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@ARTICLE{Panza:14241,
      author       = {Panza, G. and Luers, L. and Stöhr, J. and Nagel-Steger, L.
                      and Weiß, J. and Riesner, D. and Willbold, D. and Birkmann,
                      E.},
      title        = {{M}olecular interactions between prions as seeds and
                      recombinant prion proteins as substrates resemble the
                      biological interspecies barrier in vitro},
      journal      = {PLoS one},
      volume       = {5},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PreJuSER-14241},
      pages        = {e14283},
      year         = {2010},
      note         = {This authors were funded by the European Union: (Network of
                      Excellence "NeuroPrion", FOOD-CT-2004-506579,
                      http://www.neuroprion.org/en/index. html); "Presidentenfond
                      der Helmholtzgemeinschaft" (HGF, "Virtual Institute of
                      Structural Biology"), http://www.vibs-rhine-ruhr.org/; and
                      Food Standards Agency UK (M03R0005/004)
                      http://www.food.gov.uk/. Lars Luers was a fellow of the
                      Graduiertenkolleg 1033. Jan Stohr was supported by a
                      postdoctoral fellowship of the Deutsche
                      Forschungsgemeinschaft (DFG). The funders had no role in
                      study design, data collection and analysis, decision to
                      publish, or preparation of the manuscript.},
      abstract     = {Prion diseases like Creutzfeldt-Jakob disease in humans,
                      Scrapie in sheep or bovine spongiform encephalopathy are
                      fatal neurodegenerative diseases, which can be of sporadic,
                      genetic, or infectious origin. Prion diseases are
                      transmissible between different species, however, with a
                      variable species barrier. The key event of prion
                      amplification is the conversion of the cellular isoform of
                      the prion protein (PrP(C)) into the pathogenic isoform
                      (PrP(Sc)). We developed a sodiumdodecylsulfate-based PrP
                      conversion system that induces amyloid fibril formation from
                      soluble α-helical structured recombinant PrP (recPrP). This
                      approach was extended applying pre-purified PrP(Sc) as seeds
                      which accelerate fibrillization of recPrP. In the present
                      study we investigated the interspecies coherence of prion
                      disease. Therefore we used PrP(Sc) from different species
                      like Syrian hamster, cattle, mouse and sheep and seeded
                      fibrillization of recPrP from the same or other species to
                      mimic in vitro the natural species barrier. We could show
                      that the in vitro system of seeded fibrillization is in
                      accordance with what is known from the naturally occurring
                      species barriers.},
      keywords     = {Amyloid: chemistry / Animals / Brain: metabolism / Cattle /
                      Circular Dichroism / Cricetinae / Kinetics / Mesocricetus /
                      Mice / Neurodegenerative Diseases: metabolism / Prion
                      Diseases: genetics / Prion Diseases: metabolism / Prion
                      Diseases: transmission / Prions: chemistry / Protein
                      Structure, Secondary / Recombinant Proteins: chemistry /
                      Sheep / Sodium Dodecyl Sulfate: chemistry / Species
                      Specificity / Ultracentrifugation / Amyloid (NLM Chemicals)
                      / Prions (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / Sodium Dodecyl Sulfate (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {500},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21151607},
      pmc          = {pmc:PMC3000319},
      UT           = {WOS:000285135800013},
      doi          = {10.1371/journal.pone.0014283},
      url          = {https://juser.fz-juelich.de/record/14241},
}