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@ARTICLE{Resenberger:136455,
      author       = {Resenberger, Ulrike K and Winklhofer, Konstanze F and
                      Tatzelt, Jörg},
      title        = {{N}europrotective and neurotoxic signaling by the prion
                      protein.},
      journal      = {Topics in current chemistry},
      volume       = {305},
      issn         = {0340-1022},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {DZNE-2020-02777},
      isbn         = {978-3-642-24066-9 (print)},
      series       = {Topics in Current Chemistry},
      pages        = {101-119},
      year         = {2011},
      comment      = {Prion Proteins / Tatzelt, Jörg (Editor) ; Berlin,
                      Heidelberg : Springer Berlin Heidelberg, 2012, Chapter 160 ;
                      ISSN: 0340-1022=1436-5049 ; ISBN:
                      978-3-642-24066-9=978-3-642-24067-6 ;
                      doi:10.1007/978-3-642-24067-6},
      booktitle     = {Prion Proteins / Tatzelt, Jörg
                       (Editor) ; Berlin, Heidelberg :
                       Springer Berlin Heidelberg, 2012,
                       Chapter 160 ; ISSN: 0340-1022=1436-5049
                       ; ISBN:
                       978-3-642-24066-9=978-3-642-24067-6 ;
                       doi:10.1007/978-3-642-24067-6},
      abstract     = {Prion diseases in humans and animals are characterized by
                      progressive neurodegeneration and the formation of
                      infectious particles called prions. Both features are
                      intimately linked to a conformational transition of the
                      cellular prion protein (PrP(C)) into aberrantly folded
                      conformers with neurotoxic and self-replicating activities.
                      Interestingly, there is increasing evidence that the
                      infectious and neurotoxic properties of PrP conformers are
                      not necessarily coupled. Transgenic mouse models revealed
                      that some PrP mutants interfere with neuronal function in
                      the absence of infectious prions. Vice versa, propagation of
                      prions can occur without causing neurotoxicity.
                      Consequently, it appears plausible that two partially
                      independent pathways exist, one pathway leading to the
                      propagation of infectious prions and another one that
                      mediates neurotoxic signaling. In this review we will
                      summarize current knowledge of neurotoxic PrP conformers and
                      discuss the role of PrP(C) as a mediator of both
                      stress-protective and neurotoxic signaling cascades.},
      subtyp        = {Review Article},
      keywords     = {Animals / Humans / Mice / Models, Biological / Mutation /
                      Neurodegenerative Diseases: metabolism / Neurons: metabolism
                      / Neurons: pathology / Neurotoxicity Syndromes: metabolism /
                      Prion Diseases: metabolism / Prion Diseases: pathology /
                      Prions: metabolism / Protein Conformation / Protein
                      Denaturation / Protein Folding / Protein Structure, Tertiary
                      / Signal Transduction / Prions (NLM Chemicals)},
      cin          = {AG Winklhofer / Ext AG Tatzelt},
      ddc          = {540},
      cid          = {I:(DE-2719)5000047 / I:(DE-2719)5000053},
      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)3 / PUB:(DE-HGF)16},
      pubmed       = {pmid:21598098},
      doi          = {10.1007/128_2011_160},
      url          = {https://pub.dzne.de/record/136455},
}