PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22560157-15 2012 Altogether, these findings suggest that Erk signaling inhibition could play a role in both suppressing TNFalpha production and inducing oxidative stress generation and astrogliosis, therefore modulating a dual action of EtOH plus LPS in glial cells. Ethanol 220-224 mitogen-activated protein kinase 1 Homo sapiens 40-43 24365239-6 2014 We have shown that ethanol injury decreased the transepithelial electrical resistance (TER) along with the reduction of ERK and FAK phosphorylation. Ethanol 19-26 mitogen-activated protein kinase 1 Homo sapiens 120-123 24201001-9 2014 Some increase (1.8-fold) was also seen in the phosphorylation of ERK2 at 48 h, in cells exposed to both ethanol and nicotine. Ethanol 104-111 mitogen-activated protein kinase 1 Homo sapiens 65-69 24026251-8 2013 In addition, inhibitors of casein kinase 2 (CK2) and extracellular signal-regulated kinase (ERK) augmented ethanol-induced p75NTR expression. Ethanol 107-114 mitogen-activated protein kinase 1 Homo sapiens 53-90 24026251-8 2013 In addition, inhibitors of casein kinase 2 (CK2) and extracellular signal-regulated kinase (ERK) augmented ethanol-induced p75NTR expression. Ethanol 107-114 mitogen-activated protein kinase 1 Homo sapiens 92-95 24026251-9 2013 Our results also demonstrate that inhibition of ERK and CK2 caused a further increase in the activation of the p75NTR proximal promoter induced by ethanol. Ethanol 147-154 mitogen-activated protein kinase 1 Homo sapiens 48-51 24026251-14 2013 These data suggest that ethanol increases p75NTR expression, and CK2 and ERK signaling inversely regulate Sp1-mediated p75NTR expression in ethanol-treated neuroblastoma cells. Ethanol 140-147 mitogen-activated protein kinase 1 Homo sapiens 73-76 21876711-0 2011 The Ethanol Extract of Fructus trichosanthis Promotes Fetal Hemoglobin Production via p38 MAPK Activation and ERK Inactivation in K562 Cells. Ethanol 4-11 mitogen-activated protein kinase 1 Homo sapiens 110-113 22454661-0 2012 Ethanol extracts of fruiting bodies of Antrodia cinnamomea suppress CL1-5 human lung adenocarcinoma cells migration by inhibiting matrix metalloproteinase-2/9 through ERK, JNK, p38, and PI3K/Akt signaling pathways. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 167-170 22454661-0 2012 Ethanol extracts of fruiting bodies of Antrodia cinnamomea suppress CL1-5 human lung adenocarcinoma cells migration by inhibiting matrix metalloproteinase-2/9 through ERK, JNK, p38, and PI3K/Akt signaling pathways. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 177-180 21876711-8 2011 Furthermore, FT ethanol extract activated p38 MAPK and inhibited ERK signaling pathways in K562 cells, as revealed in western blotting analysis. Ethanol 16-23 mitogen-activated protein kinase 1 Homo sapiens 65-68 19351710-3 2011 The aim of this study was to investigate the effects of ethanol extract of Brazilian propolis (EEBP) on two major survival signals, extracellular signal-regulated kinase 1/2 (ERK1/2) and Akt, and to elucidate whether changes in these signals were actually involved in antiangiogenic effects of the propolis. Ethanol 56-63 mitogen-activated protein kinase 1 Homo sapiens 132-173 19127349-4 2009 The loss in countering capacity of leptin on the ethanol-induced cytotoxicity was attained with Src kinase inhibitor, PP2, and EGFR kinase inhibitor, AG1478, as well as ERK inhibitor, PD98059. Ethanol 49-56 mitogen-activated protein kinase 1 Homo sapiens 169-172 21525764-9 2010 RESULTS: Ethanol and TGF-beta rapidly increase ROI and reduce GSH in hHeps, causing apoptosis with a release of approximately 40% total LDH after 72 h. Similar to incubation with hemin preincubation and co-incubation of cells with nifedipine, verapamil and quercetin significantly reduce oxidative stress and resulting cellular damage, in a dose-dependent manner, by initiating nuclear translocation