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O-GlcNAc modification and the tauopathies: insights from chemical biology. Current Alzheimer research [Curr Alzheimer Res] Journal article

 
Yuzwa SA, Vocadlo DJ 
O-GlcNAc modification and the tauopathies: insights from chemical biology. [Journal Article, Research Support, Non-U.S. Gov't]
Curr Alzheimer Res 2009 Oct; 6(5):451-4.


The aggregation of the microtubule-associated protein tau into paired-helical filaments is the defining characteristic of the tauopathies. It has become apparent that the hyperphosphorylation of tau likely plays a role in the aggregation process and thus strategies to reduce tau phosphorylation are generating wide interest. The O-GlcNAc posttranslational modification of tau has been shown to be reciprocal to its phosphorylation; increasing O-GlcNAc leads to reductions in tau phosphorylation. In this mini-review, we highlight the use of chemical compounds as a means of understanding the reciprocal nature of tau phosphorylation and tau O-GlcNAcylation and highlight some recent progress in this area.



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