Matches in Nanopublications for { ?s ?p "Intriguingly, RET can be activated independently of the GFL-GFR-a complexes. Nerve growth factor (NGF)-triggered activation of the TrkA kinase receptor promotes RET phosphorylation through GFL-independent interreceptor kinase signaling (fig. 1) [30]. This TrkA-RET interaction selectively involves RET51, one of the two RET alternative protein products (see below). Of note, both RET and TrkA, the two kinases involved in this developmental interaction, are also involved in the pathogenesis of papillary carcinomas of the thyroid gland" ?g. }
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- _5 value "Intriguingly, RET can be activated independently of the GFL-GFR-a complexes. Nerve growth factor (NGF)-triggered activation of the TrkA kinase receptor promotes RET phosphorylation through GFL-independent interreceptor kinase signaling (fig. 1) [30]. This TrkA-RET interaction selectively involves RET51, one of the two RET alternative protein products (see below). Of note, both RET and TrkA, the two kinases involved in this developmental interaction, are also involved in the pathogenesis of papillary carcinomas of the thyroid gland" provenance.
- _5 value "Intriguingly, RET can be activated independently of the GFL-GFR-a complexes. Nerve growth factor (NGF)-triggered activation of the TrkA kinase receptor promotes RET phosphorylation through GFL-independent interreceptor kinase signaling (fig. 1) [30]. This TrkA-RET interaction selectively involves RET51, one of the two RET alternative protein products (see below). Of note, both RET and TrkA, the two kinases involved in this developmental interaction, are also involved in the pathogenesis of papillary carcinomas of the thyroid gland" provenance.