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Volumn 43, Issue 5, 2013, Pages 455-465

Soluble and membrane-bound Drosophila melanogaster CYP6G1 expressed in Escherichia coli: Purification, activity, and binding properties toward multiple pesticides

Author keywords

CYP6G1; Cytochrome P450; Insecticide resistance; Multi pesticide resistance; Pesticide

Indexed keywords

CYP6G1 PROTEIN, DROSOPHILA; CYTOCHROME P450; DROSOPHILA PROTEIN; INSECTICIDE; RECOMBINANT PROTEIN;

EID: 84875622108     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2013.02.003     Document Type: Article
Times cited : (39)

References (79)
  • 1
    • 1942424174 scopus 로고    scopus 로고
    • Point mutations associated with insecticide resistance in the Drosophila cytochrome P450 Cyp6a2 enable DDT metabolism
    • Amichot M., Tares S., Brun-Barale A., Arthaud L., Bride J.M., Berge J.B. Point mutations associated with insecticide resistance in the Drosophila cytochrome P450 Cyp6a2 enable DDT metabolism. Eur. J. Biochem. 2004, 271:1250-1257.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1250-1257
    • Amichot, M.1    Tares, S.2    Brun-Barale, A.3    Arthaud, L.4    Bride, J.M.5    Berge, J.B.6
  • 2
    • 0028287065 scopus 로고
    • Expression of house fly CYP6A1 and NADPH-cytochrome P450 reductase in Escherichia coli and reconstitution of an insecticide-metabolizing P450 system
    • Andersen J.F., Utermohlen J.G., Feyereisen R. Expression of house fly CYP6A1 and NADPH-cytochrome P450 reductase in Escherichia coli and reconstitution of an insecticide-metabolizing P450 system. Biochemistry 1994, 33:2171-2177.
    • (1994) Biochemistry , vol.33 , pp. 2171-2177
    • Andersen, J.F.1    Utermohlen, J.G.2    Feyereisen, R.3
  • 3
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli
    • Barnes H.J., Arlotto M.P., Waterman M.R. Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli. Proc. Natl. Acad. Sci. USA 1991, 88:5597-5601.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 4
    • 0016170054 scopus 로고
    • Maximal exponential growth rate and yield of E. coli obtainable in a bench-scale fermentor
    • Bauer S., Shiloach J. Maximal exponential growth rate and yield of E. coli obtainable in a bench-scale fermentor. Biotechnol. Bioeng. 1974, 16:933-941.
    • (1974) Biotechnol. Bioeng. , vol.16 , pp. 933-941
    • Bauer, S.1    Shiloach, J.2
  • 5
    • 33846459990 scopus 로고    scopus 로고
    • Synergism studies with binary mixtures of pyrethroid, carbamate and organophosphate insecticides on Frankliniella occidentalis (Pergande)
    • Bielza P., Espinosa P.J., Quinto V., Abellan J., Contreras J. Synergism studies with binary mixtures of pyrethroid, carbamate and organophosphate insecticides on Frankliniella occidentalis (Pergande). Pest Manag. Sci. 2007, 63:84-89.
    • (2007) Pest Manag. Sci. , vol.63 , pp. 84-89
    • Bielza, P.1    Espinosa, P.J.2    Quinto, V.3    Abellan, J.4    Contreras, J.5
  • 10
    • 33748894308 scopus 로고    scopus 로고
    • Metabolism of endosulfan-alpha by human liver microsomes and its utility as a simultaneous in vitro probe for CYP2B6 and CYP3A4
    • Casabar R.C.T., Wallace A.D., Hodgson E., Rose R.L. Metabolism of endosulfan-alpha by human liver microsomes and its utility as a simultaneous in vitro probe for CYP2B6 and CYP3A4. Drug Metab. Dispos. 2006, 34:1779-1785.
