Localization of O-GlcNAc modification on the serum response transcription factor.

This publication has 35 references indexed in Scilit:

• Glycosylation of nuclear and cytoplasmic proteins is ubiquitous and dynamic
  Biochemical Society Transactions, 1992
• Human vitamin D receptor is selectively phosphorylated by protein kinase C on serine 51, a residue crucial to its trans-activation function.
  Proceedings of the National Academy of Sciences, 1991
• Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
  Cell, 1991
• Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase.
  Journal of Biological Chemistry, 1990
• Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133
  Cell, 1989
• GLYCOSYLATION IN THE NUCLEUS AND CYTOPLASM
  Annual Review of Biochemistry, 1989
• Partial cDNA sequence encoding a nuclear pore protein modified by O-linked N-acetylglucosamine.
  Proceedings of the National Academy of Sciences, 1988
• Nuclear and cytoplasmic glycosylation: novel saccharide linkages in unexpected places
  Trends in Biochemical Sciences, 1988
• Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.
  The Journal of cell biology, 1987
• Collagen cross-links. A mass-spectrometric and1H- and13C-nuclear-magnetic-resonance study
  Biochemical Journal, 1973