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@ARTICLE{Lers:9742,
      author       = {Lüers, L. and Panza, G. and Henke, F. and Aygenim, T. and
                      Weiß, J. and Willbold, D. and Birkmann, E.},
      title        = {{A}myloid formation: {A}ge-related mechanism in
                      {C}reutzfeldt-{J}akob disease?},
      journal      = {Rejuvenation research},
      volume       = {13},
      issn         = {1549-1684},
      address      = {Larchmont, NY},
      publisher    = {Liebert},
      reportid     = {PreJuSER-9742},
      year         = {2010},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Protein aggregation occurs in many age-related
                      neurodegenerative diseases, where it can lead to deposits of
                      naturally occurring proteins in the brain. In case of
                      Creutzfeldt-Jakob disease (CJD), these deposits consist of
                      prion protein (PrP). CJD has three etiologies: spontaneous,
                      genetic, or caused by infection. A polymorphism within the
                      PrP gene is associated with susceptibility of infection. The
                      main event in prion diseases is the conversion of PrP from
                      its naturally occurring isoform to its disease-associated
                      isoform. Here, we present the adaption of a previously
                      reported in vitro conversion system based on hamster
                      recombinant PrP to analyze amyloid fibril formation of human
                      recombinant PrP. We further compare the aggregation
                      characteristics of the human PrP according to the
                      polymorphism variants M129 and V129.},
      keywords     = {Aging: metabolism / Aging: physiology / Amyloid: metabolism
                      / Circular Dichroism / Congo Red: pharmacology /
                      Creutzfeldt-Jakob Syndrome: etiology / Creutzfeldt-Jakob
                      Syndrome: metabolism / Creutzfeldt-Jakob Syndrome: pathology
                      / Humans / Microscopy, Electron, Transmission / Models,
                      Biological / PrPSc Proteins: chemistry / PrPSc Proteins:
                      metabolism / Recombinant Proteins: analysis / Recombinant
                      Proteins: chemistry / Recombinant Proteins: metabolism /
                      Staining and Labeling / Thiazoles: pharmacology / Amyloid
                      (NLM Chemicals) / PrPSc Proteins (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / Thiazoles (NLM
                      Chemicals) / thioflavin T (NLM Chemicals) / Congo Red (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {610},
      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    = {Geriatrics $\&$ Gerontology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20017612},
      UT           = {WOS:000277602200020},
      doi          = {10.1089/rej.2009.0932},
      url          = {https://juser.fz-juelich.de/record/9742},
}