of Nrf2 which in turn induces HO-1 under the control of p38 and ERK. Ethanol 9-16 mitogen-activated protein kinase 1 Homo sapiens 464-467 19321179-8 2009 RESULTS: Ethanol treatment (10-40 mM) increased ERK activation in HepG2 and SKHep HCC cells but not in Hep3B or human hepatocyte cells. Ethanol 9-16 mitogen-activated protein kinase 1 Homo sapiens 48-51 19321179-14 2009 The TGF-a neutralization antibody also prevented ERK activation by ethanol in HepG2 cells. Ethanol 67-74 mitogen-activated protein kinase 1 Homo sapiens 49-52 19321179-15 2009 CONCLUSIONS: These data demonstrate that clinically relevant doses of ethanol stimulate ERK-dependent proliferation of HCC cells. Ethanol 70-77 mitogen-activated protein kinase 1 Homo sapiens 88-91 19321179-16 2009 Ethanol up-regulates TGF-alpha levels in HCC cells and enhances growth through cell cycles changes, which appear to be mediated through TGF-alpha-MEK-ERK signaling. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 150-153 19320634-0 2009 Ethanol-induced extracellular signal regulated kinase: role of dopamine D1 receptors. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 16-53 19320634-2 2009 The aim of this study was to demonstrate the ethanol-induced activation of ERK in the nucleus accumbens (Acb) and in the extended amygdala [bed nucleus of the stria terminalis lateralis (BSTL) and central nucleus of the amygdala (CeA)] and to highlight the role of dopamine (DA) D(1) receptors in these effects. Ethanol 45-52 mitogen-activated protein kinase 1 Homo sapiens 75-78 19320634-5 2009 RESULTS: Quantitative microscopic examination showed that ethanol, dose-dependently increased phospho-ERK immunoreactivity (optical and neuronal densities) in the shell and core of nucleus Acb, BSTL, and CeA. Ethanol 58-65 mitogen-activated protein kinase 1 Homo sapiens 102-105 19320634-7 2009 CONCLUSIONS: The results of this study indicate that ethanol, similar to other addictive drugs, activates ERK in nucleus Acb and extended amygdala via a DA D(1) receptor-mediated mechanism. Ethanol 53-60 mitogen-activated protein kinase 1 Homo sapiens 106-109 19320634-8 2009 Overall, these results suggest that the D(1) receptors/ERK pathway may play a critical role in the motivational properties of ethanol. Ethanol 126-133 mitogen-activated protein kinase 1 Homo sapiens 55-58 19120063-7 2009 BDNF-mediated activation of the ERK cascade was found to be continuously impaired by ethanol. Ethanol 85-92 mitogen-activated protein kinase 1 Homo sapiens 32-35 19120063-13 2009 RKIP, acting as a signaling switch at the merge of the PKC cascade and the Raf/MEK/ERK cascade, was associated with neuronal differentiation and significantly reduced in ethanol treatment. Ethanol 170-177 mitogen-activated protein kinase 1 Homo sapiens 83-86 19120063-16 2009 Thus, reduced RKIP and PKC levels and subsequently reduced positive feedback on ERK activation provide an explanation for the striking effects of long-term ethanol exposure on BDNF signal transduction and neuronal differentiation, respectively. Ethanol 156-163 mitogen-activated protein kinase 1 Homo sapiens 80-83 18622047-8 2008 Our findings demonstrate that leptin protection of gastric mucosa against ethanol cytotoxicity involves Src kinase-mediated bifurcated activation of MAPK/ERK and Akt that leads to up-regulation of the respective prostaglandin and nitric oxide synthase pathways. Ethanol 74-81 mitogen-activated protein kinase 1 Homo sapiens 149-153 18595723-3 2008 To explore lithium"s mechanism of action, we focused on kinase signaling systems (ERK, Akt, JNK) that are believed to play a regulatory role in cell survival, and found that very rapidly after ethanol administration there is a suppression of ERK phosphorylation, and that lithium stimulates ERK phosphorylation and prevents ethanol from suppressing this phosphorylation process. Ethanol 193-200 mitogen-activated protein kinase 1 Homo sapiens 