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.
authors: Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD, 21205-2185, USA.
authors: Junfeng
authors: J
authors: Ma
authors: Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD, 21205-2185, USA. gwhart@jhmi.edu.
authors: Gerald W
authors: GW
authors: Hart
mesh_terms: D000117:Acetylglucosamine / Q000737:chemistry; D006031:Glycosylation; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational
chemical_list: D000117:Acetylglucosamine
keywords: Chemoenzymatic labeling; Electron transfer dissociation (ETD); GalT1 labeling; O-GlcNAcome; O-GlcNAcylation; Photocleavage; Quantitative mass spectrometry; SILAC; Site mapping