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@ARTICLE{Frenzel:151829,
      author       = {Frenzel, Daniel and Glück, Julian M. and Brener, Oleksandr
                      and Oesterhelt, Filipp and Nagel-Steger, Luitgard and
                      Willbold, Dieter},
      title        = {{I}mmobilization of {H}omogeneous {M}onomeric, {O}ligomeric
                      and {F}ibrillar {A}β {S}pecies for {R}eliable {SPR}
                      {M}easurements},
      journal      = {PLoS one},
      volume       = {9},
      number       = {3},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2014-01699},
      pages        = {e89490 (1 - 7)},
      year         = {2014},
      abstract     = {There is strong evidence that the amyloid-beta peptide
                      (Aß) plays a central role in the pathogenesis of
                      Alzheimer’s disease (AD). In this context, a detailed
                      quantitative description of the interactions with different
                      Aß species is essential for characterization of
                      physiological and artificial ligands. However, the high
                      aggregation propensity of Aß in concert with its
                      susceptibility to structural changes due to even slight
                      changes in solution conditions has impeded surface plasmon
                      resonance (SPR) studies with homogeneous Aß conformer
                      species. Here, we have adapted the experimental procedures
                      to state-of-the-art techniques and established novel
                      approaches to reliably overcome the aforementioned
                      challenges. We show that the application of density gradient
                      centrifugation (DGC) for sample purification and the use of
                      a single chain variable fragment (scFv) of a monoclonal
                      antibody directed against the amino-terminus of Aß allows
                      reliable SPR measurements and quality control of the
                      immobilized Aß aggregate species at any step throughout the
                      experiment.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000332468900019},
      pubmed       = {pmid:24594736},
      doi          = {10.1371/journal.pone.0089490},
      url          = {https://juser.fz-juelich.de/record/151829},
}