Impairment of protein N-glycosylation disrupts neural cell adhesion mediated by highly glycosylated members of the IgSF-CAM protein family.

N-glycans commonly present in the protease domains are required for calnexin-mediated protein folding and intracellular trafficking.

The crenarchaeon Sulfolobus synthesizes the N-glycan core in the identical way as all Eukaryotes, which strengthens the hypothesis that the eukaryotic N-glycosylation is acquired from an ancient archaeon during eukaryogenesis.

Metabolic switches between oxidative phosphorylation and aerobic glycolysis plus glutaminolysis direct T cell function by altering the flux of glucose and glutamine to N-glycosylation.

Glycosylation of flagellins with pseudaminic acid in the bacterial cytoplasm governed by an unknown type of modular glycosyltransferase harboring an N-terminal substrate binding domain and a C-terminal glycosyltransferase domain.

The cytoplasmic enzyme N-glycanase 1 plays an evolutionary conserved role in promoting the ERAD-mediated retrotranslocation of misfolded Dpp/BMP4 from the ER, thereby allowing BMP signaling in specific contexts.

Adhesion force measurements reveal that proper N-glycosylation of flagellar membrane proteins is crucial for adhering C. reinhardtii cells onto surfaces.

Hexosamine salvage through the enzyme N-acetylglucosamine kinase is stimulated in nutrient-limited conditions and supports pancreatic tumor growth.

Targeted therapies induce an aberrant fucosylation of complex tumor secretomes stimulating the expansion of minority drug-resistant clones and promoting therapy resistance.

The combined use of NAD+ with ribitol or ribose potentiates the rescue of α-dystroglycan functional glycosylation in FKRP-mutant patient-specific iPSC-derived myotubes, representing potential novel treatments for FKRP muscular dystrophies.