Current strategies and findings in clinically relevant post-translational modification-specific proteomics

Expert Rev Proteomics. 2015 Jun;12(3):235-53. doi: 10.1586/14789450.2015.1042867. Epub 2015 May 8.


Mass spectrometry-based proteomics has considerably extended our knowledge about the occurrence and dynamics of protein post-translational modifications (PTMs). So far, quantitative proteomics has been mainly used to study PTM regulation in cell culture models, providing new insights into the role of aberrant PTM patterns in human disease. However, continuous technological and methodical developments have paved the way for an increasing number of PTM-specific proteomic studies using clinical samples, often limited in sample amount. Thus, quantitative proteomics holds a great potential to discover, validate and accurately quantify biomarkers in body fluids and primary tissues. A major effort will be to improve the complete integration of robust but sensitive proteomics technology to clinical environments. Here, we discuss PTMs that are relevant for clinical research, with a focus on phosphorylation, glycosylation and proteolytic cleavage; furthermore, we give an overview on the current developments and novel findings in mass spectrometry-based PTM research.

Keywords: ERLIC; LC-MS; PTM; biomarkers; clinical proteomics; degradomics; glycoproteomics; phosphoproteomics; quantification.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biomarkers
  • Biomedical Research
  • Clinical Medicine / trends*
  • Glycosylation
  • Humans
  • Mass Spectrometry
  • Phosphorylation
  • Protein Processing, Post-Translational / physiology*
  • Proteolysis
  • Proteomics*


  • Biomarkers