Energy Landscapes of Human Acetylcholinesterase and Its Huperzine A-Inhibited Counterpart-Reference-Cited by-同舟云学术

Energy Landscapes of Human Acetylcholinesterase and Its Huperzine A-Inhibited Counterpart

Published:2012-12-13 Issue:51 Volume:116 Page:14744-14753
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Trapp Marcus¹²³⁴,Trovaslet Marie⁵,Nachon Florian⁵,Koza Marek M.⁴,van Eijck Lambert⁶,Hill Flynn⁷,Weik Martin¹²³,Masson Patrick¹²³⁵,Tehei Moeava⁷⁸,Peters Judith¹²³⁴

Affiliation:

1. Comissariat à l’Energie Atomique, Institut de Biologie Structurale, F-38054 Grenoble, France

2. Centre National De La Recherche Scientifique, UMR5075, F-38027 Grenoble, France

3. Université Joseph Fourier, UFR PhITEM, F-38041 Grenoble Cédex 9, France

4. Institut Laue Langevin, F-38042 Grenoble Cédex 9, France

5. Institut de Recherche Biomédicale des Armées, F-38700 La Tronche, France

6. Delft University of Technology, Faculty of Applied Sciences, RST/NPM2 Mekelweg 15, 2629JB Delft Netherlands

7. School of Chemistry and Centre for Medical Bioscience, University of Wollongong, Wollongong, NSW 2522, Australia

8. Australian Institute of Nuclear Science and Engineering (AINSE), Menai, NSW, Australia

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/jp304704h

Reference64 articles.

1. Protein dynamics studied by neutron scattering

2. Neutron scattering lengths and cross sections

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

4. On the Mechanism of Acetylcholinesterase Action: The Electrostatically Induced Acceleration of the Catalytic Acylation Step

5. Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.

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