Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 α-subunit

This publication has 14 references indexed in Scilit:

• Nuclear and cytoplasmic glycosylation: novel saccharide linkages in unexpected places
  Trends in Biochemical Sciences, 1988
• O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation
  Cell, 1988
• Roles of a 67-kDa polypeptide in reversal of protein synthesis inhibition in heme-deficient reticulocyte lysate.
  Proceedings of the National Academy of Sciences, 1988
• Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway.
  Proceedings of the National Academy of Sciences, 1987
• Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.
  The Journal of cell biology, 1987
• Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
  The Journal of cell biology, 1987
• Identification and characterization of a nuclear pore complex protein
  Cell, 1986
• Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.
  Journal of Biological Chemistry, 1984
• A New Mouse Myeloma Cell Line that Has Lost Immunoglobulin Expression but Permits the Construction of Antibody-Secreting Hybrid Cell Lines
  The Journal of Immunology, 1979
• On the nature of α-mannosidase-resistant linkages in glycoproteins
  Biochemical and Biophysical Research Communications, 1971