liquid chromatography/mass spectrometry and comparison of amounts with other adducts
    • 2-ethenoguanine and 5,6,7,9-tetrahydro-7-hydroxy-9-oxoimidazo[1,2-a]purine in DNA treated with 2-chlorooxirane by high-performance liquid chromatography/mass spectrometry and comparison of amounts with other adducts, Chem. Res. Toxicol., 10, 242-247, 1997.
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 242-247
    • Müller, M.1    Belas, F.J.2    Blair, I.A.3    Guengerich, F.P.4
  • 74
    • 0018697931 scopus 로고
    • Activation of vinyl chloride to covalently bound metabolites: Roles of 2-chloroethylene oxide and 2-chloroacetal-dehyde
    • Guengerich, F. P., Crawford, Jr., W. M., and Watanabe, P. G., Activation of vinyl chloride to covalently bound metabolites: roles of 2-chloroethylene oxide and 2-chloroacetal-dehyde, Biochemistry, 18, 5177-5182, 1979.
    • (1979) Biochemistry , vol.18 , pp. 5177-5182
    • Guengerich, F.P.1    Crawford, W.M.2    Watanabe, P.G.3
  • 75
    • 0021047310 scopus 로고
    • Olefin oxidation by cytochrome P-450: Evidence for group migration in catalytic intermediates formed with vinylidene chloride and trans-1-phenyl-1-butene
    • Liebler, D. C. and Guengerich, F. P., Olefin oxidation by cytochrome P-450: evidence for group migration in catalytic intermediates formed with vinylidene chloride and trans-1-phenyl-1-butene, Biochemistry, 22, 5482-5489, 1983.
    • (1983) Biochemistry , vol.22 , pp. 5482-5489
    • Liebler, D.C.1    Guengerich, F.P.2
  • 76
    • 0020683796 scopus 로고
    • Metabolism of trichlo-roethylene in isolated hepatocytes, microsomes, and reconstituted enzyme systems containing cytochrome P-450
    • Miller, R. E. and Guengerich, F. P., Metabolism of trichlo-roethylene in isolated hepatocytes, microsomes, and reconstituted enzyme systems containing cytochrome P-450, Cancer Res., 43, 1145-1152, 1983.
    • (1983) Cancer Res , vol.43 , pp. 1145-1152
    • Miller, R.E.1    Guengerich, F.P.2
  • 77
    • 0019808974 scopus 로고
    • Roles of 2-haloethylene oxides and 2-haloacetaldehydes derived from vinyl bromide and vinyl chloride in irreversible binding to protein and DNA
    • Guengerich, F. P., Mason, P. S., Stott, W. T., Fox, T. R., and Watanabe, P. G., Roles of 2-haloethylene oxides and 2-haloacetaldehydes derived from vinyl bromide and vinyl chloride in irreversible binding to protein and DNA, Cancer Res., 41, 4391-4398, 1981.
    • (1981) Cancer Res , vol.41 , pp. 4391-4398
    • Guengerich, F.P.1    Mason, P.S.2    Stott, W.T.3    Fox, T.R.4    Watanabe, P.G.5
  • 78
    • 0026035519 scopus 로고
    • Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects
    • Guengerich, F. P., Kim, D.-H., and Iwasaki, M., Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects, Chem. Res. Toxicol., 4, 168-179, 1991.
    • (1991) Chem. Res. Toxicol , vol.4 , pp. 168-179
    • Guengerich, F.P.1    Kim, D.-H.2    Iwasaki, M.3
  • 79
    • 0019404603 scopus 로고
    • The metabolic formation of N-acetyl-S-2-hydroxyethyl-l-cys-teine from tetradeutero-1,2-dibromoethane: Relative importance of oxidation and glutathione conjugation in vivo
    • van Bladeren, P. J., Breimer, D. D., van Huijgevoort, J. A. T. C. M., Vermeulen, N. P. E., and van der Gen, A., The metabolic formation of N-acetyl-S-2-hydroxyethyl-l-cys-teine from tetradeutero-1,2-dibromoethane: relative importance of oxidation and glutathione conjugation in vivo, Biochem. Pharmacol., 30, 2499-2502, 1981.
    • (1981) Biochem. Pharmacol , vol.30 , pp. 2499-2502
    • van Bladeren, P.J.1    Breimer, D.D.2    van Huijgevoort, J.A.T.C.M.3    Vermeulen, N.P.E.4    van der Gen, A.5
  • 81
    • 0024424137 scopus 로고
    • 7-guanyl)ethyl]-N-acetylcysteine in urine following administration of ethylene dibromide to rats
    • 7-guanyl)ethyl]-N-acetylcysteine in urine following administration of ethylene dibromide to rats, Cancer Res., 49, 5843-5851, 1989.
    • (1989) Cancer Res , vol.49 , pp. 5843-5851
    • Kim, D.H.1    Guengerich, F.P.2
  • 83
    • 0038544198 scopus 로고    scopus 로고
    • Activation of dihaloalkanes by thiol-dependent mechanisms
    • Guengerich, F. P., Activation of dihaloalkanes by thiol-dependent mechanisms, J. Biochem. Mol. Biol., 36, 20-27, 2003.
    • (2003) J. Biochem. Mol. Biol , vol.36 , pp. 20-27
    • Guengerich, F.P.1
  • 84
    • 0025268190 scopus 로고
    • Selectivity of rat and human glutathione S-transferases in activation of ethylene dibromide by glutathione conjugation and DNA binding and induction of unscheduled DNA synthesis in human hepatocytes
    • Cmarik, J. L., Inskeep, P. B., Meyer, D. J., Meredith, M. J., Ketterer, B., and Guengerich, F. P., Selectivity of rat and human glutathione S-transferases in activation of ethylene dibromide by glutathione conjugation and DNA binding and induction of unscheduled DNA synthesis in human hepatocytes, Cancer Res., 50, 2747-2752, 1990.
    • (1990) Cancer Res , vol.50 , pp. 2747-2752
    • Cmarik, J.L.1    Inskeep, P.B.2    Meyer, D.J.3    Meredith, M.J.4    Ketterer, B.5    Guengerich, F.P.6
  • 85
    • 0008252723 scopus 로고
    • 7-guanyl)ethyl]glutathione adduct in glu-tathione-mediated binding of 1,2-dibromoethane to DNA
    • 7-guanyl)ethyl]glutathione adduct in glu-tathione-mediated binding of 1,2-dibromoethane to DNA, Proc. Natl. Acad. Sci. U.S.A., 80, 5266-5270, 1983.
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 5266-5270
    • Ozawa, N.1    Guengerich, F.P.2
  • 88
    • 0018286242 scopus 로고
    • Metabolism of estrogens: Natural and synthetic
    • Bolt, H. M., Metabolism of estrogens: natural and synthetic, Pharmacol. Ther., 4, 155-181, 1979.
    • (1979) Pharmacol. Ther , vol.4 , pp. 155-181
    • Bolt, H.M.1
  • 90
    • 0021130765 scopus 로고
    • Metabolic oxidation phenotypes as markers for susceptibility to lung cancer
    • Ayesh, R., Idle, J. R., Ritchie, J. C., Crothers, M. J., and Hetzel, M. R., Metabolic oxidation phenotypes as markers for susceptibility to lung cancer, Nature, 312, 169-170, 1984.
    • (1984) Nature , vol.312 , pp. 169-170
    • Ayesh, R.1    Idle, J.R.2    Ritchie, J.C.3    Crothers, M.J.4    Hetzel, M.R.5
  • 91
    • 0019380168 scopus 로고
    • Some observations on the oxidation phenotype status of Nigerian patients presenting with cancer
    • Idle, J. R., Mahgoub, A., Sloan, T. P., Smith, R. L., Mbanefo, C. O., and Bababunmi, E. A., Some observations on the oxidation phenotype status of Nigerian patients presenting with cancer, Cancer Lett., 11, 331-338, 1981.
    • (1981) Cancer Lett , vol.11 , pp. 331-338
    • Idle, J.R.1    Mahgoub, A.2    Sloan, T.P.3    Smith, R.L.4    Mbanefo, C.O.5    Bababunmi, E.A.6
  • 92
    • 0025940815 scopus 로고
    • Molecular genetics of the debrisoquin-sparteine polymorphism
    • Gonzalez, F. J. and Meyer, U. A., Molecular genetics of the debrisoquin-sparteine polymorphism, Clin. Pharmacol. Ther., 50, 233-238, 1991.
    • (1991) Clin. Pharmacol. Ther , vol.50 , pp. 233-238
    • Gonzalez, F.J.1    Meyer, U.A.2
  • 93
    • 0017687117 scopus 로고
    • Studies on the activation of a model furan compound: Toxicity and covalent binding of 2-(N-ethylcarbamoylhydroxymethyl)furan
    • Guengerich, F. P., Studies on the activation of a model furan compound: toxicity and covalent binding of 2-(N-ethylcarbamoylhydroxymethyl)furan, Biochem. Pharmacol., 26, 1909-1915, 1977.
    • (1977) Biochem. Pharmacol , vol.26 , pp. 1909-1915
    • Guengerich, F.P.1
  • 94
    • 0016174577 scopus 로고
    • Preparation and properties of partially purified cytochrome P-450 and reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase from rabbit liver microsomes
    • van der Hoeven, T. A. and Coon, M. J., Preparation and properties of partially purified cytochrome P-450 and reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase from rabbit liver microsomes, J. Biol. Chem., 249, 6302-6310, 1974.
    • (1974) J. Biol. Chem , vol.249 , pp. 6302-6310
    • van der Hoeven, T.A.1    Coon, M.J.2
  • 95
    • 0017870984 scopus 로고
    • The drug and carcinogen metabolism system of rat colon microsomes
    • Fang, W. F. and Strobel, H. W., The drug and carcinogen metabolism system of rat colon microsomes, Arch. Biochem. Biophys., 186, 128-138, 1978.
    • (1978) Arch. Biochem. Biophys , vol.186 , pp. 128-138
    • Fang, W.F.1    Strobel, H.W.2
  • 97
    • 0016704020 scopus 로고
    • Solubilization and partial purification of cytochrome P-450 from rat lung microsomes
    • Jernström, B., Capdevila, J., Jakobsson, S., and Orrenius, S., Solubilization and partial purification of cytochrome P-450 from rat lung microsomes, Biochem. Biophys. Res. Commun., 64, 814-822, 1975.
    • (1975) Biochem. Biophys. Res. Commun , vol.64 , pp. 814-822
    • Jernström, B.1    Capdevila, J.2    Jakobsson, S.3    Orrenius, S.4
  • 98
    • 0015906360 scopus 로고
    • Isolation of rat liver microsomes by gel filtration
    • Taugen, O., Jonasson, J., and Orrenius, S., Isolation of rat liver microsomes by gel filtration, Anal. Biochem., 54, 597-603, 1973.
    • (1973) Anal. Biochem , vol.54 , pp. 597-603
    • Taugen, O.1    Jonasson, J.2    Orrenius, S.3
  • 100
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemopro-tein nature
    • Omura, T. and Sato, R., The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemopro-tein nature, J. Biol. Chem., 239, 2370-2378, 1964.
    • (1964) J. Biol. Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 101
    • 0017057951 scopus 로고
    • Properties of electrophoret-ically homogenous phenobarbital-inducible and ß-naph-thoflavone-inducible forms of liver microsomal cytochrome P-450
    • Haugen, D. A. and Coon, M. J., Properties of electrophoret-ically homogenous phenobarbital-inducible and ß-naph-thoflavone-inducible forms of liver microsomal cytochrome P-450, J. Biol. Chem., 251, 7929-7939, 1976.
    • (1976) J. Biol. Chem , vol.251 , pp. 7929-7939
    • Haugen, D.A.1    Coon, M.J.2
  • 102
    • 0016633563 scopus 로고
    • Multiple forms of cytochrome P-450 in phenobarbital- and 3-meth-ylcholanthrene-treated rats
    • Ryan, D., Lu, A. Y. H., West, S., and Levin, W., Multiple forms of cytochrome P-450 in phenobarbital- and 3-meth-ylcholanthrene-treated rats, J. Biol. Chem., 250, 2157-2163, 1975.
    • (1975) J. Biol. Chem , vol.250 , pp. 2157-2163
    • Ryan, D.1    Lu, A.Y.H.2    West, S.3    Levin, W.4
  • 103
    • 0000124075 scopus 로고
    • Isolation of cytochromes P-450 and P-420
    • Omura, T. and Sato, R., Isolation of cytochromes P-450 and P-420, Meth. Enzymol., 10, 556-561, 1967.
    • (1967) Meth. Enzymol , vol.10 , pp. 556-561
    • Omura, T.1    Sato, R.2
  • 104
    • 0017168412 scopus 로고
    • Quantitative determination of cytochrome P-450 in rat liver homogenate
    • Matsubara, T., Koike, M., Touchi, A., Tochino, Y., and Sugeno, K., Quantitative determination of cytochrome P-450 in rat liver homogenate, Anal. Biochem., 75, 596-603, 1976.
    • (1976) Anal. Biochem , vol.75 , pp. 596-603
    • Matsubara, T.1    Koike, M.2    Touchi, A.3    Tochino, Y.4    Sugeno, K.5
  • 105
    • 0018081845 scopus 로고
    • Measurements of cytochrome P-450 in the presence of large amounts of contaminating hemoglobin and methemoglobin
    • Johannesen, K. A. M. and DePierre, J. W., Measurements of cytochrome P-450 in the presence of large amounts of contaminating hemoglobin and methemoglobin, Anal. Biochem., 86, 725-732, 1978.
    • (1978) Anal. Biochem , vol.86 , pp. 725-732
    • Johannesen, K.A.M.1    DePierre, J.W.2
  • 106
    • 73849173955 scopus 로고
    • Hepatic triphosphopy-ridine nucleotide-cytochrome c reductase: Isolation, characterization, and kinetic studies
    • Phillips, A. H. and Langdon, R. G., Hepatic triphosphopy-ridine nucleotide-cytochrome c reductase: isolation, characterization, and kinetic studies, J. Biol. Chem., 237, 2652-2660, 1962.
    • (1962) J. Biol. Chem , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 107
    • 0017801794 scopus 로고
    • Purified liver microsomal NADPH-cytochrome P-450 reductase: Spectral characterization of oxidation-reduction states
    • Vermilion, J. L. and Coon, M. J., Purified liver microsomal NADPH-cytochrome P-450 reductase: spectral characterization of oxidation-reduction states, J. Biol. Chem., 253, 2694-2704, 1978.
    • (1978) J. Biol. Chem , vol.253 , pp. 2694-2704
    • Vermilion, J.L.1    Coon, M.J.2
  • 108
    • 0015465498 scopus 로고
    • Microsomal electron transport: Tetrazolium reduction by rat liver microsomal NADPH-cytochrome c reductase
    • Roerig, D. L., Mascaro, Jr., L., and Aust, S. D., Microsomal electron transport: tetrazolium reduction by rat liver microsomal NADPH-cytochrome c reductase, Arch. Biochem. Biophys., 153, 475-479, 1972.
    • (1972) Arch. Biochem. Biophys , vol.153 , pp. 475-479
    • Roerig, D.L.1    Mascaro, L.2    Aust, S.D.3
  • 109
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash, T., The colorimetric estimation of formaldehyde by means of the Hantzsch reaction, Biochem. J., 55, 416-421, 1953.
    • (1953) Biochem. J , vol.55 , pp. 416-421
    • Nash, T.1
  • 110
    • 33751368029 scopus 로고
    • Biochemical and pharmacological changes in the rat following chronic administration of morphine, nalorphine, and normorphine
    • Cochin, J. and Axelrod, J., Biochemical and pharmacological changes in the rat following chronic administration of morphine, nalorphine, and normorphine, J. Pharmacol. Exp. Ther., 125, 105-110, 1959.