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 1779-1785
    • Casabar, R.C.T.1    Wallace, A.D.2    Hodgson, E.3    Rose, R.L.4
  • 11
    • 3242720690 scopus 로고    scopus 로고
    • World-wide survey of an Accord insertion and its association with DDT resistance in Drosophila melanogaster
    • Catania F., Kauer M.O., Daborn P.J., Yen J.L., ffrench-Constant R.H., Schlotterer C. World-wide survey of an Accord insertion and its association with DDT resistance in Drosophila melanogaster. Mol. Ecol. 2004, 13:2491-2504.
    • (2004) Mol. Ecol. , vol.13 , pp. 2491-2504
    • Catania, F.1    Kauer, M.O.2    Daborn, P.J.3    Yen, J.L.4    ffrench-Constant, R.H.5    Schlotterer, C.6
  • 12
    • 33745125943 scopus 로고    scopus 로고
    • Spectrophotometric analysis of human CYP2E1-catalyzed p-nitrophenol hydroxylation
    • Humana Press, Totowa, N.J, I.R. Phillips, E.A. Shephard (Eds.)
    • Chang T.K., Crespi C.L., Waxman D.J. Spectrophotometric analysis of human CYP2E1-catalyzed p-nitrophenol hydroxylation. Cytochrome P450 Protocols 2006, 127-131. Humana Press, Totowa, N.J. I.R. Phillips, E.A. Shephard (Eds.).
    • (2006) Cytochrome P450 Protocols , pp. 127-131
    • Chang, T.K.1    Crespi, C.L.2    Waxman, D.J.3
  • 13
    • 0038691507 scopus 로고    scopus 로고
    • Rabbit CYP4B1 engineered for high-level expression in Escherichia coli: ligand stabilization and processing of the N-terminus and heme prosthetic group
    • Cheesman M.J., Baer B.R., Zheng Y.M., Gillam E.M.J., Rettie A.E. Rabbit CYP4B1 engineered for high-level expression in Escherichia coli: ligand stabilization and processing of the N-terminus and heme prosthetic group. Arch. Biochem. Biophys. 2003, 416:17-24.
    • (2003) Arch. Biochem. Biophys. , vol.416 , pp. 17-24
    • Cheesman, M.J.1    Baer, B.R.2    Zheng, Y.M.3    Gillam, E.M.J.4    Rettie, A.E.5
  • 14
    • 48249088926 scopus 로고    scopus 로고
    • Comparative molecular modeling of Anopheles gambiae CYP6Z1, a mosquito P450 capable of metabolizing DDT
    • Chiu T.L., Wen Z.M., Rupasinghe S.G., Schuler M.A. Comparative molecular modeling of Anopheles gambiae CYP6Z1, a mosquito P450 capable of metabolizing DDT. Proc. Natl. Acad. Sci. USA 2008, 105:8855-8860.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8855-8860
    • Chiu, T.L.1    Wen, Z.M.2    Rupasinghe, S.G.3    Schuler, M.A.4
  • 15
    • 34247854158 scopus 로고    scopus 로고
    • Cis-regulatory elements in the Accord retrotransposon result in tissue-specific expression of the Drosophila melanogaster insecticide resistance gene Cyp6g1
    • Chung H., Bogwitz M.R., McCart C., Andrianopoulos A., ffrench-Constant R.H., Batterham P., Daborn P.J. Cis-regulatory elements in the Accord retrotransposon result in tissue-specific expression of the Drosophila melanogaster insecticide resistance gene Cyp6g1. Genetics 2007, 175:1071-1077.
    • (2007) Genetics , vol.175 , pp. 1071-1077
    • Chung, H.1    Bogwitz, M.R.2    McCart, C.3    Andrianopoulos, A.4    ffrench-Constant, R.H.5    Batterham, P.6    Daborn, P.J.7
  • 18
    • 0035207207 scopus 로고    scopus 로고
    • DDT resistance in Drosophila correlates with Cyp6g1 over-expression and confers cross-resistance to the neonicotinoid imidacloprid
    • Daborn P., Boundy S., Yen J., Pittendrigh B., ffrench-Constant R. DDT resistance in Drosophila correlates with Cyp6g1 over-expression and confers cross-resistance to the neonicotinoid imidacloprid. Mol. Genet. Genomics 2001, 266:556-563.
