Kod viših eukariota posttranslaciona modifikacija proteinskih serina/treonina sa N-acetilglukozaminom (O-GlcNAc) je dinamička, induktivna i izobilna. Njome se regulišu mnogi ćelijski procesi putem ometanja proteinske fosforilacije.
↑Gao, Y., Wells, L., Comer, F.I., Parker, G.J. and Hart, G.W. (2001). "Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain". J. Biol. Chem.276: 9838–9845. PMID11148210.
↑Wells, L., Gao, Y., Mahoney, J.A., Vosseller, K., Chen, C., Rosen, A. and Hart, G.W. (2002). "Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic β-N-acetylglucosaminidase, O-GlcNAcase". J. Biol. Chem.277: 1755–1761. PMID11788610.
↑Cetinbas, N., Macauley, M.S., Stubbs, K.A., Drapala, R. and Vocadlo, D.J. (2006). "Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants". Biochemistry45: 3835–3844. PMID16533067.
↑Dennis, R.J., Taylor, E.J., Macauley, M.S., Stubbs, K.A., Turkenburg, J.P., Hart, S.J., Black, G.N., Vocadlo, D.J. and Davies, G.J. (2006). "Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity". Nat. Struct. Mol. Biol.13: 365–371. PMID16565725.
↑Kim, E.J., Kang, D.O., Love, D.C. and Hanover, J.A. (2006). "Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate". Carbohydr. Res.341: 971–982. PMID16584714.
↑Dong, D.L. and Hart, G.W. (1994). "Purification and characterization of an O-GlcNAc selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol". J. Biol. Chem.269: 19321–19330. PMID8034696.
