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10.1002/anie.201511524 http://scihub22266oqcxt.onion/10.1002/anie.201511524 C4864496!4864496!26954430     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26954430&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26954430.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Angew+Chem+Int+Ed+Engl 2016 ; 55 (15): 4822-5 Nephropedia Template TP {{tp|p=26954430|t=2016. Polymorphism of amyloid fibrils in vivo |pdf=|usr=}}{{26954430}} gab.com Text Polymorphism of amyloid fibrils in vivo JO: Angew Chem Int Ed Engl http://www.kidney.de/pget.php?&tw=1&pmid=26954430 #FOAvip Polymorphism is a wide-spread feature of amyloid-like fibrils formed in vitro, but it has so far remained unclear whether the fibrils formed within a patient are also affected by this phenomenon. In this study we show that the amyloid fibrils within a diseased individual can vary considerably in their three-dimensional architecture. We demonstrate this heterogeneity with amyloid fibrils deposited within different organs, formed from sequentially non-homologous polypeptide chains and affecting human or animals. Irrespective of amyloid type or source, we found in vivo fibrils to be polymorphic. These data imply that the chemical principles of fibril assembly that lead to such polymorphism are fundamentally conserved in vivo and in vitro. Twit Text FOAVip Polymorphism of amyloid fibrils in vivo ????Angew Chem Int Ed Engl http://www.kidney.de/pget.php?&tw=1&pmid=26954430 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26954430 #FOAvip English Wikipedia <ref>{{Cite pmid|26954430}}</ref> Polymorphism of amyloid fibrils in vivo #MMPMID26954430 Annamalai K; Gührs KH; Koehler R; Schmidt M; Michel H; Loos C; Gaffney PM; Sigurdson CJ; Hegenbart U; Schönland S; Fändrich M Angew Chem Int Ed Engl 2016[Apr]; 55 (15): 4822-5 PMID26954430show ga Polymorphism is a wide-spread feature of amyloid-like fibrils formed in vitro, but it has so far remained unclear whether the fibrils formed within a patient are also affected by this phenomenon. In this study we show that the amyloid fibrils within a diseased individual can vary considerably in their three-dimensional architecture. We demonstrate this heterogeneity with amyloid fibrils deposited within different organs, formed from sequentially non-homologous polypeptide chains and affecting human or animals. Irrespective of amyloid type or source, we found in vivo fibrils to be polymorphic. These data imply that the chemical principles of fibril assembly that lead to such polymorphism are fundamentally conserved in vivo and in vitro. äPolymorphism of amyloid fibrils in vivo (epmc).pdf DeepDyve Pubget Overpricing