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 556-563
    • Daborn, P.1    Boundy, S.2    Yen, J.3    Pittendrigh, B.4    ffrench-Constant, R.5
  • 19
    • 34247166695 scopus 로고    scopus 로고
    • Evaluating the insecticide resistance potential of eight Drosophila melanogaster cytochrome P450 genes by transgenic over-expression
    • Daborn P.J., Lumb C., Boey A., Wong W., ffrench-Constant R.H., Batterham P. Evaluating the insecticide resistance potential of eight Drosophila melanogaster cytochrome P450 genes by transgenic over-expression. Insect Biochem. Molec. Biol. 2007, 37:512-519.
    • (2007) Insect Biochem. Molec. Biol. , vol.37 , pp. 512-519
    • Daborn, P.J.1    Lumb, C.2    Boey, A.3    Wong, W.4    ffrench-Constant, R.H.5    Batterham, P.6
  • 21
    • 0037183882 scopus 로고    scopus 로고
    • Evolutionary genetics. Insecticide resistance on the move
    • Denholm I., Devine G.J., Williamson M.S. Evolutionary genetics. Insecticide resistance on the move. Science 2002, 297:2222-2223.
    • (2002) Science , vol.297 , pp. 2222-2223
    • Denholm, I.1    Devine, G.J.2    Williamson, M.S.3
  • 23
    • 0036070213 scopus 로고    scopus 로고
    • In vivo and in vitro metabolism of fipronil by larvae of the European corn borer Ostrinia nubilalis
    • Durham E.W., Siegfried B.D., Scharf M.E. In vivo and in vitro metabolism of fipronil by larvae of the European corn borer Ostrinia nubilalis. Pest Manag. Sci. 2002, 58:799-804.
    • (2002) Pest Manag. Sci. , vol.58 , pp. 799-804
    • Durham, E.W.1    Siegfried, B.D.2    Scharf, M.E.3
  • 24
    • 0024559081 scopus 로고
    • Reduction of 7-alkoxyresorufins by NADPH-cytochrome-P450 reductase and its differential-effects on their O-dealkylation by rat-liver microsomal cytochrome-P450
    • Dutton D.R., Parkinson A. Reduction of 7-alkoxyresorufins by NADPH-cytochrome-P450 reductase and its differential-effects on their O-dealkylation by rat-liver microsomal cytochrome-P450. Arch. Biochem. Biophys. 1989, 268:617-629.
    • (1989) Arch. Biochem. Biophys. , vol.268 , pp. 617-629
    • Dutton, D.R.1    Parkinson, A.2
  • 25
    • 0024532060 scopus 로고
    • Redox cycling of resorufin catalyzed by rat-liver microsomal NADPH-cytochrome-P450 reductase
    • Dutton D.R., Reed G.A., Parkinson A. Redox cycling of resorufin catalyzed by rat-liver microsomal NADPH-cytochrome-P450 reductase. Arch. Biochem. Biophys. 1989, 268:605-616.
    • (1989) Arch. Biochem. Biophys. , vol.268 , pp. 605-616
    • Dutton, D.R.1    Reed, G.A.2    Parkinson, A.3
  • 26
    • 33748802003 scopus 로고    scopus 로고
    • Structural basis for ligand promiscuity in cytochrome P450 3A4
    • Ekroos M., Sjögren T. Structural basis for ligand promiscuity in cytochrome P450 3A4. Proc. Natl. Acad. Sci. USA 2006, 103:13682-13687.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13682-13687
    • Ekroos, M.1    Sjögren, T.2
  • 27
    • 0017869007 scopus 로고
    • The measurement of difference spectra: application to the cytochromes of microsomes
    • Estabrook R.W., Werringloer J. The measurement of difference spectra: application to the cytochromes of microsomes. Methods Enzymol. 1978, 52:212-220.
    • (1978) Methods Enzymol. , vol.52 , pp. 212-220
    • Estabrook, R.W.1    Werringloer, J.2
  • 29
    • 84882470016 scopus 로고    scopus 로고
    • Insect CYP genes and P450 enzymes
    • Elsevier B.V., London, L.I. Gilbert (Ed.)
