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Phosphoproteomics for the Masses

Authors :
Grimsrud, Paul A.
Swaney, Danielle L.
Wenger, Craig D.
Beauchene, Nicole A.
Coon, Joshua J.
Source :
ACS Chemical Biology; January 2010, Vol. 5 Issue: 1 p105-119, 15p
Publication Year :
2010

Abstract

Protein phosphorylation serves as a primary mechanism of signal transduction in the cells of biological organisms. Technical advancements over the last several years in mass spectrometry now allow for the large-scale identification and quantitation of in vivophosphorylation at unprecedented levels. These developments have occurred in the areas of sample preparation, instrumentation, quantitative methodology, and informatics so that today, 10 000−20 000 phosphorylation sites can be identified and quantified within a few weeks. With the rapid development and widespread availability of such data, its translation into biological insight and knowledge is a current obstacle. Here we present an overview of how this technology came to be and is currently applied, as well as future challenges for the field.

Details

Language :
English
ISSN :
15548929 and 15548937
Volume :
5
Issue :
1
Database :
Supplemental Index
Journal :
ACS Chemical Biology
Publication Type :
Periodical
Accession number :
ejs20494179
Full Text :
https://doi.org/10.1021/cb900277e