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10.1371/journal.pone.0187841 http://scihub22266oqcxt.onion/10.1371/journal.pone.0187841 C5683630!5683630!29131828     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+One 2017 ; 12 (11): ä Nephropedia Template TP {{tp|p=29131828|t=2017. Inhibition of HEWL fibril formation by taxifolin: Mechanism of action |pdf=|usr=}}{{29131828}} gab.com Text Inhibition of HEWL fibril formation by taxifolin: Mechanism of action JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=29131828 #FOAvip Among therapeutic approaches for amyloid-related diseases, attention has recently turned to the use of natural products as effective anti-aggregation compounds. Although a wealth of in vitro and in vivo evidence indicates some common inhibitory activity of these compounds, they don?t generally suggest the same mechanism of action. Here, we show that taxifolin, a ubiquitous bioactive constituent of foods and herbs, inhibits formation of HEWL amyloid fibrils and their related toxicity by causing formation of very large globular, chain-like aggregates. A range of amyloid-specific techniques were employed to characterize this process. We found that taxifolin exerts its effect by binding to HEWL prefibrillar species, rather than by stabilizing the molecule in its native-like state. Furthermore, it?s binding results in diverting the amyloid pathway toward formation of very large globular, chain-like aggregates with low ?-sheet content and reduced solvent-exposed hydrophobic patches. ThT fluorescence measurements show that the binding capacity of taxifolin is significantly reduced, upon generation of large protofibrillar aggregates at the end of growth phase. We believe these results may help design promising inhibitors of protein aggregation for amyloid-related diseases. Twit Text FOAVip Inhibition of HEWL fibril formation by taxifolin: Mechanism of action ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=29131828 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29131828 #FOAvip English Wikipedia <ref>{{Cite pmid|29131828}}</ref> Inhibition of HEWL fibril formation by taxifolin: Mechanism of action #MMPMID29131828 Mahdavimehr M; Meratan AA; Ghobeh M; Ghasemi A; Saboury AA; Nemat-Gorgani M PLoS One 2017[]; 12 (11): ä PMID29131828show ga Among therapeutic approaches for amyloid-related diseases, attention has recently turned to the use of natural products as effective anti-aggregation compounds. Although a wealth of in vitro and in vivo evidence indicates some common inhibitory activity of these compounds, they don?t generally suggest the same mechanism of action. Here, we show that taxifolin, a ubiquitous bioactive constituent of foods and herbs, inhibits formation of HEWL amyloid fibrils and their related toxicity by causing formation of very large globular, chain-like aggregates. A range of amyloid-specific techniques were employed to characterize this process. We found that taxifolin exerts its effect by binding to HEWL prefibrillar species, rather than by stabilizing the molecule in its native-like state. Furthermore, it?s binding results in diverting the amyloid pathway toward formation of very large globular, chain-like aggregates with low ?-sheet content and reduced solvent-exposed hydrophobic patches. ThT fluorescence measurements show that the binding capacity of taxifolin is significantly reduced, upon generation of large protofibrillar aggregates at the end of growth phase. We believe these results may help design promising inhibitors of protein aggregation for amyloid-related diseases. äInhibition of HEWL fibril formation by taxifolin: Mechanism of action (epmc).pdf DeepDyve Pubget Overpricing