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@ARTICLE{Sthr:62861,
      author       = {Stöhr, J. and Weinmann, N. and Wille, H. and Kaimann, K.
                      and Nagel-Steger, L. and Birkmann, E. and Panza, G. and
                      Prusinder, S. B. and Eigen, M. and Riesner, D.},
      title        = {{M}echanisms of prion protein assembly into amyloid},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {105},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-62861},
      pages        = {2409 - 2414},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The conversion of the alpha-helical, cellular isoform of
                      the prion protein (PrP(C)) to the insoluble,
                      beta-sheet-rich, infectious, disease-causing isoform
                      (PrP(Sc)) is the key event in prion diseases. In an earlier
                      study, several forms of PrP were converted into a fibrillar
                      state by using an in vitro conversion system consisting of
                      low concentrations of SDS and 250 mM NaCl. Here, we
                      characterize the structure of the fibril precursor state,
                      that is, the soluble state under fibrillization conditions.
                      CD spectroscopy, analytical ultracentrifugation, and
                      chemical cross-linking indicate that the precursor state
                      exists in a monomer-dimer equilibrium of partially
                      denatured, alpha-helical PrP, with a well defined contact
                      site of the subunits in the dimer. Using fluorescence with
                      thioflavin T, we monitored and quantitatively described the
                      kinetics of seeded fibril formation, including dependence of
                      the reaction on substrate and seed concentrations.
                      Exponential, seed-enhanced growth can be achieved in
                      homogeneous solution, which can be enhanced by sonication.
                      From these data, we propose a mechanistic model of
                      fibrillization, including the presence of several
                      intermediate structures. These studies also provide a
                      simplified amplification system for prions.},
      keywords     = {Amyloid: chemistry / Amyloid: metabolism / Amyloid:
                      ultrastructure / Circular Dichroism / Cross-Linking
                      Reagents: chemistry / Dimerization / Microscopy, Electron /
                      Prions: chemistry / Prions: metabolism / Prions:
                      ultrastructure / Ultracentrifugation / Amyloid (NLM
                      Chemicals) / Cross-Linking Reagents (NLM Chemicals) / Prions
                      (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {000},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18268326},
      pmc          = {pmc:PMC2268150},
      UT           = {WOS:000253469900031},
      doi          = {10.1073/pnas.0712036105},
      url          = {https://juser.fz-juelich.de/record/62861},
}