Rat Dual Serine/Threonine And

Regulation of MAPK Cascades by Protein Tyrosine Phosphatases

, dephosphorylation of any of these two residues is sufficient to inactivate the MAPKs. Thus, the protein serine/threonine phosphatases PP2A and PP2C can inactivate, in intact cells, the MAPKs extracellular signal-regulated kinase 1/2 (ERK1/2) and p38α, respectively

Discovery of Protein Kinase Phosphatase Inhibitors

both kinases and phosphatases in the cell. Dual specificity phosphatases, which act on phosphorylated serine, threonine, and tyrosine residues in proteins, are valid targets for drug discovery. Chemical complementation combines genetic manipulations

Direct Kinase Assay Screening for Inhibitors of MAP Kinase

how anticancer drugs if at all act on this kinase. MAP kinase is activated by sequential phosphorylation on both tyrosine and threonine residues by either the dual tyrosine/threonine kinase MEK (MAPK kinase) alone or by MEK in conjunction