Aperçu des produits pour JNK Protéines (MAPK8)

Full name:
Mitogen-Activated Protein Kinase 8 Protéines (MAPK8)
Chez www.anticorps-enligne.fr sont 30 Mitogen-Activated Protein Kinase 8 (MAPK8) Protéines de 10 de différents fournisseurs disponibles. De plus, nous expédions JNK Anticorps (432) et JNK Kits (27) et beaucoup plus de produits pour cette protéine. Un total de 523 JNK produits sont actuellement listés.
Synonymes:
AI849689, Bsk, BSK/DJNK, c-Jun, CG5680, D-JNK, D-junk, DBSK/JNK, dJNK, DJNK/bsk, Dmel\\CG5680, jnk, JNK-46, JNK/SAPK, jnk1, JNK1A2, JNK21B1/2, Junk, mapk8, Prkm8, sapk1, SAPK1c, SAPKa, T10F20.15, zgc:112379
afficher tous les protéines Gène GeneID UniProt
MAPK8 5599 P45983
MAPK8 26419 Q91Y86
MAPK8 116554 P49185

Afficher tous les synonymes

JNK Protéines (MAPK8) par origine

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JNK Protéines mieux référencés

  1. Human JNK Protein expressed in Baculovirus infected Insect Cells - ABIN2003397 : Slack, Seternes, Gabrielsen, Keyse: Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1. dans The Journal of biological chemistry 2001 (PubMed)
    Show all 3 references for 2003397

  2. 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 (PubMed)

  3. 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 (PubMed)

Plus protéines pour JNK partenaires d'interaction

Fruit Fly (Drosophila melanogaster) Mitogen-Activated Protein Kinase 8 (MAPK8) interaction partners

  1. 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

  2. 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

  3. 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.

  4. Diminished MTORC1-dependent JNK activation underlies the neurodevelopmental defects associated with lysosomal dysfunction.

  5. 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.

  6. 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.

  7. 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)

  8. Study solves the crystal structure of unphosphorylated DJNK in complex with adenylyl imidodiphosphate (AMP (Montrer AMPH Protéines)-PNP (Montrer NP Protéines)) and magnesium.

  9. PERK/ATF4 activated the JNK pathway through Rac1 and Slpr activation in apoptotic cells.

  10. Data show that oxidative stress and neuroinflammation are intrinsic components of TDP-43 (Montrer TARDBP Protéines)-associated neurodegeneration and the balance between cytoprotective JNK and cytotoxic p38 (Montrer MAPK14 Protéines) signaling dictates phenotypic outcome to TDP-43 (Montrer TARDBP Protéines) expression in Drosophila.

Human Mitogen-Activated Protein Kinase 8 (MAPK8) interaction partners

  1. 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

  2. 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...

  3. 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.

  4. 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.

  5. identified the c-Jun N-terminal kinase 1 (JNK1) as the kinase involved in the phosphorylation of NEIL1 (Montrer NEIL1 Protéines)

  6. This study suggests that advanced glycation end products (AGEs) and activation of AGEs receptor could induce the proliferation of smooth muscle cells from Saphenous vein but not smooth muscle cells from internal thoracic arteryvia MAP kinase (Montrer MAPK1 Protéines) pathway in diabetes mellitus.

  7. The increase in c-Jun N-terminal kinase (c-Jun) and specificity protein 1 (SP1 (Montrer SP1 Protéines)) expressions was positively correlated with transforming growth factor beta 1 (TGFbeta1 (Montrer TGFB1 Protéines)) in both high glucose-treated renal mesangial cells (HRMCs) and diabetic kidneys.

  8. JNK1 physically and functionally interacted with VDR (Montrer CYP27B1 Protéines) and positively regulated VDR (Montrer CYP27B1 Protéines) expression at transcriptional and translational levels, which influenced calcitriol-mediated inhibition of cancer cell proliferation.

  9. In conclusion, our findings revealed DIP2 as a novel effector downstream of Bsk (Montrer FRK Protéines) modulating the direction of axon projection.

  10. The release of infectious respiratory syncytial virus (RSV) virions from infected cells was significantly reduced by JNK1/2 siRNA knockdown, implicating JNK1/2 as a key host factor for RSV virus production.

Mouse (Murine) Mitogen-Activated Protein Kinase 8 (MAPK8) interaction partners

  1. 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.

  2. 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.

  3. 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.

  4. 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.

