Visualization of O-GlcNAc glycosylation stoichiometry and dynamics using resolvable poly(ethylene glycol) mass tags.

Quantitation of O-Glycosylation Stoichiometry and Dynamics using Resolvable Mass Tags

Mechanistic studies of O-GlcNAc glycosylation have been limited by an inability to monitor the glycosylation stoichiometries of proteins obtained from cells. Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags. This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins w...

Electrocatalytic Oxidation of Ethanol and Ethylene Glycol onto Poly (o-Anisidine)-Nickel Composite Electrode

In this work, poly (o-Anisidine) (POA) was prepared by consecutive potential cycling in an acidic monomer solution at the surface of Carbon Paste Electrode (CPE). Nickel ions were dispersed into the polymer by immersing the electrode in NiSO4 solution. The prepared Ni/POA/CPE was characterized by scanning electron microscopy, energy dispersive X-ray spectroscopy, Atomic Force Mic...

Study of Surface Tension of Binary Mixtures of Poly (Ethylene Glycol) in Water and Poly (Propylene Glycol) in Ethanol and its Modeling Using Neural Network

Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics.

The addition of the monosaccharide beta-N-acetyl-D-glucosamine to proteins (O-GlcNAc glycosylation) is an intracellular, post-translational modification that shares features with phosphorylation. Understanding the cellular mechanisms and signaling pathways that regulate O-GlcNAc glycosylation has been challenging because of the difficulty of detecting and quantifying the modification. Here, we ...

Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry

O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications. Proteins modified by O-GlcNAc play key cellular roles in signaling, transcription, metabolism, and cell division. Mechanistic studies on protein O-GlcNAcylation are hampered by the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry, and monitor O-...