An overview of mammalian p38 mitogen-activated protein kinases, central regulators of cell stress and receptor signaling. [PDF]
F1000Res, 2020 The p38 family is a highly evolutionarily conserved group of mitogen-activated protein kinases (MAPKs) that is involved in and helps co-ordinate cellular responses to nearly all stressful stimuli.
Han J, Wu J, Silke J.
europepmc +2 more sources
Roles of Mitogen-Activated Protein Kinases in Osteoclast Biology. [PDF]
Int J Mol Sci, 2018 Bone undergoes continuous remodeling, which is homeostatically regulated by concerted communication between bone-forming osteoblasts and bone-degrading osteoclasts.
Lee K, Seo I, Choi MH, Jeong D.
europepmc +2 more sources
Inferring Compensatory Kinase Networks in Yeast using Prolog [PDF]
EPTCS 385, 2023, pp. 260-273, 2023 Signalling pathways are conserved across different species, therefore making yeast a model organism to study these via disruption of kinase activity. Yeast has 159 genes that encode protein kinases and phosphatases, and 136 of these have counterparts in humans.
arxiv +1 more source
The Regulation of AP-1 Activity by Mitogen-activated Protein Kinases (*)
Journal of Biological Chemistry, 1995 AP-1 is a collection of dimeric sequence specific, DNA binding, transcriptional activators composed ofJun and Fos subunits. The composition, the level and the activity of AP1 complexes are regulated in response to extracellular stimuli. An important role
M. Karin
semanticscholar +1 more source
Regulation of signal duration and the statistical dynamics of kinase activation by scaffold proteins [PDF]
PLoS Comput Biol. 2008 Jun 27;4(6):e1000099, 2008 Scaffolding proteins that direct the assembly of multiple kinases into a spatially localized signaling complex are often essential for the maintenance of an appropriate biological response. Although scaffolds are widely believed to have dramatic effects on the dynamics of signal propagation, the mechanisms that underlie these consequences are not well ...
arxiv +1 more source
Resolving the binding-kinase discrepancy in bacterial chemotaxis: A nonequilibrium allosteric model and the role of energy dissipation [PDF]
Proc. Natl. Acad. Sci. U.S.A. 120, e2303115120 (2023), 2023 The Escherichia coli chemotaxis signaling pathway has served as a model system for studying the adaptive sensing of environmental signals by large protein complexes. The chemoreceptors control the kinase activity of CheA in response to the extracellular ligand concentration and adapt across a wide concentration range by undergoing methylation and ...
arxiv +1 more source
Mitogen-Activated Protein Kinases and Reactive Oxygen Species: How Can ROS Activate MAPK Pathways?
Journal of signal transduction, 2011 Mitogen-activated protein kinases (MAPKs) are serine-threonine protein kinases that play the major role in signal transduction from the cell surface to the nucleus.
Yong Son +5 more
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Advance in Reversible Covalent Kinase Inhibitors [PDF]
arXiv, 2021 Reversible covalent kinase inhibitors (RCKIs) are a class of novel kinase inhibitors attracting increasing attention because they simultaneously show the selectivity of covalent kinase inhibitors, yet avoid permanent protein-modification-induced adverse effects.
arxiv
Positional information readout in $Ca^{2+}$ signaling [PDF]
Phys. Rev. Lett. 123, 058102 (2019), 2017 Living cells respond to spatial signals. Signal transmission to the cell interior often involves the release of second messengers like $Ca^{2+}$ . They will eventually trigger a physiological response by activating kinases that in turn activate target proteins through phosphorylation. Here, we investigate theoretically how positional information can be
arxiv +1 more source
Mitogen-activated protein kinases p42mapk and p44mapk are required for fibroblast proliferation.
Proceedings of the National Academy of Sciences of the United States of America, 1993 The mitogen-activated protein kinases (MAP kinases) p42mapk and p44mapk are serine/threonine kinases rapidly activated in cells stimulated with various extracellular signals by dual phosphorylation of tyrosine and threonine residues.
G. Pagès +5 more
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