Identification of new allosteric sites and modulators of AChE through computational and experimental tools-Reference-Cited by-同舟云学术

Identification of new allosteric sites and modulators of AChE through computational and experimental tools

Published:2018-01-01 Issue:1 Volume:33 Page:1034-1047
ISSN:1475-6366
Container-title:Journal of Enzyme Inhibition and Medicinal Chemistry
language:en
Short-container-title:Journal of Enzyme Inhibition and Medicinal Chemistry

Author:

Roca Carlos¹,Requena Carlos¹,Sebastián-Pérez Víctor¹^ORCID,Malhotra Sony²,Radoux Chris²³,Pérez Concepción⁴,Martinez Ana¹^ORCID,Antonio Páez Juan⁴,Blundell Tom L.²,Campillo Nuria E.¹^ORCID

Affiliation:

1. Centro de Investigaciones Biológicas (CIB-CSIC), C/Ramiro de Maeztu, Madrid, Spain;

2. Department of Biochemistry, University of Cambridge, Cambridge, UK;

3. Cambridge Crystallographic Data Centre, Cambridge, UK;

4. Instituto de Química Médica (IQM-CSIC), C/Juan de la Cierva, Madrid, Spain

Funder

Ministerio de Economía y Competitividad

Publisher

Informa UK Limited

Subject

Drug Discovery,Pharmacology,General Medicine

Link

https://www.tandfonline.com/doi/pdf/10.1080/14756366.2018.1476502

Reference59 articles.

1. Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates precedes general acid-base catalysis.

2. Stress-induced alternative splicing of acetylcholinesterase results in enhanced fear memory and long-term potentiation

3. Acetylcholinesterase: ‘classical’ and ‘non-classical’ functions and pharmacology

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