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@ARTICLE{Panza:313,
      author       = {Panza, G. and Stöhr, J. and Dumpitak, C. and
                      Papathanassiou, D. and Weiss, J. and Riesner, D. and
                      Willbold, D. and Birkmann, E.},
      title        = {{S}pontaneous and {BSE}-prion-seeded amyloid formation of
                      full length recombinant bovine prion protein},
      journal      = {Biochemical and biophysical research communications},
      volume       = {373},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PreJuSER-313},
      pages        = {493 - 497},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The conversion of the cellular isoform of the prion protein
                      into the pathogenic isoform PrP(Sc) is the key event in
                      prion diseases. The disease can occur spontaneously
                      genetically or by infection. In earlier studies we presented
                      an in vitro conversion system which simulates the structural
                      transition in recPrP by varying low concentrations of SDS at
                      constant NaCl. In the present study we adopted the
                      conversion system from experimental Scrapie in hamster to
                      bovine recPrP and generated amyloid fibrils. The
                      intermediate state which is optimal for fibril formation is
                      a soluble, beta-rich state. The system was extended using
                      BSE-prions as seeds and led to an acceleration of fibril
                      formation by orders of magnitude. This seeded amyloid
                      formation assay avoids any PK-treatment, is therefore able
                      to detect even PK-sensitive PrP(Sc) and does not require
                      cellular components.},
      keywords     = {Amyloid: biosynthesis / Amyloid: chemistry / Animals /
                      Cattle / Cricetinae / Encephalopathy, Bovine Spongiform:
                      metabolism / Models, Molecular / PrPSc Proteins: chemistry /
                      PrPSc Proteins: metabolism / Protein Conformation /
                      Recombinant Proteins: chemistry / Recombinant Proteins:
                      metabolism / Amyloid (NLM Chemicals) / PrPSc Proteins (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals) / J
                      (WoSType)},
      cin          = {INB-2 / JARA-SIM},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805 / I:(DE-Juel1)VDB1045},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18585368},
      UT           = {WOS:000258208500008},
      doi          = {10.1016/j.bbrc.2008.06.059},
      url          = {https://juser.fz-juelich.de/record/313},
}