ArticleProtein engineering, design & selection : PEDS2014
In vitro Fab display: a cell-free system for IgG discovery.
Article in Protein engineering, design & selection : PEDS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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.
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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
21 citing papers in PubMed, 42 citations in OpenAlex.
- Artificial intelligence advancements in monoclonal antibody development technology.Frontiers in immunology · 2026Review
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- Monoclonal antibodies: From magic bullet to precision weapon.Molecular biomedicine · 2024Review
- Human-derived monoclonal autoantibodies as interrogators of cellular proteotypes in the brain.Trends in neurosciences · 2024Review
- Development, High-Throughput Profiling, and Biopanning of a Large Phage Display Single-Domain Antibody Library.International journal of molecular sciences · 2024Article
- An Integrated In Vivo/In Vitro Protein Production Platform for Site-Specific Antibody Drug Conjugates.Bioengineering (Basel, Switzerland) · 2023Article
- Discovery of STRO-002, a Novel Homogeneous ADC Targeting Folate Receptor Alpha, for the Treatment of Ovarian and Endometrial Cancers.Molecular cancer therapeutics · 2023Article
- Ribosome Display Technology: Applications in Disease Diagnosis and Control.Antibodies (Basel, Switzerland) · 2020Review
- Cell-Free Protein Synthesis: A Promising Option for Future Drug Development.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020Review
- Synthetic antibodies against BRIL as universal fiducial marks for single-particle cryoEM structure determination of membrane proteins.Nature communications · 2020Article
- Synthetic Biology Goes Cell-Free.BMC biology · 2019Review
- High frequency of CD74 expression in lymphomas: implications for targeted therapy using a novel anti-CD74-drug conjugate.The journal of pathology. Clinical research · 2019Article
- Targeting CD74 in multiple myeloma with the novel, site-specific antibody-drug conjugate STRO-001.Oncotarget · 2018Article
- Ecobody technology: rapid monoclonal antibody screening method from single B cells using cell-free protein synthesis for antigen-binding fragment formation.Scientific reports · 2017Article
- The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Methods in molecular biology (Clifton, N.J.) · 2017Review
- Cell-Free Synthetic Biology: Engineering Beyond the Cell.Cold Spring Harbor perspectives in biology · 2016Review
- Yeast knockout library allows for efficient testing of genomic mutations for cell-free protein synthesis.Synthetic and systems biotechnology · 2016Article
- Conceptual and methodological advances in cell-free directed evolution.Current opinion in structural biology · 2015Review
- An improved single-chain Fab platform for efficient display and recombinant expression.Journal of molecular biology · 2015Article
- Advances in the directed evolution of proteins.Current opinion in chemical biology · 2014Review
Corrections and comments
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Authors and funding
19 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selection technologies such as ribosome display enable the rapid discovery of novel antibody fragments entirely in vitro. It has been assumed that the open nature of the cell-free reactions used in these technologies limits selections to single-chain protein fragments. We present a simple approach for the selection of multi-chain proteins, such as antibody Fab fragments, using ribosome display. Specifically, we show that a two-chain trastuzumab (Herceptin) Fab domain can be displayed in a format which tethers either the heavy or light chain to the ribosome while retaining functional antigen binding. Then, we constructed synthetic Fab HC and LC libraries and performed test selections against carcinoembryonic antigen (CEA) and vascular endothelial growth factor (VEGF). The Fab selection output was reformatted into full-length immunoglobulin Gs (IgGs) and directly expressed at high levels in an optimized cell-free system for immediate screening, purification and characterization. Several novel IgGs were identified using this cell-free platform that bind to purified CEA, CEA positive cells and VEGF.
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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.