PugNAc
PugNAc structure
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Common Name | PugNAc | ||
|---|---|---|---|---|
| CAS Number | 132489-69-1 | Molecular Weight | 353.33 | |
| Density | 1.53g/cm3 | Boiling Point | N/A | |
| Molecular Formula | C15H19N3O7 | Melting Point | 172-175°C | |
| MSDS | USA | Flash Point | N/A | |
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Carbamidomethylation Side Reactions May Lead to Glycan Misassignments in Glycopeptide Analysis.
Anal. Chem. 87 , 6297-302, (2015) Iodoacetamide is perhaps the most widely used reagent for the alkylation of free sulfhydryls in proteomic experiments. Here, we report that both incomplete derivatization of Cys side chains and overalkylation of the peptides may lead to the misassignment of g... |
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The Role of PTP1B O-GlcNAcylation in Hepatic Insulin Resistance.
Int. J. Mol. Sci. 16 , 22856-69, (2015) Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance. Accumulating evide... |
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Glucosamine-induced Sp1 O-GlcNAcylation ameliorates hypoxia-induced SGLT dysfunction in primary cultured renal proximal tubule cells.
J. Cell Physiol. 229(10) , 1557-68, (2014) The aim of this study is to determine whether GlcN could recover the endoplasmic reticulum (ER) stress-induced dysfunction of Na(+) /glucose cotransporter (SGLT) in renal proximal tubule cells (PTCs) under hypoxia. With the rabbit model, the renal ischemia in... |
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The augmentation of O-GlcNAcylation reduces glyoxal-induced cell injury by attenuating oxidative stress in human retinal microvascular endothelial cells.
Int. J. Mol. Med. 36 , 1019-27, (2015) It has recently been reported that O-linked β-N-acetyl glucosamine (O-GlcNAc) modification (a simple intracellular serine (Ser)/threonine (Thr)-linked monosaccharide) in human retinal microvascular endothelial cells (HRECs) is related to diabetic retinopathy ... |
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Transcription factor Nrf1 is negatively regulated by its O-GlcNAcylation status.
FEBS Lett. 589 , 2347-58, (2015) O-Linked N-acetylglucosamine transferase (OGT) was identified as an Nrf1-interacting protein. Herein, we show that Nrf1 enables interaction with OGT and their co-immunoprecipitates are O-GlcNAcylated by the enzyme. The putative O-GlcNAcylation negatively regu... |
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Global increase in O-linked N-acetylglucosamine modification promotes osteoblast differentiation.
Exp. Cell Res. 338 , 194-202, (2015) The balance between bone formation and bone resorption is maintained by osteoblasts and osteoclasts, and an imbalance in this bone metabolism leads to osteoporosis. Here, we found that osteoblast differentiation in MC3T3-E1 cells is promoted by the inactivati... |
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NOS1AP O-GlcNAc Modification Involved in Neuron Apoptosis Induced by Excitotoxicity.
Int. J. Mol. Sci. 16 , 16560-75, (2015) O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins. In addition to cancer and inflammation diseases, O-GlcNAc modificatio... |
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Hyper-O-GlcNAcylation inhibits the induction of heat shock protein 70 (Hsp 70) by sodium arsenite in HeLa cells.
Biol. Pharm. Bull. 37(8) , 1308-14, (2014) O-Linked β-N-acetylglucosamine-modification (O-GlcNAcylation) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress. However, the role of O-GlcNAcylation in t... |
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Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.
Biochim. Biophys. Acta 1840(1) , 191-8, (2014) O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosa... |
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A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells
Exp. Cell Res. 319(10) , 1482-90, (2013) O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins. In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked ... |