{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,24]],"date-time":"2026-02-24T03:30:14Z","timestamp":1771903814645,"version":"3.50.1"},"reference-count":48,"publisher":"MDPI AG","issue":"24","license":[{"start":{"date-parts":[[2022,12,12]],"date-time":"2022-12-12T00:00:00Z","timestamp":1670803200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Institute on Aging of the National Institutes of Health","award":["RF1AG073434-01A1"],"award-info":[{"award-number":["RF1AG073434-01A1"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>The brains of Alzheimer\u2019s disease (AD) patients contain numerous amyloid plaques that are diagnostic of the disease. The plaques are primarily composed of the amyloidogenic peptides proteins A\u03b240 and A\u03b242, which are derived by the processing of the amyloid pre-cursor protein (APP) by two proteases called \u03b2-secretase and \u03b3-secretase. A\u03b242 differs from A\u03b240 in having two additional hydrophobic amino acids, ILE and ALA, at the C-terminus. A small percentage of AD is autosomal dominant (ADAD) and linked either to the genes for the presenilins, which are part of \u03b3-secretase, or APP. Because ADAD shares most pathogenic features with widespread late-onset AD, A\u03b2 peptides have become the focus of AD research. Fibrils formed by the aggregation of these peptides are the major component of plaques and were initially targeted in AD therapy. However, the fact that the abundance of plaques does not correlate well with cognitive decline in AD patients has led investigators to examine smaller A\u03b2 aggregates called oligomers. The low levels and heterogeneity of A\u03b2 oligomers have made the determination of their structures difficult, but recent structure determinations of oligomers either formed or initiated in detergents have been achieved. We report here on the structures of these oligomers and suggest how they may be involved in AD.<\/jats:p>","DOI":"10.3390\/molecules27248804","type":"journal-article","created":{"date-parts":[[2022,12,13]],"date-time":"2022-12-13T03:32:32Z","timestamp":1670902352000},"page":"8804","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Oligomer Formation by Amyloid-\u03b242 in a Membrane-Mimicking Environment in Alzheimer\u2019s Disease"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3579-7681","authenticated-orcid":false,"given":"Terrone L.","family":"Rosenberry","sequence":"first","affiliation":[{"name":"The Departments of Neuroscience and Pharmacology, Mayo Clinic, Jacksonville, FL 32224, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9020-0302","authenticated-orcid":false,"given":"Huan-Xiang","family":"Zhou","sequence":"additional","affiliation":[{"name":"Departments of Chemistry and Physics, University of Illinois Chicago, Chicago, IL 60608, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Scott M.","family":"Stagg","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA"},{"name":"Department of Biological Sciences, Florida State University, Tallahassee, FL 32306, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7183-1942","authenticated-orcid":false,"given":"Anant K.","family":"Paravastu","sequence":"additional","affiliation":[{"name":"School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 311 Ferst Drive NW, Atlanta, GA 30332, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2022,12,12]]},"reference":[{"key":"ref_1","first-page":"269","article-title":"Ultrastructural studies in Alzheimer\u2019s presenile dementia","volume":"44","author":"Terry","year":"1964","journal-title":"Am. 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