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@ARTICLE{Panza:9743,
      author       = {Panza, G. and Dumpitak, C. and Birkmann, E.},
      title        = {{I}nfluence of the {M}aillard {R}eaction to {P}rion
                      {P}rotein {A}ggregation},
      journal      = {Rejuvenation research},
      volume       = {13},
      issn         = {1549-1684},
      address      = {Larchmont, NY},
      publisher    = {Liebert},
      reportid     = {PreJuSER-9743},
      year         = {2010},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Prion diseases are fatal neurodegenerative diseases that
                      occur either spontaneously or genetically or are caused by
                      infection. Spontaneously occurring prion diseases are age
                      related. The infectious agents, called prions, are
                      proteinaceous infectious particles, composed mainly of the
                      host-encoded prion protein (PrP) in a misfolded, insoluble,
                      and aggregated isoform. Advanced glycation end products
                      (AGEs) are well known to contribute to protein misfolding,
                      insolubility, and aggregation. Thus, we studied if
                      AGE-modification could influence PrP aggregation. We
                      analyzed PrP preparations immunochemically to determine if
                      they contain AGE-modified PrP. We also studied the influence
                      of AGE modifications on the PrP aggregation process in
                      vitro.},
      keywords     = {Animals / Antibodies: pharmacology / CHO Cells / Chemical
                      Precipitation / Cricetinae / Cricetulus / Glycosylation End
                      Products, Advanced: chemistry / Glycosylation End Products,
                      Advanced: immunology / Glycosylation End Products, Advanced:
                      metabolism / Maillard Reaction / Prions: chemistry / Prions:
                      metabolism / Protein Multimerization: physiology / Protein
                      Processing, Post-Translational / Recombinant Proteins:
                      chemistry / Recombinant Proteins: metabolism / Antibodies
                      (NLM Chemicals) / Glycosylation End Products, Advanced (NLM
                      Chemicals) / Prions (NLM Chemicals) / Recombinant Proteins
                      (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3},
      ddc          = {610},
      cid          = {I:(DE-Juel1)VDB942},
      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:20370497},
      UT           = {WOS:000277602200022},
      doi          = {10.1089/rej.2009.0954},
      url          = {https://juser.fz-juelich.de/record/9743},
}