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10.1016/j.celrep.2015.05.021 http://scihub22266oqcxt.onion/10.1016/j.celrep.2015.05.021 C4494129!4494129!26051935     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 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Rep 2015 ; 11 (11): 1760-71 Nephropedia Template TP {{tp|p=26051935|t=2015. Quaternary structure defines a large class of amyloid-? oligomers neutralized by sequestration |pdf=|usr=}}{{26051935}} gab.com Text Quaternary structure defines a large class of amyloid- oligomers neutralized by sequestration JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=26051935 #FOAvip The accumulation of amyloid-? (A?) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer's disease (AD). However, there are numerous potentially toxic oligomers and little is known about their neurological effects when generated in the living brain. Here, we show that A? oligomers can be assigned to one of at least two classes (Type 1 and Type 2) based on their temporal, spatial and structural relationships to amyloid fibrils. The Type 2 oligomers are related to amyloid fibrils and represent the majority of oligomers generated in vivo, but remain confined to the vicinity of amyloid plaques and do not impair cognition at levels relevant to AD. Type 1 oligomers are unrelated to amyloid fibrils and may have greater potential to cause global neural dysfunction in AD because they are dispersed. These results refine our understanding of the pathogenicity of A? oligomers in vivo. Twit Text FOAVip Quaternary structure defines a large class of amyloid- oligomers neutralized by sequestration ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=26051935 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26051935 #FOAvip English Wikipedia <ref>{{Cite pmid|26051935}}</ref> Quaternary structure defines a large class of amyloid-? oligomers neutralized by sequestration #MMPMID26051935 Liu P; Reed MN; Kotilinek LA; Grant MK; Forster CL; Qiang W; Shapiro SL; Reichl JH; Chiang AC; Jankowsky JL; Wilmot CM; Cleary JP; Zahs KR; Ashe KH Cell Rep 2015[Jun]; 11 (11): 1760-71 PMID26051935show ga The accumulation of amyloid-? (A?) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer's disease (AD). However, there are numerous potentially toxic oligomers and little is known about their neurological effects when generated in the living brain. Here, we show that A? oligomers can be assigned to one of at least two classes (Type 1 and Type 2) based on their temporal, spatial and structural relationships to amyloid fibrils. The Type 2 oligomers are related to amyloid fibrils and represent the majority of oligomers generated in vivo, but remain confined to the vicinity of amyloid plaques and do not impair cognition at levels relevant to AD. Type 1 oligomers are unrelated to amyloid fibrils and may have greater potential to cause global neural dysfunction in AD because they are dispersed. These results refine our understanding of the pathogenicity of A? oligomers in vivo. äQuaternary structure defines a large class of amyloid-? oligomers neut(epmc).pdf DeepDyve Pubget Overpricing