O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease.

By Fei Liu, K. Iqbal, I. Grundke‐Iqbal, Gerald W. Hart, C. Gong. Proceedings of the National Academy of Sciences of the United States of America, 2004

755 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/2c00a7ef7b5c005bdceac54c2aacef11107b5d80

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Citations in the corpus

Mechanisms of tau-induced neurodegeneration (2009, positive): “Decreased glucose metabolism in cultured cells and in mice, which decreases the OGlcNA-cylation of tau, produces abnormal hyperphosphorylation of this protein [110,118].”
BRAIN FUEL METABOLISM, AGING AND ALZHEIMER’S DISEASE (2010, background): “Because the reciprocal changes in O-glycosylation and hyperphosphorylation of tau respond very rapidly to lower glucose supply in the fasted mouse model and because tau hyperphosphorylation is acutely sensitive to glucose and is directly linked to cognitive decline in AD, decreasing brain glucose up”
Tau-mediated neurodegeneration in Alzheimer's disease and related disorders (2007, background): “, although other post-translational modifications, such as glycosylatio”
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins (2007, background): “O-GlcNAcylation of human tau negatively regulates its O-phosphorylation in a site-specific manner both in vitro and in vivo”
Post-translational modifications of tau protein: implications for Alzheimer's disease. (2011, positive): “In fact, impairing brain glucose uptake/metabolism leads to down-regulation of OGlcNAcylation (and over-activation of GSK3b), which in turn facilitates abnormal tau hyperphosphorylation (Deng et al., 2009; Hernandez et al., 2010; Liu et al., 2004, 2009b).”
A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. (2008, background): “Work carried out over ten years ago showed that bovine tau is also extensively post-translationally modified by the addition of O -linked β- N -acetylglucosamine ( O -GlcNAc) moieties, and the same has been shown more recently for human ta”
Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease (2011, background): “Several studies in neuronal cells document interplay between OGlcNAcylation and phosphorylation on tau (194, 199).”