PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34020277-7 2021 Molecular docking simulations using the ERK-ulixertinib crystallographic complex showed compound 25a could potentially compete with ATP for binding to ERK in a slightly higher affinity than the reference ERK1/2 inhibitor. Adenosine Triphosphate 132-135 mitogen-activated protein kinase 1 Homo sapiens 40-43 34020277-7 2021 Molecular docking simulations using the ERK-ulixertinib crystallographic complex showed compound 25a could potentially compete with ATP for binding to ERK in a slightly higher affinity than the reference ERK1/2 inhibitor. Adenosine Triphosphate 132-135 mitogen-activated protein kinase 1 Homo sapiens 151-154 29259132-9 2018 Furthermore, mass spectrometry analysis indicated Lys-72 as an acetylation site in the ERK1 N terminus, adjacent to Lys-71, which binds to ATP, suggesting that acetylation status of Lys-72 may affect ERK1 ATP binding. Adenosine Triphosphate 139-142 mitogen-activated protein kinase 1 Homo sapiens 87-91 33655414-11 2021 Moreover, ATP supplementation completely reversed linalool-induced ERK phosphorylation. Adenosine Triphosphate 10-13 mitogen-activated protein kinase 1 Homo sapiens 67-70 31965713-7 2020 In addition, TMS could activate ERK/Nrf2/HO-1 signaling which increased the expression of ATP-binding cassette transporters. Adenosine Triphosphate 90-93 mitogen-activated protein kinase 1 Homo sapiens 32-35 31745079-1 2019 Recently, the targeting of ERK with ATP-competitive inhibitors has emerged as a potential clinical strategy to overcome acquired resistance to BRAF and MEK inhibitor combination therapies. Adenosine Triphosphate 36-39 mitogen-activated protein kinase 1 Homo sapiens 27-30 31311868-3 2019 An X-ray structure of active 2P-ERK2 complexed with AMP-PNP reveals a shift in the Gly-rich loop along with domain closure to position the nucleotide in a more catalytically productive conformation relative to inactive 0P-ERK2:ATP. Adenosine Triphosphate 227-230 mitogen-activated protein kinase 1 Homo sapiens 32-36 30396063-8 2019 Kinetic mechanism studies revealed that the inhibitors are ATP-competitive inhibitors where 6 inhibited ERK2 with a Ki of 0.09 microM. Adenosine Triphosphate 59-62 mitogen-activated protein kinase 1 Homo sapiens 104-108 30396063-14 2019 Finally, a molecular docking study showed the potential binding mode of 3b and 6 within the ATP catalytic binding site of ERK2. Adenosine Triphosphate 92-95 mitogen-activated protein kinase 1 Homo sapiens 122-126 32545311-4 2020 Proliferation is upregulated through two mechanisms: (1) ATP binding to the G-protein-coupled receptor P2Y2, commencing a kinase signaling cascade that activates the serine-threonine kinase Akt, and (2) the transactivation of the epidermal growth factor receptor (EGFR), leading to a series of protein signals that activate the extracellular signal-regulated kinases (ERK) 1/2. Adenosine Triphosphate 57-60 mitogen-activated protein kinase 1 Homo sapiens 328-376 31744895-7 2020 Here, we report identification and activity of LY3214996, a potent, selective, ATP-competitive ERK inhibitor. Adenosine Triphosphate 79-82 mitogen-activated protein kinase 1 Homo sapiens 95-98 31022583-6 2019 Molecular modeling simulations suggested the potential of MMA-102 and MMA-132 to compete with ATP within the catalytic binding domains of EGFR and MAPK pathway. Adenosine Triphosphate 94-97 mitogen-activated protein kinase 1 Homo sapiens 147-151 31058487-4 2019 Targeting these sites on ERK in a therapeutic context may overcome many problems associated with traditional ATP-competitive inhibitors. Adenosine Triphosphate 109-112 mitogen-activated protein kinase 1 Homo sapiens 25-28 31058487-12 2019 The structural and biochemical insights reported here provide the basis for developing new ERK inhibitors that are not ATP-competitive but instead function by disrupting critical protein-protein interactions. Adenosine Triphosphate 119-122 mitogen-activated protein kinase 1 Homo sapiens 91-94 30268050-7 2018 To further elucidate the mechanism of action of these newly synthesized compounds, compounds 3a, 3b, 4e and 4f were selected to investigate for their MAP Kinases pathway inhibition together with molecular docking using ATP-binding site of ERK2. Adenosine Triphosphate 219-222 mitogen-activated protein kinase 1 Homo sapiens 239-243 30268050-9 2018 Also, compound 4f showed highest potency for ERK2 inhibition with ATP-competitive inhibition mechanism which was confirmed by the formation of three hydrogen bond in the molecular docking studies. Adenosine Triphosphate 66-69 mitogen-activated protein kinase 1 Homo sapiens 45-49 30019396-3 2018 NIR-triggered release of PP2A specially dephosphorylates and inactivates mitogen-activated protein kinase kinase (MAP2K, also known as MEK) and extracellular regulated protein kinases (ERK) in the MAPK pathway, meanwhile, the NIR-triggered activation of NC decreases the level of intracellular adenosine triphosphate to attenuate protein phosphorylation of MEK and ERK. Adenosine Triphosphate 294-316 mitogen-activated protein kinase 1 Homo sapiens 144-183 30019396-3 2018 NIR-triggered release of PP2A specially dephosphorylates and inactivates mitogen-activated protein kinase kinase (MAP2K, also known as MEK) and extracellular regulated protein kinases (ERK) in the MAPK pathway, meanwhile, the NIR-triggered activation of NC decreases the level of intracellular adenosine triphosphate to attenuate protein phosphorylation of MEK and ERK. Adenosine Triphosphate 294-316 mitogen-activated protein kinase 1 Homo sapiens 185-188 30019396-3 2018 NIR-triggered release of PP2A specially dephosphorylates and inactivates mitogen-activated protein kinase kinase (MAP2K, also known as MEK) and extracellular regulated protein kinases (ERK) in the MAPK pathway, meanwhile, the NIR-triggered activation of NC decreases the level of intracellular adenosine triphosphate to attenuate protein phosphorylation of MEK and ERK. Adenosine Triphosphate 294-316 mitogen-activated protein kinase 1 Homo sapiens 365-368 29760222-6 2018 Here, we aimed to model the mechanism of resistance to ERK inhibitors.Experimental Design: We tested five structurally different ATP-competitive ERK inhibitors representing three different scaffolds on BRAF/RAS-mutant cancer cell lines of different tissue types to generate resistant lines. Adenosine Triphosphate 129-132 mitogen-activated protein kinase 1 Homo sapiens 55-58 29760222-6 2018 Here, we aimed to model the mechanism of resistance to ERK inhibitors.Experimental Design: We tested five structurally different ATP-competitive ERK inhibitors representing three different scaffolds on BRAF/RAS-mutant cancer cell lines of different tissue types to generate resistant lines. Adenosine Triphosphate 129-132 mitogen-activated protein kinase 1 Homo sapiens 145-148 29510947-2 2018 Herein a combination of 19F NMR and SPR was used to find novel binders to the ATP-binding pocket of MAP kinase extracellular regulated kinase 2 (ERK2) by fragment screening with an original fluorinated-fragment library. Adenosine Triphosphate 78-81 mitogen-activated protein kinase 1 Homo sapiens 145-149 29510947-3 2018 The 19F NMR screening yielded a high primary hit rate of binders to the ERK2 ATP-binding pocket compared with the rate for the SPR screening. Adenosine Triphosphate 77-80 mitogen-activated protein kinase 1 Homo sapiens 72-76 29259132-9 2018 Furthermore, mass spectrometry analysis indicated Lys-72 as an acetylation site in the ERK1 N terminus, adjacent to Lys-71, which binds to ATP, suggesting that acetylation status of Lys-72 may affect ERK1 ATP binding. Adenosine Triphosphate 139-142 mitogen-activated protein kinase 1 Homo sapiens 200-204 29259132-9 2018 Furthermore, mass spectrometry analysis indicated Lys-72 as an acetylation site in the ERK1 N terminus, adjacent to Lys-71, which binds to ATP, suggesting that acetylation status of Lys-72 may affect ERK1 ATP binding. Adenosine Triphosphate 205-208 mitogen-activated protein kinase 1 Homo sapiens 87-91 29259132-9 2018 Furthermore, mass spectrometry analysis indicated Lys-72 as an acetylation site in the ERK1 N terminus, adjacent to Lys-71, which binds to ATP, suggesting that acetylation status of Lys-72 may affect ERK1 ATP binding. Adenosine Triphosphate 205-208 mitogen-activated protein kinase 1 Homo sapiens 200-204 28740606-5 2017 Here, we report the design and structural/functional characterization of a set of bivalent ERK inhibitors that combine a small molecule inhibitor that binds to the ATP-binding pocket with a peptide that selectively binds to an ERK protein interaction surface, the D-site recruitment site (DRS). Adenosine Triphosphate 164-167 mitogen-activated protein kinase 1 Homo sapiens 91-94 28030988-3 2018 Binding free energy predictions indicate that Mg2+ binding produces an important effect on binding ability of adenosine triphosphate (ATP) to ERK2 and strengthens the ATP binding. Adenosine Triphosphate 110-132 mitogen-activated protein kinase 1 Homo sapiens 142-146 28030988-3 2018 Binding free energy predictions indicate that Mg2+ binding produces an important effect on binding ability of adenosine triphosphate (ATP) to ERK2 and strengthens the ATP binding. Adenosine Triphosphate 134-137 mitogen-activated protein kinase 1 Homo sapiens 142-146 27633746-0 2016 Enrichment of Metabolite-Binding Proteins by Affinity Elution in Tandem Hydrophobic Interaction Chromatography (AETHIC) Reveals RKIP Regulating ERK Signaling in an ATP-Dependent Manner. Adenosine Triphosphate 164-167 mitogen-activated protein kinase 1 Homo sapiens 144-147 