Kinetic, equilibrium and spectroscopic studies on cation association at the active center of acetylcholinesterase: topographic distinction between trimethyl and trimethylammonium sites
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference29 articles.
1. Hydrolysis by acetylcholinesterase. Apparent molal volumes and trimethyl and methyl subsites.
2. Cationic and uncharged substrates and reversible inhibitors in hydrolysis by acetylcholinesterase (EC 3.1.1.7). The trimethyl subsite.
3. Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands
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1. Methyl 2-(2-(4-formylphenoxy)acetamido)-2-substituted acetate derivatives: A new class of acetylcholinesterase inhibitors;Bioorganic & Medicinal Chemistry Letters;2007-04
2. Substrate and Product Trafficking through the Active Center Gorge of Acetylcholinesterase Analyzed by Crystallography and Equilibrium Binding;Journal of Biological Chemistry;2006-09
3. Synthesis, anticholinesterase activity and structure–Activity relationships of m-Aminobenzoic acid derivatives;Bioorganic & Medicinal Chemistry Letters;2003-05
4. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site;The EMBO Journal;2003-01-02
5. Acceleration of Oxime-Induced Reactivation of Organophosphate-Inhibited Fetal Bovine Serum Acetylcholinesterase by Monoquaternary and Bisquaternary Ligands;Molecular Pharmacology;1998-04-01
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