    • (1959) J. Pharmacol. Exp. Ther , vol.125 , pp. 105-110
    • Cochin, J.1    Axelrod, J.2
  • 111
    • 0018140102 scopus 로고
    • Reconstituted mammalian mixed-function oxidases: Requirements, specificities and other properties
    • Lu, A. Y. H. and West, S. B., Reconstituted mammalian mixed-function oxidases: requirements, specificities and other properties, Pharmacol. Ther., 2, 337-358, 1978.
    • (1978) Pharmacol. Ther , vol.2 , pp. 337-358
    • Lu, A.Y.H.1    West, S.B.2
  • 112
    • 0016814154 scopus 로고
    • Purified liver microsomal cytochrome P-450: Electron-accepting properties and oxidation-reduction potential
    • Guengerich, F. P., Ballou, D. P., and Coon, M. J., Purified liver microsomal cytochrome P-450: electron-accepting properties and oxidation-reduction potential, J. Biol. Chem., 250, 7405-7414, 1975.
    • (1975) J. Biol. Chem , vol.250 , pp. 7405-7414
    • Guengerich, F.P.1    Ballou, D.P.2    Coon, M.J.3
  • 113
    • 0018802951 scopus 로고
    • Hydrodynamic characterization of highly purified and functionally active liver microsomal cytochrome P-450
    • Guengerich, F. P. and Holladay, L. A., Hydrodynamic characterization of highly purified and functionally active liver microsomal cytochrome P-450, Biochemistry, 18, 5442-5449, 1979.
    • (1979) Biochemistry , vol.18 , pp. 5442-5449
    • Guengerich, F.P.1    Holladay, L.A.2
  • 114
    • 0023180336 scopus 로고
    • Regulation of cytochrome P-450j, a high-affinity N-nitrosodimethylamine demethylase, in rat hepatic microsomes
    • Thomas, P. E., Bandiera, S., Maines, S. L., Ryan, D. E., and Levin, W., Regulation of cytochrome P-450j, a high-affinity N-nitrosodimethylamine demethylase, in rat hepatic microsomes, Biochemistry, 26, 2280-2289, 1987.
    • (1987) Biochemistry , vol.26 , pp. 2280-2289
    • Thomas, P.E.1    Bandiera, S.2    Maines, S.L.3    Ryan, D.E.4    Levin, W.5
  • 115
    • 0023877321 scopus 로고
    • Metabolism of N-nitrosodialkylamines by human liver microsomes
    • Yoo, J. S. H., Guengerich, F. P., and Yang, C. S., Metabolism of N-nitrosodialkylamines by human liver microsomes, Cancer Res., 48, 1499-1504, 1988.
    • (1988) Cancer Res , vol.48 , pp. 1499-1504
    • Yoo, J.S.H.1    Guengerich, F.P.2    Yang, C.S.3
  • 116
    • 0014791009 scopus 로고
    • Properties of a solubilized form of the cytochrome P-450-containing mixed-function oxidase of liver microsomes
    • Lu, A. Y. H., Strobel, H. W., and Coon, M. J., Properties of a solubilized form of the cytochrome P-450-containing mixed-function oxidase of liver microsomes, Mol. Pharmacol., 6, 213-220, 1970.
    • (1970) Mol. Pharmacol , vol.6 , pp. 213-220
    • Lu, A.Y.H.1    Strobel, H.W.2    Coon, M.J.3
  • 117
    • 0017409578 scopus 로고
    • Hydrogen peroxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome P-450
    • Nordblom, G. D. and Coon, M. J., Hydrogen peroxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome P-450, Arch. Biochem. Biophys., 180, 343-347, 1977.
    • (1977) Arch. Biochem. Biophys , vol.180 , pp. 343-347
    • Nordblom, G.D.1    Coon, M.J.2
  • 118
    • 0017283437 scopus 로고
    • Studies of the metabolism of parathion with an apparently homogeneous preparation of rabbit liver cytochrome P-450
    • Kamataki, T., Lin, M. L., Belcher, D. H., and Neal, R. A., Studies of the metabolism of parathion with an apparently homogeneous preparation of rabbit liver cytochrome P-450, Drug Metab. Dispos., 4, 180-189, 1976.
    • (1976) Drug Metab. Dispos , vol.4 , pp. 180-189
    • Kamataki, T.1    Lin, M.L.2    Belcher, D.H.3    Neal, R.A.4
  • 119
    • 0017847465 scopus 로고
    • An improved assay of 7-ethoxycoumarin O-deethylase activity: Induction of hepatic enzyme activity in C57BL/6J and DBA/2J mice by phenobarbital, 3-methylcholanthrene and 2,3,7,8-tetra-chlorodibenzo-p-dioxin
    • Greenlee, W. F. and Poland, A., An improved assay of 7-ethoxycoumarin O-deethylase activity: induction of hepatic enzyme activity in C57BL/6J and DBA/2J mice by phenobarbital, 3-methylcholanthrene and 2,3,7,8-tetra-chlorodibenzo-p-dioxin, J. Pharmacol. Exp. Ther., 205, 596-605, 1978.
    • (1978) J. Pharmacol. Exp. Ther , vol.205 , pp. 596-605
    • Greenlee, W.F.1    Poland, A.2
  • 120
    • 0018265604 scopus 로고
    • Separation and purification of multiple forms of microsomal cytochrome P-450: Partial characterization of three apparently homogeneous cytochromes P-450 prepared from livers of phenobarbital- and 3-methyl-cholanthrene-treated rats
    • Guengerich, F. P., Separation and purification of multiple forms of microsomal cytochrome P-450: partial characterization of three apparently homogeneous cytochromes P-450 prepared from livers of phenobarbital- and 3-methyl-cholanthrene-treated rats, J. Biol. Chem., 253, 7931-7939, 1978.
    • (1978) J. Biol. Chem , vol.253 , pp. 7931-7939
    • Guengerich, F.P.1
  • 121
    • 0014410265 scopus 로고
    • Substrate-inducible microsomal arylhydroxylase in mammalian cell culture: Assay and properties of induced enzyme
    • Nebert, D. W. and Gelboin, H. V., Substrate-inducible microsomal arylhydroxylase in mammalian cell culture: assay and properties of induced enzyme, J. Biol. Chem., 243, 6242-6249, 1968.
    • (1968) J. Biol. Chem , vol.243 , pp. 6242-6249
    • Nebert, D.W.1    Gelboin, H.V.2
  • 122
    • 0015858864 scopus 로고
    • A modified method for the assay of benzo(a)pyrene hydroxylase
    • Dehnen, W., Tomingas, R., and Roos, J., A modified method for the assay of benzo(a)pyrene hydroxylase, Anal. Biochem., 53, 373-383, 1973.
    • (1973) Anal. Biochem , vol.53 , pp. 373-383
    • Dehnen, W.1    Tomingas, R.2    Roos, J.3
  • 123
    • 0017794226 scopus 로고
    • Radioactive assay of aryl hydrocarbon monooxygenase and epoxide hydrase
    • DePierre, J. W., Johannesen, K. A. M., Moron, M. S., and Seidegård, J., Radioactive assay of aryl hydrocarbon monooxygenase and epoxide hydrase, Meth. Enzymol., 52, 412-418, 1978.
    • (1978) Meth. Enzymol , vol.52 , pp. 412-418
    • DePierre, J.W.1    Johannesen, K.A.M.2    Moron, M.S.3    Seidegård, J.4
  • 124
    • 0016274247 scopus 로고
    • High-pressure liquid chromatographic analysis of benzo(a)pyrene metabolism and covalent binding and the mechanism of action of 7,8-benzoflavone and 1,2-epoxy-3,3,3-trichloropropane
    • Selkirk, J. K., Croy, R. G., Roller, P. P., and Gelboin, H. V., High-pressure liquid chromatographic analysis of benzo(a)pyrene metabolism and covalent binding and the mechanism of action of 7,8-benzoflavone and 1,2-epoxy-3,3,3-trichloropropane, Cancer Res., 34, 3474-3480, 1974.
    • (1974) Cancer Res , vol.34 , pp. 3474-3480
    • Selkirk, J.K.1    Croy, R.G.2    Roller, P.P.3    Gelboin, H.V.4
  • 125
    • 0017831697 scopus 로고
    • Analysis of polycyclic aromatic hydrocarbons and their metabolites by high-pressure liquid chromatography
    • Thakker, D. R., Yagi, H., and Jerina, D. M., Analysis of polycyclic aromatic hydrocarbons and their metabolites by high-pressure liquid chromatography, Meth. Enzymol., 52, 279-296, 1978.
    • (1978) Meth. Enzymol , vol.52 , pp. 279-296
    • Thakker, D.R.1    Yagi, H.2    Jerina, D.M.3
  • 126
    • 0028797624 scopus 로고
    • Oxidation of benzo(a)pyrene by recombinant human cytochrome P450 enzymes
    • Bauer, E., Guo, Z., Ueng, Y.-F., Bell, L. C., and Guenger-ich, F. P., Oxidation of benzo(a)pyrene by recombinant human cytochrome P450 enzymes, Chem. Res. Toxicol., 8, 136-142, 1995.
    • (1995) Chem. Res. Toxicol , vol.8 , pp. 136-142
    • Bauer, E.1    Guo, Z.2    Ueng, Y.-F.3    Bell, L.C.4    Guenger-ich, F.P.5
  • 127
    • 0018139858 scopus 로고
    • Regio- and stereoselectivity of various forms of purified cytochrome P-450 in the metabolism of benzo(a)pyrene and (-)trans-7,8-dihydroxy-7,8-dihydrobenzo(a)pyrene as shown by product formation and binding to DNA
    • Deutsch, J., Leutz, J. C., Yang, S. K., Gelboin, H. V., Chiang, Y. L., Vatsis, K. P., and Coon, M. J., Regio- and stereoselectivity of various forms of purified cytochrome P-450 in the metabolism of benzo(a)pyrene and (-)trans-7,8-dihydroxy-7,8-dihydrobenzo(a)pyrene as shown by product formation and binding to DNA, Proc. Natl. Acad. Sci. USA, 75, 3123-3127, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3123-3127
    • Deutsch, J.1    Leutz, J.C.2    Yang, S.K.3    Gelboin, H.V.4    Chiang, Y.L.5    Vatsis, K.P.6    Coon, M.J.7
  • 128
    • 0022998708 scopus 로고
    • Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism
    • Guengerich, F. P., Martin, M. V., Beaune, P. H., Kremers, P., Wolff, T., and Waxman, D. J., Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism, J. Biol. Chem, 261, 5051-5060, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 5051-5060
    • Guengerich, F.P.1    Martin, M.V.2    Beaune, P.H.3    Kremers, P.4    Wolff, T.5    Waxman, D.J.6
  • 129
    • 0022550688 scopus 로고
    • Oxidation of 4-aryl-and 4-alkyl-substituted 2,6-dimethyl-3,5-bis(alkoxycarbo-nyl)-1,4-dihydropyridines by human liver microsomes and immunochemical evidence for the involvement of a form of cytochrome P-450
    • Böcker, R. H. and Guengerich, F. P., Oxidation of 4-aryl-and 4-alkyl-substituted 2,6-dimethyl-3,5-bis(alkoxycarbo-nyl)-1,4-dihydropyridines by human liver microsomes and immunochemical evidence for the involvement of a form of cytochrome P-450, J. Med. Chem, 29, 1596-1603, 1986.
    • (1986) J. Med. Chem , vol.29 , pp. 1596-1603
    • Böcker, R.H.1    Guengerich, F.P.2
  • 130
    • 0025860978 scopus 로고
    • Oxidation of dihydro-pyridine calcium channel blockers and analogues by human liver cytochrome P-450 IIIA4
    • Guengerich, F. P., Brian, W. R., Iwasaki, M., Sari, M.-A., Bäärnhielm, C., and Berntsson, P., Oxidation of dihydro-pyridine calcium channel blockers and analogues by human liver cytochrome P-450 IIIA4, J. Med. Chem., 34, 1838-1844, 1991.
    • (1991) J. Med. Chem , vol.34 , pp. 1838-1844
    • Guengerich, F.P.1    Brian, W.R.2    Iwasaki, M.3    Sari, M.-A.4    Bäärnhielm, C.5    Berntsson, P.6
  • 132
    • 0028037221 scopus 로고
    • Effect of fasting and obesity in humans on the 6-hydrox-ylation of chloroxazone: A putative probe of CYP2E1 activity
    • O'Shea, D., Davis, S. N., Kim, R. B., and Wilkinson, G. R., Effect of fasting and obesity in humans on the 6-hydrox-ylation of chloroxazone: a putative probe of CYP2E1 activity, Clin. Pharmacol. Ther., 56, 359-367, 1994.
    • (1994) Clin. Pharmacol. Ther , vol.56 , pp. 359-367
    • O'Shea, D.1    Davis, S.N.2    Kim, R.B.3    Wilkinson, G.R.4
  • 135
    • 0025273823 scopus 로고
    • Enzymatic oxidation of xenobiotic chemicals
    • Guengerich, F. P., Enzymatic oxidation of xenobiotic chemicals, CRC Crit. Rev. Biochem. Mol. Biol., 25, 97-153, 1990.
    • (1990) CRC Crit. Rev. Biochem. Mol. Biol , vol.25 , pp. 97-153
    • Guengerich, F.P.1
  • 136
    • 0027470428 scopus 로고
    • Evidence for specific base catalysis in N-dealkylation reactions catalyzed by cytochrome P450 and chloroperoxidase: Differences in rates of deprotonation of aminium radicals as an explanation for high kinetic hydrogen isotope effects observed with peroxidases
    • Okazaki, O. and Guengerich, F. P., Evidence for specific base catalysis in N-dealkylation reactions catalyzed by cytochrome P450 and chloroperoxidase: differences in rates of deprotonation of aminium radicals as an explanation for high kinetic hydrogen isotope effects observed with peroxidases, J. Biol. Chem., 268, 1546-1552, 1993.
    • (1993) J. Biol. Chem , vol.268 , pp. 1546-1552
    • Okazaki, O.1    Guengerich, F.P.2
  • 137
    • 0029970784 scopus 로고    scopus 로고
    • Evidence for a one-electron oxidation mechanism in N-dealkylation of N,N-dialkylanilines by cytochrome P450 2B1: Kinetic hydrogen isotope effects, linear free energy relationships, comparisons with horseradish peroxidase, and studies with oxygen surrogates
    • Guengerich, F. P., Yun, C.-H., and Macdonald, T. L., Evidence for a one-electron oxidation mechanism in N-dealkylation of N,N-dialkylanilines by cytochrome P450 2B1: kinetic hydrogen isotope effects, linear free energy relationships, comparisons with horseradish peroxidase, and studies with oxygen surrogates, J. Biol. Chem., 271, 27321-27329, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 27321-27329
    • Guengerich, F.P.1    Yun, C.-H.2    Macdonald, T.L.3
  • 138
    • 0021100472 scopus 로고
    • The use of intramolecular isotope effects to distinguish between deprotonation and hydrogen atom abstraction mechanisms in cytochrome P-450- and peroxidase-catalyzed N-demethylation reactions
    • Miwa, G. T., Walsh, J. S., Kedderis, G. L., and Hollenberg, P. F., The use of intramolecular isotope effects to distinguish between deprotonation and hydrogen atom abstraction mechanisms in cytochrome P-450- and peroxidase-catalyzed N-demethylation reactions, J. Biol. Chem., 258, 14445-14449, 1983.
    • (1983) J. Biol. Chem , vol.258 , pp. 14445-14449
    • Miwa, G.T.1    Walsh, J.S.2    Kedderis, G.L.3    Hollenberg, P.F.4
  • 141
    • 0018076222 scopus 로고
    • Vinyl carbam-ate as a promutagen and a more carcinogenic analog of ethyl carbamate
    • Dahl, G. A., Miller, J. A., and Miller, E. C., Vinyl carbam-ate as a promutagen and a more carcinogenic analog of ethyl carbamate, Cancer Res., 38, 3793-3804, 1978.
