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@ARTICLE{Panza:62863,
      author       = {Panza, G. and Stöhr, J. and Birkmann, E. and Riesner, D.
                      and Willbold, D. and Baba, O. and Terashima, T. and
                      Dumpitak, C.},
      title        = {{A}ggregation and amyloid fibril formation of the prion
                      protein is accelerated in presence of glycogen},
      journal      = {Rejuvenation research},
      volume       = {11},
      issn         = {1549-1684},
      address      = {Larchmont, NY},
      publisher    = {Liebert},
      reportid     = {PreJuSER-62863},
      pages        = {365 - 369},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Prion diseases like Creutzfeldt-Jakob disease in humans or
                      scrapie in sheep and goats are infectious neurodegenerative
                      diseases. Their infectious agent, called prion, is composed
                      mainly of aggregated and misfolded prion protein and
                      non-proteinaceous components. An example of such a common
                      non-proteinaceous secondary component of natural prions is
                      the polysaccharide scaffold. We studied the influence of
                      such a polysaccharide on the conformational transition of
                      PrP applying an in vitro conversion system. Here we report
                      that glycogen supports and accelerates PrP amorphous
                      aggregation similar to seeded aggregation and leads to
                      co-aggregates. Furthermore, PrP fibril formation was highly
                      accelerated in the presence of glycogen.},
      keywords     = {Amyloid: chemistry / Animals / Circular Dichroism /
                      Cricetinae / Glycogen: pharmacology / Mesocricetus / Prions:
                      chemistry / Prions: metabolism / Protein Structure,
                      Quaternary / Recombinant Proteins: chemistry / Recombinant
                      Proteins: metabolism / Amyloid (NLM Chemicals) / Prions (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals) / Glycogen
                      (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {610},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Geriatrics $\&$ Gerontology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18341429},
      UT           = {WOS:000255773200015},
      doi          = {10.1089/rej.2008.0698},
      url          = {https://juser.fz-juelich.de/record/62863},
}