82-85 18595723-3 2008 To explore lithium"s mechanism of action, we focused on kinase signaling systems (ERK, Akt, JNK) that are believed to play a regulatory role in cell survival, and found that very rapidly after ethanol administration there is a suppression of ERK phosphorylation, and that lithium stimulates ERK phosphorylation and prevents ethanol from suppressing this phosphorylation process. Ethanol 193-200 mitogen-activated protein kinase 1 Homo sapiens 242-245 18595723-3 2008 To explore lithium"s mechanism of action, we focused on kinase signaling systems (ERK, Akt, JNK) that are believed to play a regulatory role in cell survival, and found that very rapidly after ethanol administration there is a suppression of ERK phosphorylation, and that lithium stimulates ERK phosphorylation and prevents ethanol from suppressing this phosphorylation process. Ethanol 193-200 mitogen-activated protein kinase 1 Homo sapiens 242-245 18595723-3 2008 To explore lithium"s mechanism of action, we focused on kinase signaling systems (ERK, Akt, JNK) that are believed to play a regulatory role in cell survival, and found that very rapidly after ethanol administration there is a suppression of ERK phosphorylation, and that lithium stimulates ERK phosphorylation and prevents ethanol from suppressing this phosphorylation process. Ethanol 324-331 mitogen-activated protein kinase 1 Homo sapiens 242-245 18595723-3 2008 To explore lithium"s mechanism of action, we focused on kinase signaling systems (ERK, Akt, JNK) that are believed to play a regulatory role in cell survival, and found that very rapidly after ethanol administration there is a suppression of ERK phosphorylation, and that lithium stimulates ERK phosphorylation and prevents ethanol from suppressing this phosphorylation process. Ethanol 324-331 mitogen-activated protein kinase 1 Homo sapiens 242-245 18622047-8 2008 Our findings demonstrate that leptin protection of gastric mucosa against ethanol cytotoxicity involves Src kinase-mediated bifurcated activation of MAPK/ERK and Akt that leads to up-regulation of the respective prostaglandin and nitric oxide synthase pathways. Ethanol 74-81 mitogen-activated protein kinase 1 Homo sapiens 154-157 18263590-11 2008 Hydrogen peroxide and ethanol enhanced FGF2-stimulated pGSK3beta(Tyr-216), ERK/pGSK3beta(Tyr-216) association, and cytoplasmic retention of pERK1/2. Ethanol 22-29 mitogen-activated protein kinase 1 Homo sapiens 75-78 18340408-9 2008 Our findings demonstrate that leptin protection of salivary gland acinar cells against ethanol cytotoxicity involves Src kinase-mediated parallel activation of MAPK/ERK and Akt that result in up-regulation of the respective prostaglandin and nitric oxide synthase pathways. Ethanol 87-94 mitogen-activated protein kinase 1 Homo sapiens 160-164 18340408-9 2008 Our findings demonstrate that leptin protection of salivary gland acinar cells against ethanol cytotoxicity involves Src kinase-mediated parallel activation of MAPK/ERK and Akt that result in up-regulation of the respective prostaglandin and nitric oxide synthase pathways. Ethanol 87-94 mitogen-activated protein kinase 1 Homo sapiens 165-168 18040815-3 2006 Results from these studies suggest that EtOH intoxication prior to burn injury augments corticosterone release, which in turn suppresses intestinal T cell function by inhibiting mitogen-activated protein kinase (i.e., p38 and ERK) pathway. Ethanol 40-44 mitogen-activated protein kinase 1 Homo sapiens 226-229 16938627-4 2006 These experiments were undertaken to determine the interactions between membrane depolarization, BDNF concentration, and ethanol concentration on extracellular signal-regulated protein kinase (ERK) activation in neurons. Ethanol 121-128 mitogen-activated protein kinase 1 Homo sapiens 146-191 16938627-4 2006 These experiments were undertaken to determine the interactions between membrane depolarization, BDNF concentration, and ethanol concentration on extracellular signal-regulated protein kinase (ERK) activation in neurons. Ethanol 121-128 mitogen-activated protein kinase 1 Homo sapiens 193-196 16938627-7 2006 Ethanol decreased basal pERK and reduced the magnitude of BDNF stimulation of ERK under both conditions. