These findings indicate that oxidative environment promotes O-GlcNAcylation in skeletal muscle and suggest an interrelationship between cellular redox state and O-GlcNAc protein modificatio | Glutathione depletion and acute exercise increase O-GlcNAc protein modification in rat skeletal muscle. Peternelj TT, Marsh SA, Strobel NA, Matsumoto A, Briskey D, Dalbo VJ, Tucker PS, Coombes JS. | 09/26/2015 |
Findings suggest that, by dynamically regulating Milton GlcNAcylation, OGT tailors mitochondrial dynamics in neurons based on nutrient availability. | Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase. Pekkurnaz G, Trinidad JC, Wang X, Kong D, Schwarz TL., Free PMC Article | 09/20/2014 |
protein O-GlcNAcylation, OGT, and OGA in the rat brain at various ages from embryonic day 15 to the age of 2 years | Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain. Liu Y, Li X, Yu Y, Shi J, Liang Z, Run X, Li Y, Dai CL, Grundke-Iqbal I, Iqbal K, Liu F, Gong CX., Free PMC Article | 02/2/2013 |
results suggest that cultured podocytes possess limited ability to synthesize glucosamine (GlcN) internally and therefore may need to receive GlcN from the extracellular environment. | Expression of GFAT1 and OGT in podocytes: transport of glucosamine and the implications for glucose uptake into these cells. Rogacka D, Piwkowska A, Jankowski M, Kocbuch K, Dominiczak MH, Stepiński JK, Angielski S. | 10/23/2010 |
Exerts pro-survival actions during hypoxia-reoxygenation in cardiac myocytes, particularly at the level of mitochondria. | Non-canonical glycosyltransferase modulates post-hypoxic cardiac myocyte death and mitochondrial permeability transition. Ngoh GA, Watson LJ, Facundo HT, Dillmann W, Jones SP., Free PMC Article | 01/21/2010 |
CaMKIV activates OGT (o-linked GlcNAc transferase), and OGT has an essential role on the process of CaMKIV-dependent AP-1 activation under depolarization in neuronal cells. | o-GlcNAc transferase is activated by CaMKIV-dependent phosphorylation under potassium chloride-induced depolarization in NG-108-15 cells. Song M, Kim HS, Park JM, Kim SH, Kim IH, Ryu SH, Suh PG. | 01/21/2010 |
These data support the notion that O-GlcNAc may play an important role as an internal stress response and that glucosamine-induced cardioprotection may be mediated via the p38 MAPK pathway. | Glucosamine cardioprotection in perfused rat hearts associated with increased O-linked N-acetylglucosamine protein modification and altered p38 activation. Fülöp N, Zhang Z, Marchase RB, Chatham JC., Free PMC Article | 01/21/2010 |
O-GlcNAc transferase binds to protein phosphatase 1 catalytic subunits | O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits. Wells L, Kreppel LK, Comer FI, Wadzinski BE, Hart GW. | 01/21/2010 |
Neurodegenerative disease protein ataxin-10 (Atx-10) is associated with cytoplasmic O-linked beta-N-acetylglucosamine transferase in in the brain | Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain. März P, Stetefeld J, Bendfeldt K, Nitsch C, Reinstein J, Shoeman RL, Dimitriades-Schmutz B, Schwager M, Leiser D, Ozcan S, Otten U, Ozbek S. | 01/21/2010 |
Purification of a glycosylated protein p135, and it's identification as a O-GlcNAc transferase | Purification of the O-glycosylated protein p135 and identification as O-GlcNAc transferase. Konrad RJ, Tolar JF, Hale JE, Knierman MD, Becker GW, Kudlow JE. | 01/21/2010 |
The 26S proteasome can be inhibited by modification with the enzyme, O-GlcNAc transferase (OGT), thus inhibiting the proteolysis of transcription factor Sp1 and a hydrophobic peptide through inhibition of ATPase activity. | O-GlcNAc modification is an endogenous inhibitor of the proteasome. Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, Kudlow JE. | 01/21/2010 |
the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its tetratricopeptide repeat protein-protein interaction domains | Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. Iyer SP, Hart GW. | 01/21/2010 |
examined the characteristics and subcellular distribution of OGT protein and OGT activity and relationship to O-linked glycosylation; cytosolic OGT activity is 10 times more abundant in brain tissue compared with muscle, adipose, heart, and liver | UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme. Okuyama R, Marshall S. | 01/21/2010 |