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. 2023 May 1;32(5):e4639. doi: 10.1002/pro.4639

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© 2023 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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Schematic illustration of the overall extraction process of Aβ aggregates from brain tissues of deceased AD patients. Freshly frozen cortical brain samples are homogenized/soaked with extraction buffer and then centrifuged to obtain a soluble brain fraction supernatant and a mixture of insoluble brain fraction pellet. The insoluble pellet (1) is subjected to detergent‐containing buffer and/or formic acid to obtain solubilized amyloid‐enriched fibrils. On the other hand, the soluble brain fraction supernatant (2) is further subjected to ultracentrifugation and/or immunoprecipitation to selectively purify soluble Aβ oligomers and dimers.