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Activation of the mitogen-activated protein kinase pathway in U937 leukemic cells induces phosphorylation of the amino terminus of the TATA-binding protein.
Distinct domains of the human granulocyte-macrophage colony-stimulating factor receptor alpha subunit mediate activation of Jak/Stat signaling and differentiation.
Regulation of dual-specificity phosphatases M3/6 and hVH5 by phorbol esters. Analysis of a delta-like domain.
Elevation of receptor tyrosine kinases by small molecule AKT inhibitors in prostate cancer is mediated by Pim-1.
Interaction of the growth hormone receptor cytoplasmic domain with the JAK2 tyrosine kinase.
Co-purification of mitogen-activated protein kinases with phorbol ester-induced c-Jun kinase activity in U937 leukaemic cells.
The kinase domain of Jak2 mediates induction of bcl-2 and delays cell death in hematopoietic cells.
Tyrosine kinase and phosphotyrosine phosphatase activity in human promyelocytic leukemia cells and human polymorphonuclear leukocytes.
Regions of the JAK2 tyrosine kinase required for coupling to the growth hormone receptor.
The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulating factor receptor beta c chain.
Multiple signal transduction pathways mediate c-Jun protein phosphorylation.
Growth hormone receptor cytoplasmic domain differentially promotes tyrosine phosphorylation of signal transducers and activators of transcription 5b and 3 by activated JAK2 kinase.
The cytoplasmic domain of granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor alpha subunit is essential for both GM-CSF-mediated growth and differentiation.
Receptor Protein-Tyrosine Kinases
The Pim-1 protein kinase is an important regulator of MET receptor tyrosine kinase levels and signaling.
Protein Tyrosine Kinases