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Human ERK2 Protein expressed in Baculovirus infected Insect Cells - ABIN2001936
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. in The Journal of biological chemistry 2001
Show all 2 Pubmed References
Human ERK2 Protein expressed in Wheat germ - ABIN1310256
Abeydeera, Egli, Cox, Mercier, Conde, Pallan, Mizurini, Sierant, Hibti, Hassell, Wang, Liu, Liu, Martinez, Sood, Lybrand, Frydman, Monteiro, Gomer, Nawrot, Yang: Evoking picomolar binding in RNA by a single phosphorodithioate linkage. in Nucleic acids research 2016
MKP1 (show DUSP1 Proteins) is a negative regulator of signaling pathways required for some, but not all, early and late pathogen-associated molecular pattern responses.
MKP1 (show DUSP1 Proteins) and PTP1 act redundantly to suppress salicylic acid and camalexin biosynthesis, and regulate growth homeostasis and PR gene expression in an MPK3 (show MAPK3 Proteins)- and MPK6 (show MAPK6 Proteins)-dependent manner.
Regulation of AtMPK1/2 kinase activity in Arabidopsis might be under the control of signals involved in different kinds of stress.
AtMKP2, a novel MKP protein in Arabidopsis, acts upon MPK3 (show MAPK3 Proteins) and -6, and serves as a positive regulator of the cellular response to oxidant challenge
The present results suggest that demecolcine might contribute to the activation of the Mos (show MOCOS Proteins)/MAPK pathway and affect spindle structure
MAPK1 upregulated milk protein (show CSN2 Proteins) synthesis through the Stat5 (show STAT5A Proteins) and mTOR (show FRAP1 Proteins) pathways.
Chronic hypoxia induces Egr-1 via activation of ERK1/2 and contributes to pulmonary vascular remodeling.
ER Ca(2+) release enhances eNOS Ser-635 phosphorylation and function via ERK1/2 activation.
Cyclin-dependent kinase (show CDK1 Proteins) inhibition did not affect the expression (mRNA and protein levels) and localization of maturation promoting factor(MPF (show MSLN Proteins)) and MAPK, and had nearly no effect on kinase activities during maturation.
Thrombospondin 1 (show THBS1 Proteins), fibronectin (show FN1 Proteins), and vitronectin (show VTN Proteins) are differentially dependent upon RAS, ERK1/2, and p38 (show MAPK14 Proteins) for induction of vascular smooth muscle cell chemotaxis.
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
These data suggest that Gab1-ERK1/2 binding and their nuclear translocation play a crucial role in Egr-1 (show EGR1 Proteins) nuclear accumulation.
Role of CaMKII (show CAMK2G Proteins) in hydrogen peroxide activation of p38 MAPK (show MAPK14 Proteins)/heat shock protein 27 pathway and ERK1/2
data demonstrate that hypoxia-induced adventitial fibroblast proliferation requires activation and interaction of PI3K, Akt, mTOR, p70S6K, and ERK1/2.
Excess PLAC8 promotes an unconventional ERK2-dependent EMT (show ITK Proteins) in colon cancer.
ERK1/2-Akt1 (show AKT1 Proteins) crosstalk regulates arteriogenesis in mice and zebrafish.
eena (show SH3GL1 Proteins) plays an important role in the development of the myeloid cell through activation of the ERK1 (show MAPK3 Proteins)/ERK2 pathway
ERK1 (show MAPK3 Proteins) and ERK2 target common and distinct gene sets, confirming diverse roles for these kinases during embryogenesis; for ERK2 genes involved in cell-migration, mesendoderm differentiation and patterning were identified.
These results demonstrate that induction of Hsp70 (show HSPA1A Proteins) in response to heat stress is dependent on ERK activation in Pac2 (show PSMG2 Proteins) cells.
Data define distinct roles for ERK1 (show MAPK3 Proteins) and ERK2 in developmental cell migration processes during zebrafish embryogenesis.