    • Feyereisen R. Insect CYP genes and P450 enzymes. Insect Molecular Biology and Biochemistry 2012, Elsevier B.V., London. L.I. Gilbert (Ed.).
    • (2012) Insect Molecular Biology and Biochemistry
    • Feyereisen, R.1
  • 32
    • 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., Guengerich F.P. Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys. 1993, 305:123-131.
    • (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
  • 34
    • 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. 2001, 14:611-650.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 36
    • 0022351118 scopus 로고
    • Genetic-regulation of the cytochrome P-450 system in Drosophila melanogaster. 2. Localization of some genes regulating cytochrome P-450 activity
    • Hallstrom I. Genetic-regulation of the cytochrome P-450 system in Drosophila melanogaster. 2. Localization of some genes regulating cytochrome P-450 activity. Chem.-Biol. Interact. 1985, 56:173-184.
    • (1985) Chem.-Biol. Interact. , vol.56 , pp. 173-184
    • Hallstrom, I.1
  • 37
    • 0022367879 scopus 로고
    • Genetic-regulation of the cytochrome-P-450 system in Drosophila melanogaster. 1. Chromosomal determination of some cytochrome-P-450-dependent reactions
    • Hallstrom I., Blanck A. Genetic-regulation of the cytochrome-P-450 system in Drosophila melanogaster. 1. Chromosomal determination of some cytochrome-P-450-dependent reactions. Chem.-Biol. Interact. 1985, 56:157-171.
    • (1985) Chem.-Biol. Interact. , vol.56 , pp. 157-171
    • Hallstrom, I.1    Blanck, A.2
  • 38
    • 79960169841 scopus 로고    scopus 로고
    • Molecular genetics of insecticide resistance in Lepidoptera
    • CRC Press, Boca Raton, M.R. Goldsmith, F. Marec (Eds.)
    • Heckel D.G. Molecular genetics of insecticide resistance in Lepidoptera. Molecular Biology and Genetics of the Lepidoptera 2010, 239-270. CRC Press, Boca Raton. M.R. Goldsmith, F. Marec (Eds.).
    • (2010) Molecular Biology and Genetics of the Lepidoptera , pp. 239-270
    • Heckel, D.G.1
  • 39
    • 0024259273 scopus 로고
    • Genes controlling malathion resistance in a laboratory-selected population of Drosophila melanogaster
    • Houpt D.R., Pursey J.C., Morton R.A. Genes controlling malathion resistance in a laboratory-selected population of Drosophila melanogaster. Genome 1988, 30:844-853.
    • (1988) Genome , vol.30 , pp. 844-853
    • Houpt, D.R.1    Pursey, J.C.2    Morton, R.A.3
  • 40
    • 0022655255 scopus 로고
    • Detoxification of the organophosphorus insecticide chlorfenvinphos by rat, rabbit and human liver enzymes
    • Hutson D.H., Logan C.J. Detoxification of the organophosphorus insecticide chlorfenvinphos by rat, rabbit and human liver enzymes. Xenobiotica 1986, 16:87-93.
    • (1986) Xenobiotica , vol.16 , pp. 87-93
    • Hutson, D.H.1    Logan, C.J.2
  • 41
    • 0017794351 scopus 로고
    • Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy
    • Jefcoate C.R. Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical-difference spectroscopy. Methods Enzymol. 1978, 52:258-279.
    • (1978) Methods Enzymol. , vol.52 , pp. 258-279
    • Jefcoate, C.R.1
  • 43
    • 38349004538 scopus 로고    scopus 로고
    • Metabolism of imidacloprid and DDT by P450 GYP6G1 expressed in cell cultures of Nicotiana tabacum suggests detoxification of these insecticides in Cyp6g1-overexpressing strains of Drosophila melanogaster, leading to resistance
    • Joußen N., Heckel D.G., Haas M., Schuphan I., Schmidt B. Metabolism of imidacloprid and DDT by P450 GYP6G1 expressed in cell cultures of Nicotiana tabacum suggests detoxification of these insecticides in Cyp6g1-overexpressing strains of Drosophila melanogaster, leading to resistance. Pest Manag. Sci. 2008, 64:65-73.
