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@ARTICLE{Viennet:856614,
      author       = {Viennet, Thibault and Wördehoff, Michael M. and Uluca,
                      Boran and Poojari, Chetan and Shaykhalishahi, Hamed and
                      Willbold, Dieter and Strodel, Birgit and Heise, Henrike and
                      Buell, Alexander K. and Hoyer, Wolfgang and Etzkorn, Manuel},
      title        = {{S}tructural insights from lipid-bilayer nanodiscs link
                      α-{S}ynuclein membrane-binding modes to amyloid fibril
                      formation},
      journal      = {Communications biology},
      volume       = {1},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2018-05981},
      pages        = {44},
      year         = {2018},
      abstract     = {The protein α-Synuclein (αS) is linked to Parkinson’s
                      disease through its abnormal aggregation, which is thought
                      to involve cytosolic and membrane-bound forms of αS.
                      Following previous studies using micelles and vesicles, we
                      present a comprehensive study of αS interaction with
                      phospholipid bilayer nanodiscs. Using a combination of
                      NMR-spectroscopic, biophysical, and computational methods,
                      we structurally and kinetically characterize αS interaction
                      with different membrane discs in a quantitative and
                      site-resolved way. We obtain global and residue-specific αS
                      membrane affinities, and determine modulations of αS
                      membrane binding due to αS acetylation, membrane
                      plasticity, lipid charge density, and accessible membrane
                      surface area, as well as the consequences of the different
                      binding modes for αS amyloid fibril formation. Our results
                      establish a structural and kinetic link between the observed
                      dissimilar binding modes and either aggregation-inhibiting
                      properties, largely unperturbed aggregation, or accelerated
                      aggregation due to membrane-assisted fibril nucleation.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30271927},
      UT           = {WOS:000461126500044},
      doi          = {10.1038/s42003-018-0049-z},
      url          = {https://juser.fz-juelich.de/record/856614},
}