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- W23025822 abstract "Mitogen-activated protein kinases (MAPKs) are a family of serine, threonine phosphorelay enzymes activated by cytokines, growth factors, stress, immune receptors and G-protein coupled receptors (GPCRs). The three major MAPK families, whose regulation and function have been conserved during evolution in eukaryotic cells, are extracellular signal-regulated protein kinase (ERK), c-Jun NH2-terminal kinase (JNK) and p38. In inflammatory cells such as macrophages, stimulation of selected Toll family receptors like TLR4 by microbial pathogens or other immunogenic factors leads to the activation of the ERK pathway. Stimulation of TLR4 activates Tpl-2, a MKKK, which phosphorylates and activates MEK1/2 (MKK1/2) leading to the activation of ERK1/2. Activated ERK1/2 regulates expression of tumor necrosis factor-α(TNFα) and other cytokines, which are the key mediators of inflammation and immune responses. The ERK pathway can also be activated in other cell types, by binding of a growth factor such as epidermal growth factor (EGF) to its receptor resulting in the activation of Ras which then activates Raf serine/threonine kinase. The stimulus- and location-selective activation of the p38 MAPK pathway is also controlled by the scaffolding proteins—TAB1 and OSM." @default.
- W23025822 created "2016-06-24" @default.
- W23025822 creator A5052715687 @default.
- W23025822 date "2007-01-01" @default.
- W23025822 modified "2023-09-23" @default.
- W23025822 title "Chapter 17 MAP Kinase Inhibitors in Inflammation and Autoimmune Disorders" @default.
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- W23025822 doi "https://doi.org/10.1016/s0065-7743(07)42017-6" @default.
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