{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T03:56:56Z","timestamp":1790308616384,"version":"4.1.0"},"reference-count":71,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2024,6,26]]},"abstract":"<jats:p>Protein mislocalization is a key initial step in neurodegeneration, regardless of etiology, and has been linked to changes in the dynamic addition of saturated fatty acids to proteins, a process known as S-acylation. With the advent of new techniques to study S-acylation and the recent discovery of new enzymes that facilitate protein deacylation, novel small molecules are emerging as potential new therapeutic treatments. Huntington disease (HD) is a devastating, fatal neurodegenerative disease characterized by motor, cognitive, and psychiatric deficits caused by a CAG repeat expansion in the HTT gene. The protein that is mutated in HD, huntingtin, is less S-acylated which is associated with mutant HTT aggregation and cytotoxicity. Recent exciting findings indicate that restoring S-acylation in HD models using small molecule inhibitors of the deacylation enzymes is protective. Herein, we set out to describe the known roles of S-acylation in HD and how it can be targeted for therapeutic design.<\/jats:p>","DOI":"10.1042\/bst20231290","type":"journal-article","created":{"date-parts":[[2024,5,2]],"date-time":"2024-05-02T09:38:58Z","timestamp":1714642738000},"page":"1385-1392","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Let's get fat: emergence of\n                    <i>S<\/i>\n                    -acylation as a therapeutic target in Huntington disease"],"prefix":"10.1042","volume":"52","author":[{"given":"Dale D.O.","family":"Martin","sequence":"first","affiliation":[{"name":"1NeurdyPhagy Lab, Department of Biology, Faculty of Science, University of Waterloo, Waterloo, Ontario, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9661-141X","authenticated-orcid":false,"given":"Shaun S.","family":"Sanders","sequence":"additional","affiliation":[{"name":"2NeuroPalm Lab, Department of Molecular and Cellular Biology, College of Biological Sciences, University of Guelph, Guelph, Ontario, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2024,5,2]]},"reference":[{"key":"2024062609302226600_BST-2023-1290CC1","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1186\/s13024-020-00397-1","article-title":"The role of TDP-43 mislocalization in amyotrophic lateral sclerosis","volume":"15","year":"2020","journal-title":"Mol. 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