ArticleBiotechnology reports (Amsterdam, Netherlands)2015
Improving the biophysical properties of anti-ricin single-domain antibodies.
Article in Biotechnology reports (Amsterdam, Netherlands), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Computational Prediction of Single-Domain Immunoglobulin Aggregation Propensities Facilitates Discovery and Humanization of Recombinant Nanobodies.Antibodies (Basel, Switzerland) · 2025Article
- Anti-CTLA-4 nanobody as a promising approach in cancer immunotherapy.Cell death & disease · 2024Review
- Integrating Single Domain Antibodies into Field-Deployable Rapid Assays.Antibodies (Basel, Switzerland) · 2022Article
- Research progress on unique paratope structure, antigen binding modes, and systematic mutagenesis strategies of single-domain antibodies.Frontiers in immunology · 2022Review
- Camelid Single-Domain Antibodies for the Development of Potent Diagnosis Platforms.Molecular diagnosis & therapy · 2021Review
- Protein design and variant prediction using autoregressive generative models.Nature communications · 2021Article
- Stabilization of a Broadly Neutralizing Anti-Chikungunya Virus Single Domain Antibody.Frontiers in medicine · 2021Article
- Toward Drug-Like Multispecific Antibodies by Design.International journal of molecular sciences · 2020Review
- Evaluation of a noncanonical Cys40-Cys55 disulfide linkage for stabilization of single-domain antibodies.Protein science : a publication of the Protein Society · 2019Article
- Selection and Characterization of Anti-Dengue NS1 Single Domain Antibodies.Scientific reports · 2018Article
- Selection of Single-Domain Antibodies towards Western Equine Encephalitis Virus.Antibodies (Basel, Switzerland) · 2018Article
- Orthogonal Synthetic Zippers as Protein Scaffolds.ACS omega · 2018Article
- The structural basis of nanobody unfolding reversibility and thermoresistance.Scientific reports · 2018Article
- Selection, characterization, and thermal stabilization of llama single domain antibodies towards Ebola virus glycoprotein.Microbial cell factories · 2017Article
- Exploiting sequence and stability information for directing nanobody stability engineering.Biochimica et biophysica acta. General subjects · 2017Article
- Pairing Alpaca and Llama-Derived Single Domain Antibodies to Enhance Immunoassays for Ricin.Antibodies (Basel, Switzerland) · 2017Article
- Enhancing Stability of Camelid and Shark Single Domain Antibodies: An Overview.Frontiers in immunology · 2017Review
- Article
- Activity-based assessment of an engineered hyperthermophilic protein as a capture agent in paper-based diagnostic tests.Molecular systems design & engineering · 2016Article
- Conjugation of biotin-coated luminescent quantum dots with single domain antibody-rhizavidin fusions.Biotechnology reports (Amsterdam, Netherlands) · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-domain antibodies (sdAbs) derived from heavy-chain only antibodies produced in camelids are attractive immunoreagents due to their small size, high affinity, and ability to refold and retain binding activity after denaturation. It has been observed that some sdAbs, however, exhibit undesirable properties including reduced solubility when subjected to heating or upon long-term storage at production-relevant concentrations, which can limit their usefulness. Using a multi-step, rational design approach that included consensus-sequence driven sequence repairs, the alteration of net protein charge, and the introduction of non-native disulfide bonds, augmented solubility and increased melting temperatures were achieved. The improved sdAbs tolerated storage in solution at high concentration (10 mg/mL) and were able to withstand multiple cycles of heating to high temperature (70 °C). This work demonstrates a pathway for improving the biophysical characteristics of sdAbs which is essential for expanding their utility for both diagnostic as well as therapeutic applications.
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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.