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@ARTICLE{Shaykhalishahi:279291,
      author       = {Shaykhalishahi, Hamed and Gauhar, Aziz and Wördehoff,
                      Michael M. and Grüning, Clara S. R. and Klein, Antonia N.
                      and Bannach, Oliver and Stoldt, Matthias and Willbold,
                      Dieter and Härd, Torleif and Hoyer, Wolfgang},
      title        = {{C}ontact between the β1 and β2 {S}egments of
                      α-{S}ynuclein that {I}nhibits {A}myloid {F}ormation},
      journal      = {Angewandte Chemie / International edition},
      volume       = {54},
      number       = {30},
      issn         = {1433-7851},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2015-07306},
      pages        = {8837 - 8840},
      year         = {2015},
      abstract     = {Conversion of the intrinsically disordered protein
                      α-synuclein (α-syn) into amyloid aggregates is a key
                      process in Parkinson’s disease. The sequence region
                      35–59 contains β-strand segments β1 and β2 of α-syn
                      amyloid fibril models and most disease-related mutations.
                      β1 and β2 frequently engage in transient interactions in
                      monomeric α-syn. The consequences of β1–β2 contacts are
                      evaluated by disulfide engineering, biophysical techniques,
                      and cell viability assays. The double-cysteine mutant
                      α-synCC, with a disulfide linking β1 and β2, is
                      aggregation-incompetent and inhibits aggregation and
                      toxicity of wild-type α-syn. We show that α-syn delays the
                      aggregation of amyloid-β peptide and islet amyloid
                      polypeptide involved in Alzheimer’s disease and type 2
                      diabetes, an effect enhanced in the α-synCC mutant.
                      Tertiary interactions in the β1–β2 region of α-syn
                      interfere with the nucleation of amyloid formation,
                      suggesting promotion of such interactions as a potential
                      therapeutic approach.},
      cin          = {ICS-6},
      ddc          = {540},
      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},
      UT           = {WOS:000358051600050},
      pubmed       = {pmid:26119103},
      doi          = {10.1002/anie.201503018},
      url          = {https://juser.fz-juelich.de/record/279291},
}