ArticleFrontiers in immunology2017
Dual-Specificity Phosphatase 12 Targets p38 MAP Kinase to Regulate Macrophage Response to Intracellular Bacterial Infection.
Article in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- rs1051838 Promotes Intracellular Survival ofMicroorganisms · 2026Article
- Dual-specific phosphatases-8: a new target for clinical disease intervention.Journal of translational medicine · 2025Review
- From GWAS signal to function: targeted CRISPR activation enables functional characterization of non-coding SNPs in chickens.Frontiers in genome editing · 2025Article
- Genome-wide characterization and comparative expression profiling ofFrontiers in immunology · 2024Article
- Dual-Specificity Phosphatases in Regulation of Tumor-Associated Macrophage Activity.International journal of molecular sciences · 2023Review
- FOXP1‑induced DUSP12 alleviates vascular endothelial cell inflammation and oxidative stress injury induced by ox‑LDL via MAP3K5 signaling pathway.Experimental and therapeutic medicine · 2023Article
- Meta-transcriptomic comparison of two sponge holobionts feeding on coral- and macroalgal-dissolved organic matter.BMC genomics · 2022Article
- Expansion of Intestinal Secretory Cell Population Induced byFrontiers in cellular and infection microbiology · 2022Article
- Estradiol AggravateFrontiers in immunology · 2022Article
- Zinc-binding domain mediates pleiotropic functions of Yvh1 in Cryptococcus neoformans.Journal of microbiology (Seoul, Korea) · 2021Article
- Expression of DUSP12 Reduces Lung Vascular Endothelial Cell Damage in a Murine Model of Lipopolysaccharide-Induced Acute Lung Injury via the Apoptosis Signal-Regulating Kinase 1 (ASK1)-Jun N-Terminal Kinase Activation (JNK) Pathway.Medical science monitor : international medical journal of experimental and clinical research · 2021Article
- Article
- Comparative Analysis of Multiple Neurodegenerative Diseases Based on Advanced Epigenetic Aging Brain.Frontiers in genetics · 2021Article
- Investigation of the Genome-Wide Genetic and Epigenetic Networks for Drug Discovery Based on Systems Biology Approaches in Colorectal Cancer.Frontiers in genetics · 2020Article
- Functions of p38 MAP Kinases in the Central Nervous System.Frontiers in molecular neuroscience · 2020Review
- An overview of mammalian p38 mitogen-activated protein kinases, central regulators of cell stress and receptor signaling.F1000Research · 2020Review
- Phosphorylation Dynamics of JNK Signaling: Effects of Dual-Specificity Phosphatases (DUSPs) on the JNK Pathway.International journal of molecular sciences · 2019Review
- Dual Specificity Phosphatase 12 Regulates Hepatic Lipid Metabolism Through Inhibition of the Lipogenesis and Apoptosis Signal-Regulating Kinase 1 Pathways.Hepatology (Baltimore, Md.) · 2019Article
- Dual-Specificity Phosphatases in Immunity and Infection: An Update.International journal of molecular sciences · 2019Review
- Dual-Specificity Phosphatases in Neuroblastoma Cell Growth and Differentiation.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitogen-activated protein kinase (MAPK) cascades are activated in innate immune cells such as macrophages upon the detection of microbial infection, critically regulating the expression of proinflammatory cytokines and chemokines such as TNF-α, IL-6, and MCP-1. As a result, activation of MAPKs is tightly regulated to ensure appropriate and adequate immune responses. Dual-specificity phosphatases (DUSPs) are a family of proteins which specifically dephosphorylates threonine and tyrosine residues essential for MAPK activation to negatively regulate their activation. DUSP12 is a member of atypical DUSPs that lack MAPK-binding domain. Its substrate and function in immune cells are unknown. In this study, we demonstrated that DUSP12 is able to interact with all the three groups of MAPKs, including extracellular signal-regulated protein kinase, JNK, and p38. To investigate the function of DUSP12 in macrophages in response to TLR activation and microbial infection, we established RAW264.7 cell lines stably overexpressing DUSP12 and found that overexpression of DUSP12 inhibited proinflammatory cytokine and chemokine production in response to TLR4 activation, heat-inactivated
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.