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@ARTICLE{Binolfi:201340,
      author       = {Binolfi, Andrés and Rodriguez, Esaú E. and Valensin,
                      Daniela and D’Amelio, Nicola and Ippoliti, Emiliano and
                      Obal, Gonzalo and Duran, Rosario and Magistrato, Alessandra
                      and Pritsch, Otto and Zweckstetter, Markus and Valensin,
                      Gianni and Carloni, Paolo and Quintanar, Liliana and
                      Griesinger, Christian and Fernández, Claudio O.},
      title        = {{B}ioinorganic {C}hemistry of {P}arkinson’s {D}isease:
                      {S}tructural {D}eterminants for the {C}opper-{M}ediated
                      {A}myloid {F}ormation of {A}lpha-{S}ynuclein},
      journal      = {Inorganic chemistry},
      volume       = {49},
      number       = {22},
      issn         = {1520-510X},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2015-03637},
      pages        = {10668 - 10679},
      year         = {2010},
      abstract     = {The aggregation of alpha-synuclein (AS) is a critical step
                      in the etiology of Parkinson’s disease (PD). A central,
                      unresolved question in the pathophysiology of PD relates to
                      the role of AS-metal interactions in amyloid fibril
                      formation and neurodegeneration. Our previous works
                      established a hierarchy in alpha-synuclein-metal ion
                      interactions, where Cu(II) binds specifically to the protein
                      and triggers its aggregation under conditions that might be
                      relevant for the development of PD. Two independent,
                      non-interacting copper-binding sites were identified at the
                      N-terminal region of AS, with significant difference in
                      their affinities for the metal ion. In this work we have
                      solved unknown details related to the structural binding
                      specificity and aggregation enhancement mediated by Cu(II).
                      The high-resolution structural characterization of the
                      highest affinity N-terminus AS-Cu(II) complex is reported
                      here. Through the measurement of AS aggregation kinetics we
                      proved conclusively that the copper-enhanced AS amyloid
                      formation is a direct consequence of the formation of the
                      AS-Cu(II) complex at the highest affinity binding site. The
                      kinetic behavior was not influenced by the His residue at
                      position 50, arguing against an active role for this residue
                      in the structural and biological events involved in the
                      mechanism of copper-mediated AS aggregation. These new
                      findings are central to elucidate the mechanism through
                      which the metal ion participates in the fibrillization of AS
                      and represent relevantprogress in the understanding of the
                      bionorganic chemistry of PD.},
      cin          = {GRS / IAS-5},
      ddc          = {540},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000283810800058},
      doi          = {10.1021/ic1016752},
      url          = {https://juser.fz-juelich.de/record/201340},
}