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Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. Additionally we are shipping Dual Specificity Phosphatase 14 Antibodies (99) and many more products for this protein.
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these findings reveal a novel mechanism by which TRAF2 (show TRAF2 Proteins) mediates Lys63-linked ubiquitination of DUSP14, leading to DUSP14 activation in T cells
findings suggest that DUSP14 negatively regulates TNF (show TNF Proteins)- or IL-1 (show IL1A Proteins)-induced NF-kappaB (show NFKB1 Proteins) activation by dephosphorylating TAK1 (show MAP3K7 Proteins) at Thr (show TRH Proteins)-187
DUSP14 may be a susceptibility gene for pulmonary tuberculosis.
The overproduction, purification and crystal structure at 1.88 A resolution of human dual-specificity phosphatase 14, DUSP14 (MKP6), are reported.
Activation of ATM (show ATM Proteins) by radiation down-regulates phospho-ERK1/2 and its downstream signaling via increased expression of mitogen-activated protein kinase (show MAPK1 Proteins) phosphatase MKP-1 (show DUSP1 Proteins).
The binding of Lipomannan to TLR2 triggers MAPK (show MAPK1 Proteins) activation, followed by an up-regulation of MKP-1 (show DUSP1 Proteins) expression, which in turn may act as a negative regulator of MAPK (show MAPK1 Proteins) activation.
DUSP14 negatively regulates TCR signaling and immune responses by inhibiting TAB1 (show TAB1 Proteins) activation.
dual specificity phosphatases (Dusps) 6 and 14 are up-regulated by activation of beta-catenin (show CTNNB1 Proteins) in murine liver cells
critical role for JNK1 (show MAPK8 Proteins) in the regulation of Mkp1 (show DUSP1 Proteins) induction and in LPS (show TLR4 Proteins)-dependent macrophage activation.
knockdown of CREMalpha or DUSP14 or expression of a dominant-negative form of DUSP14 increased beta-cell line proliferation and enhanced the GLP-1 (show GCG Proteins)-induced proliferation of primary beta-cells
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP14 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009
dual specificity phosphatase 14
, dual specificity protein phosphatase 14
, MAP kinase phosphatase 6
, MKP-1 like protein tyrosine phosphatase
, MKP-1-like protein tyrosine phosphatase
, mitogen-activated protein kinase phosphatase 6
, MAP kinase phsophatase 6
, Mkp-1 like protein tyrosine phosphatase