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A plethora of reports suggest that distinct diseases have in common the ability of protein aggregates to spread and amplify within the central nervous system. This review summarizes briefly what is known about the nature of the protein aggregates that are infectious and the reason they are toxic to cells. The chameleon property of polypeptides which aggregation into distinct high-molecular weight assemblies is associated to different diseases, in particular, that of alpha-synuclein which aggregation is the hallmark of distinct synucleinopathies, is discussed. Finally, strategies targeting the formation and propagation of structurally distinct alpha-synuclein assemblies associated to different synucleinopathies are presented and their therapeutic and diagnostic potential is discussed.<\/jats:p>","DOI":"10.3233\/jpd-150543","type":"journal-article","created":{"date-parts":[[2015,6,2]],"date-time":"2015-06-02T17:46:21Z","timestamp":1433267181000},"page":"217-227","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":129,"title":["Role of Different Alpha-Synuclein Strains in Synucleinopathies, Similarities with other Neurodegenerative Diseases"],"prefix":"10.1177","volume":"5","author":[{"given":"Ronald","family":"Melki","sequence":"first","affiliation":[{"name":"Paris-Saclay Institute of Neuroscience, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2015,6,1]]},"reference":[{"key":"r1","doi-asserted-by":"publisher","DOI":"10.1038\/nature10317"},{"key":"r2","doi-asserted-by":"publisher","DOI":"10.1126\/science.181.4096.223"},{"key":"r3","doi-asserted-by":"publisher","DOI":"10.1038\/nsb0197-10"},{"key":"r4","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.physchem.48.1.545"},{"key":"r5","doi-asserted-by":"publisher","DOI":"10.1101\/sqb.2012.76.010637"},{"key":"r6","doi-asserted-by":"publisher","DOI":"10.1126\/science.1141448"},{"key":"r7","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-biochem-060809-095203"},{"key":"r8","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.R500010200"},{"key":"r9","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.1001998"},{"key":"r10","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2013.06.031"},{"key":"r11","doi-asserted-by":"publisher","DOI":"10.1016\/j.ceb.2010.10.001"},{"key":"r12","doi-asserted-by":"crossref","unstructured":"Ross CA, Poirier  MA 2014 Protein aggregation and neurodegenerative disease. 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