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Chemotherapy increased DUSP9 expression and decreased DUSP16 expression in a HIF1-dependent manner.
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The crystal structure of JNK1 bound to the catalytic domain of MKP7 at 2.4-A resolution, providing high-resolution structural insight into the FXF-docking interaction, is reported.
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The DUSP16 ablation leads to a G1/S transition arrest, reduced incorporation of 5-bromodeoxyuridine, enhanced senescence-associated beta-galactosidase activity, and formation of senescence-associated heterochromatic foci.
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analysis of the interaction of the MAPK binding domain of DUSP16 with p38alpha
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PPARdelta-mediated messenger RNA stabilization of mitogen-activated protein kinase phosphatase (MKP)-7 was responsible for the GW501516-mediated inhibition of JNK signaling.
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Data indicate that the activities of phosphoprotein phosphatases MKP5 and MKP7 were determined in the system.
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Data indicate that LRP6, BCL2L14, DUSP16, CREBL2, and CDKN1B were involed in centromeric (12p11.21-12p13.2) deletion in ETV6-RUNX1 B-cell precursor acute lymphoblastic leukemia (BCP-ALL).
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MKP-7, a negative regulator of JNK, regulates VCAM-1 expression in activated endothelial cells through IRF-1 but not GATA6.
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DUSPs 10 and 16 are positive regulators of activation, apparently acting by modulating cross-talk between the p38 and ERK pathways.
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DUSP16 is a new epigenetically regulated determinant of JNK activation in BL.
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MKP-7 down-regulates ERK-dependent gene expression by blocking nuclear accumulation of phospho-ERK.
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context-dependent role for DUSP16 on cell transformation and apoptosis.
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activation of the ERK pathway strongly blocks JNK activation through stabilization of MKP-7 mediated by phosphorylation
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MKP7 binds beta-arrestin 2 via amino acids 394-443 of MKP7, the same region that interacts with JIP-1
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identification of an intricate SDF-1alpha-induced signaling cascade that involves eNOS, JNK3, and MKP7and enhances endothelial migration