ArticleStructure (London, England : 1993)2013
Structural evaluation of EGFR inhibition mechanisms for nanobodies/VHH domains.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 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.
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Who cites it
118 citing papers in PubMed, 242 citations in OpenAlex.
- A potential mechanism for tetraspanin CD82-mediated regulation of EGFR.Life science alliance · 2026Article
- Multispecific nanobody degraders co-deplete membrane receptors and enable targeted delivery of diverse payloads.bioRxiv : the preprint server for biology · 2026Article
- Plant-Produced Viral Nanoparticles Decorated with Nanobodies Against HER2 Improve Retention and Recruitment of Immune Cells in Solid Tumors.Advanced healthcare materials · 2026Article
- Engineering tandem VHHs to target different epitopes to enhance antibody-dependent cell-mediated cytotoxicity.FEBS open bio · 2026Article
- Camelid-Derived Nanobodies Targeting Human Epidermal Growth Factor Receptor: Screening, Expression, and Functional Validation.Antibodies (Basel, Switzerland) · 2026Article
- Nanobody-Based Drug Delivery: Emerging Strategies for Targeted Cancer Therapy.International journal of nanomedicine · 2026Review
- Dissecting the disconnect between circuit activation and dominant adaptive evolution in cytoplasmic phage-assisted continuous evolution (PACE) of an EGFR nanobody.Frontiers in bioengineering and biotechnology · 2026Article
- Thiol-thiol cross-clicking using bromo-ynone reagents.Nature communications · 2025Article
- Interleukin 21-Armed EGFR-VHH-CAR-T Cell Therapy for the Treatment of Esophageal Squamous Cell Carcinoma.Biomedicines · 2025Article
- It's a match: use of the radionuclide theranostic pairEJNMMI radiopharmacy and chemistry · 2025Article
- Nanobodies: From Discovery to AI-Driven Design.Biology · 2025Review
- Affinity-stability trade-off mechanism of residue 35 in framework region 2 of VProtein science : a publication of the Protein Society · 2025Article
- Presence of EGF ligand restricts the binding ability of EgB4 nanobody to EGFR extracellular domain.Scientific reports · 2025Article
- Enhancing substrate specificity of microbial transglutaminase for precise nanobody labeling.Synthetic and systems biotechnology · 2025Article
- Protein purification with light via a genetically encoded azobenzene side chain.Nature communications · 2024Article
- Arginine Accelerates Sulfur Fluoride Exchange and Phosphorus Fluoride Exchange Reactions between Proteins.Angewandte Chemie (International ed. in English) · 2024Article
- CYpHER: catalytic extracellular targeted protein degradation with high potency and durable effect.Nature communications · 2024Article
- Analysis of EGFR binding hotspots for design of new EGFR inhibitory biologics.Protein science : a publication of the Protein Society · 2024Review
- Structural insights into the role and targeting of EGFRvIII.Structure (London, England : 1993) · 2024Article
- Rapid discovery and evolution of nanosensors containing fluorogenic amino acids.Nature communications · 2024Article
58 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The epidermal growth factor receptor (EGFR) is implicated in human cancers and is the target of several classes of therapeutic agents, including antibody-based drugs. Here, we describe X-ray crystal structures of the extracellular region of EGFR in complex with three inhibitory nanobodies, the variable domains of heavy chain only antibodies (VHH). VHH domains, the smallest natural antigen-binding modules, are readily engineered for diagnostic and therapeutic applications. All three VHH domains prevent ligand-induced EGFR activation, but use two distinct mechanisms. 7D12 sterically blocks ligand binding to EGFR in a manner similar to that of cetuximab. EgA1 and 9G8 bind an epitope near the EGFR domain II/III junction, preventing receptor conformational changes required for high-affinity ligand binding and dimerization. This epitope is accessible to the convex VHH paratope but inaccessible to the flatter paratope of monoclonal antibodies. Appreciating the modes of binding and inhibition of these VHH domains will aid in developing them for tumor imaging and/or cancer therapy.
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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.