    • (2008) Pest Manag. Sci. , vol.64 , pp. 65-73
    • Joußen, N.1    Heckel, D.G.2    Haas, M.3    Schuphan, I.4    Schmidt, B.5
  • 46
    • 70349832438 scopus 로고    scopus 로고
    • Structural model and functional characterization of the Bemisia tabaci CYP6CM1vQ, a cytochrome P450 associated with high levels of imidacloprid resistance
    • Karunker I., Morou E., Nikou D., Nauen R., Sertchook R., Stevenson B.J., Paine M.J.I., Morin S., Vontas J. Structural model and functional characterization of the Bemisia tabaci CYP6CM1vQ, a cytochrome P450 associated with high levels of imidacloprid resistance. Insect Biochem. Molec. Biol. 2009, 39:697-706.
    • (2009) Insect Biochem. Molec. Biol. , vol.39 , pp. 697-706
    • Karunker, I.1    Morou, E.2    Nikou, D.3    Nauen, R.4    Sertchook, R.5    Stevenson, B.J.6    Paine, M.J.I.7    Morin, S.8    Vontas, J.9
  • 47
    • 0017813014 scopus 로고
    • Correlation of type I, type II, and reverse type I difference spectra with absolute changes in spin state of hepatic microsomal cytochrome P-450 iron from five mammalian species
    • Kumaki K., Sato M., Kon H., Nebert D.W. Correlation of type I, type II, and reverse type I difference spectra with absolute changes in spin state of hepatic microsomal cytochrome P-450 iron from five mammalian species. J. Biol. Chem. 1978, 253:1048-1058.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1048-1058
    • Kumaki, K.1    Sato, M.2    Kon, H.3    Nebert, D.W.4
  • 48
    • 33845750558 scopus 로고    scopus 로고
    • High expression of Cyp6g1, a cytochrome P450 gene, does not necessarily confer DDT resistance in Drosophila melanogaster
    • Kuruganti S., Lam V., Zhou X., Bennett G., Pittendrigh B.R., Ganguly R. High expression of Cyp6g1, a cytochrome P450 gene, does not necessarily confer DDT resistance in Drosophila melanogaster. Gene 2007, 388:43-53.
    • (2007) Gene , vol.388 , pp. 43-53
    • Kuruganti, S.1    Lam, V.2    Zhou, X.3    Bennett, G.4    Pittendrigh, B.R.5    Ganguly, R.6
  • 49
    • 0033167089 scopus 로고    scopus 로고
    • Protein synthesis inhibitors and ethanol selectively enhance heterologous expression of P450s and related proteins in Escherichia coli
    • Kusano K., Waterman M.R., Sakaguchi M., Omura T., Kagawa N. Protein synthesis inhibitors and ethanol selectively enhance heterologous expression of P450s and related proteins in Escherichia coli. Arch. Biochem. Biophys. 1999, 367:129-136.
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 129-136
    • Kusano, K.1    Waterman, M.R.2    Sakaguchi, M.3    Omura, T.4    Kagawa, N.5
  • 51
    • 6344250770 scopus 로고    scopus 로고
    • 57 varieties: the human cytochromes P450
    • Lewis D.F.V. 57 varieties: the human cytochromes P450. Pharmacogenomics 2004, 5:305-318.
    • (2004) Pharmacogenomics , vol.5 , pp. 305-318
    • Lewis, D.F.V.1
  • 52
    • 33846401539 scopus 로고    scopus 로고
    • Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics
    • Li X.C., Schuler M.A., Berenbaum M.R. Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics. Annu. Rev. Entomol. 2007, 52:231-253.
    • (2007) Annu. Rev. Entomol. , vol.52 , pp. 231-253
    • Li, X.C.1    Schuler, M.A.2    Berenbaum, M.R.3
  • 53
    • 0029585123 scopus 로고
    • Atom/fragment contribution method for estimating octanol-water partition coefficients
    • Meylan W.M., Howard P.H. Atom/fragment contribution method for estimating octanol-water partition coefficients. J. Pharm. Sci. 1995, 84:83-92.
