메뉴 건너뛰기




Volumn 20, Issue 12, 2007, Pages 1942-1946

Nitroso-imidacloprid irreversibly inhibits rabbit aldehyde oxidase

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE OXIDASE; AMINOGUANIDINE; CATALASE; CYTOCHROME P450; GLUTATHIONE; IMIDACLOPRID; N METHYLNICOTINAMIDE; NITROSOGUANIDINE; SUPEROXIDE DISMUTASE; TRITIUM;

EID: 38149011614     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx700265r     Document Type: Article
Times cited : (20)

References (23)
  • 1
    • 0031912487 scopus 로고    scopus 로고
    • Golden age of insecticide research: Past, present, or future?
    • Casida, J. E., and Quistad, G. B. (1998) Golden age of insecticide research: Past, present, or future? Annu. Rev. Entomol. 43, 1-16.
    • (1998) Annu. Rev. Entomol , vol.43 , pp. 1-16
    • Casida, J.E.1    Quistad, G.B.2
  • 3
    • 13844280231 scopus 로고    scopus 로고
    • Neonicotinoid insecticide toxicology: Mechanisms of selective action
    • Tomizawa, M., and Casida, J. E. (2005) Neonicotinoid insecticide toxicology: mechanisms of selective action. Annu. Rev. Pharmacol. Toxicol. 45, 247-268.
    • (2005) Annu. Rev. Pharmacol. Toxicol , vol.45 , pp. 247-268
    • Tomizawa, M.1    Casida, J.E.2
  • 4
    • 0036739990 scopus 로고    scopus 로고
    • Neonicotinoid insecticides: Reduction and cleavage of imidacloprid nitroimine substituent by liver microsomal and cytosolic enzymes
    • Schulz-Jander, D. A., Leimkuehler, W. M., and Casida, J. E. (2002) Neonicotinoid insecticides: Reduction and cleavage of imidacloprid nitroimine substituent by liver microsomal and cytosolic enzymes. Chem Res. Toxicol. 15, 1158-1165.
    • (2002) Chem Res. Toxicol , vol.15 , pp. 1158-1165
    • Schulz-Jander, D.A.1    Leimkuehler, W.M.2    Casida, J.E.3
  • 7
    • 0009704661 scopus 로고    scopus 로고
    • Photolysis of imidacloprid (NTN 33893) on the leaf surface of tomato plants
    • Scholz, K., and Reinhard, F. (1999) Photolysis of imidacloprid (NTN 33893) on the leaf surface of tomato plants. Pestic. Sci. 55, 633-654.
    • (1999) Pestic. Sci , vol.55 , pp. 633-654
    • Scholz, K.1    Reinhard, F.2
  • 8
    • 33746211295 scopus 로고    scopus 로고
    • Chloropyridinyl neonicotinoid insecticides: Diverse molecular substituents contribute to facile metabolism in mice
    • Ford, K. A., and Casida, J. E. (2006) Chloropyridinyl neonicotinoid insecticides: Diverse molecular substituents contribute to facile metabolism in mice. Chem. Res. Toxicol. 19, 944-951.
    • (2006) Chem. Res. Toxicol , vol.19 , pp. 944-951
    • Ford, K.A.1    Casida, J.E.2
  • 9
    • 13844294285 scopus 로고    scopus 로고
    • Identification of aldehyde oxidase as the neonicotinoid nitroreductase
    • Dick, R. A., Kanne, D. B., and Casida, J. E. (2005) Identification of aldehyde oxidase as the neonicotinoid nitroreductase. Chem. Res. Toxicol. 18, 317-323.
    • (2005) Chem. Res. Toxicol , vol.18 , pp. 317-323
    • Dick, R.A.1    Kanne, D.B.2    Casida, J.E.3
  • 10
    • 31844451913 scopus 로고    scopus 로고
    • Substrate specificity of rabbit aldehyde oxidase for nitroguanidine and nitromethylene neonicotinoid insecticides
    • Dick, R. A., Kanne, D. B., and Casida, J. E. (2006) Substrate specificity of rabbit aldehyde oxidase for nitroguanidine and nitromethylene neonicotinoid insecticides. Chem. Res. Toxicol. 19, 38-43.
    • (2006) Chem. Res. Toxicol , vol.19 , pp. 38-43
    • Dick, R.A.1    Kanne, D.B.2    Casida, J.E.3
  • 11
    • 25444471829 scopus 로고    scopus 로고
    • Neonicotinoid nitroguanidine insecticide metabolites: Synthesis and nicotinic receptor potency of guanidines, aminoguanidines, and their derivatives
    • Kanne, D. B., Dick, R. A., Tomizawa, M., and Casida, J. E. (2005) Neonicotinoid nitroguanidine insecticide metabolites: Synthesis and nicotinic receptor potency of guanidines, aminoguanidines, and their derivatives. Chem. Res. Toxicol. 18, 1479-1484.
    • (2005) Chem. Res. Toxicol , vol.18 , pp. 1479-1484
    • Kanne, D.B.1    Dick, R.A.2    Tomizawa, M.3    Casida, J.E.4
  • 14
    • 0001568992 scopus 로고
    • Xanthine oxidase and aldehyde oxidase
