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Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1.
O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
Identification of O-linked N-acetylglucosamine (O-GlcNAc)-modified osteoblast proteins by electron transfer dissociation tandem mass spectrometry reveals proteins critical for bone formation.
Protein O-linked ?-N-acetylglucosamine: a novel effector of cardiomyocyte metabolism and function.
O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
Intracellular protein O-GlcNAc modification integrates nutrient status with transcriptional and metabolic regulation.
The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation.
Regulation of IGF-1 and Insulin Signaling by O-GlcNAc Glycosylation