A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo.
By S. Yuzwa, Matthew S Macauley, J. Heinonen, X. Shan, R. Dennis, Yuan He, G. Whitworth, K. Stubbs, E. McEachern, G. Davies and 1 more. Nature Chemical Biology, 2008
661 citations recorded by the source corpus.
Subfields: Molecular Biology, Organic Chemistry, Physiology
View Paper: https://www.semanticscholar.org/paper/0732460ea61b9dadf6314a4fb1a1938ae2054605
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Citations in the corpus
- Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease (2011, background): “Recent studies documented that a highly specific OGlcNAcase inhibitor, which increases global O-GlcNAcylation in living mice and crosses the blood brain barrier, prevents the abnormal hyperphosphorylation of tau in a murine model of AD (92).”
- Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “Downregulation of O-GlcNAc transferase leads to reduced O-GlcNAcylation and increased tau phosphorylation, whereas inhibition of O-GlcNAcase reduces tau phosphorylation [187, 188].”
- Post-translational modifications of tau protein: implications for Alzheimer's disease. (2011, positive): “has been shown to reduce tau phosphorylation in rat cortex and hippocampus (Yuzwa et al., 2008).”
- Mechanisms of tau-induced neurodegeneration (2009, positive): “In AD, probably due to impaired glucose uptake/metabolism, there is a global decrease in O-GlcNAcylation including that of tau and neurofilaments [34, 118].”