{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T04:23:23Z","timestamp":1791606203100,"version":"4.3.4"},"reference-count":103,"publisher":"MDPI AG","issue":"21","license":[{"start":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T00:00:00Z","timestamp":1761523200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010927","name":"Southern Connecticut State University","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100010927","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Acetylcholinesterase (AChE) inhibitors are the primary target for single-molecule anti-Alzheimer\u2019s disease (AD) therapeutics. Though AChE has historically been the focus of investigation for small-molecule inhibitors, interest in another cholinergic enzyme, butyrylcholinesterase (BChE), has grown in recent years. Attention stems from BChE\u2019s role in \u03b2-amyloid (A\u03b2) protein aggregation and an increase in BChE concentration during the late stages of AD, where a decrease in AChE concentration is also observed. Currently, five FDA-approved drugs are on the market for inhibiting AChE, though no BChE-selective drugs have been approved so far. In this review, we focus on newly identified BChE selective inhibitors and present the ideas behind these discoveries.<\/jats:p>","DOI":"10.3390\/molecules30214201","type":"journal-article","created":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T02:23:28Z","timestamp":1761704608000},"page":"4201","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["The Selectivity of Butyrylcholinesterase Inhibitors Revisited"],"prefix":"10.3390","volume":"30","author":[{"given":"Michael D.","family":"Gambardella","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA"},{"name":"Department of Chemistry and Biochemistry, Southern Connecticut State University, New Haven, CT 06515, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yigui","family":"Wang","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Southern Connecticut State University, New Haven, CT 06515, USA"},{"name":"Department of Chemistry and Chemical & Biochemical Engineering, University of New Haven, West Haven, CT 06516, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiongdong","family":"Pang","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Southern Connecticut State University, New Haven, CT 06515, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,10,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"315","DOI":"10.2174\/1570159X11311030006","article-title":"Acetylcholinesterase inhibitors: Pharmacology and toxicology","volume":"11","year":"2013","journal-title":"Curr. 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