Literature DB >> 26867740

Mass Spectrometry-Based Quantitative O-GlcNAcomic Analysis.

Junfeng Ma1, Gerald W Hart2.   

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.

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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


  1 in total

1.  Analysis of Protein O-GlcNAcylation by Mass Spectrometry.

Authors:  Junfeng Ma; Gerald W Hart
Journal:  Curr Protoc Protein Sci       Date:  2017-02-02
  1 in total

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