Glycosylation of the c-Myc transactivation domain.

@article{Chou1995GlycosylationOT,
  title={Glycosylation of the c-Myc transactivation domain.},
  author={T Y Chou and Chi V. Dang and Gerald W. Hart},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 10},
  pages={4417-21}
}
O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues. Although O-GlcNAc occurs on a myriad of nuclear and cytoplasmic proteins, only a few have thus far been identified. These O-GlcNAc-bearing proteins are also modified by phosphorylation and form reversible… CONTINUE READING

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O - linked N - acetylglucosamine ( O - GlcNAc ) is an abundant and dynamic posttranslational modification composed of a single monosaccharide , GlcNAc , glycosidically composed of a single monosaccharide , GlcNAc , glycosidically linked to the side - chain hydroxyl of serine or threonine residues .
O - linked N - acetylglucosamine ( O - GlcNAc ) is an abundant and dynamic posttranslational modification composed of a single monosaccharide , GlcNAc , glycosidically composed of a single monosaccharide , GlcNAc , glycosidically linked to the side - chain hydroxyl of serine or threonine residues .
O - linked N - acetylglucosamine ( O - GlcNAc ) is an abundant and dynamic posttranslational modification composed of a single monosaccharide , GlcNAc , glycosidically composed of a single monosaccharide , GlcNAc , glycosidically linked to the side - chain hydroxyl of serine or threonine residues .
O - linked N - acetylglucosamine ( O - GlcNAc ) is an abundant and dynamic posttranslational modification composed of a single monosaccharide , GlcNAc , glycosidically composed of a single monosaccharide , GlcNAc , glycosidically linked to the side - chain hydroxyl of serine or threonine residues .
Here we present evidence for O - GlcNAc glycosylation of the oncoprotein c - Myc , a helix - loop - helix / leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells .
Here we present evidence for O - GlcNAc glycosylation of the oncoprotein c - Myc , a helix - loop - helix / leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells .
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