26961545-7 2017 The presence of ATP during TLR4 activation leads to NLRP3 inflammasome activation and caspase-1-mediated IL-1beta secretion which was inhibited during CD40 activation, accompanied with inhibition of ERK1/2 and reactive oxygen species (ROS), and elevation in p38 MAPK phosphorylation. Adenosine Triphosphate 16-19 mitogen-activated protein kinase 1 Homo sapiens 258-261 28024406-2 2016 Conformational flexibility of the ATP-binding site in the CDK2 and ERK2 kinases was identified using molecular dynamics simulations. Adenosine Triphosphate 34-37 mitogen-activated protein kinase 1 Homo sapiens 67-71 27905300-6 2016 We found that uniaxial stretch raised the ATP concentration in the culture medium and that inhibition of ATP signaling by apyrase or suramin suppressed the stretch-induced ERK activation in TRT-HU1 cells. Adenosine Triphosphate 105-108 mitogen-activated protein kinase 1 Homo sapiens 172-175 27633746-9 2016 In parallel, short-term ATP depletion in cultured HEK293 cells augments interaction between RKIP and Raf-1, resulting in decreased activation of the downstream ERK signaling. Adenosine Triphosphate 24-27 mitogen-activated protein kinase 1 Homo sapiens 160-163 26305625-9 2015 The results showed that the RasGAP protein could be further cleaved, leading to the activation of the Ras/Raf/MEK (mitogen/extracellular signal-regulated kinase)/ERK pathway and that CVB3 infection could result in an increase in the concentration of calcium in the cytoplasm, resulting in mitochondrial damage, a decrease in the concentration of ATP and activation of the AMPK (AMP-activated protein kinase)/MEK/ERK pathway. Adenosine Triphosphate 346-349 mitogen-activated protein kinase 1 Homo sapiens 162-165 25183652-5 2015 In this study, we demonstrated that adenosine triphosphate (ATP) restrained serum deprivation-induced cell death in hMSC by preventing caspases 3/7 activation and modulating ERK1/2 and p38 MAPK signaling pathways. Adenosine Triphosphate 36-58 mitogen-activated protein kinase 1 Homo sapiens 185-188 25884645-3 2015 As activation of the Raf/MEK/ERK signaling pathway was also found in the CD26(+) CSCs and therefore, we hypothesized that an ATP-competitive pan-Raf inhibitor, Raf265, is effective in eliminating the cancer cells and the CD26(+) CSCs in CRC patients. Adenosine Triphosphate 125-128 mitogen-activated protein kinase 1 Homo sapiens 29-32 25485998-6 2015 Moreover, exogenous factors, such as ATP, retinoic acid, substance P, thioredoxin, inosine and laminin, can have cytoprotective effects against hyperoxia-induced cell damage, through promotion of ERK activation and/or limiting JNK and p38 involvement. Adenosine Triphosphate 37-40 mitogen-activated protein kinase 1 Homo sapiens 196-199 25485998-6 2015 Moreover, exogenous factors, such as ATP, retinoic acid, substance P, thioredoxin, inosine and laminin, can have cytoprotective effects against hyperoxia-induced cell damage, through promotion of ERK activation and/or limiting JNK and p38 involvement. Adenosine Triphosphate 37-40 mitogen-activated protein kinase 1 Homo sapiens 235-238 25183652-5 2015 In this study, we demonstrated that adenosine triphosphate (ATP) restrained serum deprivation-induced cell death in hMSC by preventing caspases 3/7 activation and modulating ERK1/2 and p38 MAPK signaling pathways. Adenosine Triphosphate 60-63 mitogen-activated protein kinase 1 Homo sapiens 185-188 25118288-0 2014 Shock wave treatment enhances cell proliferation and improves wound healing by ATP release-coupled extracellular signal-regulated kinase (ERK) activation. Adenosine Triphosphate 79-82 mitogen-activated protein kinase 1 Homo sapiens 99-136 23798356-6 2014 RESULTS: Gravity loading and ATP increased ERK phosphorylation by 5 and 2.5 times, respectively. Adenosine Triphosphate 29-32 mitogen-activated protein kinase 1 Homo sapiens 43-46 23798356-8 2014 Apyrase and suramin diminished ERK phosphorylation induced by both gravity loading and ATP. Adenosine Triphosphate 87-90 mitogen-activated protein kinase 1 Homo sapiens 31-34 25118288-0 2014 Shock wave treatment enhances cell proliferation and improves wound healing by ATP release-coupled extracellular signal-regulated kinase (ERK) activation. Adenosine Triphosphate 79-82 mitogen-activated protein kinase 1 Homo sapiens 138-141 23935097-5 2013 Remarkably, this compound binds to the ATP-binding pocket of ERK in an entirely different conformation to that of IGF-1R/IR, explaining the potency against these two structurally distinct kinase families. Adenosine Triphosphate 39-42 mitogen-activated protein kinase 1 Homo sapiens 61-64 24856138-1 2014 In this issue of Chemistry & Biology, Hari and colleagues show that conformation-selective ATP-competitive kinase inhibitors have distinct noncatalytic effects on Erk2, including the ability to modulate protein-protein interactions outside the ATP-binding site. Adenosine Triphosphate 95-98 mitogen-activated protein kinase 1 Homo sapiens 167-171 24856138-1 2014 In this issue of Chemistry & Biology, Hari and colleagues show that conformation-selective ATP-competitive kinase inhibitors have distinct noncatalytic effects on Erk2, including the ability to modulate protein-protein interactions outside the ATP-binding site. Adenosine Triphosphate 248-251 mitogen-activated protein kinase 1 Homo sapiens 167-171 24704509-3 2014 Here, we show that stabilizing alternative ATP-binding site conformations of the mitogen-activated protein kinases (MAPKs) p38alpha and Erk2 with ATP-competitive inhibitors differentially, and in some cases divergently, modulates the abilities of these kinases to interact with upstream activators and deactivating phosphatases. Adenosine Triphosphate 43-46 mitogen-activated protein kinase 1 Homo sapiens 136-140 24704509-3 2014 Here, we show that stabilizing alternative ATP-binding site conformations of the mitogen-activated protein kinases (MAPKs) p38alpha and Erk2 with ATP-competitive inhibitors differentially, and in some cases divergently, modulates the abilities of these kinases to interact with upstream activators and deactivating phosphatases. Adenosine Triphosphate 146-149 mitogen-activated protein kinase 1 Homo sapiens 136-140 24704509-4 2014 Conformation-selective ligands are also able to modulate Erk2"s ability to allosterically activate the MAPK phosphatase DUSP6, highlighting how ATP-competitive ligands can control noncatalytic kinase functions. Adenosine Triphosphate 144-147 mitogen-activated protein kinase 1 Homo sapiens 57-61 24704509-4 2014 Conformation-selective ligands are also able to modulate Erk2"s ability to allosterically activate the MAPK phosphatase DUSP6, highlighting how ATP-competitive ligands can control noncatalytic kinase functions. Adenosine Triphosphate 144-147 mitogen-activated protein kinase 1 Homo sapiens 103-107 24031026-2 2014 In this study, we found that magnolin, a compound found in the Magnolia species, directly targeted and inhibited ERK1 and ERK2 kinase activities with IC50 values of 87 and 16.5 nM by competing with adenosine triphosphate in an active pocket. Adenosine Triphosphate 198-220 mitogen-activated protein kinase 1 Homo sapiens 122-126 23647195-9 2013 These observations indicate that ROS/PKC-alpha, Src/Raf/ERK signaling and cPLA2 are active participants in diethylmaleate/iodoacetate-induced astrocyte death and contribute to a vicious cycle between the depletion of ATP/glutathione and the mobilization of chelatable zinc as critical upstream effectors in initiating cytotoxic cascades. Adenosine Triphosphate 217-220 mitogen-activated protein kinase 1 Homo sapiens 56-59 22982122-6 2012 Docking experiments have shown that the active molecules interact and bind well in the ATP binding pocket of ERK protein. Adenosine Triphosphate 87-90 mitogen-activated protein kinase 1 Homo sapiens 109-112 23685672-3 2013 Unexpectedly, several ATP-competitive RAF inhibitors were recently found to promote dimerization and transactivation of RAF kinases in a RAS-dependent manner and, as a result, undesirably stimulate RAS/ERK pathway-mediated cell growth. Adenosine Triphosphate 22-25 mitogen-activated protein kinase 1 Homo sapiens 202-205 23410953-7 2013 In characterizing JD123 further, we noted its ATP-competitive inhibition of the related p38-gamma MAPK, but not ERK1, ERK2, or p38-alpha, p38-beta or p38-delta. Adenosine Triphosphate 46-49 mitogen-activated protein kinase 1 Homo sapiens 88-91 23192020-0 2012 Structure of extracellular signal-regulated kinase 2 in complex with ATP and ADP. Adenosine Triphosphate 69-72 mitogen-activated protein kinase 1 Homo sapiens 13-52 23192020-4 2012 The detailed structural analysis of ERK complexed with ATP can provide valuable information for the design of new ligands that can bind in the ATP-binding pocket and inhibit ERK activity. Adenosine Triphosphate 55-58 mitogen-activated protein kinase 1 Homo sapiens 36-39 23192020-4 2012 The detailed structural analysis of ERK complexed with ATP can provide valuable information for the design of new ligands that can bind in the ATP-binding pocket and inhibit ERK activity. Adenosine Triphosphate 55-58 mitogen-activated protein kinase 1 Homo sapiens 174-177 23192020-4 2012 The detailed structural analysis of ERK complexed with ATP can provide valuable information for the design of new ligands that can bind in the ATP-binding pocket and inhibit ERK activity. Adenosine Triphosphate 143-146 mitogen-activated protein kinase 1 Homo sapiens 36-39 23192020-4 2012 The detailed structural analysis of ERK complexed with ATP can provide valuable information for the design of new ligands that can bind in