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000009743 0247_ $$2DOI$$a10.1089/rej.2009.0954
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000009743 037__ $$aPreJuSER-9743
000009743 041__ $$aeng
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000009743 084__ $$2WoS$$aGeriatrics & Gerontology
000009743 1001_ $$0P:(DE-HGF)0$$aPanza, G.$$b0
000009743 245__ $$aInfluence of the Maillard Reaction to Prion Protein Aggregation
000009743 260__ $$aLarchmont, NY$$bLiebert$$c2010
000009743 300__ $$a
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000009743 440_0 $$018202$$aRejuvenation Research$$v13$$x1549-1684$$y2
000009743 500__ $$aRecord converted from VDB: 12.11.2012
000009743 520__ $$aPrion diseases are fatal neurodegenerative diseases that occur either spontaneously or genetically or are caused by infection. Spontaneously occurring prion diseases are age related. The infectious agents, called prions, are proteinaceous infectious particles, composed mainly of the host-encoded prion protein (PrP) in a misfolded, insoluble, and aggregated isoform. Advanced glycation end products (AGEs) are well known to contribute to protein misfolding, insolubility, and aggregation. Thus, we studied if AGE-modification could influence PrP aggregation. We analyzed PrP preparations immunochemically to determine if they contain AGE-modified PrP. We also studied the influence of AGE modifications on the PrP aggregation process in vitro.
000009743 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000009743 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000009743 588__ $$aDataset connected to Web of Science, Pubmed
000009743 650_2 $$2MeSH$$aAnimals
000009743 650_2 $$2MeSH$$aAntibodies: pharmacology
000009743 650_2 $$2MeSH$$aCHO Cells
000009743 650_2 $$2MeSH$$aChemical Precipitation
000009743 650_2 $$2MeSH$$aCricetinae
000009743 650_2 $$2MeSH$$aCricetulus
000009743 650_2 $$2MeSH$$aGlycosylation End Products, Advanced: chemistry
000009743 650_2 $$2MeSH$$aGlycosylation End Products, Advanced: immunology
000009743 650_2 $$2MeSH$$aGlycosylation End Products, Advanced: metabolism
000009743 650_2 $$2MeSH$$aMaillard Reaction
000009743 650_2 $$2MeSH$$aPrions: chemistry
000009743 650_2 $$2MeSH$$aPrions: metabolism
000009743 650_2 $$2MeSH$$aProtein Multimerization: physiology
000009743 650_2 $$2MeSH$$aProtein Processing, Post-Translational
000009743 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000009743 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000009743 650_7 $$00$$2NLM Chemicals$$aAntibodies
000009743 650_7 $$00$$2NLM Chemicals$$aGlycosylation End Products, Advanced
000009743 650_7 $$00$$2NLM Chemicals$$aPrions
000009743 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000009743 650_7 $$2WoSType$$aJ
000009743 7001_ $$0P:(DE-HGF)0$$aDumpitak, C.$$b1
000009743 7001_ $$0P:(DE-Juel1)VDB65870$$aBirkmann, E.$$b2$$uFZJ
000009743 773__ $$0PERI:(DE-600)2155984-3$$a10.1089/rej.2009.0954$$gVol. 13$$q13$$tRejuvenation research$$v13$$x1549-1684$$y2010
000009743 8567_ $$uhttp://dx.doi.org/10.1089/rej.2009.0954
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000009743 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x1
000009743 9132_ $$0G:(DE-HGF)POF3-553$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vPhysical Basis of Diseases$$x0
000009743 9141_ $$y2010
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000009743 9201_ $$0I:(DE-Juel1)VDB942$$d31.12.2010$$gISB$$kISB-3$$lStrukturbiochemie$$x0
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