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Volumn 21, Issue 13, 2007, Pages 3584-3591

Do mosquitoes acquire organophosphate resistance by functional changes in carboxylesterases?

Author keywords

Hydrolase; Organophosphorus; Site directed mutagenesis

Indexed keywords

CARBOXYLESTERASE; CLOFENVINFOS; ESTERASE B1; HYDROLASE; INSECTICIDE; MALATHION; MONOCROTOPHOS; ORGANOPHOSPHATE; PARATHION METHYL; UNCLASSIFIED DRUG;

EID: 35949000478     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-8237com     Document Type: Article
Times cited : (28)

References (24)
  • 1
    • 0025826133 scopus 로고
    • Role of esterases in resistance of insects to insecticides
    • Devonshire, A. L. (1991) Role of esterases in resistance of insects to insecticides. Biochem. Soc. Trans. 19, 755-759
    • (1991) Biochem. Soc. Trans , vol.19 , pp. 755-759
    • Devonshire, A.L.1
  • 2
    • 0028272286 scopus 로고
    • Modification of acetylcholinesterase as a mechanism of resistance to insecticides
    • Fournier, D., and Mutéro, A. (1994) Modification of acetylcholinesterase as a mechanism of resistance to insecticides. Comp. Biochem. Physiol. 108C, 19-31
    • (1994) Comp. Biochem. Physiol , vol.108 C , pp. 19-31
    • Fournier, D.1    Mutéro, A.2
  • 3
    • 0033486287 scopus 로고    scopus 로고
    • Carboxyl/cholinesterases: A case study of the evolution of a successful multigene family
    • Oakeshott, J. G., Claudianos, C., Russell, R. J., and Robin, G. C. (1999) Carboxyl/cholinesterases: a case study of the evolution of a successful multigene family. Bioessays 21, 1031-1042
    • (1999) Bioessays , vol.21 , pp. 1031-1042
    • Oakeshott, J.G.1    Claudianos, C.2    Russell, R.J.3    Robin, G.C.4
  • 4
    • 33846401539 scopus 로고    scopus 로고
    • Molecular mechanisms of metabolic resistance of synthetic and natural xenobiotics
    • Li, X., Schuler, M. A., and Berenbaum, M. R. (2007) Molecular mechanisms of metabolic resistance of synthetic and natural xenobiotics. Annu. Rev. Entomol. 52, 231-253
    • (2007) Annu. Rev. Entomol , vol.52 , pp. 231-253
    • Li, X.1    Schuler, M.A.2    Berenbaum, M.R.3
  • 5
    • 0030612598 scopus 로고    scopus 로고
    • A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly
    • Newcomb, R. D., Campbell, P. M., Ollis, D. L., Cheah, E., Russell, R. J., and Oakeshott, J. G. (1997) A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly. Proc. Natl. Acad. Sci. U. S. A. 94, 7464-7468
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 7464-7468
    • Newcomb, R.D.1    Campbell, P.M.2    Ollis, D.L.3    Cheah, E.4    Russell, R.J.5    Oakeshott, J.G.6
  • 7
    • 0033179577 scopus 로고    scopus 로고
    • The same amino acid substitution in orthologous esterases confers organophosphate resistance on the house fly and a blowfly
    • Claudianos, C., Russell, R. J., and Oakeshott, J. G. (1999) The same amino acid substitution in orthologous esterases confers organophosphate resistance on the house fly and a blowfly. Insect. Biochem. Mol. Biol. 29, 675-686
    • (1999) Insect. Biochem. Mol. Biol , vol.29 , pp. 675-686
    • Claudianos, C.1    Russell, R.J.2    Oakeshott, J.G.3
  • 10
    • 0035706526 scopus 로고    scopus 로고
    • Insecticide resistance in the mosquito Culex pipiens: What have we learned about adaptation
    • Raymond, M., Berticat, C., Weill, M., Pasteur, N., and Chevillon, C. (2001) Insecticide resistance in the mosquito Culex pipiens: what have we learned about adaptation. Genetica 112-113, 287-296
    • (2001) Genetica , vol.112-113 , pp. 287-296
