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- W4246189391 abstract "The mutant pp60F527 protein possesses an activated protein-tyrosine kinase (PTK) activity correlated with a trasforming activity. We have studied the inhibition of the pp60F527 PTK activity by two EGF-R tyrosine kinase inhibitors for the ATP binding site and one of its derivatives, lavendustin C6. In vitro, both molecules were non-competitive inhibitors for the ATP binding site and uncompetitive inhibitors for the peptide binding site. The determined IC50s of the inhibition of pp60F527 kinase activity were 18 μM for lavendustin A and 5 μM for lavendustin C6, as determined on the exogenous substrate enolase, showing that lavendustin C6 was more potent than lavendustin A. Lavendustin C6, but not lavendustin A, inhibited the tyrosine phosphorylation of pp60F527 cellular substrates (the GAP-associated p190, pp125FAK and cortactin) in intact cells. However, this in situ inhibitory effect did not results in a reversion of the morphological changes induced by pp60F527 in cells. On the other hand, lavendustin C6 and lavendustin A exerted antiproliferative effects on cells, suggesting that inhibition of cellular targets related or not to the kinase was also possible." @default.
- W4246189391 created "2022-05-12" @default.
- W4246189391 date "1866-03-01" @default.
- W4246189391 modified "2023-09-30" @default.
- W4246189391 title "Increasing the speed of steamers—Form of propelling blades—The oar and paddle" @default.
- W4246189391 doi "https://doi.org/10.1016/0016-0032(66)90169-4" @default.
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