n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime has been researched along with Insulin Resistance in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 5 (55.56) | 29.6817 |
| 2010's | 3 (33.33) | 24.3611 |
| 2020's | 1 (11.11) | 2.80 |
| Authors | Studies |
|---|---|
| Bubb, AK; Davies, GJ; Macauley, MS; Martinez-Fleites, C; Vocadlo, DJ | 1 |
| Aydogdu, G; Sermikli, BP; Yilmaz, E | 1 |
| Dehennaut, V; Lefebvre, T | 1 |
| El-Karim, EG; Teo, CF; Wells, L | 1 |
| Davies, GJ; Gloster, TM; He, Y; Macauley, MS; Stubbs, KA; Vocadlo, DJ | 1 |
| Arias, EB; Cartee, GD; Kim, J | 1 |
| Arias, EB; Cartee, GD | 1 |
| Lee, W; Park, SY; Ryu, J | 1 |
| Hart, GW; Lane, MD; Vosseller, K; Wells, L | 1 |
9 other study(ies) available for n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime and Insulin Resistance
| Article | Year |
|---|---|
Elevation of global O-GlcNAc levels in 3T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance.
Topics: 3T3-L1 Cells; Acetylglucosamine; Acetylglucosaminidase; Adipocytes; Animals; Bridged Bicyclo Compounds, Heterocyclic; Catalytic Domain; Dose-Response Relationship, Drug; Insulin Resistance; Kinetics; Mice; Models, Biological; Models, Chemical; Molecular Conformation; Phosphorylation; Protein Processing, Post-Translational | 2008 |
Role of the O-GlcNAc modification on insulin resistance and endoplasmic reticulum stress in 3T3-L1 cells.
Topics: 3T3-L1 Cells; Acetylglucosamine; Adipocytes; Animals; beta-N-Acetylhexosaminidases; Drug Resistance; Endoplasmic Reticulum Stress; Glucosamine; Glycolysis; Hexosamines; Insulin Resistance; Mice; N-Acetylglucosaminyltransferases; Oximes; Phenylcarbamates; Protein Processing, Post-Translational; RNA Interference; RNA, Small Interfering; Signal Transduction; Tunicamycin; Unfolded Protein Response | 2020 |
Proteomics and PUGNAcity will overcome questioning of insulin resistance induction by nonselective inhibition of O-GlcNAcase.
Topics: 3T3-L1 Cells; Acetylglucosamine; Animals; beta-N-Acetylhexosaminidases; Chromatography, Affinity; Glycosylation; Hep G2 Cells; Humans; Insulin Resistance; Mice; Oximes; Phenylcarbamates; Proteomics | 2013 |
Dissecting PUGNAc-mediated inhibition of the pro-survival action of insulin.
Topics: Acetylglucosamine; Animals; Apoptosis; beta-N-Acetylhexosaminidases; Cells, Cultured; CHO Cells; Cricetulus; Dose-Response Relationship, Drug; Enzyme Inhibitors; Insulin; Insulin Resistance; Oximes; Phenylcarbamates; Structure-Activity Relationship | 2016 |
Inhibition of O-GlcNAcase using a potent and cell-permeable inhibitor does not induce insulin resistance in 3T3-L1 adipocytes.
Topics: 3T3-L1 Cells; Acetylglucosamine; Adipocytes; Animals; beta-N-Acetylhexosaminidases; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Deoxyglucose; Enzyme Inhibitors; Humans; Indolizines; Insulin; Insulin Receptor Substrate Proteins; Insulin Resistance; Mice; Oximes; Phenylcarbamates; Phosphorylation; Proto-Oncogene Proteins c-akt | 2010 |
Prolonged incubation in PUGNAc results in increased protein O-Linked glycosylation and insulin resistance in rat skeletal muscle.
Topics: Acetylglucosamine; Animals; Biological Transport; Glucose; Glycosylation; Insulin; Insulin Resistance; Kinetics; Male; Muscle Proteins; Muscle, Skeletal; Oximes; Phenylcarbamates; Phosphorylation; Phosphoserine; Phosphothreonine; Protein Processing, Post-Translational; Rats; Rats, Wistar | 2004 |
Relationship between protein O-linked glycosylation and insulin-stimulated glucose transport in rat skeletal muscle following calorie restriction or exposure to O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate.
Topics: Acetylglucosamine; Animals; beta-N-Acetylhexosaminidases; Biological Transport, Active; Caloric Restriction; Electrophoresis, Polyacrylamide Gel; Glucose; Glycosylation; Insulin; Insulin Resistance; Liver; Male; Muscle Proteins; Muscle, Skeletal; Oximes; Phenylcarbamates; Rats; Rats, Inbred F344; Tissue Culture Techniques | 2005 |
O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes.
Topics: Acetylglucosamine; Adipocytes; Animals; beta-N-Acetylhexosaminidases; Deoxyglucose; Glucose Transporter Type 5; Glycosylation; Immunoprecipitation; Insulin Receptor Substrate Proteins; Insulin Resistance; Male; Monosaccharide Transport Proteins; Oximes; Phenylcarbamates; Phosphoproteins; Phosphorylation; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-akt; Rats; Rats, Sprague-Dawley; Subcellular Fractions | 2005 |
Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes.
Topics: 3T3 Cells; Acetylglucosamine; Adipocytes; Animals; beta Catenin; Blotting, Western; Calcium-Calmodulin-Dependent Protein Kinases; Catalysis; Cell Line; Cell Nucleus; Cytoplasm; Cytoskeletal Proteins; Dose-Response Relationship, Drug; Enzyme Activation; Glucosamine; Glucose; Glycogen Synthase Kinase 3; Glycogen Synthase Kinases; Glycosylation; Insulin; Insulin Receptor Substrate Proteins; Insulin Resistance; Mice; Oximes; Phenylcarbamates; Phosphoproteins; Phosphorylation; Precipitin Tests; Protein Binding; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-akt; Signal Transduction; Time Factors; Trans-Activators; Tyrosine | 2002 |