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Sci."},{"key":"10.1016\/j.ymeth.2010.12.008_b0465","doi-asserted-by":"crossref","first-page":"2720","DOI":"10.1021\/bi027166s","article-title":"Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes","volume":"42","author":"Munishkina","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.ymeth.2010.12.008_b0470","doi-asserted-by":"crossref","unstructured":"V. L. Anderson, T. F. Ramlall, C. C. Rospigliosi, W. W. Webb, D. Eliezer, Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation, Proc. Natl. Acad. Sci. USA. Oct 14 (2010) (Epub).","DOI":"10.1073\/pnas.1012336107"},{"key":"10.1016\/j.ymeth.2010.12.008_b0475","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.jmb.2004.06.089","article-title":"Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin","volume":"342","author":"Pallares","year":"2004","journal-title":"J. Mol. 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