ArticleInternational journal of molecular sciences2017
Rapid and Direct VHH and Target Identification by Staphylococcal Surface Display Libraries.
Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed.
- Camelid VHHs as a Versatile Platform for Combating Viral Infections.Pharmaceuticals (Basel, Switzerland) · 2026Review
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Discovery of nanobodies: a comprehensive review of their applications and potential over the past five years.Journal of nanobiotechnology · 2024Review
- Monoclonal antibodies: From magic bullet to precision weapon.Molecular biomedicine · 2024Review
- Nanobodies: Robust miniprotein binders in biomedicine.Advanced drug delivery reviews · 2023Review
- Article
- Article
- Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020Review
- Molecular dynamics simulation and experimental study of the surface-display of SPA protein via Lpp-OmpA system for screening of IgG.AMB Express · 2020Article
- FimH-based display of functional eukaryotic proteins on bacteria surfaces.Scientific reports · 2019Article
- Engineering E. coli cell surface in order to develop a one-step purification method for recombinant proteins.AMB Express · 2018Article
- Single-Domain Antibodies and the Promise of Modular Targeting in Cancer Imaging and Treatment.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
Unbiased and simultaneous identification of a specific antibody and its target antigen has been difficult without prior knowledge of at least one interaction partner. Immunization with complex mixtures of antigens such as whole organisms and tissue extracts including tumoral ones evokes a highly diverse immune response. During such a response, antibodies are generated against a variety of epitopes in the mixture. Here, we propose a surface display design that is suited to simultaneously identify camelid single domain antibodies and their targets. Immune libraries of single-domain antigen recognition fragments from camelid heavy chain-only antibodies (VHH) were attached to the peptidoglycan of Gram-positive
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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.