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10.1155/2016/2798269 http://scihub22266oqcxt.onion/10.1155/2016/2798269 C4662979!4662979!26649319     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Diabetes+Res 2016 ; 2016 (ä): ä Nephropedia Template TP {{tp|p=26649319|t=2016. Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology |pdf=|usr=}}{{26649319}} gab.com Text Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology JO: J Diabetes Res http://www.kidney.de/pget.php?&tw=1&pmid=26649319 #FOAvip The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose homeostasis but aggregates to form islet amyloid in type-2 diabetes. Islet amyloid formation contributes to ?-cell dysfunction and death in the disease and to the failure of islet transplants. Recent work suggests a role for IAPP aggregation in cardiovascular complications of type-2 diabetes and hints at a possible role in type-1 diabetes. The mechanisms of IAPP amyloid formation in vivo or in vitro are not understood and the mechanisms of IAPP induced ?-cell death are not fully defined. Activation of the inflammasome, defects in autophagy, ER stress, generation of reactive oxygen species, membrane disruption, and receptor mediated mechanisms have all been proposed to play a role. Open questions in the field include the relative importance of the various mechanisms of ?-cell death, the relevance of reductionist biophysical studies to the situation in vivo, the molecular mechanism of amyloid formation in vitro and in vivo, the factors which trigger amyloid formation in type-2 diabetes, the potential role of IAPP in type-1 diabetes, the development of clinically relevant inhibitors of islet amyloidosis toxicity, and the design of soluble, bioactive variants of IAPP for use as adjuncts to insulin therapy. Twit Text FOAVip Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology ????J Diabetes Res http://www.kidney.de/pget.php?&tw=1&pmid=26649319 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26649319 #FOAvip English Wikipedia <ref>{{Cite pmid|26649319}}</ref> Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology #MMPMID26649319 Akter R; Cao P; Noor H; Ridgway Z; Tu LH; Wang H; Wong AG; Zhang X; Abedini A; Schmidt AM; Raleigh DP J Diabetes Res 2016[]; 2016 (ä): ä PMID26649319show ga The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose homeostasis but aggregates to form islet amyloid in type-2 diabetes. Islet amyloid formation contributes to ?-cell dysfunction and death in the disease and to the failure of islet transplants. Recent work suggests a role for IAPP aggregation in cardiovascular complications of type-2 diabetes and hints at a possible role in type-1 diabetes. The mechanisms of IAPP amyloid formation in vivo or in vitro are not understood and the mechanisms of IAPP induced ?-cell death are not fully defined. Activation of the inflammasome, defects in autophagy, ER stress, generation of reactive oxygen species, membrane disruption, and receptor mediated mechanisms have all been proposed to play a role. Open questions in the field include the relative importance of the various mechanisms of ?-cell death, the relevance of reductionist biophysical studies to the situation in vivo, the molecular mechanism of amyloid formation in vitro and in vivo, the factors which trigger amyloid formation in type-2 diabetes, the potential role of IAPP in type-1 diabetes, the development of clinically relevant inhibitors of islet amyloidosis toxicity, and the design of soluble, bioactive variants of IAPP for use as adjuncts to insulin therapy. äIslet Amyloid Polypeptide: Structure, Function, and Pathophysiology (epmc).pdf DeepDyve Pubget Overpricing