ReviewFrontiers in immunology2017
Single-Domain Antibodies As Versatile Affinity Reagents for Analytical and Diagnostic Applications.
Review in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 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.
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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
102 citing papers in PubMed.
- Combining AI Structure Prediction and Integrative Modeling for Nanobody-Antigen Complexes.Journal of chemical information and modeling · 2026Article
- Recent insights for fish allergens: novel processing techniques and detection technology.Journal of the science of food and agriculture · 2026Review
- Contact Occupancy and Per-Residue Energetic Contributions Distinguish Aflatoxin B1 Nanobodies with Different Binding Affinities.Biomolecules · 2026Article
- Advanced nanobiosensors for the detection of neurovascular damage in cerebral infarction: prospects and challenges.Journal of biological engineering · 2026Article
- Film, function, flexibility: label-free nanobody sensorsNanoscale · 2026Article
- A High-Affinity Nanobody Selectively Recognizing KPC-2/KPC-3: Biochemical and Structural Insights.Biomolecules · 2026Article
- Nanobody-Based Drug Delivery: Emerging Strategies for Targeted Cancer Therapy.International journal of nanomedicine · 2026Review
- Nanobody Therapeutics in Alzheimer's Disease: From Molecular Mechanisms to Translational Approaches.Antibodies (Basel, Switzerland) · 2025Review
- Methods for Conjugating Antibodies with Quantum Dots.Molecules (Basel, Switzerland) · 2025Review
- Computational Prediction of Single-Domain Immunoglobulin Aggregation Propensities Facilitates Discovery and Humanization of Recombinant Nanobodies.Antibodies (Basel, Switzerland) · 2025Article
- CD45 sequestration lowers the signaling threshold in lymphocytes and enhances anti-tumor immunity.bioRxiv : the preprint server for biology · 2025Article
- Nanobodies: From Discovery to AI-Driven Design.Biology · 2025Review
- Single-Domain Antibodies That Specifically Recognize Intact Capsids of Multiple Foot-and-Mouth Disease Serotype O Strains.Vaccines · 2025Article
- A synthetic heavy chain variable domain antibody library (VHL) provides highly functional antibodies with favorable developability.Protein science : a publication of the Protein Society · 2025Article
- Nanobodies in animal infectious disease control: diagnosis and therapy.Frontiers in cellular and infection microbiology · 2025Review
- Mass spectrometry-complemented molecular modeling predicts the interaction interface for a camelid single-domain antibody targeting theComputational and structural biotechnology journal · 2024Article
- Characteristics and Genomic Localization of Nurse Shark (International journal of molecular sciences · 2024Article
- Protein Biomarkers in Lung Cancer Screening: Technical Considerations and Feasibility Assessment.Archivos de bronconeumologia · 2024Review
- Scalable, robust, high-throughput expression & purification of nanobodies enabled by 2-stage dynamic control.Metabolic engineering · 2024Article
- Construction and validation of a synthetic phage-displayed nanobody library.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2024Article
42 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
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
With just three CDRs in their variable domains, the antigen-binding site of camelid heavy-chain-only antibodies (HcAbs) has a more limited structural diversity than that of conventional antibodies. Even so, this does not seem to limit their specificity and high affinity as HcAbs against a broad range of structurally diverse antigens have been reported. The recombinant form of their variable domain [nanobody (Nb)] has outstanding properties that make Nbs, not just an alternative option to conventional antibodies, but in many cases, these properties allow them to reach analytical or diagnostic performances that cannot be accomplished with conventional antibodies. These attributes include comprehensive representation of the immune specificity in display libraries, easy adaptation to high-throughput screening, exceptional stability, minimal size, and versatility as affinity building block. Here, we critically reviewed each of these properties and highlight their relevance with regard to recent developments in different fields of immunosensing applications.
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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.