Relevant bibliographies by topics / DUSP12

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Academic literature on the topic 'DUSP12'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "DUSP12"

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Chen, Hsueh-Fen, Huai-Chia Chuang, and Tse-Hua Tan. "Regulation of Dual-Specificity Phosphatase (DUSP) Ubiquitination and Protein Stability." International Journal of Molecular Sciences 20, no. 11 (May 30, 2019): 2668. http://dx.doi.org/10.3390/ijms20112668.

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Mitogen-activated protein kinases (MAPKs) are key regulators of signal transduction and cell responses. Abnormalities in MAPKs are associated with multiple diseases. Dual-specificity phosphatases (DUSPs) dephosphorylate many key signaling molecules, including MAPKs, leading to the regulation of duration, magnitude, or spatiotemporal profiles of MAPK activities. Hence, DUSPs need to be properly controlled. Protein post-translational modifications, such as ubiquitination, phosphorylation, methylation, and acetylation, play important roles in the regulation of protein stability and activity. Ubiquitination is critical for controlling protein degradation, activation, and interaction. For DUSPs, ubiquitination induces degradation of eight DUSPs, namely, DUSP1, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8, DUSP9, and DUSP16. In addition, protein stability of DUSP2 and DUSP10 is enhanced by phosphorylation. Methylation-induced ubiquitination of DUSP14 stimulates its phosphatase activity. In this review, we summarize the knowledge of the regulation of DUSP stability and ubiquitination through post-translational modifications.
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Chuang and Tan. "MAP4K Family Kinases and DUSP Family Phosphatases in T-Cell Signaling and Systemic Lupus Erythematosus." Cells 8, no. 11 (November 13, 2019): 1433. http://dx.doi.org/10.3390/cells8111433.

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T cells play a critical role in the pathogenesis of systemic lupus erythematosus (SLE), which is a severe autoimmune disease. In the past 60 years, only one new therapeutic agent with limited efficacy has been approved for SLE treatment; therefore, the development of early diagnostic biomarkers and therapeutic targets for SLE is desirable. Mitogen-activated protein kinase kinase kinase kinases (MAP4Ks) and dual-specificity phosphatases (DUSPs) are regulators of MAP kinases. Several MAP4Ks and DUSPs are involved in T-cell signaling and autoimmune responses. HPK1 (MAP4K1), DUSP22 (JKAP), and DUSP14 are negative regulators of T-cell activation. Consistently, HPK1 and DUSP22 are downregulated in the T cells of human SLE patients. In contrast, MAP4K3 (GLK) is a positive regulator of T-cell signaling and T-cell-mediated immune responses. MAP4K3 overexpression-induced RORγt–AhR complex specifically controls interleukin 17A (IL-17A) production in T cells, leading to autoimmune responses. Consistently, MAP4K3 and the RORγt–AhR complex are overexpressed in the T cells of human SLE patients, as are DUSP4 and DUSP23. In addition, DUSPs are also involved in either human autoimmune diseases (DUSP2, DUSP7, DUSP10, and DUSP12) or T-cell activation (DUSP1, DUSP5, and DUSP14). In this review, we summarize the MAP4Ks and DUSPs that are potential biomarkers and/or therapeutic targets for SLE.
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Lim, S., J. A. Green, H. Wong, M. E. VanderBurg, and T. Crook. "DUSP7 and DUSP8 promoter hypermethylations: Predictors of clinical outcomes in advanced epithelial ovarian carcinoma." Journal of Clinical Oncology 25, no. 18_suppl (June 20, 2007): 5501. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.5501.

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5501 Background: The Dual specificity phosphatases (DUSPs) are a subclass of the protein tyrosine phosphatase (PTP) gene family which appears to be selective for dephosphorylating the critical phosphothreonine and phosphotyrosine residues within the mitogen-activated protein kinases (MAPKs) leading to inactivation. MAPK activation is a downstream target of several oncogenes and may give rise to oncogenic transformation, and hence DUSPs are potential tumor suppressor genes. The aim of this study was to investigate if DUSPs are subject to methylation-dependent silencing in epithelial ovarian cancer. Methods: In this study, promoter methylation and gene expression of the DUSPs genes (DUSP1, DUSP2, DUSP3, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8 and DUSP10) were investigated in 9 ovarian cancer cell lines and in 74 primary epithelial ovarian tumors (Stage III/IV), using methylation specific PCR (MSP) and Reverse- transcription PCR (RT-PCR). The 74 clinical samples were retrospectively retrieved from a large Phase III RCT (the EORTC 55931/NCIC OV10) with clinical follow-up in excess of 6.5 years. Results: Ovarian Cancer Cell lines: Aberrant CpG methylation detected in DUSP1, DUSP2, DUSP4, DUSP6, DUSP7 and DUSP8. DUSP7 promoter methylation was associated with downregulation of mRNA expression. Primary Ovarian Tumors: Methylation of DUSP1, DUSP2, DUSP7 and DUSP8 was observed in 15–38% of the primary tumors. DUSP7 methylation is a predictor of adverse PFS in both univariate (median PFS 10.6 m versus 13.3m, p=0.002) and multivariate (Cox Regression HR 2.76, p<0.001) analyses, and is associated with a trend for poorer OS (22.1 m versus 29.3 m, p=0.07). In contrast, DUSP8 methylation is an independent predictor of favorable PFS (median 23.7m versus 11.5m; Cox Regression HR 0.30, p=0.006) and OS (HR 0.31, p=0.013). 5-year OS for DUSP8 methylated patients was 58.3% compared with 16.1% for DUSP8 unmethylated (HR 0.277, p=0.005). Conclusion: This is the first report of DUSP methylation in epithelial ovarian cancer. The study suggests that methylation-dependent transcriptional silencing of DUSP7 in advanced epithelial ovarian cancer may represent an independent predictor of adverse PFS. DUSP8 methylation, on the other hand, is a favorable clinical outcome marker. No significant financial relationships to disclose.
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Li, Wei-ming, Yi-fan Zhao, Guo-fu Zhu, Wen-hui Peng, Meng-yun Zhu, Xue-jing Yu, Wei Chen, Da-chun Xu, and Ya-wei Xu. "Dual specific phosphatase 12 ameliorates cardiac hypertrophy in response to pressure overload." Clinical Science 131, no. 2 (December 23, 2016): 141–54. http://dx.doi.org/10.1042/cs20160664.

