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10.1371/journal.pone.0200251 http://scihub22266oqcxt.onion/10.1371/journal.pone.0200251 C6034844!6034844!29979775     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+One 2018 ; 13 (7): ä Nephropedia Template TP {{tp|p=29979775|t=2018. Soluble amyloid-beta buffering by plaques in Alzheimer disease dementia versus high-pathology controls |pdf=|usr=}}{{29979775}} gab.com Text Soluble amyloid-beta buffering by plaques in Alzheimer disease dementia versus high-pathology controls JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=29979775 #FOAvip An unanswered question regarding Alzheimer disease dementia (ADD) is whether amyloid-beta (A?) plaques sequester toxic soluble A? species early during pathological progression. We previously reported that the concentration of soluble A? aggregates from patients with mild dementia was higher than soluble A? aggregates from patients with modest A? plaque burden but no dementia. The ratio of soluble A? aggregate concentration to A? plaque area fully distinguished these groups of patients. We hypothesized that initially plaques may serve as a reservoir or sink for toxic soluble A? aggregates, sequestering them from other targets in the extracellular space and thereby preventing their toxicity. To initially test a generalized version of this hypothesis, we have performed binding assessments using biotinylated synthetic A?1?42 peptide. A?1-42-biotin peptide was incubated on unfixed frozen sections from non-demented high plaque pathology controls and patients with ADD. The bound peptide was measured using ELISA and confocal microscopy. We observed no quantitative difference in A? binding between the groups using either method. Further testing of the buffering hypothesis using various forms of synthetic and human derived soluble A? aggregates will be required to definitively address the role of plaque buffering as it relates to ADD. Twit Text FOAVip Soluble amyloid-beta buffering by plaques in Alzheimer disease dementia versus high-pathology controls ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=29979775 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29979775 #FOAvip English Wikipedia <ref>{{Cite pmid|29979775}}</ref> Soluble amyloid-beta buffering by plaques in Alzheimer disease dementia versus high-pathology controls #MMPMID29979775 Esparza TJ; Gangolli M; Cairns NJ; Brody DL PLoS One 2018[]; 13 (7): ä PMID29979775show ga An unanswered question regarding Alzheimer disease dementia (ADD) is whether amyloid-beta (A?) plaques sequester toxic soluble A? species early during pathological progression. We previously reported that the concentration of soluble A? aggregates from patients with mild dementia was higher than soluble A? aggregates from patients with modest A? plaque burden but no dementia. The ratio of soluble A? aggregate concentration to A? plaque area fully distinguished these groups of patients. We hypothesized that initially plaques may serve as a reservoir or sink for toxic soluble A? aggregates, sequestering them from other targets in the extracellular space and thereby preventing their toxicity. To initially test a generalized version of this hypothesis, we have performed binding assessments using biotinylated synthetic A?1?42 peptide. A?1-42-biotin peptide was incubated on unfixed frozen sections from non-demented high plaque pathology controls and patients with ADD. The bound peptide was measured using ELISA and confocal microscopy. We observed no quantitative difference in A? binding between the groups using either method. Further testing of the buffering hypothesis using various forms of synthetic and human derived soluble A? aggregates will be required to definitively address the role of plaque buffering as it relates to ADD. äSoluble amyloid-beta buffering by plaques in Alzheimer disease dementi(epmc).pdf DeepDyve Pubget Overpricing