    • (1995) J. Pharm. Sci. , vol.84 , pp. 83-92
    • Meylan, W.M.1    Howard, P.H.2
  • 54
    • 0035257283 scopus 로고    scopus 로고
    • Genetic variation and correlations among responses to five insecticides within natural populations of Drosophila melanogaster (Diptera: Drosophilidae)
    • Miyo T., Takamori H., Kono Y., Oguma Y. Genetic variation and correlations among responses to five insecticides within natural populations of Drosophila melanogaster (Diptera: Drosophilidae). J. Econ. Entomol. 2001, 94:223-232.
    • (2001) J. Econ. Entomol. , vol.94 , pp. 223-232
    • Miyo, T.1    Takamori, H.2    Kono, Y.3    Oguma, Y.4
  • 55
    • 0027163005 scopus 로고
    • Evolution of Drosophila insecticide resistance
    • Morton R.A. Evolution of Drosophila insecticide resistance. Genome 1993, 36:1-7.
    • (1993) Genome , vol.36 , pp. 1-7
    • Morton, R.A.1
  • 56
    • 55749090372 scopus 로고    scopus 로고
    • P450 reductase and cytochrome b(5) interactions with cytochrome P450: effects on house fly CYP6A1 catalysis
    • Murataliev M.B., Guzov V.M., Walker F.A., Feyereisen R. P450 reductase and cytochrome b(5) interactions with cytochrome P450: effects on house fly CYP6A1 catalysis. Insect Biochem. Molec. Biol. 2008, 38:1008-1015.
    • (2008) Insect Biochem. Molec. Biol. , vol.38 , pp. 1008-1015
    • Murataliev, M.B.1    Guzov, V.M.2    Walker, F.A.3    Feyereisen, R.4
  • 57
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese Cedar pollen, Cryj2, in Escherichia coli
    • Nishihara K., Kanemori M., Kitagawa M., Yanagi H., Yura T. Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese Cedar pollen, Cryj2, in Escherichia coli. Appl. Environ. Microbiol. 1998, 64:1694-1699.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 58
    • 0002450195 scopus 로고
    • Genetical and biochemical studies on negatively correlated cross-resistance in Drosophila melanogaster. I. An attempt to reduce and increase insecticide-resistance in D. melanogaster by selection pressure
    • Ogita Z. Genetical and biochemical studies on negatively correlated cross-resistance in Drosophila melanogaster. I. An attempt to reduce and increase insecticide-resistance in D. melanogaster by selection pressure. Botyu-kagaku (Sci. Insect Control.) 1961, 26:7-18.
    • (1961) Botyu-kagaku (Sci. Insect Control.) , vol.26 , pp. 7-18
    • Ogita, Z.1
  • 59
    • 0002450197 scopus 로고
    • Genetical and biochemical studies on negatively correlated cross-resistance in Drosophila melanogaster. III. Genetical studies on actions of mixed insecticides with negatively correlated substances
    • Ogita Z. Genetical and biochemical studies on negatively correlated cross-resistance in Drosophila melanogaster. III. Genetical studies on actions of mixed insecticides with negatively correlated substances. Botyu-kagaku (Sci. Insect Control) 1961, 26:88-93.
    • (1961) Botyu-kagaku (Sci. Insect Control) , vol.26 , pp. 88-93
    • Ogita, Z.1
  • 60
    • 78651149545 scopus 로고
    • Negatively correlated cross-resistance in Drosophila melanogaster
    • Ogita Z.I. Negatively correlated cross-resistance in Drosophila melanogaster. Jpn. J. Med. Sci. Biol. 1964, 17:54-587.
    • (1964) Jpn. J. Med. Sci. Biol. , vol.17 , pp. 54-587
    • Ogita, Z.I.1
  • 61
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 1964, 239:2370-2378.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 62
    • 0030843652 scopus 로고    scopus 로고
    • Drug metabolism by Escherichia coli expressing human cytochromes P450
    • Parikh A., Gillam E.M.J., Guengerich F.P. Drug metabolism by Escherichia coli expressing human cytochromes P450. Nat. Biotech. 1997, 15:784-788.
