메뉴 건너뛰기




Volumn 119-120, Issue , 1999, Pages 147-157

Inhibition of Drosophila acetylcholinesterase by 7-(methylethoxyphosphinyloxy)1-methyl-quinolinium iodide

Author keywords

Acetylcholinesterase; Kinetic model; Organophosphonate; Progress curves; Stopped flow

Indexed keywords

ACETYLCHOLINESTERASE; METHYLPHOSPHONIC ACID; ORGANOPHOSPHATE;

EID: 0032998177     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(99)00023-X     Document Type: Conference Paper
Times cited : (7)

References (22)
  • 1
    • 0005483756 scopus 로고
    • A.M. Goldberg, & I. Hanin. New York: Raven Press
    • Main A.R. Goldberg A.M., Hanin I. Biology of Cholinergic Function. 1976;312-315 Raven Press, New York.
    • (1976) Biology of Cholinergic Function , pp. 312-315
    • Main, A.R.1
  • 2
    • 0023605724 scopus 로고
    • Horse serum butyrylcholinesterase kinetics: A molecular mechanism based on inhibition studies with dansylaminoethyl-trimethylammonium
    • Cauet G., Friboulet A., Thomas D. Horse serum butyrylcholinesterase kinetics: a molecular mechanism based on inhibition studies with dansylaminoethyl-trimethylammonium. Biochem. Cell. Biol. 65:1987;529-535.
    • (1987) Biochem. Cell. Biol. , vol.65 , pp. 529-535
    • Cauet, G.1    Friboulet, A.2    Thomas, D.3
  • 3
    • 0029092671 scopus 로고
    • Fasciculin 2 binds to the peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation
    • Eastman J., Wilson E.J., Cervenansky C., Rosenberry T.L. Fasciculin 2 binds to the peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation. J. Biol. Chem. 270(34):1995;19694-19701.
    • (1995) J. Biol. Chem. , vol.270 , Issue.34 , pp. 19694-19701
    • Eastman, J.1    Wilson, E.J.2    Cervenansky, C.3    Rosenberry, T.L.4
  • 5
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein. Science. 253:1991;872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 6
    • 0028818897 scopus 로고
    • Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
    • Bourne Y., Taylor P., Marchot P. Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex. Cell. 83:1995;503-512.
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 7
    • 0032518976 scopus 로고    scopus 로고
    • Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration
    • Marcel V., Palacios L.G., Pertuy C., Masson P., Fournier D. Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration. Biochem. J. 329:1998;329-334.
    • (1998) Biochem. J. , vol.329 , pp. 329-334
    • Marcel, V.1    Palacios, L.G.2    Pertuy, C.3    Masson, P.4    Fournier, D.5
  • 8
    • 0026681643 scopus 로고
    • Acetylcholinesterase: Two types of modification confer resistance to insecticides
    • Fournier D., Bride J.M., Hoffman F., Karch F. Acetylcholinesterase: Two types of modification confer resistance to insecticides. J. Biol. Chem. 267(20):1992;14270-14274.
    • (1992) J. Biol. Chem. , vol.267 , Issue.20 , pp. 14270-14274
    • Fournier, D.1    Bride, J.M.2    Hoffman, F.3    Karch, F.4
  • 10
    • 0031552058 scopus 로고    scopus 로고
    • Kinetic characterization of all steps of the interaction between acetylcholinesterase and eserine
    • Stojan J., Zorko M. Kinetic characterization of all steps of the interaction between acetylcholinesterase and eserine. Biochim. Biophys. Acta. 1337:1997;75-84.
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 75-84
    • Stojan, J.1    Zorko, M.2
  • 11
    • 2642670423 scopus 로고    scopus 로고
    • Analysis of progress curves in an acetylcholinesterase reaction: A numerical integration treatment
    • Stojan J. Analysis of progress curves in an acetylcholinesterase reaction: a numerical integration treatment. J. Chem. Infor. Comp. Sci. 37:1997;1025-1027.
