@inbook{fb4e04c484514ba9a363cdc4b263a780,
title = "Mass spectrometry-based quantitative O-GlcNAcomic analysis",
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.",
keywords = "Chemoenzymatic labeling, Electron transfer dissociation (ETD), GalT1 labeling, O-GlcNAcome, O-GlcNAcylation, Photocleavage, Quantitative mass Spectrometry, SILAC, Site mapping",
author = "Junfeng Ma and Hart, {Gerald Warren}",
year = "2016",
month = feb,
day = "1",
doi = "10.1007/978-1-4939-3524-6_6",
language = "English (US)",
volume = "1410",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "91--103",
booktitle = "Methods in Molecular Biology",
}