    • (1997) Nat. Biotech. , vol.15 , pp. 784-788
    • Parikh, A.1    Gillam, E.M.J.2    Guengerich, F.P.3
  • 63
    • 2342646702 scopus 로고    scopus 로고
    • Genome-wide transcription profile of field- and laboratory-selected dichlorodiphenyltrichloroethane (DDT)-resistant Drosophila
    • Pedra J.H., McIntyre L.M., Scharf M.E., Pittendrigh B.R. Genome-wide transcription profile of field- and laboratory-selected dichlorodiphenyltrichloroethane (DDT)-resistant Drosophila. Proc. Natl. Acad. Sci. USA 2004, 101:7034-7039.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7034-7039
    • Pedra, J.H.1    McIntyre, L.M.2    Scharf, M.E.3    Pittendrigh, B.R.4
  • 65
    • 1842430820 scopus 로고    scopus 로고
    • The genetic basis of resistance to diazinon in natural populations of Drosophila melanogaster
    • Pyke F.M., Bogwitz M.R., Perry T., Monk A., Batterham P., McKenzie J.A. The genetic basis of resistance to diazinon in natural populations of Drosophila melanogaster. Genetica 2004, 121:13-24.
    • (2004) Genetica , vol.121 , pp. 13-24
    • Pyke, F.M.1    Bogwitz, M.R.2    Perry, T.3    Monk, A.4    Batterham, P.5    McKenzie, J.A.6
  • 66
    • 77957682630 scopus 로고    scopus 로고
    • Intramolecular heme ligation of the cytochrome P450 2C9 R108H mutant demonstrates pronounced conformational flexibility of the B-C loop region: Implications for substrate binding
    • Roberts A.G., Cheesman M.J., Primak A., Bowman M.K., Atkins W.M., Rettie A.E. Intramolecular heme ligation of the cytochrome P450 2C9 R108H mutant demonstrates pronounced conformational flexibility of the B-C loop region: Implications for substrate binding. Biochemistry 2010, 49:8700-8708.
    • (2010) Biochemistry , vol.49 , pp. 8700-8708
    • Roberts, A.G.1    Cheesman, M.J.2    Primak, A.3    Bowman, M.K.4    Atkins, W.M.5    Rettie, A.E.6
  • 67
    • 0029940691 scopus 로고    scopus 로고
    • Metabolism of promutagens catalyzed by Drosophila melanogaster CYP6A2 enzyme in Saccharomyces cerevisiae
    • Saner C., Weibel B., Wurgler F.E., Sengstag C. Metabolism of promutagens catalyzed by Drosophila melanogaster CYP6A2 enzyme in Saccharomyces cerevisiae. Environ. Mol. Mutagen. 1996, 27:46-58.
    • (1996) Environ. Mol. Mutagen. , vol.27 , pp. 46-58
    • Saner, C.1    Weibel, B.2    Wurgler, F.E.3    Sengstag, C.4
  • 68
    • 0002892893 scopus 로고    scopus 로고
    • Piperonylic acid, a selective, mechanism-based inactivator of the trans-cinnamate 4-hydroxylase: a new tool to control the flux of metabolites in the phenylpropanoid pathway
    • Schalk M., Cabello-Hurtado F., Pierrel M.A., Atanossova R., Saindrenan P., Werck-Reichhart D. Piperonylic acid, a selective, mechanism-based inactivator of the trans-cinnamate 4-hydroxylase: a new tool to control the flux of metabolites in the phenylpropanoid pathway. Plant Physiol. 1998, 118:209-218.
    • (1998) Plant Physiol. , vol.118 , pp. 209-218
    • Schalk, M.1    Cabello-Hurtado, F.2    Pierrel, M.A.3    Atanossova, R.4    Saindrenan, P.5    Werck-Reichhart, D.6
  • 69
    • 0014059179 scopus 로고
    • Spectral studies of drug interaction with hepatic microsomal cytochrome
    • Schenkman J.B., Remmer H., Estabrook R.W. Spectral studies of drug interaction with hepatic microsomal cytochrome. Mol. Pharmacol. 1967, 3:113.
