Michael Moran

TL;DR: Comparison of the HMS-PCI data set with interactions reported in the literature revealed an average threefold higher success rate in detection of known complexes compared with large-scale two-hybrid studies.

TL;DR: Observations suggest that SH2 and SH3 domains participate in the control of intracellular responses to growth factor stimulation.

TL;DR: In‐depth mining of the data set shows that it represents a valuable source of novel protein–protein interactions with relevance to human diseases, and via the preliminary analysis, many novel protein interactions and pathway associations are reported.

TL;DR: It is shown that GAP, and two co-precipitating proteins of relative molecular masses 62,000 and 190,000 (p62 and p190) are phosphorylated on tyrosine in cells that have been transformed by cytoplasmic and receptor-like tyrosin kinases, which supports the idea that SH2 sequences direct the interactions of cytopLasmic proteins involved in signal transduction.

TL;DR: SH2 domains provide a common mechanism by which enzymatically diverse regulatory proteins can physically associate with the same activated receptors and thereby couple growth factor stimulation to intracellular signal transduction pathways.