    • Raymond, M.1    Berticat, C.2    Weill, M.3    Pasteur, N.4    Chevillon, C.5
  • 13
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 14
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 15
    • 15444381280 scopus 로고
    • Protein modeling by e-mail
    • Peitsch, M. C. (1995) Protein modeling by e-mail. Biotechnology 13, 658-660
    • (1995) Biotechnology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 16
    • 0035231872 scopus 로고    scopus 로고
    • Cloning and fusion expression of detoxifying gene in Escherichia coli
    • Huang, J., Qiao, Ch-L., Li, X., and Xing, J. M. (2001) Cloning and fusion expression of detoxifying gene in Escherichia coli. Acta. Genetica. Sinica. 28, 583-588
    • (2001) Acta. Genetica. Sinica , vol.28 , pp. 583-588
    • Huang, J.1    Qiao, C.-L.2    Li, X.3    Xing, J.M.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 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. (1976) 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) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0012712133 scopus 로고
    • The biodegradation of the decis, acetofenate (7504) and DDT by the perfusion isolated rat cells
    • Leng, X. F., and Qiao, C. L. (1986) The biodegradation of the decis, acetofenate (7504) and DDT by the perfusion isolated rat cells. Science Bulletin 19, 1505-1508
    • (1986) Science Bulletin , vol.19 , pp. 1505-1508
    • Leng, X.F.1    Qiao, C.L.2
  • 21
    • 0021708080 scopus 로고
    • Stereochemical aspects of cholinesterase catalysis
    • Järv, J. (1984) Stereochemical aspects of cholinesterase catalysis. Bioorg. Chem. 12, 259-278
    • (1984) Bioorg. Chem , vol.12 , pp. 259-278
    • Järv, J.1
  • 22
    • 0032029864 scopus 로고    scopus 로고
    • Two different amino acid substitutions in the ali-esterase, E3, confer alternative types of organophosphorus insecticide resistance in the sheep blowfly
    • Campbell, P. M., Newcomb, R. D., Russell, R. J., and Oakeshott, J. G. (1998) Two different amino acid substitutions in the ali-esterase, E3, confer alternative types of organophosphorus insecticide resistance in the sheep blowfly, Lucilia cuprina. Insect. Biochem. Mol. Biol. 28, 139-150
    • (1998) Lucilia cuprina. Insect. Biochem. Mol. Biol , vol.28 , pp. 139-150
    • Campbell, P.M.1    Newcomb, R.D.2    Russell, R.J.3    Oakeshott, J.G.4
  • 23
    • 0029949918 scopus 로고    scopus 로고
    • Scalloped wings is the Lucilia cuprina Notch homologue and a candidate for the Modifier of fitness and asymmetry of diazinon resistance
    • Davies, A. G., Game, A. Y., Chen, Z., Williams, T. J., Goodall, S., Yen, J. L., McKenzie, J. A., and Batterham, P. (1996) Scalloped wings is the Lucilia cuprina Notch homologue and a candidate for the Modifier of fitness and asymmetry of diazinon resistance. Genetics 143, 1321-1337
    • (1996) Genetics , vol.143 , pp. 1321-1337
    • Davies, A.G.1    Game, A.Y.2    Chen, Z.3    Williams, T.J.4    Goodall, S.5    Yen, J.L.6    McKenzie, J.A.7    Batterham, P.8
  • 24
    • 0031930105 scopus 로고    scopus 로고
    • Mosquito carboxylesterases: A review of the molecular biology and biochemistry of a major insecticide resistance mechanism
    • Hemingway, J., and Karunaratane, S. H. P. P. (1998) Mosquito carboxylesterases: a review of the molecular biology and biochemistry of a major insecticide resistance mechanism. Med. Vet. Entomol. 12, 1-12
    • (1998) Med. Vet. Entomol , vol.12 , pp. 1-12
    • Hemingway, J.1    Karunaratane, S.H.P.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.