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 25-28 16938627-9 2006 These data characterize the pharmacological effects of ethanol on growth factor signaling and provide the basis of a model for further characterization of the biochemical mechanisms of ERK inhibition by ethanol. Ethanol 203-210 mitogen-activated protein kinase 1 Homo sapiens 185-188 12383974-0 2002 ERK regulation in chronic ethanol exposure and withdrawal. Ethanol 26-33 mitogen-activated protein kinase 1 Homo sapiens 0-3 16324217-2 2005 High physiological concentrations of acute ethanol activated the Jak-Stat and p38 MAPK pathways and inhibited HCV replication in several independent replicon cell lines. Ethanol 43-50 mitogen-activated protein kinase 1 Homo sapiens 78-81 16324217-3 2005 Moreover, acute ethanol induced Stat1 serine phosphorylation, which was partially mediated by the p38 MAPK pathway. Ethanol 16-23 mitogen-activated protein kinase 1 Homo sapiens 98-101 16272348-6 2005 We show in this study that ethanol, at physiologically relevant concentrations, is capable of inducing rapid phosphorylation within 10 min of IL-1R-associated kinase, ERK1/2, stress-activated protein kinase/JNK, and p38 MAPK in astrocytes. Ethanol 27-34 mitogen-activated protein kinase 1 Homo sapiens 216-219 15189113-5 2004 In response to ethanol exposure, specific signal transduction pathways, including NFkappaB and the mitogen-activated protein kinase family members ERK1/2, JNK, and p38, are activated. Ethanol 15-22 mitogen-activated protein kinase 1 Homo sapiens 164-167 14713309-6 2003 Furthermore, we show that ethanol-induced ERK activation triggers the stimulation of cyclo-oxygenase-2 (COX-2) and the release of prostaglandin E2, and that blockade of the mitogen-activated protein kinase kinase (MEK)/ERK pathway by PD98059 abolishes the up-regulation of COX-2 induced by ethanol plus ceramide, and decreases the ethanol-induced apoptosis. Ethanol 26-33 mitogen-activated protein kinase 1 Homo sapiens 219-222 14713309-6 2003 Furthermore, we show that ethanol-induced ERK activation triggers the stimulation of cyclo-oxygenase-2 (COX-2) and the release of prostaglandin E2, and that blockade of the mitogen-activated protein kinase kinase (MEK)/ERK pathway by PD98059 abolishes the up-regulation of COX-2 induced by ethanol plus ceramide, and decreases the ethanol-induced apoptosis. Ethanol 290-297 mitogen-activated protein kinase 1 Homo sapiens 42-45 14713309-6 2003 Furthermore, we show that ethanol-induced ERK activation triggers the stimulation of cyclo-oxygenase-2 (COX-2) and the release of prostaglandin E2, and that blockade of the mitogen-activated protein kinase kinase (MEK)/ERK pathway by PD98059 abolishes the up-regulation of COX-2 induced by ethanol plus ceramide, and decreases the ethanol-induced apoptosis. Ethanol 290-297 mitogen-activated protein kinase 1 Homo sapiens 219-222 14713309-6 2003 Furthermore, we show that ethanol-induced ERK activation triggers the stimulation of cyclo-oxygenase-2 (COX-2) and the release of prostaglandin E2, and that blockade of the mitogen-activated protein kinase kinase (MEK)/ERK pathway by PD98059 abolishes the up-regulation of COX-2 induced by ethanol plus ceramide, and decreases the ethanol-induced apoptosis. Ethanol 290-297 mitogen-activated protein kinase 1 Homo sapiens 42-45 14713309-6 2003 Furthermore, we show that ethanol-induced ERK activation triggers the stimulation of cyclo-oxygenase-2 (COX-2) and the release of prostaglandin E2, and that blockade of the mitogen-activated protein kinase kinase (MEK)/ERK pathway by PD98059 abolishes the up-regulation of