| Literature DB >> 26867740 |
Abstract
The dynamic co- and post-translational modification (PTM) of proteins, O-linked β-D-N-acetylglucosamine modification (O-GlcNAcylation) of serine/threonine residues is critical in many cellular processes, contributing to multiple physiological and pathological events. The term "O-GlcNAcome" refers to not only the complete set of proteins that undergo O-GlcNAcylation but also the O-GlcNAc status at individual residues, as well as the dynamics of O-GlcNAcylation in response to various stimuli. O-GlcNAcomic analyses have been a challenge for many years. In this chapter, we describe a recently developed approach for the identification and quantification of O-GlcNAc proteins/peptides from complex samples.Entities:
Keywords: Chemoenzymatic labeling; Electron transfer dissociation (ETD); GalT1 labeling; O-GlcNAcome; O-GlcNAcylation; Photocleavage; Quantitative mass spectrometry; SILAC; Site mapping
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Year: 2016 PMID: 26867740 DOI: 10.1007/978-1-4939-3524-6_6
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745