{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T16:56:57Z","timestamp":1778864217870,"version":"3.51.4"},"reference-count":55,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2026,1,29]],"date-time":"2026-01-29T00:00:00Z","timestamp":1769644800000},"content-version":"vor","delay-in-days":28,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Nutrition Food Res"],"published-print":{"date-parts":[[2026,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Amyloid\u2010\u03b2\u201042 (A\u03b242) internalization plays a critical role in Alzheimer's disease (AD) pathology. We investigated whether biflavonoids, natural small molecules, could inhibit A\u03b242 uptake and mitigate its cytotoxicity. Biochemical and imaging analyses revealed that biflavonoids dose\u2010dependently blocked A\u03b242 internalization, preventing lamin fragmentation and caspase activation which are considered as key steps in A\u03b242\u2010induced cell death. Confocal microscopy and Western blotting confirmed reduced A\u03b242 entry, while aggregation assays in cell\u2010free conditions demonstrated biflavonoids suppress A\u03b242 fibril, oligomer, and \u03b2\u2010sheet formation. These findings suggest biflavonoids exert cytoprotective effects by inhibiting both A\u03b242 conformational changes and cellular uptake, positioning them as promising anti\u2010amyloidogenic agents for AD therapy.<\/jats:p>","DOI":"10.1002\/mnfr.70406","type":"journal-article","created":{"date-parts":[[2026,1,29]],"date-time":"2026-01-29T10:48:19Z","timestamp":1769683699000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Biflavonoids can Potentially Inhibit Amyloid Beta Internalization to Mitigate Its Cytotoxic Events"],"prefix":"10.1002","volume":"70","author":[{"given":"Md. Aminul","family":"Haque","sequence":"first","affiliation":[{"name":"School of Pharmacy BRAC University, Merul Badda  Dhaka Bangladesh"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Md. Selim","family":"Hossain","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences Chosun University, Dong\u2010gu  Gwangju South Korea"},{"name":"Vascular Biology Centre Medical College of Georgia at Augusta University  Augusta Georgia USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vijay Sankar","family":"Ramasamy","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences Chosun University, Dong\u2010gu  Gwangju South Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Il Seon","family":"Park","sequence":"additional","affiliation":[{"name":"Department of Biomedical Sciences Chosun University, Dong\u2010gu  Gwangju South Korea"},{"name":"Department of Cellular and Molecular Medicine Chosun University, Dong\u2010gu  Gwangju South Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2026,1,29]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1474\u20104422(11)70072\u20102"},{"key":"e_1_2_10_3_1","doi-asserted-by":"publisher","DOI":"10.3389\/fphar.2015.00221"},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/aps.2017.28"},{"key":"e_1_2_10_5_1","first-page":"269","article-title":"Ultrastructural Studies in Alzheimer's Presenile Dementia","volume":"44","author":"Terry R. 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