{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T20:42:49Z","timestamp":1772829769118,"version":"3.50.1"},"reference-count":31,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2025,5,20]],"date-time":"2025-05-20T00:00:00Z","timestamp":1747699200000},"content-version":"vor","delay-in-days":139,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100016846","name":"Shimadzu Corporation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100016846","id-type":"DOI","asserted-by":"publisher"}]},{"name":"European Union\u2019s Horizon 2020 Research and Innovation Programme"},{"name":"Marie Sk\u0142odowska-Curie","award":["860197"],"award-info":[{"award-number":["860197"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2025,4,30]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The differential diagnosis of \u03b1-synucleinopathies, including Parkinson\u2019s disease, dementia with Lewy bodies (DLB) and multiple system atrophy (MSA), remains challenging due to overlapping clinical features and the absence of reliable biomarkers. We developed a targeted mass spectrometry assay to profile \u03b1-synuclein peptides in plasma from Parkinson\u2019s disease (n = 82), DLB (n = 32), MSA (n = 8) and controls (n = 21). We hypothesized that disease-specific truncations or post-translational modifications would alter levels of non-modified \u03b1-synuclein peptides across \u03b1-synucleinopathies. The assay quantified non-modified peptides derived from the N-terminus and non-amyloid component (NAC) domain, regions implicated in aggregate formation. Although peptide levels were consistent across disease groups, a distinct NAC domain pattern observed in MSA may reflect unique pathological processes. This study presents the first blood-based profiling of \u03b1-synuclein peptides in these disorders, offering a basis for further investigation into disease mechanisms. Refinement of the assay to include post-translational modifications could enhance understanding of \u03b1-synucleinopathies and support future biomarker development.<\/jats:p>","DOI":"10.1093\/braincomms\/fcaf189","type":"journal-article","created":{"date-parts":[[2025,5,20]],"date-time":"2025-05-20T17:54:08Z","timestamp":1747763648000},"source":"Crossref","is-referenced-by-count":1,"title":["Plasma \u03b1-synuclein domain profiles across \u03b1-synucleinopathies"],"prefix":"10.1093","volume":"7","author":[{"given":"Marie-Laure","family":"Pons","sequence":"first","affiliation":[{"name":"LBPC-PPC, Universit\u00e9 de Montpellier, IRMB CHU de Montpellier , INM INSERM, Montpellier 34295 ,","place":["France"]},{"name":"Shimadzu Corporation , LC-MS & Life Sciences, Duisburg 47269 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