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Data show that dual specificity phosphatase 5 (DUSP5) is a downstream target of p68 RNA helicase (p68).
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Methylation the DUSP5 gene promoter can serve as an additional means of identifying CIMP-high colorectal cancers.
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DUSP5 expression in skeletal muscle was ninefold higher immediately after exercise and returned to pre-exercise level within 2 h.
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Findings indicate that zinc-finger protein X-linked (ZFX) promotes colorectal cancer (CRC) progression by suppressing dual specificity phosphatase 5 (DUSP5) expression and suggest that ZFX is a prognostic biomarker and potentially useful therapeutic target in stage II/III CRC patients.
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Results show that DUSP5 and DUSP6 mRNA are overexpressed in human PTCs, especially in BRAFV600E mutated papillary thyroid carcinomas (PTCs), and positively control cell migration and invasion.
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role of the secondary binding site in assembling the DUSP5-pERK pre-reactive complex was further demonstrated by molecular dynamics simulations that showed that the remote C197-C219 disulfide linkage controls the structure of the secondary binding pocket based on its redox state (i.e., disulfide/dithiol) and, in turn, the enzymatic activity of DUSP5
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The DUSP5 S147P protein is hypoactive compared to the DUSP5 wild-type protein.
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Data indicate that cells from Burkitt's lymphoma, leukemia, neuroblastoma and Ewing sarcoma showed a higher dual-specificity phosphatase 5 pseudogene 1 (DUSP5P1)/dual specificity phosphatase 5 (DUSP5 ratio than normal cells.
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DUSP1, DUSP4, and DUSP5 differentially modulate endothelial MAPK signaling pathways downstream of Tie-2 receptors.
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DUSP5 methylation may serve as a prognostic marker for gastric cancer (GC), but this requires validation in a larger set of GC samples.
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Studies indicate that dual-specificity MAP kinase phosphatases (MKPs) DUSP6/MKP-3 and DUSP5 are localized in the cytoplasm and nuclear compartments.
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DUSP5 and DUSP6 selectively control ERK pathway activity and proliferation.
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the differential up-regulation of MKP3 by Ets2 and of DUSP5 by c-Jun may converge in similar functional roles for these MAP kinase phosphatases in the growth arrest versus proliferation decisions of breast cancer cells
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In FD-Fms cells, overexpression of human DUSP5 increased M-CSF-dependent proliferation & decreased differentiation. Overexpression in multipotent EGER-Fms cells increased M-CSF-induced proliferation & caused granulocytic, not macrophage, differentiation.
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DUSP5 is a direct target of p53.
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DUSP5 inactivates ERK2 and causes both nuclear translocation and sequestration of inactive ERK2.
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the crystal structure of the catalytic domain of DUSP5 in an active conformation.
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These results suggest the existence of an ERK1/2-driven negative feed-back regulation of ERK5 signaling in epidermal growth factor-stimulated HK-2 cells, which is mediated by MKP-3, DUSP5 and/or MKP-1.
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proper regulation of DUSP5 activity is critical for normal immune system development, IL-2 actions, and tolerance
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mutations in dusp-5 and snrk-1 have been identified in affected tissues of patients with vascular anomalies, implicating the Snrk-1-Dusp-5 signaling pathway in human disease.
