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@ARTICLE{Frieg:165261,
      author       = {Frieg, Benedikt and Geraets, James A and Strohäker, Timo
                      and Dienemann, Christian and Mavroeidi, Panagiota and Jung,
                      Byung Chul and Kim, Woojin S and Lee, Seung-Jae and Xilouri,
                      Maria and Zweckstetter, Markus and Schröder, Gunnar F},
      title        = {{Q}uaternary structure of patient-homogenate amplified
                      α-synuclein fibrils modulates seeding of endogenous
                      α-synuclein.},
      journal      = {Communications biology},
      volume       = {5},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2022-01554},
      pages        = {1040},
      year         = {2022},
      note         = {CC BY: https://creativecommons.org/licenses/by/4.0/},
      abstract     = {Parkinson's disease (PD) and Multiple System Atrophy (MSA)
                      are progressive and unremitting neurological diseases that
                      are neuropathologically characterized by α-synuclein
                      inclusions. Increasing evidence supports the aggregation of
                      α-synuclein in specific brain areas early in the disease
                      course, followed by the spreading of α-synuclein pathology
                      to multiple brain regions. However, little is known about
                      how the structure of α-synuclein fibrils influence its
                      ability to seed endogenous α-synuclein in recipient cells.
                      Here, we aggregated α-synuclein by seeding with homogenates
                      of PD- and MSA-confirmed brain tissue, determined the
                      resulting α-synuclein fibril structures by cryo-electron
                      microscopy, and characterized their seeding potential in
                      mouse primary oligodendroglial cultures. The combined
                      analysis shows that the two patient material-amplified
                      α-synuclein fibrils share a similar protofilament fold but
                      differ in their inter-protofilament interface and their
                      ability to recruit endogenous α-synuclein. Our study
                      indicates that the quaternary structure of α-synuclein
                      fibrils modulates the seeding of α-synuclein pathology
                      inside recipient cells. It thus provides an important
                      advance in the quest to understand the connection between
                      the structure of α-synuclein fibrils, cellular
                      seeding/spreading, and ultimately the clinical
                      manifestations of different synucleinopathies.},
      keywords     = {alpha-Synuclein: metabolism / Animals / Cryoelectron
                      Microscopy / Mice / Multiple System Atrophy: pathology /
                      Parkinson Disease / Synucleinopathies / alpha-Synuclein:
                      chemistry / alpha-Synuclein (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {570},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36180728},
      pmc          = {pmc:PMC9525671},
      doi          = {10.1038/s42003-022-03948-y},
      url          = {https://pub.dzne.de/record/165261},
}