    • (1967) Mol. Pharmacol. , vol.3 , pp. 113
    • Schenkman, J.B.1    Remmer, H.2    Estabrook, R.W.3
  • 72
    • 0035987896 scopus 로고    scopus 로고
    • Cytochrome P450 fluorometric substrates: Identification of isoform-selective probes for rat CYP2D2 and human CYP3A4
    • Stresser D.M., Turner S.D., Blanchard A.P., Miller V.P., Crespi C.L. Cytochrome P450 fluorometric substrates: Identification of isoform-selective probes for rat CYP2D2 and human CYP3A4. Drug Metab. Dispos. 2002, 30:845-852.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 845-852
    • Stresser, D.M.1    Turner, S.D.2    Blanchard, A.P.3    Miller, V.P.4    Crespi, C.L.5
  • 73
    • 0034787025 scopus 로고    scopus 로고
    • Direct selection for paraquat resistance in Drosophila results in a different extended longevity phenotype
    • Vettraino J., Buck S., Arking R. Direct selection for paraquat resistance in Drosophila results in a different extended longevity phenotype. J. Gerontol. A Biol. Sci. Med. Sci. 2001, 56:B415-B425.
    • (2001) J. Gerontol. A Biol. Sci. Med. Sci. , vol.56
    • Vettraino, J.1    Buck, S.2    Arking, R.3
  • 74
    • 0021772510 scopus 로고
    • Natural variation in the expression of cytochrome P-450 and dimethylnitrosamine demethylase in Drosophila
    • Waters L.C., Simms S.I., Nix C.E. Natural variation in the expression of cytochrome P-450 and dimethylnitrosamine demethylase in Drosophila. Biochem. Biophys. Res. Comm. 1984, 123:907-913.
    • (1984) Biochem. Biophys. Res. Comm. , vol.123 , pp. 907-913
    • Waters, L.C.1    Simms, S.I.2    Nix, C.E.3
  • 75
    • 33745165600 scopus 로고    scopus 로고
    • Spectrofluorometric analysis of CYP2A6-catalyzed coumarin 7-hydroxylation
    • Humana Press, Totowa N.J, I.R. Phillips, E.A. Shephard (Eds.)
    • Waxman D.J., Chang T.K.H. Spectrofluorometric analysis of CYP2A6-catalyzed coumarin 7-hydroxylation. Cytochrome P450 Protocols 2006, 91-96. Humana Press, Totowa N.J. I.R. Phillips, E.A. Shephard (Eds.).
    • (2006) Cytochrome P450 Protocols , pp. 91-96
    • Waxman, D.J.1    Chang, T.K.H.2
  • 76
    • 33745147237 scopus 로고    scopus 로고
    • Use of 7-ethoxycoumarin to monitor multiple enzymes in the human CYP1, CYP2, and CYP3 families
    • Humana Press, Totowa N.J, I.R. Phillips, E.A. Shephard (Eds.)
    • Waxman D.J., Chang T.K.H. Use of 7-ethoxycoumarin to monitor multiple enzymes in the human CYP1, CYP2, and CYP3 families. Cytochrome P450 Protocols 2006, 153-156. Humana Press, Totowa N.J. I.R. Phillips, E.A. Shephard (Eds.).
    • (2006) Cytochrome P450 Protocols , pp. 153-156
    • Waxman, D.J.1    Chang, T.K.H.2
  • 77
    • 70350121593 scopus 로고    scopus 로고
    • Enhanced bacterial expression of several mammalian cytochrome P450s by codon optimization and chaperone coexpression
    • Wu Z.L., Qiao J., Zhang Z.G., Guengerich F.P., Liu Y., Pei X.Q. Enhanced bacterial expression of several mammalian cytochrome P450s by codon optimization and chaperone coexpression. Biotechnol. Lett. 2009, 31:1589-1593.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1589-1593
    • Wu, Z.L.1    Qiao, J.2    Zhang, Z.G.3    Guengerich, F.P.4    Liu, Y.5    Pei, X.Q.6
  • 79
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi Y., 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. 1976, 251:5337-5344.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.S.2


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