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10.1371/journal.pone.0132309 http://scihub22266oqcxt.onion/10.1371/journal.pone.0132309 C4501548!4501548!26172440     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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+One 2015 ; 10 (7): ä Nephropedia Template TP {{tp|p=26172440|t=2015. Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry |pdf=|usr=}}{{26172440}} gab.com Text Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26172440 #FOAvip There is an ongoing debate regarding the culprits of cytotoxicity associated with amyloid disorders. Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce cytotoxicity. To investigate membrane disruption and cytotoxic effects associated with intact and fragmented fibrils, the novel in situ spectroscopic technique of Total Internal Reflection Ellipsometry (TIRE) was used. Fibril lipid interactions were monitored using natively derived whole cell membranes as a model of the in vivo environment. We show that fragmented fibrils have an increased ability to disrupt these natively derived membranes by causing a loss of material from the deposited surface when compared with unfragmented fibrils. This effect was corroborated by observations of membrane disruption in live cells, and by dye release assay using synthetic liposomes. Through these studies we demonstrate the use of TIRE for the analysis of protein-lipid interactions on natively derived lipid surfaces, and provide an explanation on how amyloid fibrils can cause a toxic gain of function, while entangled amyloid plaques exert minimal biological activity. Twit Text FOAVip Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26172440 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26172440 #FOAvip English Wikipedia <ref>{{Cite pmid|26172440}}</ref> Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry #MMPMID26172440 Smith RAS; Nabok A; Blakeman BJF; Xue WF; Abell B; Smith DP PLoS One 2015[]; 10 (7): ä PMID26172440show ga There is an ongoing debate regarding the culprits of cytotoxicity associated with amyloid disorders. Although small pre-fibrillar amyloid oligomers have been implicated as the primary toxic species, the fibrillar amyloid material itself can also induce cytotoxicity. To investigate membrane disruption and cytotoxic effects associated with intact and fragmented fibrils, the novel in situ spectroscopic technique of Total Internal Reflection Ellipsometry (TIRE) was used. Fibril lipid interactions were monitored using natively derived whole cell membranes as a model of the in vivo environment. We show that fragmented fibrils have an increased ability to disrupt these natively derived membranes by causing a loss of material from the deposited surface when compared with unfragmented fibrils. This effect was corroborated by observations of membrane disruption in live cells, and by dye release assay using synthetic liposomes. Through these studies we demonstrate the use of TIRE for the analysis of protein-lipid interactions on natively derived lipid surfaces, and provide an explanation on how amyloid fibrils can cause a toxic gain of function, while entangled amyloid plaques exert minimal biological activity. äAnalysis of Toxic Amyloid Fibril Interactions at Natively Derived Memb(epmc).pdf DeepDyve Pubget Overpricing