https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 Protein phosphatase 2A dysfunction in Alzheimer's disease https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:21291 in vivo and in AD. Disruption of PP2A/Bα-Tau protein interactions likely contribute to Tau deregulation in AD. Significantly, alterations in one-carbon metabolism that impair PP2A methylation are associated with increased risk for sporadic AD, and enhanced AD-like pathology in animal models. Experimental studies have linked deregulation of PP2A methylation with down-regulation of PP2A/Bα, enhanced phosphorylation of Tau and amyloid precursor protein, Tau mislocalization, microtubule destabilization and neuritic defects. While it remains unclear what are the primary events that underlie "PP2A" dysfunction in AD, deregulation of PP2A enzymes definitely affects key players in the pathogenic process. As such, there is growing interest in developing PP2A-centric therapies for AD, but this may be a daunting task without a better understanding of the regulation and function of specific PP2A enzymes.]]> Wed 11 Apr 2018 12:53:23 AEST ]]> miRNA enriched in human neuroblast nuclei bind the MAZ transcription factor and their precursors contain the MAZ consensus motif https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:33472 Wed 04 Sep 2019 09:48:55 AEST ]]> Early history of glycine receptor biology in mammalian spinal cord circuits https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:11009 Sat 24 Mar 2018 08:07:11 AEDT ]]>