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@ARTICLE{Agerschou:140939,
      author       = {Agerschou, Emil Dandanell and Flagmeier, Patrick and
                      Saridaki, Theodora and Galvagnion, Céline and Komnig,
                      Daniel and Heid, Laetitia and Prasad, Vibha and
                      Shaykhalishahi, Hamed and Willbold, Dieter and Dobson,
                      Christopher M and Voigt, Aaron and Falkenburger, Bjoern and
                      Hoyer, Wolfgang and Buell, Alexander K},
      title        = {{A}n engineered monomer binding-protein for α-synuclein
                      efficiently inhibits the proliferation of amyloid fibrils.},
      journal      = {eLife},
      volume       = {8},
      issn         = {2050-084X},
      address      = {Cambridge},
      publisher    = {eLife Sciences Publications},
      reportid     = {DZNE-2020-07261},
      pages        = {e46112},
      year         = {2019},
      abstract     = {Removing or preventing the formation of [Formula: see
                      text]-synuclein aggregates is a plausible strategy against
                      Parkinson's disease. To this end, we have engineered the
                      [Formula: see text]-wrapin AS69 to bind monomeric [Formula:
                      see text]-synuclein with high affinity. In cultured cells,
                      AS69 reduced the self-interaction of [Formula: see
                      text]-synuclein and formation of visible [Formula: see
                      text]-synuclein aggregates. In flies, AS69 reduced [Formula:
                      see text]-synuclein aggregates and the locomotor deficit
                      resulting from [Formula: see text]-synuclein expression in
                      neuronal cells. In biophysical experiments in vitro, AS69
                      highly sub-stoichiometrically inhibited both primary and
                      autocatalytic secondary nucleation processes, even in the
                      presence of a large excess of monomer. We present evidence
                      that the AS69-[Formula: see text]-synuclein complex, rather
                      than the free AS69, is the inhibitory species responsible
                      for sub-stoichiometric inhibition of secondary nucleation.
                      These results represent a new paradigm that high affinity
                      monomer binders can lead to strongly sub-stoichiometric
                      inhibition of nucleation processes.},
      keywords     = {Amyloid: antagonists $\&$ inhibitors / HEK293 Cells /
                      Humans / Protein Aggregation, Pathological / Protein
                      Multimerization: drug effects / Recombinant Proteins:
                      genetics / Recombinant Proteins: metabolism /
                      alpha-Synuclein: metabolism},
      cin          = {AG Di Monte},
      ddc          = {600},
      cid          = {I:(DE-2719)1013008},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31389332},
      pmc          = {pmc:PMC6721797},
      doi          = {10.7554/eLife.46112},
      url          = {https://pub.dzne.de/record/140939},
}