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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. in 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 ... in Molecular & cellular proteomics : MCP 2015
aken together, these results reveal that inactivation of Rpd3 (show HDAC1 Proteins) independently regulates JNK and Yki (show YAP1 Proteins) activities and that both Hippo and JNK signaling pathways contribute to Rpd3 (show HDAC1 Proteins) RNAi-induced apoptosis.
Data show that JNK signalling inhibits the growth of losers, while JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) signalling promotes competition-induced winner cell proliferation.
Here we uncover a cell non-autonomous requirement for the Epidermal growth factor receptor (Egfr (show EGFR Proteins)) pathway in the lateral epidermis for sustained dpp (show TGFb Proteins) expression in the LE. Specifically, we demonstrate that Egfr (show EGFR Proteins) 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 (show ETS1 Proteins)-domain factor Ets21c and the nuclear receptor Ftz-F1 (show NR5A2 Proteins), all acting downstream of Jun-N-terminal kinase.
Diminished MTORC1-dependent JNK activation underlies the neurodevelopmental defects associated with lysosomal dysfunction.
ROS (show ROS1 Proteins)/JNK/p38 (show MAPK14 Proteins)/Upd (show UROD Proteins) 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 (show NOTCH1 Proteins)-Src (show SRC Proteins) synergy.
This study demonstrated that the mechanism by which Bsk (show FRK Proteins) is required for pruning is through reducing the membrane levels of the adhesion molecule (show NCAM1 Proteins) Fasciclin II (show NCAM2 Proteins) (FasII)
Study solves the crystal structure of unphosphorylated DJNK in complex with adenylyl imidodiphosphate (AMP (show AMPH Proteins)-PNP (show NP Proteins)) and magnesium.
Thus, the present study indicated that parkin (show PARK2 Proteins) knockout inhibits neural stem cell differentiation by JNK-dependent proteasomal degradation of p21 (show CDKN1A Proteins).
JNK activation contributes to glioma cell parthanatos caused by oxidative stress via increase of intracellular reactive oxygen species generation.
ERK1 (show MAPK3 Proteins) Directly Interacts With JNK1 Leading to Regulation of JNK1/c-Jun (show JUN Proteins) Activity and Cell Transformation.
TGM2 (show TGM2 Proteins) is involved in amyloid-beta (1-42)-induced pro-inflammatory activation via AP1 (show FOSB Proteins)/JNK signaling pathways in cultured monocytes.
NleL-induced JNK ubiquitylation, particularly mono-ubiquitylation at the Lys (show LYZ Proteins) 68 residue of JNK, impairs JNK's interaction with an upstream kinase MKK7 (show MAP2K7 Proteins), thus disrupting JNK phosphorylation and activation.
The surface immune molecule CD274 (show CD274 Proteins) plays a critical role in the proliferation of leukemia-initiating cells, LICs. The CD274 (show CD274 Proteins)/JNK/Cyclin D2 (show CCND2 Proteins) pathway promotes the cell cycle entry of LIC.
These data implicate HTRA1 (show HTRA1 Proteins) as a negative regulator of mesenchymal stem cell adipogenesis.
Our findings indicate that GADD45 (show GADD45A Proteins) essentially suppresses the MKK7 (show MAP2K7 Proteins)-JNK pathway and suggest that differentially expressed GADD45 (show GADD45A Proteins) 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 (show SIRT6 Proteins) to DNA damage sites and is required for efficient recruitment of poly (ADP-ribose) polymerase 1 (PARP1 (show PARP1 Proteins)) to DNA break sites and for efficient repair of double-strand break.
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 (show PLA2G2A Proteins) keratinocytes showed enhanced activation of EGFR (show EGFR Proteins) and JNK1/2 that led to c-Jun (show JUN Proteins) activation.
p53 (show TP53 Proteins) 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 (show PTF1A Proteins)(Cre/+) ;Kras(G12D/+) mice with JNK1(-/-) mice to generate Ptf1a (show PTF1A Proteins)(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 (show CCL20 Proteins) secretion
BOC (show BOC Proteins) interacts with ABL (show ABL1 Proteins) 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 (show NLRP3 Proteins) phosphorylation at S194 is a critical priming event and is essential for NLRP3 (show NLRP3 Proteins) 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 (show CASP3 Proteins)-dependent Proteolysis of JNK1-2 and Bid (show BID Proteins).
JNK signaling is required to establish microtubule stability and maintain tissue cohesion in the gut (show GUSB Proteins).
Data show that the death pathway is independent of ERK (show MAPK1 Proteins) but relies on activating Bad phosphorylation through the control of both kinases Cdk1 (show CDK1 Proteins) and JNK.
study reports MPK8 connects protein phosphorylation, Ca(2 (show CA2 Proteins))+ and ROS (show ROS1 Proteins) in wound-signaling pathway; suggests 2 major activation modes, Ca(2 (show CA2 Proteins))+/CaMs and MAP kinase (show MAPK1 Proteins) phosphorylation cascade, converge at MPK8 to monitor or maintain an essential part of ROS (show ROS1 Proteins) homeostasis
our data provide strong evidence that Jip3 in fact serves as an adapter protein linking these cargos to dynein
P38 (show MAPK14 Proteins) and JNK have opposing effects on persistence of in vivo leukocyte migration in zebrafish.
A dorsalization pathway that is exerted by Axin (show AXIN1 Proteins)/JNK signaling and its inhibitor Aida (show AIDA Proteins) during vertebrate embryogenesis, is defined.
JNK-Mmp13 (show MMP13 Proteins) signaling pathway plays an essential role in regulating the innate immune cell migration in response to severe injury in vivo
Findings indicate the MIG-15/JNK-1 pathway can restrict both glutamatergic synapse formation and short-term learning.
Our genetic study unravelled the underlying pathway where JNK-1 is acting independently of insulin (show INS Proteins)-IGF-1 (show IGF1 Proteins) 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 (show MAPK1 Proteins) (MAPK (show MAPK1 Proteins)) signaling pathway, which is regulated by MLK-1 (show MAP3K9 Proteins) MAPK (show MAPK1 Proteins) kinase kinase (MAPKKK), MEK-1 (show MAP2K1 Proteins) MAPK (show MAPK1 Proteins) kinase (MAPKK), and KGB-1 (show KCNJ3 Proteins) JNK-like MAPK (show MAPK1 Proteins).
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