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Human JNK Protein expressed in Baculovirus infected Insect Cells - ABIN593493
Sury, McShane, Hernandez-Miranda, Birchmeier, Selbach et al.: Quantitative proteomics reveals dynamic interaction of c-Jun N-terminal kinase (JNK) with RNA transport granule proteins splicing factor proline- and glutamine-rich (Sfpq) and non-POU ... dans Molecular & cellular proteomics : MCP 2015
Human JNK Protein expressed in Wheat germ - ABIN1310303
Prause, Christensen, Billestrup, Mandrup-Poulsen: JNK1 protects against glucolipotoxicity-mediated beta-cell apoptosis. dans PLoS ONE 2014
Data show that JNK signalling inhibits the growth of losers, while JAK (Montrer JAK3 Protéines)/STAT (Montrer STAT1 Protéines) signalling promotes competition-induced winner cell proliferation.
Here we uncover a cell non-autonomous requirement for the Epidermal growth factor receptor (Egfr (Montrer EGFR Protéines)) pathway in the lateral epidermis for sustained dpp (Montrer TGFb Protéines) expression in the LE. Specifically, we demonstrate that Egfr (Montrer EGFR Protéines) pathway activity in the lateral epidermis prevents expression of the gene scarface (scaf), encoding a secreted antagonist of JNK signaling
n addition to significantly increasing the number of JNK target genes identified so far, our results reveal that the LE is a highly heterogeneous morphogenetic organizer, sculpted through crosstalk between JNK, segmental and AP signalling. This fine-tuning regulatory mechanism is essential to coordinate morphogenesis and dynamics of tissue sealing
malignant transformation of the ras(V12)scrib(1) tumors requires bZIP protein Fos, the ETS (Montrer ETS1 Protéines)-domain factor Ets21c and the nuclear receptor Ftz-F1 (Montrer NR5A2 Protéines), all acting downstream of Jun-N-terminal kinase.
Diminished MTORC1-dependent JNK activation underlies the neurodevelopmental defects associated with lysosomal dysfunction.
ROS (Montrer ROS1 Protéines)/JNK/p38 (Montrer MAPK14 Protéines)/Upd (Montrer UROD Protéines) stress responsive module restores tissue homeostasis. This module is not only activated after cell death induction but also after physical damage and reveals one of the earliest responses for imaginal disc regeneration.
Significantly, the JNK pathway is responsible for the majority of the phenotypes and transcriptional changes downstream of Notch (Montrer NOTCH1 Protéines)-Src (Montrer SRC Protéines) synergy.
This study demonstrated that the mechanism by which Bsk (Montrer FRK Protéines) is required for pruning is through reducing the membrane levels of the adhesion molecule (Montrer NCAM1 Protéines) Fasciclin II (Montrer NCAM2 Protéines) (FasII)
Study solves the crystal structure of unphosphorylated DJNK in complex with adenylyl imidodiphosphate (AMP (Montrer AMPH Protéines)-PNP (Montrer NP Protéines)) and magnesium.
PERK/ATF4 activated the JNK pathway through Rac1 and Slpr activation in apoptotic cells.
PRDM5 (Montrer PRDM5 Protéines) promotes the proliferation and invasion of murine melanoma cells through up-regulating JNK expression and strategies targeting PRDM5 (Montrer PRDM5 Protéines) may be promising for the therapy of melanoma.
This study showed that the induction level of IL-32 (Montrer IL32 Protéines) was increased in chronic rhinosinusitis with nasal polyps compared to normal nasal mucosa and that LPS (Montrer IRF6 Protéines)-induced IL-32 (Montrer IL32 Protéines) expression in nasal polyp-derived fibroblasts was regulated via the TLR4 (Montrer TLR4 Protéines)/JNK/AKT (Montrer AKT1 Protéines)/CREB (Montrer CREB1 Protéines) signaling pathway.
These results suggest that Bacteroides fragilis enterotoxin induced accumulation of autophagosomes in endothelial cells, but activation of a signaling pathway involving JNK, AP-1 (Montrer FOSB Protéines), and CHOP (Montrer DDIT3 Protéines) may interfere with complete autophagy.
The findings indicate that ERK (Montrer EPHB2 Protéines) and JNK signaling pathways, as well as NF-kappaB (Montrer NFKB1 Protéines)-mediated signaling are important contributors to the pathogenesis of Kashin-Beck disease.
