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Last Updated: 3 years ago

Possible Interaction: Tyrosine and Dasatinib

supplement:

Tyrosine

Research Papers that Mention the Interaction

Dasatinib markedly inhibited tyrosine phosphorylation of p130 Crk‐associated substrate (p130cas), paxillin and vinculin.
These results suggest that the inhibition of tyrosine phosphorylation of the focal adhesion plaque components by dasatinib may alter the assembly of actin fibers resulting in the activation of RhoA/ROCK pathway.
Cancer medicine  •  2017  |  View Paper
Dasatinib , imatinib, and bosutinib all suppressed tyrosine phosphorylation of PKCδ and inhibited IR-induced apoptosis in vitro.
Molecular Cancer Therapeutics  •  2017  |  View Paper
As dasatinib profoundly inhibited Blk(Y501F)-transformed Ba/F3 cells and tyrosine phosphorylation of Blk in the MyLa2059 cells (Figure 2a), we hypothesized that dasatinib—which is used for treatment of chronic myelogenous leukemia and other malignancies7—has a potential for treatment of CTCL.
Leukemia  •  2014  |  View Paper
In fact, incubation with the Src family kinase inhibitor dasatinib could decrease p27 tyrosine 88 phosphorylation in these patient samples, indicating that p27 phosphorylated on tyrosine 88 may be a therapeutic marker for the treatment of AML patients with tyrosine kinase inhibitors.
Haematologica  •  2017  |  View Paper
Conversely, dasatinib enhanced tyrosine phosphorylation in a panel of RTK and their signaling adaptor complexes, including EGFR, MET/GAB1, and IGF1R/IRS2, implicating a RTK-driven adaptive response associated with dasatinib.
Cancer research  •  2014  |  View Paper
Moreover, dasatinib completely abrogated the phosphorylation of FAK at all tyrosine sites (Y576, Y577, Y861, Y925) with the exception of the autoactivation site (Y397).
Molecular Cancer  •  2010  |  View Paper
In this study, we confirm that dasatinib inhibits tyrosine phosphorylation of SFKs, including Src, Hck, and Lyn, in K562 human CML cells.
Molecular Cancer Therapeutics  •  2007  |  View Paper
Experiments with site‐directed mutants of Pyk2 and Fyn indicated that dasatinib enhanced the binding of Pyk2 autophosphorylated at Tyr402 and the Src homology 2 domain in Fyn.
The FEBS journal  •  2020  |  View Paper
Dasatinib , a potent and specific Src tyrosine kinase inhibitor, was found to decrease the levels of β-dystroglycan phosphorylation on tyrosine and to increase the relative levels of non-phosphorylated β-dystroglycan in sapje zebrafish.
Human molecular genetics  •  2016  |  View Paper