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10.1038/nature14510 http://scihub22266oqcxt.onion/10.1038/nature14510 C4486072!4486072!26061765     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nature 2015 ; 522 (7557): 478-81 Nephropedia Template TP {{tp|p=26061765|t=2015. A naturally occurring variant of the human prion protein completely prevents prion disease |pdf=|usr=}}{{26061765}} gab.com Text A naturally occurring variant of the human prion protein completely prevents prion disease JO: Nature http://www.kidney.de/pget.php?&tw=1&pmid=26061765 #FOAvip Mammalian prions, transmissible agents causing lethal neurodegenerative diseases, are composed of assemblies of misfolded cellular prion protein (PrP) 1. A novel PrP variant, G127V, was under positive evolutionary selection during the epidemic of kuru, an acquired prion disease epidemic of the Fore population in Papua New Guinea, and appeared to provide strong protection against disease in the heterozygous state2. We have now investigated the protective role of this variant and its interaction with the common worldwide M129V PrP polymorphism; V127 was seen exclusively on a M129PRNP allele. Here we demonstrate that transgenic mice expressing both variant and wild type human PrP are completely resistant to both kuru and classical CJD prions (which are closely similar) but can be infected with variant CJD prions, a human prion strain resulting from exposure to BSE prions to which the Fore were not exposed. Remarkably however, mice expressing only PrP V127 were completely resistant to all prion strains demonstrating a different molecular mechanism to M129V, which provides its relative protection against classical CJD and kuru in the heterozygous state. Indeed this single amino acid substitution (G?V) at a residue invariant in vertebrate evolution is as protective as deletion of the protein. Further study in transgenic mice expressing different ratios of variant and wild type PrP indicates that not only is PrP V127 completely refractory to prion conversion, but acts as a potent dose-dependent inhibitor of wild type prion propagation. Twit Text FOAVip A naturally occurring variant of the human prion protein completely prevents prion disease ????Nature http://www.kidney.de/pget.php?&tw=1&pmid=26061765 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26061765 #FOAvip English Wikipedia <ref>{{Cite pmid|26061765}}</ref> A naturally occurring variant of the human prion protein completely prevents prion disease #MMPMID26061765 Asante EA; Smidak M; Grimshaw A; Houghton R; Tomlinson A; Jeelani A; Jakubcova T; Hamdan S; Richard-Londt A; Linehan JM; Brandner S; Alpers M; Whitfield J; Mead S; Wadsworth JD; Collinge J Nature 2015[Jun]; 522 (7557): 478-81 PMID26061765show ga Mammalian prions, transmissible agents causing lethal neurodegenerative diseases, are composed of assemblies of misfolded cellular prion protein (PrP) 1. A novel PrP variant, G127V, was under positive evolutionary selection during the epidemic of kuru, an acquired prion disease epidemic of the Fore population in Papua New Guinea, and appeared to provide strong protection against disease in the heterozygous state2. We have now investigated the protective role of this variant and its interaction with the common worldwide M129V PrP polymorphism; V127 was seen exclusively on a M129PRNP allele. Here we demonstrate that transgenic mice expressing both variant and wild type human PrP are completely resistant to both kuru and classical CJD prions (which are closely similar) but can be infected with variant CJD prions, a human prion strain resulting from exposure to BSE prions to which the Fore were not exposed. Remarkably however, mice expressing only PrP V127 were completely resistant to all prion strains demonstrating a different molecular mechanism to M129V, which provides its relative protection against classical CJD and kuru in the heterozygous state. Indeed this single amino acid substitution (G?V) at a residue invariant in vertebrate evolution is as protective as deletion of the protein. Further study in transgenic mice expressing different ratios of variant and wild type PrP indicates that not only is PrP V127 completely refractory to prion conversion, but acts as a potent dose-dependent inhibitor of wild type prion propagation. äA naturally occurring variant of the human prion protein completely pr(epmc).pdf DeepDyve Pubget Overpricing