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@ARTICLE{VillarPiqu:830503,
      author       = {Villar-Piqué, Anna and Rossetti, Giulia and Ventura,
                      Salvador and Carloni, Paolo and Fernández, Claudio O. and
                      Outeiro, Tiago Fleming},
      title        = {{C}opper({II}) and the pathological {H}50{Q} α-synuclein
                      mutant: {E}nvironment meets genetics},
      journal      = {Communicative $\&$ integrative biology},
      volume       = {10},
      number       = {1},
      issn         = {1942-0889},
      address      = {Austin, Tex.},
      publisher    = {Landes Bioscience},
      reportid     = {FZJ-2017-04044},
      pages        = {e1270484 -},
      year         = {2017},
      abstract     = {Copper is one of the metals described to bind the Parkinson
                      disease-related protein α-synuclein (aSyn), and to promote
                      its aggregation. Although histidine at position 50 in the
                      aSyn sequence is one of the most studied copper-anchoring
                      sites, its precise role in copper binding and aSyn
                      aggregation is still unclear. Previous studies suggested
                      that this residue does not significantly affect
                      copper-mediated aSyn aggregation. However, our findings
                      showed that the aggregation of the pathological H50Q aSyn
                      mutant is enhanced by copper hints otherwise. Despite the
                      inexistence of a model for aSyn H50Q-copper complexation, we
                      discuss possible mechanisms by which this metal contributes
                      to the misfolding and self-assembly of this particular aSyn
                      mutant. Considering the genetic association of the H50Q
                      mutation with familial forms of Parkinson disease, and the
                      fact that copper homeostasis is deregulated in this
                      disorder, understanding the interplay between both factors
                      will shed light into the molecular and cellular mechanisms
                      triggering the development and spreading of the aSyn
                      pathology.},
      cin          = {IAS-5 / INM-9 / JSC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {572 - (Dys-)function and Plasticity (POF3-572) / 511 -
                      Computational Science and Mathematical Methods (POF3-511)},
      pid          = {G:(DE-HGF)POF3-572 / G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28289488},
      doi          = {10.1080/19420889.2016.1270484},
      url          = {https://juser.fz-juelich.de/record/830503},
}