Conversion of Acetylcholinesterase to Butyrylcholinesterase: Modeling and Mutagenesis

Autor: Harel, M., Sussman, J. L., Krejci, E., Bon, S., Chanal, P., Massoulie, J., Silman, I.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 1992 Nov . 89(22), 10827-10831.

Externí odkaz: https://www.jstor.org/stable/2362004

Two distinct proteins are associated with tetrameric acetylcholinesterase on the cell surface

Autor: Perrier, A., Xavier Cousin, Boschetti, N., Haas, R., Chatel, Jm, Bon, S., Roberts, Wl, Pickett, Sr, Massoulie, J., Rosenberry, Tl, Krejci, E.

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2000, 275 (44), pp.34260-34265
Journal of Biological Chemistry 44 (275), 34260-34265. (2000)
ResearcherID

International audience

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::d1c39d67903da312aa31df183d4c5b33
https://hal.inrae.fr/hal-02692986

Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle

Autor: Cousin, Xavier, Bon, S., Massoulie, J., Bon, Camille

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1998, 273 (16), pp.9812-9820

International audience

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::6412b72c1e6c4998c5f72b5e01b680ef
https://hal.inrae.fr/hal-02688292

6-Coumarin diazonium salt: a specific affinity label of the Torpedo acetylcholinesterase peripheral site

Autor: Schalk I, Ehret-Sabatier L, Yves Le Feuvre, Bon S, Massoulie J, Goeldner M

Publikováno v: Molecular Pharmacology
Molecular Pharmacology, American Society for Pharmacology and Experimental Therapeutics, 1995, 48 (6), pp.1063-7
Europe PubMed Central

A 6-coumarin diazonium salt was synthesized and tested on Torpedo acetylcholinesterase as a site-directed irreversible probe for quaternary ammonium binding. The rate of the inactivation was examined as a function of time, inhibitor concentration, an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::9f45c5ebd14b7ded44b5a8900c2f414e
https://hal.archives-ouvertes.fr/hal-00174698

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