Aperçu des produits pour anti-MAPK3 (MAPK3) Anticorps

Human Mitogen-Activated Protein Kinase 3 (MAPK3) interaction partners

1. CSNK2A1 plays a role in the nuclear translocation of ERK1/2. Ser246 phosphorylation by CK2 is sufficient for full ERK translocation, while Ser244 phosphorylation accelerates it.

2. The computer prediction was confirmed with pulldown and in vitro kinase assays, in which IBC directly bound with ERK1/2 and RSK2, and dosedependently blocked RSK2 kinase activity in liver cancer cells

3. Shear stress loading for 6h promotes liver cancer stem cells (LCSCs) migration and activation of the focal adhesion kinase (FAK) and extracellular signal regulated kinase1/2 (ERK1/2) signalling pathways.

4. both HSP60 knockdown and oxidative phosphorylation (OXPHOS) inhibition by metformin decreased Erk1/2 phosphorylation and induced apoptosis and cell cycle arrest.

5. GPS2 enhances BK channel activity and its protein expression by reducing ERK1/2 signaling-mediated degradation of the channel.

6. High ERK1 expression is associated with glioma cell growth and invasiveness.

7. FSHR specific residues K589 and A590 in the EL3 of FSHR seem to be crucial for FSH-induced internalization and ERK phosphorylation

8. In pulmonary artery hypertension miR-205-5p suppressed pulmonary artery smooth muscle cell proliferation by targeting MICAL2, which activated ERK1/2 signaling.

9. Activation of ERK1 is associated with initiation and progression of glioma.

10. These results suggest that quick induction of PSMD11 or other acute apoptosis inhibitors through activation of the MEK1/ERK1/2 signaling pathway may be one of the important surviving mechanism which can help pancreatic cancer cells avoid acute apoptosis

11. The results suggested that cartilage endplate stem cells might promote nucleus pulposus cells proliferation in a paracrine pathway, which was partially mediated by SDF-1/CXCR4 axis via ERK1/ERK2 signaling transduction pathway.

12. ERK1/2 is a critical molecule in the mediation ofthe osteogenic differentiation of hPDLCs under mechanical stimulation. ERK1/2 activation induced the elevation of Runx2 protein levels, which may be involved in the stretch-induced expressions of OCN and BSP.

13. A novel mutation of MSX1 in oligodontia found in a Chinese pedigree inhibits odontogenesis of dental pulp stem cells via the ERK pathway.

14. High ERK1 expression is associated with dilated cardiomyopathy.

15. High ERK1 expression promotes invasion of colorectal cancer.

16. High ERK1 expression is associated with acute lymphoblastic leukemia.

17. ERK1 and -2 are acetylated and that HDAC6 promotes ERK1 activity via deacetylation.

18. EGFR-mediated matrix metalloproteinase-7 up-regulation promotes epithelial-mesenchymal transition via ERK1-AP1 axis during ovarian endometriosis progression.

19. A2B adenosine receptor in MDA-MB-231 breast cancer cells diminishes ERK1/2 phosphorylation by activation of MAPK-phosphatase-1

20. these results suggest that sustained presence of lipid inflammatory mediator LTD4 could induce human airway epithelial cell proliferation through ERK1/2 phosphorylation, either directly via CysLT1 receptor or by transactivating EGFR.

Mouse (Murine) Mitogen-Activated Protein Kinase 3 (MAPK3) interaction partners

1. spinophilin fulfills an essential role in cocaine-induced behavioral sensitization, likely via ERK1/2 phosphorylation and induction of c-Fos and FosB in the striatum.

2. DUSP5 functions in the feedback inhibition of ERK1/2 signaling in response to TNFalpha, which resulted in increased inflammatory gene expression.

3. Data suggest diabetes is accompanied by increases in arterial miR-221 and -222 expression that promotes intimal thickening via extracellular signal-regulated kinases 1/2 signaling.

4. IL-17A aggravates inflammatory response during Acute myocardial infarction by inducing macrophages infiltration and activating NLRP3 inflammasome through AMPKalpha/p38MAPK/ERK1/2 pathway.

5. we show that the H222P amino acid substitution in lamin A enhances its binding to ERK1/2 and increases sequestration at the nuclear envelope. Finally, we show that genetic deletion of Dusp4 has beneficial effects on heart function and prolongs survival in LmnaH222P/H222P mice. These results further establish Dusp4 as a key contributor to the pathogenesis of LMNA cardiomyopathy and a potential target for drug therapy.

6. SIRT6 attenuates cisplatin-induced acute kidney injury by binding to the promoters of ERK1 and ERK2 and deacetylated histone 3 at Lys9 (H3K9) thereby inhibiting ERK1/2 expression.

