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@ARTICLE{Wolff:279294,
      author       = {Wolff, Martin and Unuchek, Dmitry and Zhang, Bo and
                      Gordeliy, Valentin and Willbold, Dieter and Nagel-Steger,
                      Luitgard},
      title        = {{A}myloid β {O}ligomeric {S}pecies {P}resent in the {L}ag
                      {P}hase of {A}myloid {F}ormation},
      journal      = {PLoS one},
      volume       = {10},
      number       = {5},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2015-07309},
      pages        = {e0127865},
      year         = {2015},
      abstract     = {Alzheimer’s disease (AD)-associated amyloid β peptide
                      (Aβ) is one of the main actors in AD pathogenesis. Aβ is
                      characterized by its high tendency to self-associate,
                      leading to the generation of oligomers and amyloid fibrils.
                      The elucidation of pathways and intermediates is crucial for
                      the understanding of protein assembly mechanisms in general
                      and in conjunction with neurodegenerative diseases, e.g.,
                      for the identification of new therapeutic targets. Our study
                      focused on Aβ42 and its oligomeric assemblies in the lag
                      phase of amyloid formation, as studied by sedimentation
                      velocity (SV) centrifugation. The assembly state of Aβ
                      during the lag phase, the time required by an Aβ solution
                      to reach the exponential growth phase of aggregation, was
                      characterized by a dominant monomer fraction below 1 S and a
                      population of oligomeric species between 4 and 16 S. From
                      the oligomer population, two major species close to a 12-mer
                      and an 18-mer with a globular shape were identified. The
                      recurrence of these two species at different initial
                      concentrations and experimental conditions as the smallest
                      assemblies present in solution supports the existence of
                      distinct, energetically favored assemblies in solution. The
                      sizes of the two species suggest an Aβ42 aggregation
                      pathway that is based on a basic hexameric building block.
                      The study demonstrates the potential of SV analysis for the
                      evaluation of protein aggregation pathways.},
      cin          = {ICS-6 / ICS-1},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)ICS-1-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000355319400055},
      pubmed       = {pmid:26024352},
      doi          = {10.1371/journal.pone.0127865},
      url          = {https://juser.fz-juelich.de/record/279294},
}