The DOI matches its Crossref record.
Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAcetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition statesDaniel M. QuinnCite this: Chem. Rev. 1987, 87, 5, 955–979Publication Date (Print):October 1, 1987Publication History Published online1 May 2002Published inissue 1 October 1987https://pubs.acs.org/doi/10.1021/cr00081a005https://doi.org/10.1021/cr00081a005research-articleACS PublicationsRequest reuse permissionsArticle Views6491Altmetric-Citations884LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
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“An increase of acetylcholine concentration (ACh) at the synapse by inhibiting the acetylcholinesterase (AChE) is one of the approaches to slow down the progression of AD [18,19,20,21,22,23,24,25,26].”
From Acetylcholinesterase Inhibitory Potential of Various Sesquiterpene Analogues for Alzheimer’s Disease Therapy (2021) · cites this paper as [20]
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Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., & Silman, I. (1991) · Science · doi:10.1126/science.1678899 · Cited by 2,740
Acetylcholinesterase Inhibitors: Pharmacology and Toxicology
Colovic, M. B., Krstic, D. Z., Lazarevic-Pasti, T. D., Bondzic, A. M., & Vasic, V. M. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311030006 · Cited by 2,611
Molecular and cellular biology of cholinesterases
Massoulié, J., Pezzementi, L., Bon, S., Krejci, E., & Vallette, F.-M. (1993) · Progress in Neurobiology · doi:10.1016/0301-0082(93)90040-y · Cited by 1,214
Destruction and Detection of Chemical Warfare Agents
Kim, K., Tsay, O. G., Atwood, D. A., & Churchill, D. G. (2011) · Chemical Reviews · doi:10.1021/cr100193y · Cited by 1,013
Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products
Nicolet, Y., Lockridge, O., Masson, P., Fontecilla-Camps, J. C., & Nachon, F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210241200 · Cited by 851
Metadata
- Authors
- Quinn, D. M.
- Corresponding author
- Quinn, Daniel M.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 1987-10-01
- Volume
- 87
- Issue
- 5
- Pages
- 955-979
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2013132270
- Cited by
- 1,072
- References
- 0
- Citations by year
- 2026: 15 · 2025: 23 · 2024: 32 · 2023: 40 · 2022: 37 · 2021: 40 · 2020: 42 · 2019: 52 · 2018: 49 · 2017: 42 · 2016: 39 · 2015: 44 · 2014: 50 · 2013: 36 · 2012: 33
- FWCI
- 5.92
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Chemical Reviews (publishedVersion)
- Topics
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Physical Sciences › Chemistry › Organic Chemistry › Physical Organic Chemistry and Reaction Kinetics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
- Keywords
- acetylcholinesterase, enzyme structure, reaction dynamics, enzyme catalysis, acetylcholine hydrolysis, enzyme mechanism
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