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N-linked galactose-terminated glycans are a class of carbohydrates covalently attached to the asparagine (N) residue of proteins, predominantly on the cell surface. The primary structure consists of a core N-glycan to which various sugars—including galactose—are added, with galactose serving as a "terminal" sugar moiety. These terminal galactose residues play a critical role in cell–cell interactions, protein folding, and as binding sites for pathogens such as the AAV9 vector, which uses these glycans for cell entry. Alterations in the pattern of terminal galactose are associated with diseases such as cancer, immune disorders, and infection, but these structures are not themselves discrete and classically druggable molecular targets—they reflect a modification shared across many proteins and cell types.
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