Kinomics: methods for deciphering the kinome.

@article{Johnson2005, abstract = {Phosphorylation by protein kinases is the most widespread and well-studied signaling mechanism in eukaryotic cells. Phosphorylation can regulate almost every property of a protein and is involved in all fundamental cellular processes. Cataloging and understanding protein phosphorylation is no easy task: many kinases may be expressed in a cell, and one-third of all intracellular proteins may be phosphorylated, representing as many as 20,000 distinct phosphoprotein states. Defining the kinase complement of the human genome, the kinome, has provided an excellent starting point for understanding the scale of the problem. The kinome consists of 518 kinases, and every active protein kinase phosphorylates a distinct set of substrates in a regulated manner. Deciphering the complex network of phosphorylation-based signaling is necessary for a thorough and therapeutically applicable understanding of the functioning of a cell in physiological and pathological states. We review contemporary techniques for identifying physiological substrates of the protein kinases and studying phosphorylation in living cells.}, author = {Johnson, Sam A. and Hunter, Tony }, citeulike-article-id = {2054430}, doi = {10.1038/nmeth731}, journal = {Nat Methods}, keywords = {adenosine, animal, article-nar, article-predikin, biology, computational, computer-assisted, genetics, genome, human, image, kinase, mass-spec, phosphorylation, processing, protein, proteome, software, structure, techniques, tertiary, triphosphate}, month = {Jan}, number = {1}, pages = {17--25}, posted-at = {2007-12-04 03:22:13}, priority = {2}, title = {Kinomics: methods for deciphering the kinome.}, url = {http://dx.doi.org/10.1038/nmeth731}, volume = {2}, year = {2005} }

TY - JOUR ID - Johnson2005 L3 - citeulike-article-id:2054430 TI - Kinomics: methods for deciphering the kinome. JF - Nat Methods VL - 2 IS - 1 SP - 17 EP - 25 N2 - Phosphorylation by protein kinases is the most widespread and well-studied signaling mechanism in eukaryotic cells. Phosphorylation can regulate almost every property of a protein and is involved in all fundamental cellular processes. Cataloging and understanding protein phosphorylation is no easy task: many kinases may be expressed in a cell, and one-third of all intracellular proteins may be phosphorylated, representing as many as 20,000 distinct phosphoprotein states. Defining the kinase complement of the human genome, the kinome, has provided an excellent starting point for understanding the scale of the problem. The kinome consists of 518 kinases, and every active protein kinase phosphorylates a distinct set of substrates in a regulated manner. Deciphering the complex network of phosphorylation-based signaling is necessary for a thorough and therapeutically applicable understanding of the functioning of a cell in physiological and pathological states. We review contemporary techniques for identifying physiological substrates of the protein kinases and studying phosphorylation in living cells. KW - adenosine KW - animal KW - article-nar KW - article-predikin KW - biology KW - computational KW - computer-assisted KW - genetics KW - genome KW - human KW - image KW - kinase KW - mass-spec KW - phosphorylation KW - processing KW - protein KW - proteome KW - software KW - structure KW - techniques KW - tertiary KW - triphosphate AU - Johnson, Sam AU - Hunter, Tony PY - 2005/Jan// UR - http://dx.doi.org/10.1038/nmeth731 ER -