{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T08:23:32Z","timestamp":1791102212009,"version":"4.1.0"},"reference-count":135,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2012,3,7]],"date-time":"2012-03-07T00:00:00Z","timestamp":1331078400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The aggregation of proteins into insoluble amyloid fibrils coincides with the onset of numerous diseases. An array of techniques is available to study the different stages of the amyloid aggregation process. Recently, emphasis has been placed upon the analysis of oligomeric amyloid species, which have been hypothesized to play a key role in disease progression. This paper reviews techniques utilized to study aggregation of the amyloid-\u03b2 protein (A\u03b2) associated with Alzheimer\u2019s disease. In particular, the review focuses on techniques that provide information about the size or quantity of oligomeric A\u03b2 species formed during the early stages of aggregation, including native-PAGE, SDS-PAGE, Western blotting, capillary electrophoresis, mass spectrometry, fluorescence correlation spectroscopy, light scattering, size exclusion chromatography, centrifugation, enzyme-linked immunosorbent assay, and dot blotting.<\/jats:p>","DOI":"10.3390\/ijms13033038","type":"journal-article","created":{"date-parts":[[2012,3,7]],"date-time":"2012-03-07T12:43:39Z","timestamp":1331124219000},"page":"3038-3072","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":108,"title":["Unraveling the Early Events of Amyloid-\u03b2 Protein (A\u03b2) Aggregation: Techniques for the Determination of A\u03b2 Aggregate Size"],"prefix":"10.3390","volume":"13","author":[{"given":"N. Elizabeth","family":"Pryor","sequence":"first","affiliation":[{"name":"Ralph E. Martin Department of Chemical Engineering, 3202 Bell Engineering Center, University of Arkansas, Fayetteville, AR 72701, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Melissa A.","family":"Moss","sequence":"additional","affiliation":[{"name":"Department of Chemical Engineering, 2C02 Swearingen Engineering Center, University of South Carolina, Columbia, SC 29208, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christa N.","family":"Hestekin","sequence":"additional","affiliation":[{"name":"Ralph E. Martin Department of Chemical Engineering, 3202 Bell Engineering Center, University of Arkansas, Fayetteville, AR 72701, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2012,3,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3708","DOI":"10.1093\/brain\/awr308","article-title":"Neocortical and hippocampal amyloid-\u03b2 and tau measures associate with dementia in the oldest-old","volume":"134","author":"Robinson","year":"2011","journal-title":"Brain"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00401-011-0910-3","article-title":"National institute on aging-alzheimer\u2019s association guidelines for the neuropathologic assessment of alzheimer\u2019s disease: A practical approach","volume":"123","author":"Montine","year":"2012","journal-title":"Acta Neuropathol"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Kagan, B.L., Jang, H., Capone, R., Arce, F.T., Ramachandran, S., Lal, R., and Nussinov, R (2011). 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