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10.1021/bi5011442 http://scihub22266oqcxt.onion/10.1021/bi5011442 C4318585!4318585 !25541905     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25541905 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochemistry 2015 ; 54 (4 ): 987-93 Nephropedia Template TP {{tp|p=25541905 |t=2015. Peptide amyloid surface display |pdf=|usr=}}{{25541905 }} gab.com Text Peptide amyloid surface display JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=25541905 #FOAvip Homomeric self-assembly of peptides into amyloid fibers is a feature of many diseases. A central role has been suggested for the lateral fiber surface affecting gains of toxic function. To investigate this, a protein scaffold that presents a discrete, parallel ?-sheet surface for amyloid subdomains up to eight residues in length has been designed. Scaffolds that present the fiber surface of islet amyloid polypeptide (IAPP) were prepared. The designs show sequence-specific surface effects apparent in that they gain the capacity to attenuate rates of IAPP self-assembly in solution and affect IAPP-induced toxicity in insulin-secreting cells. Twit Text FOAVip Peptide amyloid surface display ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=25541905 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25541905 #FOAvip English Wikipedia <ref>{{Cite pmid|25541905 }}</ref> Peptide amyloid surface display #MMPMID25541905 Rubio MA ; Schlamadinger DE ; White EM ; Miranker AD Biochemistry 2015[Feb]; 54 (4 ): 987-93 PMID25541905 show ga Homomeric self-assembly of peptides into amyloid fibers is a feature of many diseases. A central role has been suggested for the lateral fiber surface affecting gains of toxic function. To investigate this, a protein scaffold that presents a discrete, parallel ?-sheet surface for amyloid subdomains up to eight residues in length has been designed. Scaffolds that present the fiber surface of islet amyloid polypeptide (IAPP) were prepared. The designs show sequence-specific surface effects apparent in that they gain the capacity to attenuate rates of IAPP self-assembly in solution and affect IAPP-induced toxicity in insulin-secreting cells. |Animals [MESH] |Cattle [MESH] |Cell Line, Tumor [MESH] |Humans [MESH] |Islet Amyloid Polypeptide/antagonists & inhibitors/*chemistry/*metabolism [MESH] |Peptides/antagonists & inhibitors/chemistry/metabolism [MESH] |Protein Structure, Secondary [MESH] |Rats [MESH] |Serum Albumin, Bovine/pharmacology [MESH]Peptide amyloid surface display (epmc).pdf DeepDyve Pubget Overpricing