Abstract
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 language | English |
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Pages (from-to) | 79-92 |
Number of pages | 14 |
Journal | Expert Review of Proteomics |
Volume | 7 |
Issue number | 1 |
DOIs | |
State | Published - Feb 2010 |
Keywords
- Electron-capture dissociation
- Electron-transfer dissociation
- Histone code
- Mass spectrometry
- Middle-down approach
- Post-translational modification
- Proteomics
- Top-down approach