Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states

Quinn, Daniel M.

doi:10.1021/cr00081a005

Cited by 1,072Cholinesterase and Neurodegenerative DiseasesChemical Reaction MechanismsEnzyme function and inhibition

Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states

Quinn, Daniel M.·1987·Chemical Reviews

DOI 10.1021/cr00081a005

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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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Increasing acetylcholine concentration at the synapse by inhibiting AChE is one approach to slow down the progression of AD.
“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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“The catalytic power of AChE supports spatially and temporally constrained cholinergic signaling The catalytic power of AChE has been called “amazing” and “a hallmark of an evolutionarily perfect enzyme” (Quinn, 1987).”
Background
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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
DOI: 10.1021/cr00081a005
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 › Cholinesterase and Neurodegenerative Diseases
Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
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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Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states

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