Ontology highlight
ABSTRACT:
SUBMITTER: Liu TW
PROVIDER: S-EPMC6055616 | biostudies-literature | 2018 Jun
REPOSITORIES: biostudies-literature
Liu Tai-Wei TW Zandberg Wesley F WF Gloster Tracey M TM Deng Lehua L Murray Kelsey D KD Shan Xiaoyang X Vocadlo David J DJ
Angewandte Chemie (International ed. in English) 20180524 26
O-Linked glycosylation of serine and threonine residues of nucleocytoplasmic proteins with N-acetylglucosamine (O-GlcNAc) residues is catalyzed by O-GlcNAc transferase (OGT). O-GlcNAc is conserved within mammals and is implicated in a wide range of physiological processes. Herein, we describe metabolic precursor inhibitors of OGT suitable for use both in cells and in vivo in mice. These 5-thiosugar analogues of N-acetylglucosamine are assimilated through a convergent metabolic pathway, most like ...[more]