  5. activation of JNK in the endoplasmic reticulum stress response precedes activation of XBP1 (Montrer XBP1 Protéines).

  6. Data suggest that single muscle immobilization induces a shift of myosin heavy chain (MHC) isoforms composition toward a faster contractile phenotype and decreases the polymorphic profile of single fibres, and that activation of p38 and JNK could be a potential mechanism involved in these contractile phenotype modifications during muscle immobilization.

  7. JNK/FoxO1 (Montrer FOXO1 Protéines) is involved in the regulation of oxidative stress-induced (Montrer SQSTM1 Protéines) cell apoptosis in MGCs

  8. apoE (Montrer APOE Protéines)(-/-) mouse carrying a visceral fat graft from obese dnJNK donors were protected against enhanced systemic inflammation and atherogenesis.

  9. These data provide evidence for involvement of the TNF-alpha (Montrer TNF Protéines)-JNK axis in extracellular matrix remodeling.

  10. Phosphorylation levels of P38 (Montrer CRK Protéines) and JNK in siRNA-TMEM16A (Montrer ANO1 Protéines) group were lower than that of the Model group. Thus, TMEM16A (Montrer ANO1 Protéines) is one of the critical components of a signal transduction pathway that links renal injury to podocyte apoptosis in DN.

Xenopus laevis Mitogen-Activated Protein Kinase 8 (MAPK8) interaction partners

  1. Hyperosmotic Shock Engages Two Positive Feedback Loops through Caspase-3 (Montrer CASP3 Protéines)-dependent Proteolysis of JNK1-2 and Bid (Montrer BID Protéines).

  2. JNK signaling is required to establish microtubule stability and maintain tissue cohesion in the gut (Montrer GUSB Protéines).

  3. 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.

Arabidopsis thaliana Mitogen-Activated Protein Kinase 8 (MAPK8) interaction partners

  1. 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

Zebrafish Mitogen-Activated Protein Kinase 8 (MAPK8) interaction partners

  1. our data provide strong evidence that Jip3 in fact serves as an adapter protein linking these cargos to dynein

  2. P38 (Montrer MAPK14 Protéines) and JNK have opposing effects on persistence of in vivo leukocyte migration in zebrafish.

  3. 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.

  4. 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

Caenorhabditis elegans (C. elegans) Mitogen-Activated Protein Kinase 8 (MAPK8) interaction partners

  1. 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

  2. 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.

  3. 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.

  4. 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).

Profil protéine JNK (MAPK8)

Profil protéine

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.

Alternative names and synonyms associated with JNK (MAPK8)

  • basket (bsk)
  • mitogen-activated protein kinase 8 (MAPK8)
  • mitogen-activated protein kinase 8 (Mapk8)
  • mitogen-activated protein kinase 8 (mapk8)
  • mitogen-activated protein kinase 8 (ATMPK8)
  • mitogen-activated protein kinase 8b (mapk8b)
  • Protein JNK-1 (jnk-1)
  • AI849689 Protéine
  • Bsk Protéine
  • BSK/DJNK Protéine
  • c-Jun Protéine
  • CG5680 Protéine
  • D-JNK Protéine
  • D-junk Protéine
  • DBSK/JNK Protéine
  • dJNK Protéine
  • DJNK/bsk Protéine
  • Dmel\\CG5680 Protéine
  • jnk Protéine
  • JNK-46 Protéine
  • JNK/SAPK Protéine
  • jnk1 Protéine
  • JNK1A2 Protéine
  • JNK21B1/2 Protéine
  • Junk Protéine
  • mapk8 Protéine
  • Prkm8 Protéine
  • sapk1 Protéine
  • SAPK1c Protéine
  • SAPKa Protéine
  • T10F20.15 Protéine
  • zgc:112379 Protéine

Protein level used designations for MAPK8

CG5680-PB , CG5680-PE , CG5680-PF , JNK , JUN kinase , Jun N-terminal kinase , Jun NH2-terminal kinase , Jun-N-terminal kinase , Jun-kinase , bsk-PB , bsk-PE , bsk-PF , 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 , jnk1a-1 , mitogen-activated protein kinase 8

GENE ID SPECIES
44801 Drosophila melanogaster
5599 Homo sapiens
26419 Mus musculus
116554 Rattus norvegicus
379876 Xenopus laevis
838394 Arabidopsis thaliana
65236 Danio rerio
177460 Caenorhabditis elegans
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