PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11425486-3 2001 Depending on their concentrations, GO and MGO promoted phosphorylations of ERK1 and ERK2, which were blocked by the protein-tyrosine kinase (PTK) inhibitors herbimycin A and staurosporine, thereby being PTK-dependent. Pyruvaldehyde 42-45 mitogen-activated protein kinase 3 Homo sapiens 75-79 26021238-6 2015 Signaling kinetic observation indicated that MGO remarkably triggered phosphorylation of Akt, ERK1/2, p38 MAPK, and JNK1/2. Pyruvaldehyde 45-48 mitogen-activated protein kinase 3 Homo sapiens 94-100 26021238-7 2015 Blockade of kinase activity demonstrated that the hyperphosphorylation of Akt, ERK1/2, JNK, and p38 MAPK were all involved in the MGO-enhanced autophagy and growth-arresting effect in ARPE-19 cells. Pyruvaldehyde 130-133 mitogen-activated protein kinase 3 Homo sapiens 79-85 26021238-7 2015 Blockade of kinase activity demonstrated that the hyperphosphorylation of Akt, ERK1/2, JNK, and p38 MAPK were all involved in the MGO-enhanced autophagy and growth-arresting effect in ARPE-19 cells. Pyruvaldehyde 130-133 mitogen-activated protein kinase 3 Homo sapiens 100-104 11425486-9 2001 These results demonstrated that GO and MGO triggered two distinct signal cascades, one for PTK-dependent control of ERK and another for PTK-independent redox-linked activation of JNK/p38 MAPK and caspases in HUVECs, depending on the structure of the carbon skeleton of the chemicals. Pyruvaldehyde 39-42 mitogen-activated protein kinase 3 Homo sapiens 187-191 31369791-5 2019 Quantitative RT-PCR revealed that bergenin decreased the expression of ERK1, Akt2, MMP-9, and OSTM1 genes in the presence of MG. Pyruvaldehyde 125-127 mitogen-activated protein kinase 3 Homo sapiens 71-75 28000163-9 2017 Therefore, PB activated the Erk1/2-Nrf2 signaling pathway resulting in mitochondrial protection in SH-SY5Y cells exposed to MG. Pyruvaldehyde 124-126 mitogen-activated protein kinase 3 Homo sapiens 28-34 17174344-10 2007 MG-AGE-induced phosphorylation of ERK1/2 and p38 was nullified by neutralizing AGE with specific anti-AGE antibody but not nonspecific antiserum. Pyruvaldehyde 0-2 mitogen-activated protein kinase 3 Homo sapiens 34-40 11425486-4 2001 GO and MGO also induced phosphorylations of JNK, p38 MAPK, and c-Jun, either PTK-dependently (GO) or -independently (MGO). Pyruvaldehyde 7-10 mitogen-activated protein kinase 3 Homo sapiens 53-57 11425486-4 2001 GO and MGO also induced phosphorylations of JNK, p38 MAPK, and c-Jun, either PTK-dependently (GO) or -independently (MGO). Pyruvaldehyde 117-120 mitogen-activated protein kinase 3 Homo sapiens 53-57 11425486-6 2001 Curcumin and SB203580, which inhibit JNK and p38 MAPK signaling pathways, but not herbimycin A/staurosporine, prevented the MGO-induced PARP degradation. Pyruvaldehyde 124-127 mitogen-activated protein kinase 3 Homo sapiens 49-53 32746708-8 2021 Additionally, GO and MGO significantly activated extracellular signal-regulated kinase 1/2 (ERK1/2), p38 MAPK, and NF-kappaB. Pyruvaldehyde 21-24 mitogen-activated protein kinase 3 Homo sapiens 92-98 32746708-9 2021 Whether ERK1/2, p38 MAPK, and NF-kappaB signaling pathway were involved in GO and MGO-induced production of pro-inflammatory cytokines (IL-1beta and IL-6) and MUC5AC/5B, we used specific inhibitors and siRNA transfection. Pyruvaldehyde 82-85 mitogen-activated protein kinase 3 Homo sapiens 8-14 32746708-11 2021 CONCLUSIONS: GO and MGO induced pro-inflammatory cytokines and MUC5AC/5B expression via ERK1/2, p38 MAPK, and NF-kappaB in human nasal epithelial cells. Pyruvaldehyde 20-23 mitogen-activated protein kinase 3 Homo sapiens 88-94