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000141650 1001_ $$0P:(DE-2719)2812850$$aStrohäker, Timo$$b0$$eFirst author
000141650 245__ $$aStructural heterogeneity of α-synuclein fibrils amplified from patient brain extracts.
000141650 260__ $$a[London]$$bNature Publishing Group UK$$c2019
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000141650 520__ $$aParkinson's disease (PD) and Multiple System Atrophy (MSA) are clinically distinctive diseases that feature a common neuropathological hallmark of aggregated α-synuclein. Little is known about how differences in α-synuclein aggregate structure affect disease phenotype. Here, we amplified α-synuclein aggregates from PD and MSA brain extracts and analyzed the conformational properties using fluorescent probes, NMR spectroscopy and electron paramagnetic resonance. We also generated and analyzed several in vitro α-synuclein polymorphs. We found that brain-derived α-synuclein fibrils were structurally different to all of the in vitro polymorphs analyzed. Importantly, there was a greater structural heterogeneity among α-synuclein fibrils from the PD brain compared to those from the MSA brain, possibly reflecting on the greater variability of disease phenotypes evident in PD. Our findings have significant ramifications for the use of non-brain-derived α-synuclein fibrils in PD and MSA studies, and raise important questions regarding the one disease-one strain hypothesis in the study of α-synucleinopathies.
000141650 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000141650 542__ $$2Crossref$$i2019-12-01$$uhttps://creativecommons.org/licenses/by/4.0
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000141650 650_2 $$2MeSH$$aAged
000141650 650_2 $$2MeSH$$aAged, 80 and over
000141650 650_2 $$2MeSH$$aBrain: metabolism
000141650 650_2 $$2MeSH$$aFemale
000141650 650_2 $$2MeSH$$aHumans
000141650 650_2 $$2MeSH$$aMale
000141650 650_2 $$2MeSH$$aModels, Molecular
000141650 650_2 $$2MeSH$$aMultiple System Atrophy: diagnosis
000141650 650_2 $$2MeSH$$aMultiple System Atrophy: metabolism
000141650 650_2 $$2MeSH$$aParkinson Disease: diagnosis
000141650 650_2 $$2MeSH$$aParkinson Disease: metabolism
000141650 650_2 $$2MeSH$$aProtein Aggregation, Pathological: metabolism
000141650 650_2 $$2MeSH$$aProtein Conformation
000141650 650_2 $$2MeSH$$aSynucleinopathies: diagnosis
000141650 650_2 $$2MeSH$$aSynucleinopathies: metabolism
000141650 650_2 $$2MeSH$$aTissue Extracts: metabolism
000141650 650_2 $$2MeSH$$aalpha-Synuclein: chemistry
000141650 650_2 $$2MeSH$$aalpha-Synuclein: metabolism
000141650 7001_ $$aJung, Byung Chul$$b1
000141650 7001_ $$aLiou, Shu-Hao$$b2
000141650 7001_ $$aFernandez, Claudio O$$b3
000141650 7001_ $$aRiedel, Dietmar$$b4
000141650 7001_ $$aBecker, Stefan$$b5
000141650 7001_ $$aHalliday, Glenda M$$b6
000141650 7001_ $$aBennati, Marina$$b7
000141650 7001_ $$aKim, Woojin S$$b8
000141650 7001_ $$aLee, Seung-Jae$$b9
000141650 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b10$$eLast author
000141650 77318 $$2Crossref$$3journal-article$$a10.1038/s41467-019-13564-w$$b : Springer Science and Business Media LLC, 2019-12-01$$n1$$p5535$$tNature Communications$$v10$$x2041-1723$$y2019
000141650 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-019-13564-w$$gVol. 10, no. 1, p. 5535$$n1$$p5535$$q10:1<5535$$tNature Communications$$v10$$x2041-1723$$y2019
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