    • Jakoby, W. B, Ed, Academic Press, Orlando, FL
    • Rajagopalan, K. V. (1980) Xanthine oxidase and aldehyde oxidase. In Enzymatic Basis of Detoxication (Jakoby, W. B., Ed.) Vol. 1, pp 295-309, Academic Press, Orlando, FL.
    • (1980) Enzymatic Basis of Detoxication , vol.1 , pp. 295-309
    • Rajagopalan, K.V.1
  • 15
    • 0016156485 scopus 로고
    • Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase
    • Branzoli, U., and Massey, V. (1974) Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase. J. Biol. Chem. 249, 4346-4349.
    • (1974) J. Biol. Chem , vol.249 , pp. 4346-4349
    • Branzoli, U.1    Massey, V.2
  • 16
    • 0036544597 scopus 로고    scopus 로고
    • Xanthine oxidase and aldehyde oxidase: A simple procedure for the simultaneous purification from rat liver
    • Maia, L., and Mira, L. (2002) Xanthine oxidase and aldehyde oxidase: A simple procedure for the simultaneous purification from rat liver. Arch. Biochem. Biophys. 400, 48-53.
    • (2002) Arch. Biochem. Biophys , vol.400 , pp. 48-53
    • Maia, L.1    Mira, L.2
  • 17
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R., and Wilson, I. B. (1962) Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J. Biol. Chem. 237, 3245-3249.
    • (1962) J. Biol. Chem , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 18
    • 0001842796 scopus 로고
    • Mechanism-based enzyme inactivation
    • CRC Press, Inc, Boca Raton, FL
    • Silverman, R. B. (1988) Mechanism-based enzyme inactivation. Chemistry and Enzymology, p 288, CRC Press, Inc., Boca Raton, FL.
    • (1988) Chemistry and Enzymology , pp. 288
    • Silverman, R.B.1
  • 19
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: Structure, genetics, regulation, function and pathophysiology
    • Garattini, E., Mendel, R., Romão, M. J., Wright, R., and Terao, M. (2003) Mammalian molybdo-flavoenzymes, an expanding family of proteins: Structure, genetics, regulation, function and pathophysiology. Biochem. J. 372, 15-32.
    • (2003) Biochem. J , vol.372 , pp. 15-32
    • Garattini, E.1    Mendel, R.2    Romão, M.J.3    Wright, R.4    Terao, M.5
  • 20
    • 0019487878 scopus 로고
    • Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes
    • Badwey, J. A., Robinson, J. M., Karnovsky, M. J., and Karnovsky, M. L. (1981) Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes. J. Biol. Chem. 256, 3479-3486.
    • (1981) J. Biol. Chem , vol.256 , pp. 3479-3486
    • Badwey, J.A.1    Robinson, J.M.2    Karnovsky, M.J.3    Karnovsky, M.L.4
  • 21
    • 0020982223 scopus 로고
    • Oxidation of glutathione by the superoxide radical to the disulfide and the sulfonate yielding singlet oxygen
    • Wefers, H., and Seis, H. (1983) Oxidation of glutathione by the superoxide radical to the disulfide and the sulfonate yielding singlet oxygen. Eur. J. Biochem. 137, 29-36.
    • (1983) Eur. J. Biochem , vol.137 , pp. 29-36
    • Wefers, H.1    Seis, H.2
  • 22
    • 13244299150 scopus 로고    scopus 로고
    • Mechanism-based inactivation of CYP3A4 by HIV protease inhibitors
    • Ernest, C. S., II, Hall, S. D., and Jones, D. R. (2005) Mechanism-based inactivation of CYP3A4 by HIV protease inhibitors. J. Pharmacol. Exp. Ther. 312, 583-591.
    • (2005) J. Pharmacol. Exp. Ther , vol.312 , pp. 583-591
    • Ernest II, C.S.1    Hall, S.D.2    Jones, D.R.3
  • 23
    • 0033026601 scopus 로고    scopus 로고
    • Metabolic interactions between mibefradil and HMG-CoA reductase inhibitors: An in vitro investigation with human liver preparations
    • Prueksaritanont, T., Ma, B., Tang, C., Meng, Y., Assang, C., Lu, P., Reider, P. J., Lin, J. H., and Baillie, T. A. (1999) Metabolic interactions between mibefradil and HMG-CoA reductase inhibitors: An in vitro investigation with human liver preparations. Br. J. Clin. Pharmacol. 47, 291-298.
    • (1999) Br. J. Clin. Pharmacol , vol.47 , pp. 291-298
    • Prueksaritanont, T.1    Ma, B.2    Tang, C.3    Meng, Y.4    Assang, C.5    Lu, P.6    Reider, P.J.7    Lin, J.H.8    Baillie, T.A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.