PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26683671-6 2016 The subsequent in vitro experiments showed that H2 treatment inhibited the phosphorylation of extracellular signal-regulated kinase (ERK), c-jun N-terminal kinase (JNK), and p38 MAPK, and activated NF-kappaB and the expression of tumor necrosis factor alpha and interleukin-1beta, while simultaneously preventing the translocation of phospho-ERK, phospho-JNK, and phospho-p38 from the cytoplasm to the nucleus. Hydrogen 48-50 mitogen-activated protein kinase 1 Homo sapiens 94-131 34507982-6 2021 Here, we investigated the mechanism of arrestin-2 scaffolding of cRaf, MEK1, and ERK2 using hydrogen/deuterium exchange-mass spectrometry, tryptophan-induced bimane fluorescence quenching, and NMR. Hydrogen 92-100 mitogen-activated protein kinase 1 Homo sapiens 81-85 31284641-6 2019 This new conformation is modulated by the irregularly structured C-terminal tail when it first recognizes and binds to ERK2 at the d-peptide recruitment site (DRS) in an allosteric manner, and is facilitated by the rearrangement of the surface electrostatic and hydrogen-bonding interactions on the DED. Hydrogen 262-270 mitogen-activated protein kinase 1 Homo sapiens 119-123 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. Hydrogen 149-157 mitogen-activated protein kinase 1 Homo sapiens 45-49 29988358-11 2018 Conclusions: Our results suggest that it is the first time to report the compound-1H with benzimidazoleisoquinolinone core playing antitumor activity in human glioblastoma cells by inhibiting Raf/MEK/ERK and PI3K/AKT signaling pathways, and it could be as a lead compound for the further development of targeted glioblastoma cancer therapy. Hydrogen 82-84 mitogen-activated protein kinase 1 Homo sapiens 200-203 27329786-5 2016 De novo design efforts of a novel scaffold derived from SCH772984 by employing hydrogen bond interactions specific for ERK in the binding pocket identified 1-(1H-pyrazolo[4,3-c]pyridin-6-yl)ureas as a viable lead series. Hydrogen 79-87 mitogen-activated protein kinase 1 Homo sapiens 119-122 26683671-6 2016 The subsequent in vitro experiments showed that H2 treatment inhibited the phosphorylation of extracellular signal-regulated kinase (ERK), c-jun N-terminal kinase (JNK), and p38 MAPK, and activated NF-kappaB and the expression of tumor necrosis factor alpha and interleukin-1beta, while simultaneously preventing the translocation of phospho-ERK, phospho-JNK, and phospho-p38 from the cytoplasm to the nucleus. Hydrogen 48-50 mitogen-activated protein kinase 1 Homo sapiens 133-136 26683671-6 2016 The subsequent in vitro experiments showed that H2 treatment inhibited the phosphorylation of extracellular signal-regulated kinase (ERK), c-jun N-terminal kinase (JNK), and p38 MAPK, and activated NF-kappaB and the expression of tumor necrosis factor alpha and interleukin-1beta, while simultaneously preventing the translocation of phospho-ERK, phospho-JNK, and phospho-p38 from the cytoplasm to the nucleus. Hydrogen 48-50 mitogen-activated protein kinase 1 Homo sapiens 342-345 26683671-9 2016 In conclusion, H2 treatment can ameliorate the inflammatory response and reduce the expression of inflammatory mediators during the early phase of AP by inhibiting the MAPK pathways and increasing Hsc70 expression. Hydrogen 15-17 mitogen-activated protein kinase 1 Homo sapiens 168-172 23827636-11 2013 Phospho-ERK was activated by 50 muM PS at 30 min and 1h in growth medium. Hydrogen 53-55 mitogen-activated protein kinase 1 Homo sapiens 8-11 26875562-7 2016 Hydrogen treatment also blocked Ang II-induced phosphorylation of the extracellular signal-regulated kinase1/2 (ERK1/2), p38 MAPK, c-Jun NH2-terminal kinase (JNK) and the ezrin/radixin/moesin (ERM) in vitro. Hydrogen 0-8 mitogen-activated protein kinase 1 Homo sapiens 70-110 26875562-7 2016 Hydrogen treatment also blocked Ang II-induced phosphorylation of the extracellular signal-regulated kinase1/2 (ERK1/2), p38 MAPK, c-Jun NH2-terminal kinase (JNK) and the ezrin/radixin/moesin (ERM) in vitro. Hydrogen 0-8 mitogen-activated protein kinase 1 Homo sapiens 121-124 26875562-8 2016 Taken