Structural and functional studies of GlcNAc-modified Tau

@inproceedings{Cheung2013StructuralAF,
  title={Structural and functional studies of GlcNAc-modified Tau},
  author={Adrienne H Cheung},
  year={2013}
}
.................................................................................................................................... ii Table of contents ...................................................................................................................... iv List of figures ........................................................................................................................... vi List of tables… 

References

SHOWING 1-10 OF 97 REFERENCES
Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
TLDR
Three O-GlcNAc sites are identified by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo.
TLDR
Thiamet-G will find wide use in probing the functional role of O-GlcNAc in vertebrate brain, and it may also offer a route to blocking pathological hyperphosphorylation of tau in AD.
Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody
TLDR
A method for the production of recombinant O-GlcNAc modified tau is described and, using this tau, sites of O- GlcNAC on tau are mapped using mass spectrometry and detected in rat brain, which confirms the validity of this in vitro mapping approach.
O-GlcNAc modification in diabetes and Alzheimer's disease.
TLDR
Data support the hypothesis that hypoglycemia within the brain may reduce the normal GlcNAcylation of tau, exposing kinase acceptor sites, thus leading to hyperphosphorylation, which induces tangle formation and neuronal death in Alzheimer's neurons.
Structure of human O-GlcNAc transferase and its complex with a peptide substrate
TLDR
The structures provide clues to the enzyme mechanism, show how OGT recognizes target peptide sequences, and reveal the fold of the unique domain between the two halves of the catalytic region will accelerate the rational design of biological experiments to investigate OGT’s functions.
c-Myc Is Glycosylated at Threonine 58, a Known Phosphorylation Site and a Mutational Hot Spot in Lymphomas (*)
TLDR
Threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc, a helix-loop-helix leucine zipper phosphoprotein that regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
Characterization of β-N-Acetylglucosaminidase Cleavage by Caspase-3 during Apoptosis*
TLDR
O-GlcNAcase is cleaved by caspase-3 into two fragments during apoptosis, an N-terminal fragment containing the O-GlCNAcase active site and a C-terminAL fragment containing a region with homology to GCN5 histone acetyl-transferases.
Regulation of the O-Linked β-N-Acetylglucosamine Transferase by Insulin Signaling*
TLDR
It is shown that OGT is activated by insulin signaling, a well characterized insulin receptor substrate, and it is concluded that insulin stimulates the tyrosine phosphorylation and activity of OGT.
Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity
TLDR
Mutagenesis and kinetics studies show that the bacterial enzyme, very similarly to its human counterpart, operates via an unusual 'substrate-assisted' catalytic mechanism, which will inform the rational design of enzyme inhibitors.
...
1
2
3
4
5
...