O-GlcNAc profiling: From proteins to proteomes

Junfeng Ma, Gerald Warren Hart

Research output: Contribution to journalArticlepeer-review

156 Scopus citations


O-linked β-D-N-Acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) onto serine and threonine residues of proteins is an important post-Translational modification (PTM), which is involved in many crucial biological processes including transcription, translation, proteasomal degradation, and signal transduction. Aberrant protein O-GlcNAcylation is directly linked to the pathological progression of chronic diseases including diabetes, cancer, and neurodegenerative disorders. Identification, site mapping, and quantification of O-GlcNAc proteins are a prerequisite to decipher their functions. In this review, we mainly focus on technological developments regarding O-GlcNAc protein profiling. Specifically, on one hand, we show how these techniques are being used for the comprehensive characterization of certain targeted proteins in which biologists are most interested. On the other hand, we present several newly developed approaches for O-GlcNAcomic profiling as well as how they provide us with a systems perspective to crosstalk amongst different PTMs and complicated biological events. Promising technical trends are also highlighted to evoke more efforts by diverse laboratories, which would further expand our understanding of the physiological and pathological roles of protein O-GlcNAcylation in chronic diseases.

Original languageEnglish (US)
Article number8
JournalClinical Proteomics
Issue number1
StatePublished - 2014


  • Enrichment
  • Mass spectrometry
  • O-GlcNAc
  • O-GlcNAcome
  • O-GlcNAcomics
  • Proteomics
  • Quantification
  • Site mapping

ASJC Scopus subject areas

  • Molecular Biology
  • Molecular Medicine
  • Clinical Biochemistry


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