ArticleCell2010
Structural basis for negative cooperativity in growth factor binding to an EGF receptor.
Article in Cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
104 citing papers in PubMed, 189 citations in OpenAlex.
- Yes/No Quantitative Analysis of Single-Stranded Oligonucleotides with Lateral Flow Assays.Biosensors · 2026Article
- Ligand regulation and function of preformed EGFR dimers.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Epidermal growth factor receptor as a target enzyme in cancer therapy: Structural and functional insights from crystallography.Indian journal of pharmacology · 2026Review
- Article
- Discovery of highly potent α-keto ester-based peptidomimetic inhibitors of the Hip1 protease for the treatment ofEuropean journal of medicinal chemistry reports · 2025Article
- Active regulation of the epidermal growth factor receptor by the membrane bilayer.bioRxiv : the preprint server for biology · 2025Article
- Building a dynamic model for EGFR-family dimerization using quantitative, live-cell fluorescence methods.Biophysical journal · 2025Review
- EGFR: New Insights on Its Activation and Mutation in Tumor and Tumor Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- A live-cell biosensor of in vivo receptor tyrosine kinase activity reveals feedback regulation of a developmental gradient.Cell reports · 2025Article
- Article
- Probing phosphorylation events in biological membranes: The transducer function.Biochimica et biophysica acta. Biomembranes · 2024Review
- Unexpected Single-Ligand Occupancy and Negative Cooperativity in the SARS-CoV-2 Main Protease.Journal of chemical information and modeling · 2024Article
- A perspective of fluorescence microscopy for cellular structural biology with EGFR as witness.Journal of microscopy · 2023Article
- The EGFR phosphatase RPTPγ is a redox-regulated suppressor of promigratory signaling.The EMBO journal · 2023Article
- Structural insights into the mechanism of leptin receptor activation.Nature communications · 2023Article
- Structure and dynamics of the EGFR/HER2 heterodimer.Cell discovery · 2023Article
- Review
- Stoichiometric approach to quantitative analysis of biomolecules: the case of nucleic acids.Analytical and bioanalytical chemistry · 2022Article
- Article
- Fluorescently tagged nanobodies and NanoBRET to study ligand-binding and agonist-induced conformational changes of full-length EGFR expressed in living cells.Frontiers in immunology · 2022Article
44 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Transmembrane signaling by the epidermal growth factor receptor (EGFR) involves ligand-induced dimerization and allosteric regulation of the intracellular tyrosine kinase domain. Crystallographic studies have shown how ligand binding induces dimerization of the EGFR extracellular region but cannot explain the "high-affinity" and "low-affinity" classes of cell-surface EGF-binding sites inferred from curved Scatchard plots. From a series of crystal structures of the Drosophila EGFR extracellular region, we show here how Scatchard plot curvature arises from negatively cooperative ligand binding. The first ligand-binding event induces formation of an asymmetric dimer with only one bound ligand. The unoccupied site in this dimer is structurally restrained, leading to reduced affinity for binding of the second ligand, and thus negative cooperativity. Our results explain the cell-surface binding characteristics of EGF receptors and suggest how individual EGFR ligands might stabilize distinct dimeric species with different signaling properties.
Indexed as
Identifiers
What OpenQuestion holds
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.