Most of the cellular processes are regulated by reversible phosphorylation of proteins, which in turn plays a critical role in the regulation of gene expression, cell division, signal transduction, metabolism, differentiation, and apoptosis. Mass spectrometry of phosphopeptides obtained from tryptic protein digests has become a powerful tool for characterization of phosphoproteins involved in these processes. However, there is a general need to significantly enrich the phosphopeptide content to compensate their low abundance, insufficient ionization, and suppression effects of non-phosphorylated peptides.This paper aims to give a comprehensive overview on the methods involved in recent phosphoproteomics. It presents a description of contemporary enrichment techniques with references to particular studies and compares different approaches to characterization of phosphoproteome by mass spectrometry. © 2011 Elsevier B.V.
CITATION STYLE
Tichy, A., Salovska, B., Rehulka, P., Klimentova, J., Vavrova, J., Stulik, J., & Hernychova, L. (2011, November 18). Phosphoproteomics: Searching for a needle in a haystack. Journal of Proteomics. https://doi.org/10.1016/j.jprot.2011.07.018
Mendeley helps you to discover research relevant for your work.