COX-2 induced by ethanol plus ceramide, and decreases the ethanol-induced apoptosis. Ethanol 290-297 mitogen-activated protein kinase 1 Homo sapiens 219-222 14512869-8 2003 In conclusion, these results suggest that HCV core protein cooperates with ethanol for the activation of some MAPK pathways, and leads to the modulation of several genes, contributing to the pathogenesis of liver disease of HCV-infected patients with high ethanol consumption. Ethanol 75-82 mitogen-activated protein kinase 1 Homo sapiens 110-114 12223228-4 2002 However, the picrotoxin-induced phosphorylation of ERK was inhibited by ethanol, but was not affected by MK-801. Ethanol 72-79 mitogen-activated protein kinase 1 Homo sapiens 51-54 12223228-5 2002 These results indicate that ethanol"s inhibitory effect on ERK phosphorylation may involve the modulation of GABA(A) receptor function. Ethanol 28-35 mitogen-activated protein kinase 1 Homo sapiens 59-62 14634061-0 2004 Acute ethanol exposure inhibits macrophage IL-6 production: role of p38 and ERK1/2 MAPK. Ethanol 6-13 mitogen-activated protein kinase 1 Homo sapiens 68-71 14634061-5 2004 We demonstrated that a single dose of ethanol transiently down-regulated p38 and ERK1/2 activation levels (3-24 h after treatment) and impaired IL-6 synthesis. Ethanol 38-45 mitogen-activated protein kinase 1 Homo sapiens 73-76 14634061-7 2004 These results demonstrate that acute ethanol exposure can impair macrophage IL-6 production and indicate that this effect may result from ethanol-induced alterations in intracellular signaling through p38 and ERK1/2. Ethanol 37-44 mitogen-activated protein kinase 1 Homo sapiens 201-204 14634061-7 2004 These results demonstrate that acute ethanol exposure can impair macrophage IL-6 production and indicate that this effect may result from ethanol-induced alterations in intracellular signaling through p38 and ERK1/2. Ethanol 138-145 mitogen-activated protein kinase 1 Homo sapiens 201-204 14713309-4 2003 Cell death induced by ethanol is associated with stimulation of neutral and acidic sphingomyelinase (SMase) and ceramide generation, as well as with activation of stress-related kinases, c-Jun N-terminal kinase (JNK), p38 mitogen-activated protein kinase (p38) and extracellular signal-regulated kinase (ERK) pathways. Ethanol 22-29 mitogen-activated protein kinase 1 Homo sapiens 265-302 14713309-4 2003 Cell death induced by ethanol is associated with stimulation of neutral and acidic sphingomyelinase (SMase) and ceramide generation, as well as with activation of stress-related kinases, c-Jun N-terminal kinase (JNK), p38 mitogen-activated protein kinase (p38) and extracellular signal-regulated kinase (ERK) pathways. Ethanol 22-29 mitogen-activated protein kinase 1 Homo sapiens 304-307 14713309-6 2003 Furthermore, we show that ethanol-induced ERK activation triggers the stimulation of cyclo-oxygenase-2 (COX-2) and the release of prostaglandin E2, and that blockade of the mitogen-activated protein kinase kinase (MEK)/ERK pathway by PD98059 abolishes the up-regulation of COX-2 induced by ethanol plus ceramide, and decreases the ethanol-induced apoptosis. Ethanol 26-33 mitogen-activated protein kinase 1 Homo sapiens 42-45 12968059-7 2003 Recent studies have identified specific modules in the TLR-4 signaling cascade that are disrupted after chronic ethanol exposure, including CD14 and the mitogen-activated protein kinase family members, ERK1/2 and p38. Ethanol 112-119 mitogen-activated protein kinase 1 Homo sapiens 213-216 12716028-0 2003 Regulation of ERK phosphorylation by ethanol in fetal cortical neurons. Ethanol 37-44 mitogen-activated protein kinase 1 Homo sapiens 14-17 12223228-1 2002 In the present study, we demonstrate the involvement of GABA(A) receptors in the ethanol-mediated modulation of extracellular signal-regulated kinases (ERK). Ethanol 81-88 mitogen-activated protein kinase 1 Homo sapiens 112-150 12223228-1 