    • (1978) Cancer Res , vol.38 , pp. 3793-3804
    • Dahl, G.A.1    Miller, J.A.2    Miller, E.C.3
  • 142
    • 0018898536 scopus 로고
    • Comparative carcinogenicities and mutagenicities of vinyl carbamate, ethyl carbamate, and ethyl N-hydroxycarbamate
    • Dahl, G. A., Miller, E. C., and Miller, J. A., Comparative carcinogenicities and mutagenicities of vinyl carbamate, ethyl carbamate, and ethyl N-hydroxycarbamate, Cancer Res., 40, 1194-1203, 1980.
    • (1980) Cancer Res , vol.40 , pp. 1194-1203
    • Dahl, G.A.1    Miller, E.C.2    Miller, J.A.3
  • 143
    • 0025193585 scopus 로고
    • 6-Ethenoadenosine formation, mutagenicity and murine tumor induction as indicators of the generation of an electrophilic epoxide metabolite of the closely related carcinogens ethyl carbamate (urethane) and vinyl carbamate
    • 6-Ethenoadenosine formation, mutagenicity and murine tumor induction as indicators of the generation of an electrophilic epoxide metabolite of the closely related carcinogens ethyl carbamate (urethane) and vinyl carbamate, Carcinogenesis, 11, 463-473, 1990.
    • (1990) Carcinogenesis , vol.11 , pp. 463-473
    • Leithauser, M.T.1    Liem, A.2    Stewart, B.C.3    Miller, E.C.4    Miller, J.A.5
  • 144
    • 0023263168 scopus 로고
    • Nature of N-nitrosodimethylamine demethylase and its inhibitors
    • Yoo, J. S. H., Cheung, R. J., Patten, C. J., Wade, D., and Yang, C. S., Nature of N-nitrosodimethylamine demethylase and its inhibitors, Cancer Res., 47, 3378-3383, 1987.
    • (1987) Cancer Res , vol.47 , pp. 3378-3383
    • Yoo, J.S.H.1    Cheung, R.J.2    Patten, C.J.3    Wade, D.4    Yang, C.S.5
  • 148
    • 0035912853 scopus 로고    scopus 로고
    • Binding and oxidation of alkyl 4-nitrophenyl ethers by rabbit cytochrome P450 1A2: Evidence for two binding sites
    • Miller, G. P. and Guengerich, F. P., Binding and oxidation of alkyl 4-nitrophenyl ethers by rabbit cytochrome P450 1A2: evidence for two binding sites, Biochemistry, 40, 7262-7272, 2001.
    • (2001) Biochemistry , vol.40 , pp. 7262-7272
    • Miller, G.P.1    Guengerich, F.P.2
  • 149
    • 0025022689 scopus 로고
    • The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes
    • Yamano, S., Tatsuno, J., and Gonzalez, F. J., The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes, Biochemistry, 29, 1322-1329, 1990.
    • (1990) Biochemistry , vol.29 , pp. 1322-1329
    • Yamano, S.1    Tatsuno, J.2    Gonzalez, F.J.3
  • 150
    • 0025841777 scopus 로고
    • Purification and characterization of human liver microsomal cytochrome P-450 2A6
    • Yun, C.-H., Shimada, T., and Guengerich, F. P., Purification and characterization of human liver microsomal cytochrome P-450 2A6, Mol. Pharmacol., 40, 679-685, 1991.
    • (1991) Mol. Pharmacol , vol.40 , pp. 679-685
    • Yun, C.-H.1    Shimada, T.2    Guengerich, F.P.3
  • 151
    • 16844371090 scopus 로고    scopus 로고
    • Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6
    • Yun, C.-H., Kim, K.-H., Calcutt, M. W., and Guengerich, F. P., Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6, J. Biol. Chem., 280, 12279-12291, 2005.
    • (2005) J. Biol. Chem , vol.280 , pp. 12279-12291
    • Yun, C.-H.1    Kim, K.-H.2    Calcutt, M.W.3    Guengerich, F.P.4
  • 152
    • 0033861614 scopus 로고    scopus 로고
    • CYP3A activity in African American and European American men: Population differences and functional effect of the CYP3A4*1B5'-promoter region polymorphism
    • Wandel, C., Witte, J. S., Hall, J. M., Stein, C. M., Wood, A. J., and Wilkinson, G. R., CYP3A activity in African American and European American men: population differences and functional effect of the CYP3A4*1B5'-promoter region polymorphism, Clin. Pharmacol. Ther., 68, 82-91, 2000.
    • (2000) Clin. Pharmacol. Ther , vol.68 , pp. 82-91
    • Wandel, C.1    Witte, J.S.2    Hall, J.M.3    Stein, C.M.4    Wood, A.J.5    Wilkinson, G.R.6
  • 153
  • 154
    • 0018958906 scopus 로고
    • A new method for measuring covalent binding of chemicals to cellular macromolecules
    • Sun, J. D. and Dent, J. G., A new method for measuring covalent binding of chemicals to cellular macromolecules, Chem. Biol. Interact., 32, 41-61, 1980.
    • (1980) Chem. Biol. Interact , vol.32 , pp. 41-61
    • Sun, J.D.1    Dent, J.G.2
  • 155
    • 0019821990 scopus 로고
    • A rapid and sensitive method for determination of covalent binding of benzo(a)pyrene to proteins
    • Wallin, H., Schelin, C., Tunek, A., and Jergil, B., A rapid and sensitive method for determination of covalent binding of benzo(a)pyrene to proteins, Chem. Biol. Interact., 38, 109-118,1981.
    • (1981) Chem. Biol. Interact , vol.38 , pp. 109-118
    • Wallin, H.1    Schelin, C.2    Tunek, A.3    Jergil, B.4
  • 157
    • 0021241496 scopus 로고
    • Glutathione-mediated binding of dibromoalkanes to DNA: Specificity of rat glu-tathione S-transferases and dibromoalkane structure
    • Inskeep, P. B. and Guengerich, F. P., Glutathione-mediated binding of dibromoalkanes to DNA: specificity of rat glu-tathione S-transferases and dibromoalkane structure, Carcinogenesis, 5, 805-808, 1984.
    • (1984) Carcinogenesis , vol.5 , pp. 805-808
    • Inskeep, P.B.1    Guengerich, F.P.2
  • 158
    • 0007343585 scopus 로고
    • Color reactions of nucleic acid components
    • Vol. 1, Chargoff, E. and Davidson, J. N. Academic Press, New York
    • Dische, Z., Color reactions of nucleic acid components, in The Nucleic Acids, Vol. 1, Chargoff, E. and Davidson, J. N. Academic Press, New York, 1955, pp. 285-305.
    • (1955) The Nucleic Acids , pp. 285-305
    • Dische, Z.1
  • 159
    • 0018568031 scopus 로고
    • Improved microfluorometric DNA determinations in biological material using 33258 Hoechst
    • Cerasone, C. F., Bolognesi, C., and Santi, L., Improved microfluorometric DNA determinations in biological material using 33258 Hoechst, Anal. Biochem., 100, 188-197, 1979.
    • (1979) Anal. Biochem , vol.100 , pp. 188-197
    • Cerasone, C.F.1    Bolognesi, C.2    Santi, L.3
  • 160
    • 0001477412 scopus 로고
    • SOS function tests for studies of chemical carcinogenesis in Salmonella typhimurium TA 1535/pSK1002, NM2009, and NM3009, in Methods in Molecular Genetics, Vol. 5
    • Adolph, K. W., Ed., Academic Press, Orlando, FL
    • Shimada, T., Oda, Y., Yamazaki, H., Mimura, M., and Guengerich, F. P., SOS function tests for studies of chemical carcinogenesis in Salmonella typhimurium TA 1535/pSK1002, NM2009, and NM3009, in Methods in Molecular Genetics, Vol. 5, Gene and Chromosome Analysis, Adolph, K. W., Ed., Academic Press, Orlando, FL, 1994, pp. 342-355.
    • (1994) Gene and Chromosome Analysis , pp. 342-355
    • Shimada, T.1    Oda, Y.2    Yamazaki, H.3    Mimura, M.4    Guengerich, F.P.5
  • 161
    • 2642703427 scopus 로고    scopus 로고
    • Metabolic activation of aromatic amine mutagens by simultaneous expression of human cytochrome P450 1A2, NADPH-cytochrome P450 reductase, and N-acetyltrans-ferase in Escherichia coli
    • Josephy, P. D., Evans, D. H., Parikh, A., and Guengerich, F. P., Metabolic activation of aromatic amine mutagens by simultaneous expression of human cytochrome P450 1A2, NADPH-cytochrome P450 reductase, and N-acetyltrans-ferase in Escherichia coli, Chem. Res. Toxicol., 11, 70-74, 1998.
    • (1998) Chem. Res. Toxicol , vol.11 , pp. 70-74
    • Josephy, P.D.1    Evans, D.H.2    Parikh, A.3    Guengerich, F.P.4
  • 164
    • 2542635063 scopus 로고    scopus 로고
    • Generation of new protein kinase inhibitors utilizing cytochrome P450 mutant enzymes for indigoid coupling
    • Guengerich, F. P., Sorrells, J. L., Schmitt, S., Krauser, J. A., Aryal, P., and Meijer, L., Generation of new protein kinase inhibitors utilizing cytochrome P450 mutant enzymes for indigoid coupling, J. Med. Chem., 43, 3236-3241, 2004.
    • (2004) J. Med. Chem , vol.43 , pp. 3236-3241
    • Guengerich, F.P.1    Sorrells, J.L.2    Schmitt, S.3    Krauser, J.A.4    Aryal, P.5    Meijer, L.6
  • 168
    • 0035998274 scopus 로고    scopus 로고
    • 1 dialdehyde adduct formed from reaction with methylamine
    • 1 dialdehyde adduct formed from reaction with methylamine, Chem. Res. Toxicol., 15, 793-798, 2002.
    • (2002) Chem. Res. Toxicol , vol.15 , pp. 793-798
    • Guengerich, F.P.1
  • 170
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R. W., Circular dichroism, Methods Enzymol., 246, 34-71, 1995.
    • (1995) Methods Enzymol , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 171
    • 0036683168 scopus 로고    scopus 로고
    • In vitro biotransformation of (R)- and (S)-thalidomide: Application of circular dichroism spectroscopy to the stere-ochemical characterization of the hydroxylated metabolites
    • Meyring, M., Muhlbacher, J., Messer, K., Kastner-Pustet, N., Bringmann, G., Mannschreck, A., and Blaschke, G., In vitro biotransformation of (R)- and (S)-thalidomide: application of circular dichroism spectroscopy to the stere-ochemical characterization of the hydroxylated metabolites, Anal. Chem., 74, 3726-3735, 2002.
    • (2002) Anal. Chem , vol.74 , pp. 3726-3735
    • Meyring, M.1    Muhlbacher, J.2    Messer, K.3    Kastner-Pustet, N.4    Bringmann, G.5    Mannschreck, A.6    Blaschke, G.7
  • 172
    • 0035298653 scopus 로고    scopus 로고
    • NMR spectroscopy: Past and present
    • Rabenstein, D. L., NMR spectroscopy: past and present, Anal. Chem., 73, 214A-223A, 2001.
    • (2001) Anal. Chem , vol.73 , pp. 214A-223A
    • Rabenstein, D.L.1
  • 173
    • 84889582115 scopus 로고    scopus 로고
    • NMR chemical shifts of common laboratory solvents as trace impurities
    • Gottlieb, H. E., Kotlyar, V., and Nudelman, A., NMR chemical shifts of common laboratory solvents as trace impurities, J. Org. Chem., 62, 7512-7515, 1997.
    • (1997) J. Org. Chem , vol.62 , pp. 7512-7515
    • Gottlieb, H.E.1    Kotlyar, V.2    Nudelman, A.3
  • 174
    • 16844383089 scopus 로고    scopus 로고
    • Biosynthesis of new indigoid inhibitors of protein kinases using recombinant cytochrome P450 2A6
    • Wu, Z., Aryal, P., Lozach, O., Meijer, L., and Guengerich, F. P., Biosynthesis of new indigoid inhibitors of protein kinases using recombinant cytochrome P450 2A6, Chem. Biodiversity, 2, 51-65, 2005.
    • (2005) Chem. Biodiversity , vol.2 , pp. 51-65
    • Wu, Z.1    Aryal, P.2    Lozach, O.3    Meijer, L.4    Guengerich, F.P.5
  • 175
    • 84990475783 scopus 로고
    • Methods in Enzymology
    • Academic Press, San Diego, CA
    • Goeddel, D. W., Ed., Methods in Enzymology, Vol. 185, Gene Expression Technology, Academic Press, San Diego, CA, 1990.
    • (1990) Gene Expression Technology , vol.185
    • Goeddel, D.W.1
  • 176
    • 85132684043 scopus 로고
    • Methods in Enzymol-ogy
    • Academic Press, San Diego, CA
    • Waterman, M. R. and Johnson, E. F., Methods in Enzymol-ogy, Vol. 206, Cytochrome P450, Academic Press, San Diego, CA, 1991.
    • (1991) Cytochrome P450 , vol.206
    • Waterman, M.R.1    Johnson, E.F.2
  • 177
    • 0029852566 scopus 로고    scopus 로고
    • New applications of bacterial systems to problems in toxicology
    • Guengerich, F. P., Gillam, E. M. J., and Shimada, T., New applications of bacterial systems to problems in toxicology, CRC Crit. Rev. Toxicol., 26, 551-583, 1996.
    • (1996) CRC Crit. Rev. Toxicol , vol.26 , pp. 551-583
    • Guengerich, F.P.1    Gillam, E.M.J.2    Shimada, T.3
  • 178
    • 0034014663 scopus 로고    scopus 로고
    • Inhibition of human cytochrome P450 enzymes by 1,2-dithiole-3-thione, olt-ipraz and its derivatives, and sulforaphane
    • Langouët, S., Furge, L. L., Kerriguy, N., Nakamura, K., Guillouzo, A., and Guengerich, F. P., Inhibition of human cytochrome P450 enzymes by 1,2-dithiole-3-thione, olt-ipraz and its derivatives, and sulforaphane, Chem. Res. Toxicol., 13, 245-252, 2000.
    • (2000) Chem. Res. Toxicol , vol.13 , pp. 245-252
    • Langouët, S.1    Furge, L.L.2    Kerriguy, N.3    Nakamura, K.4    Guillouzo, A.5    Guengerich, F.P.6
  • 179
    • 0033608962 scopus 로고    scopus 로고
    • Selection and characterization of human cytochrome P450 1A2 mutants with altered catalytic properties
    • Parikh, A., Josephy, P. D., and Guengerich, F. P., Selection and characterization of human cytochrome P450 1A2 mutants with altered catalytic properties, Biochemistry, 38, 5283-5289, 1999.
    • (1999) Biochemistry , vol.38 , pp. 5283-5289
    • Parikh, A.1    Josephy, P.D.2    Guengerich, F.P.3
  • 180
    • 0029883931 scopus 로고    scopus 로고
    • Paracetamol-induced spindle disturbances in V79 cells with and without expression of human CYP1A2
    • Jensen, K. G., Poulsen, H. E., Doehmer, J., and Loft, S., Paracetamol-induced spindle disturbances in V79 cells with and without expression of human CYP1A2, Pharmacol. Toxicol., 78, 224-228, 1996.
