ArticleFrontiers in immunology2017
Article 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 31 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.
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Who cites it
31 citing papers in PubMed.
- Engineering and Partial Characterization of an Anti-IL-23/Anti-TNF-α Bispecific Domain Antibody Fused to Human Serum Albumin Domain for Inflammatory Disease Therapy.Applied biochemistry and biotechnology · 2026Article
- A Rationally Designed Novel Bifunctional Human TNF-α- and Janus Kinase-Targeted soloMER Drug Conjugate (SDC) with a Neutrophil Elastase Cleavable Linker Delivering Inflammation Site-Specific Release of Payload.Journal of medicinal chemistry · 2026Article
- The structural basis for the selective antagonism of soluble TNF-alpha by shark variable new antigen receptors.Nature communications · 2025Article
- The characterization of variable new antigen receptors targeting FAP isolated from a novel immunized library.Communications biology · 2025Article
- Development of FAP-targeted theranostics discovered by next-generation sequencing-augmented mining of a novel immunized VNAR library.bioRxiv : the preprint server for biology · 2025Article
- T cell assays for non-clinical immunogenicity risk assessment: best practices recommended by the European Immunogenicity Platform.Frontiers in immunology · 2025Review
- VNAR: shark single-domain antibodies for the new era of medical biotechnology.Frontiers in immunology · 2025Review
- Osteoarthritis versus psoriasis arthritis: Physiopathology, cellular signaling, and therapeutic strategies.Genes & diseases · 2024Review
- Development of a cationic polyethyleneimine-poly(lactic-RSC advances · 2023Article
- Structure and Dynamics Guiding Design of Antibody Therapeutics and Vaccines.Antibodies (Basel, Switzerland) · 2023Review
- Shark IgNAR: The Next Broad Application Antibody in Clinical Diagnoses and Tumor Therapies?Marine drugs · 2023Review
- Humanization of the Shark VCurrent protocols · 2023Article
- Unleashing the power of shark variable single domains (VNARs): broadly neutralizing tools for combating SARS-CoV-2.Frontiers in immunology · 2023Review
- Single domain antibodies derived from ancient animals as broadly neutralizing agents for SARS-CoV-2 and other coronaviruses.Biomedical engineering advances · 2022Review
- VHHs as tools for therapeutic protein delivery to the central nervous system.Fluids and barriers of the CNS · 2022Article
- Production and Purification of Shark and Camel Single-Domain Antibodies from Bacterial and Mammalian Cell Expression Systems.Current protocols · 2022Article
- The influence of antibody humanization on shark variable domain (VNAR) binding site ensembles.Frontiers in immunology · 2022Article
- Shark New Antigen Receptor (IgNAR): Structure, Characteristics and Potential Biomedical Applications.Cells · 2021Review
- Bamboo Shark as a Small Animal Model for Single Domain Antibody Production.Frontiers in bioengineering and biotechnology · 2021Article
- Therapeutic Antibodies Targeting Potassium Ion Channels.Handbook of experimental pharmacology · 2021Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular engineering to increase the percentage identity to common human immunoglobulin sequences of non-human therapeutic antibodies and scaffolds has become standard practice. This strategy is often used to reduce undesirable immunogenic responses, accelerating the clinical development of candidate domains. The first humanized shark variable domain (VNAR) was reported by Kovalenko and colleagues and used the anti-human serum albumin (HSA) domain, clone E06, as a model to construct a number of humanized versions including huE06v1.10. This study extends this work by using huE06v1.10 as a template to isolate domains with improved biophysical properties and reduced antigenicity. Random mutagenesis was conducted on huE06v1.10 followed by refinement of clones through an off-rate ranking-based selection on target antigen. Many of these next-generation binders retained high affinity for target, together with good species cross-reactivity. Lead domains were assessed for any tendency to dimerize, tolerance to N- and C-terminal fusions, affinity, stability, and relative antigenicity in human dendritic cell assays. Functionality of candidate clones was verified
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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.