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@ARTICLE{Rsener:877637,
      author       = {Rösener, Nadine and Gremer, Lothar and Wördehoff, Michael
                      M. and Kupreichyk, Tatsiana and Etzkorn, Manuel and
                      Neudecker, Philipp and Hoyer, Wolfgang},
      title        = {{C}lustering of human prion protein and α-synuclein
                      oligomers requires the prion protein {N}-terminus},
      journal      = {Communications biology},
      volume       = {3},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2020-02352},
      pages        = {365},
      year         = {2020},
      abstract     = {The interaction of prion protein (PrP) and α-synuclein
                      (αSyn) oligomers causes synaptic impairment that might
                      trigger Parkinson’s disease and other synucleinopathies.
                      Here, we report that αSyn oligomers (αSynO) cluster with
                      human PrP (huPrP) into micron-sized condensates.
                      Multivalency of αSyn within oligomers is required for
                      condensation, since clustering with huPrP is not observed
                      for monomeric αSyn. The stoichiometry of the
                      heteroassemblies is well defined with an αSyn:huPrP molar
                      ratio of about 1:1. The αSynO−huPrP interaction is of
                      high affinity, signified by slow dissociation. The huPrP
                      region responsible for condensation of αSynO, residues
                      95−111 in the intrinsically disordered N-terminus,
                      corresponds to the region required for αSynO-mediated
                      cognitive impairment. HuPrP, moreover, achieves
                      co-clustering of αSynO and Alzheimer’s disease-associated
                      amyloid-β oligomers, providing a case of a
                      cross-interaction of two amyloidogenic proteins through an
                      interlinking intrinsically disordered protein region. The
                      results suggest that αSynO-mediated condensation of huPrP
                      is involved in the pathogenesis of synucleinopathies.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32647130},
      UT           = {WOS:000552080500008},
      doi          = {10.1038/s42003-020-1085-z},
      url          = {https://juser.fz-juelich.de/record/877637},
}