ArticleInternational journal of cancer2011
A biparatopic anti-EGFR nanobody efficiently inhibits solid tumour growth.
Article in International journal of cancer, 2011. 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.
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Who cites it
137 citing papers in PubMed, 272 citations in OpenAlex.
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- 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
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- Enhancing the sensitivity of nanobodies through covalent and non-covalent polymerization.RSC advances · 2026Article
- Nanobody-Based Drug Delivery: Emerging Strategies for Targeted Cancer Therapy.International journal of nanomedicine · 2026Review
- Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation.Military Medical Research · 2026Review
- Bioorthogonal Photocatalytic Protein Labeling and Cross-Linking Enabled by Stabilized Ketyl Radicals.Journal of the American Chemical Society · 2025Article
- Retargeted oncolytic viruses engineered to remodel the tumor microenvironment for glioblastoma immunotherapy.Nature cancer · 2025Article
- Development of leptospiral virulence-modifying protein detection assay: implications for pathogenesis and diagnostic test development.Microbiology spectrum · 2025Article
- Advances in Nanobody-Based Platforms for Precision Cancer Diagnosis and Therapy.Polymer science & technology (Washington, D.C.) · 2025Review
- Potentiating cancer immunotherapies with modular albumin-hitchhiking nanobody-STING agonist conjugates.Nature biomedical engineering · 2025Article
- It's a match: use of the radionuclide theranostic pairEJNMMI radiopharmacy and chemistry · 2025Article
- Modular Platform for Efficient Assembly of Multifunctional Antibodies Using Orthogonal Protein-Protein Interactions.ACS applied materials & interfaces · 2025Article
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
9 authors at 4 institutions in 3 countries.
Funding
Abstract
The epidermal growth factor receptor (EGFR) has been shown to be a valid cancer target for antibody-based therapy. At present, several anti-EGFR monoclonal antibodies have been successfully used, such as cetuximab and matuzumab. X-ray crystallography data show that these antibodies bind to different epitopes on the ecto-domain of EGFR, providing a rationale for the combined use of these two antibody specificities. We have previously reported on the successful isolation of antagonistic anti-EGFR nanobodies. In our study, we aimed to improve the efficacy of these molecules by combining nanobodies with specificities similar to both cetuximab and matuzumab into a single biparatopic molecule. Carefully designed phage nanobody selections resulted in two sets of nanobodies that specifically blocked the binding of either matuzumab or cetuximab to EGFR and that did not compete for each others' binding. A combination of nanobodies from both epitope groups into the biparatopic nanobody CONAN-1 was shown to block EGFR activation more efficiently than monovalent or bivalent (monospecific) nanobodies. In addition, this biparatopic nanobody potently inhibited EGF-dependent cell proliferation. Importantly, in an in vivo model of athymic mice bearing A431 xenografts, CONAN-1 inhibited tumour outgrowth with an almost similar potency as the whole mAb cetuximab, despite the fact that CONAN-1 is devoid of an Fc portion that could mediate immune effector functions. Compared to therapy using bivalent, monospecific nanobodies, CONAN-1 was clearly more potent in tumour growth inhibition. These results show that the rational design of biparatopic nanobody-based anticancer therapeutics may yield potent lead molecules for further development.
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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.