7. results demonstrate the mechanism for the maintenance of the undifferentiated state of embryonic stem cells via the inhibition of the FGF4-PKCzeta-MEK-ERK1/2 pathway by O-GlcNAcylation on PKCzeta.

8. Selective inhibition or knockdown of Rac1 decreased IL-6 and IL-8 release in 16HBE cells induced by cigarette smoke extract (CSE), which correlated with CSE-induced Rac1-regulated Erk1/2 mitogen-activated protein kinase (MAPK) and signal transducer and activator of transcription-3 (STAT3) signaling.

9. M-CSF-evoked ERK1/2 activation was decreased, whereas AKT activation was enhanced in SHP2-deficient BMMs. ERK1/2, via its downstream target RSK2, mediates this negative feedback by negatively regulating phosphorylation of M-CSF receptor at Tyr721 and, consequently, its binding to p85 subunit of PI3K and PI3K activation.

10. Low ERK1 Phosphorylation is associated with low liver regeneration.

11. ERK5 provides a common bypass route in intestinal epithelial cells, which rescues cell proliferation upon abrogation of ERK1/2 signalling, with therapeutic implications in colorectal cancer.

12. In a retinitis pigmentosa mouse model, TrkC activity generates phosphorylated Erk, which upregulates glial TNF-alpha, causing selective neuronal death.

13. A. fumigatus increased PAR-2 expression and elevated disease, PMN infiltration, and proinflammatory cytokine expreERK1 Kinasession through PAR-2, which may be modified by p-ERK1/2.

14. ERK1 and ERK2 play specific roles in beta cells. ERK2 cannot always compensate for the lack of ERK1 but the absence of a clear-cut phenotype in Erk1 (-/-) mice shows that ERK1 is dispensable in normal conditions.

15. The Macrophage Activation Induced by Bacillus thuringiensis Cry1Ac Protoxin Involves ERK1/2 and p38 Pathways and the Interaction with Cell-Surface-HSP70.

16. hBD-1 potentiates the induction of in vitro osteoclastogenesis by RANKL via enhanced phosphorylation of the p44/42 MAPKs.

17. ERK1 role in the osteoclast differentiation.Insulin induces RANK expression via ERK1/2, which contributes to the enhancement of osteoclast differentiation.

18. Suppressing P38 promoted adipogenic trans-differentiation and intensified adipolytic metabolism in differentiated cells. However, inhibition of ERK1/2 had the opposite effects on adipogenesis and no effect on adipolysis. Blocking JNK weakly blocked trans-differentiation but stimulated adipolysis and induced apoptosis.

19. Taken together, the results of our present study indicated that DHCE could inhibit cellular proliferation and induce cell apoptosis in myeloma cells mediated through different mechanisms, possibly through inhibiting the IL-6/STAT3 and ERK1/2 pathways. And it may provide a new therapeutic option for MM patients.

20. Betacellulin promotes the proliferation of corneal epithelial stem cells through the phosphorylation of Erk1/Erk2.

Zebrafish Mitogen-Activated Protein Kinase 3 (MAPK3) interaction partners

1. MAPK3 role in the oocyte maturation

2. ERK1/2-Akt1 crosstalk regulates arteriogenesis in mice and zebrafish.

3. eena plays an important role in the development of the myeloid cell through activation of the ERK1/ERK2 pathway

4. ERK1 and ERK2 target common and distinct gene sets, confirming diverse roles for these kinases during embryogenesis; for ERK1 different specific genes involved in dorsal-ventral patterning and subsequent embryonic cell migration were identified.

5. These results demonstrate that induction of Hsp70 in response to heat stress is dependent on ERK activation in Pac2 cells.

6. Data define distinct roles for ERK1 and ERK2 in developmental cell migration processes during zebrafish embryogenesis.

Cow (Bovine) Mitogen-Activated Protein Kinase 3 (MAPK3) interaction partners

1. MAPK3/1 is involved in luteinizing hormone-mediated decrease of C-type natriuretic peptide and this process is related to the EGFR and MAPK3/1 signal pathways

2. Chronic hypoxia induces Egr-1 via activation of ERK1/2 and contributes to pulmonary vascular remodeling.

3. ER Ca(2+) release enhances eNOS Ser-635 phosphorylation and function via ERK1/2 activation.

4. Thrombospondin 1, fibronectin, and vitronectin are differentially dependent upon RAS, ERK1/2, and p38 for induction of vascular smooth muscle cell chemotaxis.

5. results suggest that Nav1.7-Ca2+ influx-protein kinase C-alpha pathway activated ERK1/ERK2 and p38, which increased phosphorylation of glycogen synthase kinase-3beta, decreasing tau phosphorylation

6. These data suggest that Gab1-ERK1/2 binding and their nuclear translocation play a crucial role in Egr-1 nuclear accumulation.