    • (1996) Pharmacol. Toxicol , vol.78 , pp. 224-228
    • Jensen, K.G.1    Poulsen, H.E.2    Doehmer, J.3    Loft, S.4
  • 181
    • 0034705191 scopus 로고    scopus 로고
    • Elucidation of distinct binding sites for cytochrome P450 3A4
    • Hosea, N. A., Miller, G. P., and Guengerich, F. P., Elucidation of distinct binding sites for cytochrome P450 3A4, Biochemistry, 39, 5929-5939, 2000.
    • (2000) Biochemistry , vol.39 , pp. 5929-5939
    • Hosea, N.A.1    Miller, G.P.2    Guengerich, F.P.3
  • 182
    • 85132684984 scopus 로고    scopus 로고
    • Purification of cytochrome P450: Products of bacterial recombinant expression systems
    • Phillips, I. R. and Shephard, E., Ed., Academic Press, Orlando, FL
    • Guengerich, F. P. and Martin, M. V., Purification of cytochrome P450: products of bacterial recombinant expression systems, in Methods in Molecular Genetics, Cytochrome P450 Protocols, Phillips, I. R. and Shephard, E., Ed., Academic Press, Orlando, FL, 2005.
    • (2005) Methods in Molecular Genetics, Cytochrome P450 Protocols
    • Guengerich, F.P.1    Martin, M.V.2
  • 183
    • 0034234293 scopus 로고    scopus 로고
    • Cytochrome P450 1B1 (CYP1B1) pharmaco-genetics: Association of polymorphisms with functional differences in estrogen hydroxylation activity
    • Hanna, I. H., Dawling, S., Roodi, N., Guengerich, F. P., and Parl, F., Cytochrome P450 1B1 (CYP1B1) pharmaco-genetics: association of polymorphisms with functional differences in estrogen hydroxylation activity, Cancer Res., 60, 3440-3444, 2000.
    • (2000) Cancer Res , vol.60 , pp. 3440-3444
    • Hanna, I.H.1    Dawling, S.2    Roodi, N.3    Guengerich, F.P.4    Parl, F.5
  • 184
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17a-hydroxylase in Escherichia coli
    • Barnes, H. J., Arlotto, M. P., and Waterman, M. R., Expression and enzymatic activity of recombinant cytochrome P450 17a-hydroxylase in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A., 88, 5597-5601, 1991.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 185
    • 0027321555 scopus 로고
    • Expression of mammalian glutathione S-transferase 5-5 in Salmonella typhimurium TA1535 leads to base-pair mutations upon exposure to dihalomethanes
    • Thier, R., Pemble, S. E., Taylor, J. B., Humphreys, W. G., Persmark, M., Ketterer, B., and Guengerich, F. P., Expression of mammalian glutathione S-transferase 5-5 in Salmonella typhimurium TA1535 leads to base-pair mutations upon exposure to dihalomethanes, Proc. Natl. Acad. Sci. U.S.A., 90, 8576-8580, 1993.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 8576-8580
    • Thier, R.1    Pemble, S.E.2    Taylor, J.B.3    Humphreys, W.G.4    Persmark, M.5    Ketterer, B.6    Guengerich, F.P.7
  • 186
    • 0028834113 scopus 로고
    • Bio-activation of aromatic amines by recombinant human cytochrome P450 1A2 expressed in bacteria: A substitute for mammalian tissue preparations in mutagenicity testing
    • Josephy, P. D., DeBruin, L. S., Lord, H. L., Oak, J., Evans, D. H., Guo, Z., Dong, M.-S., and Guengerich, F. P., Bio-activation of aromatic amines by recombinant human cytochrome P450 1A2 expressed in bacteria: a substitute for mammalian tissue preparations in mutagenicity testing, Cancer Res., 55, 799-802, 1995.
    • (1995) Cancer Res , vol.55 , pp. 799-802
    • Josephy, P.D.1    DeBruin, L.S.2    Lord, H.L.3    Oak, J.4    Evans, D.H.5    Guo, Z.6    Dong, M.-S.7    Guengerich, F.P.8
  • 188
    • 0029757088 scopus 로고    scopus 로고
    • Maximizing expression of eukaryotic cytochrome P450s in Escherichia coli
    • Barnes, H. J., Maximizing expression of eukaryotic cytochrome P450s in Escherichia coli, Methods Enzymol., 272, 3-14, 1996.
    • (1996) Methods Enzymol , vol.272 , pp. 3-14
    • Barnes, H.J.1
  • 190
    • 0026336750 scopus 로고
    • Expression of mammalian cytochrome P450 enzymes using yeast-based vectors
    • Guengerich, F. P., Brian, W. R., Sari, M.-A., and Ross, J. T., Expression of mammalian cytochrome P450 enzymes using yeast-based vectors, Meth. Enzymol., 206, 130-145, 1991.
    • (1991) Meth. Enzymol , vol.206 , pp. 130-145
    • Guengerich, F.P.1    Brian, W.R.2    Sari, M.-A.3    Ross, J.T.4
  • 191
    • 2642611948 scopus 로고    scopus 로고
    • Yeast expressed cytochrome P450 2D6 (CYP2D6) exposed on the external face of plasma membrane is functionally competent
    • Loeper, J., Louérat-Oriou, B., Duport, C., and Pompon, D., Yeast expressed cytochrome P450 2D6 (CYP2D6) exposed on the external face of plasma membrane is functionally competent, Mol. Pharmacol., 54, 8-13, 1998.
    • (1998) Mol. Pharmacol , vol.54 , pp. 8-13
    • Loeper, J.1    Louérat-Oriou, B.2    Duport, C.3    Pompon, D.4
  • 192
    • 0038687263 scopus 로고    scopus 로고
    • Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochrome P450 2Cs: Identification of a new high affinity substrate common to those CYP 2C enzymes
    • Marques-Soares, C., Dijols, S., Macherey, A.-C., Wester, M. R., Johnson, E. F., Dansette, P. M., and Mansuy, D., Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochrome P450 2Cs: identification of a new high affinity substrate common to those CYP 2C enzymes, Biochemistry 42, 6363-6369, 2003.
    • (2003) Biochemistry , vol.42 , pp. 6363-6369
    • Marques-Soares, C.1    Dijols, S.2    Macherey, A.-C.3    Wester, M.R.4    Johnson, E.F.5    Dansette, P.M.6    Mansuy, D.7
  • 193
    • 0033773601 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase B in Pichia pastoris
    • Newton-Vinson, P., Hubalek, F., and Edmondson, D. E., High-level expression of human liver monoamine oxidase B in Pichia pastoris, Prot. Express. Purif., 20, 334-345, 2000.
    • (2000) Prot. Express. Purif , vol.20 , pp. 334-345
    • Newton-Vinson, P.1    Hubalek, F.2    Edmondson, D.E.3
  • 194
    • 0028061322 scopus 로고
    • Expression, purification, and characterization of porcine leukocyte 12-lipoxygenase produced in the methyltrophic yeast
    • Reddy, R. G., Yoshimoto, T., Yamamoto, S., and Marnett, L. J., Expression, purification, and characterization of porcine leukocyte 12-lipoxygenase produced in the methyltrophic yeast, Pichia pastoris, Biochem. Biophys. Res. Commun., 205, 381-388, 1994.
    • (1994) Pichia pastoris, Biochem. Biophys. Res. Commun , vol.205 , pp. 381-388
    • Reddy, R.G.1    Yoshimoto, T.2    Yamamoto, S.3    Marnett, L.J.4
  • 195
    • 0024354143 scopus 로고
    • Expression of a human liver cytochrome P-450 protein with tolbutamide hydroxylase activity in Saccharomyces cerevisiae
    • Brian, W. R., Srivastava, P. K., Umbenhauer, D. R., Lloyd, R. S., and Guengerich, F. P., Expression of a human liver cytochrome P-450 protein with tolbutamide hydroxylase activity in Saccharomyces cerevisiae, Biochemistry 28, 4993-4999, 1989.
    • (1989) Biochemistry , vol.28 , pp. 4993-4999
    • Brian, W.R.1    Srivastava, P.K.2    Umbenhauer, D.R.3    Lloyd, R.S.4    Guengerich, F.P.5
  • 196
    • 0025646757 scopus 로고
    • Catalytic activities of human liver cytochrome P-450 IIIA4 expressed in Saccharomyces cerevisiae
    • Brian, W. R., Sari, M.-A., Iwasaki, M., Shimada, T., Kaminsky, L. S., and Guengerich, F. P., Catalytic activities of human liver cytochrome P-450 IIIA4 expressed in Saccharomyces cerevisiae, Biochemistry 29, 11280-11292, 1990.
    • (1990) Biochemistry , vol.29 , pp. 11280-11292
    • Brian, W.R.1    Sari, M.-A.2    Iwasaki, M.3    Shimada, T.4    Kaminsky, L.S.5    Guengerich, F.P.6
  • 197
    • 0024152865 scopus 로고
    • Baculoviruses as gene expression vectors
    • Miller, L. K., Baculoviruses as gene expression vectors, Annu. Rev. Microbiol., 42, 177-199, 1988.
    • (1988) Annu. Rev. Microbiol , vol.42 , pp. 177-199
    • Miller, L.K.1
  • 198
    • 0026574235 scopus 로고
    • Baculovirus-mediated expression and functional characterization of human NADPH-P450 oxidoreductase
    • Tamura, S., Korzekwa, K. R., Kimura, S., Gelboin, H. V., and Gonzalez, F. J., Baculovirus-mediated expression and functional characterization of human NADPH-P450 oxidoreductase, Arch. Biochem. Biophys., 293, 219-223, 1992.
    • (1992) Arch. Biochem. Biophys , vol.293 , pp. 219-223
    • Tamura, S.1    Korzekwa, K.R.2    Kimura, S.3    Gelboin, H.V.4    Gonzalez, F.J.5
  • 199
    • 0022847113 scopus 로고
    • Expression of bovine 17a-hydroxylase cytochrome P-450 cDNA in nonsteroidogenic (COS 1) cells
    • Zuber, M. X., Simpson, E. R., and Waterman, M. R., Expression of bovine 17a-hydroxylase cytochrome P-450 cDNA in nonsteroidogenic (COS 1) cells, Science, 234, 1258-1261, 1986.
    • (1986) Science , vol.234 , pp. 1258-1261
    • Zuber, M.X.1    Simpson, E.R.2    Waterman, M.R.3
  • 200
    • 0026324032 scopus 로고
    • Expression of mammalian cytochrome P450 using vaccinia virus
    • Gonzalez, F. J., Aoyama, T., and Gelboin, H. V., Expression of mammalian cytochrome P450 using vaccinia virus, Meth. Enzymol., 206, 85-92, 1991.
    • (1991) Meth. Enzymol , vol.206 , pp. 85-92
    • Gonzalez, F.J.1    Aoyama, T.2    Gelboin, H.V.3
  • 201
    • 0036082545 scopus 로고    scopus 로고
    • Functional characterization of coding polymorphisms in the human MDR1 gene using a vaccinia virus expression system
    • Kimchi-Sarfaty, C., Gribar, J. J., and Gottesman, M. M., Functional characterization of coding polymorphisms in the human MDR1 gene using a vaccinia virus expression system, Mol. Pharmacol., 62, 1-6, 2002.
    • (2002) Mol. Pharmacol , vol.62 , pp. 1-6
    • Kimchi-Sarfaty, C.1    Gribar, J.J.2    Gottesman, M.M.3
  • 202
    • 0037225752 scopus 로고    scopus 로고
    • Study of P450 function using gene knockout and transgenic mice
    • Gonzalez, F. J. and Kimura, S., Study of P450 function using gene knockout and transgenic mice, Arch. Biochem. Biophys., 409, 153-158, 2003.
    • (2003) Arch. Biochem. Biophys , vol.409 , pp. 153-158
    • Gonzalez, F.J.1    Kimura, S.2
  • 203
    • 0001786847 scopus 로고
    • Enzymology of rat liver cytochromes P-450
    • Vol. 1, Guenger-ich, F. P., Ed., CRC Press, Boca Raton, FL
    • Guengerich, F. P., Enzymology of rat liver cytochromes P-450, in Mammalian Cytochromes P-450, Vol. 1, Guenger-ich, F. P., Ed., CRC Press, Boca Raton, FL, 1987, pp. 1-54.
    • (1987) Mammalian Cytochromes P-450 , pp. 1-54
    • Guengerich, F.P.1
  • 208
    • 0022344604 scopus 로고
    • Participation of a rat liver cytochrome P-450 induced by pregnenolone 16a-carbonitrile and other compounds in the 4-hydroxylation of mephenytoin
    • Shimada, T. and Guengerich, F. P., Participation of a rat liver cytochrome P-450 induced by pregnenolone 16a-carbonitrile and other compounds in the 4-hydroxylation of mephenytoin, Mol. Pharmacol., 28, 215-219, 1985.
    • (1985) Mol. Pharmacol , vol.28 , pp. 215-219
    • Shimada, T.1    Guengerich, F.P.2
  • 209
    • 0030735150 scopus 로고    scopus 로고
    • Comparisons of catalytic selectivity of cytochrome P450 subfamily members from different species
    • Guengerich, F. P., Comparisons of catalytic selectivity of cytochrome P450 subfamily members from different species, Chem. Biol. Interact., 106, 161-182, 1997.
    • (1997) Chem. Biol. Interact , vol.106 , pp. 161-182
    • Guengerich, F.P.1
  • 210
    • 0022916021 scopus 로고
    • Comparison of monooxygenase activities and cytochrome P-450 isozyme concentrations in human liver microsomes
    • Beaune, P., Kremers, P. G., Kaminsky, L. S., de Graeve, J., and Guengerich, F. P., Comparison of monooxygenase activities and cytochrome P-450 isozyme concentrations in human liver microsomes, Drug Metab. Dispos., 14, 437-442, 1986.
    • (1986) Drug Metab. Dispos , vol.14 , pp. 437-442
    • Beaune, P.1    Kremers, P.G.2    Kaminsky, L.S.3    de Graeve, J.4    Guengerich, F.P.5
  • 211
    • 0025992864 scopus 로고
    • Oxidation of toxic and carcinogenic chemicals by human cytochrome P-450 enzymes
    • Guengerich, F. P. and Shimada, T., Oxidation of toxic and carcinogenic chemicals by human cytochrome P-450 enzymes, Chem. Res. Toxicol., 4, 391-407, 1991.
    • (1991) Chem. Res. Toxicol , vol.4 , pp. 391-407
    • Guengerich, F.P.1    Shimada, T.2
  • 212
    • 0024343858 scopus 로고
    • PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines
    • PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines, Proc. Natl. Acad. Sci. U.S.A., 86, 7696-7700, 1989.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 7696-7700
    • Butler, M.A.1    Iwasaki, M.2    Guengerich, F.P.3    Kad-lubar, F.F.4
  • 213
    • 0342672887 scopus 로고
    • Characterization of a human liver cytochrome P-450 involved in the oxidation of debrisoquine and other drugs using antibodies raised to the analogous rat enzyme
    • Distlerath, L. M. and Guengerich, F. P., Characterization of a human liver cytochrome P-450 involved in the oxidation of debrisoquine and other drugs using antibodies raised to the analogous rat enzyme, Proc. Natl. Acad. Sci. USA, 81, 7348-7352, 1984.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7348-7352
    • Distlerath, L.M.1    Guengerich, F.P.2
  • 214
    • 0017760071 scopus 로고
    • Accessibility of cytochrome P450 in microsomal membranes: Inhibition of metabolism by antibodies to cytochrome P450
    • Thomas, P. E., Lu, A. Y. H., West, S. B., Ryan, D., Miwa, G. T., and Levin, W., Accessibility of cytochrome P450 in microsomal membranes: inhibition of metabolism by antibodies to cytochrome P450, Mol. Pharmacol., 13, 819-831,1977.