The data suggested that JNK-enhanced Tudor-SN phosphorylation promotes the interaction between Tudor-SN and G3BP (Montrer G3BP1 Protéines) and facilitates the efficient recruitment of Tudor-SN into stress granules under conditions of sodium arsenite-induced oxidative stress.
Taken together, our data demonstrate that JNK regulates triple-negative breast cancer (TNBC)tumorigenesis by promoting CSC phenotype through Notch1 (Montrer NOTCH1 Protéines) signaling via activation of c-Jun (Montrer JUN Protéines) and indicate that JNK/c-Jun/Notch1 (Montrer NOTCH1 Protéines) signaling is a potential therapeutic target for TNBC
Here, the authors show that the CDK (Montrer CDK4 Protéines) inhibitor p21 (CDKN1A (Montrer CDKN1A Protéines)) maintains the viability of DNA damage-induced senescent cells. Upon p21 (Montrer CDKN1A Protéines) knockdown, senescent cells acquired multiple DNA lesions that activated ataxia telangiectasia mutated (ATM (Montrer ATM Protéines)) and nuclear factor (NF)-kappaB (Montrer NFKB1 Protéines) kinase, leading to decreased cell survival. NF-kappaB (Montrer NFKB1 Protéines) activation induced TNF-alpha (Montrer TNF Protéines) secretion and JNK activation to mediate death of senescent cells in a...
Results indicate that cordycepin promotes caveolin-1 (CAV1 (Montrer CAV1 Protéines))upregulation to enhance c-jun N-terminal kinase (JNK)/forkhead box O3A (Montrer FOXO3 Protéines) protein (Foxo3a (Montrer FOXO3 Protéines)) signaling pathway activation, inducing apoptosis in lung cancer cells.
The combination of 2-deoxyglucose (2-DG) and ABT-199 initiated cell death through the reduction of myeloid cell leukemia sequence 1 protein (Mcl-1 (Montrer MCL1 Protéines)) expression and c-Jun N-terminal kinase 1 (JNK1) activation and subsequent Bcl-xL (Montrer BCL2L1 Protéines) protein degradation.
identified the c-Jun N-terminal kinase 1 (JNK1) as the kinase involved in the phosphorylation of NEIL1 (Montrer NEIL1 Protéines)
The authors have found that JNK signaling is required for proper vascular morphogenesis and the normal formation of collateral arteries in muscle.
JNK1-mediated NLRP3 (Montrer NLRP3 Protéines) phosphorylation at S194 is a critical priming event and is essential for NLRP3 (Montrer NLRP3 Protéines) inflammasome activation.
The purpose of this study was to investigate mechanisms that govern the regulation of Npnt (Montrer NPNT Protéines) gene expression by IL-1beta (Montrer IL1B Protéines) in osteoblasts.
Doxorubicin (Dox)-administration to cardiomyocytes increased the levels of reactive oxygen species (ROS (Montrer ROS1 Protéines)) in a time-dependent manner that followed the activation of stress-induced proteins p53 (Montrer TP53 Protéines), p38 (Montrer CRK Protéines) and JNK MAPKs, culminating in an increase in autophagy and apoptosis markers.
IL-6 (Montrer IL6 Protéines) likely up-regulates IRP1 (Montrer ACO1 Protéines) and DMT1 (Montrer SLC11A2 Protéines) expression and down-regulates FPN1 (Montrer SLC40A1 Protéines) expression in BV2 microglial cells through JNK signaling pathways
Study examined whether JNK is present at the presynaptic site and its activity after presynaptic NMDA receptors stimulation; found that JNK, via the JBD domain, acts as a physiological effector on T-SNARE (Montrer VTI1B Protéines) proteins; data suggest that JNK-dependent phosphorylation of T-SNARE (Montrer VTI1B Protéines) proteins may have an important functional role in synaptic plasticity.
JNK signaling, which is inversely correlated with WNT4 (Montrer WNT4 Protéines), plays an important role in perinatal germline cyst breakdown and primordial follicle formation by regulating E-cadherin (Montrer CDH1 Protéines) junctions between oocytes in mouse ovaries.
It was concluded that compounds targeting JNK1 activity in brain and adipose tissue, which do not accumulate in the skin, may be safer and most effective.
JNK1 activation suppresses antifungal immunity in mice. JNK1-deficient mice had a significantly higher survival rate than wild-type control mice in response to Candida albicans infection, and the expression of JNK1 in hematopoietic innate immune cells was critical for this effect.
activation of JNK in the endoplasmic reticulum stress response precedes activation of XBP1 (Montrer XBP1 Protéines).