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Pathological cardiac hypertrophy is an independent risk factor of heart failure. However, we still lack effective methods to reverse cardiac hypertrophy. DUSP12 is a member of the dual specific phosphatase (DUSP) family, which is characterized by its DUSP activity to dephosphorylate both tyrosine and serine/threonine residues on one substrate. Some DUSPs have been identified as being involved in the regulation of cardiac hypertrophy. However, the role of DUSP12 during pathological cardiac hypertrophy is still unclear. In the present study, we observed a significant decrease in DUSP12 expression in hypertrophic hearts and cardiomyocytes. Using a genetic loss-of-function murine model, we demonstrated that DUSP12 deficiency apparently aggravated pressure overload-induced cardiac hypertrophy and fibrosis as well as impaired cardiac function, whereas cardiac-specific overexpression of DUPS12 was capable of reversing this hypertrophic and fibrotic phenotype and improving contractile function. Furthermore, we demonstrated that JNK1/2 activity but neither ERK1/2 nor p38 activity was increased in the DUSP12 deficient group and decreased in the DUSP12 overexpression group both in vitro and in vivo under hypertrophic stress conditions. Pharmacological inhibition of JNK1/2 activity (SP600125) is capable of reversing the hypertrophic phenotype in DUSP12 knockout (KO) mice. DUSP12 protects against pathological cardiac hypertrophy and related pathologies. This regulatory role of DUSP12 is primarily through c-Jun N-terminal kinase (JNK) inhibition. DUSP12 could be a promising therapeutic target of pathological cardiac hypertrophy. DUSP12 is down-regulated in hypertrophic hearts. An absence of DUSP12 aggravated cardiac hypertrophy, whereas cardiomyocyte-specific DUSP12 overexpression can alleviate this hypertrophic phenotype with improved cardiac function. Further study demonstrated that DUSP12 inhibited JNK activity to attenuate pathological cardiac hypertrophy.
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Qiu, Tao, Tianyu Wang, Jiangqiao Zhou, Zhongbao Chen, Jilin Zou, Long Zhang, and Xiaoxiong Ma. "DUSP12 protects against hepatic ischemia–reperfusion injury dependent on ASK1-JNK/p38 pathway in vitro and in vivo." Clinical Science 134, no. 17 (September 2020): 2279–94. http://dx.doi.org/10.1042/cs20191272.

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Abstract Hepatic ischemia–reperfusion (I/R) injury is an important risk factor resulting in liver failure during liver surgery. However, there is still lack of effective therapeutic methods to treat hepatic I/R injury. DUSP12 is a member of the dual specific phosphatase (DUSP) family. Some DUSPs have been identified as being involved in the regulation of hepatic I/R injury. However, the role of DUSP12 during hepatic I/R injury is still unclear. In the present study, we observed a significant decrease in DUSP12 expression in a hepatic I/R injury mouse model in vivo and in hypoxia/reoxygenation (H/R) model in vitro. Using hepatocyte-specific DUSP12 knockout mice and DUSP12 transgenic mice, we demonstrated that DUSP12 apparently relieved I/R-induced liver injury. Moreover, DUSP12 inhibited hepatic inflammatory responses and alleviated apoptosis both in vitro and in vivo. Furthermore, we demonstrated that JNK and p38 activity, but not ERK1/2, was increased in the DUSP12-deficient mice and decreased in the DUSP12 transgenic mice under I/R condition. ASK1 was required for DUSP12 function in hepatic I/R injury and inhibition of ASK1 prevented inflammation and apoptosis in DUSP12-deficient hepatocytes and mice. In conclusion, DUSP12 protects against hepatic I/R injury and related inflammation and apoptosis. This regulatory role of DUSP12 is primarily through ASK1-JNK/p38 signaling pathway. Taken together, DUSP12 could be a potential therapeutic target for hepatic I/R injury.
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Ju, Gaoda, Tianhao Zhou, Rui Zhang, Xiaozao Pan, Bing Xue, and Sen Miao. "DUSP12 regulates the tumorigenesis and prognosis of hepatocellular carcinoma." PeerJ 9 (August 3, 2021): e11929. http://dx.doi.org/10.7717/peerj.11929.

