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The structure shows striking similarity to MSA-amplified and PD-associated E46K fibrils. However, mouse \u03b1-synuclein fibrils display altered packing arrangements, reduced hydrophobicity, and heightened fragmentation sensitivity and evoke only weak immunological responses. Furthermore, mouse \u03b1-synuclein fibrils exhibit exacerbated pathological spread in neurons and humanized \u03b1-synuclein mice. These findings provide critical insights into the structural underpinnings of \u03b1-synuclein pathogenicity and emphasize a need to reassess the role of mouse \u03b1-synuclein fibrils in the development of related diagnostic probes and therapeutic interventions.<\/jats:p>","DOI":"10.1126\/sciadv.adq3539","type":"journal-article","created":{"date-parts":[[2024,11,1]],"date-time":"2024-11-01T13:59:14Z","timestamp":1730469554000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":39,"title":["Mouse \u03b1-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases"],"prefix":"10.1126","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6654-5773","authenticated-orcid":true,"given":"Arpine","family":"Sokratian","sequence":"first","affiliation":[{"name":"Duke Center for Neurodegeneration Research, Department of Pharmacology and Cancer Biology, Duke University, Durham, 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