    • (1977) Mol. Pharmacol , vol.13 , pp. 819-831
    • Thomas, P.E.1    Lu, A.Y.H.2    West, S.B.3    Ryan, D.4    Miwa, G.T.5    Levin, W.6
  • 215
    • 0019741894 scopus 로고
    • Production and application of antibodies to rat liver cytochrome P-450
    • Kaminsky, L. S., Fasco, M. J., and Guengerich, F. P., Production and application of antibodies to rat liver cytochrome P-450, Meth. Enzymol., 74, 262-272, 1981.
    • (1981) Meth. Enzymol , vol.74 , pp. 262-272
    • Kaminsky, L.S.1    Fasco, M.J.2    Guengerich, F.P.3
  • 216
    • 0028865663 scopus 로고
    • Identification of a common epitope near the conserved heme-binding region with polyclonal antibodies raised against cytochrome P450 family 2 proteins
    • Soucek, P., Martin, M. V., Ueng, Y.-F., and Guengerich, F. P., Identification of a common epitope near the conserved heme-binding region with polyclonal antibodies raised against cytochrome P450 family 2 proteins, Biochemistry, 34, 16013-16021, 1995.
    • (1995) Biochemistry , vol.34 , pp. 16013-16021
    • Soucek, P.1    Martin, M.V.2    Ueng, Y.-F.3    Guengerich, F.P.4
  • 217
    • 0020288436 scopus 로고
    • Phe-notyping of cytochromes P-450 in human tissues with monoclonal antibodies
    • Fujino, T., Park, S. S., West, D., and Gelboin, H. V., Phe-notyping of cytochromes P-450 in human tissues with monoclonal antibodies, Proc. Natl. Acad. Sci. U.S.A., 79, 3682-3686, 1982.
    • (1982) Proc. Natl. Acad. Sci. U.S.A , vol.79 , pp. 3682-3686
    • Fujino, T.1    Park, S.S.2    West, D.3    Gelboin, H.V.4
  • 218
    • 0027759647 scopus 로고
    • Cytochrome P450 and monoclonal antibodies
    • Gelboin, H. V., Cytochrome P450 and monoclonal antibodies, Pharmacol. Rev., 45, 413-453, 1993.
    • (1993) Pharmacol. Rev , vol.45 , pp. 413-453
    • Gelboin, H.V.1
  • 219
    • 0021742125 scopus 로고
    • Use of monoclonal antibody probes against rat hepatic cytochromes P-450c and P-450d to detect immunochemically related isozymes in liver microsomes from different species
    • Thomas, P. E., Reidy, J., Reik, L. M., Ryan, D. E., Koop, D. R., and Levin, W., Use of monoclonal antibody probes against rat hepatic cytochromes P-450c and P-450d to detect immunochemically related isozymes in liver microsomes from different species, Arch. Biochem. Biophys., 235, 239-253, 1984.
    • (1984) Arch. Biochem. Biophys , vol.235 , pp. 239-253
    • Thomas, P.E.1    Reidy, J.2    Reik, L.M.3    Ryan, D.E.4    Koop, D.R.5    Levin, W.6
  • 220
    • 0021363306 scopus 로고
    • Three monoclonal antibodies to rabbit microsomal cytochrome P-450 1 recognize distinct epitopes that are shared to different degrees among other electrophoretic types of cytochrome P-450
    • Reubi, I., Griffin, K. J., Raucy, J. L., and Johnson, E. F., Three monoclonal antibodies to rabbit microsomal cytochrome P-450 1 recognize distinct epitopes that are shared to different degrees among other electrophoretic types of cytochrome P-450, J. Biol. Chem., 259, 5887-5892, 1984.
    • (1984) J. Biol. Chem , vol.259 , pp. 5887-5892
    • Reubi, I.1    Griffin, K.J.2    Raucy, J.L.3    Johnson, E.F.4
  • 221
    • 0029073965 scopus 로고
    • Antipeptide antibodies against overlapping sequences differentially inhibit human CYP2D6
    • Cribb, A., Nuss, C., and Wang, R., Antipeptide antibodies against overlapping sequences differentially inhibit human CYP2D6, Drug Metab. Dispos, 23, 671-675, 1995.
    • (1995) Drug Metab. Dispos , vol.23 , pp. 671-675
    • Cribb, A.1    Nuss, C.2    Wang, R.3
  • 222
    • 0030923770 scopus 로고    scopus 로고
    • Inhibitory anti-peptide antibody against human CYP3A4
    • Wang, R. W. and Lu, A. Y. H., Inhibitory anti-peptide antibody against human CYP3A4, Drug Metab. Dispos., 25, 762-767, 1997.
    • (1997) Drug Metab. Dispos , vol.25 , pp. 762-767
    • Wang, R.W.1    Lu, A.Y.H.2
  • 223
    • 0030924508 scopus 로고    scopus 로고
    • Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
    • Baca, M., Scanlan, T. S., Stephenson, R. C., and Wells, J. A., Phage display of a catalytic antibody to optimize affinity for transition-state analog binding, Proc. Natl. Acad. Sci. USA., 94, 10063-10068, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10063-10068
    • Baca, M.1    Scanlan, T.S.2    Stephenson, R.C.3    Wells, J.A.4
  • 225
    • 0002138411 scopus 로고
    • Toxicokinetics: Pharmacokinetics in toxicology
    • 3rd ed., Hayes, A. W., Ed., Raven Press, New York
    • Renwick, A. G., Toxicokinetics: pharmacokinetics in toxicology, in Principles and Methods of Toxicology, 3rd ed., Hayes, A. W., Ed., Raven Press, New York, 1994, pp. 101-147.
    • (1994) Principles and Methods of Toxicology , pp. 101-147
    • Renwick, A.G.1
  • 226
    • 0029085760 scopus 로고
    • Applying simulation modeling to problems in toxicology and risk assessment: A short perspective
    • Andersen, M. E., Clewell, H. J., and Frederick, C. B., Applying simulation modeling to problems in toxicology and risk assessment: a short perspective, Toxicol. Appl. Pharmacol, 133, 181-187, 1995.
    • (1995) Toxicol. Appl. Pharmacol , vol.133 , pp. 181-187
    • Andersen, M.E.1    Clewell, H.J.2    Frederick, C.B.3
  • 227
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillam, E. M. J., Baba, T., Kim, B.-R., Ohmori, S., and Guengerich, F. P., Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme, Arch. Biochem. Biophys., 305, 123-131,1993.
    • (1993) Arch. Biochem. Biophys , vol.305 , pp. 123-131
    • Gillam, E.M.J.1    Baba, T.2    Kim, B.-R.3    Ohmori, S.4    Guengerich, F.P.5
  • 228
    • 0029757089 scopus 로고    scopus 로고
    • Purification of recombinant human cytochrome P450 enzymes expressed in bacteria
    • Guengerich, F. P., Martin, M. V., Guo, Z., and Chun, Y.-J., Purification of recombinant human cytochrome P450 enzymes expressed in bacteria, Meth. Enzymol., 272, 35-44, 1996.
    • (1996) Meth. Enzymol , vol.272 , pp. 35-44
    • Guengerich, F.P.1    Martin, M.V.2    Guo, Z.3    Chun, Y.-J.4
  • 229
    • 0031824305 scopus 로고    scopus 로고
    • Analysis of four residues within substrate recognition site 4 of human cytochrome P450 3A4: Role in steroid hydroxylase activity and a-naphthoflavone stimulation
    • Domanski, T. L., Liu, J., Harlow, G. R., and Halpert, J. R., Analysis of four residues within substrate recognition site 4 of human cytochrome P450 3A4: role in steroid hydroxylase activity and a-naphthoflavone stimulation, Arch. Biochem. Biophys., 350, 223-232, 1998.
    • (1998) Arch. Biochem. Biophys , vol.350 , pp. 223-232
    • Domanski, T.L.1    Liu, J.2    Harlow, G.R.3    Halpert, J.R.4
  • 230
    • 0011111919 scopus 로고    scopus 로고
    • Purification of P450s. Products of bacterial recombinant systems, in Methods in Molecular Genetics, Vol. 107
    • Phillips, I. R. and Shephard, E., Eds., Academic Press, Orlando, FL
    • Guengerich, F. P., Hosea, N. A., and Martin, M. V., Purification of P450s. Products of bacterial recombinant systems, in Methods in Molecular Genetics, Vol. 107, Cytochrome P450 Protocols, Phillips, I. R. and Shephard, E., Eds., Academic Press, Orlando, FL, 1998, pp. 77-83.
    • (1998) Cytochrome P450 Protocols , pp. 77-83
    • Guengerich, F.P.1    Hosea, N.A.2    Martin, M.V.3
  • 231
    • 0026910385 scopus 로고
    • Immobilized metal ion affinity chromatography
    • Porath, J., Immobilized metal ion affinity chromatography, Prot. Express. Purif., 3, 263-281, 1992.
    • (1992) Prot. Express. Purif , vol.3 , pp. 263-281
    • Porath, J.1
  • 232
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath, J., Carlsson, J., Olsson, I., and Belfrage, G., Metal chelate affinity chromatography, a new approach to protein fractionation, Nature, 258, 598-599, 1975.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 233
    • 0028104977 scopus 로고
    • Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities
    • Jenkins, C. M. and Waterman, M. R., Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities, J. Biol. Chem., 269, 27401-27408, 1994.
    • (1994) J. Biol. Chem , vol.269 , pp. 27401-27408
    • Jenkins, C.M.1    Waterman, M.R.2
  • 234
    • 0027198401 scopus 로고
    • Expression and purification of functional human 17alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17alpha-hydroxylase/17,20-lyase deficiency
    • Imai, T., Globerman, H., Gertner, J. M., Kagawa, N., and Waterman, M. R., Expression and purification of functional human 17alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17alpha-hydroxylase/17,20-lyase deficiency, J. Biol. Chem., 268, 19681-19689, 1993.
    • (1993) J. Biol. Chem , vol.268 , pp. 19681-19689
    • Imai, T.1    Globerman, H.2    Gertner, J.M.3    Kagawa, N.4    Waterman, M.R.5
  • 235
    • 0029128324 scopus 로고
    • Truncated human P450 2D6: Expression in Escherichia coli: Nichelate affinity purification, and characterization of solubility and aggregation
    • Kempf, A., Zanger, U. M., and Meyer, U. A., Truncated human P450 2D6: expression in Escherichia coli: Nichelate affinity purification, and characterization of solubility and aggregation, Arch. Biochem. Biophys., 321, 277-288, 1995.
    • (1995) Arch. Biochem. Biophys , vol.321 , pp. 277-288
    • Kempf, A.1    Zanger, U.M.2    Meyer, U.A.3
  • 236
    • 0027420580 scopus 로고
    • Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity
    • Sandhu, P., Baba, T., and Guengerich, F. P., Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity, Arch. Biochem. Biophys., 306, 443-450, 1993.
    • (1993) Arch. Biochem. Biophys , vol.306 , pp. 443-450
    • Sandhu, P.1    Baba, T.2    Guengerich, F.P.3
  • 237
    • 0028023169 scopus 로고
    • Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties
    • Gillam, E. M. J., Guo, Z., and Guengerich, F. P., Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties, Arch. Biochem. Biophys., 312, 59-66, 1994.
    • (1994) Arch. Biochem. Biophys , vol.312 , pp. 59-66
    • Gillam, E.M.J.1    Guo, Z.2    Guengerich, F.P.3
  • 238
    • 0028912205 scopus 로고
    • Expression of cytochrome P450 3A5 in Escherichia coli: Effects of 5' modifications, purification, spectral characterization, reconstitution conditions, and catalytic activities
    • Gillam, E. M. J., Guo, Z., Ueng, Y.-F., Yamazaki, H., Cock, I., Reilly, P. E. B., Hooper, W. D., and Guengerich, F. P., Expression of cytochrome P450 3A5 in Escherichia coli: effects of 5' modifications, purification, spectral characterization, reconstitution conditions, and catalytic activities, Arch. Biochem. Biophys., 317, 374-384, 1995.
    • (1995) Arch. Biochem. Biophys , vol.317 , pp. 374-384
    • Gillam, E.M.J.1    Guo, Z.2    Ueng, Y.-F.3    Yamazaki, H.4    Cock, I.5    Reilly, P.E.B.6    Hooper, W.D.7    Guengerich, F.P.8
  • 239
    • 0028071497 scopus 로고
    • Expression of modified human cytochrome P450 1A1 in Escherichia coli: Effects of 5' substitution, stabilization, purification, spectral characterization, and catalytic properties
    • Guo, Z., Gillam, E. M. J., Ohmori, S., Tukey, R. H., and Guengerich, F. P., Expression of modified human cytochrome P450 1A1 in Escherichia coli: effects of 5' substitution, stabilization, purification, spectral characterization, and catalytic properties, Arch. Biochem. Biophys., 312, 436-446, 1994.
    • (1994) Arch. Biochem. Biophys , vol.312 , pp. 436-446
    • Guo, Z.1    Gillam, E.M.J.2    Ohmori, S.3    Tukey, R.H.4    Guengerich, F.P.5
  • 240
    • 0032524690 scopus 로고    scopus 로고
    • Oxidation of non-ionic detergents by cytochrome P450 enzymes
    • Hosea, N. A. and Guengerich, F. P., Oxidation of non-ionic detergents by cytochrome P450 enzymes, Arch. Biochem. Biophys., 353, 365-373, 1998.
    • (1998) Arch. Biochem. Biophys , vol.353 , pp. 365-373
    • Hosea, N.A.1    Guengerich, F.P.2
  • 241
    • 0034687092 scopus 로고    scopus 로고
    • Ratedetermining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants
    • Yun, C.-H., Miller, G. P., and Guengerich, F. P., Ratedetermining steps in phenacetin oxidations by human cytochrome P450 1A2 and selected mutants, Biochemistry, 39, 11319-11329, 2000.
    • (2000) Biochemistry , vol.39 , pp. 11319-11329
    • Yun, C.-H.1    Miller, G.P.2    Guengerich, F.P.3
  • 242
    • 0942301388 scopus 로고    scopus 로고
    • Selection of human cytochrome P450 1A2 mutants with selectivity enhanced catalytic activity for heterocyclic amine N-hydroxylation
    • Kim, D. and Guengerich, F. P., Selection of human cytochrome P450 1A2 mutants with selectivity enhanced catalytic activity for heterocyclic amine N-hydroxylation, Biochemistry, 43, 981-988, 2004.
    • (2004) Biochemistry , vol.43 , pp. 981-988
    • Kim, D.1    Guengerich, F.P.2
  • 243
    • 0035883891 scopus 로고    scopus 로고
    • Heterologous expression of cytochrome P450 2D6 mutants, electron transfer, and catalysis of bufuralol hydroxylation: The role of aspartate 301 in structural integrity
    • Hanna, I. H., Kim, M.-S., and Guengerich, F. P., Heterologous expression of cytochrome P450 2D6 mutants, electron transfer, and catalysis of bufuralol hydroxylation: the role of aspartate 301 in structural integrity, Arch. Biochem. Biophys., 393, 255-261, 2001.
    • (2001) Arch. Biochem. Biophys , vol.393 , pp. 255-261
    • Hanna, I.H.1    Kim, M.-S.2    Guengerich, F.P.3
  • 244
    • 0035890772 scopus 로고    scopus 로고
    • A new selective and potent inhibitor of human cytochrome P450 1B1 and its application to antimutagenesis
    • Chun, Y.-J., Kim, S., Kim, D., Lee, S.-K., and Guengerich, F. P., A new selective and potent inhibitor of human cytochrome P450 1B1 and its application to antimutagenesis, Cancer Res., 61, 8164-8170, 2001.
    • (2001) Cancer Res , vol.61 , pp. 8164-8170
    • Chun, Y.-J.1    Kim, S.2    Kim, D.3    Lee, S.-K.4    Guengerich, F.P.5
  • 246
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi, Y. and Masters, B. S. S., Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography, J. Biol. Chem., 251, 5337-5344, 1976.
