Publication details

A review on recent trends in the phosphoproteomics workflow. From sample preparation to data analysis

Investor logo


Year of publication 2022
Type Article in Periodical
Magazine / Source Analytica Chimica Acta
MU Faculty or unit

Faculty of Science

Keywords Mass spectrometry; Phosphoproteomics; Receptor tyrosine kinase; Signaling pathways; Workflow
Description Phosphorylation is one of the quickest post-translational modifications that controls downstream signaling pathways regulating processes like cell proliferation, survival, and differentiation. Nowadays, mass spectrometry-based phosphoproteomics is a well-established method providing unprecedented characterization and quantification of phosphorylated proteins and peptides in complex samples. A comprehensive phosphoproteomics workflow consists of protein digestion, phosphopeptide enrichment, sample fractionation, chromatographic separation, and final detection by mass spectrometry. Each of these stages provides its own contribution to overall data variability and should be optimized thoroughly. This review aims to provide an overview of current developments in individual steps of phosphoproteomics workflow with a special focus on applied analytical methods. Recent efforts in all experimental steps are discussed. Finally, possible future development in the field of (phospho)proteomics is proposed.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info