%0 Journal Article
%A Panza, G.
%A Dumpitak, C.
%A Birkmann, E.
%T Influence of the Maillard Reaction to Prion Protein Aggregation
%J Rejuvenation research
%V 13
%@ 1549-1684
%C Larchmont, NY
%I Liebert
%M PreJuSER-9743
%D 2010
%Z Record converted from VDB: 12.11.2012
%X 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.
%K Animals
%K Antibodies: pharmacology
%K CHO Cells
%K Chemical Precipitation
%K Cricetinae
%K Cricetulus
%K Glycosylation End Products, Advanced: chemistry
%K Glycosylation End Products, Advanced: immunology
%K Glycosylation End Products, Advanced: metabolism
%K Maillard Reaction
%K Prions: chemistry
%K Prions: metabolism
%K Protein Multimerization: physiology
%K Protein Processing, Post-Translational
%K Recombinant Proteins: chemistry
%K Recombinant Proteins: metabolism
%K Antibodies (NLM Chemicals)
%K Glycosylation End Products, Advanced (NLM Chemicals)
%K Prions (NLM Chemicals)
%K Recombinant Proteins (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:20370497
%U <Go to ISI:>//WOS:000277602200022
%R 10.1089/rej.2009.0954
%U https://juser.fz-juelich.de/record/9743