    • (1976) J. Biol. Chem , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.S.2
  • 247
    • 0017795019 scopus 로고
    • Purification and properties of NADPH-cytochrome P-450 reductase
    • Strobel, H. W. and Dignam, J. D., Purification and properties of NADPH-cytochrome P-450 reductase, Meth. Enzymol., 52, 89-96, 1978.
    • (1978) Meth. Enzymol , vol.52 , pp. 89-96
    • Strobel, H.W.1    Dignam, J.D.2
  • 248
    • 0017409770 scopus 로고
    • Separation and purification of multiple forms of microsomal cytochrome P-450: Activities of different forms of cytochrome P-450 towards several compounds of environmental interest
    • Guengerich, F. P., Separation and purification of multiple forms of microsomal cytochrome P-450: activities of different forms of cytochrome P-450 towards several compounds of environmental interest, J. Biol. Chem., 252, 3970-3979, 1977.
    • (1977) J. Biol. Chem , vol.252 , pp. 3970-3979
    • Guengerich, F.P.1
  • 249
    • 0017671864 scopus 로고
    • Preparation and properties of highly purified cytochrome P-450 and NADPH-cytochrome P-450 reductase from pulmonary microsomes of untreated rabbits
    • Guengerich, F. P., Preparation and properties of highly purified cytochrome P-450 and NADPH-cytochrome P-450 reductase from pulmonary microsomes of untreated rabbits, Mol. Pharmacol., 13, 911-923, 1977.
    • (1977) Mol. Pharmacol , vol.13 , pp. 911-923
    • Guengerich, F.P.1
  • 250
    • 0019249174 scopus 로고
    • Purification of cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydratase from a single preparation of rat liver microsomes
    • Guengerich, F. P. and Martin, M. V., Purification of cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydratase from a single preparation of rat liver microsomes, Arch. Biochem. Biophys., 205, 365-379, 1980.
    • (1980) Arch. Biochem. Biophys , vol.205 , pp. 365-379
    • Guengerich, F.P.1    Martin, M.V.2
  • 251
    • 0017145532 scopus 로고
    • The use of 8-aminooctyl sepharose for the separation of some components of the hepatic microsomal electron transfer system
    • Imai, Y., The use of 8-aminooctyl sepharose for the separation of some components of the hepatic microsomal electron transfer system, J. Biochem., 80, 267-276, 1976.
    • (1976) J. Biochem , vol.80 , pp. 267-276
    • Imai, Y.1
  • 252
    • 0016280416 scopus 로고
    • A gel-electrophoretically homogeneous preparation of cytochrome P-450 from liver microsomes of phenobarbital-pretreated rabbits
    • Imai, Y. and Sato, R., A gel-electrophoretically homogeneous preparation of cytochrome P-450 from liver microsomes of phenobarbital-pretreated rabbits, Biochem. Biophys. Res. Commun., 60, 8-14, 1974.
    • (1974) Biochem. Biophys. Res. Commun , vol.60 , pp. 8-14
    • Imai, Y.1    Sato, R.2
  • 253
    • 0018877218 scopus 로고
    • Purification of human liver cytochrome P-450 and comparison to the enzyme isolated from rat liver
    • Wang, P., Mason, P. S., and Guengerich, F. P., Purification of human liver cytochrome P-450 and comparison to the enzyme isolated from rat liver, Arch. Biochem. Biophys., 199, 206-219,1980.
    • (1980) Arch. Biochem. Biophys , vol.199 , pp. 206-219
    • Wang, P.1    Mason, P.S.2    Guengerich, F.P.3
  • 254
    • 0031822496 scopus 로고    scopus 로고
    • Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities
    • Hanna, I. H., Teiber, J. F., Kokones, K. L., and Hollenberg, P. F., Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities, Arch. Biochem. Biophys., 350, 324-332, 1998.
    • (1998) Arch. Biochem. Biophys , vol.350 , pp. 324-332
    • Hanna, I.H.1    Teiber, J.F.2    Kokones, K.L.3    Hollenberg, P.F.4
  • 255
    • 0018095311 scopus 로고
    • Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase
    • Guengerich, F. P., Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase, Biochemistry, 17, 3633-3639, 1978.
    • (1978) Biochemistry , vol.17 , pp. 3633-3639
    • Guengerich, F.P.1
  • 256
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem., 72, 248-254, 1976.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 257
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: Elimination of interfering substances
    • Brown, R. E., Jarvis, K. L., and Hyland, K. J., Protein measurement using bicinchoninic acid: elimination of interfering substances, Anal. Biochem., 180, 136-139, 1989.
    • (1989) Anal. Biochem , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvis, K.L.2    Hyland, K.J.3
  • 258
    • 0033551102 scopus 로고    scopus 로고
    • Explanation of pre-steady-state kinetics and decreased burst amplitude of HIV-1 reverse transcriptase at sites of modified DNA bases with an additional non-productive enzyme-DNA-nucle-otide complex
    • Furge, L. L. and Guengerich, F. P., Explanation of pre-steady-state kinetics and decreased burst amplitude of HIV-1 reverse transcriptase at sites of modified DNA bases with an additional non-productive enzyme-DNA-nucle-otide complex, Biochemistry, 38, 4818-4825, 1999.
    • (1999) Biochemistry , vol.38 , pp. 4818-4825
    • Furge, L.L.1    Guengerich, F.P.2
  • 260
    • 0034717125 scopus 로고    scopus 로고
    • Kinetic analysis of nucleotide incorporation by mammalian DNA polymerase 5
    • Einolf, H. J. and Guengerich, F. P., Kinetic analysis of nucleotide incorporation by mammalian DNA polymerase 5, J. Biol. Chem., 275, 16316-16322, 2000.
    • (2000) J. Biol. Chem , vol.275 , pp. 16316-16322
    • Einolf, H.J.1    Guengerich, F.P.2
  • 261
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G. and Dyer, W. J., A rapid method of total lipid extraction and purification, Can. J. Biochem. Physiol., 37, 911-917, 1959.
    • (1959) Can. J. Biochem. Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 262
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • Chen, Jr., P. S., Toribara, T. Y., and Warner, H., Microdetermination of phosphorus, Anal. Chem., 28, 1756-1758, 1956.
    • (1956) Anal. Chem , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 263
    • 0015810106 scopus 로고
    • A procedure for the estimation of microgram quantities of Triton X-100
    • Garewal, H. S., A procedure for the estimation of microgram quantities of Triton X-100, Anal. Biochem., 54, 319-324,1973.
    • (1973) Anal. Biochem , vol.54 , pp. 319-324
    • Garewal, H.S.1
  • 264
    • 0016654522 scopus 로고
    • The spectrophotometric assay for the polyethoxy nonionic detergents in membrane extracts: A critique
    • Goldstein, S. and Blecher, M., The spectrophotometric assay for the polyethoxy nonionic detergents in membrane extracts: a critique, Anal. Biochem., 64, 130-135, 1975.
    • (1975) Anal. Biochem , vol.64 , pp. 130-135
    • Goldstein, S.1    Blecher, M.2
  • 265
    • 0021105317 scopus 로고
    • Reversible transfer of heme between different molecular species of microsome-bound cytochrome P-450 in rat liver
    • Sadano, H. and Omura, T., Reversible transfer of heme between different molecular species of microsome-bound cytochrome P-450 in rat liver, Biochem. Biophys. Res. Commun., 116, 1013-1019, 1983.
    • (1983) Biochem. Biophys. Res. Commun , vol.116 , pp. 1013-1019
    • Sadano, H.1    Omura, T.2
  • 266
    • 0001207115 scopus 로고
    • Comparative structures of P-450 cytochromes
    • Ortiz de Mon-tellano, P. R., Ed., Plenum, New York
    • Black, S. D. and Coon, M. J., Comparative structures of P-450 cytochromes, in Cytochrome P-450, Ortiz de Mon-tellano, P. R., Ed., Plenum, New York, 1986, pp. 161-216.
    • (1986) Cytochrome P-450 , pp. 161-216
    • Black, S.D.1    Coon, M.J.2
  • 267
    • 0017348626 scopus 로고
    • NADPH-cytochrome P-450 reductase: Circular dichroism and physical studies
    • Knapp, J. A., Dignam, J. D., and Strobel, H. W., NADPH-cytochrome P-450 reductase: circular dichroism and physical studies, J. Biol. Chem., 252, 437-443, 1977.
    • (1977) J. Biol. Chem , vol.252 , pp. 437-443
    • Knapp, J.A.1    Dignam, J.D.2    Strobel, H.W.3
  • 268
    • 0020366526 scopus 로고
    • Immunochemical comparison and quantitation of microsomal flavin-containing monooxygenases in various hog, mouse, rat, rabbit, dog, and human tissues
    • Dannan, G. A. and Guengerich, F. P., Immunochemical comparison and quantitation of microsomal flavin-containing monooxygenases in various hog, mouse, rat, rabbit, dog, and human tissues, Mol. Pharmacol., 22, 787-794, 1982.
    • (1982) Mol. Pharmacol , vol.22 , pp. 787-794
    • Dannan, G.A.1    Guengerich, F.P.2
  • 269
    • 0018802432 scopus 로고
    • Artifacts in isoelectric focusing of the microsomal enzymes cytochrome P-450 and NADPH-cytochrome P-450 reductase
    • Guengerich, F. P., Artifacts in isoelectric focusing of the microsomal enzymes cytochrome P-450 and NADPH-cytochrome P-450 reductase, Biochim. Biophys. Acta, 577, 132-141, 1979.
    • (1979) Biochim. Biophys. Acta , vol.577 , pp. 132-141
    • Guengerich, F.P.1
  • 270
    • 0018750584 scopus 로고
    • Isolation and purification of cytochrome P-450, and the existence of multiple forms
    • Guengerich, F. P., Isolation and purification of cytochrome P-450, and the existence of multiple forms, Pharmacol. Ther., 6, 99-121, 1979.
    • (1979) Pharmacol. Ther , vol.6 , pp. 99-121
    • Guengerich, F.P.1
  • 271
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell, P. Z., Goodman, H. M., and O'Farrell, P. H., High resolution two-dimensional electrophoresis of basic as well as acidic proteins, Cell, 12, 1133-1142, 1977.
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 272
    • 0019031283 scopus 로고
    • Liver endoplasmic retic-ulum polypeptides resolved by two-dimensional gel elec-trophoresis
    • Vlasuk, G. P. and Walz, Jr., F. G., Liver endoplasmic retic-ulum polypeptides resolved by two-dimensional gel elec-trophoresis, Anal. Biochem., 105, 112-120, 1980.
    • (1980) Anal. Biochem , vol.105 , pp. 112-120
    • Vlasuk, G.P.1    Walz, F.G.2
  • 273
    • 0019405311 scopus 로고
    • Immuno-logical comparison of rat, rabbit, and human liver NADPH-cytochrome P-450 reductases
    • Guengerich, F. P., Wang, P., and Mason, P. S., Immuno-logical comparison of rat, rabbit, and human liver NADPH-cytochrome P-450 reductases, Biochemistry, 20, 2379-2385, 1981.
    • (1981) Biochemistry , vol.20 , pp. 2379-2385
    • Guengerich, F.P.1    Wang, P.2    Mason, P.S.3
  • 274
    • 0019434137 scopus 로고
    • Immunological comparison of rat, rabbit, and human microsomal cytochromes P-450
    • Guengerich, F. P., Wang, P., Mason, P. S., and Mitchell, M. B., Immunological comparison of rat, rabbit, and human microsomal cytochromes P-450, Biochemistry, 20, 2370-2378, 1981.
    • (1981) Biochemistry , vol.20 , pp. 2370-2378
    • Guengerich, F.P.1    Wang, P.2    Mason, P.S.3    Mitchell, M.B.4
  • 275
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas, P. E., Ryan, D., and Levin, W., An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels, Anal. Biochem., 75, 168-176, 1976.
    • (1976) Anal. Biochem , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 276
    • 0039703180 scopus 로고
    • Reverse-phase HPLC isolation and microse-quence analysis
    • Shively, J. E., Ed., Humana Press, Clifton, NJ
    • Shively, J. E., Reverse-phase HPLC isolation and microse-quence analysis, in Methods of Protein Microcharacterization, Shively, J. E., Ed., Humana Press, Clifton, NJ, 1986, pp. 41-87.
    • (1986) Methods of Protein Microcharacterization , pp. 41-87
    • Shively, J.E.1
  • 278
    • 0029763107 scopus 로고    scopus 로고
    • Identification of retained N-formylmethionine in bacterial recombinant cytochrome P450 proteins with the N-terminal sequence MALĽLAVFL...: Roles of residues 3-5 in retention and membrane topology
    • Dong, M.-S., Bell, L. C., Guo, Z., Phillips, D. R., Blair, I. A., and Guengerich, F. P., Identification of retained N-formylmethionine in bacterial recombinant cytochrome P450 proteins with the N-terminal sequence MALĽLAVFL...: roles of residues 3-5 in retention and membrane topology, Biochemistry, 35, 10031-10040, 1996.
    • (1996) Biochemistry , vol.35 , pp. 10031-10040
    • Dong, M.-S.1    Bell, L.C.2    Guo, Z.3    Phillips, D.R.4    Blair, I.A.5    Guengerich, F.P.6
  • 279
    • 0016213883 scopus 로고
    • The resolution and reconstitution of the liver microsomal hydroxylation system
    • Lu, A. Y. H. and Levin, W., The resolution and reconstitution of the liver microsomal hydroxylation system, Biochim. Biophys. Acta, 344, 205-240, 1974.
    • (1974) Biochim. Biophys. Acta , vol.344 , pp. 205-240
    • Lu, A.Y.H.1    Levin, W.2
  • 280
    • 0016275622 scopus 로고
    • Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds and endogenous substrates. VII. Stimulation of benzphetamine N-demethylation by lipid and detergent
    • Lu, A. Y. H., Levin, W., and Kuntzman, R., Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds and endogenous substrates. VII. Stimulation of benzphetamine N-demethylation by lipid and detergent, Biochem. Biophys. Res. Commun., 60, 266-272, 1974.
    • (1974) Biochem. Biophys. Res. Commun , vol.60 , pp. 266-272
    • Lu, A.Y.H.1    Levin, W.2    Kuntzman, R.3
  • 281
    • 0014678449 scopus 로고
    • Hydroxyla-tion of benzphetamine and other drugs by a solubilized form of cytochrome P-450 from liver microsomes: Lipid requirement for drug demethylation
    • Lu, A. Y. H., Strobel, H. W., and Coon, M. J., Hydroxyla-tion of benzphetamine and other drugs by a solubilized form of cytochrome P-450 from liver microsomes: lipid requirement for drug demethylation, Biochem. Biophys. Res. Commun., 36, 545-551, 1969.
    • (1969) Biochem. Biophys. Res. Commun , vol.36 , pp. 545-551
    • Lu, A.Y.H.1    Strobel, H.W.2    Coon, M.J.3
  • 282
    • 0019321102 scopus 로고
    • Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system
    • French, J. S., Guengerich, F. P., and Coon, M. J., Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system, J. Biol. Chem., 255, 4112-4119, 1980.
    • (1980) J. Biol. Chem , vol.255 , pp. 4112-4119
    • French, J.S.1    Guengerich, F.P.2    Coon, M.J.3
  • 283
    • 0031940804 scopus 로고    scopus 로고
    • Effect of common organic solvents on in vitro cytochrome P450-mediated metabolic activities in human liver microsomes
    • Chauret, N., Gauthier, A., and Nicoll-Griffith, D. A., Effect of common organic solvents on in vitro cytochrome P450-mediated metabolic activities in human liver microsomes, Drug Metab. Dispos., 26, 1-4, 1998.
