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10.1038/srep24656 http://scihub22266oqcxt.onion/10.1038/srep24656 C4838910!4838910 !27098162     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 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27098162 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2016 ; 6 (ä): 24656 Nephropedia Template TP {{tp|p=27098162 |t=2016. Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones |pdf=|usr=}}{{27098162 }} gab.com Text Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27098162 #FOAvip Polypeptide aggregation into amyloid is linked with several debilitating human diseases. Despite the inherent risk of aggregation-induced cytotoxicity, bacteria control the export of amyloid-prone subunits and assemble adhesive amyloid fibres during biofilm formation. An Escherichia protein, CsgC potently inhibits amyloid formation of curli amyloid proteins. Here we unlock its mechanism of action, and show that CsgC strongly inhibits primary nucleation via electrostatically-guided molecular encounters, which expands the conformational distribution of disordered curli subunits. This delays the formation of higher order intermediates and maintains amyloidogenic subunits in a secretion-competent form. New structural insight also reveal that CsgC is part of diverse family of bacterial amyloid inhibitors. Curli assembly is therefore not only arrested in the periplasm, but the preservation of conformational flexibility also enables efficient secretion to the cell surface. Understanding how bacteria safely handle amyloidogenic polypeptides contribute towards efforts to control aggregation in disease-causing amyloids and amyloid-based biotechnological applications. Twit Text FOAVip Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27098162 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27098162 #FOAvip English Wikipedia <ref>{{Cite pmid|27098162 }}</ref> Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones #MMPMID27098162 Taylor JD ; Hawthorne WJ ; Lo J ; Dear A ; Jain N ; Meisl G ; Andreasen M ; Fletcher C ; Koch M ; Darvill N ; Scull N ; Escalera-Maurer A ; Sefer L ; Wenman R ; Lambert S ; Jean J ; Xu Y ; Turner B ; Kazarian SG ; Chapman MR ; Bubeck D ; de Simone A ; Knowles TP ; Matthews SJ Sci Rep 2016[Apr]; 6 (ä): 24656 PMID27098162 show ga Polypeptide aggregation into amyloid is linked with several debilitating human diseases. Despite the inherent risk of aggregation-induced cytotoxicity, bacteria control the export of amyloid-prone subunits and assemble adhesive amyloid fibres during biofilm formation. An Escherichia protein, CsgC potently inhibits amyloid formation of curli amyloid proteins. Here we unlock its mechanism of action, and show that CsgC strongly inhibits primary nucleation via electrostatically-guided molecular encounters, which expands the conformational distribution of disordered curli subunits. This delays the formation of higher order intermediates and maintains amyloidogenic subunits in a secretion-competent form. New structural insight also reveal that CsgC is part of diverse family of bacterial amyloid inhibitors. Curli assembly is therefore not only arrested in the periplasm, but the preservation of conformational flexibility also enables efficient secretion to the cell surface. Understanding how bacteria safely handle amyloidogenic polypeptides contribute towards efforts to control aggregation in disease-causing amyloids and amyloid-based biotechnological applications. |*Static Electricity [MESH] |Active Transport, Cell Nucleus [MESH] |Amyloid/*chemistry/classification/genetics/metabolism [MESH] |Escherichia coli Proteins/*chemistry/metabolism [MESH] |Kinetics [MESH] |Molecular Chaperones/*chemistry/metabolism [MESH] |Osmolar Concentration [MESH] |Protein Binding [MESH] |Protein Conformation [MESH]Electrostatically-guided inhibition of Curli amyloid nucleation by the(epmc).pdf DeepDyve Pubget Overpricing