{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T12:37:37Z","timestamp":1788871057673,"version":"build-2803163510"},"reference-count":31,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2014,8,1]],"date-time":"2014-08-01T00:00:00Z","timestamp":1406851200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["5P20RR016476-11"],"award-info":[{"award-number":["5P20RR016476-11"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["8P20GM103476-11"],"award-info":[{"award-number":["8P20GM103476-11"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["OISE-1132079"],"award-info":[{"award-number":["OISE-1132079"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"name":"US Department of Education","award":["P200A090066"],"award-info":[{"award-number":["P200A090066"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2014,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Amyloid aggregates of \u03b1\u2010synuclein (\u03b1S) protein are the predominant species present within the intracellular inclusions called Lewy bodies in Parkinson's disease (PD) patients. Among various aggregates, the low\u2010molecular weight ones broadly ranging between 2 and 30 mers are known to be the primary neurotoxic agents responsible for the impairment of neuronal function. Recent research has indicated that the neurotransmitter dopamine (DA) is one of the key physiological agents promoting and augmenting \u03b1S aggregation, which is thought to be a significant event in PD pathologenesis. Specifically, DA is known to induce the formation of soluble oligomers of \u03b1S, which in turn are responsible for inducing several important cellular changes leading to cellular toxicity. In this report, we present the generation, isolation, and biophysical characterization of five different dopamine\u2010derived \u03b1S oligomers (DSOs) ranging between 3 and 15 mers, corroborating previously published reports. More importantly, we establish that these DSOs are also capable of replication by self\u2010propagation, which leads to the replication of DSOs upon interaction with \u03b1S monomers, a process similar to that observed in mammilian prions. In addition, DSOs are also able to cross\u2010propagate amyloid\u2010\u03b2 (A\u03b2) aggregates involved in Alzheimer's disease (AD). Interestingly, while self\u2010propagation of DSOs occur with no net gain in protein structure, cross\u2010propagation proceeds with an overall gain in \u03b2\u2010sheet conformation. These results implicate the involvement of DSOs in the progression of PD, and, in part, provide a molecular basis for the observed co\u2010existence of AD\u2010like pathology among PD patients.<\/jats:p>","DOI":"10.1002\/pro.2521","type":"journal-article","created":{"date-parts":[[2014,7,16]],"date-time":"2014-07-16T07:13:32Z","timestamp":1405494812000},"page":"1369-1379","source":"Crossref","is-referenced-by-count":35,"title":["Dopamine\u2010induced \u03b1\u2010synuclein oligomers show self\u2010 and cross\u2010propagation properties"],"prefix":"10.1002","volume":"23","author":[{"given":"Matthew S.","family":"Planchard","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry University of Southern Mississippi Hattiesburg Mississippi 39406"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah E.","family":"Exley","sequence":"additional","affiliation":[{"name":"School of Polymers and High Performance Materials University of Southern Mississippi Hattiesburg Mississippi 39406"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah E.","family":"Morgan","sequence":"additional","affiliation":[{"name":"School of Polymers and High Performance Materials University of Southern Mississippi Hattiesburg Mississippi 39406"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vijayaraghavan","family":"Rangachari","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry University of Southern Mississippi Hattiesburg Mississippi 39406"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2014,8]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/ana.23746"},{"issue":"1","key":"e_1_2_6_3_1","first-page":"S67","article-title":"Molecular mechanisms of amyloid oligomers toxicity","volume":"33","author":"Kayed R","year":"2013","journal-title":"J Alzheimers 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