    • (1998) Drug Metab. Dispos , vol.26 , pp. 1-4
    • Chauret, N.1    Gauthier, A.2    Nicoll-Griffith, D.A.3
  • 284
    • 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., 19, 1-32, 1988.
    • (1988) Drug Metab. Rev , vol.19 , pp. 1-32
    • Ziegler, D.M.1
  • 285
    • 0027462628 scopus 로고
    • Recent studies on the structure and function of multisubstrate flavin-containing monooxy-genases
    • Ziegler, D. M., Recent studies on the structure and function of multisubstrate flavin-containing monooxy-genases, Annu. Rev. Pharmacol. Toxicol., 33, 179-199, 1993.
    • (1993) Annu. Rev. Pharmacol. Toxicol , vol.33 , pp. 179-199
    • Ziegler, D.M.1
  • 286
    • 0001440167 scopus 로고
    • Microsomal flavin-containing monooxy-genase: Oxygenation of nucleophilic nitrogen and sulfur compounds
    • Vol. 1, Jakoby, W. B., Ed., Academic Press, New York
    • Ziegler, D. M., Microsomal flavin-containing monooxy-genase: oxygenation of nucleophilic nitrogen and sulfur compounds, in Enzymatic Basis of Detoxication, Vol. 1, Jakoby, W. B., Ed., Academic Press, New York, 1980, pp. 201-227.
    • (1980) Enzymatic Basis of Detoxication , pp. 201-227
    • Ziegler, D.M.1
  • 287
  • 289
    • 0017401995 scopus 로고
    • Multiple forms of cytochrome P-450: Resolution and purification of rabbit liver aryl hydrocarbon hydroxylase
    • Johnson, E. F. and Muller-Eberhard, U., Multiple forms of cytochrome P-450: resolution and purification of rabbit liver aryl hydrocarbon hydroxylase, Biochem. Biophys. Res. Commun., 76, 644-651, 1977.
    • (1977) Biochem. Biophys. Res. Commun , vol.76 , pp. 644-651
    • Johnson, E.F.1    Muller-Eberhard, U.2
  • 290
    • 0017183355 scopus 로고
    • Studies of the metabolism of diethyl p-nitrophenyl phosphorothionate (parathion) and benzphetamine using an apparently homogeneous preparation of rat liver cytochrome P-450: Effect of a cytochrome P-450 antibody preparation
    • Kamataki, T., Belcher, D. H., and Neal, R. A., Studies of the metabolism of diethyl p-nitrophenyl phosphorothionate (parathion) and benzphetamine using an apparently homogeneous preparation of rat liver cytochrome P-450: effect of a cytochrome P-450 antibody preparation, Mol. Pharmacol., 12, 921-932, 1976.
    • (1976) Mol. Pharmacol , vol.12 , pp. 921-932
    • Kamataki, T.1    Belcher, D.H.2    Neal, R.A.3
  • 291
    • 0018668106 scopus 로고
    • Comparison of different forms of liver, kidney, and lung microsomal cytochrome P-450 by immunological inhibition of regio- and stereoselective metabolism of warfarin
    • Kaminsky, L. S., Fasco, M. J., and Guengerich, F. P., Comparison of different forms of liver, kidney, and lung microsomal cytochrome P-450 by immunological inhibition of regio- and stereoselective metabolism of warfarin, J. Biol. Chem., 254, 9657-9662, 1979.
    • (1979) J. Biol. Chem , vol.254 , pp. 9657-9662
    • Kaminsky, L.S.1    Fasco, M.J.2    Guengerich, F.P.3
  • 292
    • 0018905637 scopus 로고
    • Comparison of different forms of purified cytochrome P-450 from rat liver by immunological inhibition of regio- and stereoselective metabolism of warfarin
    • Kaminsky, L. S., Fasco, M. J., and Guengerich, F. P., Comparison of different forms of purified cytochrome P-450 from rat liver by immunological inhibition of regio- and stereoselective metabolism of warfarin, J. Biol. Chem., 255, 85-91, 1980.
    • (1980) J. Biol. Chem , vol.255 , pp. 85-91
    • Kaminsky, L.S.1    Fasco, M.J.2    Guengerich, F.P.3
  • 293
    • 0018436383 scopus 로고
    • Preparation of monospecific antibodies against two forms of rat liver cytochrome P-450 and quantitation of these antigens in microsomes
    • Thomas, P. E., Koreniowski, D., Ryan, D., and Levin, W., Preparation of monospecific antibodies against two forms of rat liver cytochrome P-450 and quantitation of these antigens in microsomes, Arch. Biochem. Biophys., 192, 524-532, 1979.
    • (1979) Arch. Biochem. Biophys , vol.192 , pp. 524-532
    • Thomas, P.E.1    Koreniowski, D.2    Ryan, D.3    Levin, W.4
  • 294
    • 0015218137 scopus 로고
    • Immunochemical studies on electron transport chains involving cytochrome P-450. I. Effects of antibodies to pig liver microsomal reduced triphosphopy-ridine nucleotide-cytochrome c reductase and the non-heme iron protein from bovine adrenocortical mitochondria
    • Masters, B. S. S., Baron, J., Taylor, W. E., Isaacson, E. L., and LoSpalluto, J., Immunochemical studies on electron transport chains involving cytochrome P-450. I. Effects of antibodies to pig liver microsomal reduced triphosphopy-ridine nucleotide-cytochrome c reductase and the non-heme iron protein from bovine adrenocortical mitochondria, J. Biol. Chem, 246, 4143-4150, 1971.
    • (1971) J. Biol. Chem , vol.246 , pp. 4143-4150
    • Masters, B.S.S.1    Baron, J.2    Taylor, W.E.3    Isaacson, E.L.4    LoSpalluto, J.5
  • 295
    • 0016696937 scopus 로고
    • Purification of rat liver epoxide hydratase to apparent homogeneity
    • Bentley, P. and Oesch, F., Purification of rat liver epoxide hydratase to apparent homogeneity, FEBS Lett., 59, 291-295, 1975.
    • (1975) FEBS Lett , vol.59 , pp. 291-295
    • Bentley, P.1    Oesch, F.2
  • 296
    • 0017380815 scopus 로고
    • Resolution of two forms of cytochrome P-450 from liver microsomes of rabbits treated with 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Johnson, E. F. and Muller-Eberhard, U., Resolution of two forms of cytochrome P-450 from liver microsomes of rabbits treated with 2,3,7,8-tetrachlorodibenzo-p-dioxin, J. Biol. Chem., 252, 2839-2845, 1977.
    • (1977) J. Biol. Chem , vol.252 , pp. 2839-2845
    • Johnson, E.F.1    Muller-Eberhard, U.2
  • 297
    • 0017649345 scopus 로고
    • Purification of the major cytochrome P-450 of liver microsomes from rabbits treated with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)
    • Johnson, E. F. and Muller-Eberhard, U., Purification of the major cytochrome P-450 of liver microsomes from rabbits treated with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), Biochem. Biophys. Res. Commun., 76, 652-659, 1977.
    • (1977) Biochem. Biophys. Res. Commun , vol.76 , pp. 652-659
    • Johnson, E.F.1    Muller-Eberhard, U.2
  • 298
    • 0017396890 scopus 로고
    • A simple method for purification of epoxide hydratase from rat liver
    • Knowles, R. G. and Burchell, B., A simple method for purification of epoxide hydratase from rat liver, Biochem. J., 163, 381-383, 1977.
    • (1977) Biochem. J , vol.163 , pp. 381-383
    • Knowles, R.G.1    Burchell, B.2
  • 299
    • 0018405140 scopus 로고
    • Separation and characterization of highly purified forms of liver microsomal cytochrome P-450 from rats treated with polychlorinated biphenyls, phenobarbital, and 3-methylcholanthrene
    • Ryan, D. E., Thomas, P. E., Korzeniowski, D., and Levin, W., Separation and characterization of highly purified forms of liver microsomal cytochrome P-450 from rats treated with polychlorinated biphenyls, phenobarbital, and 3-methylcholanthrene, J. Biol. Chem., 254, 1365-1374, 1979.
    • (1979) J. Biol. Chem , vol.254 , pp. 1365-1374
    • Ryan, D.E.1    Thomas, P.E.2    Korzeniowski, D.3    Levin, W.4
  • 300
    • 0023294510 scopus 로고
    • Determination of the membrane topology of the phenobarbital-inducible rat liver cytochrome P-450 isoenzyme PB-4 using site-specific antibodies
    • De Lemos-Chiarandini, C., Frey, A. B., Sabatini, D. D., and Kreibich, G., Determination of the membrane topology of the phenobarbital-inducible rat liver cytochrome P-450 isoenzyme PB-4 using site-specific antibodies, J. Cell Biol., 104, 209-219, 1987.
    • (1987) J. Cell Biol , vol.104 , pp. 209-219
    • de Lemos-Chiarandini, C.1    Frey, A.B.2    Sabatini, D.D.3    Kreibich, G.4
  • 301
    • 0019823042 scopus 로고
    • An immu-nohistochemical study on the localization and distribution of epoxide hydrolase within livers of untreated rats
    • Kawabata, T. T., Guengerich, F. P., and Baron, J., An immu-nohistochemical study on the localization and distribution of epoxide hydrolase within livers of untreated rats, Mol. Pharmacol., 20, 709-714, 1981.
    • (1981) Mol. Pharmacol , vol.20 , pp. 709-714
    • Kawabata, T.T.1    Guengerich, F.P.2    Baron, J.3
  • 302
    • 0031801294 scopus 로고    scopus 로고
    • Immunohistochemical demonstration of β-naph-thoflavone-inducible cytochrome P450 1A1/1A2 in rat intrahepatic biliary epithelial cells
    • Shen, J., Moy, J. A., Green, M. D., Guengerich, F. P., and Baron, J., Immunohistochemical demonstration of β-naph-thoflavone-inducible cytochrome P450 1A1/1A2 in rat intrahepatic biliary epithelial cells, Hepatology, 27, 1483-1491, 1998.
    • (1998) Hepatology , vol.27 , pp. 1483-1491
    • Shen, J.1    Moy, J.A.2    Green, M.D.3    Guengerich, F.P.4    Baron, J.5
  • 303
    • 0019479074 scopus 로고
    • From antibody diversity to monoclonal antibodies
    • Milstein, C., From antibody diversity to monoclonal antibodies, Eur. J. Biochem., 118, 429-436, 1981.
    • (1981) Eur. J. Biochem , vol.118 , pp. 429-436
    • Milstein, C.1
  • 304
    • 0342936291 scopus 로고
    • The chemistry of antigens and its influence on immunogenicity
    • Borek, F., Ed., Elsevier, New York
    • Gill III, T. J., The chemistry of antigens and its influence on immunogenicity, in Imunogenicity, Borek, F., Ed., Elsevier, New York, 1972, pp. 5-44.
    • (1972) Imunogenicity , pp. 5-44
    • Gill, T.J.1
  • 305
    • 0022263133 scopus 로고
    • Purification and characterization of the human liver cytochromes P-450 involved in debrisoquine 4-hydroxylation and phenacetin O-deethylation, two prototypes for genetic polymorphism in oxidative drug metabolism
    • Distlerath, L. M., Reilly, P. E. B., Martin, M. V., Davis, G. G., Wilkinson, G. R., and Guengerich, F. P., Purification and characterization of the human liver cytochromes P-450 involved in debrisoquine 4-hydroxylation and phenacetin O-deethylation, two prototypes for genetic polymorphism in oxidative drug metabolism, J. Biol. Chem., 260, 9057-9067, 1985.
    • (1985) J. Biol. Chem , vol.260 , pp. 9057-9067
    • Distlerath, L.M.1    Reilly, P.E.B.2    Martin, M.V.3    Davis, G.G.4    Wilkinson, G.R.5    Guengerich, F.P.6
  • 306
    • 0022574425 scopus 로고
    • Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxi-dative drug metabolism: Purification and characterization of two similar forms involved in the reaction
    • Shimada, T., Misono, K. S., and Guengerich, F. P., Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxi-dative drug metabolism: purification and characterization of two similar forms involved in the reaction, J. Biol. Chem., 261, 909-921, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 909-921
    • Shimada, T.1    Misono, K.S.2    Guengerich, F.P.3
  • 307
    • 0016896069 scopus 로고
    • Antibodies against homogeneous epoxide hydratase provide evidence for a single enzyme hydrating styrene oxide and benzo(a)pyrene 4,5-oxide
    • Oesch, F. and Bentley, P., Antibodies against homogeneous epoxide hydratase provide evidence for a single enzyme hydrating styrene oxide and benzo(a)pyrene 4,5-oxide, Nature, 259, 53-55, 1976.
    • (1976) Nature , vol.259 , pp. 53-55
    • Oesch, F.1    Bentley, P.2
  • 308
    • 0021282110 scopus 로고
    • Monoclonal antibodies to phenobarbital-induced rat liver cytochrome P-450
    • Park, S. S., Fujino, T., Miller, H., Guengerich, F. P., and Gelboin, H. V., Monoclonal antibodies to phenobarbital-induced rat liver cytochrome P-450, Biochem. Pharmacol., 33, 2071-2081, 1984.
    • (1984) Biochem. Pharmacol , vol.33 , pp. 2071-2081
    • Park, S.S.1    Fujino, T.2    Miller, H.3    Guengerich, F.P.4    Gelboin, H.V.5
  • 309
    • 0020071879 scopus 로고
    • Monoclonal antibodies that inhibit enzyme activity of 3-methylcholanthrene-induced cytochrome P-450
    • Park, S. S., Fujino, T., West, D., Guengerich, F. P., and Gelboin, H. V., Monoclonal antibodies that inhibit enzyme activity of 3-methylcholanthrene-induced cytochrome P-450, Cancer Res., 42, 1798-1808, 1982.
    • (1982) Cancer Res , vol.42 , pp. 1798-1808
    • Park, S.S.1    Fujino, T.2    West, D.3    Guengerich, F.P.4    Gelboin, H.V.5
  • 311
    • 0020028678 scopus 로고
    • Estimation of isozymes of microsomal cytochrome P-450 in rats, rabbits, and humans using immunochemical staining coupled with sodium dodecyl sulfate-polyacrylamide gel elec-trophoresis
    • Guengerich, F. P., Wang, P., and Davidson, N. K., Estimation of isozymes of microsomal cytochrome P-450 in rats, rabbits, and humans using immunochemical staining coupled with sodium dodecyl sulfate-polyacrylamide gel elec-trophoresis, Biochemistry, 21, 1698-1706, 1982.
    • (1982) Biochemistry , vol.21 , pp. 1698-1706
    • Guengerich, F.P.1    Wang, P.2    Davidson, N.K.3
  • 312
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications, Proc. Natl. Acad. Sci. U.S.A., 76, 4350-4354, 1979.
    • (1979) Proc. Natl. Acad. Sci. U.S.A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 313
    • 0026008005 scopus 로고
    • The human dioxin-inducible NAD(P)H: Quinone oxidoreductase cDNA-encoded protein expressed in COS-1 cells is identical to diaphorase 4
    • Shaw, P. M., Reiss, A., Adesnik, M., Nebert, D. W., Schem-bri, J., and Jaiswal, A. K., The human dioxin-inducible NAD(P)H:quinone oxidoreductase cDNA-encoded protein expressed in COS-1 cells is identical to diaphorase 4, Eur. J. Biochem., 195, 171-176, 1991.
    • (1991) Eur. J. Biochem , vol.195 , pp. 171-176
    • Shaw, P.M.1    Reiss, A.2    Adesnik, M.3    Nebert, D.W.4    Schem-bri, J.5    Jaiswal, A.K.6
  • 314
    • 0020579390 scopus 로고
    • Protein blotting: Principles and applications
    • Gershoni, J. M. and Palade, G. E., Protein blotting: principles and applications, Anal. Biochem., 131, 1-15, 1983.
