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10.1016/j.tcb.2017.03.001 http://scihub22266oqcxt.onion/10.1016/j.tcb.2017.03.001 C5476492!5476492 !28359692     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28359692 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Trends+Cell+Biol 2017 ; 27 (7 ): 465-467 Nephropedia Template TP {{tp|p=28359692 |t=2017. Disentangling a Bad Reputation: Changing Perceptions of Amyloids |pdf=|usr=}}{{28359692 }} gab.com Text Disentangling a Bad Reputation: Changing Perceptions of Amyloids JO: Trends Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=28359692 #FOAvip Historically, amyloids were perceived as toxic/irreversible protein aggregates associated with neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Recent papers are challenging this perception by uncovering widespread cellular roles for physiological amyloidogenesis. These findings suggest that the amyloid-fold should be considered, alongside the native-fold and unfolded configurations, as a physiological and reversible protein organization. Twit Text FOAVip Disentangling a Bad Reputation: Changing Perceptions of Amyloids ????Trends Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=28359692 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28359692 #FOAvip English Wikipedia <ref>{{Cite pmid|28359692 }}</ref> Disentangling a Bad Reputation: Changing Perceptions of Amyloids #MMPMID28359692 Wang M ; Audas TE ; Lee S Trends Cell Biol 2017[Jul]; 27 (7 ): 465-467 PMID28359692 show ga Historically, amyloids were perceived as toxic/irreversible protein aggregates associated with neurodegenerative disorders including Alzheimer's and Parkinson's diseases. Recent papers are challenging this perception by uncovering widespread cellular roles for physiological amyloidogenesis. These findings suggest that the amyloid-fold should be considered, alongside the native-fold and unfolded configurations, as a physiological and reversible protein organization. |Amyloid/genetics/*metabolism [MESH] |Amyloidosis/genetics [MESH] |Humans [MESH] |Neurodegenerative Diseases/metabolism/pathology [MESH] |Protein Aggregates [MESH]Disentangling a Bad Reputation: Changing Perceptions of Amyloids (epmc).pdf DeepDyve Pubget Overpricing