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10.1038/s41598-017-10422-x http://scihub22266oqcxt.onion/10.1038/s41598-017-10422-x C5572664!5572664!28842697     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2017 ; 7 (ä): ä Nephropedia Template TP {{tp|p=28842697|t=2017. Diversity of Amyloid-beta Proteoforms in the Alzheimer?s Disease Brain |pdf=|usr=}}{{28842697}} gab.com Text Diversity of Amyloid-beta Proteoforms in the Alzheimer s Disease Brain JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28842697 #FOAvip Amyloid-beta (A?) plays a key role in the pathogenesis of Alzheimer?s disease (AD), but little is known about the proteoforms present in AD brain. We used high-resolution mass spectrometry to analyze intact A? from soluble aggregates and insoluble material in brains of six cases with severe dementia and pathologically confirmed AD. The soluble aggregates are especially relevant because they are believed to be the most toxic form of A?. We found a diversity of A? peptides, with 26 unique proteoforms including various N- and C-terminal truncations. N- and C-terminal truncations comprised 73% and 30%, respectively, of the total A? proteoforms detected. The A? proteoforms segregated between the soluble and more insoluble aggregates with N-terminal truncations predominating in the insoluble material and C- terminal truncations segregating into the soluble aggregates. In contrast, canonical A? comprised the minority of the identified proteoforms (15.3%) and did not distinguish between the soluble and more insoluble aggregates. The relative abundance of many truncated A? proteoforms did not correlate with post-mortem interval, suggesting they are not artefacts. This heterogeneity of A? proteoforms deepens our understanding of AD and offers many new avenues for investigation into pathological mechanisms of the disease, with implications for therapeutic development. Twit Text FOAVip Diversity of Amyloid-beta Proteoforms in the Alzheimer s Disease Brain ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28842697 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28842697 #FOAvip English Wikipedia <ref>{{Cite pmid|28842697}}</ref> Diversity of Amyloid-beta Proteoforms in the Alzheimer?s Disease Brain #MMPMID28842697 Wildburger NC; Esparza TJ; LeDuc RD; Fellers RT; Thomas PM; Cairns NJ; Kelleher NL; Bateman RJ; Brody DL Sci Rep 2017[]; 7 (ä): ä PMID28842697show ga Amyloid-beta (A?) plays a key role in the pathogenesis of Alzheimer?s disease (AD), but little is known about the proteoforms present in AD brain. We used high-resolution mass spectrometry to analyze intact A? from soluble aggregates and insoluble material in brains of six cases with severe dementia and pathologically confirmed AD. The soluble aggregates are especially relevant because they are believed to be the most toxic form of A?. We found a diversity of A? peptides, with 26 unique proteoforms including various N- and C-terminal truncations. N- and C-terminal truncations comprised 73% and 30%, respectively, of the total A? proteoforms detected. The A? proteoforms segregated between the soluble and more insoluble aggregates with N-terminal truncations predominating in the insoluble material and C- terminal truncations segregating into the soluble aggregates. In contrast, canonical A? comprised the minority of the identified proteoforms (15.3%) and did not distinguish between the soluble and more insoluble aggregates. The relative abundance of many truncated A? proteoforms did not correlate with post-mortem interval, suggesting they are not artefacts. This heterogeneity of A? proteoforms deepens our understanding of AD and offers many new avenues for investigation into pathological mechanisms of the disease, with implications for therapeutic development. äDiversity of Amyloid-beta Proteoforms in the Alzheimer?s Disease Brain(epmc).pdf DeepDyve Pubget Overpricing