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DUSP16 encodes a mitogen-activated protein kinase phosphatase that is a member of the dual specificity protein phosphatase subfamily. Additionally we are shipping DUSP16 Antibodies (54) and many more products for this protein.
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The crystal structure of JNK1 (show MAPK8 Proteins) bound to the catalytic domain of MKP7 at 2.4-A resolution, providing high-resolution structural insight into the FXF-docking interaction, is reported.
The DUSP16 ablation leads to a G1/S transition arrest, reduced incorporation of 5-bromodeoxyuridine, enhanced senescence-associated beta-galactosidase (show GLB1 Proteins) activity, and formation of senescence-associated heterochromatic foci.
analysis of the interaction of the MAPK (show MAPK1 Proteins) binding domain of DUSP16 with p38alpha (show MAPK14 Proteins)
PPARdelta (show PPARD Proteins)-mediated messenger RNA stabilization of mitogen-activated protein kinase (show MAPK1 Proteins) phosphatase (MKP)-7 was responsible for the GW501516-mediated inhibition of JNK (show MAPK8 Proteins) signaling.
Data indicate that the activities of phosphoprotein phosphatases MKP5 (show DUSP10 Proteins) and MKP7 were determined in the system.
Data indicate that LRP6 (show LRP6 Proteins), BCL2L14 (show BCL2L14 Proteins), DUSP16, CREBL2 (show CREBL2 Proteins), and CDKN1B (show CDKN1B Proteins) were involed in centromeric (12p11.21-12p13.2) deletion in ETV6 (show ETV6 Proteins)-RUNX1 (show RUNX1 Proteins) B-cell precursor acute lymphoblastic leukemia (BCP (show OPN1SW Proteins)-ALL).
MKP-7, a negative regulator of JNK (show MAPK8 Proteins), regulates VCAM-1 (show VCAM1 Proteins) expression in activated endothelial cells through IRF-1 (show IRF1 Proteins) but not GATA6 (show GATA6 Proteins).
DUSPs 10 and 16 are positive regulators of activation, apparently acting by modulating cross-talk between the p38 (show CRK Proteins) and ERK (show EPHB2 Proteins) pathways.
DUSP16 is a new epigenetically regulated determinant of JNK (show MAPK8 Proteins) activation in BL.
MKP-7 down-regulates ERK (show EPHB2 Proteins)-dependent gene expression by blocking nuclear accumulation of phospho-ERK (show EPHB2 Proteins).
MAPK phosphatase 7 regulates T cell differentiation via inhibiting ERK (show EPHB2 Proteins)-mediated IL-2 (show IL2 Proteins) expression.
ADCY5 (show ADCY5 Proteins) repression by miR-17 facilitated the translocation of EGFR (show EGFR Proteins) and MKP7 from membrane into cytoplasmic and mitochondrial fractions.
Production of IL-10 (show IL10 Proteins) and its inhibitory effect on IL-12 (show IL12A Proteins) production were unaltered in Dusp16tp/tp macrophages.
the functional role of DUSP16 in Th1 (show HAND1 Proteins)/Th2 balance.
the contrasting effects of acute and chronic stress on insulin (show INS Proteins) sensitivity are driven by changes in subcellular distribution of MKP7 and activated JNK (show MAPK8 Proteins)
DUSP16 is an important regulator of JNK (show MAPK8 Proteins) activity and effector functions of CD4 (show CD4 Proteins) and CD8 (show CD8A Proteins) T cells.
JIP-1 (show MAPK8IP1 Proteins) targets MKP-7 to dephosphorylate JNK (show MAPK8 Proteins).
This gene encodes a mitogen-activated protein kinase phosphatase that is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. The encoded protein specifically regulates the c-Jun amino-terminal kinase (JNK) and extracellular signal-regulated kinase (ERK) pathways.
dual specificity phosphatase 16
, dual specificity protein phosphatase 16-like
, MAP kinase phosphatase 7
, MAPK phosphatase-7
, dual specificity protein phosphatase 16
, mitogen-activated protein kinase phosphatase 7
, MAP kinase phosphatase-7
, map kinase phosphatase-M