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10.1038/s41598-017-09489-3 http://scihub22266oqcxt.onion/10.1038/s41598-017-09489-3 C5575253!5575253 !28851967     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28851967 &cmd=llinks): Failed to open stream: HTTP request failed! 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Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome |pdf=|usr=}}{{28851967 }} gab.com Text Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28851967 #FOAvip Human transmissible spongiform encephalopathies (TSEs) or prion diseases are a group of fatal neurodegenerative disorders that include Kuru, Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker syndrome (GSS), and fatal familial insomnia. GSS is a genetically determined TSE caused by a range of mutations within the prion protein (PrP) gene. Several animal models, based on the expression of PrPs carrying mutations analogous to human heritable prion diseases, support that mutations might predispose PrP to spontaneously misfold. An adapted Protein Misfolding Cyclic Amplification methodology based on the use of human recombinant PrP (recPMCA) generated different self-propagating misfolded proteins spontaneously. These were characterized biochemically and structurally, and the one partially sharing some of the GSS PrP(Sc) molecular features was inoculated into different animal models showing high infectivity. This constitutes an infectious recombinant prion which could be an invaluable model for understanding GSS. Moreover, this study proves the possibility to generate recombinant versions of other human prion diseases that could provide a further understanding on the molecular features of these devastating disorders. Twit Text FOAVip Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28851967 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28851967 #FOAvip English Wikipedia <ref>{{Cite pmid|28851967 }}</ref> Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome #MMPMID28851967 Elezgarai SR ; Fernández-Borges N ; Eraña H ; Sevillano AM ; Charco JM ; Harrathi C ; Saá P ; Gil D ; Kong Q ; Requena JR ; Andréoletti O ; Castilla J Sci Rep 2017[Aug]; 7 (1 ): 9584 PMID28851967 show ga Human transmissible spongiform encephalopathies (TSEs) or prion diseases are a group of fatal neurodegenerative disorders that include Kuru, Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker syndrome (GSS), and fatal familial insomnia. GSS is a genetically determined TSE caused by a range of mutations within the prion protein (PrP) gene. Several animal models, based on the expression of PrPs carrying mutations analogous to human heritable prion diseases, support that mutations might predispose PrP to spontaneously misfold. An adapted Protein Misfolding Cyclic Amplification methodology based on the use of human recombinant PrP (recPMCA) generated different self-propagating misfolded proteins spontaneously. These were characterized biochemically and structurally, and the one partially sharing some of the GSS PrP(Sc) molecular features was inoculated into different animal models showing high infectivity. This constitutes an infectious recombinant prion which could be an invaluable model for understanding GSS. Moreover, this study proves the possibility to generate recombinant versions of other human prion diseases that could provide a further understanding on the molecular features of these devastating disorders. |*Recombination, Genetic [MESH] |Amino Acid Substitution [MESH] |Animals [MESH] |Disease Models, Animal [MESH] |Evolution, Molecular [MESH] |Gerstmann-Straussler-Scheinker Disease/*etiology/metabolism/pathology [MESH] |Humans [MESH] |Mice [MESH] |Mice, Transgenic [MESH] |Mutation [MESH] |Prion Proteins/chemistry/*genetics/metabolism [MESH] |Protein Aggregates [MESH] |Protein Aggregation, Pathological [MESH] |Protein Conformation [MESH] |Protein Folding [MESH]Generation of a new infectious recombinant prion: a model to understan(epmc).pdf DeepDyve Pubget Overpricing