Hauptseite > Publikationsdatenbank > Aggregation and amyloid fibril formation of the prion protein is accelerated in presence of glycogen > print

001     62863
005     20200402210514.0
024 7 _ |2 pmid
|a pmid:18341429
024 7 _ |2 DOI
|a 10.1089/rej.2008.0698
024 7 _ |2 WOS
|a WOS:000255773200015
037 _ _ |a PreJuSER-62863
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 Aggregation and amyloid fibril formation of the prion protein is accelerated in presence of glycogen
260 _ _ |a Larchmont, NY
|b Liebert
|c 2008
300 _ _ |a 365 - 369
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 11
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Prion diseases like Creutzfeldt-Jakob disease in humans or scrapie in sheep and goats are infectious neurodegenerative diseases. Their infectious agent, called prion, is composed mainly of aggregated and misfolded prion protein and non-proteinaceous components. An example of such a common non-proteinaceous secondary component of natural prions is the polysaccharide scaffold. We studied the influence of such a polysaccharide on the conformational transition of PrP applying an in vitro conversion system. Here we report that glycogen supports and accelerates PrP amorphous aggregation similar to seeded aggregation and leads to co-aggregates. Furthermore, PrP fibril formation was highly accelerated in the presence of glycogen.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amyloid: chemistry
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Circular Dichroism
650 _ 2 |2 MeSH
|a Cricetinae
650 _ 2 |2 MeSH
|a Glycogen: pharmacology
650 _ 2 |2 MeSH
|a Mesocricetus
650 _ 2 |2 MeSH
|a Prions: chemistry
650 _ 2 |2 MeSH
|a Prions: metabolism
650 _ 2 |2 MeSH
|a Protein Structure, Quaternary
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Recombinant Proteins: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid
650 _ 7 |0 0
|2 NLM Chemicals
|a Prions
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |0 9005-79-2
|2 NLM Chemicals
|a Glycogen
650 _ 7 |a J
|2 WoSType
700 1 _ |a Stöhr, J.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Birkmann, E.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB65870
700 1 _ |a Riesner, D.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Willbold, D.
|b 4
|u FZJ
|0 P:(DE-Juel1)132029
700 1 _ |a Baba, O.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Terashima, T.
|b 6
|0 P:(DE-HGF)0
700 1 _ |a Dumpitak, C.
|b 7
|u FZJ
|0 P:(DE-Juel1)VDB72720
773 _ _ |a 10.1089/rej.2008.0698
|g Vol. 11, p. 365 - 369
|p 365 - 369
|q 11<365 - 369
|0 PERI:(DE-600)2155984-3
|t Rejuvenation research
|v 11
|y 2008
|x 1549-1684
856 7 _ |u http://dx.doi.org/10.1089/rej.2008.0698
909 C O |o oai:juser.fz-juelich.de:62863
|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
914 1 _ |y 2008
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k INB-2
|l Molekulare Biophysik
|d 31.12.2008
|g INB
|0 I:(DE-Juel1)VDB805
|x 0
970 _ _ |a VDB:(DE-Juel1)99746
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

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