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http://purl.uniprot.org/citations/17097676http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17097676http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17097676http://www.w3.org/2000/01/rdf-schema#comment"Prions are self-propagating, infectious protein conformations. The mammalian prion, PrP(Sc), responsible for neurodegenerative diseases like bovine spongiform encephalopathy (BSE; "mad cow" disease) and Creutzfeldt-Jakob's disease, appears to be a beta-sheet-rich amyloid conformation of PrP(c) that converts PrP(c) into PrP(Sc). However, an unequivocal demonstration of "protein-only" infection by PrP(Sc) is still lacking. So far, protein only infection has been proven for three prions, [PSI(+)], [URE3] and [Het-s], all of fungal origin. Considerable evidence supports the hypothesis that another protein, the yeast Rnq1p, can form a prion, [PIN(+)]. While Rnq1p does not lose any known function upon prionization, [PIN(+)] has interesting positive phenotypes: facilitating the appearance and destabilization of other prions as well as the aggregation of polyglutamine extensions of the Huntingtin protein. Here, we polymerize a Gln/Asn-rich recombinant fragment of Rnq1p into beta-sheet-rich amyloid-like aggregates. While the method used for [PSI(+)] and [URE3] infectivity assays did not yield protein-only infection for the Rnq1p aggregates, we did successfully obtain protein-only infection by modifying the protocol. This work proves that [PIN(+)] is a prion mediated by amyloid-like aggregates of Rnq1p, and supports the hypothesis that heterologous prions affect each other's appearance and propagation through interaction of their amyloid-like regions."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.10.069"xsd:string
http://purl.uniprot.org/citations/17097676http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2006.10.069"xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/author"Liebman S.W."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/author"Liebman S.W."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/author"Patel B.K."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/author"Patel B.K."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/pages"773-782"xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/pages"773-782"xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/title"'Prion-proof' for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+]."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/title"'Prion-proof' for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+]."xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/volume"365"xsd:string
http://purl.uniprot.org/citations/17097676http://purl.uniprot.org/core/volume"365"xsd:string
http://purl.uniprot.org/citations/17097676http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17097676
http://purl.uniprot.org/citations/17097676http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17097676
http://purl.uniprot.org/citations/17097676http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17097676
http://purl.uniprot.org/citations/17097676http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17097676
http://purl.uniprot.org/uniprot/P25367http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17097676
http://purl.uniprot.org/uniprot/P25367#attribution-429710DBC6075305D00A616085ABE761http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17097676