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Gerrits, Bertran; Bodenmiller, Bernd (2010). Mapping of phosphorylation sites by LC-MS/MS. Methods in Molecular Biology, 658:127-136.

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Abstract

Reversible protein phosphorylation ranks among the most important post-translational modifications that occurs in the cell. It is therefore highly relevant to elucidate the phosphorylation states of a given biological system, albeit challenging. Most notably the often low stoichiometry of phosphorylation is inherently incompatible with standard LC-MS analysis of a complex protein digest mixture, primarily due to the relative low dynamic range of current mass analyzers. Therefore a need for specific enrichment of phosphorylated peptides or proteins exists. Significant progress surrounding the biochemical analysis of reversible protein phosphorylation in the past years has led to the development of several new techniques to isolate or enrich phosphopeptides, particularly in large-scale analyses. This chapter deals with three such examples.

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2 citations in Web of Science®
2 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Functional Genomics Center Zurich
07 Faculty of Science > Institute of Molecular Life Sciences
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:2010
Deposited On:04 Jun 2012 12:10
Last Modified:27 Nov 2013 20:27
Publisher:Springer
ISSN:1064-3745
Publisher DOI:10.1007/978-1-60761-780-8_7
PubMed ID:20839101

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