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Porcine reproductive and respiratory syndrome virus -activated TAK-1 (show NR2C2 Proteins) was essential for the activation of JNK (show MAPK8 Proteins) and NF-kappaB (show NFKB1 Proteins) pathways and IL-8 (show IL8 Proteins) expression.
Data indicate that transmissible gastroenteritis virus (TGEV) infection activates the janus kinase signal transducer and activator of the transcription 1 (JAK (show JAK3 Proteins)-STAT1 (show STAT1 Proteins)) signaling pathway.
Data show that proinflammatory cytokines induction was ERK1/2 and JNK1 (show MAPK8 Proteins)/2 dependent.
These data suggest that the p38 (show MAPK14 Proteins) and JNK (show MAPK8 Proteins) signaling pathways play pivotal roles in PRRSV replication and may regulate immune responses during virus infection.
based on the data, we can conclude that JNK (show MAPK8 Proteins) plays an active role in fragmentation of pig oocytes and that p38 MAPK (show MAPK14 Proteins) is not involved in this process
Retinal ischemia-reperfusion alters expression of mitogen-activated protein kinases, particularly ERK1/2, in the neuroretina and retinal arteries.
PP2A (show PPP2R2B Proteins) and AIP1 (show PDCD6IP Proteins) cooperatively induce activation of ASK1 (show MAP3K5 Proteins)-JNK (show MAPK8 Proteins) signaling and vascular endothelial cell apoptosis.
Phorbol 12-myristate 13-acetate activation of ERK (show MAPK1 Proteins) and JNK (show MAPK8 Proteins) signaling is relevant in the regulation of gene expression during follicular development, ovulation, and luteinization.
This is the first report of the genetic polymorphisms of the JAK1 and STAT3 (show STAT3 Proteins) genes and their associations with the incidence of non-specific digestive disorder in rabbits.
This study demonstrates that the nuclear import of JAK1 is essential for the optimal fitness of ABC (show ABCB6 Proteins) DLBCL cells.
JAK1 rs11576173 and rs1497056 genotypes were significantly related to severe necroinflammatory activity (NIA) grade of chronic hepatitis C patients.
Multiple myeloma cells over express JAK1/2 and suggest combined chemotherapy with ruxolitinib, bortezomib and lenalidomide to inhibit JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) pathway.
Mechanistic investigations reveal that AJUBA (show AJUBA Proteins) specifically binds the FERM domain of JAK1 to dissociate JAK1 from the IFNgamma recepter, resulting in an inhibition of STAT1 (show STAT1 Proteins) phosporylation and concomitantly its nuclear translocation. Clinically, the level of AJUBA (show AJUBA Proteins) in CRC (show CALR Proteins) specimens is negatively correlated with the levels of IFIT2 (show IFIT2 Proteins) and pSTAT1
Multilevel genomic analyses of microsatellite instability+ colorectal cancer revealed molecular heterogeneity with clinical relevance, including tumor immunogenicity and a favorable patient outcome associated with JAK1 mutations and the transcriptomic subgroup CMS1
a causal relationship between MLH1 (show MLH1 Proteins)-deficiency and incidence of oncogenic point mutations in tyrosine kinases driving cell transformation and acquired resistance to kinase-targeted cancer therapies, is reported.
Data show that moringin (GMG-ITC) had a limited inhibitory effect on IFNalpha-induced STAT1 (show STAT1 Proteins) and STAT2 (show STAT2 Proteins) activity, indicating differentially targeting JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) signaling pathways.
our studies highlight Jak1 as the first identified substrate for USP6, and they offer a mechanistic rationale for the clinical investigation of Jak and STAT3 inhibitors as therapeutics for the treatment of bone and soft tissue tumors along with other neoplasms driven by USP6 overexpression
In this structure, the receptor peptide forms an 85-A-long extended chain, in which both the previously identified box1 and box2 regions bind simultaneously to the FERM and SH2-like domains of JAK1.
Results reveal the structure of box1 from class II cytokine receptors IFNLR1 (show IL28RA Proteins) and IL10RA (show IL10RA Proteins) bound to the FERM-SH2 domain of human JAK1, identifying a consensus motif for JAK1 interaction.
JAK1-mediated signaling cascades in skin regulate the expression of proteases associated with the maintenance of skin barrier function and demonstrate that perturbation of these pathways can lead to the development of spontaneous pruritic dermatitis.
Small-scale in vivo screening identified several genes, including Cd109 (show CD109 Proteins), that encode novel pro-metastatic factors. We uncovered signaling mediated by Janus kinases (Jaks) and the transcription factor Stat3 (show STAT3 Proteins) as a critical, pharmacologically targetable effector of CD109 (show CD109 Proteins)-driven lung cancer metastasis
High JAK1 expression is associated with Hepatic Fibrosis.
findings demonstrate that clinically relevant doses of the JAK1/2 inhibitor ruxolitinib suppresses the harmful consequences of macrophage overactivation characterizing Hemophagocytic lymphohistiocytosis in 2 murine models.
Data show that CUZD1 (show CUZD1 Proteins) interacts with a complex containing JAK1/JAK2 (show JAK2 Proteins) and STAT5 (show STAT5A Proteins), downstream transducers of prolactin (show PRL Proteins) signaling in the mammary gland.
JAK1 conditional knockout mice will be an invaluable tool to study cytokine signaling during normal development and disease progression in adult animals.
JAK1, JAK2 (show JAK2 Proteins), and JAK3 (show JAK3 Proteins) are involved in stimulation of functional activity of mesenchymal progenitor cells by fibroblast growth factor.
JAK (show JAK3 Proteins) mediated signaling is involved in the differentiation and proliferation of mesenchymal progenitor cells.
Data indicate thar Janus kinase 1 (Jak1) degradation is dependent on Nedd4 family interacting proteins Ndfip1 (show NDFIP1 Proteins)/Ndfip2 (show NDFIP2 Proteins).
JAK1 activating mutants are insufficient to drive hepatocellular carcinoma development in vivo.
Janus kinase 1 (JAK1), is a member of a new class of protein-tyrosine kinases (PTK) characterized by the presence of a second phosphotransferase-related domain immediately N-terminal to the PTK domain. The second phosphotransferase domain bears all the hallmarks of a protein kinase, although its structure differs significantly from that of the PTK and threonine/serine kinase family members. JAK1 is a large, widely expressed membrane-associated phosphoprotein. JAK1 is involved in the interferon-alpha/beta and -gamma signal transduction pathways. The reciprocal interdependence between JAK1 and TYK2 activities in the interferon-alpha pathway, and between JAK1 and JAK2 in the interferon-gamma pathway, may reflect a requirement for these kinases in the correct assembly of interferon receptor complexes. These kinases couple cytokine ligand binding to tyrosine phosphorylation of various known signaling proteins and of a unique family of transcription factors termed the signal transducers and activators of transcription, or STATs.
Janus kinase 1 (a protein tyrosine kinase)
, protein tyrosine kinase
, tyrosine kinase JAK1
, tyrosine-protein kinase JAK1
, janus kinase 1
, Janus kinase 1
, Tyrosine-protein kinase Jak1
, tyrosine-protein kinase JAK1-like
, Janus protein tyrosine kinase 1
, jak1 kinase