PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 14567689-12 2003 In addition, the model suggests that in the presence of saturating concentrations of both magnesium and substrates ERK2 subunits dissociate with a dissociation constant (K(d)) of 32 +/- 16 nM. Magnesium 90-99 mitogen-activated protein kinase 1 Homo sapiens 115-119 19027753-11 2009 These results suggest that the inhibition of ERK phosphorylation is an essential intermediate in the effects of FK506 on magnesium. Magnesium 121-130 mitogen-activated protein kinase 1 Homo sapiens 45-48 15023352-0 2004 A kinetic approach towards understanding substrate interactions and the catalytic mechanism of the serine/threonine protein kinase ERK2: identifying a potential regulatory role for divalent magnesium. Magnesium 190-199 mitogen-activated protein kinase 1 Homo sapiens 131-135 15023352-6 2004 Here we review several steady-state kinetic experiments that reveal details of the ERK2 mechanism and a hitherto unknown process of ERK2 activation by free magnesium. Magnesium 156-165 mitogen-activated protein kinase 1 Homo sapiens 132-136 32411326-0 2020 MicroRNA-16, via FGF2 Regulation of the ERK/MAPK Pathway, Is Involved in the Magnesium-Promoted Osteogenic Differentiation of Mesenchymal Stem Cells. Magnesium 77-86 mitogen-activated protein kinase 1 Homo sapiens 40-43 12627962-7 2003 The velocity dependence on magnesium at saturating concentrations of the protein substrate, Ets138, over a range of ATP4- and Mg2+ ion concentrations, supports the notion that magnesium is an essential activator of ERK2. Magnesium 176-185 mitogen-activated protein kinase 1 Homo sapiens 215-219 11812784-5 2002 The kinetic mechanism of ERK2 was examined, with excess magnesium, by initial velocity measurements, both in the absence and presence of products at 27 degrees C, pH 7.5, and ionic strength 0.1 m (KCl). Magnesium 56-65 mitogen-activated protein kinase 1 Homo sapiens 25-29 12627962-0 2003 Physiological concentrations of divalent magnesium ion activate the serine/threonine specific protein kinase ERK2. Magnesium 41-50 mitogen-activated protein kinase 1 Homo sapiens 109-113 12627962-6 2003 Now we provide kinetic evidence that ERK2 must bind two divalent magnesium ions to facilitate catalysis at a physiologically relevant rate, because a second magnesium ion promotes both MgATP2- binding and phosphoryl transfer. Magnesium 65-74 mitogen-activated protein kinase 1 Homo sapiens 37-41 12627962-6 2003 Now we provide kinetic evidence that ERK2 must bind two divalent magnesium ions to facilitate catalysis at a physiologically relevant rate, because a second magnesium ion promotes both MgATP2- binding and phosphoryl transfer. Magnesium 157-166 mitogen-activated protein kinase 1 Homo sapiens 37-41 12627962-7 2003 The velocity dependence on magnesium at saturating concentrations of the protein substrate, Ets138, over a range of ATP4- and Mg2+ ion concentrations, supports the notion that magnesium is an essential activator of ERK2. Magnesium 27-36 mitogen-activated protein kinase 1 Homo sapiens 215-219 31161622-0 2019 High concentration magnesium inhibits extracellular matrix calcification and protects articular cartilage via Erk/autophagy pathway. Magnesium 19-28 mitogen-activated protein kinase 1 Homo sapiens 110-113 31823825-0 2019 Magnesium-enriched microenvironment promotes odontogenic differentiation in human dental pulp stem cells by activating ERK/BMP2/Smads signaling. Magnesium 0-9 mitogen-activated protein kinase 1 Homo sapiens 119-122 31823825-13 2019 Consistently, ERK and BMP2/Smads pathways were activated in DPSCs treated with high extracellular Mg2+. Magnesium 98-102 mitogen-activated protein kinase 1 Homo sapiens 14-17 31823825-14 2019 In agreement, ERK signaling inhibition by U0126 blunted the effect of high extracellular Mg2+ on mineralization and odontogenic differentiation in DPSCs. Magnesium 89-93 mitogen-activated protein kinase 1 Homo sapiens 14-17 31823825-16 2019 CONCLUSIONS: Mg2+-enriched microenvironment promotes odontogenic differentiation in DPSCs by activating ERK/BMP2/Smads signaling via intracellular Mg2+ increase. Magnesium 13-16 mitogen-activated protein kinase 1 Homo sapiens 104-107 31823825-16 2019 CONCLUSIONS: Mg2+-enriched microenvironment promotes odontogenic differentiation in DPSCs by activating ERK/BMP2/Smads signaling via intracellular Mg2+ increase. Magnesium 13-17 mitogen-activated protein kinase 1 Homo sapiens 104-107 32254870-7 2018 These results demonstrated that the degradation of Mg was able to promote the proliferation and differentiation of osteoblasts, which may be related to the newly created alkaline microenvironment and the osteogenesis potential of released Mg2+ through the MAPK/ERK signaling pathway. Magnesium 51-53 mitogen-activated protein kinase 1 Homo sapiens 261-264 29853102-6 2018 Moreover, Mg element could promote osteogenic differentiation through ERK/MAPK pathway and the maximum concentration was about the range between 200 and 500 ppm. Magnesium 10-12 mitogen-activated protein kinase 1 Homo sapiens 70-73 29853102-6 2018 Moreover, Mg element could promote osteogenic differentiation through ERK/MAPK pathway and the maximum concentration was about the range between 200 and 500 ppm. Magnesium 10-12 mitogen-activated protein kinase 1 Homo sapiens 74-78 28030988-0 2018 Functional roles of magnesium binding to extracellular signal-regulated kinase 2 explored by molecular dynamics simulations and principal component analysis. Magnesium 20-29 mitogen-activated protein kinase 1 Homo sapiens 41-80 29516972-6 2018 Conclusions: LPS promoted the growth of MG-63 cells through the ERK pathway. Magnesium 40-42 mitogen-activated protein kinase 1 Homo sapiens 64-67 21705076-11 2011 Briefly, Ca, Mg and Si ions extracted from akermanite in the concentrations of 2.36, 1.11, 1.03 mM, respectively, could facilitate the osteogenic differentiation of hASCs via an ERK pathway, and suppress the proliferation of hASCs without significant cytotoxicity. Magnesium 13-15 mitogen-activated protein kinase 1 Homo sapiens 178-181 21506533-1 2011 The extracellular signal-regulated protein kinase, ERK2, fully activated by phosphorylation and without a His(6) tag, shows little tendency to dimerize with or without either calcium or magnesium ions when analyzed by light scattering or analytical ultracentrifugation. Magnesium 186-195 mitogen-activated protein kinase 1 Homo sapiens 51-55