O-Linked N-Acetylglucosaminylation Is Involved in the Ca2+ Activation Properties of Rat Skeletal Muscle

This publication has 57 references indexed in Scilit:

• O-GlcNAc Modification Is an Endogenous Inhibitor of the Proteasome
  Cell, 2003
• Proteomic Approaches to Analyze the Dynamic Relationships Between Nucleocytoplasmic Protein Glycosylation and Phosphorylation
  Circulation Research, 2003
• O-GlcNAc: a regulatory post-translational modification
  Biochemical and Biophysical Research Communications, 2003
• Glycan‐dependent signaling: O‐linked N‐acetylglucosamine
  The FASEB Journal, 2001
• Reciprocity between O-GlcNAc and O-Phosphate on the Carboxyl Terminal Domain of RNA Polymerase II
  Biochemistry, 2001
• Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc
  Science, 2001
• Alternative O-Glycosylation/O-Phosphorylation of the Murine Estrogen Receptor β
  Biochemistry, 2000
• Reduced O Glycosylation of Sp1 Is Associated with Increased Proteasome Susceptibility
  Molecular and Cellular Biology, 1997
• Dynamic O-GlcNAcylation of the Small Heat Shock Protein αB-Crystallin
  Biochemistry, 1996
• Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.
  Journal of Cell Biology, 1987