ArticleProceedings of the National Academy of Sciences of the United States of America2012
Selection of antibodies that regulate phenotype from intracellular combinatorial antibody libraries.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 70 citations in OpenAlex.
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- Tetravalent antibodies are more potent and efficacious erythropoiesis-stimulating agents than erythropoietin in vivo.Protein science : a publication of the Protein Society · 2026Article
- An asymmetric tetrabody is a potent and efficacious agonist of the erythropoietin receptor in vitro and in vivo.Protein science : a publication of the Protein Society · 2025Article
- The JAK-STAT pathway: from structural biology to cytokine engineering.Signal transduction and targeted therapy · 2024Review
- Increased stable integration efficiency in CHO cells through enhanced nuclear localization of Bxb1 serine integrase.BMC biotechnology · 2024Article
- De novo-designed transmembrane proteins bind and regulate a cytokine receptor.Nature chemical biology · 2024Article
- Advancements in mammalian display technology for therapeutic antibody development and beyond: current landscape, challenges, and future prospects.Frontiers in immunology · 2024Review
- Selection of biophysically favorable antibody variants using a modified Flp-In CHO mammalian display platform.Frontiers in bioengineering and biotechnology · 2023Article
- Joined at the hip: The role of light chain complementarity determining region 2 in antibody self-association.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Agonist antibody discovery: Experimental, computational, and rational engineering approaches.Drug discovery today · 2022Review
- High-throughput functional screening for next-generation cancer immunotherapy using droplet-based microfluidics.Science advances · 2021Article
- Antibody Libraries as Tools to Discover Functional Antibodies and Receptor Pleiotropism.International journal of molecular sciences · 2021Review
- A phage-displayed single-chain Fab library optimized for rapid production of single-chain IgGs.Protein science : a publication of the Protein Society · 2020Article
- Selection of a Full Agonist Combinatorial Antibody that Rescues Leptin Deficiency In Vivo.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- A strategy for the selection of monovalent antibodies that span protein dimer interfaces.The Journal of biological chemistry · 2019Article
- Article
- Phenotypic selection with an intrabody library reveals an anti-apoptotic function of PKM2 requiring Mitofusin-1.PLoS biology · 2019Article
- A Human-Derived Monoclonal Antibody Targeting Extracellular Connexin Domain Selectively Modulates Hemichannel Function.Frontiers in physiology · 2019Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A method is presented that uses combinatorial antibody libraries to endow cells with new binding energy landscapes for the purpose of regulating their phenotypes. Antibodies that are expressed in cells infected with a lentiviral combinatorial antibody library are selected directly for function rather than only for binding. The potential diversity space can be very large because more than one lentivirus can infect a single cell. Thus, the initial combinatorial diversity of ~1.0 × 10(11) members generated by the random association of antibody heavy and light chains is greatly increased by the reassortment of the antibody Fv domains themselves inside cells. The power of the system is illustrated by its ability to select unusual antibodies. Here, the selected antibodies are potent erythropoietin agonists whose ontogeny depends on recombination at the protein level of pairs of antibodies expressed in the same cell to generate heterodimeric bispecific antibodies. The obligate synergy between the different binding specificities of the antibody's monomeric subunits appears to replicate the asymmetric binding mechanism of authentic erythropoietin.
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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.