    • (1997) J. Chem. Infor. Comp. Sci. , vol.37 , pp. 1025-1027
    • Stojan, J.1
  • 12
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland W.W. Statistical analysis of enzyme kinetic data. Methods Enzymol. 63:1963;103-138.
    • (1963) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 13
    • 0022539620 scopus 로고
    • Synthesis and in vitro properties of a powerful quaternary methylphosphonate inhibitor of acetylcholinesterase.
    • Levy D., Ashsni Y. Synthesis and in vitro properties of a powerful quaternary methylphosphonate inhibitor of acetylcholinesterase. Biochem. Pharmacol. 35(7):1986;1079-1085.
    • (1986) Biochem. Pharmacol. , vol.35 , Issue.7 , pp. 1079-1085
    • Levy, D.1    Ashsni, Y.2
  • 14
    • 0002015571 scopus 로고
    • Rapid reaction methods in biochemistry
    • A. Neuberger, & L.L.M. Van Deenen. Amsterdam: Elsevier
    • Gibbson Q. Rapid reaction methods in biochemistry. Neuberger A., Van Deenen L.L.M. Modern Physical Methods in Biochemistry, Part B. 1988;65-84 Elsevier, Amsterdam.
    • (1988) Modern Physical Methods in Biochemistry, Part B , pp. 65-84
    • Gibbson, Q.1
  • 15
    • 0026442882 scopus 로고
    • Velocity of Ellman's reaction and its implication for kinetic studies in the millisecond time range.
    • Stojan J., Pavlic M.R. Velocity of Ellman's reaction and its implication for kinetic studies in the millisecond time range. Neurochem. Res. 17(12):1992;1207-1210.
    • (1992) Neurochem. Res. , vol.17 , Issue.12 , pp. 1207-1210
    • Stojan, J.1    Pavlic, M.R.2
  • 16
    • 0031745115 scopus 로고    scopus 로고
    • Equations for progress curves of some kinetic models of enzyme-single substrate-single slow binding modifier system
    • Stojan J. Equations for progress curves of some kinetic models of enzyme-single substrate-single slow binding modifier system. J. Enzyme Inhibition. 13:1998;161-176.
    • (1998) J. Enzyme Inhibition , vol.13 , pp. 161-176
    • Stojan, J.1
  • 17
    • 0014429144 scopus 로고
    • A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady-state
    • Cha S. A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady-state. J. Biol. Chem. 243(4):1968;820-825.
    • (1968) J. Biol. Chem. , vol.243 , Issue.4 , pp. 820-825
    • Cha, S.1
  • 18
    • 0021636975 scopus 로고
    • Regression analysis of nonlinear Arrhenius plot: An empirical model and a computer program
    • Duggleby R.G. Regression analysis of nonlinear Arrhenius plot: an empirical model and a computer program. Comput. Biol. Med. 14(4):1984;447-455.
    • (1984) Comput. Biol. Med. , vol.14 , Issue.4 , pp. 447-455
    • Duggleby, R.G.1
  • 20
    • 0026653485 scopus 로고
    • Simultaneous analysis for testing of models and parameter estimation
    • Senear D.F., Bolen D.W. Simultaneous analysis for testing of models and parameter estimation. Methods Enzymol. 210:1992;463-485.
    • (1992) Methods Enzymol. , vol.210 , pp. 463-485
    • Senear, D.F.1    Bolen, D.W.2
  • 21
    • 0028878141 scopus 로고
    • Acetylcholinesterase: Diffusional encounter rate constants for dumbbell models of ligand
    • Antosiewicz J., Gilson M.K., Lee I.H., McCammon J.A. Acetylcholinesterase: diffusional encounter rate constants for dumbbell models of ligand. Biophys. J. 68:1995;62-68.
    • (1995) Biophys. J. , vol.68 , pp. 62-68
    • Antosiewicz, J.1    Gilson, M.K.2    Lee, I.H.3    McCammon, J.A.4
  • 22
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison J.F., Walsh C.T. The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. 61:1988;207.
    • (1988) Adv. Enzymol. , vol.61 , pp. 207
    • Morrison, J.F.1    Walsh, C.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.