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Background Dual specificity protein phosphatase (DUSP)12 is an atypical member of the protein tyrosine phosphatase family, which are overexpressed in multiple types of malignant tumors. This protein family protect cells from apoptosis and promotes the proliferation and motility of cells. However, the pathological role of DUSP12 in hepatocellular carcinoma (HCC) is incompletely understood. Methods We analyzed mRNA expression of DUSP12 between HCC and normal liver tissues using multiple online databases, and explored the status of DUSP12 mutants using the cBioPortal database. The correlation between DUSP12 expression and tumor-infiltrating immune cells was demonstrated using the Tumor Immune Estimation Resource database and the Tumor and Immune System Interaction Database. Loss of function assay was utilized to evaluate the role of DUSP12 in HCC progression. Results DUSP12 had higher expression along with mRNA amplification in HCC tissues compared with those in normal liver tissues, which suggested that higher DUSP12 expression predicted shorter overall survival. Analyses of functional enrichment of differentially expressed genes suggested that DUSP12 regulated HCC tumorigenesis, and that knockdown of DUSP12 expression by short hairpin (sh)RNA decreased the proliferation and migration of HCC cells. Besides, DUSP12 expression was positively associated with the infiltration of cluster of differentiation (CD)4+ T cells (especially CD4+ regulatory T cells), macrophages, neutrophils and dendritic cells. DUSP12 expression was positively associated with immune-checkpoint moieties, and was downregulated in a C3 immune-subgroup of HCC (which had the longest survival). Conclusion These data suggest that DUSP12 may have a critical role in the tumorigenesis, infiltration of immune cells, and prognosis of HCC.
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Boldorini, Renzo, Nausicaa Clemente, Elisa Alchera, and Rita Carini. "DUSP12 acts as a novel endogenous protective signal against hepatic ischemia–reperfusion damage by inhibiting ASK1 pathway." Clinical Science 135, no. 1 (January 2021): 161–66. http://dx.doi.org/10.1042/cs20201091.

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Abstract Ischemia–reperfusion injury (IRI) consequent to major liver surgery is a still unmet clinical problem. The activation of endogenous systems of hepatoprotection can prevent the damaging effects of ischemia–reperfusion (IR) as shown by the phenomenon known as ‘ischemic preconditioning’. The identification of endogenous signal mediators of hepatoprotection is of main interest since they could be targeted in future therapeutic interventions. Qiu et al. recently reported in Clin. Sci. (Lond.) (2020) 134(17), 2279–2294, the discovery of a novel protective molecule against hepatic IR damage: dual-specificity phosphatase 12 (DUSP12). IR significantly decreased DUSP12 expression in liver whereas DUSP12 overexpression in hepatocytes protected IRI and DUSP12 deletion in DUSP12 KO mice exacerbated IRI. The protective effects of DUSP12 depended on apoptosis signal-regulating kinase 1 (ASK1) and acted through the inhibition of the ASK1-dependent kinases c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (MAPK). These results enlighten DUSP12 as a novel intermediate negative regulator of the pro-inflammatory and pro-apoptotic ASK1/JNK-p38 MAPK pathway activated during hepatic IR and identify DUSP12 as potential therapeutic target for IRI.
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Bermudez, O., G. Pagès, and C. Gimond. "The dual-specificity MAP kinase phosphatases: critical roles in development and cancer." American Journal of Physiology-Cell Physiology 299, no. 2 (August 2010): C189—C202. http://dx.doi.org/10.1152/ajpcell.00347.2009.

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Intracellular signaling by mitogen-activated protein (MAP) kinases (MAPK) is involved in many cellular responses and in the regulation of various physiological and pathological conditions. Tight control of the localization and duration of extracellular-regulated kinase (ERK), c-Jun NH2-terminal kinase (JNK), or p38 MAPK activity is thus a fundamental aspect of cell biology. Several members of the dual-specificity phosphatase (DUSPs) family are able to dephosphorylate MAPK isoforms with different specificity, cellular, and tissue localization. Understanding how these phosphatases are themselves regulated during development or in physiological and pathological conditions is therefore fundamental. Over the years, gene deletion and knockdown studies have completed initial in vitro studies and shed a new light on the global and specific roles of DUSPs in vivo. Whereas DUSP1, DUSP2, and DUSP10 appear as crucial players in the regulation of immune responses, other members of the family, like the ERK-specific DUSP6, were shown to play a major role in development. Recent findings on the involvement of DUSPs in cancer progression and resistance will also be discussed.
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Hahn, Cynthia K., Rachel J. West, Elizabeth R. Macari, Emily K. Schaeffer, and Christopher H. Lowrey. "Dual-Specificity Phosphatases (DUSPs) Are Potential Targets for Pharmacologic Induction of Fetal Hemoglobin." Blood 116, no. 21 (November 19, 2010): 2075. http://dx.doi.org/10.1182/blood.v116.21.2075.2075.

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Abstract Abstract 2075 Morbidities of sickle cell anemia and β-thalassemia can be alleviated by increased fetal hemoglobin (HbF) production. However, currently available HbF inducing agents, such as HU, butyrate, and DNA methyltransferase inhibitors are not ideal due to suppression of hematopoiesis and other short and long-term side effects. Our goal is to identify novel HbF induction strategies that have the safety, efficacy and ease of use to make them applicable to most hemoglobinopathy patients. Recently, we proposed that most inducing agents increase γ-globin gene expression through activation of cell stress signaling pathways, including the p38 MAPK pathway (Mabaera et al, Exp Hematol. 2008). Evidence supporting the involvement of p38 signaling in HbF induction includes publications from multiple groups showing that γ-globin mRNA induction by several agents activates p38 signaling and can be suppressed by inhibitors of p38. Our lab has shown that physical stresses such as hyperosmotic shock, UV and X-ray irradiation, and heat shock are capable of activating p38 and inducing γ-globin mRNA expression in erythroid cells that is blocked by SB203580, a p38 inhibitor. If our model is correct, strategies that increase p38 signaling without cellular stress could be therapeutically beneficial. One possible approach is inhibition of the dual-specificity phosphatases (DUSPs) that are induced by MAPK signaling and then feedback to dephosphorylate activated MAPKs including p38. If this model is correct, suppression of DUSP activity could increase basal levels of p38 signaling without stress. Regulation of specific MAPK pathways by different DUSPs is cell-type and stress-type dependent. To determine which DUSPs are likely to be involved in p38 signaling in erythroid cells, we first used RT-PCR to determine which of ten DUSPs that are known to modulate MAPK signaling (DUSPs 1, 2, 4, 5, 6, 7, 8, 9, 10, and 16) are expressed in human erythroid progenitors and K562 cells. All ten DUSPs were expressed in both cell types. Next, we determined the effects of hemin (10 and 20μM) and Na butyrate (1 and 2mM), two known inducers of HbF and p38 MAPK signaling, on mRNA levels of the ten DUSP genes in K562 cells. γ-globin mRNA was induced by both drugs at these doses. DUSP gene expression was assessed during a short time course ranging from 5 minutes to 5 hours and a longer time course from 24 to 72 hours. At early time points, DUSP5 expression was induced up to 4-fold with both drugs when compared to untreated controls. DUSP5 continued to have the greatest level of induction at later time points (up to 8-fold) while DUSP4 and DUSP6 reached maximum induction (up to 4-fold) at 72 hours. Treatment of K562 cells with a small molecule inhibitor of DUSP1 and DUSP6, (E)-2-benzylidene-3-(cyclohexylamino)-2,3-dihydro-1H-iden-1-one (BCI, gift of Dr. John Lazo) at 1μM increased γ-globin mRNA levels 5-fold, similar to levels seen with hemin and butyrate, and increased p38 phosphorylation by western blotting. Together, these data suggest that DUSPs may be a molecular target for the development of novel HbF inducing agents. Disclosures: No relevant conflicts of interest to declare.
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De Roock, W., M. Janssens, B. Biesmans, B. Jacobs, J. De Schutter, S. Fieuws, E. Van Cutsem, and S. Tejpar. "DUSPs as markers of MEK/Erk activation in primary colorectal cancer." Journal of Clinical Oncology 27, no. 15_suppl (May 20, 2009): 4064. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.4064.

