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- W1589566049 abstract "A bewildering array of receptor and nonreceptor protein tyrosine kinases have been uncovered during the past two decades. During this time it has become clear that the autophosphorylation of these protein kinases on tyrosine residues has two major effects on their function. First, the phosphorylation event often enhances the activity of the protein kinase such that it may then phosphorylate other intracellular substrates on tyrosines; this is the case for the insulin receptor and pp60c-src, for example. However, a more widespread role among the tyrosine kinases is the generation of a phosphotyrosine binding site for effector proteins that contain either src homology 2(SH2) or “Phospho Tyrosine Binding” (PTB) domains. It is these latter effector proteins that then further transmit the signal into the cell interior (1,2)." @default.
- W1589566049 created "2016-06-24" @default.
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- W1589566049 date "2003-11-14" @default.
- W1589566049 modified "2023-09-25" @default.
- W1589566049 title "Two-Dimensional Phosphopeptide Mapping of Receptor Tyrosine Kinases" @default.
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- W1589566049 doi "https://doi.org/10.1385/1-59259-059-4:67" @default.
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