Abstract
For proteins, phosphorylation is the most important known post-translational modification that affects activity. Virtually any basic process of a eukaryotic cell is regulated at some point by the phosphorylation of one or more of its key protein components (Krebs 1994). The regulation of gene transcription, cell-cycle progression, cell division and proliferation, cell differentiation, cytoskeletal dynamics, energy storage and retrieval are all phosphorylation dependent. The functional relevance of protein phosphorylation is even more striking, considering its relatively small quantitative importance. Only a few percent of proteins are phosphorylated and, of these, only 0.03% are phosphorylated at a tyrosine residue.
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Quadroni, M. (2001). Specific Detection and Analysis of Phosphorylated Peptides by Mass Spectrometry. In: Proteome Research: Mass Spectrometry. Principles and Practice. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56895-4_10
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DOI: https://doi.org/10.1007/978-3-642-56895-4_10
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-67256-2
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