Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc.

@article{Wells2001GlycosylationON,
  title={Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc.},
  author={Lance Wells and Keith Vosseller and Gerald W. Hart},
  journal={Science},
  year={2001},
  volume={291 5512},
  pages={2376-8}
}
The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) is abundant in all multicellular eukaryotes. On several proteins, O-GlcNAc and O-phosphate alternatively occupy the same or adjacent sites, leading to the hypothesis that one function of this saccharide is to transiently block phosphorylation. The diversity of proteins modified by O-GlcNAc implies its importance in many basic cellular and disease processes… CONTINUE READING
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G

  • X. Cheng, R. N. Cole, J. Zaia
  • W. Hart, Biochemistry 39,
  • 1160

Chem

  • W. G. Kelly, M. E. Dahmus, G. W. Hart, J. Biol
  • 268,
  • 1041

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