Charging it up: global analysis of protein phosphorylation.

@article{citeulike:822477, abstract = {Protein phosphorylation affects most, if not all, cellular activities in eukaryotes and is essential for cell proliferation and development. An estimated 30\% of cellular proteins are phosphorylated, representing the phosphoproteome, and phosphorylation can alter a protein's function, activity, localization and stability. Recent studies for large-scale identification of phosphosites using mass spectrometry are revealing the components of the phosphoproteome. The development of new tools, such as kinase assays using modified kinases or protein microarrays, enables rapid kinase substrate identification. The dynamics of specific phosphorylation events can now be monitored using mass spectrometry, single-cell analysis of flow cytometry, or fluorescent reporters. Together, these techniques are beginning to elucidate cellular processes and pathways regulated by phosphorylation, in addition to global regulatory networks.}, address = {Department of Molecular Biophysics \& Biochemistry and Molecular, Cellular \& Developmental Biology, Yale University, New Haven, CT 06511, USA.}, author = {Ptacek, Jason and Snyder, Michael }, citeulike-article-id = {822477}, doi = {10.1016/j.tig.2006.08.005}, issn = {0168-9525}, journal = {Trends Genet}, keywords = {global, kinase, mass-spec, phosphorylation}, month = {August}, posted-at = {2008-01-25 00:02:42}, priority = {2}, title = {Charging it up: global analysis of protein phosphorylation.}, url = {http://dx.doi.org/10.1016/j.tig.2006.08.005}, year = {2006} }

TY - JOUR ID - citeulike:822477 L3 - citeulike-article-id:822477 TI - Charging it up: global analysis of protein phosphorylation. JF - Trends Genet AD - Department of Molecular Biophysics & Biochemistry and Molecular, Cellular & Developmental Biology, Yale University, New Haven, CT 06511, USA. SN - 0168-9525 N2 - Protein phosphorylation affects most, if not all, cellular activities in eukaryotes and is essential for cell proliferation and development. An estimated 30% of cellular proteins are phosphorylated, representing the phosphoproteome, and phosphorylation can alter a protein's function, activity, localization and stability. Recent studies for large-scale identification of phosphosites using mass spectrometry are revealing the components of the phosphoproteome. The development of new tools, such as kinase assays using modified kinases or protein microarrays, enables rapid kinase substrate identification. The dynamics of specific phosphorylation events can now be monitored using mass spectrometry, single-cell analysis of flow cytometry, or fluorescent reporters. Together, these techniques are beginning to elucidate cellular processes and pathways regulated by phosphorylation, in addition to global regulatory networks. KW - global KW - kinase KW - mass-spec KW - phosphorylation AU - Ptacek, Jason AU - Snyder, Michael PY - 2006/08/12/ UR - http://dx.doi.org/10.1016/j.tig.2006.08.005 ER -