TY  - JOUR
AU  - Panza, G.
AU  - Dumpitak, C.
AU  - Birkmann, E.
TI  - Influence of the Maillard Reaction to Prion Protein Aggregation
JO  - Rejuvenation research
VL  - 13
SN  - 1549-1684
CY  - Larchmont, NY
PB  - Liebert
M1  - PreJuSER-9743
PY  - 2010
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Animals
KW  - Antibodies: pharmacology
KW  - CHO Cells
KW  - Chemical Precipitation
KW  - Cricetinae
KW  - Cricetulus
KW  - Glycosylation End Products, Advanced: chemistry
KW  - Glycosylation End Products, Advanced: immunology
KW  - Glycosylation End Products, Advanced: metabolism
KW  - Maillard Reaction
KW  - Prions: chemistry
KW  - Prions: metabolism
KW  - Protein Multimerization: physiology
KW  - Protein Processing, Post-Translational
KW  - Recombinant Proteins: chemistry
KW  - Recombinant Proteins: metabolism
KW  - Antibodies (NLM Chemicals)
KW  - Glycosylation End Products, Advanced (NLM Chemicals)
KW  - Prions (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:20370497
UR  - <Go to ISI:>//WOS:000277602200022
DO  - DOI:10.1089/rej.2009.0954
UR  - https://juser.fz-juelich.de/record/9743
ER  -