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000151598 0247_ $$2doi$$a10.1016/j.ijbiomac.2020.03.238
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000151598 037__ $$aDZNE-2020-01182
000151598 041__ $$aEnglish
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000151598 1001_ $$0P:(DE-2719)9000203$$aTayaranian Marvian, Amir$$b0$$eFirst author$$udzne
000151598 245__ $$aThe status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization
000151598 260__ $$aNew York, NY [u.a.]$$bElsevier$$c2020
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000151598 520__ $$aThe α-synuclein (αSN) amyloid fibrillization process is known to be a crucial phenomenon associated with neuronal loss in various neurodegenerative diseases, most famously Parkinson's disease. The process involves different aggregated species and ultimately leads to formation of β-sheet rich fibrillar structures. Despite the essential role of αSN aggregation in the pathoetiology of various neurological disorders, the characteristics of various assemblies are not fully understood. Here, we established a fluorescence-based model for studying the end-parts of αSN to decipher the structural aspects of aggregates during the fibrillization. Our model proved highly sensitive to the events at the early stage of the fibrillization process, which are hardly detectable with routine techniques. Combining fluorescent and PAGE analysis, we found different oligomeric aggregates in the nucleation phase of fibrillization with different sensitivity to SDS and different structures based on αSN termini. Moreover, we found that these oligomers are highly dynamic: after reaching peak levels during fibrillization, they decline and eventually disappear, suggesting their transformation into other αSN aggregated species. These findings shed light on the structural features of various αSN aggregates and their dynamics in synucleinopathies.
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000151598 542__ $$2Crossref$$i2020-07-01$$uhttps://www.elsevier.com/tdm/userlicense/1.0/
000151598 542__ $$2Crossref$$i2020-04-11$$uhttp://creativecommons.org/licenses/by/4.0/
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000151598 650_2 $$2MeSH$$aAmyloid: chemistry
000151598 650_2 $$2MeSH$$aHumans
000151598 650_2 $$2MeSH$$aMutant Proteins: chemistry
000151598 650_2 $$2MeSH$$aMutant Proteins: genetics
000151598 650_2 $$2MeSH$$aMutant Proteins: metabolism
000151598 650_2 $$2MeSH$$aMutation
000151598 650_2 $$2MeSH$$aProtein Interaction Domains and Motifs
000151598 650_2 $$2MeSH$$aProtein Multimerization
000151598 650_2 $$2MeSH$$aalpha-Synuclein: chemistry
000151598 650_2 $$2MeSH$$aalpha-Synuclein: genetics
000151598 650_2 $$2MeSH$$aalpha-Synuclein: metabolism
000151598 7001_ $$aAliakbari, Farhang$$b1
000151598 7001_ $$aMohammad-Beigi, Hossein$$b2
000151598 7001_ $$aAhmadi, Zeinab Alsadat$$b3
000151598 7001_ $$aMehrpooyan, Sina$$b4
000151598 7001_ $$aLermyte, Frederik$$b5
000151598 7001_ $$aNasouti, Mahour$$b6
000151598 7001_ $$aCollingwood, Joanna F.$$b7
000151598 7001_ $$aOtzen, Daniel E.$$b8
000151598 7001_ $$0P:(DE-HGF)0$$aMorshedi, Dina$$b9$$eCorresponding author
000151598 77318 $$2Crossref$$3journal-article$$a10.1016/j.ijbiomac.2020.03.238$$b : Elsevier BV, 2020-07-01$$p543-550$$tInternational Journal of Biological Macromolecules$$v155$$x0141-8130$$y2020
000151598 773__ $$0PERI:(DE-600)1483284-7$$a10.1016/j.ijbiomac.2020.03.238$$gVol. 155, p. 543 - 550$$p543-550$$tInternational journal of biological macromolecules$$v155$$x0141-8130$$y2020
000151598 8564_ $$uhttps://www.sciencedirect.com/science/article/pii/S0141813020328257
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