Abstract
Protein phosphorylation is a reversible post-translational modification crucial in the control of numerous regulatory pathways. Understanding the highly interconnected nature of such networks requires new broader-scale analysis techniques. This report summarizes recent advances in the use of mass spectrometry to assess phosphorylation events in ever more complex systems.
Keywords: Phosphoproteome, phosphorylation, spectrometry
Mini-Reviews in Medicinal Chemistry
Title: Exploring the Phosphoproteome with Mass Spectrometry
Volume: 4 Issue: 3
Author(s): Eric C. Peters, Ansgar Brock and Scott B. Ficarro
Affiliation:
Keywords: Phosphoproteome, phosphorylation, spectrometry
Abstract: Protein phosphorylation is a reversible post-translational modification crucial in the control of numerous regulatory pathways. Understanding the highly interconnected nature of such networks requires new broader-scale analysis techniques. This report summarizes recent advances in the use of mass spectrometry to assess phosphorylation events in ever more complex systems.
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Cite this article as:
Peters C. Eric, Brock Ansgar and Ficarro B. Scott, Exploring the Phosphoproteome with Mass Spectrometry, Mini-Reviews in Medicinal Chemistry 2004; 4 (3) . https://dx.doi.org/10.2174/1389557043487330
DOI https://dx.doi.org/10.2174/1389557043487330 |
Print ISSN 1389-5575 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5607 |
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