The in vivo modification of the canonical intermediate filament protein vimentin with O-linked beta-N-acetylglucosamine affects its function in filament assembly, cell migration and host-pathogen interactions.

The transfer of O-GlcNAc by EOGT to specific EGF repeats of NOTCH1 promotes DLL4 binding, Notch signaling, and retinal vascular development.

Brain region-specific profiling of O-GlcNAcylation interactome in Drosophila mushroom body suggests that hypo-O-GlcNAcylation impacts cognitive function by regulating translational activity.

AMDHD2 restricts the activity of the essential hexosamine pathway in mouse embryonic stem cells where GFPT2/GFAT2 instead of the common paralog GFPT1/GFAT1 controls metabolite entry.

A post-translational modification called O-GlcNAcylation modulates the activity of the SOX2 transcription factor in pluripotent stem cells.

OGT-mediated protein O-GlcNAcylation balances osteogenic versus adipogenic differentiation and controls hematopoietic niche function of bone marrow stromal cells.

The correct enzymatic activity of a previously misnamed enzyme is defined, placing the enzyme upstream of LARGE in building functional O-mannose structures on α-dystroglycan that are disrupted in multiple forms of congenital muscular dystrophy.

Active site migration establishes kinase activity in protein O-mannose kinase.

Extracellular glucose promotes O-GlcNAcylation of DNMT1 and inhibition of DNMT1 function in the maintenance of genomic methylation.

The specific metabolic pathways that increase neuron regeneration in ogt-1 mutant C. elegans following in vivo laser axotomy, highlighting the potential power for such metabolic targets in the treatment of neuronal injury.