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10.1007/s12551-017-0289-z http://scihub22266oqcxt.onion/10.1007/s12551-017-0289-z C5578932!5578932!28812278     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+Rev 2017 ; 9 (4): 329-38 Nephropedia Template TP {{tp|p=28812278|t=2017. Monomer-dependent secondary nucleation in amyloid formation |pdf=|usr=}}{{28812278}} gab.com Text Monomer-dependent secondary nucleation in amyloid formation JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28812278 #FOAvip Secondary nucleation of monomers on the surface of an already existing aggregate that is formed from the same kind of monomers may lead to autocatalytic amplification of a self-assembly process. Such monomer-dependent secondary nucleation occurs during the crystallization of small molecules or proteins and self-assembled materials, as well as in protein self-assembly into fibrous structures. Indications of secondary nucleation may come from analyses of kinetic experiments starting from pure monomers or monomers supplemented with a low concentration of pre-formed aggregates (seeds). More firm evidence requires additional experiments, for example those employing isotope labels to distinguish new aggregates arising from the monomer from those resulting from fragmentation of the seed. In cases of amyloid formation, secondary nucleation leads to the formation of toxic oligomers, and inhibitors of secondary nucleation may serve as starting points for therapeutic developments. Secondary nucleation displays a high degree of structural specificity and may be enhanced by mutations or screening of electrostatic repulsion. Twit Text FOAVip Monomer-dependent secondary nucleation in amyloid formation ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28812278 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28812278 #FOAvip English Wikipedia <ref>{{Cite pmid|28812278}}</ref> Monomer-dependent secondary nucleation in amyloid formation #MMPMID28812278 Linse S Biophys Rev 2017[Aug]; 9 (4): 329-38 PMID28812278show ga Secondary nucleation of monomers on the surface of an already existing aggregate that is formed from the same kind of monomers may lead to autocatalytic amplification of a self-assembly process. Such monomer-dependent secondary nucleation occurs during the crystallization of small molecules or proteins and self-assembled materials, as well as in protein self-assembly into fibrous structures. Indications of secondary nucleation may come from analyses of kinetic experiments starting from pure monomers or monomers supplemented with a low concentration of pre-formed aggregates (seeds). More firm evidence requires additional experiments, for example those employing isotope labels to distinguish new aggregates arising from the monomer from those resulting from fragmentation of the seed. In cases of amyloid formation, secondary nucleation leads to the formation of toxic oligomers, and inhibitors of secondary nucleation may serve as starting points for therapeutic developments. Secondary nucleation displays a high degree of structural specificity and may be enhanced by mutations or screening of electrostatic repulsion. äMonomer-dependent secondary nucleation in amyloid formation (epmc).pdf DeepDyve Pubget Overpricing