{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T23:52:41Z","timestamp":1791330761262,"version":"4.3.1"},"reference-count":50,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2012,5,1]]},"abstract":"<jats:p>Parkinson's disease is an age-related movement disorder characterized by the presence in the mid-brain of amyloid deposits of the 140-amino-acid protein AS (\u03b1-synuclein). AS fibrillation follows a nucleation polymerization pathway involving diverse transient prefibrillar species varying in size and morphology. Similar to other neurodegenerative diseases, cytotoxicity is currently attributed to these prefibrillar species rather than to the insoluble aggregates. Nevertheless, the underlying molecular mechanisms responsible for cytotoxicity remain elusive and structural studies may contribute to the understanding of both the amyloid aggregation mechanism and oligomer-induced toxicity. It is already recognized that soluble oligomeric AS species adopt \u03b2-sheet structures that differ from those characterizing the fibrillar structure. In the present study we used ATR (attenuated total reflection)\u2013FTIR (Fourier-transform infrared) spectroscopy, a technique especially sensitive to \u03b2-sheet structure, to get a deeper insight into the \u03b2-sheet organization within oligomers and fibrils. Careful spectral analysis revealed that AS oligomers adopt an antiparallel \u03b2-sheet structure, whereas fibrils adopt a parallel arrangement. The results are discussed in terms of regions of the protein involved in the early \u03b2-sheet interactions and the implications of such conformational arrangement for the pathogenicity associated with AS oligomers.<\/jats:p>","DOI":"10.1042\/bj20111924","type":"journal-article","created":{"date-parts":[[2012,2,9]],"date-time":"2012-02-09T07:26:24Z","timestamp":1328772384000},"page":"719-726","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":250,"title":["Toxic prefibrillar \u03b1-synuclein amyloid oligomers adopt a distinctive antiparallel \u03b2-sheet structure"],"prefix":"10.1042","volume":"443","author":[{"given":"Mar\u00eda\u00a0Soledad","family":"Celej","sequence":"first","affiliation":[{"name":"Centro de Investigaciones en Qu\u00edmica Biol\u00f3gica de C\u00f3rdoba (CIQUIBIC, UNC-CONICET), Departamento de Qu\u00edmica Biol\u00f3gica, Facultad de Ciencias Qu\u00edmicas, Universidad Nacional de C\u00f3rdoba, Haya de la Torre y Medina Allende, Ciudad Universitaria, X5000HUA C\u00f3rdoba, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rabia","family":"Sarroukh","sequence":"additional","affiliation":[{"name":"Centre for Structural Biology and Bioinformatics, Laboratory for Structure and Function of Biological Membranes, Universit\u00e9 Libre de Bruxelles, CP 206\/2, Blvd. du Triomphe, B-1050 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erik","family":"Goormaghtigh","sequence":"additional","affiliation":[{"name":"Centre for Structural Biology and Bioinformatics, Laboratory for Structure and Function of Biological Membranes, Universit\u00e9 Libre de Bruxelles, CP 206\/2, Blvd. du Triomphe, B-1050 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerardo\u00a0D.","family":"Fidelio","sequence":"additional","affiliation":[{"name":"Centro de Investigaciones en Qu\u00edmica Biol\u00f3gica de C\u00f3rdoba (CIQUIBIC, UNC-CONICET), Departamento de Qu\u00edmica Biol\u00f3gica, Facultad de Ciencias Qu\u00edmicas, Universidad Nacional de C\u00f3rdoba, Haya de la Torre y Medina Allende, Ciudad Universitaria, X5000HUA C\u00f3rdoba, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Marie","family":"Ruysschaert","sequence":"additional","affiliation":[{"name":"Centre for Structural Biology and Bioinformatics, Laboratory for Structure and Function of Biological Membranes, Universit\u00e9 Libre de Bruxelles, CP 206\/2, Blvd. du Triomphe, B-1050 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent","family":"Raussens","sequence":"additional","affiliation":[{"name":"Centre for Structural Biology and Bioinformatics, Laboratory for Structure and Function of Biological Membranes, Universit\u00e9 Libre de Bruxelles, CP 206\/2, Blvd. du Triomphe, B-1050 Brussels, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2012,4,16]]},"reference":[{"key":"2021112217291260100_B1","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. 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