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10.1021/acschemneuro.5b00324 http://scihub22266oqcxt.onion/10.1021/acschemneuro.5b00324 C4800427!4800427!26800462     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 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Chem+Neurosci 2016 ; 7 (3): 399-406 Nephropedia Template TP {{tp|p=26800462|t=2016. Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids |pdf=|usr=}}{{26800462}} gab.com Text Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids JO: ACS Chem Neurosci http://www.kidney.de/pget.php?&tw=1&pmid=26800462 #FOAvip The misfolding and aggregation of proteins into amyloid fibrils characterizes many neurodegenerative disorders such as Parkinson?s and Alzheimer?s diseases. We report here a method, termed SAVE (single aggregate visualization by enhancement) imaging, for the ultrasensitive detection of individual amyloid fibrils and oligomers using single-molecule fluorescence microscopy. We demonstrate that this method is able to detect the presence of amyloid aggregates of ?-synuclein, tau, and amyloid-?. In addition, we show that aggregates can also be identified in human cerebrospinal fluid (CSF). Significantly, we see a twofold increase in the average aggregate concentration in CSF from Parkinson?s disease patients compared to age-matched controls. Taken together, we conclude that this method provides an opportunity to characterize the structural nature of amyloid aggregates in a key biofluid, and therefore has the potential to study disease progression in both animal models and humans to enhance our understanding of neurodegenerative disorders. Twit Text FOAVip Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids ????ACS Chem Neurosci http://www.kidney.de/pget.php?&tw=1&pmid=26800462 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26800462 #FOAvip English Wikipedia <ref>{{Cite pmid|26800462}}</ref> Single-Molecule Imaging of Individual Amyloid Protein Aggregates in Human Biofluids #MMPMID26800462 Horrocks M; Lee SF; Gandhi S; Magdalinou NK; Chen SW; Devine MJ; Tosatto L; Kjaergaard M; Beckwith J; Zetterberg H; Iljina M; Cremades N; Dobson C; Wood NW; Klenerman D ACS Chem Neurosci 2016[Mar]; 7 (3): 399-406 PMID26800462show ga The misfolding and aggregation of proteins into amyloid fibrils characterizes many neurodegenerative disorders such as Parkinson?s and Alzheimer?s diseases. We report here a method, termed SAVE (single aggregate visualization by enhancement) imaging, for the ultrasensitive detection of individual amyloid fibrils and oligomers using single-molecule fluorescence microscopy. We demonstrate that this method is able to detect the presence of amyloid aggregates of ?-synuclein, tau, and amyloid-?. In addition, we show that aggregates can also be identified in human cerebrospinal fluid (CSF). Significantly, we see a twofold increase in the average aggregate concentration in CSF from Parkinson?s disease patients compared to age-matched controls. Taken together, we conclude that this method provides an opportunity to characterize the structural nature of amyloid aggregates in a key biofluid, and therefore has the potential to study disease progression in both animal models and humans to enhance our understanding of neurodegenerative disorders. äSingle-Molecule Imaging of Individual Amyloid Protein Aggregates in Hu(epmc).pdf DeepDyve Pubget Overpricing