ArticleCancer immunology, immunotherapy : CII2007
Efficient inhibition of EGFR signaling and of tumour growth by antagonistic anti-EFGR Nanobodies.
Article in Cancer immunology, immunotherapy : CII, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
137 citing papers in PubMed, 339 citations in OpenAlex.
- Article
- Nanobodies Open New Avenues in Cancer Treatment: From Molecular Engineering to Therapeutic Platforms.Cell biochemistry and biophysics · 2026Review
- Nanobody-based targeted cancer therapy and immunotherapy: fear not the future.Acta pharmacologica Sinica · 2026Review
- Resolving Heterogeneity of Targeted Lipid Nanoparticles Through Solution-Based Biophysical Analyses.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Plant-Produced Viral Nanoparticles Decorated with Nanobodies Against HER2 Improve Retention and Recruitment of Immune Cells in Solid Tumors.Advanced healthcare materials · 2026Article
- Resolving heterogeneity of targeted lipid nanoparticles through solution-based biophysical analyses.bioRxiv : the preprint server for biology · 2026Article
- Identification and Nonclinical Characterization of SAR444200, a Novel Anti-GPC3 NANOBODY T-cell Engager, for the Treatment of GPC3+ Solid Tumors.Molecular cancer therapeutics · 2026Article
- Bioorthogonal Photocatalytic Protein Labeling and Cross-Linking Enabled by Stabilized Ketyl Radicals.Journal of the American Chemical Society · 2025Article
- A Comparative Study on the Effect of Near-Infrared Fluorescent Dyes on the Pharmacokinetic Behavior of Nanobody-Based Tracers for In Vivo Imaging.Journal of medicinal chemistry · 2025Article
- Presence of EGF ligand restricts the binding ability of EgB4 nanobody to EGFR extracellular domain.Scientific reports · 2025Article
- Nanobodies: From High-Throughput Identification to Therapeutic Development.Molecular & cellular proteomics : MCP · 2024Review
- 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
- Development of novel humanized VHH synthetic libraries based on physicochemical analyses.Scientific reports · 2024Article
- CYpHER: Catalytic extracellular targeted protein degradation with high potency and durable effect.bioRxiv : the preprint server for biology · 2024Article
- Novel Anti-Mesothelin Nanobodies and Recombinant Immunotoxins withMolecules and cells · 2023Article
- Construction of IgG-FabScientific reports · 2023Article
- NANOBODYInternational journal of molecular sciences · 2023Review
- Method To Diversify Cyanine Chromophore Functionality Enables Improved Biomolecule Tracking and Intracellular Imaging.Journal of the American Chemical Society · 2023Article
77 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
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The development of a number of different solid tumours is associated with over-expression of ErbB1, or the epidermal growth factor receptor (EGFR), and this over-expression is often correlated with poor prognosis of patients. Therefore, this receptor tyrosine kinase is considered to be an attractive target for antibody-based therapy. Indeed, antibodies to the EGFR have already proven their value for the treatment of several solid tumours, especially in combination with chemotherapeutic treatment regimens. Variable domains of camelid heavy chain-only antibodies (called Nanobodies) have superior properties compared with classical antibodies in that they are small, very stable, easy to produce in large quantities and easy to re-format into multi-valent or multi-specific proteins. Furthermore, they can specifically be selected for a desired function by phage antibody display. In this report, we describe the successful selection and the characterisation of antagonistic anti-EGFR Nanobodies. By using a functional selection strategy, Nanobodies that specifically competed for EGF binding to the EGFR were isolated from "immune" phage Nanobody repertoires. The selected antibody fragments were found to efficiently inhibit EGF binding to the EGFR without acting as receptor agonists themselves. In addition, they blocked EGF-mediated signalling and EGF-induced cell proliferation. In an in vivo murine xenograft model, the Nanobodies were effective in delaying the outgrowth of A431-derived solid tumours. This is the first report describing the successful use of untagged Nanobodies for the in vivo treatment of solid tumours. The results show that functional phage antibody selection, coupled to the rational design of Nanobodies, permits the rapid development of novel anti-cancer antibody-based therapeutics.
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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.