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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
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
aken together, these results reveal that inactivation of Rpd3 (Montrer HDAC1 Protéines) independently regulates JNK and Yki (Montrer YAP1 Protéines) activities and that both Hippo and JNK signaling pathways contribute to Rpd3 (Montrer HDAC1 Protéines) RNAi-induced apoptosis.
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.
ERK1 (Montrer MAPK3 Protéines) Directly Interacts With JNK1 Leading to Regulation of JNK1/c-Jun (Montrer JUN Protéines) Activity and Cell Transformation.
TGM2 (Montrer TGM2 Protéines) is involved in amyloid-beta (1-42)-induced pro-inflammatory activation via AP1 (Montrer FOSB Protéines)/JNK signaling pathways in cultured monocytes.
NleL-induced JNK ubiquitylation, particularly mono-ubiquitylation at the Lys (Montrer LYZ Protéines) 68 residue of JNK, impairs JNK's interaction with an upstream kinase MKK7 (Montrer MAP2K7 Protéines), thus disrupting JNK phosphorylation and activation.
The surface immune molecule CD274 (Montrer CD274 Protéines) plays a critical role in the proliferation of leukemia-initiating cells, LICs. The CD274 (Montrer CD274 Protéines)/JNK/Cyclin D2 (Montrer CCND2 Protéines) pathway promotes the cell cycle entry of LIC.
These data implicate HTRA1 (Montrer HTRA1 Protéines) as a negative regulator of mesenchymal stem cell adipogenesis.
Our findings indicate that GADD45 (Montrer GADD45A Protéines) essentially suppresses the MKK7 (Montrer MAP2K7 Protéines)-JNK pathway and suggest that differentially expressed GADD45 (Montrer GADD45A Protéines) family members fine-tune stress-inducible JNK activity.
Quantitative phosphoproteomic analysis identifies the critical role of JNK1 in neuroinflammation induced by Japanese encephalitis virus
post-translational modification facilitates the mobilization of SIRT6 (Montrer SIRT6 Protéines) to DNA damage sites and is required for efficient recruitment of poly (ADP-ribose) polymerase 1 (PARP1 (Montrer PARP1 Protéines)) to DNA break sites and for efficient repair of double-strand break.
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.
the effects of JNK1 deficiency in an experimental model of familial Alzheimer's disease, was investigated.
Irradiation coupled with JNK inhibition in beta1 integrin -/- transgenic adenocarcinoma of prostate (TRAMP) leads to increased levels of nuclear focal adhesion kinase (FAK) in tumor cells.
transgenic mice overexpressing sPLA2 -IIA (Montrer PLA2G2A Protéines) keratinocytes showed enhanced activation of EGFR (Montrer EGFR Protéines) and JNK1/2 that led to c-Jun (Montrer JUN Protéines) activation.
p53 (Montrer TP53 Protéines) plays a novel protective role in APAP induced liver injury through inhibiting the activation of JNK, a key mediator in APAP-induced oxidative stress.
We crossed Ptf1a (Montrer PTF1A Protéines)(Cre/+) ;Kras(G12D/+) mice with JNK1(-/-) mice to generate Ptf1a (Montrer PTF1A Protéines)(Cre/+) ;Kras(G12D/+) ;JNK1(-/-) (Kras;JNK1(-/-) ) mice. Tumor weight was significantly lower in Kras;JNK1(-/-) mice than in Kras;JNK1(+/-) mice, whereas histopathological features were similar.we concluded that inhibition of activated JNK in pancreatic tumor stroma could be a potential therapeutic target to increase Ccl20 (Montrer CCL20 Protéines) secretion
BOC (Montrer BOC Protéines) interacts with ABL (Montrer ABL1 Protéines) and activates JNK thereby promoting neuronal differentiation and neurite outgrowth.
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 results of this study suggest that JNK has a role in the disassembly adherens junctions by means of endocytosis that is required during buccopharyngeal membrane perforation.
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