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000062863 0247_ $$2DOI$$a10.1089/rej.2008.0698
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000062863 084__ $$2WoS$$aGeriatrics & Gerontology
000062863 1001_ $$0P:(DE-HGF)0$$aPanza, G.$$b0
000062863 245__ $$aAggregation and amyloid fibril formation of the prion protein is accelerated in presence of glycogen
000062863 260__ $$aLarchmont, NY$$bLiebert$$c2008
000062863 300__ $$a365 - 369
000062863 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000062863 440_0 $$018202$$aRejuvenation Research$$v11$$x1549-1684$$y2
000062863 500__ $$aRecord converted from VDB: 12.11.2012
000062863 520__ $$aPrion 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.
000062863 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000062863 650_2 $$2MeSH$$aAmyloid: chemistry
000062863 650_2 $$2MeSH$$aAnimals
000062863 650_2 $$2MeSH$$aCircular Dichroism
000062863 650_2 $$2MeSH$$aCricetinae
000062863 650_2 $$2MeSH$$aGlycogen: pharmacology
000062863 650_2 $$2MeSH$$aMesocricetus
000062863 650_2 $$2MeSH$$aPrions: chemistry
000062863 650_2 $$2MeSH$$aPrions: metabolism
000062863 650_2 $$2MeSH$$aProtein Structure, Quaternary
000062863 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000062863 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000062863 650_7 $$00$$2NLM Chemicals$$aAmyloid
000062863 650_7 $$00$$2NLM Chemicals$$aPrions
000062863 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000062863 650_7 $$09005-79-2$$2NLM Chemicals$$aGlycogen
000062863 650_7 $$2WoSType$$aJ
000062863 7001_ $$0P:(DE-HGF)0$$aStöhr, J.$$b1
000062863 7001_ $$0P:(DE-Juel1)VDB65870$$aBirkmann, E.$$b2$$uFZJ
000062863 7001_ $$0P:(DE-HGF)0$$aRiesner, D.$$b3
000062863 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000062863 7001_ $$0P:(DE-HGF)0$$aBaba, O.$$b5
000062863 7001_ $$0P:(DE-HGF)0$$aTerashima, T.$$b6
000062863 7001_ $$0P:(DE-Juel1)VDB72720$$aDumpitak, C.$$b7$$uFZJ
000062863 773__ $$0PERI:(DE-600)2155984-3$$a10.1089/rej.2008.0698$$gVol. 11, p. 365 - 369$$p365 - 369$$q11<365 - 369$$tRejuvenation research$$v11$$x1549-1684$$y2008
000062863 8567_ $$uhttp://dx.doi.org/10.1089/rej.2008.0698
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000062863 9141_ $$y2008
000062863 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000062863 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
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