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@ARTICLE{Rudolph:283460,
      author       = {Rudolph, Stephan and Klein, Antonia Nicole and Tusche,
                      Markus and Schlosser, Christine and Elfgen, Anne and Brener,
                      Oleksandr and Teunissen, Charlotte and Gremer, Lothar and
                      Funke, Susanne Aileen and Kutzsche, Janine and Willbold,
                      Dieter},
      title        = {{C}ompetitive {M}irror {I}mage {P}hage {D}isplay {D}erived
                      {P}eptide {M}odulates {A}myloid {B}eta {A}ggregation and
                      {T}oxicity},
      journal      = {PLoS one},
      volume       = {11},
      number       = {2},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2016-01815},
      pages        = {e0147470 -},
      year         = {2016},
      abstract     = {Alzheimer´s disease is the most prominent type of dementia
                      and currently no causative treatment is available. According
                      to recent studies, oligomeric species of the amyloid beta
                      (Aβ) peptide appear to be the most toxic Aβ assemblies.
                      Aβ monomers, however, may be not toxic per se and may even
                      have a neuroprotective role. Here we describe a competitive
                      mirror image phage display procedure that allowed us to
                      identify preferentially Aβ1–42 monomer binding and
                      thereby stabilizing peptides, which destabilize and thereby
                      eliminate toxic oligomer species. One of the peptides,
                      called Mosd1 (monomer specific d-peptide 1), was
                      characterized in more detail. Mosd1 abolished oligomers from
                      a mixture of Aβ1–42 species, reduced Aβ1–42 toxicity
                      in cell culture, and restored the physiological phenotype in
                      neuronal cells stably transfected with the gene coding for
                      human amyloid precursor protein.},
      cin          = {ICS-6},
      ddc          = {500},
      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:000369550200041},
      pubmed       = {pmid:26840229},
      doi          = {10.1371/journal.pone.0147470},
      url          = {https://juser.fz-juelich.de/record/283460},
}