ArticleNew biotechnology2016
Platform for high-throughput antibody selection using synthetically-designed antibody libraries.
Article in New biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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
9 citing papers in PubMed.
- A versatile platform for combinatorial antibody library cloning and NGS-based quality control with high accuracy.Nucleic acids research · 2025Article
- Combining computational modeling and experimental library screening to affinity-mature VEEV-neutralizing antibody F5.Protein science : a publication of the Protein Society · 2025Article
- Use of Epivolve phage display to generate a monoclonal antibody with opsonic activity directed against a subdominant epitope on extracellular loop 4 ofFrontiers in immunology · 2023Article
- Epivolve: A Protocol for Site-Directed Antibodies.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Derivation of splice junction-specific antibodies using a unique hapten targeting strategy and directed evolution.New biotechnology · 2022Article
- NADK is activated by oncogenic signaling to sustain pancreatic ductal adenocarcinoma.Cell reports · 2021Article
- Rational library design by functional CDR resampling.New biotechnology · 2018Article
- Virus-Derived Peptides for Clinical Applications.Chemical reviews · 2017Review
- pMINERVA: A donor-acceptor system for the in vivo recombineering of scFv into IgG molecules.Journal of immunological methods · 2016Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Synthetic humanized antibody libraries are frequently generated by random incorporation of changes at multiple positions in the antibody hypervariable regions. Although these libraries have very large theoretical diversities (>10(20)), the practical diversity that can be achieved by transformation of Escherichia coli is limited to about 10(10). To constrain the practical diversity to sequences that more closely mimic the diversity of natural human antibodies, we generated a scFv phage library using entirely pre-defined complementarity determining regions (CDR). We have used this library to select for novel antibodies against four human protein targets and demonstrate that identification of enriched sequences at each of the six CDRs in early selection rounds can be used to reconstruct a consensus antibody with selectivity for the target.
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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.