ArticleScientific reports2018
The structural basis of nanobody unfolding reversibility and thermoresistance.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 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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Who cites it
104 citing papers in PubMed, 187 citations in OpenAlex.
- Development of a high-specificity nanobody-based enzyme-linked immunosorbent assay for the rapid detection of mebendazole residues.Analytical and bioanalytical chemistry · 2026Article
- Camelid VHHs as a Versatile Platform for Combating Viral Infections.Pharmaceuticals (Basel, Switzerland) · 2026Review
- High-cell-density Escherichia coli-based nanobody production: benchmarking of subcellular targeting, strain background and process development strategies.Microbial cell factories · 2026Article
- Balancing Stealth and Targetability: cCPP- and PEG-Modified Liposomes for the Targeted Delivery of Anti-HER2 Nanobodies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Nanobody-based targeted cancer therapy and immunotherapy: fear not the future.Acta pharmacologica Sinica · 2026Review
- Hypervariable loop profiling decodes sequence determinants of antibody stability.Nature structural & molecular biology · 2026Article
- Tiny tools closing the gap: nanobodies in research and therapy.Function (Oxford, England) · 2026Review
- Bridging Inflammation and Oncology: The Role and Therapeutic Potential of Macrophage Migration Inhibitory Factor in Lung Cancer.International journal of molecular sciences · 2026Review
- A Nanobody-Based Lateral Flow Assay for Point-of-Care Diagnostics.Biosensors · 2026Article
- NanoBondy Reaction through NeissLock Anhydride Allows Covalent Immune Cell Decoration.Bioconjugate chemistry · 2026Article
- Nanobody-Based Drug Delivery: Emerging Strategies for Targeted Cancer Therapy.International journal of nanomedicine · 2026Review
- NbBayesLM: bayesian prediction of nanobody thermostability using protein language model.Frontiers in bioinformatics · 2026Article
- Structural mechanisms and insights on multiple nanobodies binding diverse SOD1 epitopes.Communications biology · 2025Article
- Article
- CD38-specific nanobody-based bispecific antibody recruiters (BARs) redirect complement-dependent cytotoxicity toward multiple myeloma cells.Scientific reports · 2025Article
- Computational Prediction of Single-Domain Immunoglobulin Aggregation Propensities Facilitates Discovery and Humanization of Recombinant Nanobodies.Antibodies (Basel, Switzerland) · 2025Article
- Protein-based Radiopharmaceuticals that target fibroblast activation protein alpha: a review of current progress.EJNMMI radiopharmacy and chemistry · 2025Review
- Modulating ion channels with nanobodies.Synthetic and systems biotechnology · 2025Review
- Sensitizing solid tumors to CAR-mediated cytotoxicity by lipid nanoparticle delivery of synthetic antigens.Nature cancer · 2025Article
- Nanobodies: From Discovery to AI-Driven Design.Biology · 2025Review
44 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
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nanobodies represent the variable binding domain of camelid heavy-chain antibodies and are employed in a rapidly growing range of applications in biotechnology and biomedicine. Their success is based on unique properties including their reported ability to reversibly refold after heat-induced denaturation. This view, however, is contrasted by studies which involve irreversibly aggregating nanobodies, asking for a quantitative analysis that clearly defines nanobody thermoresistance and reveals the determinants of unfolding reversibility and aggregation propensity. By characterizing nearly 70 nanobodies, we show that irreversible aggregation does occur upon heat denaturation for the large majority of binders, potentially affecting application-relevant parameters like stability and immunogenicity. However, by deriving aggregation propensities from apparent melting temperatures, we show that an optional disulfide bond suppresses nanobody aggregation. This effect is further enhanced by increasing the length of a complementarity determining loop which, although expected to destabilize, contributes to nanobody stability. The effect of such variations depends on environmental conditions, however. Nanobodies with two disulfide bonds, for example, are prone to lose their functionality in the cytosol. Our study suggests strategies to engineer nanobodies that exhibit optimal performance parameters and gives insights into general mechanisms which evolved to prevent protein aggregation.
Identifiers
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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.