Kinomics: methods for deciphering the kinome View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-01

AUTHORS

Sam A Johnson, Tony Hunter

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. More... »

PAGES

17

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nmeth731

    DOI

    http://dx.doi.org/10.1038/nmeth731

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1033723733

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/15789031


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