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Issue 9, 2008
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Linking the kinome and phosphorylome—a comprehensive review of approaches to find kinase targets

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Abstract

Protein phosphorylation is associated with most cell signaling and developmental processes in eukaryotes. Despite the vast extent of the phosphoproteome within the cell, connecting specific kinases with relevant targets remains a significant experimental frontier. The challenge of linking kinases and their substrates reflects the complexity of kinase function. For example, kinases tend to exert their biological effects through supernumerary, redundant phosphorylation, often on multiple protein complex components. Although these types of phosphorylation events are biologically significant, those kinases responsible are often difficult to identify. Recent methods for global analysis of proteinphosphorylation promise to substantially accelerate efforts to map the dynamic phosphorylome. Here, we review both conventional methods to identify kinase targets and more comprehensive genomic and proteomic approaches to connect the kinome and phosphorylome.

Graphical abstract: Linking the kinome and phosphorylome—a comprehensive review of approaches to find kinase targets

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Publication details

The article was received on 30 Jan 2008, accepted on 10 Jun 2008 and first published on 17 Jul 2008


Article type: Review Article
DOI: 10.1039/B801724G
Mol. BioSyst., 2008,4, 920-933

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    Linking the kinome and phosphorylome—a comprehensive review of approaches to find kinase targets

    R. Sopko and B. J. Andrews, Mol. BioSyst., 2008, 4, 920
    DOI: 10.1039/B801724G

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