the ATP-binding pocket and inhibit ERK activity. Adenosine Triphosphate 143-146 mitogen-activated protein kinase 1 Homo sapiens 174-177 23192020-5 2012 In this study, the structures of apo-form ERK2 and of its complexes with the substrate ATP and the product ADP were determined. Adenosine Triphosphate 87-90 mitogen-activated protein kinase 1 Homo sapiens 42-46 23847348-2 2013 SCH772984, a selective, ATP-competitive inhibitor of ERK1 and ERK2, is effective in BRAF-mutant models in which resistance is the result of ERK reactivation. Adenosine Triphosphate 24-27 mitogen-activated protein kinase 1 Homo sapiens 62-66 23847348-2 2013 SCH772984, a selective, ATP-competitive inhibitor of ERK1 and ERK2, is effective in BRAF-mutant models in which resistance is the result of ERK reactivation. Adenosine Triphosphate 24-27 mitogen-activated protein kinase 1 Homo sapiens 53-56 23224888-6 2013 Bradykinin-induced migration is controlled by a G(i/o)-protein-independent pathway, while ATP-induced migration involves G(i/o) proteins as well as mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK)-dependent pathway. Adenosine Triphosphate 90-93 mitogen-activated protein kinase 1 Homo sapiens 182-186 23224888-6 2013 Bradykinin-induced migration is controlled by a G(i/o)-protein-independent pathway, while ATP-induced migration involves G(i/o) proteins as well as mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK)-dependent pathway. Adenosine Triphosphate 90-93 mitogen-activated protein kinase 1 Homo sapiens 227-230 22028470-3 2011 We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5"-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. Adenosine Triphosphate 119-144 mitogen-activated protein kinase 1 Homo sapiens 67-71 22828512-11 2012 Furthermore, extracellular ATP led to an activation of MEK/ERK- and PI3K/Akt-signaling pathways. Adenosine Triphosphate 27-30 mitogen-activated protein kinase 1 Homo sapiens 59-62 22828512-12 2012 Accordingly, inhibition of MEK/ERK-signaling by UO126 or inhibition of PI3K/Akt-signaling by LY294002 abolished the anti-apoptotic effects of ATP. Adenosine Triphosphate 142-145 mitogen-activated protein kinase 1 Homo sapiens 31-34 22830536-5 2012 These studies have revealed that (i) ligand binding does not depend on chemical bonding but on molecular interaction (molecular orbital analysis), (ii) the cis-enone moiety of inhibitors is in the range of Michael addition reaction with the Cys166 residue in ERK2 (docking simulation study), and (iii) molecular shape of M1(8) conformations is the best fit for the ATP binding site of kinases. Adenosine Triphosphate 365-368 mitogen-activated protein kinase 1 Homo sapiens 259-263 22615491-2 2012 Using an engineered extracellular signal-regulated kinase 2 (ERK2) that can utilize ATP analogs, we have identified the alternative mRNA splicing factor 45 (SPF45), which is overexpressed in cancer, as a novel coimmunoprecipitating ERK2 substrate. Adenosine Triphosphate 84-87 mitogen-activated protein kinase 1 Homo sapiens 20-59 22615491-2 2012 Using an engineered extracellular signal-regulated kinase 2 (ERK2) that can utilize ATP analogs, we have identified the alternative mRNA splicing factor 45 (SPF45), which is overexpressed in cancer, as a novel coimmunoprecipitating ERK2 substrate. Adenosine Triphosphate 84-87 mitogen-activated protein kinase 1 Homo sapiens 61-65 22615491-2 2012 Using an engineered extracellular signal-regulated kinase 2 (ERK2) that can utilize ATP analogs, we have identified the alternative mRNA splicing factor 45 (SPF45), which is overexpressed in cancer, as a novel coimmunoprecipitating ERK2 substrate. Adenosine Triphosphate 84-87 mitogen-activated protein kinase 1 Homo sapiens 232-236 22113612-2 2011 ATP-competitive RAF inhibitors activate ERK signalling by transactivating RAF dimers. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 40-43 22892241-7 2012 However, unlike (V600E)Braf, Mek/Erk pathway activation was mediated by both Craf and Braf, and ATP-competitive RAF inhibitors induced paradoxical Mek/Erk pathway activation. Adenosine Triphosphate 96-99 mitogen-activated protein kinase 1 Homo sapiens 151-154 22028470-3 2011 We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5"-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. Adenosine Triphosphate 119-144 mitogen-activated protein kinase 1 Homo sapiens 83-87 22028470-3 2011 We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5"-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. Adenosine Triphosphate 119-144 mitogen-activated protein kinase 1 Homo sapiens 83-87 22028470-3 2011 We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5"-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. Adenosine Triphosphate 146-149 mitogen-activated protein kinase 1 Homo sapiens 67-71 22028470-3 2011 We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5"-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. Adenosine Triphosphate 146-149 mitogen-activated protein kinase 1 Homo sapiens 83-87 22028470-3 2011 We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5"-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. Adenosine Triphosphate 146-149 mitogen-activated protein kinase 1 Homo sapiens 83-87 21413023-11 2011 ATP induces HB-EGF synthesis and release by interacting with the P2 purinergic receptor and through p38 and ERK1/2 signaling in response to a challenging environment. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 100-103 21483442-2 2011 Here, to enhance the BMS-214662 apoptotic effect, we further targeted the extracellular signal-regulated kinase (ERK) pathway, downstream of BCR-ABL, by treating CD34+ CML stem/progenitor cells with a highly selective adenosine triphosphate (ATP) non-competitive MEK inhibitor, PD184352. Adenosine Triphosphate 218-240 mitogen-activated protein kinase 1 Homo sapiens 74-111 21483442-2 2011 Here, to enhance the BMS-214662 apoptotic effect, we further targeted the extracellular signal-regulated kinase (ERK) pathway, downstream of BCR-ABL, by treating CD34+ CML stem/progenitor cells with a highly selective adenosine triphosphate (ATP) non-competitive MEK inhibitor, PD184352. Adenosine Triphosphate 218-240 mitogen-activated protein kinase 1 Homo sapiens 113-116 21483442-2 2011 Here, to enhance the BMS-214662 apoptotic effect, we further targeted the extracellular signal-regulated kinase (ERK) pathway, downstream of BCR-ABL, by treating CD34+ CML stem/progenitor cells with a highly selective adenosine triphosphate (ATP) non-competitive MEK inhibitor, PD184352. Adenosine Triphosphate 242-245 mitogen-activated protein kinase 1 Homo sapiens 113-116 21829637-2 2011 Recently, ATP-competitive Raf inhibitors were shown to cause MAPK pathway activation via Raf kinase priming in wild-type BRaf cells and tumors, highlighting the need for a thorough understanding of signaling in the context of small molecule kinase inhibitors. Adenosine Triphosphate 10-13 mitogen-activated protein kinase 1 Homo sapiens 61-65 21494553-13 2011 Our kinetic analysis suggests that the unstructured N-terminus provides 10-fold uniform stabilization of the ground state ERK2 Ets MgATP complex and intermediates of the enzymatic reaction. Adenosine Triphosphate 131-136 mitogen-activated protein kinase 1 Homo sapiens 122-126 20562007-1 2010 BACKGROUND: In previous work, we have demonstrated that extracellular adenosine 5"-triphosphate (ATP) acts on intestinal Caco-2 cell P2Y receptors promoting a rapid increase in the phosphorylation of ERK1/2, p46 JNK and p38 MAP kinases (MAPKs). Adenosine Triphosphate 70-95 mitogen-activated protein kinase 1 Homo sapiens 220-223 20562007-1 2010 BACKGROUND: In previous work, we have demonstrated that extracellular adenosine 5"-triphosphate (ATP) acts on intestinal Caco-2 cell P2Y receptors promoting a rapid increase in the phosphorylation of ERK1/2, p46 JNK and p38 MAP kinases (MAPKs). Adenosine Triphosphate 97-100 mitogen-activated protein kinase 1 Homo sapiens 220-223 20562007-3 2010 Confocal microscopy and immunobloting studies showed that ERK1/2 and JNK translocate into the nucleus of the cells stimulated by ATP, where they participate, together with p38 MAPK, in the phosphorylation of JunD, ATF-1 and ATF-2 transcription factors. Adenosine Triphosphate 129-132 mitogen-activated protein kinase 1 Homo sapiens 172-175 20562007-6 2010 Of physiological significance, in agreement with the mitogenic role of the MAPK cascade, ATP increased Caco-2 cell proliferation, and this effect was blocked by UO126, SB203580 and SP600125, the specific inhibitors of ERK1/2, p38 MAPK and JNK1/2, respectively. Adenosine Triphosphate 89-92 mitogen-activated protein kinase 1 Homo sapiens 226-229 20477948-6 2010 ATP induced both activation of nuclear factor of activated T cells (NFAT) and MAPKs (p38, ERK, and JNK) through P2X7R. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 90-93 20477948-7 2010 ATP-induced mRNA expression of CXCL2 was inhibited by INCA-6 (an NFAT inhibitor), SB203580 (a p38 inhibitor), U0126 (a MEK-ERK inhibitor) and JNK inhibitor II (a JNK inhibitor). Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 123-126 20477948-9 2010 In addition, protein kinase C inhibitors suppressed ATP-induced ERK and JNK activation, and also inhibited ATP-induced CXCL2 expression in microglia. Adenosine Triphosphate 52-55 mitogen-activated protein kinase 1 Homo sapiens 64-67 20232875-4 2010 In addition, MEK1 and ERK2 were probed with an ATP competitor and an allosteric MEK1 inhibitor, which generated distinct phosphorylation-interaction patterns. Adenosine Triphosphate 47-50 mitogen-activated protein kinase 1 Homo sapiens 22-26 19649663-6 2010 Multiple sequence alignment and 3D structure model provided the putative ATP binding pocket of Leishmania with respect to human ERK2 and LCRK3. Adenosine Triphosphate 73-76 mitogen-activated protein kinase 1 Homo sapiens 128-132 20179705-2 2010 We found that ATP-competitive RAF inhibitors inhibit ERK signalling in cells with mutant BRAF, but unexpectedly enhance signalling in cells with wild-type BRAF. Adenosine Triphosphate 14-17 mitogen-activated protein kinase 1 Homo sapiens 53-56 20179705-5 2010 Induction of ERK signalling requires direct binding of the drug to the ATP-binding site of one kinase of the dimer and is dependent on RAS activity. Adenosine Triphosphate 71-74 mitogen-activated protein kinase 1 Homo sapiens 13-16 20306284-5 2010 In order to prove that this is viable, the workflow was tested on a database of known inhibitors of ERK2, a protein kinase possessing a cysteine in the ATP site. Adenosine Triphosphate 152-155 mitogen-activated protein kinase 1 Homo sapiens 100-104 19649663-12 2010 Further the comparative molecular electrostatic potential and cavity depth analysis of Leishmania MAPK and human ERK2 suggested several important differences in its ATP binding pocket. Adenosine Triphosphate 165-168 mitogen-activated protein kinase 1 Homo sapiens 113-117 19689374-2 2009 In this review, we will discuss approaches to identify inhibitors of ERK proteins through targeting ATP-dependent and ATP-independent mechanisms. Adenosine Triphosphate 100-103 mitogen-activated protein kinase 1 Homo sapiens 69-72 19689374-2 2009 In this review, we will discuss approaches to identify inhibitors of ERK proteins through targeting ATP-dependent and ATP-independent mechanisms. Adenosine Triphosphate 118-121 mitogen-activated protein kinase 1 Homo sapiens 69-72 18501702-5 2008 The P2X7R agonist 2",3"-O-(4-benzoylbenzoyl)-ATP (BzATP) significantly increased ERK activation and this activation could be completely inhibited by oxidized ATP and Brilliant blue G. Adenosine Triphosphate 45-48 mitogen-activated protein kinase 1 Homo sapiens 81-84 18658095-9 2009 Wounding-, LPA-, and ATP-induced HB-EGF shedding and EGFR activation were attenuated by the MAPK/ERK kinase (MEK) inhibitors PD98059 and U0126, as well as by ADAM10 and -17 inhibitors. Adenosine Triphosphate 21-24 mitogen-activated protein kinase 1 Homo sapiens 97-100 19424502-7 2009 The proposed model accounts for the structural basis of several experimental findings such as the complex-dissociating effect of ATP, or PTP-SL blocking effect on the ERK2 export to the nucleus. Adenosine Triphosphate 129-132 mitogen-activated protein kinase 1 Homo sapiens 167-171 19105050-1 2008 We have recently identified several novel ATP-independent inhibitors that target the extracellular signal-regulated kinase-2 (ERK2) protein and inhibit substrate phosphorylation. Adenosine Triphosphate 42-45 mitogen-activated protein kinase 1 Homo sapiens 126-130 18835158-5 2008 Structural features relevant to the stabilizations of the newly identified inhibitors in the ATP-binding site of ERK2 are discussed in detail. Adenosine Triphosphate 93-96 mitogen-activated protein kinase 1 Homo sapiens 113-117 18676374-5 2008 ATP sequentially activated the phosphorylation of Akt, ERK1/2, p38, RSK1, and cAMP-responding element-binding protein (CREB) in a protein kinase C-independent manner. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 63-66 18559577-3 2008 The identification of non-ATP-competitive inhibitors of the MAPK kinase MAPK/ERK kinase (MEK) resulted in the first demonstration that the ERK pathway could be effectively shut down in a highly selective fashion. Adenosine Triphosphate 26-29 mitogen-activated protein kinase 1 Homo sapiens 60-64 18434089-0 2008 Extracellular ATP activates the PLC/PKC/ERK signaling pathway through the P2Y2 purinergic receptor leading to the induction of early growth response 1 expression and the inhibition of viability in human endometrial stromal cells. Adenosine Triphosphate 14-17 mitogen-activated protein kinase 1 Homo sapiens 40-43 18434089-12 2008 ATP activated MAPKs through the P2Y2 purinoceptor/PLC/PKC/ERK signaling pathway and induced translocation of ERK1/2 into the nucleus. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 58-61 18639636-0 2008 Tyrosine hydroxylase phosphorylation increases in response to ATP and neuropeptide Y co-stimulation of ERK2 phosphorylation. Adenosine Triphosphate 62-65 mitogen-activated protein kinase 1 Homo sapiens 103-107 18559577-3 2008 The identification of non-ATP-competitive inhibitors of the MAPK kinase MAPK/ERK kinase (MEK) resulted in the first demonstration that the ERK pathway could be effectively shut down in a highly selective fashion. Adenosine Triphosphate 26-29 mitogen-activated protein kinase 1 Homo sapiens 72-76 18559577-3 2008 The identification of non-ATP-competitive inhibitors of the MAPK kinase MAPK/ERK kinase (MEK) resulted in the first demonstration that the ERK pathway could be effectively shut down in a highly selective fashion. Adenosine Triphosphate 26-29 mitogen-activated protein kinase 1 Homo sapiens 77-80 18559577-3 2008 The identification of non-ATP-competitive inhibitors of the MAPK kinase MAPK/ERK kinase (MEK) resulted in the first demonstration that the ERK pathway could be effectively shut down in a highly selective fashion. Adenosine Triphosphate 26-29 mitogen-activated protein kinase 1 Homo sapiens 139-142 18463290-5 2008 hBVR is nearly as effective as IGF1 in activating ERK; intact hBVR ATP-binding domain is necessary for Elk1 activation, whereas protein-protein interaction is the basis for hBVR activation of MEK1 and ERK. Adenosine Triphosphate 67-70 mitogen-activated protein kinase 1 Homo sapiens 50-53 18490749-0 2008 Constitutive ERK MAPK activity regulates macrophage ATP production and mitochondrial integrity. Adenosine Triphosphate 52-55 mitogen-activated protein kinase 1 Homo sapiens 13-16 18490749-0 2008 Constitutive ERK MAPK activity regulates macrophage ATP production and mitochondrial integrity. Adenosine Triphosphate 52-55 mitogen-activated protein kinase 1 Homo sapiens 17-21 18490749-5 2008 Significant levels of MEK and ERK localize to the mitochondria and inhibition of ERK activity induces an early and profound depletion in cellular ATP coincident with a loss of mitochondrial transmembrane potential. Adenosine Triphosphate 146-149 mitogen-activated protein kinase 1 Homo sapiens 81-84 18490749-6 2008 The effect of ERK suppression on ATP levels was specific, since it did not occur with PI3K/Akt, p38, or JNK suppression. Adenosine Triphosphate 33-36 mitogen-activated protein kinase 1 Homo sapiens 14-17 18490749-9 2008 The cell death induced by ERK inhibition had hallmarks of both apoptotic (caspase activation) and necrotic (ATP loss) cell death. Adenosine Triphosphate 108-111 mitogen-activated protein kinase 1 Homo sapiens 26-29 18490749-12 2008 As a composite, these data demonstrate a novel mitochondrial role for ERK in maintaining mitochondrial membrane potential and ATP production in human alveolar macrophages. Adenosine Triphosphate 126-129 mitogen-activated protein kinase 1 Homo sapiens 70-73 18280666-10 2008 Furthermore, alanine substitutions of T341 and S385 to disrupt the potential ERK phosphorylation sites present in the Kir6.2 subunit significantly abrogated the stimulatory effects of ERK2, while aspartate substitutions of T341 and S385 to mimic the (negative) charge effect of phosphorylation rendered a small yet significant reduction in the ATP sensitivity of the channel. Adenosine Triphosphate 344-347 mitogen-activated protein kinase 1 Homo sapiens 77-80 18280666-10 2008 Furthermore, alanine substitutions of T341 and S385 to disrupt the potential ERK phosphorylation sites present in the Kir6.2 subunit significantly abrogated the stimulatory effects of ERK2, while aspartate substitutions of T341 and S385 to mimic the (negative) charge effect of phosphorylation rendered a small yet significant reduction in the ATP sensitivity of the channel. Adenosine Triphosphate 344-347 mitogen-activated protein kinase 1 Homo sapiens 184-188 18280666-12 2008 The ERK2-induced K(ATP) channel stimulation can be accounted for by changes in channel gating that destabilize the closed states and by reduction in the ATP sensitivity. Adenosine Triphosphate 19-22 mitogen-activated protein kinase 1 Homo sapiens 4-8 17194451-4 2007 The X-ray crystal structure of the ERK2/FR148083 complex revealed that the compound binds to the ATP binding site of ERK2, involving a covalent bond to Sgamma of ERK2 Cys166, hydrogen bonds with the backbone NH of Met108, Nzeta of Lys114, backbone C=O of Ser153, Ndelta2 of Asn154, and hydrophobic interactions with the side chains of Ile31, Val39, Ala52, and Leu156. Adenosine Triphosphate 97-100 mitogen-activated protein kinase 1 Homo sapiens 35-39 17284517-5 2007 The wound-induced rapid activation of phosphatidylinositol-3-kinase (PI3K) and extracellular signal-regulated kinase (ERK) pathways in HCE cells was attenuated by eliminating extracellular ATP, ADP and adenosine. Adenosine Triphosphate 189-192 mitogen-activated protein kinase 1 Homo sapiens 79-116 17284517-5 2007 The wound-induced rapid activation of phosphatidylinositol-3-kinase (PI3K) and extracellular signal-regulated kinase (ERK) pathways in HCE cells was attenuated by eliminating extracellular ATP, ADP and adenosine. Adenosine Triphosphate 189-192 mitogen-activated protein kinase 1 Homo sapiens 118-121 17720133-4 2007 In addition, cell stimulation with ATP, ATPgamma-S or UTP but not ADPbeta-S induced