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000000313 0247_ $$2DOI$$a10.1016/j.bbrc.2008.06.059
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000000313 084__ $$2WoS$$aBiochemistry & Molecular Biology
000000313 084__ $$2WoS$$aBiophysics
000000313 1001_ $$0P:(DE-HGF)0$$aPanza, G.$$b0
000000313 245__ $$aSpontaneous and BSE-prion-seeded amyloid formation of full length recombinant bovine prion protein
000000313 260__ $$aOrlando, Fla.$$bAcademic Press$$c2008
000000313 300__ $$a493 - 497
000000313 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000313 440_0 $$0787$$aBiochemical and Biophysical Research Communications$$v373$$x0006-291X$$y4
000000313 500__ $$aRecord converted from VDB: 12.11.2012
000000313 520__ $$aThe conversion of the cellular isoform of the prion protein into the pathogenic isoform PrP(Sc) is the key event in prion diseases. The disease can occur spontaneously genetically or by infection. In earlier studies we presented an in vitro conversion system which simulates the structural transition in recPrP by varying low concentrations of SDS at constant NaCl. In the present study we adopted the conversion system from experimental Scrapie in hamster to bovine recPrP and generated amyloid fibrils. The intermediate state which is optimal for fibril formation is a soluble, beta-rich state. The system was extended using BSE-prions as seeds and led to an acceleration of fibril formation by orders of magnitude. This seeded amyloid formation assay avoids any PK-treatment, is therefore able to detect even PK-sensitive PrP(Sc) and does not require cellular components.
000000313 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000000313 588__ $$aDataset connected to Web of Science, Pubmed
000000313 650_2 $$2MeSH$$aAmyloid: biosynthesis
000000313 650_2 $$2MeSH$$aAmyloid: chemistry
000000313 650_2 $$2MeSH$$aAnimals
000000313 650_2 $$2MeSH$$aCattle
000000313 650_2 $$2MeSH$$aCricetinae
000000313 650_2 $$2MeSH$$aEncephalopathy, Bovine Spongiform: metabolism
000000313 650_2 $$2MeSH$$aModels, Molecular
000000313 650_2 $$2MeSH$$aPrPSc Proteins: chemistry
000000313 650_2 $$2MeSH$$aPrPSc Proteins: metabolism
000000313 650_2 $$2MeSH$$aProtein Conformation
000000313 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000000313 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000000313 650_7 $$00$$2NLM Chemicals$$aAmyloid
000000313 650_7 $$00$$2NLM Chemicals$$aPrPSc Proteins
000000313 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000000313 650_7 $$2WoSType$$aJ
000000313 65320 $$2Author$$aBSE-prions
000000313 65320 $$2Author$$aseeded vs. spontaneous conversion
000000313 65320 $$2Author$$aamyloid fibrils
000000313 65320 $$2Author$$apre-amyloid state
000000313 7001_ $$0P:(DE-HGF)0$$aStöhr, J.$$b1
000000313 7001_ $$0P:(DE-HGF)0$$aDumpitak, C.$$b2
000000313 7001_ $$0P:(DE-HGF)0$$aPapathanassiou, D.$$b3
000000313 7001_ $$0P:(DE-HGF)0$$aWeiss, J.$$b4
000000313 7001_ $$0P:(DE-HGF)0$$aRiesner, D.$$b5
000000313 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b6$$uFZJ
000000313 7001_ $$0P:(DE-Juel1)VDB65870$$aBirkmann, E.$$b7$$uFZJ
000000313 773__ $$0PERI:(DE-600)1461396-7$$a10.1016/j.bbrc.2008.06.059$$gVol. 373, p. 493 - 497$$p493 - 497$$q373<493 - 497$$tBiochemical and biophysical research communications$$v373$$x0006-291X$$y2008
000000313 8567_ $$uhttp://dx.doi.org/10.1016/j.bbrc.2008.06.059
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000000313 9141_ $$y2008
000000313 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000000313 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
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