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10.4161/19336896.2014.968464 http://scihub22266oqcxt.onion/10.4161/19336896.2014.968464 C4601197!4601197!24831240     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24831240.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Prion 2014 ; 8 (3): 233-9 Nephropedia Template TP {{tp|p=24831240|t=2014. When amyloids become prions |pdf=|usr=}}{{24831240}} gab.com Text When amyloids become prions JO: Prion http://www.kidney.de/pget.php?&tw=1&pmid=24831240 #FOAvip The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer's disease (AD), to highly infectious ones, such as human transmissible spongiform encephalopathies (TSEs). They are commonly known as prion diseases. However, since all amyloids could be considered prions (from those involved in cell-to-cell transmission to those responsible for real neuronal invasion), it is necessary to find an underlying cause of the different capacity to infect that each of the proteins prone to form amyloids has. As proposed here, both the intrinsic cytotoxicity and the number of nuclei of aggregation per cell could be key factors in this transmission capacity of each amyloid. Twit Text FOAVip When amyloids become prions ????Prion http://www.kidney.de/pget.php?&tw=1&pmid=24831240 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24831240 #FOAvip English Wikipedia <ref>{{Cite pmid|24831240}}</ref> When amyloids become prions #MMPMID24831240 Sabate R Prion 2014[May]; 8 (3): 233-9 PMID24831240show ga The conformational diseases, linked to protein aggregation into amyloid conformations, range from non-infectious neurodegenerative disorders, such as Alzheimer's disease (AD), to highly infectious ones, such as human transmissible spongiform encephalopathies (TSEs). They are commonly known as prion diseases. However, since all amyloids could be considered prions (from those involved in cell-to-cell transmission to those responsible for real neuronal invasion), it is necessary to find an underlying cause of the different capacity to infect that each of the proteins prone to form amyloids has. As proposed here, both the intrinsic cytotoxicity and the number of nuclei of aggregation per cell could be key factors in this transmission capacity of each amyloid. äWhen amyloids become prions (epmc).pdf DeepDyve Pubget Overpricing