GLUL (show GLUL Proteins) knockdown markedly inhibited the p38 MAPK (show MAPK14 Proteins) and ERK1 (show MAPK3 Proteins)/ERK2 signaling pathways in cultured breast cancer cells and reduces their proliferation.
These results suggested that HOXB7 (show HOXB7 Proteins) stimulates ERK1/2 phosphorylation and provided evidence that HOXB7 (show HOXB7 Proteins), besides its role in transcriptional regulation, also promotes cell motility and invasiveness.
High ERK2 expression is associated with castration-resistant prostate cancer.
combined use of butyrate and highly specific Syk inhibitor BAY61-3606 does not enhance differentiation and apoptosis of colonocytes. Instead, BAY completely abolishes butyrate-induced differentiation and apoptosis in a Syk- and ERK1/2-dependent manner.
new findings indicating that canonical FGFR-ERK1/2 signaling entrapped hBMSCs in a pre-committed state and arrested further maturation of committed precursors.
mutually exclusive transcriptional regulation by AP-1 (cjun (show JUN Proteins)/cfos) and non-canonical NF-kappaB (show NFKB1 Proteins) (RelB (show RELB Proteins)/p52 (show FKBP4 Proteins)) downstream of MEK (show MAP2K1 Proteins)-ERK (show EPHB2 Proteins) and NIK (show MAP3K14 Proteins)-IKK-alpha (show CHUK Proteins)-NF-kappaB2 (p100 (show CUX1 Proteins)) phosphorylation, respectively was responsible for persistent Ccl20 (show CCL20 Proteins) expression in the colonic cells.
we have demonstrated a pathogenic role for aPL (show FASL Proteins) containing samples, mediated via aPL (show FASL Proteins)-b2GPI (show APOH Proteins) interactions, resulting in activation of the pro-apoptotic p38 MAPK (show MAPK14 Proteins) pathway.
LPS (show IRF6 Proteins)-activated ERK1,2 was at least partly involved in the observed effects on periodontal ligament stem cell differentiation capacity, acquisition of myofibroblastic attributes, and changes of their immunomodulatory features.
The findings indicate that ERK (show EPHB2 Proteins) and JNK (show MAPK8 Proteins) signaling pathways, as well as NF-kappaB (show NFKB1 Proteins)-mediated signaling are important contributors to the pathogenesis of Kashin-Beck disease.
observations provide important insights into the regulation of EpCAM (show EPCAM Proteins) expression during EMT (show ITK Proteins), demonstrate an unexpected role for EpCAM (show EPCAM Proteins) in the regulation of ERK (show EPHB2 Proteins) and define a novel double-negative feedback loop between EpCAM (show EPCAM Proteins) and ERK (show EPHB2 Proteins) that contributes to the regulation of EMT (show ITK Proteins).
Cortical neuron-specific deletion of extracellular signal-regulated kinases Erk1 (show MAPK3 Proteins) or Erk2 significantly increased the duration of wakefulness.
pERK1/2 is a regulator of CD44 (show CD44 Proteins) expression, and increased CD44 (show CD44 Proteins) expression leads to a pro-sclerotic and migratory parietal epithelial cell phenotype in focal segmental glomerulosclerosis.
mmLDL increased the serum concentrations and expression of ICAM-1 (show ICAM1 Proteins) and VCAM-1 (show VCAM1 Proteins) by activating the ERK1/2 pathway, resulting in the expression of ETB (show EDNRB Proteins) receptors and the enhancement of contractile function in vascular smooth muscle.
These results indicate a crucial role of the Rapgef2 (show RAPGEF2 Proteins)-Rap1A (show RAP1A Proteins)-ERK (show EPHB2 Proteins)-c-jun (show JUN Proteins) pathway in regulation of the AJ formation in RGCs.