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4064 Background: DUSPs dephosphorylate P-MAPK and are activated as a negative feedback loop upon RTK signaling. Higher expression of DUSP 4 & 6 is also found in cells with constitutive Erk activation like KRAS mutant (MUT) cells (Bild et al. Nature 2005). We correlated DUSP1, 4, 6 (isoforms a & b) & 8 mRNA expression level in FFPE primary colorectal cancer (CRC) of 186 chemorefractory patients treated with cetuximab (CTX) with KRAS MUT state and progression-free survival (PFS) and overall survival (OS). Methods: KRAS codon 12,13, 61&146, BRAF V600E and NRAS codon 12&13 MUT were analyzed with the Sequenom MALDI TOF MassArray system. The DUSPs and 3 housekeeping genes were quantified by qRT-PCR. TwoStep cluster analysis was performed. PFS and OS were estimated by the Kaplan-Meier method. Results: KRAS MUT was associated with increased DUSP4 (MWU;p=.0006) & 6a (p=.0067). DUSP6a dephosphorylates P-Erk, DUSP4 also dephosphorylates P-JNK & P-p38. DUSP1 & 8 primarily dephosphorylate P-JNK & P-p38 and were not associated with KRAS MUT. KRAS MUT clustered into 3 groups according to DUSP4 expression: 32 high, 38 median & 13 low (t- test;p<.0001). The low MUT expression was comparable to wild-type (WT) expression. KRAS WT clustered into 2 groups: 69 low & 24 high DUSP4 (ANOVA;p<.0001). 7/24 of high expressors were found to have a BRAF or NRAS MUT. The 32 MUT high expressors had a longer median PFS (log-rank;p=.015) and OS (p=.065) after CTX. The 17 KRAS/BRAF/NRAS WT high expressors had a shorter median OS (p=.026), but not PFS (p=.745). Conclusions: There is a significantly higher DUSP4 & 6a mRNA expression in the KRAS MUT compared to WT primary CRC. However, this is not a black and white observation. In the KRAS MUT there are 3 distinct clusters of DUSP4 expression. The high expressors (= supposed attenuated Erk signaling) have a longer PFS and OS after CTX. Adaptation to constitutive KRAS signaling with differential levels of MEK/Erk activation needs to be further investigated and will be of help in selecting patients for therapy with MEK inhibitors. It suggests not all KRAS MUT will be good candidates for MEK inhibitors. In the cluster of high DUSP4 expressing KRAS WT 30% are BRAF or NRAS MUT. This suggests DUSP expression of FFPE samples could be a more sensitive marker of MEK/Erk activation and resistance to EGFR inhibitors than KRAS MUT analysis alone. [Table: see text]
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Dissertations / Theses on the topic "DUSP12"

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Cain, Erica L. "An investigation of the oncogenic potential and function of the dual specificity phosphatase 12." Diss., Kansas State University, 2012. http://hdl.handle.net/2097/16694.

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Doctor of Philosophy
Department of Biology
Alexander Beeser
Large-scale genomic approaches have demonstrated many atypical dual specificity phosphatases (DUSPs) are differentially expressed or mutated in cancer. DUSPs are proteins predicted to have the ability to dephosphorylate Ser/Thr and Tyr residues, and the atypical DUSP subgroup contains at least 16 members with diverse substrates that include proteins, nucleic acids, and sugars, and some of the atypical DUSPs function in the cell not as phosphatases but as scaffolds in signal transduction pathways. Of the atypical DUSPs, DUSP12 is one of the most evolutionarily conserved with homologs found in organisms ranging from yeast to humans. DUSP12 is of particular interest as it has been identified to be one of only two candidate genes for the target of a genetic amplification found in liposarcomas. Furthermore, DUSP12 may be an oncogene in that over-expression of dusp12 in cell culture promotes apoptosis resistance, cell motility, and the up-regulation of two established oncogenes, the hepatocyte growth factor receptor (c-met) and integrin alpha 1 (itga1). Additionally, DUSP12 may protect from apoptosis by functioning as a regulator of stress-induced translation repression and stress granule formation that may be due to its interaction with the DEAD Box RNA Helicase, DDX3.
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Buffet, Camille. "Anomalies moléculaires de la voie MAPK et cancer papillaire de la thyroïde : étude de deux phosphatases spécifiques de ERK, DUSP5 et DUSP6." Thesis, Paris 5, 2014. http://www.theses.fr/2014PA05T049/document.

