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We show by a series of in vitro measurements that amyloid fibrils of \u03b1-synuclein can grow under a wide range of solution conditions but that they can multiply rapidly only under a much more select set of solution conditions, mimicking those in endosomes and other organelles. The quantitative characterization of \u03b1-synuclein aggregation described here provides new insights into the microscopic mechanisms underlying \u03b1-synuclein aggregation in the context of Parkinson disease.<\/jats:p>","DOI":"10.1073\/pnas.1315346111","type":"journal-article","created":{"date-parts":[[2014,5,10]],"date-time":"2014-05-10T02:38:18Z","timestamp":1399689498000},"page":"7671-7676","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":691,"title":["Solution conditions determine the relative importance of nucleation and growth processes in \u03b1-synuclein aggregation"],"prefix":"10.1073","volume":"111","author":[{"given":"Alexander K.","family":"Buell","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e9line","family":"Galvagnion","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ricardo","family":"Gaspar","sequence":"additional","affiliation":[{"name":"Departments of bPhysical Chemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emma","family":"Sparr","sequence":"additional","affiliation":[{"name":"Departments of bPhysical Chemistry and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michele","family":"Vendruscolo","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tuomas P. 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