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10.1073/pnas.1410159111 http://scihub22266oqcxt.onion/10.1073/pnas.1410159111 C4273401!4273401!25453085     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25453085&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 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (50): 17869-74 Nephropedia Template TP {{tp|p=25453085|t=2014. Crucial role of nonspecific interactions in amyloid nucleation |pdf=|usr=}}{{25453085}} gab.com Text Crucial role of nonspecific interactions in amyloid nucleation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25453085 #FOAvip The assembly of normally soluble proteins into large fibrils, known as amyloid aggregation, is associated with a range of pathologies. Prefibrillar protein oligomers but not the grown fibers are believed to be the main toxic agents. It is unresolved if these oligomers are necessary for fibril assembly or just a dangerous byproduct. We show using computer simulations that, at physiological concentrations, amyloid formation must proceed through a two-step process including prefibrillar oligomers. We find that there is an optimal oligomeric size for amyloid nucleation and that classical nucleation theory cannot be applied to this process. Formation of oligomers and hence, fibrils, is controlled by the strength of nonspecific attractions, whose weakening may be crucial in preventing amyloid aggregation. Twit Text FOAVip Crucial role of nonspecific interactions in amyloid nucleation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25453085 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25453085 #FOAvip English Wikipedia <ref>{{Cite pmid|25453085}}</ref> Crucial role of nonspecific interactions in amyloid nucleation #MMPMID25453085 ?ari? A; Chebaro YC; Knowles TPJ; Frenkel D Proc Natl Acad Sci U S A 2014[Dec]; 111 (50): 17869-74 PMID25453085show ga The assembly of normally soluble proteins into large fibrils, known as amyloid aggregation, is associated with a range of pathologies. Prefibrillar protein oligomers but not the grown fibers are believed to be the main toxic agents. It is unresolved if these oligomers are necessary for fibril assembly or just a dangerous byproduct. We show using computer simulations that, at physiological concentrations, amyloid formation must proceed through a two-step process including prefibrillar oligomers. We find that there is an optimal oligomeric size for amyloid nucleation and that classical nucleation theory cannot be applied to this process. Formation of oligomers and hence, fibrils, is controlled by the strength of nonspecific attractions, whose weakening may be crucial in preventing amyloid aggregation. äCrucial role of nonspecific interactions in amyloid nucleation (epmc).pdf DeepDyve Pubget Overpricing