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10.1098/rsos.160696 http://scihub22266oqcxt.onion/10.1098/rsos.160696 C5319338!5319338!28280572     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28280572&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 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       R+Soc+Open+Sci 2017 ; 4 (1): ä Nephropedia Template TP {{tp|p=28280572|t=2017. Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation |pdf=|usr=}}{{28280572}} gab.com Text Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation JO: R Soc Open Sci http://www.kidney.de/pget.php?&tw=1&pmid=28280572 #FOAvip Formation of amyloid fibrils underlies a wide range of human disorders, including Alzheimer's and prion diseases. The amyloid fibrils can be readily detected thanks to thioflavin T (ThT), a small molecule that gives strong fluorescence upon binding to amyloids. Using the amyloid fibrils of A?40 and A?42 involved in Alzheimer's disease, and of yeast prion protein Ure2, here we study three aspects of ThT binding to amyloids: quantification of amyloid fibrils using ThT, the optimal ThT concentration for monitoring amyloid formation and the effect of ThT on aggregation kinetics. We show that ThT fluorescence correlates linearly with amyloid concentration over ThT concentrations ranging from 0.2 to 500?µM. At a given amyloid concentration, the plot of ThT fluorescence versus ThT concentration exhibits a bell-shaped curve. The maximal fluorescence signal depends mostly on the total ThT concentration, rather than amyloid to ThT ratio. For the three proteins investigated, the maximal fluorescence is observed at ThT concentrations of 20?50?µM. Aggregation kinetics experiments in the presence of different ThT concentrations show that ThT has little effect on aggregation at concentrations of 20?µM or lower. ThT at concentrations of 50?µM or more could affect the shape of the aggregation curves, but this effect is protein-dependent and not universal. Twit Text FOAVip Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation ????R Soc Open Sci http://www.kidney.de/pget.php?&tw=1&pmid=28280572 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28280572 #FOAvip English Wikipedia <ref>{{Cite pmid|28280572}}</ref> Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation #MMPMID28280572 Xue C; Lin TY; Chang D; Guo Z R Soc Open Sci 2017[Jan]; 4 (1): ä PMID28280572show ga Formation of amyloid fibrils underlies a wide range of human disorders, including Alzheimer's and prion diseases. The amyloid fibrils can be readily detected thanks to thioflavin T (ThT), a small molecule that gives strong fluorescence upon binding to amyloids. Using the amyloid fibrils of A?40 and A?42 involved in Alzheimer's disease, and of yeast prion protein Ure2, here we study three aspects of ThT binding to amyloids: quantification of amyloid fibrils using ThT, the optimal ThT concentration for monitoring amyloid formation and the effect of ThT on aggregation kinetics. We show that ThT fluorescence correlates linearly with amyloid concentration over ThT concentrations ranging from 0.2 to 500?µM. At a given amyloid concentration, the plot of ThT fluorescence versus ThT concentration exhibits a bell-shaped curve. The maximal fluorescence signal depends mostly on the total ThT concentration, rather than amyloid to ThT ratio. For the three proteins investigated, the maximal fluorescence is observed at ThT concentrations of 20?50?µM. Aggregation kinetics experiments in the presence of different ThT concentrations show that ThT has little effect on aggregation at concentrations of 20?µM or lower. ThT at concentrations of 50?µM or more could affect the shape of the aggregation curves, but this effect is protein-dependent and not universal. äThioflavin T as an amyloid dye: fibril quantification, optimal concent(epmc).pdf DeepDyve Pubget Overpricing