the phosphorylation of ERK1/2, p38 and JNK1/2 mitogen activated protein kinases (MAPKs). Adenosine Triphosphate 35-38 mitogen-activated protein kinase 1 Homo sapiens 115-118 17652083-3 2007 Kinetic studies carried out in various concentrations of sucrose revealed that both k(cat) and k(cat)/K(m) for either ATP or EtsDelta138 were highly sensitive to solvent viscosity, suggesting that the rapid equilibrium assumption is not valid for the phosphorylation of protein substrate by ERK2. Adenosine Triphosphate 118-121 mitogen-activated protein kinase 1 Homo sapiens 291-295 17194451-4 2007 The X-ray crystal structure of the ERK2/FR148083 complex revealed that the compound binds to the ATP binding site of ERK2, involving a covalent bond to Sgamma of ERK2 Cys166, hydrogen bonds with the backbone NH of Met108, Nzeta of Lys114, backbone C=O of Ser153, Ndelta2 of Asn154, and hydrophobic interactions with the side chains of Ile31, Val39, Ala52, and Leu156. Adenosine Triphosphate 97-100 mitogen-activated protein kinase 1 Homo sapiens 117-121 17194451-4 2007 The X-ray crystal structure of the ERK2/FR148083 complex revealed that the compound binds to the ATP binding site of ERK2, involving a covalent bond to Sgamma of ERK2 Cys166, hydrogen bonds with the backbone NH of Met108, Nzeta of Lys114, backbone C=O of Ser153, Ndelta2 of Asn154, and hydrophobic interactions with the side chains of Ile31, Val39, Ala52, and Leu156. Adenosine Triphosphate 97-100 mitogen-activated protein kinase 1 Homo sapiens 117-121 17000106-0 2006 Characterization of ATP-independent ERK inhibitors identified through in silico analysis of the active ERK2 structure. Adenosine Triphosphate 20-23 mitogen-activated protein kinase 1 Homo sapiens 36-39 17000106-0 2006 Characterization of ATP-independent ERK inhibitors identified through in silico analysis of the active ERK2 structure. Adenosine Triphosphate 20-23 mitogen-activated protein kinase 1 Homo sapiens 103-107 17000106-3 2006 Taking advantage of recently identified substrate docking domains on ERK2, we have used computer-aided drug design (CADD) to identify novel low molecular weight compounds that interact with ERK2 in an ATP-independent manner and disrupt substrate-specific interactions. Adenosine Triphosphate 201-204 mitogen-activated protein kinase 1 Homo sapiens 190-194 17000106-7 2006 These studies demonstrate that CADD can be used to identify lead compounds for development of novel non-ATP-dependent inhibitors selective for active ERK and its interactions with substrates involved in cancer cell proliferation. Adenosine Triphosphate 104-107 mitogen-activated protein kinase 1 Homo sapiens 150-153 16321972-2 2006 Here we report that ATP released upon hypotonic stress stimulated prostate cancer cell proliferation, activated purinergic receptors, increased intracellular [Ca(2+)](i), and initiated downstream signaling cascades that involved MAPKs ERK1/2 and p38 as well as phosphatidylinositol 3-kinase (PI3K). Adenosine Triphosphate 20-23 mitogen-activated protein kinase 1 Homo sapiens 246-249 16741950-4 2006 Here, we demonstrate that extracellular ATP has a mitogenic effect on ARO cells, increasing ERK phosphorylation, AP1 activation, and cyclin D1 expression. Adenosine Triphosphate 40-43 mitogen-activated protein kinase 1 Homo sapiens 92-95 16533496-0 2006 Extracellular ATP activates ERK1/ERK2 via a metabotropic P2Y1 receptor in a Ca2+ independent manner in differentiated human skeletal muscle cells. Adenosine Triphosphate 14-17 mitogen-activated protein kinase 1 Homo sapiens 33-37 16533496-10 2006 In addition, ATP elicited extracellular signal regulated kinase (ERK)1/2 phosphorylation in a time and concentration dependent manner, again mainly via P2Y1 receptors. Adenosine Triphosphate 13-16 mitogen-activated protein kinase 1 Homo sapiens 26-72 16781450-6 2006 Extracellular ATP can activate signaling cascades composed of protein kinases including extracellular signal-regulated kinase (ERK) and phosphatidylinositol-3-kinase (PI3K). Adenosine Triphosphate 14-17 mitogen-activated protein kinase 1 Homo sapiens 88-125 16781450-6 2006 Extracellular ATP can activate signaling cascades composed of protein kinases including extracellular signal-regulated kinase (ERK) and phosphatidylinositol-3-kinase (PI3K). Adenosine Triphosphate 14-17 mitogen-activated protein kinase 1 Homo sapiens 127-130 16781450-10 2006 The released ATP, upon binding to its specific receptors, triggers ERK and PI3K signaling and renders cells resistant to these stresses. Adenosine Triphosphate 13-16 mitogen-activated protein kinase 1 Homo sapiens 67-70 16914897-3 2006 RESULTS: ATP, 2-meSATP, UTP and UDP cause a rapid and transitory increase in the phosphorylation of MAPK/ERK. Adenosine Triphosphate 9-12 mitogen-activated protein kinase 1 Homo sapiens 105-108 16892371-1 2006 Recently developed hydrogen-bonding and hydrophobic analysis algorithms were used to investigate the interaction properties of the ATP binding sites of CDK2, CDK4, and ERK2. Adenosine Triphosphate 131-134 mitogen-activated protein kinase 1 Homo sapiens 168-172 16341234-3 2006 Here, we use macrophages to investigate the phosphorylation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) by nucleotides and the involvement of MAPKs and intracellular Ca2+ concentration in ATP-induced membrane permeabilization. Adenosine Triphosphate 203-206 mitogen-activated protein kinase 1 Homo sapiens 63-109 16914897-5 2006 ATP-dependent activation of MAPK/ERK was prevented by pretreatment of HUVEC with pertussis toxin or MEK inhibitor PD98059. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 33-36 16914897-6 2006 In addition, activation of the MAPK/ ERK cascade by ATP was blocked in cells pretreated with wortmannin and LY294002, but not by U73122, BAPTA or a Ca(2+)-free medium. Adenosine Triphosphate 52-55 mitogen-activated protein kinase 1 Homo sapiens 37-40 16914897-7 2006 Furthermore, an inhibition of ATP-dependent MAPK/ERK phosphorylation was observed in HUVEC pretreated with high doses of GF109203X or myristoylated PKC- zeta pseudosubstrate. Adenosine Triphosphate 30-33 mitogen-activated protein kinase 1 Homo sapiens 49-52 16914897-9 2006 However, ATP-stimulated MAPK/ERK activation was unaffected in cells pretreated with AG1478 or perillic acid. Adenosine Triphosphate 9-12 mitogen-activated protein kinase 1 Homo sapiens 29-32 16914897-11 2006 CONCLUSION: These observations suggest that the effects mediated by ATP in HUVEC occur via PTX-sensitive G-protein-coupled P2Y receptors through PI3K-dependent mechanisms, in which PDK1 and PKC-zeta are two key molecules within signal cascade leading to MAPK/ERK activation. Adenosine Triphosphate 68-71 mitogen-activated protein kinase 1 Homo sapiens 259-262 16253958-8 2006 In cell-free systems, ERK2 gave rise to strong ATP-dependent PLD activity and directly phosphorylated PLD2 that generated two phosphopeptides only after tryptic digestion. Adenosine Triphosphate 47-50 mitogen-activated protein kinase 1 Homo sapiens 22-26 16185715-4 2005 In both active and inactive forms of ERK2, protection from hydrogen exchange by AMP-PNP binding was observed within conserved ATP binding motifs in the N-terminal lobe, which are known to directly interact with nucleotide in various protein kinases. Adenosine Triphosphate 126-129 mitogen-activated protein kinase 1 Homo sapiens 37-41 16893669-0 2006 Modulation of ERK 1/2 and p38 MAPK signaling pathways by ATP in osteoblasts: involvement of mechanical stress-activated calcium influx, PKC and Src activation. Adenosine Triphosphate 57-60 mitogen-activated protein kinase 1 Homo sapiens 26-29 16893669-6 2006 In addition, ERK 1/2 and p38 MAPK were activated by ATP in a dose- and time-dependent manner. Adenosine Triphosphate 52-55 mitogen-activated protein kinase 1 Homo sapiens 25-28 16893669-8 2006 Ca(2+)-free extracellular medium (containing 0.5mM EGTA) and the use of gadolinium (5 microM), which suppressed MSACI, prevented ERK 1/2 and p38 phosphorylation by ATP. Adenosine Triphosphate 164-167 mitogen-activated protein kinase 1 Homo sapiens 141-144 16893669-9 2006 Altogether, these results represent the first evidence to date suggesting that P2Y(2) receptor stimulation by ATP in osteoblasts sensitizes mechanical stress activated calcium channels leading to calcium influx and a fast activation of the ERK 1/2 and p38 MAPK pathways. Adenosine Triphosphate 110-113 mitogen-activated protein kinase 1 Homo sapiens 252-255 16185715-0 2005 Hydrogen exchange solvent protection by an ATP analogue reveals conformational changes in ERK2 upon activation. Adenosine Triphosphate 43-46 mitogen-activated protein kinase 1 Homo sapiens 90-94 16185715-8 2005 The finding provides novel evidence that phosphorylation of ERK2 facilitates interdomain closure, allowing proper orientation between ATP and substrate to facilitate phosphoryl transfer. Adenosine Triphosphate 134-137 mitogen-activated protein kinase 1 Homo sapiens 60-64 16052566-6 2005 Moreover, the potentiation of ATP responses by Ap(5)A and EGF was completely abolished by the MAP kinase (MEK) inhibitor U-0126, indicating that ERK activation is a required step for the potentiation event. Adenosine Triphosphate 30-33 mitogen-activated protein kinase 1 Homo sapiens 145-148 16139248-6 2005 X-ray crystal structure analysis of the human ERK2/FR180204 complex revealed that Q105, D106, L156, and C166, which form the ATP-binding pocket on ERK, play important roles in the drug/protein interaction. Adenosine Triphosphate 125-128 mitogen-activated protein kinase 1 Homo sapiens 46-50 16139248-6 2005 X-ray crystal structure analysis