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Human MAPK9 Protein expressed in Wheat germ - ABIN1310315
Prause, Christensen, Billestrup, Mandrup-Poulsen: JNK1 protects against glucolipotoxicity-mediated beta-cell apoptosis. dans PLoS ONE 2014
Taken together, the silencing of H4R (Montrer HRH4 Protéines) inhibited the H4R (Montrer HRH4 Protéines) mediated Mast cell functions and SAPK/JNK (Montrer MAPK8 Protéines) phosphorylation. Furthermore, the H4R (Montrer HRH4 Protéines) activation utilized SAPK/JNK (Montrer MAPK8 Protéines) signaling pathway for IL-1beta (Montrer IL1B Protéines) release in HMC-1 cells.
RhoGDIbeta overexpression led to downregulation of miR (Montrer MLXIP Protéines)-200c, whereas miR (Montrer MLXIP Protéines)-200c was able directly to target 3'-UTR of jnk2mRNA and attenuated JNK2 protein translation, which resulted in attenuation of Sp1mRNA and protein expression in turn, inhibiting Sp1 (Montrer PSG1 Protéines)-dependent MMP-2 (Montrer MMP2 Protéines) transcription.
The MAP kinase (Montrer MAPK1 Protéines) JNK2 mediates cigarette smoke-induced tissue factor (Montrer F3 Protéines) activation, arterial thrombosis and reactive oxygen species production.
We found p-JNK2 up-regulation in AUC and its early down-regulation in UC-CRC (Montrer CALR Protéines) and CRC (Montrer CALR Protéines) carcinogenesis.
JNK2 was a novel direct target of miR (Montrer MLXIP Protéines)-20a-5p.
The release of infectious respiratory syncytial virus (RSV) virions from infected cells was significantly reduced by JNK1 (Montrer MAPK8 Protéines)/2 siRNA knockdown, implicating JNK1 (Montrer MAPK8 Protéines)/2 as a key host factor for RSV virus production.
PXR (Montrer NR1I2 Protéines) regulates the intestinal epithelial barrier during inflammation by modulating cytokine-induced MLCK (Montrer MYLK Protéines) expression and JNK1 (Montrer MAPK8 Protéines)/2 activation
Phloretin is able to inhibit NSCLC A549 cell growth by inducing apoptosis through P38 MAPK (Montrer MAPK14 Protéines) and JNK1 (Montrer MAPK8 Protéines)/2 pathways, and therefore may prove to be an adjuvant to the treatment of non-small cell lung cancer
In hepatocytes, JNK1 (Montrer MAPK8 Protéines) and JNK2 appear to have combined effects in protecting from drug-induced liver injury.
Inhibition of JNK1 (Montrer MAPK8 Protéines)/2 activity suppressed Hedgehog (Montrer SHH Protéines) pathway activity in acquired chemoresistant cancer cells.
these results identify a protective role of epithelial JNK2 signaling to maintain mucosal barrier function, epithelial cell integrity, and mucus layer production in the event of inflammatory tissue damage
activation of JNK (Montrer MAPK8 Protéines) in the endoplasmic reticulum stress response precedes activation of XBP1 (Montrer XBP1 Protéines).
JNK-2 regulates aggrecan (Montrer ACAN Protéines) degradation in cultured murine cartilage and surgically induced osteoarthritis in vivo following mechanical destabilization of the knee joint.
activation of astrocyte MMP2 (Montrer MMP2 Protéines)/JNK1 (Montrer MAPK8 Protéines)/2 contributes to the pathogenesis of pain hypersensitivity in the complex regional pain syndrome model
JNK1 (Montrer MAPK8 Protéines)/2-dependent regulation of p66ShcS36 phosphorylation, is reported.
This study demonstrated that the disruption of JNK2 appears to have a greater impact on tolerance than the other isoforms in the tail-flick but not the hot-plate test.
although JNK (Montrer MAPK8 Protéines) activation and RIP3 expression are induced by FS, neither contributes to the liver injury.
morphine activated JNK2 through an arrestin-independent Src- and PKC-dependent mechanism, whereas fentanyl activated JNK2 through a Src-GRK3/arrestin-2-dependent and PKC-independent mechanism.
this study indicates that JNK2 is a physiological kinase responsible for eNOS (Montrer NOS3 Protéines)-Ser (Montrer SIGLEC1 Protéines)(116) phosphorylation and regulates NO production.
Data show that proinflammatory cytokines induction was ERK1/2 and JNK1 (Montrer MAPK8 Protéines)/2 dependent.
These data suggest that the p38 (Montrer MAPK14 Protéines) and JNK (Montrer MAPK8 Protéines) signaling pathways play pivotal roles in PRRSV replication and may regulate immune responses during virus infection.
MPK9 and MPK12 (Montrer MAPK12 Protéines) are positive regulators of salicylic acid signaling in Arabidopsis guard cells.
MPK9 and MPK12 (Montrer MAPK12 Protéines) are key regulators mediating both abscisic acid (ABA) and Methyl jasmonate (MeJA) signalling in guard cells.
Data suggest that MPK9 is autoactivated via phosphorylation independent of any upstream MAPK (Montrer MAPK1 Protéines) kinase signaling; autophosphorylation occurs at both threonine and tyrosine residues in Thr (Montrer TRH Protéines)-Asp (Montrer ASIP Protéines)-Tyr (Montrer TYR Protéines) motif and in C-terminal regulatory extension.
MPK9 and MPK12 (Montrer MAPK12 Protéines) function redundantly downstream of extracellular reactive oxygen production and intracellular accumulation, cytosolic alkalisation and Ca(2 (Montrer CA2 Protéines)+)cytosolic oscillation in yeast elcictor-induced stomatal closure
MPK9 and MPK12 (Montrer MAPK12 Protéines) act downstream of ROS (Montrer ROS1 Protéines) and cytosolic Ca2 (Montrer CA2 Protéines)+ and upstream of anion channels in the guard cell abscisic acid signaling cascade.
MAP kinases MPK9 and MPK12 (Montrer MAPK12 Protéines) are preferentially expressed in guard cells and positively regulate ROS (Montrer ROS1 Protéines)-mediated ABA signaling.
The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Several alternatively spliced transcript variants encoding distinct isoforms have been reported.
mitogen-activated protein kinase 9
, Jun kinase
, MAP kinase 9
, MAPK 9
, c-Jun N-terminal kinase 2
, c-Jun kinase 2
, stress-activated protein kinase 1a
, stress-activated protein kinase JNK2
, JNK/SAPK alpha
, mitogen activated protein kinase 9
, protein kinase, mitogen-activated 9
, stress activated protein kinase alpha II
, janus kinase 2
, c-JUN amino-terminal kinase-2 alpha1