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http://scihub22266oqcxt.onion/ C4797837/?report=reader!4797837!27505013     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Yale+J+Biol+Med 2016 ; 89 (1): 5-21 Nephropedia Template TP {{tp|p=27505013|t=2016. Amyloid-beta Alzheimer targets ? protein processing, lipid rafts, and amyloid-beta pores |pdf=|usr=}}{{27505013}} gab.com Text Amyloid-beta Alzheimer targets protein processing, lipid rafts, and amyloid-beta pores JO: Yale J Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=27505013 #FOAvip Amyloid beta (A?), the hallmark of Alzheimer?s Disease (AD), now appears to be deleterious in its low number aggregate form as opposed to the macroscopic A? fibers historically seen postmortem. While Alzheimer targets, such as the tau protein, amyloid precursor protein (APP) processing, and immune system activation continue to be investigated, the recent discovery that amyloid beta aggregates at lipid rafts and likely forms neurotoxic pores has led to a new paradigm regarding why past therapeutics may have failed and how to design the next round of compounds for clinical trials. An atomic resolution understanding of A? aggregates, which appear to exist in multiple conformations, is most desirable for future therapeutic development. The investigative difficulties, structures of these small A? aggregates, and current therapeutics are summarized in this review. Twit Text FOAVip Amyloid-beta Alzheimer targets protein processing, lipid rafts, and amyloid-beta pores ????Yale J Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=27505013 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27505013 #FOAvip English Wikipedia <ref>{{Cite pmid|27505013}}</ref> Amyloid-beta Alzheimer targets ? protein processing, lipid rafts, and amyloid-beta pores #MMPMID27505013 Arbor SC; LaFontaine M; Cumbay M Yale J Biol Med 2016[Mar]; 89 (1): 5-21 PMID27505013show ga Amyloid beta (A?), the hallmark of Alzheimer?s Disease (AD), now appears to be deleterious in its low number aggregate form as opposed to the macroscopic A? fibers historically seen postmortem. While Alzheimer targets, such as the tau protein, amyloid precursor protein (APP) processing, and immune system activation continue to be investigated, the recent discovery that amyloid beta aggregates at lipid rafts and likely forms neurotoxic pores has led to a new paradigm regarding why past therapeutics may have failed and how to design the next round of compounds for clinical trials. An atomic resolution understanding of A? aggregates, which appear to exist in multiple conformations, is most desirable for future therapeutic development. The investigative difficulties, structures of these small A? aggregates, and current therapeutics are summarized in this review. äAmyloid-beta Alzheimer targets ? protein processing, lipid rafts, and (epmc).pdf DeepDyve Pubget Overpricing