@article{oai:nagoya.repo.nii.ac.jp:00028841,
 author = {Ogawa, Mitsutaka and Okajima, Tetsuya},
 journal = {Current Opinion in Structural Biology},
 month = {Jun},
 note = {Extracellular O-GlcNAc is a unique modification restricted to the epidermal growth factor (EGF) domain-containing glycoproteins. This O-GlcNAcylation is catalyzed by the EGF-domain specific O-GlcNAc transferase (EOGT), which is localized in the lumen of endoplasmic reticulum. In humans, EOGT is one of the causative genes of a congenital disease, Adams–Oliver syndrome. EOGT is highly expressed in endothelial cells and regulates vascular development and integrity by potentiating Delta-like ligand-mediated Notch signaling. In Drosophila, Eogt modifies Dumpy, an apical extracellular matrix glycoprotein, and affects Dumpy-dependent cell-matrix interaction. In this review, we summarize the current findings of the structure and functions of extracellular O-GlcNAc in animals.},
 pages = {72--77},
 title = {Structure and function of extracellular O-GlcNAc},
 volume = {56},
 year = {2019}
}