| Title | Phosphoproteomics for the Masses |
| Publication Type | Journal Article |
| Year of Publication | 2010 |
| Authors | Grimsrud, PA, Swaney, DL, Wenger, CD, Beauchene, NA, Coon, JJ |
| Journal | ACS Chemical Biology |
| Volume | 5 |
| Pagination | 105-119 |
| Date Published | Jan |
| Type of Article | Review |
| ISBN Number | 1554-8929 |
| Accession Number | ISI:000273653800008 |
| Keywords | Collisional dissociation, Electron-based dissociation, electron-transfer dissociation, embryonic stem-cells, enrichment, False discovery rate, in-vivo, ion affinity-chromatography, isobaric tagging, Isotope labeling, Phosphopeptide, phosphopeptide enrichment, Phosphoproteomics, phosphorylation, Protein phosphorylation, protein-sequence analysis, quantitative phosphoproteomics, reagents, saccharomyces-cerevisiae, Shotgun proteomics, site-specific |
| 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 vivo phosphorylation 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. |
| Short Title | ACS Chem. Biol. |