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10.1101/cshperspect.a021774 http://scihub22266oqcxt.onion/10.1101/cshperspect.a021774 C4817803!4817803!27037416     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cold+Spring+Harb+Perspect+Biol 2016 ; 8 (4): ä Nephropedia Template TP {{tp|p=27037416|t=2016. The Role of Functional Prion-Like Proteins in the Persistence of Memory |pdf=|usr=}}{{27037416}} gab.com Text The Role of Functional Prion-Like Proteins in the Persistence of Memory JO: Cold Spring Harb Perspect Biol http://www.kidney.de/pget.php?&tw=1&pmid=27037416 #FOAvip Prions are a self-templating amyloidogenic state of normal cellular proteins, such as prion protein (PrP). They have been identified as the pathogenic agents, contributing to a number of diseases of the nervous system. However, the discovery that the neuronal RNA-binding protein, cytoplasmic polyadenylation element-binding protein (CPEB), has a prion-like state that is involved in the stabilization of memory raised the possibility that prion-like proteins can serve normal physiological functions in the nervous system. Here, we review recent experimental evidence of prion-like properties of neuronal CPEB in various organisms and propose a model of how the prion-like state may stabilize memory. Twit Text FOAVip The Role of Functional Prion-Like Proteins in the Persistence of Memory ????Cold Spring Harb Perspect Biol http://www.kidney.de/pget.php?&tw=1&pmid=27037416 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27037416 #FOAvip English Wikipedia <ref>{{Cite pmid|27037416}}</ref> The Role of Functional Prion-Like Proteins in the Persistence of Memory #MMPMID27037416 Si K; Kandel ER Cold Spring Harb Perspect Biol 2016[Apr]; 8 (4): ä PMID27037416show ga Prions are a self-templating amyloidogenic state of normal cellular proteins, such as prion protein (PrP). They have been identified as the pathogenic agents, contributing to a number of diseases of the nervous system. However, the discovery that the neuronal RNA-binding protein, cytoplasmic polyadenylation element-binding protein (CPEB), has a prion-like state that is involved in the stabilization of memory raised the possibility that prion-like proteins can serve normal physiological functions in the nervous system. Here, we review recent experimental evidence of prion-like properties of neuronal CPEB in various organisms and propose a model of how the prion-like state may stabilize memory. äThe Role of Functional Prion-Like Proteins in the Persistence of Memor(epmc).pdf DeepDyve Pubget Overpricing