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@ARTICLE{Sthr:15094,
      author       = {Stöhr, J. and Elfrink, K. and Weinmann, N. and Wille, H.
                      and Willbold, D. and Birkmann, E. and Riesner, D.},
      title        = {{I}n vitro conversion and seeded fibrillization of
                      posttranslationally modified prion protein},
      journal      = {Biological chemistry},
      volume       = {392},
      issn         = {1431-6730},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {PreJuSER-15094},
      pages        = {415 - 421},
      year         = {2011},
      note         = {This work was supported by grants from the Deutsche
                      Forschungsgemeinschaft (DFG), EUNetwork of Excellence
                      (NeuroPrion) and the Praesidentenfond of the
                      Helmholtzgemeinschaft (HGF, Virtual Institute of Structural
                      Biology). Jan Stohr is supported by postdoctoral fellowship
                      of the Deutsche Forschungsgemeinschaft (DFG). We thank S.B.
                      Prusiner for critical reading and helpful discussion for
                      this manuscript. The authors thank Ilka Ostermann for her
                      assistance in the purification of CHO-PrP<SUP>C</SUP>.},
      abstract     = {The conversion of the cellular isoform of the prion protein
                      (PrP(C)) into the pathologic isoform (PrP(Sc)) is the key
                      event in prion diseases. To study the conversion process, an
                      in vitro system based on varying the concentration of low
                      amounts of sodium dodecyl sulfate (SDS) has been employed.
                      In the present study, the conversion of full-length PrP(C)
                      isolated from Chinese hamster ovary cells (CHO-PrP(C)) was
                      examined. CHO-PrP(C) harbors native, posttranslational
                      modifications, including the GPI anchor and two N-linked
                      glyco-sylation sites. The properties of CHO-PrP(C) were
                      compared with those of full-length and N-terminally
                      truncated recombinant PrP. As shown earlier with recombinant
                      PrP (recPrP90-231), transition from a soluble α-helical
                      state as known for native PrP(C) into an aggregated,
                      β-sheet-rich PrP(Sc)-like state could be induced by
                      dilution of SDS. The aggregated state is partially
                      proteinase K (PK)-resistant, exhibiting a cleavage site
                      similar to that found with PrP(Sc). Compared to recPrP
                      (90-231), fibril formation with CHO-PrP(C) requires lower
                      SDS concentrations $(0.0075\%),$ and can be drastically
                      accelerated by seeding with PrP(Sc) purified from brain
                      homogenates of terminally sick hamsters. Our results show
                      that recPrP 90-231 and CHO-PrPC behave qualitatively similar
                      but quantitatively different. The in vivo situation can be
                      simulated closer with CHO-PrP(C) because the specific PK
                      cleave site could be shown and the seed-assisted
                      fibrillization was much more efficient.},
      keywords     = {Animals / Blotting, Western / CHO Cells / Circular
                      Dichroism / Cricetinae / Cricetulus / Electrophoresis,
                      Polyacrylamide Gel / Microscopy, Electron / PrPC Proteins:
                      chemistry / PrPC Proteins: drug effects / PrPC Proteins:
                      metabolism / PrPSc Proteins: chemistry / PrPSc Proteins:
                      drug effects / PrPSc Proteins: metabolism / Protein
                      Processing, Post-Translational / Protein Structure,
                      Secondary / Sodium Dodecyl Sulfate: pharmacology / PrPC
                      Proteins (NLM Chemicals) / PrPSc Proteins (NLM Chemicals) /
                      Sodium Dodecyl Sulfate (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21476870},
      UT           = {WOS:000289343100003},
      doi          = {10.1515/bc.2011.048},
      url          = {https://juser.fz-juelich.de/record/15094},
}