MFA has a protective effect on alcohol-induced liver injury, which may be related to its antioxidant,anti-inflammatory,lipid-eliminating properties and its ability to regulate the NOX4 (show NOX4 Proteins)/ROS (show ROS1 Proteins)-MAPK signalling pathway.
MAPK3 (show MAPK3 Proteins)/1 participates in primordial follicle activation through mTORC1-KITL (show KITLG Proteins) signaling.
The purpose of this study was to investigate mechanisms that govern the regulation of Npnt (show NPNT Proteins) gene expression by IL-1beta (show IL1B Proteins) in osteoblasts.
The results of this study suggested that Erk2 activation in astrocytes plays a crucial role in aggravating demyelinating inflammation by inducing inflammatory mediators and gliosis.
At low oxLDL levels LOX-1 activates the protective Oct-1/SIRT1 pathway, while at higher levels of the lipoprotein switches to the thrombogenic ERK1/2 pathway.
Studies indicate that progesterone receptor transgenic (Pgrcre/+) mitogen inducible gene 6 (Mig-6over) phosphatase and tensin homolog protein (Ptenf/f) knockout mice exhibited an increase of phospho-ERK1/2 and its target genes.
Early activation of MAPK p44/42 is involved in deoxynivalenol -induced disruption of intestinal barrier function and tight junction network signaling.
Agonist stimulation of vascular smooth muscle increases PKC (show FYN Proteins) activity, which, in turn, increases MKP-1 (show DUSP1 Proteins) activity and maintains MAPK1 activity at submaximal values.
sub-vasomotor concentration of ET-1 (show EDN1 Proteins) leads to vascular dysfunction by impairing endothelium-dependent NO-mediated dilation via p38 (show MAPK14 Proteins) kinase-mediated production of superoxide from NADPH oxidase (show NOX1 Proteins) following ETA receptor activation
Treatment with ERK inhibitors or ERK1/2 knockdown significantly suppressed porcine epidemic diarrhea virus progeny production.
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.
CSF2 (show CSF2 Proteins) stimulates proliferation of trophectoderm cells by activation of the PI3K-and ERK1/2 MAPK-dependent MTOR (show FRAP1 Proteins) signal transduction cascades.
PGRN (show GRN Proteins) inhibits adipogenesis in porcine preadipocytes partially through ERK activation mediated PPARgamma (show PPARG Proteins) phosphorylation.
Data show that proinflammatory cytokines induction was ERK1/2 and JNK1 (show MAPK8 Proteins)/2 dependent.
The authors show that porcine circovirus type 2 (PCV2) activates ERK1/2 in PCV2-infected PK15 cells dependent on viral replication.
20-HETE activates the Raf/MEK/ERK pathway in renal epithelial cells through an EGFR- and c-Src-dependent mechanism.
Here the authors show that CPEB4 activity is regulated by ERK2- and Cdk1-mediated hyperphosphorylation. These phosphorylation events additively activate CPEB4 in M-phase by maintaining it in its monomeric state.
The reciprocal feedback observed between MPF (show MSLN Proteins) and ERK2 in meiosis is not observed during mitotic M-phase in cell-free Xenopus embryo extracts.
The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), 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. The activation of this kinase requires its phosphorylation by upstream kinases. Upon activation, this kinase translocates to the nucleus of the stimulated cells, where it phosphorylates nuclear targets. Two alternatively spliced transcript variants encoding the same protein, but differing in the UTRs, have been reported for this gene.
mitogen-activated protein kinase 1
, MAP kinase 1
, MAP kinase 2
, MAPK 1
, MAPK 2
, extracellular signal-regulated kinase 2
, mitogen-activated protein kinase 2
, MAP kinase isoform p42
, protein tyrosine kinase ERK2
, mitogen activated protein kinase 1
, extracellular-signal-regulated kinase 2
, extracellular signal-regulated kinase-2
, MAP kinase
, mitogen-activated protein kinase 1b
, myelin basic protein kinase-like protein
, mitogen-activated protein kinase 1a