{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T07:50:27Z","timestamp":1792569027592,"version":"4.5.0"},"reference-count":69,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2025,7,11]],"date-time":"2025-07-11T00:00:00Z","timestamp":1752192000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["BioEssays"],"published-print":{"date-parts":[[2025,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    The amyloid\u2010\n                    <jats:italic>\u03b2<\/jats:italic>\n                    peptide (A\n                    <jats:italic>\u03b2<\/jats:italic>\n                    ), implicated in Alzheimer's disease, exhibits significant polymorphism. At the monomer level, A\n                    <jats:italic>\u03b2<\/jats:italic>\n                    can adopt disordered, helical, and\n                    <jats:italic>\u03b2<\/jats:italic>\n                    \u2010hairpin structures, influenced by environmental conditions. Both oligomeric and fibrillar states, characterized by the prevalence of\n                    <jats:italic>\u03b2<\/jats:italic>\n                    \u2010sheets, are polymorphic in the arrangement of\n                    <jats:italic>\u03b2<\/jats:italic>\n                    \u2010strands. This chameleon\u2010like behavior arises from A\n                    <jats:italic>\u03b2<\/jats:italic>\n                    \u2019s unique sequence and relatively flat energy landscape, which facilitates aggregation and may contribute to the prevalence of Alzheimer's disease, while also enabling disaggregation, thus slowing disease progression. In contrast, Creutzfeldt\u2010Jakob disease, which is much rarer, progresses far more rapidly, likely due to the steeper energy landscape of the prion protein.\n                  <\/jats:p>","DOI":"10.1002\/bies.70039","type":"journal-article","created":{"date-parts":[[2025,7,11]],"date-time":"2025-07-11T07:00:18Z","timestamp":1752217218000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Chameleonic Nature of A\n                    <i>\u03b2<\/i>\n                    : Implications for Alzheimer's and Other Amyloid Diseases"],"prefix":"10.1002","volume":"47","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8734-7765","authenticated-orcid":false,"given":"Birgit","family":"Strodel","sequence":"first","affiliation":[{"name":"Institute of Biological Information Processing Structural Biochemistry (IBI\u20107) Forschungszentrum J\u00fclich  J\u00fclich Germany"},{"name":"Institute of Theoretical and Computational 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