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@ARTICLE{Kretzschmar:136879,
      author       = {Kretzschmar, Hans and Tatzelt, Jörg},
      title        = {{P}rion disease: a tale of folds and strains.},
      journal      = {Brain pathology},
      volume       = {23},
      number       = {3},
      issn         = {1015-6305},
      address      = {Oxford},
      publisher    = {Wiley-Blackwell},
      reportid     = {DZNE-2020-03201},
      pages        = {321-332},
      year         = {2013},
      abstract     = {Research on prions, the infectious agents of devastating
                      neurological diseases in humans and animals, has been in the
                      forefront of developing the concept of protein aggregation
                      diseases. Prion diseases are distinguished from other
                      neurodegenerative diseases by three peculiarities. First,
                      prion diseases, in addition to being sporadic or genetic
                      like all other neurodegenerative diseases, are infectious
                      diseases. Animal models were developed early on (a long time
                      before the advent of transgenic technology), and this has
                      made possible the discovery of the prion protein as the
                      infectious agent. Second, human prion diseases have true
                      equivalents in animals, such as scrapie, which has been the
                      subject of experimental research for many years. Variant
                      Creutzfeldt-Jakob disease (vCJD) is a zoonosis caused by
                      bovine spongiform encephalopathy (BSE) prions. Third, they
                      show a wide variety of phenotypes in humans and animals,
                      much wider than the variants of any other sporadic or
                      genetic neurodegenerative disease. It has now become firmly
                      established that particular PrP(Sc) isoforms are closely
                      related to specific human prion strains. The variety of
                      human prion diseases, still an enigma in its own right, is a
                      focus of this article. Recently, a series of experiments has
                      shown that the concept of aberrant protein folding and
                      templating, first developed for prions, may apply to a
                      variety of neurodegenerative diseases. In the wake of these
                      discoveries, the term prion has come to be used for Aβ,
                      α-synuclein, tau and possibly others. The self-propagation
                      of alternative conformations seems to be the common
                      denominator of these 'prions,' which in future, in order to
                      avoid confusion, may have to be specified either as
                      'neurodegenerative prions' or 'infectious prions.'},
      subtyp        = {Review Article},
      keywords     = {Animals / Blood-Brain Barrier / Creutzfeldt-Jakob Syndrome:
                      genetics / Creutzfeldt-Jakob Syndrome: pathology /
                      Genome-Wide Association Study / Humans / Kuru: genetics /
                      Kuru: pathology / PrPC Proteins: chemistry / PrPC Proteins:
                      genetics / PrPC Proteins: toxicity / Prion Diseases:
                      genetics / Prion Diseases: pathology / Prion Diseases:
                      transmission / Protein Folding / Proteostasis Deficiencies:
                      genetics / Proteostasis Deficiencies: pathology / PrPC
                      Proteins (NLM Chemicals)},
      cin          = {Ext LMU ZNP / Ext AG Tatzelt},
      ddc          = {610},
      cid          = {I:(DE-2719)5000051 / I:(DE-2719)5000053},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23587138},
      doi          = {10.1111/bpa.12045},
      url          = {https://pub.dzne.de/record/136879},
}