7. data demonstrate that hypoxia-induced adventitial fibroblast proliferation requires activation and interaction of PI3K, Akt, mTOR, p70S6K, and ERK1/2.

8. This study demonstrates for the first time that cyclic mechanical stretch induces the proliferation of bovine satellite cells and suppresses their myogenic differentiation through the activation of ERK.

9. findings indicate that exposure to DHEA, at concentrations found in human blood, causes vascular endothelial proliferation by a plasma membrane-initiated activity that is Gi/o and ERK1/2 dependent.

10. These results suggest that bGPR40 mediates LCFA signaling in mammary epithelial cells and thereby plays an important role in cell proliferation and survival.

11. Results suggest that estrogen receptors and the ERK1/2 signaling pathway are involved in the anti-apoptotic action of LY117018 in vascular endothelial cells.

12. The intracellular mechanism of action of CART in regulation of FSH-induced MAPK signaling.

13. IFN-alpha mediated activation of ERK1/2 appeared to be responsible for the increased phosphorylation of tyrosine hydroxylase.

Pig (Porcine) Mitogen-Activated Protein Kinase 3 (MAPK3) interaction partners

1. Early activation of MAPK p44/42 is involved in deoxynivalenol -induced disruption of intestinal barrier function and tight junction network signaling.

2. Pseudorabies virus glycoprotein gE-mediated ERK 1/2 phosphorylation also occurs in epithelial cells and in these cells, gE-mediated ERK 1/2 signaling is associated with degradation of the pro-apoptotic protein Bim.

3. Treatment with ERK inhibitors or ERK1/2 knockdown significantly suppressed porcine epidemic diarrhea virus progeny production.

4. This study reveals a new function of the gE glycoprotein of pseudorabies virus and suggests that pseudorabies virus, through activation of ERK1/2 signaling, has a substantial impact on T cell behavior.

5. CSF2 stimulates proliferation of trophectoderm cells by activation of the PI3K-and ERK1/2 MAPK-dependent MTOR signal transduction cascades.

6. PGRN inhibits adipogenesis in porcine preadipocytes partially through ERK activation mediated PPARgamma phosphorylation.

7. The food contaminant deoxynivalenol activates the mitogen activated protein kinases in the intestine.

8. Porcine circovirus type 2 (PCV2) might induce autophagy via the AMPK/ERK/TSC2/mTOR signaling pathway in the host cells, representing a pivotal mechanism for PCV2 pathogenesis

9. Data show that proinflammatory cytokines induction was ERK1/2 and JNK1/2 dependent.

10. Saccharomyces cerevisiae inhibits the Enterotoxigenic Escherichia coli-induced expression of pro-inflammatory transcripts and this inhibition was associated to a decrease of ERK1/2 and p38 MAPK phosphorylation

11. ERK1 phosphorylation in response to Insulin-like Growth Factor-1 does not require activation of the Insulin-like Growth Factor-1 receptor tyrosine kinase

12. Retinal ischemia-reperfusion alters expression of mitogen-activated protein kinases, particularly ERK1/2, in the neuroretina and retinal arteries.

13. Cyclosporine A/sirolimus alter claudin-1 expression in renal proximal tubular cells via ERK1/2 signaling pathway to alter barrier function.

14. Data show that treatment with GH or IGF-I reduced leptin receptor expression, and increased Phosphorylation of ERK1/2 in response to acute leptin.

15. role of ERK1 and 2 in mediating IGF-I-stimulated vascular smooth muscle cell proliferation and chemotaxis [ERK1, ERK2]

16. endogenous ceramides are important second messengers in IL-1beta-induced apoptosis in pig thyroid cells through inhibition of adenylyl cyclase and ERK1/2 activities

17. Phorbol 12-myristate 13-acetate activation of ERK and JNK signaling is relevant in the regulation of gene expression during follicular development, ovulation, and luteinization.

18. There was no correlation of infarct size with expression or phosphorylation of ERK1 in ischemic postconditioning.

19. The authors show that porcine circovirus type 2 (PCV2) activates ERK1/2 in PCV2-infected PK15 cells dependent on viral replication.

20. 20-HETE activates the Raf/MEK/ERK pathway in renal epithelial cells through an EGFR- and c-Src-dependent mechanism.

Candida albicans Mitogen-Activated Protein Kinase 3 (MAPK3) interaction partners

1. While some level of mating can occur in the presence of a single kinase, the Cek1 kinase is most important for mating, while the Cek2 kinase is involved in adaptation to signaling. While both kinases appear to be themselves regulated by dephosphorylation through the action of the Cpp1 phosphatase, this process appears important for mating only in the case of Cek1.