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Le cancer papillaire de la thyroïde (CPT) est la tumeur endocrine la plus fréquente. Des anomalies moléculaires activant la voie des MAPK (Mitogen-Activated Protein Kinases) sont identifiées, de façon mutuellement exclusive, dans environ 70% des cas. Il s’agit de réarrangements chromosomiques, le plus souvent de type RET/PTC (10%), de mutations ponctuelles activatrices des trois isoformes de l’oncogène RAS (H, N et K-RAS) (10%), ou de l’oncogène B-RAF (50%). La mutation « hot spot » B-RAFV600E est la plus fréquemment identifiée, elle est associée à une plus grande agressivité clinique (diagnostic à un stade tardif, risque de récidives et de décès accru). Ces évènements moléculaires ont pour conséquence commune l’activation de la voie des MAPK, se traduisant en aval par la phosphorylation de MEK (Mitogen-activated Extracellular signal-Regulated Kinase) puis de ERK (Extracellular signal-Regulated Kinase). Cette dernière est régulée négativement par des phosphatases, appartenant à la famille des Dual Specificity Phosphatases (DUSPs), d’expression ubiquitaire, et en particulier de deux phosphatases spécifiques de ERK, l’une cytoplasmique (DUSP6) et l’autre nucléaire (DUSP5). Nous avons fait l’hypothèse que ces phosphatases pouvaient être soit des gènes suppresseurs de tumeurs (leur perte d’expression conduisant à une augmentation de phosphorylation de ERK et une prolifération accrue), soit des marqueurs du degré d’activation de la voie MAPK dans le cadre d’une boucle de rétrocontrôle négatif. Ceci nous a conduits à analyser la régulation et l’expression de ces phosphatases dans trois modèles : la lignée cellulaire PCCL3 (thyroïde de rat), exprimant l’un des trois principaux oncogènes mutés dans les CPT (RET/PTC3 ou H-RASV12 ou B-RAFV600E) sous le contrôle d’un promoteur inductible par la doxycycline, des lignées cellulaires humaines dérivant de CPT et des CPT humains. (...)
Papillary thyroid cancer (PTC) is the most common endocrine malignancy. Mutually exclusive and activating alterations of the MAPK pathway (Mitogen-Activated Protein Kinases) are identified in 70% of cases. Common mutations found in PTCs are point mutation of the B-RAF (50%) and RAS genes (10%) as well as RET/PTC chromosomal rearrangements (10%). The hot spot B-RAFV600E mutation is the most frequently alteration identified and is connected with agressive clinical characteristics (high stage at diagnosis, high recurrence risk and death). These molecular events lead to constitutive activation of the MAPK pathway, resulting in MEK (Mitogen-activated Extracellular signal-Regulated Kinase) and ERK (Extracellular signal-Regulated Kinase) phosphorylation. ERK is negatively regulated by phosphatases and among them, Dual Specificity Phosphatases (DUSPs), ubiquitary expressed, in particular two ERK-specific phosphatases DUSP5 (nuclear) and DUSP6 (cytosolic). We hypothesized that these phosphatases could have tumor supressor properties (i.e. their loss would be associated with an increase in MAPK pathway activation) or may serve as a surrogate marker of MAPK pathway activation in the context of a negative feedback loop. We analysed regulation and expression of both phosphatases in 3 models: three PCCL3 cell lines (rat thyroid cells) expressing one of the most common oncogene identified in PTCs (RET/PTC3 or H-RASV12 or B-RAFV600E) under the control of a doxycycline-inducible promoter, human PTC-derived cell lines and human PTC. We demonstrated that MAPK pathway activation was correlated with induction of DUSP5 and DUSP6. These phosphatases are involved in a negative feedback loop that contributes to a tight regulation of phospho-ERK levels. DUSP5 and DUSP6 mRNA are overexpressed in human PTCs, especially in B-RAF mutated tumors suggesting a higher MAPK signaling output in these agressive PTCs. Silencing of DUSP5 and/or DUSP6 by small interfering RNA does not affect proliferation of human B-RAFV600E thyroid carcinoma-derived cell lines, suggesting the lack of tumor suppressor gene role. Compensatory changes in expression of DUSPs when a specific one is inactivated may explain this lack of effect. On the opposite, a DUSP6 pharmacological inhibitor induced a concentration dependent decrease in proliferation of human B-RAFV600E cells, suggesting « off-target » effect of this inhibitor. In a second part, we analysed the regulation of DUSP5 expression, which is a target of the MAPK pathway activation. We demonstrated, using pharmacological inhibitors, that DUSP5 is an early response gene, regulated mostly by the MAPK pathway, at the transcriptional level. Two contiguous CArG boxes that bind serum response factor (SRF) were found in a 1Kb promoter region, as well as several E twenty-six transcription factor family binding sites (EBS). These sites potentially bind Elk-1, a transcription factor activated by ERK1/2. Using wild type or mutated DUSP5 promoter reporters, we demonstrated that SRF plays a crucial role in serum induction of DUSP5 promoter activity, the proximal CArG box being important for SRF binding in vitro and in living cells. Moreover Elk-1 was bound in vitro to a promoter region containing the proximal CArG box and a putative EBS. Its specific binding to SRF was necessary to elicit promoter response to dominant positive Elk-VP16 and to enhance the response to serum stimulation. Altogether our results suggest that the MAPK pathway is more active in B-RAFV600E PTC than in PTC with other genetic alteration and could explain their clinical agressivity. DUSP5 and DUSP6, as well as phosphorylated MEK, are markers of activation of the MAPK pathway. Neither phosphatase has tumor suppressor properties in our thyroid cancer cell models. Our results suggest redundancy and functional compensation among DUSPs. (...)
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Patterson, Kate Isabel Garvan Institute of Medical Research Faculty of Medicine UNSW. "Characterisation of the atypical dual specificity phosphatase DUSP26." Publisher:University of New South Wales. Garvan Institute of Medical Research, 2009. http://handle.unsw.edu.au/1959.4/43594.

