Viral evolution can lead to mutations that render specific glycosylation sites dispensable for folding and for supporting the protein's function, allowing changes in the shield, and in the immunogenic profile.

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

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.

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.

In mice, but not in humans, the bone-derived hormone osteocalcin is O-glycosylated, a post-translational modification controlling its half-life in vivo.

A mathematical model of glycosylation in the Golgi apparatus to investigate how the fidelity of synthesising a complex glycan distribution at the plasma membrane depends on parameters such as the number of Golgi cisternae or enzyme specificity.

The first inhibitor identified against an iso-enzyme that initiates O-glycosylation in the Golgi complex promises new therapeutic approaches for cancer and chronic kidney disease.

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.

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

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.