Results 41 to 50 of about 4,448 (184)
Fatty acid synthase inhibits the O-GlcNAcase during oxidative stress [PDF]
Journal of Biological Chemistry, 2017 The dynamic post-translational modification O-linked β-N-acetylglucosamine (O-GlcNAc) regulates thousands of nuclear, cytoplasmic, and mitochondrial proteins. Cellular stress, including oxidative stress, results in increased O-GlcNAcylation of numerous proteins, and this increase is thought to promote cell survival. The mechanisms by which the O-GlcNAc
Jennifer A, Groves +4 more
openaire +2 more sources
Genomics Data, 2015 Adding a single O-GlcNAc moiety to a Ser/Thr molecule of a protein by O-GlcNAc transferase and transiently removing it by O-GlcNAcase is referred to as O-GlcNAc cycling (or O-GlcNAcylation).
Chithra Keembiyehetty
doaj +1 more source
Frontiers in Chemistry, 2019 O-GlcNAcase (OGA) is the only enzyme responsible for removing N-acetyl glucosamine (GlcNAc) attached to serine and threonine residues on proteins. This enzyme plays a key role in O-GlcNAc metabolism.
Shanshan Li +13 more
doaj +1 more source
Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate [PDF]
Carbohydrate Research, 2006 A highly sensitive fluorogenic hexosaminidase substrate, fluorescein di(N-acetyl-beta-D-glucosaminide) (FDGlcNAc), was prepared essentially as described previously [Chem. Pharm. Bull. 1993, 41, 314] with some modifications. The fluorescent analog is a substrate for a number of hexosaminidases but here we have focused on the cytoplasmic O-GlcNAcase ...
Eun Ju, Kim +3 more
openaire +2 more sources
O-GlcNAc as an Integrator of Signaling Pathways
Frontiers in Endocrinology, 2018 O-GlcNAcylation is an important posttranslational modification governed by a single pair of enzymes–O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). These two enzymes mediate the dynamic cycling of O-GlcNAcylation on a wide variety of cytosolic, nuclear
Qunxiang Ong +7 more
doaj +1 more source
O-GlcNAcylation in Chronic Lymphocytic Leukemia and Other Blood Cancers
Frontiers in Immunology, 2021 In the past decade, aberrant O-GlcNAcylation has emerged as a new hallmark of cancer. O-GlcNAcylation is a post-translational modification that results when the amino-sugar β-D-N-acetylglucosamine (GlcNAc) is made in the hexosamine biosynthesis pathway ...
David E. Spaner +4 more
doaj +1 more source
O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease. [PDF]
, 2015 Several aggregation-prone proteins associated with neurodegenerative diseases can be modified by O-linked N-acetyl-glucosamine (O-GlcNAc) in vivo. One of these proteins, α-synuclein, is a toxic aggregating protein associated with synucleinopathies ...
Ambroso, Mark R +8 more
core +2 more sources
Recognition of diazirine-modified O-GlcNAc by human O-GlcNAcase. [PDF]
Medchemcomm, 2014 Mutagenesis of O-GlcNAcase offers insight into its substrate binding pocket and yields a mutant enzyme capable of hydrolyzing photocrosslinking O-GlcNAc.
Rodriguez AC, Kohler JJ.
europepmc +4 more sources
Cell-Penetrant, Nanomolar O-GlcNAcase Inhibitors Selective against Lysosomal Hexosaminidases
Chemistry & Biology, 2010 Posttranslational modification of metazoan nucleocytoplasmic proteins with N-acetylglucosamine (O-GlcNAc) is essential, dynamic, and inducible and can compete with protein phosphorylation in signal transduction. Inhibitors of O-GlcNAcase, the enzyme removing O-GlcNAc, are useful tools for studying the role of O-GlcNAc in a range of cellular processes ...
Dorfmueller, Helge C. +6 more
openaire +3 more sources
Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disability [PDF]
, 2017 Contains fulltext : 177227.pdf (publisher's version ) (Open Access)N-Acetylglucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential and dynamic post-translational modification.
Elferink, Martin +11 more
core +8 more sources