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- W1964515574 abstract "An involvement of protein tyrosine kinase in the transduction of the signals initiated by nerve growth factor (NGF) was investigated. A tyrosine kinase inhibitor, herbimycin, inhibited neurite outgrowth of rat pheochromocytoma PC12 cells induced by NGF but not that by dibutyryl-cAMP. Herbimycin and genistein blocked NGF-dependent activation of ras p21 whose essential function in neuronal differentiation has been reported. These observations suggested that tyrosine kinase activity is involved in the signaling pathways. K-252a, by contrast, inhibited NGF-induced but not EGF-dependent activation of ras p21. Tyrosine kinase activity of gp140trk, a constituent of NGF receptor, is activated by NGF for much a longer period compared to the activation of EGF receptor autokinase activity by EGF. We further demonstrated that autophosphorylation of gp140trk is selectively inhibited by K-252a." @default.
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- W1964515574 date "1992-06-01" @default.
- W1964515574 modified "2023-10-14" @default.
- W1964515574 title "Specific inhibition of NGF receptor tyrosine kinase activity by K-252a" @default.
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- W1964515574 doi "https://doi.org/10.1016/0167-4889(92)90243-5" @default.
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