ReviewMolecular & cellular proteomics : MCP2024
Nanobodies: From High-Throughput Identification to Therapeutic Development.
Review in Molecular & cellular proteomics : MCP, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed.
- A PD-L1 Nanobody-Engineered Synthetic RNA Virus Enhances Hepatocellular Carcinoma Immunotherapy by Interfering PCSK9 and Upregulating MHC-I.Exploration (Beijing, China) · 2026Article
- Production of isotope-labeled nanobody KN035 inMagnetic resonance letters · 2026Article
- Efficient generation of epitope-targeted antibodies with Germinal.Nature biotechnology · 2026Article
- Engineering molecularly imprinted polymers for receptor-specific cancer therapeutics.Nanoscale · 2026Review
- Article
- Multivalent nanobodies for potent and broad neutralization of Staphylococcus aureus toxins.Nature communications · 2026Article
- Repertoire-scale antibody structural prediction informs therapeutic design.Science advances · 2026Article
- Comprehensive Mapping of Immune Nanobody Repertoires with NanoMAP.bioRxiv : the preprint server for biology · 2026Article
- Camelid-Derived Nanobodies Targeting Human Epidermal Growth Factor Receptor: Screening, Expression, and Functional Validation.Antibodies (Basel, Switzerland) · 2026Article
- Selection and optimization strategy for Rap1-targeting single-domain antibodies as platelet activation markers.Research and practice in thrombosis and haemostasis · 2026Article
- Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation.Military Medical Research · 2026Review
- Targeting angiogenesis: advances in the design and engineered applications of nanobodies.Frontiers in immunology · 2026Review
- Review
- Nano-engineered biomimetic materials: toward point-of-care diagnosis of infectious diseases.Mikrochimica acta · 2025Review
- Modulating Subcellular Localization to Preserve the Stability and Functionality of Intracellular Nanobodies.Antibodies (Basel, Switzerland) · 2025Article
- Efficient generation of epitope-targetedbioRxiv : the preprint server for biology · 2025Article
- Targeted Protein Modification with an Antibody-Based System.ACS central science · 2025Article
- Nanobodies and their derivatives: pioneering the future of cancer immunotherapy.Cell communication and signaling : CCS · 2025Review
- Development and characterization of a novel NEIL1 nanobody.DNA repair · 2025Article
- Nanobodies: From Discovery to AI-Driven Design.Biology · 2025Review
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.
Funding
Abstract
The camelid single-domain antibody fragment, commonly referred to as a nanobody, achieves the targeting power of conventional monoclonal antibodies (mAbs) at only a fraction of their size. Isolated from camelid species (including llamas, alpacas, and camels), their small size at ∼15 kDa, low structural complexity, and high stability compared with conventional antibodies have propelled nanobody technology into the limelight of biologic development. Nanobodies are proving themselves to be a potent complement to traditional mAb therapies, showing success in the treatment of, for example, autoimmune diseases and cancer, and more recently as therapeutic options to treat infectious diseases caused by rapidly evolving biological targets such as the SARS-CoV-2 virus. This review highlights the benefits of applying a proteomic approach to identify diverse nanobody sequences against a single antigen. This proteomic approach coupled with conventional yeast/phage display methods enables the production of highly diverse repertoires of nanobodies able to bind the vast epitope landscape of an antigen, with epitope sampling surpassing that of mAbs. Additionally, we aim to highlight recent findings illuminating the structural attributes of nanobodies that make them particularly amenable to comprehensive antigen sampling and to synergistic activity-underscoring the powerful advantage of acquiring a large, diverse nanobody repertoire against a single antigen. Lastly, we highlight the efforts being made in the clinical development of nanobodies, which have great potential as powerful diagnostic reagents and treatment options, especially when targeting infectious disease agents.
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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.