Crystal structures of oxime-bound fenamiphos-acetylcholinesterases: Reactivation involving flipping of the His447 ring to form a reactive Glu334–His447–oxime triad

Author:

Hörnberg Andreas,Artursson Elisabet,Wärme Rikard,Pang Yuan-Ping,Ekström Fredrik

Publisher

Elsevier BV

Subject

Pharmacology,Biochemistry

Reference40 articles.

1. The X-ray structure of a transition state analogue complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase;Harel;J Am Chem Soc,1996

2. Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivatives;Radic;Mol Pharmacol,1991

3. Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center;Shafferman;EMBO J,1992

4. Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core;Barak;J Biol Chem,1994

5. Differential effects of “peripheral” site ligands on Torpedo and chicken acetylcholinesterase;Eichler;Mol Pharmacol,1994

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