| First Author | Gschwendt M | Year | 1994 |
| Journal | FEBS Lett | Volume | 338 |
| Issue | 1 | Pages | 85-8 |
| PubMed ID | 8307162 | Mgi Jnum | J:16608 |
| Mgi Id | MGI:64676 | Doi | 10.1016/0014-5793(94)80121-5 |
| Citation | Gschwendt M, et al. (1994) Elongation factor-2 kinase: effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine. FEBS Lett 338(1):85-8 |
| abstractText | The elongation factor-2 (eEF-2) is selectively phosphorylated by the eEF-2 kinase (calmodulin-dependent kinase III). This phosphorylation can be inhibited by calmodulin antagonists, such as CGS 9343B (IC50 = 4 microM). The novel protein kinase inhibitor rottlerin is shown to suppress eEF-2 phosphorylation with an IC50 of 5.3 microM. By contrast, the eEF-2 kinase is rather resistant towards the potent but non-selective protein kinase inhibitor staurosporine (IC50 > 50 microM) and thus can be differentiated from most other protein kinases that are suppressed by staurosporine in the nM range. |
