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- W2020184457 abstract "The magnitude and duration of signalling through mitogen- and stress-activated kinases are critical determinants of biological effect. This reflects a balance between the activities of upstream activators and a complex regulatory network of protein phosphatases. These mitogen-activated protein kinase phosphatases include both dual-specificity (threonine/tyrosine) and tyrosine-specific enzymes, and recent evidence suggests that a single mitogen-activated protein kinase isoform may be acted upon by both classes of protein phosphatase. In both cases, substrate selectivity is determined by specific protein-protein interactions mediated through noncatalytic amino-terminal mitogen-activated protein kinase binding domains. Future challenges include the determination of exactly how this network of protein phosphatases interacts selectively with mitogen-activated protein kinase signalling complexes to achieve precise regulation of these key pathways in mammalian cells." @default.
- W2020184457 created "2016-06-24" @default.
- W2020184457 creator A5033321035 @default.
- W2020184457 date "2000-04-01" @default.
- W2020184457 modified "2023-10-16" @default.
- W2020184457 title "Protein phosphatases and the regulation of mitogen-activated protein kinase signalling" @default.
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- W2020184457 doi "https://doi.org/10.1016/s0955-0674(99)00075-7" @default.
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