2002 In the present study, we demonstrate the involvement of GABA(A) receptors in the ethanol-mediated modulation of extracellular signal-regulated kinases (ERK). Ethanol 81-88 mitogen-activated protein kinase 1 Homo sapiens 152-155 12383974-3 2002 Therefore, we investigated the regulation of the ERK signal transduction pathway in models of continuous and intermittent ethanol exposure and withdrawal. Ethanol 122-129 mitogen-activated protein kinase 1 Homo sapiens 49-52 12383974-7 2002 In the amygdala and the cerebellum, the activation of ERK observed during withdrawal was significantly higher after intermittent ethanol exposure than after continuous exposure, suggesting the establishment of a form of sensitization to the effects of withdrawal on ERK regulation. Ethanol 129-136 mitogen-activated protein kinase 1 Homo sapiens 54-57 12383974-7 2002 In the amygdala and the cerebellum, the activation of ERK observed during withdrawal was significantly higher after intermittent ethanol exposure than after continuous exposure, suggesting the establishment of a form of sensitization to the effects of withdrawal on ERK regulation. Ethanol 129-136 mitogen-activated protein kinase 1 Homo sapiens 266-269 10588932-3 1999 Although ethanol has been shown to modulate ERK1 and ERK2 (p44(mapk) and p42(mapk)) activity, it can also act as an antiproliferative agent in various mammalian cells. Ethanol 9-16 mitogen-activated protein kinase 1 Homo sapiens 53-57 10349837-9 1999 Ethanol also produced prolonged activation of ERK, an effect that was partially eliminated by treatment with PD98059. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 46-49 9884156-5 1998 The results demonstrated that ethanol treatment (100 mM) caused 30 to 50% reductions in the levels of insulin-stimulated tyrosyl phosphorylation of the insulin receptor beta-subunit, tyrosyl phosphorylation of IRS-1, phosphorylation of Erk2, association of phosphatidylinositol-3 kinase with tyrosyl-phosphorylated IRS-1, and MAP kinase and phosphatidylinositol-3 kinase activities. Ethanol 30-37 mitogen-activated protein kinase 1 Homo sapiens 236-240 9727648-2 1998 Current evidence supports the hypothesis that ETOH inhibits the phospholipase D-tyrosine kinase pathway involved in the phosphorylation and activation of NADPH oxidase and myeloperoxidase, which upregulates the formation of reactive oxygen intermediates and mitogen-activated protein kinase cascade, including the extracellular receptor-linked kinase 1 and 2 (erk1 and erk2). Ethanol 46-50 mitogen-activated protein kinase 1 Homo sapiens 369-373 9705842-5 1998 Incubation for 5 minutes with 2.5% ethanol resulted in increased activities of PKC and MAP kinase (ERK2) by 1.6-fold (p < 0.05) and 2.3-fold (P < 0.001), respectively. Ethanol 35-42 mitogen-activated protein kinase 1 Homo sapiens 99-103 32833955-12 2020 Moreover, the H2O2-induced downregulation of E-cadherin expression, increased ROS generation, and ERK activation in 16HBE cells were restored by treatment with QXT water or ethanol extract. Ethanol 173-180 mitogen-activated protein kinase 1 Homo sapiens 98-101 34685467-9 2021 Furthermore, ethanol treatment was associated with a significant decrease in ERK and AKT phosphorylation during the acute injury phase. Ethanol 13-20 mitogen-activated protein kinase 1 Homo sapiens 77-80 26949123-10 2017 Collectively, these findings indicate that chronic EtOH increases degradation of tight junctions and extracellular matrix in postmortem human brain and induces a neuroinflammatory response associated with activation of ERK1/2 and p-38 and greater MMP-9 activity. Ethanol 51-55 mitogen-activated protein kinase 1 Homo sapiens 230-234 31572456-10 2019 Conclusions: Bioinformatics analysis showed that differentially expressed lncRNAs were involved in regulating the ERK1 and ERK2 cascade, secondary alcohol biosynthetic process, centrosome duplication and DNA repair. Ethanol 