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10.1371/journal.pone.0136602 http://scihub22266oqcxt.onion/10.1371/journal.pone.0136602 C4551895!4551895!26313643     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       PLoS+One 2015 ; 10 (8): ä Nephropedia Template TP {{tp|p=26313643|t=2015. pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils |pdf=|usr=}}{{26313643}} gab.com Text pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26313643 #FOAvip Prions are infective proteins, which can self-assemble into different strain conformations, leading to different disease phenotypes. An increasing number of studies suggest that prion-like self-propagation may be a common feature of amyloid-like structures. Thus it is important to unravel every possible factor leading to the formation of different amyloid strains. Here we report on the formation of two types of insulin amyloid-like fibrils with distinct infrared spectroscopic features grown under slightly different pH conditions. Similar to prion strains, both insulin fibril types are able to self-propagate their conformational template under conditions, favoring spontaneous formation of different type fibrils. The low-pH-induced insulin amyloid strain is structurally very similar to previously reported strains formed either in the presence of 20% ethanol, or by modification of the amino acid sequence of insulin. A deeper analysis of literature data in the context of our current findings suggests a shift of the monomer-dimer equilibrium of insulin as a possible factor controlling the formation of different strains. Twit Text FOAVip pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26313643 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26313643 #FOAvip English Wikipedia <ref>{{Cite pmid|26313643}}</ref> pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils #MMPMID26313643 Sneideris T; Darguzis D; Botyriute A; Grigaliunas M; Winter R; Smirnovas V PLoS One 2015[]; 10 (8): ä PMID26313643show ga Prions are infective proteins, which can self-assemble into different strain conformations, leading to different disease phenotypes. An increasing number of studies suggest that prion-like self-propagation may be a common feature of amyloid-like structures. Thus it is important to unravel every possible factor leading to the formation of different amyloid strains. Here we report on the formation of two types of insulin amyloid-like fibrils with distinct infrared spectroscopic features grown under slightly different pH conditions. Similar to prion strains, both insulin fibril types are able to self-propagate their conformational template under conditions, favoring spontaneous formation of different type fibrils. The low-pH-induced insulin amyloid strain is structurally very similar to previously reported strains formed either in the presence of 20% ethanol, or by modification of the amino acid sequence of insulin. A deeper analysis of literature data in the context of our current findings suggests a shift of the monomer-dimer equilibrium of insulin as a possible factor controlling the formation of different strains. äpH-Driven Polymorphism of Insulin Amyloid-Like Fibrils (epmc).pdf DeepDyve Pubget Overpricing