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@ARTICLE{Frieg:912257,
      author       = {Frieg, Benedikt and Antonschmidt, Leif and Dienemann,
                      Christian and Geraets, James A. and Najbauer, Eszter E. and
                      Matthes, Dirk and de Groot, Bert L. and Andreas, Loren B.
                      and Becker, Stefan and Griesinger, Christian and Schröder,
                      Gunnar F.},
      title        = {{T}he 3{D} structure of lipidic fibrils of α-synuclein},
      journal      = {Nature Communications},
      volume       = {13},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2022-05454},
      pages        = {6810},
      year         = {2022},
      abstract     = {α-synuclein misfolding and aggregation into fibrils is a
                      common feature of α-synucleinopathies, such as
                      Parkinson’s disease, in which α-synuclein fibrils are a
                      characteristic hallmark of neuronal inclusions called Lewy
                      bodies. Studies on the composition of Lewy bodies extracted
                      postmortem from brain tissue of Parkinson’s patients
                      revealed that lipids and membranous organelles are also a
                      significant component. Interactions between α-synuclein and
                      lipids have been previously identified as relevant for
                      Parkinson’s disease pathology, however molecular insights
                      into their interactions have remained elusive. Here we
                      present cryo-electron microscopy structures of six
                      α-synuclein fibrils in complex with lipids, revealing
                      specific lipid-fibril interactions. We observe that
                      phospholipids promote an alternative protofilament fold,
                      mediate an unusual arrangement of protofilaments, and fill
                      the central cavities of the fibrils. Together with our
                      previous studies, these structures also indicate a mechanism
                      for fibril-induced lipid extraction, which is likely to be
                      involved in the development of α-synucleinopathies.
                      Specifically, one potential mechanism for the cellular
                      toxicity is the disruption of intracellular vesicles
                      mediated by fibrils and oligomers, and therefore the
                      modulation of these interactions may provide a promising
                      strategy for future therapeutic interventions.},
      cin          = {IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36357403},
      UT           = {WOS:000881814200030},
      doi          = {10.1038/s41467-022-34552-7},
      url          = {https://juser.fz-juelich.de/record/912257},
}