{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T11:05:39Z","timestamp":1791198339429,"version":"4.1.0"},"reference-count":199,"publisher":"Wiley","issue":"S1","license":[{"start":{"date-parts":[[2016,3,30]],"date-time":"2016-03-30T00:00:00Z","timestamp":1459296000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100003130","name":"Fonds Wetenschappelijk Onderzoek","doi-asserted-by":"publisher","award":["G.0927.14"],"award-info":[{"award-number":["G.0927.14"]}],"id":[{"id":"10.13039\/501100003130","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[2016,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:label\/><jats:p>Several decades ago, a mysterious transmissible agent was found responsible for a group of progressive and lethal encephalopathies affecting the nervous system of both animals and humans. This infectious agent showed a strain\u2010encoded manner of inheritance even though it lacked nucleic acids. The identification of infectious proteins resolved this apparent conundrum. Misfolded infectious protein particles, or prions, were found to exist as conformational isomers with a unique fingerprint that can be faithfully passaged to next generations. Protein\u2010based strain\u2010encoded inheritance is characterized by strain\u2010specific infectivity and symptomatology. It is found in diverse organisms, such as yeast, fungi, and mammals. Now, this concept is revisited to examine the pathological role of amyloid proteins involved in neurodegenerative diseases where it might underlie certain types of dementia and motor\u2010related neurodegenerative disorders. Given the discovery of the <jats:italic>SNCA<\/jats:italic> gene and the identification of its gene product, \u0251\u2010synuclein (\u0251\u2010SYN), as the main histopathological component of Parkinson's disease, dementia with Lewy bodies and multiple system atrophy, the scientific community was left puzzled by the fact that a single protein appeared to be involved in different diseases with diverging clinical phenotypes. Recent studies are now indicating that \u0251\u2010SYN may act in a way similar to prions and that \u0251\u2010SYN misfolded structural variants may behave as strains with distinct biochemical and functional properties inducing specific phenotypic traits, which might finally provide an explanation for the clinical heterogeneity observed between Parkinson's disease, MSA, and dementia with Lewy bodies patients. These crucial new findings may pave the way for unexplored therapeutic avenues and identification of new potential biomarkers.<\/jats:p><\/jats:sec><jats:sec><jats:label\/><jats:p>\n<jats:boxed-text content-type=\"graphic\" position=\"anchor\"><jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc13595-fig-0004-m.png\"><jats:alt-text>image<\/jats:alt-text><\/jats:graphic><\/jats:boxed-text>Parkinson's disease and other synucleinopathies share \u0251\u2010synuclein deposits as a common histopathological hallmark. New and ongoing developments are now showing that variations in the aggregation process and the formation of \u0251\u2010synuclein strains may be paralleled by the development of distinct synucleinopathies. Here, we review the recent developments and the role of strains in synucleinopathies.<\/jats:p><jats:p><jats:bold>This article is part of a <\/jats:bold><jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/onlinelibrary.wiley.com\/journal\/10.1111\/(ISSN)1471-4159\/homepage\/special_issues.htm\">special issue on Parkinson disease<\/jats:ext-link><jats:bold>.<\/jats:bold><\/jats:p><\/jats:sec>","DOI":"10.1111\/jnc.13595","type":"journal-article","created":{"date-parts":[[2016,2,29]],"date-time":"2016-02-29T11:59:36Z","timestamp":1456747176000},"page":"256-274","source":"Crossref","is-referenced-by-count":86,"title":["\u0251\u2010Synuclein strains and the variable pathologies of synucleinopathies"],"prefix":"10.1111","volume":"139","author":[{"given":"Wouter","family":"Peelaerts","sequence":"first","affiliation":[{"name":"Laboratory for Neurobiology and Gene Therapy Department of Neurosciences KU Leuven Leuven Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Veerle","family":"Baekelandt","sequence":"additional","affiliation":[{"name":"Laboratory for Neurobiology and Gene Therapy Department of Neurosciences KU Leuven Leuven Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2016,3,30]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.3389\/fnagi.2014.00248"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrm2204"},{"key":"e_1_2_11_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/glia.22653"},{"key":"e_1_2_11_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1067389"},{"key":"e_1_2_11_6_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1001317.s008"},{"key":"e_1_2_11_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja2017703"},{"key":"e_1_2_11_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.exger.2006.05.019"},{"key":"e_1_2_11_9_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1318306111"},{"key":"e_1_2_11_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.neuron.2013.09.004"},{"key":"e_1_2_11_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/mds.25844"},{"key":"e_1_2_11_12_1","doi-asserted-by":"crossref","first-page":"2096","DOI":"10.1128\/jvi.66.4.2096-2101.1992","article-title":"Biochemical and physical\u2010properties of the prion protein from 2 strains of the transmissible mink encephalopathy agent","volume":"66","author":"Bessen R. 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