These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Structure and function of extracellular O-GlcNAc.
    Author: Ogawa M, Okajima T.
    Journal: Curr Opin Struct Biol; 2019 Jun; 56():72-77. PubMed ID: 30669087.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]