O-GlcNAcase contributes to cognitive function in Drosophila. [PDF]
Contains fulltext : 219183.pdf (publisher's version ) (Open ...
Muha V +7 more
europepmc +10 more sources
Structural and functional insight into human O-GlcNAcase. [PDF]
O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual ...
Roth C +9 more
europepmc +14 more sources
A fluorescent probe to simultaneously detect both O-GlcNAcase and phosphatase [PDF]
O-GlcNAc modification of proteins often has crosstalk with protein phosphorylation. These posttranslational modifications are highly dynamic events that modulate a wide range of cellular processes. Owing to the physiological and pathological significance
Jihyeon Boo +5 more
doaj +4 more sources
O-GlcNAcase Fragment Discovery with Fluorescence Polarimetry. [PDF]
The attachment of the sugar N-acetyl-D-glucosamine (GlcNAc) to specific serine and threonine residues on proteins is referred to as protein O-GlcNAcylation.
Borodkin VS +6 more
europepmc +9 more sources
Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms [PDF]
Nucleocytoplasmic protein O-GlcNAcylation is a dynamic modification catalysed by O-GlcNAc transferase (OGT) and reversed by O-GlcNAc hydrolase (OGA), whose activities are regulated through largely unknown O-GlcNAc-dependent feedback mechanisms.
Sara Basse Hansen +10 more
doaj +5 more sources
O‐GlcNAcase Inhibitor Improves Denervation‐Induced Muscle Atrophy in Mice [PDF]
Background Skeletal muscle atrophy occurs in various situations, such as denervation, fasting and ageing. Disruption of the balance between protein synthesis and degradation plays an important role in muscle atrophy, and impaired Akt phosphorylation is ...
Tomoyasu Suenaga +8 more
doaj +4 more sources
Short O-GlcNAcase Is Targeted to the Mitochondria and Regulates Mitochondrial Reactive Oxygen Species Level [PDF]
O-GlcNAcylation is a reversible post-translational modification involved in the regulation of cytosolic, nuclear, and mitochondrial proteins. Only two enzymes, OGT (O-GlcNAc transferase) and OGA (O-GlcNAcase), control the attachment and removal of O ...
Patrick Pagesy +4 more
doaj +2 more sources
Region- and voxel-based quantification in human brain of [18F]LSN3316612, a radioligand for O-GlcNAcase [PDF]
Background Previous studies found that the positron emission tomography (PET) radioligand [18F]LSN3316612 accurately quantified O-GlcNAcase in human brain using a two-tissue compartment model (2TCM).
Jae-Hoon Lee +9 more
doaj +2 more sources
PET quantification of brain O-GlcNAcase with [18F]LSN3316612 in healthy human volunteers [PDF]
Background Previous studies found that [18F]LSN3316612 was a promising positron emission tomography (PET) radioligand for imaging O-GlcNAcase in nonhuman primates and human volunteers.
Jae-Hoon Lee +14 more
doaj +2 more sources
Discovery and clinical translation of ceperognastat, an O‐GlcNAcase (OGA) inhibitor, for the treatment of Alzheimer's disease [PDF]
INTRODUCTION The aggregation and spread of hyperphosphorylated, pathological tau in the human brain is hypothesized to play a key role in Alzheimer's disease (AD) as well as other neurogenerative tauopathies.
William Kielbasa +21 more
doaj +2 more sources

