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@ARTICLE{Resenberger:136510,
      author       = {Resenberger, Ulrike K and Winklhofer, Konstanze F and
                      Tatzelt, Jörg},
      title        = {{C}ellular prion protein mediates toxic signaling of
                      amyloid beta.},
      journal      = {Neurodegenerative diseases},
      volume       = {10},
      number       = {1-4},
      issn         = {1660-2862},
      address      = {Basel},
      publisher    = {Karger},
      reportid     = {DZNE-2020-02832},
      pages        = {298-300},
      year         = {2012},
      abstract     = {Prion diseases in humans and animals comprise a group of
                      invariably fatal neurodegenerative diseases characterized by
                      the formation of a pathogenic protein conformer designated
                      PrP(Sc) and infectious particles denoted prions. The
                      cellular prion protein (PrP(C)) has a central role in the
                      pathogenesis of prion disease. First, it is the precursor of
                      PrP(Sc) and infectious prions and second, its expression on
                      neuronal cells is required to mediate toxic effects of
                      prions. To specifically study the role of PrP(C) as a
                      mediator of toxic signaling, we have developed novel cell
                      culture models, including primary neurons prepared from
                      PrP-deficient mice. Using these approaches we have been able
                      to show that PrP(C) can interact with and mediate toxic
                      signaling of various β-sheet-rich conformers of different
                      origins, including amyloid β, suggesting a
                      pathophysiological role of the prion protein beyond prion
                      diseases.},
      keywords     = {Amyloid beta-Peptides: metabolism / Amyloid beta-Peptides:
                      toxicity / Animals / Humans / Mice / Mice, Transgenic /
                      Prions: genetics / Prions: metabolism / Protein Conformation
                      / Signal Transduction: drug effects / Signal Transduction:
                      physiology / Amyloid beta-Peptides (NLM Chemicals) / Prions
                      (NLM Chemicals)},
      cin          = {AG Winklhofer},
      ddc          = {610},
      cid          = {I:(DE-2719)5000047},
      pnm          = {341 - Molecular Signaling (POF3-341) / 342 - Disease
                      Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-341 / G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22156337},
      doi          = {10.1159/000332596},
      url          = {https://pub.dzne.de/record/136510},
}