Crossref journal-article
Wiley
BioEssays (311)
Abstract

AbstractCell proliferation in response to growth factors is mediated by specific high affinity receptors. Ligand‐binding by receptors of the protein tyrosine kinase family results in the stimulation of several intracellular signal transduction pathways. Key signalling enzymes are recruited to the plasma membrane through the formation of stable complexes with activated receptors. These interactions are mediated by the conserved, non‐catalytic SH2 domains present in the signalling molecules, which bind with high affinity and specificity to tyrosine‐phosphorylated sequences on the receptors. The assembly of enzyme complexes is emerging as a major mechanism of signal transduction and may regulate the pleiotropic effects of growth factors.

Bibliography

Panayotou, G., & Waterfield, M. D. (1993). The assembly of signalling complexes by receptor tyrosine kinases. BioEssays, 15(3), 171–177. Portico.

Authors 2
  1. George Panayotou (first)
  2. Michael D. Waterfield (additional)
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Dates
Type When
Created 20 years, 6 months ago (Feb. 25, 2005, 4:20 a.m.)
Deposited 1 year, 10 months ago (Oct. 25, 2023, 2:21 a.m.)
Indexed 2 months ago (June 26, 2025, 2:24 p.m.)
Issued 32 years, 5 months ago (March 1, 1993)
Published 32 years, 5 months ago (March 1, 1993)
Published Online 20 years, 6 months ago (Feb. 5, 2005)
Published Print 32 years, 5 months ago (March 1, 1993)
Funders 0

None

@article{Panayotou_1993, title={The assembly of signalling complexes by receptor tyrosine kinases}, volume={15}, ISSN={1521-1878}, url={http://dx.doi.org/10.1002/bies.950150305}, DOI={10.1002/bies.950150305}, number={3}, journal={BioEssays}, publisher={Wiley}, author={Panayotou, George and Waterfield, Michael D.}, year={1993}, month=mar, pages={171–177} }