2. independent hyperactivation of the MAP kinase kinase kinase Ste11 in wild-type cells leads to Cek1 activation and increased beta (1,3)-glucan exposure. Thus, upregulation of the Cek1 MAPK pathway causes unmasking, and may be responsible for unmasking in cho1Delta/Delta.

3. The results suggest that the MPK-1/ERK regulatory network, including FBF-1, FBF-2, and LIP-1, controls the number of sperm by regulating the timing of the sperm-oocyte switch in C. elegans.

4. data support a role for the Cek1mediated pathway in fungal cell wall maintenance, virulence and antifungal discovery

5. Cek2 has a cryptic role in cell-wall biogenesis and its role is not entirely redundant to Cek1.

6. knockdown of SUV420H1 reduced phosphorylated ERK1 and total ERK1 proteins, and interestingly suppressed ERK1 at the transcriptional level

7. Secreted aspartic protease-mediated proteolytic cleavage of Msb2 is required for activation of the Cek1 mitogen activated protein kinase pathway in response to environmental cues.

8. The authors propose that a Msb2, Cek1 and Ace2 signalling pathway addresses PMT genes as downstream targets and that different modes of regulation have evolved for PMT1 and PMT2/PMT4 genes.

9. Dfi1 function promotes matrix-dependent activation of Cek1 kinase during growth.

10. Msb2 is involved in the transmission of the signal toward Cek1 mediated by the Cdc42 GTPase.

Arabidopsis thaliana Mitogen-Activated Protein Kinase 3 (MAPK3) interaction partners

1. A positive regulatory loop consisting of MPK3/MPK6, WRKY33, ALD1, and pipecolic acid in systemic acquired resistance induction .

2. critical role in manipulating plant photosynthetic activities to promote ROS accumulation in chloroplasts and hypersensitive response cell death, which contributes to the robustness of effector-triggered immunity

3. abscisic acid and jasmonate mediate inactivation of the immune-associated MAP kinases (MAPKs), MPK3 and MPK6, in Arabidopsis thaliana ABA induced expression of genes encoding the protein phosphatases 2C (PP2Cs), HAI1, HAI2, and HAI3 through ABF/AREB transcription factors

4. Constitutive active-MPK3 plants are more resistant to the hemibiotrophic pathogen Pseudomonas syringae DC3000.

5. constitutively active (CA)-MPK3 crosses with summ1 and summ2, two known suppressors of mpk4, resulted in a partial reversion of the CA-MPK3 phenotypes.

6. that MPK3/MPK6 phosphorylate and destabilize ICE1, which negatively regulates CBF expression and freezing tolerance in plants

7. Changes in PUB22 Ubiquitination Modes Triggered by MITOGEN-ACTIVATED PROTEIN KINASE3 Dampen the Immune Response

8. MPK3 role in ultraviolet induced stomatal closure

9. Study propose that the pathogen-responsive MPK3/MPK6 cascade and ABA are two essential signaling pathways that control, respectively, the organic acid metabolism and ion channels, two main branches of osmotic regulation in guard cells that function interdependently to control stomatal opening/closure.

10. Data report that MPK3/MPK6 and their substrate ERF6 promote the biosynthesis of IGSs and the conversion of I3G to 4MI3G, a target of PEN2/PEN3-dependent chemical defenses in plant immunity.

11. Data show that the protein kinases MPK3 and MPK6 can both interact with SPOROCYTELESS/NOZZLE (SPL) in vitro and in vivo and can phosphorylate the SPL protein in vitro.

12. MKK4, MKK5, MKK7, and MKK9, are responsible for the activation of MPK3 and MPK6 by melatonin, indicating that melatonin-mediated innate immunity is triggered by MAPK signaling through MKK4/5/7/9-MPK3/6 cascades.

13. Phosphatase AP2C1, as well as AP2C1-targeted MPK3 and MPK6, are important regulators of plant-nematode interaction, where the co-ordinated action of these signalling components ensures the timely activation of plant defence.

14. Results demonstrated the contribution of MPK3 and MPK6 to riboflavin-induced resistance.

15. These results indicate that the MVB pathway is positively regulated by pathogen-responsive MPK3/6 through LIP5 phosphorylation and plays a critical role in plant immune system

16. MKK3-MPK6 is activated by blue light in a MYC2-dependent manner.

17. MPK3 and MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate immune responses.

18. MicroRNA biogenesis factor DRB1 is a phosphorylation target of mitogen activated protein kinase MPK3 in both rice and Arabidopsis

19. MPK3 represses the constitutive and flg22-induced expression of defence genes in Arabidopsis thaliana.

20. These results suggest that the MKK9-MPK3/MPK6 cascade is part of the phosphate signaling pathway in plants.