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10.1016/j.brainresbull.2016.08.002 http://scihub22266oqcxt.onion/10.1016/j.brainresbull.2016.08.002 C5292095!5292095!27497832     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27497832.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Brain+Res+Bull 2017 ; 133 (ä): 80-7 Nephropedia Template TP {{tp|p=27497832|t=2017. O-GlcNAcylation and neurodegeneration |pdf=|usr=}}{{27497832}} gab.com Text O-GlcNAcylation and neurodegeneration JO: Brain Res Bull http://www.kidney.de/pget.php?&tw=1&pmid=27497832 #FOAvip O-GlcNAcylation is a dynamic form of protein glycosylation which involves the addition of ?-D-N-acetylglucosamine (GlcNAc) via an O-linkage to serine or threonine residues of nuclear, cytoplasmic, mitochondrial and transmembrane proteins. The two enzymes responsible for O-GlcNAc cycling are O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA); their expression and activities in brain are age dependent. More than 1000 O-GlcNAc protein targets have been identified which play critical roles in many cellular processes. In mammalian brain, O-GlcNAc modification of Tau decreases its phosphorylation and toxicity, suggesting a neuroprotective role of pharmacological elevation of brain O-GlcNAc for Alzheimer?s disease treatment. Other observations suggest that elevating O-GlcNAc levels may decrease protein clearance or induce apoptosis. This review highlights some of the key findings regarding O-GlcNAcylation in models of neurodegenerative diseases. Twit Text FOAVip O-GlcNAcylation and neurodegeneration ????Brain Res Bull http://www.kidney.de/pget.php?&tw=1&pmid=27497832 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27497832 #FOAvip English Wikipedia <ref>{{Cite pmid|27497832}}</ref> O-GlcNAcylation and neurodegeneration #MMPMID27497832 Wani WY; Chatham JC; Darley-Usmar V; McMahon LL; Zhang J Brain Res Bull 2017[Jul]; 133 (ä): 80-7 PMID27497832show ga O-GlcNAcylation is a dynamic form of protein glycosylation which involves the addition of ?-D-N-acetylglucosamine (GlcNAc) via an O-linkage to serine or threonine residues of nuclear, cytoplasmic, mitochondrial and transmembrane proteins. The two enzymes responsible for O-GlcNAc cycling are O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA); their expression and activities in brain are age dependent. More than 1000 O-GlcNAc protein targets have been identified which play critical roles in many cellular processes. In mammalian brain, O-GlcNAc modification of Tau decreases its phosphorylation and toxicity, suggesting a neuroprotective role of pharmacological elevation of brain O-GlcNAc for Alzheimer?s disease treatment. Other observations suggest that elevating O-GlcNAc levels may decrease protein clearance or induce apoptosis. This review highlights some of the key findings regarding O-GlcNAcylation in models of neurodegenerative diseases. äO-GlcNAcylation and neurodegeneration (epmc).pdf DeepDyve Pubget Overpricing