Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome.

By Matthias Mann, Shao-En Ong, M. Grønborg, Hanno Steen, Ole Nørregaard Jensen, A. Pandey. Trends in Biotechnology, 2002

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Phospho.ELM: a database of phosphorylation sites—update 2011 (2010, background): “Over the past few years, many advances have been made in mass spectrometry techniques and protein enrichment strategies that have significantly improved the detection efficiency of phosphorylated proteins (1,2).”
Immunoaffinity profiling of tyrosine phosphorylation in cancer cells (2005, background): “Current phosphoproteomic approaches generally reveal only small numbers of tyrosine phosphorylation sites, in keeping with the low level of phosphotyrosine relative to phosphoserine and phosphothreonine residue”
Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling Pathway*S (2005, background): “Thus, some of the most successful phosphoproteomic studies applied selective phosphoprotein and phosphopeptide enrichment techniques in combination with sensitive mass spectrometric peptide sequencing methods (2, 5).”