Results 71 to 80 of about 4,448 (184)
GH20 human β-N-acetylhexosaminidases (hsHex) and GH84 human O-GlcNAcase (hOGA) are involved in numerous pathological processes and emerged as promising targets for drug discovery. Based on the catalytic mechanism and structure of the catalytic domains of
Shengqiang Shen +5 more
doaj +1 more source
The Role of O-GlcNAcylation in Immune Cell Activation
O-GlcNAcylation is a dynamic post-translational modification where the sugar, O-linked β-N-acetylglucosamine (O-GlcNAc) is added to or removed from various cytoplasmic, nuclear, and mitochondrial proteins.
Amy Qiang +2 more
doaj +1 more source
Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) induces vascular dysfunction via production of superoxide anion/reactive oxygen species [PDF]
Overproduction of superoxide anion (•O2-) and O-linked β-N-acetylglucosamine (O-GlcNAc)-modification in the vascular system are contributors to endothelial dysfunction.
Alves-Lopes, Rhéure +8 more
core +2 more sources
ABSTRACT Aim Mitochondrial dysfunction plays a central role in multiple neurodegenerative diseases, yet the temporal sequence of cellular events underlying neurodegeneration remains poorly defined. This study aimed to characterize the progression of neurodegeneration in a mouse model of fatal mitochondrial encephalopathy and to evaluate the therapeutic
Laura Jiménez‐Sánchez +12 more
wiley +1 more source
Characterization of tools to detect and enrich human and mouse O-GlcNAcase. [PDF]
O-linked β-N-acetylglucosamine (O-GlcNAc) is an essential regulatory post-translational modification of thousands of nuclear, cytoplasmic, and mitochondrial proteins. O-GlcNAc is dynamically added and removed from proteins by the O-GlcNAc transferase and the O-GlcNAcase (OGA), respectively.
Groves JA, Zachara NE.
europepmc +4 more sources
Three Decades of Research on O-GlcNAcylation – A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism [PDF]
Even though the dynamic modification of polypeptides by the monosaccharide, O-linked N-acetylglucosamine (O-GlcNAcylation) was discovered over thirty-years ago, its physiological significance as a major nutrient sensor that regulates myriad cellular ...
Gerald W. Hart
core +2 more sources
OGT inhibition during in vitro oocyte maturation disrupts epigenetic asymmetry in the zygote. It reduces male pronuclear size and eliminates DNA methylation asymmetry by decreasing H3K9me2‐mediated 5mC protection in the female pronucleus and suppressing TET3‐dependent DNA demethylation in the male pronucleus.
Haoxue Wang +3 more
wiley +1 more source
Perfluorooctane sulfonate (PFOS) exposure disrupts oocyte maturation and early embryonic development. This study elucidates the mechanism by which enhanced O‐GlcNAcylation of FOXK1 underlies the PFOS‐induced reduction of progesterone levels in granulosa cells and the disturbance of follicular microenvironment.
Shuwen Han +16 more
wiley +1 more source
Background: Preclinical studies have demonstrated that inhibition of the O-linked β-N-acetylglucosaminidase enzyme increases tau O-linked β-N-acetylglucosaminylation and may attenuate tau pathology in Alzheimer’s disease.
Flavia C. Nery +22 more
doaj +1 more source
Functional Analysis of O-GlcNAcylation in Cancer Metastasis
One common and reversible type of post-translational modification (PTM) is the addition of O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation), and its dynamic balance is controlled by O-GlcNAc transferase (OGT) and glycoside ...
Donglu Wu +8 more
doaj +1 more source

