Systems-wide proteomic characterization of combinatorial post-translational modification patterns

Nicolas L. Young, Mariana D. Plazas-Mayorca, Benjamin A. Garcia

Research output: Contribution to journalReview articlepeer-review

54 Scopus citations


Protein post-translational modifications (PTMs) have been widely shown to influence protein-protein interactions, direct subcellular location and transduce a variety of both internal and externally generated signals into cellular/phenotypic outcomes. Mass spectrometry has been a key tool for the elucidation of several types of PTMs in both qualitative and quantitative manners. As large datasets on the proteome-wide level are now being generated on a daily basis, the identification of combinatorial PTM patterns has become feasible. A survey of the recent literature in this area shows that many proteins undergo multiple modifications and that sequential or hierarchal patterns exist on many proteins; the biology of these modification patterns is only starting to be unraveled. This review will outline combinatorial PTM examples in biology, and the mass spectrometry-based techniques and applications utilized in the investigations of these combinatorial PTMs.

Original languageEnglish
Pages (from-to)79-92
Number of pages14
JournalExpert Review of Proteomics
Issue number1
StatePublished - Feb 2010


  • Electron-capture dissociation
  • Electron-transfer dissociation
  • Histone code
  • Mass spectrometry
  • Middle-down approach
  • Post-translational modification
  • Proteomics
  • Top-down approach


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