Phosphonylation Mechanisms of Sarin and Acetylcholinesterase: A Model DFT Study-Reference-Cited by-同舟云学术

Phosphonylation Mechanisms of Sarin and Acetylcholinesterase: A Model DFT Study

Published:2006-03-18 Issue:14 Volume:110 Page:7567-7573
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Wang Jing¹,Gu Jiande¹,Leszczynski Jerzy¹

Affiliation:

1. Computational Center for Molecular Structure and Interactions, Department of Chemistry, Jackson State University, Jackson, Mississippi 39217, and Drug Design & Discovery Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201203, P. R. China

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp060370v

Reference47 articles.

1. Rosenberry, T. L.Advances in Enzymology; Meister, A., Ed.; Jon Wiley & Sons: New York, 1975; Vol. 43, pp 103−218.

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

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

4. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.

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