of the human ERK2/FR180204 complex revealed that Q105, D106, L156, and C166, which form the ATP-binding pocket on ERK, play important roles in the drug/protein interaction. Adenosine Triphosphate 125-128 mitogen-activated protein kinase 1 Homo sapiens 46-49 15964513-7 2005 Further, Akt and ERK phosphorylation resulted from exposure to supplemental extracellular ATP. Adenosine Triphosphate 90-93 mitogen-activated protein kinase 1 Homo sapiens 17-20 15994434-5 2005 Increases in cytosolic Ca2+ and Erk activation caused by ATP were irrelevant to barrier enhancement. Adenosine Triphosphate 57-60 mitogen-activated protein kinase 1 Homo sapiens 32-35 15964513-8 2005 Thus, extracellularly released ATP signals to prevent ozone-induced death and supplementation with ATP or its analogs can augment protection, at least in part via Akt and /or ERK signaling pathways and their metabolic effects. Adenosine Triphosphate 31-34 mitogen-activated protein kinase 1 Homo sapiens 175-178 15964513-8 2005 Thus, extracellularly released ATP signals to prevent ozone-induced death and supplementation with ATP or its analogs can augment protection, at least in part via Akt and /or ERK signaling pathways and their metabolic effects. Adenosine Triphosphate 99-102 mitogen-activated protein kinase 1 Homo sapiens 175-178 15472225-5 2004 Western blot analysis, using a monoclonal antibody, which detected the total and phosphorylated forms of ERK1 and ERK2 (p42(mapk) and p44 (mapk), respectively), demonstrated that exogenous ATP evoked ERKs in a dose- and time-dependent manner. Adenosine Triphosphate 189-192 mitogen-activated protein kinase 1 Homo sapiens 114-118 15774218-7 2005 RESULTS: ATP activated ERK1/2 and p38 kinase time-dependently. Adenosine Triphosphate 9-12 mitogen-activated protein kinase 1 Homo sapiens 34-37 15774218-8 2005 Suramin significantly inhibited the activation of ERK1/2 and p38 kinase by ATP. Adenosine Triphosphate 75-78 mitogen-activated protein kinase 1 Homo sapiens 61-64 16181551-4 2005 The activation of ERK1/2 and p38 induced by P2Y receptor agonist ATP was analyzed by Western blot with phospho-specific antibodies against the dually phosphorylated, active forms of ERK1/2 and p38. Adenosine Triphosphate 65-68 mitogen-activated protein kinase 1 Homo sapiens 29-32 16181551-4 2005 The activation of ERK1/2 and p38 induced by P2Y receptor agonist ATP was analyzed by Western blot with phospho-specific antibodies against the dually phosphorylated, active forms of ERK1/2 and p38. Adenosine Triphosphate 65-68 mitogen-activated protein kinase 1 Homo sapiens 193-196 16181551-11 2005 Up-regulation of MKP5-wt inhibited phosphorylation of p38 by ATP and reduced cell invasion stimulated by ATP (22.4% and 28.7% decrease compared with ATP treated group of 1E8 and 2B4, respectively). Adenosine Triphosphate 61-64 mitogen-activated protein kinase 1 Homo sapiens 54-57 15449317-4 2004 The wave is generated by the extracellular release of ATP, which also induces phosphorylation of ERK (Yang et al. Adenosine Triphosphate 54-57 mitogen-activated protein kinase 1 Homo sapiens 97-100 15003601-7 2004 In this report, we discuss the generation and characterization of ERK2 mutants that utilize analogs of ATP and describe the methodology used to identify ERK2-associated substrates. Adenosine Triphosphate 103-106 mitogen-activated protein kinase 1 Homo sapiens 66-70 15350190-10 2004 ATP, basic fibroblastic growth factor (bFGF), EGF and VEGF induced mitogenesis and caused a rise in ERK 2 activation within 10 min. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 100-105 15350190-11 2004 L-Arginine to L-citrulline conversion assays showed that ATP, EGF and VEGF induced a significant rise in eNOS activity, and this correlates with an ability to induce Ca2+ mobilization and ERK 2 activation. Adenosine Triphosphate 57-60 mitogen-activated protein kinase 1 Homo sapiens 188-193 14761947-9 2004 Incubation with ATP scavengers abolished ATP-dependent ERK phosphorylation stimulated by hyperoxia. Adenosine Triphosphate 16-19 mitogen-activated protein kinase 1 Homo sapiens 55-58 14761947-9 2004 Incubation with ATP scavengers abolished ATP-dependent ERK phosphorylation stimulated by hyperoxia. Adenosine Triphosphate 41-44 mitogen-activated protein kinase 1 Homo sapiens 55-58 15001425-5 2004 ATP (10 microM) increased ERK2 phosphorylation from basal 17 +/- 3 to 53 +/- 4%, an effect suppressed in the presence of the MEK inhibitors PD-98059 (20 microM) or U0126 (10 microM). Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 26-30 15132853-9 2004 Pretreatment with 10 micro mol/L p38 inhibitor SB203580 antagonized the effect of ATP-induced additional growth inhibition, suggesting that ERK1/2 and p38 pathways play an important role in ATP-induced growth inhibition. Adenosine Triphosphate 82-85 mitogen-activated protein kinase 1 Homo sapiens 33-36 15132853-9 2004 Pretreatment with 10 micro mol/L p38 inhibitor SB203580 antagonized the effect of ATP-induced additional growth inhibition, suggesting that ERK1/2 and p38 pathways play an important role in ATP-induced growth inhibition. Adenosine Triphosphate 82-85 mitogen-activated protein kinase 1 Homo sapiens 151-154 15132853-9 2004 Pretreatment with 10 micro mol/L p38 inhibitor SB203580 antagonized the effect of ATP-induced additional growth inhibition, suggesting that ERK1/2 and p38 pathways play an important role in ATP-induced growth inhibition. Adenosine Triphosphate 190-193 mitogen-activated protein kinase 1 Homo sapiens 33-36 15132853-9 2004 Pretreatment with 10 micro mol/L p38 inhibitor SB203580 antagonized the effect of ATP-induced additional growth inhibition, suggesting that ERK1/2 and p38 pathways play an important role in ATP-induced growth inhibition. Adenosine Triphosphate 190-193 mitogen-activated protein kinase 1 Homo sapiens 151-154 15132853-13 2004 Treatment with ATP could restore their invasive ability, and this effect by ATP could be blocked by pretreatment with SB203580, indicating the involvement of both ERK1/2 and p38 pathways in invasive ability of prostatic cancer cells. Adenosine Triphosphate 15-18 mitogen-activated protein kinase 1 Homo sapiens 174-177 15023352-3 2004 ERK2 catalyses the transfer of the gamma-phosphate of adenosine triphosphate to serine or threonine residues found in Ser-Pro or Thr-Pro motifs on proteins. Adenosine Triphosphate 54-76 mitogen-activated protein kinase 1 Homo sapiens 0-4 12747800-6 2003 Stimulation of P2X7 receptors in HEK-293 cells led to an activation of extracellular signal-regulated kinases ERK1 and ERK2 and this activation was seen after just 1 min of stimulation with ATP. Adenosine Triphosphate 190-193 mitogen-activated protein kinase 1 Homo sapiens 119-123 14567689-4 2003 Using a quench-flow apparatus, MgATP(2-) was rapidly mixed (<1 ms) with both ERK2 and the protein substrate EtsDelta138 in the presence of a saturating total concentration (20 mM) of magnesium ion at 27 degrees C and pH 7.5. Adenosine Triphosphate 31-36 mitogen-activated protein kinase 1 Homo sapiens 80-84 14642090-6 2003 Then the total protein was extracted, SDS-PAGE and Western blotting were used to detect the activation of p38 and ERK1/2 induced by ATP with phosphospecific antibodies directed against the dually phosphorylated, active forms of p38 and ERK1/2. Adenosine Triphosphate 132-135 mitogen-activated protein kinase 1 Homo sapiens 106-109 14642090-6 2003 Then the total protein was extracted, SDS-PAGE and Western blotting were used to detect the activation of p38 and ERK1/2 induced by ATP with phosphospecific antibodies directed against the dually phosphorylated, active forms of p38 and ERK1/2. Adenosine Triphosphate 132-135 mitogen-activated protein kinase 1 Homo sapiens 228-231 14642090-9 2003 ATP time-dependently stimulated the activities of ERK1/2 and p38 kinases, inhibited the in vitro growth and colony formation on soft agar, and promoted the in vitro invasion of 1E8 cells. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 61-64 14642090-10 2003 MKP5-transfection effectively inhibited the p38 activity induced by ATP and blocked the effects by ATP stimulation on 1E8 cells. Adenosine Triphosphate 68-71 mitogen-activated protein kinase 1 Homo sapiens 44-47 14642090-11 2003 The activity of p38 kinase was significantly decreased both in the control and MKP5 transfected cells that were pretreated with SB203580 and then with ATP with an inhibition rates of 83.14% and 58.00% (P < 0.001 and P = 0.003). Adenosine Triphosphate 151-154 mitogen-activated protein kinase 1 Homo sapiens 16-19 14642090-18 2003 CONCLUSION: The p38 and ERK1/2 pathways exert different effects on the in vitro growth, invasion and colony formation of 1E8 prostate cancer cells related to ATP. Adenosine Triphosphate 158-161 mitogen-activated protein kinase 1 Homo sapiens 16-19 15714002-0 2004 ERK, PKC and PI3K/Akt pathways mediate extracellular ATP and adenosine-induced proliferation of U138-MG human glioma cell line. Adenosine Triphosphate 53-56 mitogen-activated protein kinase 1 Homo sapiens 0-3 15714002-5 2004 RESULTS: ATP or adenosine (100 microM) induced extracellular signal-regulated protein kinase (ERK), Akt and GSK3beta phosphorylation. Adenosine Triphosphate 9-12 mitogen-activated protein kinase 1 Homo sapiens 47-92 15714002-5 2004 RESULTS: ATP or adenosine (100 microM) induced extracellular signal-regulated protein kinase (ERK), Akt and GSK3beta phosphorylation. Adenosine Triphosphate 9-12 mitogen-activated protein kinase 1 Homo sapiens 94-97 12711339-2 2003 In this assay, ERK catalyzes the transfer of gamma-phosphate from adenosine 5(")-triphosphate to