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10.1128/MCB.00206-17 http://scihub22266oqcxt.onion/10.1128/MCB.00206-17 C5615180!5615180!28716950     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell+Biol 2017 ; 37 (20): ä Nephropedia Template TP {{tp|p=28716950|t=2017. Analysis of Small Critical Regions of Swi1 Conferring Prion Formation, Maintenance, and Transmission |pdf=|usr=}}{{28716950}} gab.com Text Analysis of Small Critical Regions of Swi1 Conferring Prion Formation, Maintenance, and Transmission JO: Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=28716950 #FOAvip Saccharomyces cerevisiae contains several prion elements, which are epigenetically transmitted as self-perpetuating protein conformations. One such prion is [SWI+], whose protein determinant is Swi1, a subunit of the SWI/SNF chromatin-remodeling complex. We previously reported that [SWI+] formation results in a partial loss-of-function phenotype of poor growth in nonglucose medium and abolishment of multicellular features. We also showed that the first 38 amino acids of Swi1 propagated [SWI+]. We show here that a region as small as the first 32 amino acids of Swi1 (Swi11?32) can decorate [SWI+] aggregation and stably maintain and transmit [SWI+] independently of full-length Swi1. Regions smaller than Swi11?32 are either incapable of aggregation or unstably propagate [SWI+]. When fused to Sup35MC, the [PSI+] determinant lacking its PrD, Swi11?31 and Swi11?32 can act as transferable prion domains (PrDs). The resulting fusions give rise to a novel chimeric prion, [SPS+], exhibiting [PSI+]-like nonsense suppression. Thus, an NH2-terminal region of ?30 amino acids of Swi1 contains all the necessary information for in vivo prion formation, maintenance, and transmission. This PrD is unique in size and composition: glutamine free, asparagine rich, and the smallest defined to date. Our findings broaden our understanding of what features allow a protein region to serve as a PrD. Twit Text FOAVip Analysis of Small Critical Regions of Swi1 Conferring Prion Formation, Maintenance, and Transmission ????Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=28716950 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28716950 #FOAvip English Wikipedia <ref>{{Cite pmid|28716950}}</ref> Analysis of Small Critical Regions of Swi1 Conferring Prion Formation, Maintenance, and Transmission #MMPMID28716950 Valtierra S; Du Z; Li L Mol Cell Biol 2017[Oct]; 37 (20): ä PMID28716950show ga Saccharomyces cerevisiae contains several prion elements, which are epigenetically transmitted as self-perpetuating protein conformations. One such prion is [SWI+], whose protein determinant is Swi1, a subunit of the SWI/SNF chromatin-remodeling complex. We previously reported that [SWI+] formation results in a partial loss-of-function phenotype of poor growth in nonglucose medium and abolishment of multicellular features. We also showed that the first 38 amino acids of Swi1 propagated [SWI+]. We show here that a region as small as the first 32 amino acids of Swi1 (Swi11?32) can decorate [SWI+] aggregation and stably maintain and transmit [SWI+] independently of full-length Swi1. Regions smaller than Swi11?32 are either incapable of aggregation or unstably propagate [SWI+]. When fused to Sup35MC, the [PSI+] determinant lacking its PrD, Swi11?31 and Swi11?32 can act as transferable prion domains (PrDs). The resulting fusions give rise to a novel chimeric prion, [SPS+], exhibiting [PSI+]-like nonsense suppression. Thus, an NH2-terminal region of ?30 amino acids of Swi1 contains all the necessary information for in vivo prion formation, maintenance, and transmission. This PrD is unique in size and composition: glutamine free, asparagine rich, and the smallest defined to date. Our findings broaden our understanding of what features allow a protein region to serve as a PrD. äAnalysis of Small Critical Regions of Swi1 Conferring Prion Formation,(epmc).pdf DeepDyve Pubget Overpricing