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- W1461640088 abstract "The first RTK discovered was the EGFR. It was also the first receptor that provided evidence for a relationship between activating mutations (oncogenes) and cancer. About 90 genes code for protein tyrosine kinases in the human genome, out of which 58 are receptors (rPTK) and are classified into 20 subfamilies. The remaining 32 are of the non-receptor type (nrPTK). It is also an interesting fact that mouse homologues also have been identified for nearly all of the human tyrosine kinases. Tyrosine phosphorylation is not limited to the actions of the transforming viruses or growth factors. It regulates many other important signaling processes which are specified in this chapter. The assembly of receptor signaling complexes depends on protein–protein interactions that involve phosphorylated growth factor receptors. The first clues to the mechanism came from studies of p47gag-crk, a transforming protein devoid of any catalytic activity. Many kinases and phosphatases are regulated by interactions with their substrates at non-catalytic regions, docking motifs that help to avoid indiscriminate phosphorylations or dephosphorylations. The idea that mitogen-activated protein (MAP) kinases form stable links with their substrates first arose with studies of JNK2, which was isolated from cell lysates in tight association with its substrate c-Jun. Later this chapter presents a number of signal transduction pathways that branch out from the signaling complex and also discusses pathway switching, transactivation, and metastatic progression." @default.
- W1461640088 created "2016-06-24" @default.
- W1461640088 creator A5007964369 @default.
- W1461640088 creator A5028384228 @default.
- W1461640088 creator A5073789622 @default.
- W1461640088 date "2009-01-01" @default.
- W1461640088 modified "2023-09-24" @default.
- W1461640088 title "Signalling Pathways Operated by Receptor Protein Tyrosine Kinases" @default.
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