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In many ways cancer is a disease of cellular signalling disequilibrium. When the equilibrium of key signalling pathways is upset, critical biological functions such as cell growth, survival, motility, proliferation, metabolism and apoptosis are affected, and can lead to the initiation of cancer. Reversible protein phosphorylation is an extremely important mechanism by which the activity of enzymes and proteins in signalling cascades can be regulated. Dual specificity phosphatases (DUSPs) are a unique subgroup of the protein tyrosine phosphatases (PTPs) in that they can dephosphorylate both phospho-tyrosine and phospho-serine/threonine residues within the one substrate. Many DUSPs have been implicated in cancer as critical regulators of key cancer- associated signalling cascades including the mitogen activated protein kinase (MAPK) pathway. Transcript profiling of 51 primary ovarian tumours and four normal ovaries as controls identified an uncharacterised atypical DUSP, DUSP26 as being potentially down-regulated in all histological subtypes of ovarian cancer compared with normal ovaries. DUSP26 is located at 8p12, a chromosomal region previously shown to exhibit allelic imbalance in ovarian cancer. DUSP26 is predominantly expressed in neuro-endocrine tissue, with high expression also in skeletal muscle, prostate and ovary. DUSP26 mRNA expression is reduced in brain cancer, neuroblastoma, and ovarian cancer cell lines compared to normal, consistent with a role for DUSP26 as a tumour suppressor gene. Furthermore, DUSP26 can negatively affect the proliferation of epithelial cells, also consistent with a role as a tumour suppressor gene. Expression of DUSP26 in primary ovarian cancer samples is variable however, and analysis of DUSP26 protein expression is required to reconcile these results. Preliminary results suggest that DUSP26 is epigenetically regulated and that hypermethylation may contribute to its silencing in cancer. In the literature, there is great controversy in regards to the substrate specificity of DUSP26. Results presented in this thesis conclusively demonstrate that DUSP26 is not a MAPK phosphatase, despite reports to the contrary. Instead, using a substrate trapping approach, two novel potential DUSP26 substrates were identified: DNA-dependent protein kinase (DNA-PK) and nuclear mitotic apparatus protein (NuMA), which are often dysregulated in cancer. Consequently, DUSP26 may affect the pathogenesis of cancer via DNA-PK and or NuMA.
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Casteel, Maximilian Wilhelm. "Bedeutung von DUSP1 und Expression MAPKinasen-spezifischer Transkriptionsfaktoren während der zellulären Antwort auf Deoxynivalenol." Diss., lmu, 2011. http://nbn-resolving.de/urn:nbn:de:bvb:19-128239.

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Abraham, Sonya Marie. "Dual specificity phosphatase 1 (DUSP1): an important regulator of the anti-inflammatory actions of glucocorticoids?" Thesis, Imperial College London, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.486756.

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The Mitogen Activated Protein Kinases (MAPKs) are a family of serine/threonine kinases that orchestrate changes in gene expression in response to extracellular stimuli. The c-Jun N-terminal kinase (JNK) and p38 MAPK subfamilies are strongly activated by pro-inflammatory stimuli such as UV light, cytokines such as Interleukin-l (IL-I), and pathogen-associated molecules, for example lipopolysaccharide (LPS). The JNK and p38 signalling pathways control the expression of many inflammatory mediators, including tumour necrosis factor a (lNFa) and cyclooxygenase 2 (COX-2). Activation of MAPKs requires their phosphorylation at particular threonine and tyrosine residues. Conversely, inactivation of the MAPKs is achieved by removal of the activating phosphate groups by various threonine / serine-, tyrosine-, or dual specificity phosphatases. This phosphatase-mediated inactivation ofp38 and JNK is thought to be critical for limiting the strength and duration ofan inflammatory response.We and others have shown that the dual-specificity phosphatase, DUSPI is transiently upregulated by proinflammatory stimuli such as UV light, IL-I or LPS. It is also upregulated in a more sustained fashion by the glucocorticoid dexamethasone, a powerful anti-inflammatory agonist. The induction of DUSPI gene expression coincides with the inactivation of JNK and p38. We hypothesised that DUSPI plays a role in the limitation of inflammatory responses via a negative feedback loop, and that the sustained induction of DUSPI contributes to the anti-inflammatory effects ofglucocorticoids. To test these hypotheses we have investigated inflammatory responses of cells from a DUSPI knock-out mouse.
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Manley, Grace C. A. "The roles of DUSPs in respiratory viral infection." Thesis, University of Sheffield, 2018. http://etheses.whiterose.ac.uk/19257/.

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Emond-Boisjoly, Marc-Alexandre. "Rôle de la protéine DUSP5 dans l’autophagie des cardiomyocytes." Mémoire, Université de Sherbrooke, 2016. http://hdl.handle.net/11143/8908.

