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- W69377524 endingPage "137" @default.
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- W69377524 abstract "The process of reversible tyrosine phosphorylation is a key regulatory mechanism in eukaryotic cells for controlling events in cell growth, differentiation and activation.1,2 The level of protein tyrosine phosphorylation within a cell reflects a dynamic balance between the often competing activities of the protein tyrosine kinases that phosphorylate proteins and the protein tyrosine phosphatases (PTPs) that dephosphorylate them. It is the shift in this balance brought on by microenvironmental cues that determines the phosphorylation status of a protein at any given time. In this chapter, an analysis is provided of the PTPs that are likely to be involved in the signaling pathways initiated by aggregating the high affinity IgE receptors (FcεRI) on mast cells and basophils. To be sure, relatively little work has been done in this area up to now. But that should be interpreted as an indication of just how open to exploration this area of investigation is." @default.
- W69377524 created "2016-06-24" @default.
- W69377524 creator A5071179362 @default.
- W69377524 date "1997-01-01" @default.
- W69377524 modified "2023-09-23" @default.
- W69377524 title "Protein Tyrosine Phosphatases in Signaling Through the FcεRI on Mast Cells and Basophils" @default.
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- W69377524 doi "https://doi.org/10.1007/978-3-662-22022-1_7" @default.
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