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@ARTICLE{Strohker:141650,
      author       = {Strohäker, Timo and Jung, Byung Chul and Liou, Shu-Hao and
                      Fernandez, Claudio O and Riedel, Dietmar and Becker, Stefan
                      and Halliday, Glenda M and Bennati, Marina and Kim, Woojin S
                      and Lee, Seung-Jae and Zweckstetter, Markus},
      title        = {{S}tructural heterogeneity of α-synuclein fibrils
                      amplified from patient brain extracts.},
      journal      = {Nature Communications},
      volume       = {10},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2020-07974},
      pages        = {5535},
      year         = {2019},
      abstract     = {Parkinson'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.},
      keywords     = {Aged / Aged, 80 and over / Brain: metabolism / Female /
                      Humans / Male / Models, Molecular / Multiple System Atrophy:
                      diagnosis / Multiple System Atrophy: metabolism / Parkinson
                      Disease: diagnosis / Parkinson Disease: metabolism / Protein
                      Aggregation, Pathological: metabolism / Protein Conformation
                      / Synucleinopathies: diagnosis / Synucleinopathies:
                      metabolism / Tissue Extracts: metabolism / alpha-Synuclein:
                      chemistry / alpha-Synuclein: metabolism},
      cin          = {AG Zweckstetter},
      ddc          = {500},
      cid          = {I:(DE-2719)1410001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31797870},
      pmc          = {pmc:PMC6893031},
      doi          = {10.1038/s41467-019-13564-w},
      url          = {https://pub.dzne.de/record/141650},
}