Conformational Remodeling of Femtomolar Inhibitor−Acetylcholinesterase Complexes in the Crystalline State-Reference-Cited by-同舟云学术

Conformational Remodeling of Femtomolar Inhibitor−Acetylcholinesterase Complexes in the Crystalline State

Published:2010-11-19 Issue:51 Volume:132 Page:18292-18300
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Bourne Yves¹,Radić Zoran¹,Taylor Palmer¹,Marchot Pascale¹

Affiliation:

1. Architecture et Fonction des Macromolécules Biologiques (AFMB, CNRS UMR-6098), Universités d’Aix-Marseille, Campus Luminy—Case 932, F-13288 Marseille cedex 09, France, Department of Pharmacology, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California—San Diego, La Jolla, California 92093-0657, United States, and Centre de Recherche en Neurobiologie-Neurophysiologie de Marseille (CRN2M, CNRS UMR-6231), Institut Fédératif de Recherche Jean Roche, Faculté de Médecine Secteur Nord,...

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja106820e

Reference37 articles.

1. Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states

2. Development of acetylcholinesterase inhibitors in the therapy of Alzheimer's disease

3. Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding Protein

4. Interaction of fluorescence probes with acetylcholinesterase. Site and specificity of propidium binding

5. The Complex of a Bivalent Derivative of Galanthamine with Torpedo Acetylcholinesterase Displays Drastic Deformation of the Active-Site Gorge: Implications for Structure-Based Drug Design

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