together, our studies indicate that hydrogen prevents AAC-induced vascular hypertrophy in vivo, and inhibits Ang II-induced proliferation and migration of VSMCs in vitro possibly by targeting ROS-dependent ERK1/2, p38 MAPK, JNK and ERM signaling. Hydrogen 42-50 mitogen-activated protein kinase 1 Homo sapiens 220-223 24534729-2 2014 Studies of the mitogen-activated protein kinase ERK2 (extracellular-regulated protein kinase 2) by hydrogen-exchange mass spectrometry suggest that activation enhances backbone flexibility at the linker between N- and C-terminal domains while altering nucleotide binding mode. Hydrogen 99-107 mitogen-activated protein kinase 1 Homo sapiens 48-52 24534729-2 2014 Studies of the mitogen-activated protein kinase ERK2 (extracellular-regulated protein kinase 2) by hydrogen-exchange mass spectrometry suggest that activation enhances backbone flexibility at the linker between N- and C-terminal domains while altering nucleotide binding mode. Hydrogen 99-107 mitogen-activated protein kinase 1 Homo sapiens 54-94 23247439-10 2013 Autodock simulations predicted that TMP could directly bind to ERK2 with two hydrogen bonds and low energy score, indicating that ERK2 could be a direct target molecule for TMP within HSCs. Hydrogen 77-85 mitogen-activated protein kinase 1 Homo sapiens 63-67 23247439-10 2013 Autodock simulations predicted that TMP could directly bind to ERK2 with two hydrogen bonds and low energy score, indicating that ERK2 could be a direct target molecule for TMP within HSCs. Hydrogen 77-85 mitogen-activated protein kinase 1 Homo sapiens 130-134 18501927-0 2008 Hydrogen-exchange mass spectrometry reveals activation-induced changes in the conformational mobility of p38alpha MAP kinase. Hydrogen 0-8 mitogen-activated protein kinase 1 Homo sapiens 105-108 16185715-0 2005 Hydrogen exchange solvent protection by an ATP analogue reveals conformational changes in ERK2 upon activation. Hydrogen 0-8 mitogen-activated protein kinase 1 Homo sapiens 90-94 17407569-7 2007 Amide hydrogen-deuterium experiments on the free and p41-bound R21A Spc-SH3 domain indicate that binding elicits a strong reduction in the conformational flexibility of the domain. Hydrogen 6-14 mitogen-activated protein kinase 1 Homo sapiens 53-56 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. Hydrogen 175-183 mitogen-activated protein kinase 1 Homo sapiens 35-39 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. Hydrogen 175-183 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. Hydrogen 175-183 mitogen-activated protein kinase 1 Homo sapiens 117-121 17046812-0 2006 Mapping ERK2-MKP3 binding interfaces by hydrogen/deuterium exchange mass spectrometry. Hydrogen 40-48 mitogen-activated protein kinase 1 Homo sapiens 8-12 17046812-3 2006 To understand the molecular basis of ERK2 recognition by MKP3, we carried out hydrogen/deuterium exchange mass spectrometry experiments to map the interaction surfaces between the two proteins. Hydrogen 78-86 mitogen-activated protein kinase 1 Homo sapiens 37-41 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. Hydrogen 19-27 mitogen-activated protein kinase 1 Homo sapiens 168-172 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. Hydrogen 59-67 mitogen-activated protein kinase 1 Homo sapiens 37-41 16185715-3 2005 Mass spectrometry was used to probe changes in hydrogen/deuterium exchange in the MAP kinase, ERK2, in the presence and absence of the ATP analogue, AMP-PNP. Hydrogen 47-55 mitogen-activated protein kinase 1 Homo sapiens 94-98 15698891-5 2005 ERK-like activation was found 1h after spaced training in cytosolic but not in nuclear fractions of brain homogenates, while JNK activity remained unchanged in both fractions. Hydrogen 30-32 mitogen-activated protein kinase 1 Homo sapiens 0-3 15698891-8 2005 These data support that: (1) cytoplasmic but not nuclear ERK substrates must be differentially phosphorylated during memory consolidation, and (2) ERK phosphorylation and consequent activation 1h after training is necessary for long-term memory consolidation in this arthropod model. Hydrogen 193-195 mitogen-activated protein kinase 1 Homo sapiens 147-150