Journal
AMINO ACIDS
Volume 43, Issue 3, Pages 1009-1024Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-012-1288-9
Keywords
Mass spectrometry; Proteomics; Systems biology; Cell signaling
Categories
Funding
- Barts and the London Charity
- Medical Research Council
- Cancer Research UK
- Biotechnological and Biological Sciences Research Council
- Biotechnology and Biological Sciences Research Council [BB/G015023/1] Funding Source: researchfish
- Medical Research Council [G0800914] Funding Source: researchfish
- BBSRC [BB/G015023/1] Funding Source: UKRI
- MRC [G0800914] Funding Source: UKRI
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Phosphoproteomics is increasingly used to address a wide range of biological questions. However, despite some success, techniques for phosphoproteomics are not without challenges. Phosphoproteins are present in cells in low abundance relative to their unphosphorylated counterparts; therefore phosphorylated proteins (or phosphopeptides after protein digestion) are rarely detected in standard shotgun proteomics experiments. Thus, extraction of phosphorylated polypeptides from complex mixtures is a critical step in the success of phosphoproteomics experiments. Intense research over the last decade has resulted in the development of powerful techniques for phosphopeptide enrichment prior to analysis by mass spectrometry. Here, we review how the development of IMAC, MOAC, chemical derivatization and antibody affinity purification and chromatography is contributing to the evolution of phosphoproteomics techniques. Although further developments are needed for the technology to reach maturity, current state-of-the-art techniques can already be used as powerful tools for biological research.
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