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Résumé: L’autophagie est un processus essentiel au maintien de l’homéostasie cellulaire. Elle permet de dégrader et recycler aussi bien des organelles entières que des composants cytoplasmiques non fonctionnels. De plus, l’augmentation d’autophagie en condition de stress constitue une réponse adaptative favorisant la survie cellulaire. Chez les cardiomyocytes, l’autophagie en condition basale est indispensable au renouvellement, entre autres, des mitochondries et des protéines formant les sarcomères. De plus, les stress tels l’ischémie cardiaque ou la carence en nutriments induisent une augmentation de l’autophagie protectrice. Dans certaines conditions extrêmes, il a été suggéré qu’un surcroît d’autophagie puisse toutefois exacerber la pathologie cardiaque en provoquant la mort des cardiomyocytes. Considérant l’importance de ce processus dans la physiopathologie cardiaque, l’identification des mécanismes signalétiques régulant l’autophagie chez les cardiomyocytes a été le sujet de recherches intenses. À cet effet, l’activation des Mitogen-Activated Protein Kinase (MAPK) a été démontrée pour réguler, avec d’autres voies signalétiques, l’autophagie et l’apoptose des cardiomyocytes. Il est donc probable que les Dual-Specificity Phosphatase (DUSP), enzymes clés contrôlant l’activité des MAPK, participent aussi à la régulation de l’autophagie. Afin de vérifier cette hypothèse, nous avons induit l’autophagie chez des cardiomyocytes isolés de rats nouveau-nés en culture. L’analyse de marqueurs d’autophagie par immunobuvardage démontre que l’activation des MAPK ERK1/2 et p38 corrèle avec l’activité autophagique chez les cardiomyocytes. Dans ces conditions, la diminution d’expression de la majorité des ARNm encodant les différentes DUSP retrouvées chez les cardiomyocytes contraste de façon marquée avec l’augmentation d’expression de l’ARNm Dusp5. De plus, nous avons démontré par une étude de gain de fonction que l’activation soutenue de p38 par surexpression d’un mutant MKK6 constitutivement actif stimule l’autophagie chez les cardiomyocytes. De façon surprenante, la perte de fonction de p38 obtenue par surexpression d’un mutant p38 dominant négatif n’altère en rien la réponse autophagique initiatrice dans notre modèle in vitro. Nos résultats suggèrent que les DUSP puissent réguler, via leurs actions sur les MAPK, d’importantes étapes du processus autophagique chez les cardiomyocytes.
Abstract: Autophagy is a process essential to the maintenance of cellular homeostasis. It helps degrade and recycle whole organelles and nonfunctional cytoplasmic components. In addition, the adaptative up regulation of autophagy in stress condition promotes cell survival. In cardiomyocytes basal autophagy is essential to the renewal of, among others, mitochondria and proteins forming sarcomeres. In addition, stresses such as ischemic heart or nutrient deficiency induce an increase in protective autophagy. In extreme conditions, it has been suggested that autophagy may exacerbate cardiac disease causing the death of cardiomyocytes. Considering the importance of this process in cardiac pathophysiology, identify ing safety mechanisms regulating autophagy in cardiomyocytes has been the subject of intense research. To this end, activation of mitogen-activated protein kinase (MAPK) has been demonstrated to regulate, with other signaling pathways, autophagy and cardiomyocyte apoptosis. It is therefore likely that Dual-Specificity Phosphatases (DUSPs), key enzymes that control the activity of MAPKs, also participate in the regulation of autophagy. To test this hypothesis, we have induced autophagy in isolated cardiomyocytes of newborn rats in culture. Analysis of autophagy markers by immunoblotting demonstrated that the activation of MAPKs ERK1/2 and p38 correlates with autophagic activity in cardiomyocytes. Under these conditions, the decrease in expression of the majority of mRNAs encoding different DUSPs found in cardiomyocytes contrast sharply with the increase mRNA expression of Dusp5. Furthermore, we demonstrated by again of function study that sustained activation of p38 by overexpression of a constitutively active MKK6 mutant stimulates autophagy in cardiomyocytes. Surprisingly, the loss of p38 function obtained by overexpression of a dominant negative p38 mutant does not affect the autophagic response in our in vitro model, but increases the lipidation of autophagosomes marker LC3. Our results suggest that DUSPs can regulate, through their actions on MAPKs, important stages of autophagy in cardiomyocytes.
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Tong, Tin-wing, and 唐天穎. "Investigation of transcript expression of PRKAR2A, DUSP1, STMN2 and MAPT genes in nasopharyngeal carcinoma, ovarian cancer and benignovarian tumor." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2011. http://hub.hku.hk/bib/B46632700.

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Derigs, Marcus [Verfasser], Roland [Akademischer Betreuer] Lang, Roland [Gutachter] Lang, and Jochen [Gutachter] Mattner. "Die Auswirkung von Dusp16 auf die Proliferation von Knochenmark-derivierten dendritischen Zellen / Marcus Derigs ; Gutachter: Roland Lang, Jochen Mattner ; Betreuer: Roland Lang." Erlangen : Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), 2020. http://d-nb.info/1215343221/34.

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Moreaux, Guenievre. "Investigating downstream effectors of KRas signalling in vivo : Dusp6 and Fra1." Thesis, University of Glasgow, 2012. http://theses.gla.ac.uk/4056/.

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Book chapters on the topic "DUSP12"

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Lukas, Thomas J., Daniela V. Rosa, Luiz Alexandre V. Magno, Bruno R. Souza, Marco A. Romano-Silva, Hisao Masai, Kazuhisa Kohda, et al. "DUSP24." In Encyclopedia of Signaling Molecules, 538. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100372.

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Monteiro, Lucas Falcão, Pault Yeison Minaya Ferruzo, Lilian Cristina Russo, Jessica Oliveira Farias, and Fábio Luís Forti. "DUSP3/VHR: A Druggable Dual Phosphatase for Human Diseases." In Reviews of Physiology, Biochemistry and Pharmacology, 1–35. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/112_2018_12.

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"DUSP1." In Encyclopedia of Pain, 1082. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-28753-4_100662.

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"DUSP24." In Encyclopedia of Signaling Molecules, 1447. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101058.

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"DUSP6." In Encyclopedia of Pain, 1082. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-28753-4_100663.

