ArticleMolecular bioSystems2008
A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R.
Article in Molecular bioSystems, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed.
- Effects of heterologous kinase domains on growth factor receptor specificity.Cellular signalling · 2024Article
- New analysis pipeline for high-throughput domain-peptide affinity experiments improves SH2 interaction data.The Journal of biological chemistry · 2020Article
- Analyzing expression and phosphorylation of the EGF receptor in HNSCC.Scientific reports · 2019Article
- Machine-learning techniques for the prediction of protein-protein interactions.Journal of biosciences · 2019Article
- Modeling cell line-specific recruitment of signaling proteins to the insulin-like growth factor 1 receptor.PLoS computational biology · 2019Article
- Src homology 2 domains enhance tyrosine phosphorylationThe Journal of biological chemistry · 2018Article
- Quantification of growth factor signaling and pathway cross talk by live-cell imaging.American journal of physiology. Cell physiology · 2017Article
- Mapping growth-factor-modulated Akt signaling dynamics.Journal of cell science · 2016Article
- Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases.Science signaling · 2015Article
- Phosphatase specificity and pathway insulation in signaling networks.Biophysical journal · 2015Article
- Identification of Posttranslational Modification-Dependent Protein Interactions Using Yeast Surface Displayed Human Proteome Libraries.Methods in molecular biology (Clifton, N.J.) · 2015Review
- The development and application of a quantitative peptide microarray based approach to protein interaction domain specificity space.Molecular & cellular proteomics : MCP · 2014Article
- Article
- Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome.Molecular & cellular proteomics : MCP · 2014Article
- Phosphotyrosine signaling proteins that drive oncogenesis tend to be highly interconnected.Molecular & cellular proteomics : MCP · 2013Article
- Semi-supervised prediction of SH2-peptide interactions from imbalanced high-throughput data.PloS one · 2013Article
- Completion of proteomic data sets by Kd measurement using cell-free synthesis of site-specifically labeled proteins.PloS one · 2013Article
- Phosphotyrosine recognition domains: the typical, the atypical and the versatile.Cell communication and signaling : CCS · 2012Article
- SRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactome.Cell communication and signaling : CCS · 2012Article
- Fast rebinding increases dwell time of Src homology 2 (SH2)-containing proteins near the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Receptor tyrosine kinases transmit and process extracellular cues by recruiting intracellular signaling proteins to sites of tyrosine phosphorylation. Using protein microarrays comprising virtually every human SH2 and PTB domain, we generated quantitative protein interaction maps for three well-studied receptors--EGFR, FGFR1 and IGF1R--using phosphopeptides derived from every intracellular tyrosine residue on each receptor, regardless of whether or not they are phosphorylated in vivo. We found that, in general, peptides derived from physiological sites of tyrosine phosphorylation bind to substantially more SH2 or PTB domains than do peptides derived from nonphysiological sites, supporting the idea that kinases and interaction domains co-evolve and suggesting that new sites arise predominantly through selection favoring advantageous interactions, rather than through selection disfavoring unwanted interactions. We also found substantial qualitative overlap in the recruitment profiles of these three receptors, suggesting that their different biological effects arise, at least in part, from quantitative differences in their affinities for the proteins they recruit.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.