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- W1538862365 abstract "Stimulation of fibroblasts with basic fibroblast growth factor (bFGF) led to the rapid tyrosine phosphorylation of a number of cellular proteins, including a major substrate of 90 kDa. The methyltransferase inhibitor 5'-methylthioadenosine (MTA) was found to be a specific inhibitor of bFGF-stimulated protein tyrosine phosphorylation in fibroblasts, blocking both receptor autophosphorylation and substrate phosphorylation. MTA had no effect on either epidermal growth factor- or platelet-derived growth factor-stimulated protein tyrosine phosphorylation in fibroblasts. MTA also inhibited both bFGF-stimulated protein tyrosine phosphorylation and neurite outgrowth in PC12 cells. MTA was a specific inhibitor of bFGF-stimulated protein tyrosine phosphorylation only in intact cells. MTA delayed and reduced, but did not inhibit, bFGF internalization and processing. The effects of MTA on bFGF-stimulated tyrosine phosphorylation required only a brief pretreatment with the agent and were readily reversible." @default.
- W1538862365 created "2016-06-24" @default.
- W1538862365 creator A5013055662 @default.
- W1538862365 date "1993-02-01" @default.
- W1538862365 modified "2023-09-29" @default.
- W1538862365 title "Inhibition of the tyrosine kinase activity of the fibroblast growth factor receptor by the methyltransferase inhibitor 5'-methylthioadenosine." @default.
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- W1538862365 doi "https://doi.org/10.1016/s0021-9258(18)53602-4" @default.
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