Results 31 to 40 of about 20,888 (214)

Cardiac transcription factor Nkx2.5 is downregulated under excessive O-GlcNAcylation condition. [PDF]

open access: yesPLoS ONE, 2012
Post-translational modification of proteins with O-linked N-acetylglucosamine (O-GlcNAc) is linked the development of diabetic cardiomyopathy. We investigated whether Nkx2.5 protein, a cardiac transcription factor, is regulated by O-GlcNAc.
Hoe Suk Kim   +3 more
doaj   +1 more source

Neuronal O-GlcNAcylation Improves Cognitive Function in the Aged Mouse Brain. [PDF]

open access: yes, 2019
Mounting evidence in animal models indicates potential for rejuvenation of cellular and cognitive functions in the aging brain. However, the ability to utilize this potential is predicated on identifying molecular targets that reverse the effects of ...
Albarran, Eddy   +8 more
core   +1 more source

O-GlcNAcase expression is sensitive to changes in O-GlcNAc homeostasis

open access: yesFrontiers 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
doaj   +1 more source

A nexus of lipid and O-Glcnac metabolism in physiology and disease

open access: yesFrontiers in Endocrinology, 2022
Although traditionally considered a glucose metabolism-associated modification, the O-linked β-N-Acetylglucosamine (O-GlcNAc) regulatory system interacts extensively with lipids and is required to maintain lipid homeostasis.
Amber Lockridge, John A. Hanover
doaj   +1 more source

Engineering of GlcNAc-1-phosphotransferase for production of highly phosphorylated lysosomal enzymes for enzyme replacement therapy [PDF]

open access: yes, 2017
Several lysosomal enzymes currently used for enzyme replacement therapy in patients with lysosomal storage diseases contain very low levels of mannose 6-phosphate, limiting their uptake via mannose 6-phosphate receptors on the surface of the deficient ...
Doray, Balraj   +3 more
core   +3 more sources

The glycosyltransferase EOGT regulates adropin expression in decidualizing human endometrium [PDF]

open access: yes, 2017
In pregnancy, resistance of endometrial decidual cells to stress signals is critical for the integrity of the feto-maternal interface and, by extension, survival of the conceptus. O-GlcNAcylation is an essential post-translational modification that links
Alam, Mohammad T.   +8 more
core   +2 more sources

Synthesis of heparosan oligosaccharides by Pasteurella multocida PmHS2 single-action transferases [PDF]

open access: yes, 2012
Pasteurella multocida heparosan synthase PmHS2 is a dual action glycosyltransferase that catalyzes the polymerization of heparosan polymers in a non-processive manner.
Boeriu, C.G.   +3 more
core   +2 more sources

Inhibition of O-GlcNAc transferase sensitizes prostate cancer cells to docetaxel. [PDF]

open access: yesFront Oncol, 2022
The expression of O-GlcNAc transferase (OGT) and its catalytic product, O-GlcNAcylation (O-GlcNAc), are elevated in many types of cancers, including prostate cancer (PC). Inhibition of OGT serves as a potential strategy for PC treatment alone or combinational therapy. PC is the second common cancer type in male worldwide, for which
Xia M   +8 more
europepmc   +4 more sources

The dynamic metabolism of hyaluronan regulates the cytosolic concentration of UDP-GlcNAc [PDF]

open access: yes, 2014
Hyaluronan, a macromolecular glycosaminoglycan, is normally synthesized by hyaluronan synthases at the plasma membrane using cytosolic UDP-GlcUA and UDP-GlcNAc substrates and extruding the elongating chain into the extracellular space.
Hanson, R.W.   +8 more
core   +1 more source

Bioinformatic prediction of putative conveyers of O-GlcNAc transferase intellectual disability. [PDF]

open access: yesJ Biol Chem, 2022
Protein O-GlcNAcylation is a dynamic posttranslational modification that is catalyzed by the enzyme O-GlcNAc transferase (OGT) and is essential for neurodevelopment and postnatal neuronal function. Missense mutations in OGT segregate with a novel X-linked intellectual disability syndrome, the OGT congenital disorder of glycosylation (OGT-CDG).
Mitchell CW   +2 more
europepmc   +5 more sources

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