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@ARTICLE{Karpinar:163870,
      author       = {Karpinar, Damla Pinar and Balija, Madhu Babu Gajula and
                      Kügler, Sebastian and Opazo, Felipe and Rezaei-Ghaleh,
                      Nasrollah and Wender, Nora and Kim, Hai-Young and
                      Taschenberger, Grit and Falkenburger, Björn H and Heise,
                      Henrike and Kumar, Ashutosh and Riedel, Dietmar and
                      Fichtner, Lars and Voigt, Aaron and Braus, Gerhard H and
                      Giller, Karin and Becker, Stefan and Herzig, Alf and Baldus,
                      Marc and Jäckle, Herbert and Eimer, Stefan and Schulz,
                      Jörg B and Griesinger, Christian and Zweckstetter, Markus},
      title        = {{P}re-fibrillar alpha-synuclein variants with impaired
                      beta-structure increase neurotoxicity in {P}arkinson's
                      disease models.},
      journal      = {The EMBO journal},
      volume       = {28},
      number       = {20},
      issn         = {0261-4189},
      address      = {Hoboken, NJ [u.a.]},
      publisher    = {Wiley},
      reportid     = {DZNE-2022-00557},
      pages        = {3256 - 3268},
      year         = {2009},
      abstract     = {The relation of alpha-synuclein (alphaS) aggregation to
                      Parkinson's disease (PD) has long been recognized, but the
                      mechanism of toxicity, the pathogenic species and its
                      molecular properties are yet to be identified. To obtain
                      insight into the function different aggregated alphaS
                      species have in neurotoxicity in vivo, we generated alphaS
                      variants by a structure-based rational design. Biophysical
                      analysis revealed that the alphaS mutants have a reduced
                      fibrillization propensity, but form increased amounts of
                      soluble oligomers. To assess their biological response in
                      vivo, we studied the effects of the biophysically defined
                      pre-fibrillar alphaS mutants after expression in tissue
                      culture cells, in mammalian neurons and in PD model
                      organisms, such as Caenorhabditis elegans and Drosophila
                      melanogaster. The results show a striking correlation
                      between alphaS aggregates with impaired beta-structure,
                      neuronal toxicity and behavioural defects, and they
                      establish a tight link between the biophysical properties of
                      multimeric alphaS species and their in vivo function.},
      keywords     = {Animals / Animals, Genetically Modified / Brain: metabolism
                      / Brain: pathology / Caenorhabditis elegans: metabolism /
                      Cell Line / Disease Models, Animal / Drosophila: metabolism
                      / Humans / Magnetic Resonance Spectroscopy / Neurons:
                      metabolism / Neurons: pathology / Parkinson Disease:
                      metabolism / Parkinson Disease: pathology / Protein
                      Multimerization / Protein Structure, Secondary / Rats /
                      alpha-Synuclein: chemistry / alpha-Synuclein: genetics /
                      alpha-Synuclein: metabolism / alpha-Synuclein (NLM
                      Chemicals)},
      ddc          = {570},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19745811},
      pmc          = {pmc:PMC2771093},
      doi          = {10.1038/emboj.2009.257},
      url          = {https://pub.dzne.de/record/163870},
}