147-154 mitogen-activated protein kinase 1 Homo sapiens 123-127 30568656-5 2018 U0126-EtOH was used to inhibit the MAPK/ERK signaling pathway. Ethanol 6-10 mitogen-activated protein kinase 1 Homo sapiens 40-43 30106096-9 2018 The results of the present study demonstrated that treatment with ethanol inhibited GES-1 cell proliferation, and enhanced ROS levels and apoptosis rates, potentially via downregulation of B-cell lymphoma-2 (Bcl-2) expression and upregulation of Bcl-2-associated X and caspase-3 expression levels, as well as enhancing the phosphorylation levels of ERK, JNK and p38. Ethanol 66-73 mitogen-activated protein kinase 1 Homo sapiens 349-352 25189124-8 2014 Moreover, signal transduction studies showed that COS was able to suppress the ethanol-induced phosphorylation of p38 MAPK, JNK and ERK. Ethanol 79-86 mitogen-activated protein kinase 1 Homo sapiens 118-122 25189124-8 2014 Moreover, signal transduction studies showed that COS was able to suppress the ethanol-induced phosphorylation of p38 MAPK, JNK and ERK. Ethanol 79-86 mitogen-activated protein kinase 1 Homo sapiens 132-135 28293388-0 2017 Protective role of licochalcone B against ethanol-induced hepatotoxicity through regulation of Erk signaling. Ethanol 42-49 mitogen-activated protein kinase 1 Homo sapiens 95-98 27847436-13 2016 In summary, these results suggest that p90rsk, a downstream kinase of ERK, plays a stimulatory role on ethanol-induced hepatocellular carcinoma progression by activating anti-apoptotic factor Bcl-2 and NHE1 known to regulate cell survival. Ethanol 103-110 mitogen-activated protein kinase 1 Homo sapiens 70-73 25393427-0 2014 Ethanol negatively regulates hepatic differentiation of hESC by inhibition of the MAPK/ERK signaling pathway in vitro. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 82-86 25393427-0 2014 Ethanol negatively regulates hepatic differentiation of hESC by inhibition of the MAPK/ERK signaling pathway in vitro. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 87-90 25393427-7 2014 Ethanol treatment specifically inhibited the activation of the ERK but not JNK nor the p38 MAP signaling pathway. Ethanol 0-7 mitogen-activated protein kinase 1 Homo sapiens 63-66 25393427-9 2014 Upon evaluating the effects of the inhibitors of these two signaling pathways, we determined that the Erk inhibitor replicated the effects of ethanol on the hepatocyte differentiation and attenuated the WNT/beta-catenin signaling, however, inhibitors of WNT only partially replicated the effects of ethanol on the hepatocyte differentiation. Ethanol 142-149 mitogen-activated protein kinase 1 Homo sapiens 102-105 25393427-9 2014 Upon evaluating the effects of the inhibitors of these two signaling pathways, we determined that the Erk inhibitor replicated the effects of ethanol on the hepatocyte differentiation and attenuated the WNT/beta-catenin signaling, however, inhibitors of WNT only partially replicated the effects of ethanol on the hepatocyte differentiation. Ethanol 299-306 mitogen-activated protein kinase 1 Homo sapiens 102-105 25393427-10 2014 CONCLUSION: Our results demonstrated that ethanol negatively regulated hepatic differentiation of hESC-derived hepatic progenitors through inhibiting the MAPK/ERK signaling pathway, and subsequently attenuating the WNT signaling pathway. Ethanol 42-49 mitogen-activated protein kinase 1 Homo sapiens 154-158 25393427-10 2014 CONCLUSION: Our results demonstrated that ethanol negatively regulated hepatic differentiation of hESC-derived hepatic progenitors through inhibiting the MAPK/ERK signaling pathway, and subsequently attenuating the WNT signaling pathway. Ethanol 42-49 mitogen-activated protein kinase 1 Homo sapiens 159-162 25189124-0 2014 Chitooligosaccharides inhibit ethanol-induced oxidative stress via activation of Nrf2 and reduction of MAPK phosphorylation. Ethanol 30-37 mitogen-activated protein kinase 1 Homo sapiens 103-107