001     9743
005     20200402205832.0
024 7 _ |2 pmid
|a pmid:20370497
024 7 _ |2 DOI
|a 10.1089/rej.2009.0954
024 7 _ |2 WOS
|a WOS:000277602200022
037 _ _ |a PreJuSER-9743
041 _ _ |a eng
082 _ _ |a 610
084 _ _ |2 WoS
|a Geriatrics & Gerontology
100 1 _ |a Panza, G.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Influence of the Maillard Reaction to Prion Protein Aggregation
260 _ _ |a Larchmont, NY
|b Liebert
|c 2010
300 _ _ |a
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Rejuvenation Research
|x 1549-1684
|0 18202
|y 2
|v 13
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
536 _ _ |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|0 G:(DE-Juel1)FUEK505
|x 1
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Antibodies: pharmacology
650 _ 2 |2 MeSH
|a CHO Cells
650 _ 2 |2 MeSH
|a Chemical Precipitation
650 _ 2 |2 MeSH
|a Cricetinae
650 _ 2 |2 MeSH
|a Cricetulus
650 _ 2 |2 MeSH
|a Glycosylation End Products, Advanced: chemistry
650 _ 2 |2 MeSH
|a Glycosylation End Products, Advanced: immunology
650 _ 2 |2 MeSH
|a Glycosylation End Products, Advanced: metabolism
650 _ 2 |2 MeSH
|a Maillard Reaction
650 _ 2 |2 MeSH
|a Prions: chemistry
650 _ 2 |2 MeSH
|a Prions: metabolism
650 _ 2 |2 MeSH
|a Protein Multimerization: physiology
650 _ 2 |2 MeSH
|a Protein Processing, Post-Translational
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Recombinant Proteins: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Antibodies
650 _ 7 |0 0
|2 NLM Chemicals
|a Glycosylation End Products, Advanced
650 _ 7 |0 0
|2 NLM Chemicals
|a Prions
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |a J
|2 WoSType
700 1 _ |a Dumpitak, C.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Birkmann, E.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB65870
773 _ _ |a 10.1089/rej.2009.0954
|g Vol. 13
|q 13
|0 PERI:(DE-600)2155984-3
|t Rejuvenation research
|v 13
|y 2010
|x 1549-1684
856 7 _ |u http://dx.doi.org/10.1089/rej.2009.0954
909 C O |o oai:juser.fz-juelich.de:9743
|p VDB
913 1 _ |k P33
|v Funktion und Dysfunktion des Nervensystems
|l Funktion und Dysfunktion des Nervensystems
|b Gesundheit
|0 G:(DE-Juel1)FUEK409
|x 0
913 1 _ |k P45
|v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|l Biologische Informationsverarbeitung
|b Schlüsseltechnologien
|0 G:(DE-Juel1)FUEK505
|x 1
913 2 _ |a DE-HGF
|b Key Technologies
|l BioSoft Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences
|1 G:(DE-HGF)POF3-550
|0 G:(DE-HGF)POF3-553
|2 G:(DE-HGF)POF3-500
|v Physical Basis of Diseases
|x 0
914 1 _ |y 2010
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k ISB-3
|l Strukturbiochemie
|d 31.12.2010
|g ISB
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|x 0
970 _ _ |a VDB:(DE-Juel1)119733
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980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ICS-6-20110106


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