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@ARTICLE{Falke:862752,
      author       = {Falke, Marcel and Victor, Julian and Wördehoff, Michael M.
                      and Peduzzo, Alessia and Zhang, Tao and Schröder, Gunnar F.
                      and Buell, Alexander K. and Hoyer, Wolfgang and Etzkorn,
                      Manuel},
      title        = {α-{S}ynuclein-derived lipoparticles in the study of
                      α-{S}ynuclein amyloid fibril formation},
      journal      = {Chemistry and physics of lipids},
      volume       = {220},
      issn         = {0009-3084},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2019-02994},
      pages        = {57 - 65},
      year         = {2019},
      abstract     = {Aggregation of the protein α-Synuclein (αSyn) is of great
                      interest due to its involvement in the pathology of
                      Parkinson’s disease. However, under in vitro conditions
                      αSyn is very soluble and kinetically stable for extended
                      time periods. As a result, most αSyn aggregation assays
                      rely on conditions that artificially induce or enhance
                      aggregation, often by introducing rather non-native
                      conditions. It has been shown that αSyn interacts with
                      membranes and conditions have been identified in which
                      membranes can promote as well as inhibit αSyn aggregation.
                      It has also been shown that αSyn has the intrinsic
                      capability to assemble lipid-protein-particles, in a similar
                      way as apolipoproteins can form lipid-bilayer nanodiscs.
                      Here we show that these αSyn-lipid particles (αSyn-LiPs)
                      can also effectively induce, accelerate or inhibit αSyn
                      aggregation, depending on the applied conditions. αSyn-LiPs
                      therefore provide a general platform and additional tool,
                      complementary to other setups, to study various aspects of
                      αSyn amyloid fibril formation.},
      cin          = {ICS-6},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30826264},
      UT           = {WOS:000464480000008},
      doi          = {10.1016/j.chemphyslip.2019.02.009},
      url          = {https://juser.fz-juelich.de/record/862752},
}