A mutant O-GlcNAcase enriches Drosophila developmental regulators. [PDF]
Nat Chem Biol, 2017 YesProtein O-GlcNAcylation is a reversible post-translational modification of serines/threonines on nucleocytoplasmic proteins. It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
Selvan N +9 more
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O-GlcNAcase expression is sensitive to changes in O-GlcNAc homeostasis [PDF]
Frontiers in Endocrinology, 2014 O-linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification involving an attachment of a single β-N-acetylglucosamine moiety to serine or threonine residues in nuclear and cytoplasmic proteins.
ZHEN eZHANG +4 more
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O-GlcNAcase: promiscuous hexosaminidase or key regulator of O-GlcNAc signaling? [PDF]
J Biol Chem, 2014 O-GlcNAc signaling is regulated by an opposing pair of enzymes: O-GlcNAc transferase installs and O-GlcNAcase (OGA) removes the modification from proteins.
Alonso J, Schimpl M, van Aalten DM.
europepmc +9 more sources
Differential effects of an O-GlcNAcase inhibitor on tau phosphorylation. [PDF]
PLoS ONE, 2012 Abnormal hyperphosphorylation of microtubule-associated protein tau plays a crucial role in neurodegeneration in Alzheimer's disease (AD). The aggregation of hyperphosphorylated tau into neurofibrillary tangles is also a hallmark brain lesion of AD.
Yang Yu +12 more
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Human O-GlcNAcase catalytic-stalk dimer anchors flexible histone binding domains [PDF]
Communications ChemistryAlthough thousands of proteins are specifically O-GlcNAc modified, the molecular features recognized by the enzymes of O-GlcNAc cycling (OGT/OGA) remain poorly defined.
Sarah B. Nyenhuis +4 more
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Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase [PDF]
Nature Communications, 2017 O-linked β-N-acetyl glucosamine (O-GlcNAc) is an important protein modification that is hydrolyzed by O-GlcNAcase (OGA). Here the authors give insights into OGA substrate recognition by presenting four human OGA structures complexed with glycopeptide ...
Baobin Li +3 more
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Design and Optimization of Thioglycosyl–naphthalimides as Efficient Inhibitors Against Human O-GlcNAcase [PDF]
Frontiers in Chemistry, 2019 β-N-acetylhexosaminidases represent an important class of exoglycosidases and have emerged as the promising targets for drug and pesticide discovery. Among these, human O-GlcNAcase (hOGA) has been reported to be closely linked to several diseases such as
Shengqiang Shen +6 more
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Pharmacological Inhibition of O-GlcNAcase Does Not Increase Sensitivity of Glucocorticoid Receptor-Mediated Transrepression. [PDF]
PLoS ONE, 2015 Glucocorticoid signaling regulates target genes by multiple mechanisms, including the repression of transcriptional activities of nuclear factor κ-light-chain-enhancer of activated B cells (NF-κB) though direct protein-protein interactions and subsequent
Peter J Stivers +10 more
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O-GlcNAcase targets pyruvate kinase M2 to regulate tumor growth. [PDF]
Oncogene, 2020 Cancer cells are known to adopt aerobic glycolysis in order to fuel tumor growth, but the molecular basis of this metabolic shift remains largely undefined. O-GlcNAcase (OGA) is an enzyme harboring O-linked β-N-acetylglucosamine (O-GlcNAc) hydrolase and cryptic lysine acetyltransferase activities. Here, we report that OGA is upregulated in a wide range
Singh JP +23 more
europepmc +4 more sources
An Efficient and Accessible Hectogram-Scale Synthesis for the Selective O‑GlcNAcase Inhibitor Thiamet‑G [PDF]
ACS OmegaViktor Holicek +4 more
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