Using chemical genetics and ATP analogues to dissect protein kinase function.

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dc.contributor.authorElphick, Lucy M.en
dc.contributor.authorLee, Sarah E.en
dc.contributor.authorGouverneur, Veroniqueen
dc.contributor.authorMann, David J.en
dc.date.accessioned2013-10-15T09:50:09Z
dc.date.available2013-10-15T09:50:09Z
dc.date.issued2007
dc.description.abstractProtein kinases catalyze the transfer of the γ-phosphate of ATP to a protein substrate and thereby profoundly alter the properties of the phosphorylated protein. The identification of the substrates of protein kinases has proven to be a very difficult task because of the multitude of structurally related protein kinases present in cells, their apparent redundancy of function, and the lack of absolute specificity of small-molecule inhibitors. Here, we review approaches that utilize chemical genetics to determine the functions and substrates of protein kinases, focusing on the design of ATP analogues and protein kinase binding site mutants.en
dc.funderN/Aen
dc.identifier.citationElphick. L.M. et al. (2007) Using chemical genetics and ATP analogues to dissect protein kinase function. ACS Chemical Biology, 2007, 2 (5), pp. 299-314.en
dc.identifier.doihttps://doi.org/10.1021/cb700027u
dc.identifier.issn1554-8929
dc.identifier.urihttp://hdl.handle.net/2086/9196
dc.language.isoenen
dc.projectidN/Aen
dc.publisherACSen
dc.subjectChemical geneticsen
dc.subjectProtein kinaseen
dc.subjectAdenosine triphosphate (ATP)en
dc.subjectGatekeeper residueen
dc.subjectPhosphorylationen
dc.subjectProtein kinase substrateen
dc.titleUsing chemical genetics and ATP analogues to dissect protein kinase function.en
dc.typeArticleen

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