Mass spectrometry-based quantitative O-GlcNAcomic analysis

Junfeng Ma, Gerald Warren Hart

Research output: Chapter in Book/Report/Conference proceedingChapter

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.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages91-103
Number of pages13
Volume1410
DOIs
StatePublished - Feb 1 2016

Publication series

NameMethods in Molecular Biology
Volume1410
ISSN (Print)10643745

Keywords

  • Chemoenzymatic labeling
  • Electron transfer dissociation (ETD)
  • GalT1 labeling
  • O-GlcNAcome
  • O-GlcNAcylation
  • Photocleavage
  • Quantitative mass Spectrometry
  • SILAC
  • Site mapping

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Ma, J., & Hart, G. W. (2016). Mass spectrometry-based quantitative O-GlcNAcomic analysis. In Methods in Molecular Biology (Vol. 1410, pp. 91-103). (Methods in Molecular Biology; Vol. 1410). Humana Press Inc.. https://doi.org/10.1007/978-1-4939-3524-6_6