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@ARTICLE{Agerschou:862747,
      author       = {Agerschou, Emil D. and Saridaki, Theodora and Flagmeier,
                      Patrick and Galvagnion, Céline and Komnig, Daniel and
                      Nagpal, Akansha and Gasterich, Natalie and Heid, Laetitia
                      and Prasad, Vibha and Shaykhalishahi, Hamed and Voigt, Aaron
                      and Willbold, Dieter and Dobson, Christopher M. and
                      Falkenburger, Björn H. 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     = {FZJ-2019-02989},
      pages        = {e46112},
      year         = {2019},
      abstract     = {Removing or preventing the formation of α-synuclein
                      aggregates is a plausible strategy against Parkinson’s
                      disease. To this end we have engineered the β-wrapin AS69
                      to bind monomeric α-synuclein with high affinity. In
                      cultured cells, AS69 reduced the occurrence of α-synuclein
                      oligomers and of visible α-synuclein aggregates. In flies,
                      AS69 reduced α-synuclein aggregates and the locomotor
                      deficit resulting from α-synuclein expression in neuronal
                      cells. In a mouse model based on the intracerebral injection
                      of pre-formed α-synuclein seed fibrills (PFFs), AS69
                      co-injection reduced the density of dystrophic neurites
                      observed three months later. In biophysical experiments in
                      vitro, AS69 highly sub-stoichiometrically inhibited
                      auto-catalytic secondary nucleation processes, even in the
                      presence of a large excess of monomer. We present evidence
                      that the AS69-α-synuclein complex, rather than the free
                      AS69, is the inhibitory species responsible for
                      sub-stoichiometric inhibition. These results represent a new
                      paradigm that high affinity monomer binders can be strongly
                      sub-stoichiometric inhibitors of nucleation processes.},
      cin          = {ICS-6},
      ddc          = {600},
      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:31389332},
      UT           = {WOS:000484182000001},
      doi          = {10.7554/eLife.46112},
      url          = {https://juser.fz-juelich.de/record/862747},
}