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"Dual-specificity Phosphatases (DUSP)." In Encyclopedia of Pain, 1081. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-28753-4_100657.

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Upadhyay, HC, MA Lawson, and B. Gangapurkar. "Regulation of DUSP1 Translation by GnRH in the LβT2 Pituitary Gonadotrope Cell Line." In The Endocrine Society's 92nd Annual Meeting, June 19–22, 2010 - San Diego, P3–224—P3–224. Endocrine Society, 2010. http://dx.doi.org/10.1210/endo-meetings.2010.part3.p5.p3-224.

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Furukawa, Toru, and Akira Horii. "The Role of DUSP6/MKP-3 in Pancreatic Carcinoma." In Handbook of Immunohistochemistry and in situ Hybridization of Human Carcinomas, Volume 3 - Molecular Genetics, Liver Carcinoma, and Pancreatic Carcinoma, 335–39. Elsevier, 2005. http://dx.doi.org/10.1016/s1874-5784(05)80038-8.

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Chen, Chien-Cheng, and Carole R. Mendelson. "Sp1 Response Elements within the MAPK Phosphatase-1 (MKP-1/DUSP1) Promoter Mediate Progesterone Receptor (PR) Induced MKP-1 Expression in Breast Cancer Cells." In Posters I, P3–13—P3–13. Endocrine Society, 2010. http://dx.doi.org/10.1210/endo-meetings.2010.part3.p1.p3-13.

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"Table II: Material composition of dust and feedstuff from pig and hen houses. Results from 1)= AENGST (33), 2) = HARTUNG (34), 3)= KOON et al. (21), 4)= HAR-TUNG (32). n.r. = not reported. pig hoi js e (no 1 bedding] hen hou se(b components dust” dust2) feed1) dust3> dust4) •/. •/. •/. •/. dry matter 87 87 88 92 89 92 crude protein 24 24 19 60 50 17 fa t4549 10 15 crude fibre 3554 nr. 2 ash 15 nr 5nr nr. 4 Table III: Number of particles collected by the Andersen Sampler and weight of settled dust in an experi­ mental piggery at different conditions from HONEY and McQUITTY (17) number of particles / 0.028 n3 treatment particle size settled dust 7 -16 jjm <5jjm g/rrfd ay rel humidity (low ) 51 370 119920 13.42 rel humidity (high) 32450 85230 10.03 pen volume 22.1 nf 38200 86420 12.38 pen volume 11.1m3 45630 118 730 11.08 floor feeding 42 770 883 90 15.85 self feeding 41050 116760 7.62 a irflo w 595rr?/h 38650 93820 12.08 a irflo w 297rr?/h 45170 111 330 11.37 average 41900 102580 11.37 ^ TJa." In Odour Prevention and Control of Organic Sludge and Livestock Farming, 343. CRC Press, 1986. http://dx.doi.org/10.1201/9781482286311-137.

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Conference papers on the topic "DUSP12"

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Andrade, Pamela V., Mariana T. Ruckert, Carlos Alberto O. Biagi Junior, and Vanessa S. Silveira. "Abstract C51: Targeted inhibition of DUSP1 and DUSP6 suppresses pancreatic adenocarcinoma cells’ growth and glucose metabolism via SAPK/JNK pathway activation." In Abstracts: AACR Special Conference on Pancreatic Cancer: Advances in Science and Clinical Care; September 6-9, 2019; Boston, MA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.panca19-c51.

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Tsai, Shaw-Jenq, Chu-An Wang, and I.-Heng Chang. "Abstract 1786: Effect of DUSP2 on pancreatic cancer lymphatic dissemination." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1786.

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Tsai, Shaw-Jenq, Chu-An Wang, and I.-Heng Chang. "Abstract 1786: Effect of DUSP2 on pancreatic cancer lymphatic dissemination." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-1786.

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Khadir, Abdelkrim, Ali Tiss, Jehad Abubaker, Mohamed Abu-farha, Irina Al Khairi, Preethi Cherian, Sina Kavalakatt, et al. "Map Kinase Phosphatase Dusp1 Is Overexpressed In Human Obese And Modulated By Physical Exercise." In Qatar Foundation Annual Research Conference Proceedings. Hamad bin Khalifa University Press (HBKU Press), 2014. http://dx.doi.org/10.5339/qfarc.2014.hbpp0059.

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Wang, CA, IH Chang, CF Li, PC Hou, and SJ Tsai. "PO-177 The novel function of DUSP2/VEGF-C axis in pancreatic cancer progression." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.216.

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Liu, Fang, and Murray Korc. "Abstract 2951: DUSP1 is a novel target for enhancing pancreatic cancer cell sensitivity to gemcitabine." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2951.

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Shah, Suharsh, Mahmoud Mostafa, Mohammed Altonsy, and Robert Newton. "Maintenance of IRF1 by MAPK inhibition: A mechanism by which DUSP1 reduces glucocorticoid inhibition of CXCL10." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa5068.

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Karakashev, Sergey. "Abstract 1824: Hypoxia induces lapatinib resistance in ErbB2-positive breast cancer cells via regulation of DUSP2." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-1824.

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Karakashev, Sergey V., and Reginato J. Mauricio. "Abstract PR15: Hypoxia induces lapatinib resistance in ErbB2-positive breast cancer cells via regulation of DUSP2." In Abstracts: Third AACR International Conference on Frontiers in Basic Cancer Research - September 18-22, 2013; National Harbor, MD. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.fbcr13-pr15.

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Ma, Irene T., Yihui Fan, Roma H. Patel, Jin Cheng, Eugene S. Kim, Jason M. Shohet, Jianhua Yang, and Sanjeev A. Vasudevan. "Abstract LB-352: DUSP26 inhibition: a new therapeutic pathway in neuroblastoma." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-lb-352.

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