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a p38 MAPKAPK2 kinase cascade modulates the activity of F-actin at the yolk cell margin circumference allowing the gradual closure of the blastopore as epiboly progresses
Phosphorylation of inhibitory PAS domain protein (IPAS (show HIF3A Proteins)) at Ser184 by MAPK-activated protein kinase 2 (MK2 or MAPKAPK2) enhances the proapoptotic function of IPAS (show HIF3A Proteins).
MK2 (show KCNA2 Proteins)-mediated RIPK1 (show RIPK1 Proteins) phosphorylation is an important molecular mechanism limiting the sensitivity of the cells to the cytotoxic effects of TNF (show TNF Proteins).
p38MAPK (show MAPK14 Proteins)/MK2 (show KCNA2 Proteins) phosphorylation of RIPK1 (show RIPK1 Proteins) is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.
MK2 (show KCNA2 Proteins)-mediated phosphorylation of RIPK1 (show RIPK1 Proteins) serves as a checkpoint within the TNF (show TNF Proteins) signaling pathway that integrates cell survival and cytokine production.
this study shows that the loss of MK2 (show KCNA2 Proteins) in mast cells decreases the IL-33 (show IL33 Proteins)-induced leukocyte recruitment and the resulting skin inflammation
MK2 (show KCNA2 Proteins) signaling differentially regulated CCL3 (show CCL3 Proteins) and CCL4 (show CCL4 Proteins).
In silico analyses and experimental validation demonstrated that the kinase activity of p38(MAPK (show MAPK14 Proteins)) determines signal amplitude, whereas phosphatase activity affects both signal amplitude and duration. p38(MAPK (show MAPK14 Proteins)) and MK2 (show KCNA2 Proteins) concentrations and responsiveness toward IL-1beta (show IL1B Proteins) were quantitatively compared between hepatocytes and macrophages
MK2 (show KCNA2 Proteins)-activating peptide (MK2 (show KCNA2 Proteins)-AP) blocks the effects of anthrax lethal toxin on endothelial barriers in cultured cells and reduces pulmonary vascular leak in rats.
MK2 (show KCNA2 Proteins) regulates postnatal arteriogenesis by controlling vascular recruitment of monocytes/macrophages in dual manner: regulation of endothelial MCP-1 (show CPT1B Proteins) expression in response to hemodynamic and inflammatory forces as well as MCP-1 (show CPT1B Proteins) dependent monocyte migration
these data suggest there is a sexual dimorphism in MK2 (show KCNA2 Proteins) signaling of osteoclast progenitor cell subpopulations.
According to the information mentioned above, we now report the design and synthesis of some series of new urea derivatives that were then evaluated for their inhibitory activities against MAPKAPK2, TNF-a (show TNF Proteins), and p38a (show MAPK14 Proteins)
MK2 (show KCNA2 Proteins) post-transcriptionally regulates TNF-alpha (show TNF Proteins)-induced ICAM-1 (show ICAM1 Proteins) expression by altering the cytoplasmic localization of HuR (show ELAVL1 Proteins) in human lung microvascular endothelial cells.
MK2 (show KCNA2 Proteins) overexpression is associated with primary liver tumors.
CEP131 is the key regulatory target of MK2 (show KCNA2 Proteins) and 14-3-3 (show YWHAQ Proteins) in centriolar satellite remodeling.
mTOR (show FRAP1 Proteins) controls the senescence-associated secretory phenotype by differentially regulating the translation of the MK2 (show KCNA2 Proteins) (also known as MAPKAPK2).
analysis of signaling cooperation between p38-MAPK (show MAPK14 Proteins)/MAPKAP-2/Hsp27 (show HSPB1 Proteins) and intracellular calcium release in AA-induced HBEC apoptosis
findings reveal MK2 (show KCNA2 Proteins)/MK3 (show KCNA3 Proteins) as crucial stress-responsive kinases that promote autophagy through Beclin 1 (show BECN1 Proteins) S90 phosphorylation
The protein expression of both HMGB1 (show HMGB1 Proteins) and MAPKAPK2 were increased in KLM1-R cells.
Data indicate the binding mode and molecular mechanism of action of MAPK-activated protein kinase-2 (MK2) and inhibitors.
Treatment with MK2 (show KCNA2 Proteins) or p38 (show CRK Proteins) inhibitors blocked human papillomavirus genome amplification, identifying the p38 (show CRK Proteins)/MK2 (show KCNA2 Proteins) pathway as a key regulator of the human papillomavirus life cycle.
This gene encodes a member of the Ser/Thr protein kinase family. This kinase is regulated through direct phosphorylation by p38 MAP kinase. In conjunction with p38 MAP kinase, this kinase is known to be involved in many cellular processes including stress and inflammatory responses, nuclear export, gene expression regulation and cell proliferation. Heat shock protein HSP27 was shown to be one of the substrates of this kinase in vivo. Two transcript variants encoding two different isoforms have been found for this gene.
MAP kinase-activated protein kinase 2
, betty boop
, mitogen-activated protein kinase-activated protein kinase 2
, MAPK-activated protein kinase 2
, MAPKAP kinase 2
, map kinase activated protein kinase-2