Hyperosmotic Shock Engages Two Positive Feedback Loops through Caspase-3 (Montrer CASP3 Protéines)-dependent Proteolysis of JNK1-2 and Bid (Montrer BID Protéines).
JNK signaling is required to establish microtubule stability and maintain tissue cohesion in the gut (Montrer GUSB Protéines).
Data show that the death pathway is independent of ERK (Montrer MAPK1 Protéines) but relies on activating Bad phosphorylation through the control of both kinases Cdk1 (Montrer CDK1 Protéines) and JNK.
study reports MPK8 connects protein phosphorylation, Ca(2 (Montrer CA2 Protéines))+ and ROS (Montrer ROS1 Protéines) in wound-signaling pathway; suggests 2 major activation modes, Ca(2 (Montrer CA2 Protéines))+/CaMs and MAP kinase (Montrer MAPK1 Protéines) phosphorylation cascade, converge at MPK8 to monitor or maintain an essential part of ROS (Montrer ROS1 Protéines) homeostasis
our data provide strong evidence that Jip3 in fact serves as an adapter protein linking these cargos to dynein
P38 (Montrer MAPK14 Protéines) and JNK have opposing effects on persistence of in vivo leukocyte migration in zebrafish.
A dorsalization pathway that is exerted by Axin (Montrer AXIN1 Protéines)/JNK signaling and its inhibitor Aida (Montrer AIDA Protéines) during vertebrate embryogenesis, is defined.
JNK-Mmp13 (Montrer MMP13 Protéines) signaling pathway plays an essential role in regulating the innate immune cell migration in response to severe injury in vivo
Our genetic study unravelled the underlying pathway where JNK-1 is acting independently of insulin (Montrer INS Protéines)-IGF-1 (Montrer IGF1 Protéines) signalling (IIS) pathway to modulate longevity. In support of in vivo results in silico docking study of UA with C. elegans JNK-1 ATP-binding site suggested promising binding affinity exhibiting binding energy of -8.11 kcalmol(-1). UA induced JNK-1 activation in wild-type animals underlie the importance of pharmacologi
JNK-1 directly interacts with and phosphorylates DAF-16. Moreover, in response to heat stress, JNK-1 promotes the translocation of DAF-16 into the nucleus.
The present study shows in Caenorhabditis elegans that ambient temperature (1-37 degrees C) specifically influences the activation (phosphorylation) of the MAP kinase JNK-1 as well as the nuclear translocation of DAF-16.
the stress response is controlled by a c-Jun N-terminal kinase (JNK)-like mitogen-activated protein kinase (Montrer MAPK1 Protéines) (MAPK (Montrer MAPK1 Protéines)) signaling pathway, which is regulated by MLK-1 (Montrer MAP3K9 Protéines) MAPK (Montrer MAPK1 Protéines) kinase kinase (MAPKKK), MEK-1 (Montrer MAP2K1 Protéines) MAPK (Montrer MAPK1 Protéines) kinase (MAPKK), and KGB-1 (Montrer KCNJ3 Protéines) JNK-like MAPK (Montrer MAPK1 Protéines).
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 is activated by various cell stimuli, and targets specific transcription factors, and thus mediates immediate-early gene expression in response to cell stimuli. The activation of this kinase by tumor-necrosis factor alpha (TNF-alpha) is found to be required for TNF-alpha induced apoptosis. This kinase is also involved in UV radiation induced apoptosis, which is thought to be related to cytochrom c-mediated cell death pathway. Studies of the mouse counterpart of this gene suggested that this kinase play a key role in T cell proliferation, apoptosis and differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
, JUN kinase
, Jun N-terminal kinase
, Jun NH2-terminal kinase
, Jun-N-terminal kinase
, c-Jun N-terminal kinase
, c-Jun aminoterminal kinase
, c-Jun-N-terminal kinase
, drosophila JNK
, JUN N-terminal kinase
, MAP kinase 8
, c-Jun N-terminal kinase 1
, mitogen-activated protein kinase 8 isoform JNK1 alpha1
, mitogen-activated protein kinase 8 isoform JNK1 beta2
, stress-activated protein kinase 1
, stress-activated protein kinase 1c
, JNK1 beta1 protein kinase
, MAPK 8
, mitogen activated protein kinase 8
, protein kinase mitogen-activated 8
, stress-activated protein kinase JNK1
, SAPK gamma
, c-jun NH2-terminal kinase
, p54 gamma
, mitogen-activated protein kinase 8