ArticleInternational journal of molecular sciences2019
Identification of New DR5 Agonistic Nanobodies and Generation of Multivalent Nanobody Constructs for Cancer Treatment.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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
19 citing papers in PubMed, 31 citations in OpenAlex.
- Nanobodies Open New Avenues in Cancer Treatment: From Molecular Engineering to Therapeutic Platforms.Cell biochemistry and biophysics · 2026Review
- Targeting angiogenesis: advances in the design and engineered applications of nanobodies.Frontiers in immunology · 2026Review
- Article
- Article
- Advances in nanobody multimerization and multispecificity: from in vivo assembly to in vitro production.Biochemical Society transactions · 2025Review
- Nanobodies in the fight against infectious diseases: repurposing nature's tiny weapons.World journal of microbiology & biotechnology · 2024Review
- Facile generation of biepitopic antibodies with intrinsic agonism for activating tumor necrosis factor receptors.Cell chemical biology · 2024Article
- Review
- Targeting Death Receptor 5 (DR5) for the imaging and treatment of primary bone and soft tissue tumors: an update of the literature.Frontiers in molecular biosciences · 2024Review
- Facile generation of biepitopic antibodies with intrinsic agonism for activating receptors in the tumor necrosis factor superfamily.bioRxiv : the preprint server for biology · 2023Article
- Detection of a Thermal Stable-Soluble Protein (TSSP) as a Marker of Peanut Adulteration Using a Highly Sensitive Indirect Enzyme-Linked Immunosorbent Assay based on Monoclonal Antibodies.Journal of microbiology and biotechnology · 2023Article
- Unlocking the potential of agonist antibodies for treating cancer using antibody engineering.Trends in molecular medicine · 2023Review
- Experimental validation of computerised models of clustering of platelet glycoprotein receptors that signal via tandem SH2 domain proteins.PLoS computational biology · 2022Article
- Optimized Heterologous Expression and Efficient Purification of a New TRAIL-Based Antitumor Fusion Protein SRH-DR5-B with Dual VEGFR2 and DR5 Receptor Specificity.International journal of molecular sciences · 2022Article
- Agonist antibody discovery: Experimental, computational, and rational engineering approaches.Drug discovery today · 2022Review
- Formatting and gene-based delivery of a human PD-L1 single domain antibody for immune checkpoint blockade.Molecular therapy. Methods & clinical development · 2021Article
- A guide to: generation and design of nanobodies.The FEBS journal · 2021Review
- Nanobodies targeting immune checkpoint molecules for tumor immunotherapy and immunoimaging (Review).International journal of molecular medicine · 2021Review
- Nanobodies: Next Generation of Cancer Diagnostics and Therapeutics.Frontiers in oncology · 2020Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Current cancer therapeutics suffer from a lack of specificity in targeting tumor cells and cause severe side effects. Therefore, the design of highly specialized drugs comprising antibody derivatives inducing apoptosis in targeted cancer cells is considered to be a promising strategy. Drugs acting on death receptor 5 (DR5) such as DR5 agonist antibodies replacing "TNF-related apoptosis-inducing ligand" (TRAIL) offer feasible opportunities in this direction. Although such agonists provided good antitumor activity in preclinical studies, they were less effective in clinical studies, possibly due to a disturbed Fc interaction with Fc-γ receptors. Thus, multimerized antigen binding fragments without Fc have been proposed to increase their efficacy. We generated nanobodies (Nbs), recombinant variable domains of heavy chain-only antibodies of camelids, against the DR5 ectodomain. Nb24 and Nb28 had an affinity in the nM and sub-nM range, but only Nb28 competes with TRAIL for binding to DR5. Bivalent, trivalent, and tetravalent constructs were generated, as well as an innovative pentameric Nb complex, to provoke avidity effects. In our cellular assays, these trimeric, tetrameric, and pentameric Nbs have a higher apoptotic capacity than monomeric Nbs and seem to mimic the activity of the natural TRAIL ligand on various cancer cells.
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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.