61
Views
2
CrossRef citations to date
0
Altmetric
Original Article

Homology Built Model of Acetylcholinesterase from Drosophila Melanogaster

Pages 193-201 | Received 20 May 1998, Accepted 30 Sep 1998, Published online: 02 Jul 2009

References

  • Massoulie J., Pezementi L., Bon S., Krejci E., Valette F.-M. Molecular and cell biology of cholinesterases. Prog. Neurobiol 1993; 41: 31–91
  • Usdin E. Anricholinesterase Agenrs, A. G. Karcsmar. Pergamon Press, Oxford 1970; 63–185
  • Marcel V., Palacios L. G., Pertuy C., Masson P., Fournier D. Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration. Biochem. J 1998; 329: 329–334
  • Masson P., Froment M. T., Bartels C., Lockridge O. Asp70 in the pheripheral anionic site of human butyrylcholinesterase. Eur. J. Biochem 1996; 235: 34–48
  • Estrada-Mondaca S., Fournier D., Klaebe A., Magne F., Marcel V., Masson P., Stojan J., Villatte F. Metabolisation of substrate by invertebrate cholinester-ase. 3rd International Meeting on Esterases Reacting with Organophosphorous Compounds, Dubrovnik, April, 1998. Croatia, 15–18
  • Hall L. M.C., Spierer P. The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5′ leader. EMBO J 1986; 5: 2949–2954
  • Voorintholt R., Kosters M. T., Vegter G., Vriend G., Hol W. G.J. A very fast program for visualizing protein surfaces. channels and cavities. J. Mol. Graph 1989; 243–245
  • Brooks B. R., Bruccoleri R. E., Olafson B. D., States D. J., Swaminathan S., Karplus M. CHARMM: A program for macromolecular energy, minimization, and dynamic calculations. J. Comp. Chem 1983; 4: 187–217
  • Ellinan G. L., Courtney K. D., Andres V., Featherstone R. M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharnzncol 1961; 7: 88–95
  • Duggleby R. G. Regression analysis of nonlinear Arrhenius plot: an emprical model and a computer program. Comput. Biol. Med 1984; 14: 447–455
  • Fournier D., Bride J. M., Hoffman F., Karch F. Acetylcholinesterase: Two types of modification confer resistance to insecticides. J. Biol. Chem 1992; 267: 14270–14274
  • Levy D., Ashani Y. Synthesis and in vitro properties of a powerful quaternary methylphosphonate inhibitor of acetylcholinesterase. Biochem. Pharmacol 1986; 35: 1079–1085
  • , WEB: http://www.ensam.inra.fr/cholinesterase
  • Harel M., Sussman J. L., Krejci E., Bon S., Chanal P., Massoulie J., Silman I. Conversion of acetylcholinesterase to butyrplcholinesterase: modeling and muta-genesis. Proc., Natl. Acad. Sci. USA 1992; 89: 10827–10831
  • Sussman J. L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acctylcholine-binding protein. Science 1991; 253: 872–879
  • Radi Z., Quinn D., Vellom D. C., Camp S., Taylor P. Allosteric control of acetqlcholinesterase catalysis by Fasciculin. J. Biol. Chem 1995; 270: 20391–20399
  • Szegletes T., Mallender W. D., Rosenberry T. Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands. Biochemistry, 37: 4206–4216

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.