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In this paper, we describe how sequence differences between\n                    <jats:italic>\u03b1<\/jats:italic>\n                    - and\n                    <jats:italic>\u03b2<\/jats:italic>\n                    -synuclein affect individual microscopic processes in amyloid formation. In particular, we show that\n                    <jats:italic>\u03b2<\/jats:italic>\n                    -synuclein strongly suppresses both lipid-induced aggregation and secondary nucleation of\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -synuclein by competing for binding sites at the surfaces of lipid vesicles and fibrils, respectively. These results suggest that\n                    <jats:italic>\u03b2<\/jats:italic>\n                    -synuclein can act as a natural inhibitor of\n                    <jats:italic>\u03b1<\/jats:italic>\n                    -synuclein aggregation by reducing both the initiation of its self-assembly and the proliferation of its aggregates.\n                  <\/jats:p>","DOI":"10.1038\/srep36010","type":"journal-article","created":{"date-parts":[[2016,11,3]],"date-time":"2016-11-03T06:22:24Z","timestamp":1478154144000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":88,"title":["\u03b2-Synuclein suppresses both the initiation and amplification steps of \u03b1-synuclein aggregation via competitive binding to surfaces"],"prefix":"10.1038","volume":"6","author":[{"given":"James W. 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