O-GlcNAcylation: the sweet side of epigenetics
Epigenetics & Chromatin, 2023 Histones display a wide variety of post-translational modifications, including acetylation, methylation, and phosphorylation. These epigenetic modifications can influence chromatin structure and function without altering the DNA sequence.
Thomas Dupas +2 more
doaj +1 more source
Protein O-GlcNAcylation in multiple immune cells and its therapeutic potential
Frontiers in Immunology, 2023 O-GlcNAcylation is a post-translational modification of proteins that involves the addition of O-GlcNAc to serine or threonine residues of nuclear or cytoplasmic proteins, catalyzed by O-GlcNAc transferase (OGT).
Huanhuan Cai +10 more
doaj +1 more source
Effect of Larval Nutrition on Maternal mRNA Contribution to the Drosophila Egg. [PDF]
, 2018 Embryonic development begins under the control of maternal gene products, mRNAs and proteins that the mother deposits into the egg; the zygotic genome is activated some time later. Maternal control of early development is conserved across metazoans. Gene
Cartwright, Emily L +3 more
core +2 more sources
OGA heterozygosity suppresses intestinal tumorigenesis in Apc min/+ mice [PDF]
, 2014 Emerging evidence suggests that aberrant O-GlcNAcylation is associated with tumorigenesis. Many oncogenic factors are O-GlcNAcylated, which modulates their functions.
A Sveen +24 more
core +1 more source
Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition
Chemistry & Biology, 2012 Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes. O-GlcNAc addition and removal is catalyzed by O-GlcNAc transferase and O-GlcNAcase, respectively. We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from ...
Schimpl, Marianne +3 more
openaire +3 more sources
Role of O-GlcNAcylation in Alzheimer's disease: Insights and perspectives
European Journal of Medicinal Chemistry ReportsO-GlcNAcylation is a critical post-translational modification involving the addition of N-acetylglucosamine to serine/threonine residues on proteins, significantly influencing their function and stability. In Alzheimer's disease (AD), the modification of
Anjali Sharma +4 more
doaj +1 more source
O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation. [PDF]
PLoS ONE, 2011 Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress. O-GlcNAc modification is reversibly regulated by O-linked
Takahiro Isono
doaj +1 more source
Nucleocytoplasmic human O-GlcNAc transferase is sufficient for O-GlcNAcylation of mitochondrial proteins [PDF]
, 2016 O-linked N-acetylglucosamine modification (O-GlcNAcylation) is a nutrient-dependent protein post-translational modification (PTM), dynamically and reversibly driven by two enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyse the ...
Akimoto +56 more
core +3 more sources
Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-β-galactosaminidase that uses neighbouring group participation [PDF]
, 2016 Bacteroides vulgatus is a member of the human microbiota whose abundance is increased in patients with Crohn's disease. We show that a B. vulgatus glycoside hydrolase from the carbohydrate active enzyme family GH123, BvGH123, is an N-acetyl-β ...
A. John +37 more
core +1 more source
Targeting O-GlcNAcylation to overcome resistance to anti-cancer therapies
Frontiers in Oncology, 2022 In cancer cells, metabolic reprogramming is associated with an alteration of the O-GlcNAcylation homeostasis. This post-translational modification (PTM) that attaches O-GlcNAc moiety to intracellular proteins is dynamically and finely regulated by the O ...
Ninon Very, Ikram El Yazidi-Belkoura
doaj +1 more source