articleBiochemical JournalMar 26, 2003GREEN OA

The specificities of protein kinase inhibitors: an update

University of Dundee · MRC Protein Phosphorylation and Ubiquitylation Unit

PubMed
Indexed incrossrefdatacitepubmed

Abstract

We have previously examined the specificities of 28 commercially available compounds, reported to be relatively selective inhibitors of particular serine/threonine-specific protein kinases [Davies, Reddy, Caivano and Cohen (2000) Biochem. J. 351, 95-105]. In the present study, we have extended this analysis to a further 14 compounds. Of these, indirubin-3'-monoxime, SP 600125, KT 5823 and ML-9 were found to inhibit a number of protein kinases and conclusions drawn from their use in cell-based assays are likely to be erroneous. Kenpaullone, Alsterpaullone, Purvalanol, Roscovitine, pyrazolopyrimidine 1 (PP1), PP2 and ML-7 were more specific, but still inhibited two or more protein kinases with similar potency.…

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Authors

4

Topics & keywords

Keywords
  • Kinase
  • DYRK1A
  • Biochemistry
  • Protein-Serine-Threonine Kinases
  • Protein kinase A
  • Cyclin-dependent kinase
  • Biology
  • Threonine
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