    • (1983) Anal. Biochem , vol.131 , pp. 1-15
    • Gershoni, J.M.1    Palade, G.E.2
  • 315
    • 0021154990 scopus 로고
    • Immunoblotting and dot immu-nobinding-current status and outlook
    • Towbin, H. and Gordon, J., Immunoblotting and dot immu-nobinding-current status and outlook, J. Immunol. Meth., 72, 313-340, 1984.
    • (1984) J. Immunol. Meth , vol.72 , pp. 313-340
    • Towbin, H.1    Gordon, J.2
  • 316
    • 0022000618 scopus 로고
    • Changes in the concentration of seven forms of cytochrome P-450 in primary cultures of adult rat hepatocytes
    • Steward, A. R., Dannan, G. A., Guzelian, P. S., and Guengerich, F. P., Changes in the concentration of seven forms of cytochrome P-450 in primary cultures of adult rat hepatocytes, Mol. Pharmacol., 27, 125-132, 1985.
    • (1985) Mol. Pharmacol , vol.27 , pp. 125-132
    • Steward, A.R.1    Dannan, G.A.2    Guzelian, P.S.3    Guengerich, F.P.4
  • 317
    • 0023124674 scopus 로고
    • Induction of the hepatic mixed-function oxidase system by synthetic glucocorticoids: Transcriptional and post-transcriptional regulation
    • Simmons, D. L., McQuiddy, P., and Kasper, C. B., Induction of the hepatic mixed-function oxidase system by synthetic glucocorticoids: transcriptional and post-transcriptional regulation, J. Biol. Chem., 262, 326-332, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 326-332
    • Simmons, D.L.1    McQuiddy, P.2    Kasper, C.B.3
  • 318
    • 0022869269 scopus 로고
    • Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s: Transcriptional and post-transcriptional regulation of the rat enzyme
    • Song, B. J., Gelboin, H. V., Park, S. S., Yang, C. S., and Gonzalez, F. J., Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s: transcriptional and post-transcriptional regulation of the rat enzyme, J. Biol. Chem., 261, 16689-16697, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 16689-16697
    • Song, B.J.1    Gelboin, H.V.2    Park, S.S.3    Yang, C.S.4    Gonzalez, F.J.5
  • 319
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N., Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem., 162, 156-159, 1987.
    • (1987) Anal. Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 320
    • 0028897116 scopus 로고
    • Substitution of chloroform by bromo-chloropropane in the single-step method of RNA isolation
    • Chomczynski, P. and Mackey, K., Substitution of chloroform by bromo-chloropropane in the single-step method of RNA isolation, Anal. Biochem., 225, 163-164, 1995.
    • (1995) Anal. Biochem , vol.225 , pp. 163-164
    • Chomczynski, P.1    Mackey, K.2
  • 322
    • 0023605128 scopus 로고
    • Purification and fractionation of poly(A)+ RNA
    • Jacobson, A., Purification and fractionation of poly(A)+ RNA, Meth. Enzymol., 152, -32768, 1987.
    • (1987) Meth. Enzymol , vol.152 , pp. 32768
    • Jacobson, A.1
  • 323
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M., Detection of specific sequences among DNA fragments separated by gel electrophoresis, J. Mol. Biol., 98, 503-517, 1975.
    • (1975) J. Mol. Biol , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 324
    • 0000386558 scopus 로고    scopus 로고
    • Analysis of RNA by northern and slot blot hybridization
    • Brown, T., Mackey, K., and Du, T., Analysis of RNA by northern and slot blot hybridization, Curr. Protocols Mol. Biol., 4.9.1-4.9.19, 2004.
    • (2004) Curr. Protocols Mol. Biol , pp. 491-4919
    • Brown, T.1    Mackey, K.2    Du, T.3
  • 325
    • 0023580051 scopus 로고
    • Electrophoresis in agarose and acrylamide gels
    • Ogden, R. C. and Adams, D. A., Electrophoresis in agarose and acrylamide gels, Meth. Enzymol., 152, 61-87, 1987.
    • (1987) Meth. Enzymol , vol.152 , pp. 61-87
    • Ogden, R.C.1    Adams, D.A.2
  • 327
    • 0024588897 scopus 로고
    • Characterization of mRNA species related to human liver cytochrome P-450 nifedipine oxidase and the regulation of catalytic activity
    • Bork, R. W., Muto, T., Beaune, P. H., Srivastava, P. K., Lloyd, R. S., and Guengerich, F. P., Characterization of mRNA species related to human liver cytochrome P-450 nifedipine oxidase and the regulation of catalytic activity, J. Biol. Chem., 264, 910-919, 1989.
    • (1989) J. Biol. Chem , vol.264 , pp. 910-919
    • Bork, R.W.1    Muto, T.2    Beaune, P.H.3    Srivastava, P.K.4    Lloyd, R.S.5    Guengerich, F.P.6
  • 328
    • 0000386558 scopus 로고    scopus 로고
    • Analysis of DNA sequences by blotting and hybridization
    • Brown, T., Analysis of DNA sequences by blotting and hybridization, Curr. Protocols Mol. Biol., 2.9.1-2.9.15, 1999.
    • (1999) Curr. Protocols Mol. Biol , pp. 291-2915
    • Brown, T.1
  • 329
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C. and Doly, J., A rapid alkaline extraction procedure for screening recombinant plasmid DNA, Nucl. Acids Res., 7, 1513-1523, 1979.
    • (1979) Nucl. Acids Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 330
    • 0020971311 scopus 로고
    • A rapid alkaline extraction method for the isolation of plasmid DNA
    • Birnboim, H. C., A rapid alkaline extraction method for the isolation of plasmid DNA, Meth. Enzymol., 100, 243-255, 1983.
    • (1983) Meth. Enzymol , vol.100 , pp. 243-255
    • Birnboim, H.C.1
  • 334
    • 84863754572 scopus 로고    scopus 로고
    • Enzymatic amplification of DNA by PCR: Standard procedures and optimization
    • 15.11.11-15.11.14
    • Kramer, M. and Coen, D. M., Enzymatic amplification of DNA by PCR: standard procedures and optimization, Curr. Protocols Mol. Biol., 15.11.11-15.11.14, 2001.
    • (2001) Curr. Protocols Mol. Biol
    • Kramer, M.1    Coen, D.M.2
  • 336
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Rapid and efficient site-specific mutagenesis without phenotypic selection, Proc. Natl. Acad. Sci. U.S.A., 82, 488-492, 1985.
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 337
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D., and Zakour, R. A., Rapid and efficient site-specific mutagenesis without phenotypic selection, Meth. Enzymol., 154, 367-382, 1987.
    • (1987) Meth. Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 338
    • 0017667848 scopus 로고
    • Complementary action of restriction enzymes endo R-DpnI and endo R-DpnII on bacteriophage f1 DNA
    • Vovis, G. F. and Lacks, S., Complementary action of restriction enzymes endo R-DpnI and endo R-DpnII on bacteriophage f1 DNA, J. Mol. Biol., 115, 525-538, 1977.
    • (1977) J. Mol. Biol , vol.115 , pp. 525-538
    • Vovis, G.F.1    Lacks, S.2
  • 339
    • 0021826423 scopus 로고
    • Cassette mutagenesis: An efficient method for generation of multiple mutations on defined sites
    • Wells, J. A., Vasser, M., and Powers, D. B., Cassette mutagenesis: an efficient method for generation of multiple mutations on defined sites., Gene, 34, 315-323., 1985.
    • (1985) Gene , vol.34 , pp. 315-323
    • Wells, J.A.1    Vasser, M.2    Powers, D.B.3
  • 340
    • 0023949179 scopus 로고
    • Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences
    • Reidhaar-Olson, J. R. and Sauer, R. T., Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences., Science, 241, 53-57, 1988.
    • (1988) Science , vol.241 , pp. 53-57
    • Reidhaar-Olson, J.R.1    Sauer, R.T.2
  • 342
    • 0022429804 scopus 로고
    • Base pairing involving deoxyinosine: Implications for probe design
    • Martin, F. H., Castro, M. M., Aboul-ela, F., and Tinoco, Jr., I., Base pairing involving deoxyinosine: implications for probe design, Nucl. Acids Res., 13, 8927-8938., 1985.
    • (1985) Nucl. Acids Res , vol.13 , pp. 8927-8938
    • Martin, F.H.1    Castro, M.M.2    Aboul-ela, F.3    Tinoco, I.4
  • 343
    • 0035818409 scopus 로고    scopus 로고
    • Directed evolution of single proteins, metabolic pathways, and viruses
    • Schmidt-Dannert, C., Directed evolution of single proteins, metabolic pathways, and viruses, Biochemistry, 40, 13125-13136, 2001.
    • (2001) Biochemistry , vol.40 , pp. 13125-13136
    • Schmidt-Dannert, C.1
  • 344
    • 0014107493 scopus 로고
    • An extracellular Darwinian experiment with a self-duplicating nucleic acid molecule
    • Mills, D. R., Peterson, R. L., and Spiegelman, S., An extracellular Darwinian experiment with a self-duplicating nucleic acid molecule, Proc. Natl. Acad. Sci. U.S.A., 58, 217-224, 1967.
    • (1967) Proc. Natl. Acad. Sci. U.S.A , vol.58 , pp. 217-224
    • Mills, D.R.1    Peterson, R.L.2    Spiegelman, S.3
  • 345
    • 0023513545 scopus 로고
    • New concepts for dealing with the evolution of nucleic acids
    • Eigen, M., New concepts for dealing with the evolution of nucleic acids, Cold Spring Harbor Symp. Quant. Biol., 52, 307-320, 1987.
    • (1987) Cold Spring Harbor Symp. Quant. Biol , vol.52 , pp. 307-320
    • Eigen, M.1
  • 347
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
    • Chen, K. and Arnold, F. H., Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide, Proc. Natl. Acad. Sci. U.S.A., 90, 5618-5622, 1993.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 348
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P., Rapid evolution of a protein in vitro by DNA shuffling, Nature, 370, 389-391, 1994.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 349
    • 0001270261 scopus 로고    scopus 로고
    • Design by directed evolution
    • Arnold, F. H., Design by directed evolution, Acct. Chem. Res., 31, 125-131, 1998.
    • (1998) Acct. Chem. Res , vol.31 , pp. 125-131
    • Arnold, F.H.1
  • 350
    • 3042784274 scopus 로고    scopus 로고
    • Generating mutant libraries using error-prone PCR
    • Cirino, P. C., Mayer, K. M., and Umeno, D., Generating mutant libraries using error-prone PCR, Meth. Mol. Biol., 231, 3-9, 2003.
    • (2003) Meth. Mol. Biol , vol.231 , pp. 3-9
    • Cirino, P.C.1    Mayer, K.M.2    Umeno, D.3
  • 351
    • 1842868462 scopus 로고    scopus 로고
    • Random mutagenesis by whole-plasmid PCR amplification
    • Kim, D. and Guengerich, F. P., Random mutagenesis by whole-plasmid PCR amplification, Meth. Mol. Biol., 192, 241-245, 2002.
    • (2002) Meth. Mol. Biol , vol.192 , pp. 241-245
    • Kim, D.1    Guengerich, F.P.2
  • 352
    • 0031896232 scopus 로고    scopus 로고
    • Random mutagenesis via whole plasmid PCR amplification
    • Parikh, A. and Guengerich, F. P., Random mutagenesis via whole plasmid PCR amplification, BioTechniques, 24, 428-431, 1998.
    • (1998) BioTechniques , vol.24 , pp. 428-431
    • Parikh, A.1    Guengerich, F.P.2
  • 354
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao, H., Giver, L., Shao, Z., Affholter, J. A., and Arnold, F. H., Molecular evolution by staggered extension process (StEP) in vitro recombination, Nat. Biotechnol., 16, 258-261, 1998.
    • (1998) Nat. Biotechnol , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5
  • 357
    • 3342880303 scopus 로고    scopus 로고
    • Establishment of ten strains of genetically engineered Salmonella typhimurium TA1538 each co-expressing a form of human cytochrome P450 with NADPH-cytochrome P450 reductase sensitive to various promutagens
    • Yamazaki, Y., Fujita, K.-I., Nakayama, K., Suzuki, A., Nakamura, K., Yamazaki, H., and Kamataki, T., Establishment of ten strains of genetically engineered Salmonella typhimurium TA1538 each co-expressing a form of human cytochrome P450 with NADPH-cytochrome P450 reductase sensitive to various promutagens, Mutat. Res., 562, 151-162, 2004.
    • (2004) Mutat. Res , vol.562 , pp. 151-162
    • Yamazaki, Y.1    Fujita, K.-I.2    Nakayama, K.3    Suzuki, A.4    Nakamura, K.5    Yamazaki, H.6    Kamataki, T.7
  • 358
    • 0030054504 scopus 로고    scopus 로고
    • SOS chromotest results in a broader context: Empirical relationships between genotoxic potency, mutagenic potency, and carcinogenic potency
    • White, P. A. and Rasmussen, J. B., SOS chromotest results in a broader context: empirical relationships between genotoxic potency, mutagenic potency, and carcinogenic potency, Environ. Mol. Mutagen., 27, 270-305, 1996.
    • (1996) Environ. Mol. Mutagen , vol.27 , pp. 270-305
    • White, P.A.1    Rasmussen, J.B.2
  • 359
    • 0016685233 scopus 로고
    • Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test
    • Ames, B. N., McCann, J., and Yamasaki, E., Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test, Mutat. Res., 31, 347-364, 1975.
    • (1975) Mutat. Res , vol.31 , pp. 347-364
    • Ames, B.N.1    McCann, J.2    Yamasaki, E.3
  • 360
    • 0000466382 scopus 로고
    • SOS chromotest, a direct assay of induction of an SOS function in Escherichia coli K-12 to measure genotoxicity
    • Quillardet, P., Huisman, O., D'ari, R., and Hofnung, M., SOS chromotest, a direct assay of induction of an SOS function in Escherichia coli K-12 to measure genotoxicity, Proc. Natl. Acad. Sci. USA., 79, 5971-5975, 1982.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 5971-5975
    • Quillardet, P.1    Huisman, O.2    D'ari, R.3    Hofnung, M.4
  • 361
    • 0021875107 scopus 로고
    • The SOS chromotest, a colorimetric bacterial assay for genotoxins: Procedures
    • Quillardet, P. and Hofnung, M., The SOS chromotest, a colorimetric bacterial assay for genotoxins: procedures, Mutat. Res., 147, 65-78, 1985.
    • (1985) Mutat. Res , vol.147 , pp. 65-78
    • Quillardet, P.1    Hofnung, M.2
  • 362
    • 1842691080 scopus 로고    scopus 로고
    • S-(2-chloroethyl)glutathione-generated p53 mutation spectra are influenced by differential repair rates more than sites of initial DNA damage
    • Valadez, J. G. and Guengerich, F. P., S-(2-chloroethyl)glutathione-generated p53 mutation spectra are influenced by differential repair rates more than sites of initial DNA damage, J. Biol. Chem., 279, 13435-13446, 2004.
    • (2004) J. Biol. Chem , vol.279 , pp. 13435-13446
    • Valadez, J.G.1    Guengerich, F.P.2
  • 364
    • 3042804053 scopus 로고    scopus 로고
    • 6-Alkylguanine-DNA alkyltransferase has opposing effects in modulating the genotoxicity of dibromomethane and bromomethyl acetate
    • 6-Alkylguanine-DNA alkyltransferase has opposing effects in modulating the genotoxicity of dibromomethane and bromomethyl acetate, Chem. Res. Toxicol., 17, 742-752, 2004.
    • (2004) Chem. Res. Toxicol , vol.17 , pp. 742-752
    • Liu, L.1    Williams, K.M.2    Guengerich, F.P.3    Pegg, A.E.4


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