the threonine residue of a fluorescently labeled nonapeptide (APRTPGGRR), and the phosphorylated and nonphosphorylated peptides were detected by fluorescence. Adenosine Triphosphate 66-93 mitogen-activated protein kinase 1 Homo sapiens 15-18 11931846-6 2002 PD 98059 completely inhibited ERK activation by BK and ATP in porcine aortic endothelial cells without affecting eNOS activation. Adenosine Triphosphate 55-58 mitogen-activated protein kinase 1 Homo sapiens 30-33 12657694-7 2003 When extracellular ATP was hydrolyzed by apyrase or ATP/P2 receptors were blocked, injury-induced ERK activation was significantly reduced. Adenosine Triphosphate 19-22 mitogen-activated protein kinase 1 Homo sapiens 98-101 12657694-9 2003 These findings demonstrate for the first time that ATP released by mechanical injury is one of the signals that triggers ERK activation and suggest a role for extracellular ATP, P2 purinergic receptors, and calcium-dependent ERK signaling in the astrocytic response to brain trauma. Adenosine Triphosphate 51-54 mitogen-activated protein kinase 1 Homo sapiens 121-124 12657694-9 2003 These findings demonstrate for the first time that ATP released by mechanical injury is one of the signals that triggers ERK activation and suggest a role for extracellular ATP, P2 purinergic receptors, and calcium-dependent ERK signaling in the astrocytic response to brain trauma. Adenosine Triphosphate 51-54 mitogen-activated protein kinase 1 Homo sapiens 225-228 12056917-9 2002 The data also show that binding of ATP to ERK2/pTpY has no effect on ERK2/pTpY dephosphorylation by HePTP. Adenosine Triphosphate 35-38 mitogen-activated protein kinase 1 Homo sapiens 42-46 12424250-4 2003 Within minutes, ATP treatment resulted in the phosphorylation and activation of p56(lck) kinase, extracellular signal-regulated kinase (ERK), and c-Jun N-terminal kinase but not p38 kinase. Adenosine Triphosphate 16-19 mitogen-activated protein kinase 1 Homo sapiens 97-134 12424250-4 2003 Within minutes, ATP treatment resulted in the phosphorylation and activation of p56(lck) kinase, extracellular signal-regulated kinase (ERK), and c-Jun N-terminal kinase but not p38 kinase. Adenosine Triphosphate 16-19 mitogen-activated protein kinase 1 Homo sapiens 136-139 12239162-6 2002 We found that the antagonism of P2X(1) with ADP or desensitization of this ion channel with alpha,beta-methylene ATP both resulted in impaired ERK2 phosphorylation, ATP secretion, and platelet aggregation induced by low concentrations of collagen (< or = 1 microg/mL) without affecting the minor early dense granule release. Adenosine Triphosphate 113-116 mitogen-activated protein kinase 1 Homo sapiens 143-147 12239162-9 2002 We thus conclude that mild platelet stimulation with collagen rapidly releases ATP, which activates the P2X(1)-PKC-ERK2 pathway. Adenosine Triphosphate 79-82 mitogen-activated protein kinase 1 Homo sapiens 115-119 11839761-7 2002 We have prepared extracellular signal-regulated protein kinase 2 (ERK2) in all phosphorylated forms and kinetically characterized them using two proteins (the myelin basic protein and Elk-1) and ATP as substrates. Adenosine Triphosphate 195-198 mitogen-activated protein kinase 1 Homo sapiens 17-64 11839761-7 2002 We have prepared extracellular signal-regulated protein kinase 2 (ERK2) in all phosphorylated forms and kinetically characterized them using two proteins (the myelin basic protein and Elk-1) and ATP as substrates. Adenosine Triphosphate 195-198 mitogen-activated protein kinase 1 Homo sapiens 66-70 11798872-1 2001 OBJECTIVE: To investigate the mechanism of the activation of signal transduction of ERK induced by purinergic receptor agonist ATP in prostate cancer cells with different metastatic potential. Adenosine Triphosphate 127-130 mitogen-activated protein kinase 1 Homo sapiens 84-87 11641267-6 2001 Exogenous ATP activated the extracellular signal-regulated kinase 1/2 (ERK1/2) mitogen-activated protein kinase (MAPK) pathway, which was blunted by the MAPK/ERK kinase 1/2 (MEK1/2) antagonist PD98059. Adenosine Triphosphate 10-13 mitogen-activated protein kinase 1 Homo sapiens 28-69 11549724-8 2001 Blocking either the ERK1/ERK2 or the p38 pathway (with PD98059 or SB203580, respectively) significantly inhibited Bz-ATP-induced MCP-1 expression. Adenosine Triphosphate 117-120 mitogen-activated protein kinase 1 Homo sapiens 25-29 11549724-8 2001 Blocking either the ERK1/ERK2 or the p38 pathway (with PD98059 or SB203580, respectively) significantly inhibited Bz-ATP-induced MCP-1 expression. Adenosine Triphosphate 117-120 mitogen-activated protein kinase 1 Homo sapiens 37-40 11250936-4 2001 Western blot analysis, using a monoclonal antibody that detected the phosphorylated forms of extracellular signal-regulated kinase-1 and -2 (p42(mapk) and p44 (mapk), respectively), demonstrated that ATP activated MAPK in a dose- and time-dependent manner. Adenosine Triphosphate 200-203 mitogen-activated protein kinase 1 Homo sapiens 93-139 11798872-10 2001 CONCLUSION: The metastatic 1E8 and non-metastatic 2B4 cells show differential response to ATP-induced ERK activation. Adenosine Triphosphate 90-93 mitogen-activated protein kinase 1 Homo sapiens 102-105 11798872-5 2001 ATP activated both ERK1 and ERK2 in 1E8 and 2B4 cells with a time and dose dependent pattern. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 28-32 11798872-8 2001 ATP-stimulated ERK activation was sensitive to treatment with G protein modulator pertussis toxin (PTX) with an inhibitory rate of 50% +/- 3% for 1E8 and 51% +/- 4% for 2B4. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 15-18 10861219-8 2000 Our results reveal the importance of cellular metabolism in ERK activation, and introduce ATP as a novel participant in the mechanisms underlying the ERK cascade. Adenosine Triphosphate 90-93 mitogen-activated protein kinase 1 Homo sapiens 150-153 11158979-5 2001 A similar synergistic stimulation of extracellular signal-regulated kinase (ERK) and mitogen-activated protein or ERK kinase activities was observed (ATP, 7-fold; insulin, 2-fold; and ATP + insulin, 16-fold over basal). Adenosine Triphosphate 150-153 mitogen-activated protein kinase 1 Homo sapiens 37-74 11158979-5 2001 A similar synergistic stimulation of extracellular signal-regulated kinase (ERK) and mitogen-activated protein or ERK kinase activities was observed (ATP, 7-fold; insulin, 2-fold; and ATP + insulin, 16-fold over basal). Adenosine Triphosphate 150-153 mitogen-activated protein kinase 1 Homo sapiens 76-79 11158979-5 2001 A similar synergistic stimulation of extracellular signal-regulated kinase (ERK) and mitogen-activated protein or ERK kinase activities was observed (ATP, 7-fold; insulin, 2-fold; and ATP + insulin, 16-fold over basal). Adenosine Triphosphate 150-153 mitogen-activated protein kinase 1 Homo sapiens 114-117 11158979-5 2001 A similar synergistic stimulation of extracellular signal-regulated kinase (ERK) and mitogen-activated protein or ERK kinase activities was observed (ATP, 7-fold; insulin, 2-fold; and ATP + insulin, 16-fold over basal). Adenosine Triphosphate 184-189 mitogen-activated protein kinase 1 Homo sapiens 37-74 11158979-5 2001 A similar synergistic stimulation of extracellular signal-regulated kinase (ERK) and mitogen-activated protein or ERK kinase activities was observed (ATP, 7-fold; insulin, 2-fold; and ATP + insulin, 16-fold over basal). Adenosine Triphosphate 184-189 mitogen-activated protein kinase 1 Homo sapiens 76-79 11158979-5 2001 A similar synergistic stimulation of extracellular signal-regulated kinase (ERK) and mitogen-activated protein or ERK kinase activities was observed (ATP, 7-fold; insulin, 2-fold; and ATP + insulin, 16-fold over basal). Adenosine Triphosphate 184-189 mitogen-activated protein kinase 1 Homo sapiens 114-117 11016942-2 2001 The structural consequences of dual-phosphorylation in the MAP kinase ERK2 (extracellular signal-regulated kinase 2) include active site closure, alignment of key catalytic residues that interact with ATP, and remodeling of the activation loop. Adenosine Triphosphate 201-204 mitogen-activated protein kinase 1 Homo sapiens 70-74 11016942-2 2001 The structural consequences of dual-phosphorylation in the MAP kinase ERK2 (extracellular signal-regulated kinase 2) include active site closure, alignment of key catalytic residues that interact with ATP, and remodeling of the activation loop. Adenosine Triphosphate 201-204 mitogen-activated protein kinase 1 Homo sapiens 76-115 11158979-10 2001 Thus these results are consistent with ATP relieving an insulin-induced Akt-dependent inhibitory effect on the ERK signaling pathway, leading to synergistic stimulation of CASMC proliferation. Adenosine Triphosphate 39-42 mitogen-activated protein kinase 1 Homo sapiens 111-114 10997919-9 2000 Post-ATP depletion, phosphorylation of ERK1/ERK2 was reduced to 36 +/- 9/51 +/- 14% vs. 9 +/- 5/7 +/- 6% in NG (P < 0.05, n = 5). Adenosine Triphosphate 5-8 mitogen-activated protein kinase 1 Homo sapiens 44-48 10821702-9 2000 Furthermore, MBP binds to the ERK2 x ATP complex at least 1500-fold more tightly than does ERKtide (K(d(ERKtide)) >/= 1.5 mM). Adenosine Triphosphate 37-40 mitogen-activated protein kinase 1 Homo sapiens 30-34 9827991-4 1998 Crystal structures of two pyridinyl imidazoles complexed with p38 revealed these compounds bind in the ATP site. Adenosine Triphosphate 103-106 mitogen-activated protein kinase 1 Homo sapiens 62-65 9843424-5 1998 Three active site ATP-binding domain residues in p38, T106, M109, and A157, selected based on primary sequence alignment, molecular modeling, and X-ray crystal structure data, were mutated to assess their role in inhibitor binding and enzymatic catalysis. Adenosine Triphosphate 18-21 mitogen-activated protein kinase 1 Homo sapiens 49-52 9746468-4 1998 ATP binding to a UTP-sensitive P2Y nucleotide receptor activates ERK1/ERK2 in a time- and dose-dependent manner in coronary artery smooth muscle cells (CASMC). Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 70-74 9746468-5 1998 ATP-induced activation of ERK1/ERK2 is dependent on the dual-specificity kinase mitogen-activated protein kinase/ERK kinase (i.e., MEK) but independent of phosphatidylinositol 3-kinase (PI3K) activity. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 31-35 9746468-0 1998 ATP-stimulated smooth muscle cell proliferation requires independent ERK and PI3K signaling pathways. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 69-72 9746468-3 1998 We have studied the effect of extracellular ATP on ERK activation and cell proliferation. Adenosine Triphosphate 44-47 mitogen-activated protein kinase 1 Homo sapiens 51-54 9746468-5 1998 ATP-induced activation of ERK1/ERK2 is dependent on the dual-specificity kinase mitogen-activated protein kinase/ERK kinase (i.e., MEK) but independent of phosphatidylinositol 3-kinase (PI3K) activity. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 26-29 9746468-7 1998 Thus ATP-stimulation of CASMC proliferation requires independent activation of both the ERK and PI3K signaling pathways. Adenosine Triphosphate 5-8 mitogen-activated protein kinase 1 Homo sapiens 88-91 9517568-12 1998 Similarly, ATP or TPA promoted AA release was inhibited by the mitogen-activated protein kinase (MAPK) cascade inhibitor PD 98059. Adenosine Triphosphate 11-14 mitogen-activated protein kinase 1 Homo sapiens 97-101 9517568-13 1998 ATP, TPA, or A23187 induced an increase in the activity and tyrosine phosphorylation of p42 MAPK, as well as a molecular weight shift, consistent with phosphorylation, of cytosolic phospholipase A2 (cPLA2). Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 88-96 9517568-14 1998 ATP- and TPA-stimulated activation of p42 MAPK activity and tyrosine phosphorylation were inhibited by long-term TPA treatment, while A23187-stimulated effects were completely blocked. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 42-46 8947491-5 1996 By using separation on Resource Q columns, peptide kinase activity associated with the phosphorylated MAPK enzymes distributes into two peaks, one mainly p42mapk and one mainly p44mapk, both of which are stimulated by ATP with respect to kinase activity and phospho-MAPK immunoreactivity. Adenosine Triphosphate 218-221 mitogen-activated protein kinase 1 Homo sapiens 154-161 9530930-7 1998 An inhibitor of the MAPK activator MEK, PD 098059, effectively blocked ATP- and 2-chloroadenosine-induced DNA synthesis, thereby indicating that the ERK/MAPK cascade mediates mitogenic signaling by P2 and P1 purinergic receptors in human fetal astrocytes. Adenosine Triphosphate 71-74 mitogen-activated protein kinase 1 Homo sapiens 149-152 9755813-2 1998 In these cells, it has been shown that ATP stimulates myelin basic protein (MBP) kinase activity which is believed to represent the Erk family of MAP kinases. Adenosine Triphosphate 39-42 mitogen-activated protein kinase 1 Homo sapiens 132-135 9755813-3 1998 Indeed, we show that ATP activates simultaneously MBP kinase activity and phosphotyrosine incorporation in p42 Erk2 and p44 Erk1. Adenosine Triphosphate 21-24 mitogen-activated protein kinase 1 Homo sapiens 111-115 9530930-3 1998 In addition, ATP activated a mitogen-activated protein kinase (MAPK) termed ERK (extracellular signal-regulated protein kinase), a key component of signal transduction pathways involved in cellular proliferation and differentiation. Adenosine Triphosphate 13-16 mitogen-activated protein kinase 1 Homo sapiens 76-79 9530930-3 1998 In addition, ATP activated a mitogen-activated protein kinase (MAPK) termed ERK (extracellular signal-regulated protein kinase), a key component of signal transduction pathways involved in cellular proliferation and differentiation. Adenosine Triphosphate 13-16 mitogen-activated protein kinase 1 Homo sapiens 81-126 9122194-3 1997 The peptide substrate binding site and the ATP binding site are also different from those of ERK2. Adenosine Triphosphate 43-46 mitogen-activated protein kinase 1 Homo sapiens 93-97 34583590-6 2021 Analogues maintaining key interactions with amino acid residues in the ATP-binding domain of ERK2 were selected and duly synthesized. Adenosine Triphosphate 71-74 mitogen-activated protein kinase 1 Homo sapiens 93-97 8639522-0 1996 Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5"-triphosphate. Adenosine Triphosphate 73-98 mitogen-activated protein kinase 1 Homo sapiens 27-31 8639522-7 1996 The three-dimensional structure of unphosphorylated K52R ERK2 in the absence and presence of bound ATP was determined and compared with the structure of unphosphorylated wild-type ERK2. Adenosine Triphosphate 99-102 mitogen-activated protein kinase 1 Homo sapiens 57-61 8639522-8 1996 ATP adopted a well-defined but distinct binding mode in K52R ERK2 compared to the binding mode in the wild-type enzyme. Adenosine Triphosphate 0-3 mitogen-activated protein kinase 1 Homo sapiens 61-65 1378617-2 1992 Structural analyses were performed to identify the site(s) of tyrosine phosphorylation of recombinant p42mapk, both during expression of the protein in E. coli and during in vitro incubations with ATP/Mg2+/Mn2+. Adenosine Triphosphate 197-200 mitogen-activated protein kinase 1 Homo sapiens 102-109 7536808-3 1995 A subpopulation of ERK2 species in soluble brain fractions can be efficiently phosphorylated and activated in cell-free systems, simply by adding Mg(2+)-ATP. Adenosine Triphosphate 153-156 mitogen-activated protein kinase 1 Homo sapiens 19-23 1628739-2 1992 Tyr- but not Thr-phosphorylated p42mapk, accumulates when ATP is limiting. Adenosine Triphosphate 58-61 mitogen-activated protein kinase 1 Homo sapiens 32-39 34833046-0 2021 Extracellular ATP Induced S-Phase Cell Cycle Arrest via P2Y Receptor-Activated ERK Signaling in Poorly Differentiated Oral Squamous Cell Carcinoma SAS Cells. Adenosine Triphosphate 14-17 mitogen-activated protein kinase 1 Homo sapiens 79-82 34833046-5 2021 Western blotting and flow cytometry analyses revealed that ATP phosphorylated ERK and elevated intracellular calcium signaling in all tested cell lines. Adenosine Triphosphate 59-62 mitogen-activated protein kinase 1 Homo sapiens 78-81 34833046-8 2021 Overall, we postulate that the ATP-induced S-phase arrest effect in SAS cells may be regulated through P2Y receptor-mediated ERK signaling, thus suggesting a potential antitumor effect of ATP via interaction with its distinct profile of P2Y receptors. Adenosine Triphosphate 31-34 mitogen-activated protein kinase 1 Homo sapiens 125-128 34833046-8 2021 Overall, we postulate that the ATP-induced S-phase arrest effect in SAS cells may be regulated through P2Y receptor-mediated ERK signaling, thus suggesting a potential antitumor effect of ATP via interaction with its distinct profile of P2Y receptors. Adenosine Triphosphate 188-191 mitogen-activated protein kinase 1 Homo sapiens 125-128 35439648-8 2022 We observe that ectopic ATP synthase is located on the surface of MSCs and excreted extracellular ATP into the lung cancer microenvironment to trigger the ERK/phospho-c-Fos-S374 pathway, which is consistent with these previous findings. Adenosine Triphosphate 98-101 mitogen-activated protein kinase 1 Homo sapiens 155-158 33290316-11 2021 Our data suggest that LY294002 may directly inhibit the activation of MEK and ERK by its ability to bind to the ATP-binding site of the MAPK molecules. Adenosine Triphosphate 112-115 mitogen-activated protein kinase 1 Homo sapiens 78-81 34507982-8 2021 The ATP binding status of MEK1 or ERK2 affected arrestin-2 binding; ATP-bound MEK1 interacted with arrestin-2, whereas only empty ERK2 bound arrestin-2. Adenosine Triphosphate 4-7 mitogen-activated protein kinase 1 Homo sapiens 34-38 35566048-6 2022 The results indicated that DHCE obviously inhibited the kinase activity of ERK2 via targeting its ATP-binding domain, destroyed F-actin microfilament, and reduced the expression levels of Ras, p-c-Raf, ERK, p-ERK, and MMP9 proteins. Adenosine Triphosphate 98-101 mitogen-activated protein kinase 1 Homo sapiens 75-79 35439648-9 2022 Our results suggest that ectopic ATP synthase on the surface of MSCs releases extracellular ATP into the tumor microenvironment, which promotes cancer progression via activation of the ERK/phospho-c-Fos-S374 pathway. Adenosine Triphosphate 92-95 mitogen-activated protein kinase 1 Homo sapiens 185-188 35063772-0 2022 Identification of a novel target site for ATP-independent ERK2 inhibitors. Adenosine Triphosphate 42-45 mitogen-activated protein kinase 1 Homo sapiens 58-62 35074408-7 2022 After OPG treatment, the expression of P2X7R significantly reduced, the ATP level and Ca2+-ATPase activity decreased rapidly, and concomitantly suppressed calcium and MAPK signaling. Adenosine Triphosphate 72-75 mitogen-activated protein kinase 1 Homo sapiens 167-171 34987637-7 2022 Results: We demonstrated a distinct mechanism in which Hsp90 inhibitors that block N-terminal ATP-binding pocket causes transcriptional upregulation of Wnt ligands through Akt- and ERK-mediated activation of STAT3, resulting in NSCLC cell survival in an autocrine or paracrine manner. Adenosine Triphosphate 94-97 mitogen-activated protein kinase 1 Homo sapiens 181-184