The specificities of protein kinase inhibitors: an update
University of Dundee · MRC Protein Phosphorylation and Ubiquitylation Unit
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.…
Citation impact
- FWCI
- 86.51
- Percentile
- 100%
- References
- 42
Authors
4Topics & keywords
- Kinase
- DYRK1A
- Biochemistry
- Protein-Serine-Threonine Kinases
- Protein kinase A
- Cyclin-dependent kinase
- Biology
- Threonine