ArticleScientific reports2018
Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 25 citations in OpenAlex.
- Antibodies targeting a shared epitope exploit IgE allostery to drive distinct functional outcomes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A Comparison of Natural and Therapeutic Anti-IgE Antibodies.Antibodies (Basel, Switzerland) · 2024Review
- IgE Immune Complexes Mitigate Eosinophilic Immune Responses through NLRC4 Inflammasome.Mediators of inflammation · 2023Article
- Immunologic, genetic, and ecological interplay of factors involved in allergic diseases.Frontiers in allergy · 2023Review
- IgE-neutralizing UB-221 mAb, distinct from omalizumab and ligelizumab, exhibits CD23-mediated IgE downregulation and relieves urticaria symptoms.The Journal of clinical investigation · 2022Article
- Bispecific T-Cell Engagers Targeting Membrane-Bound IgE.Biomedicines · 2021Article
- Review
- Anti-IgE for the Treatment of Chronic Urticaria.ImmunoTargets and therapy · 2021Review
- Past, present, and future of anti-IgE biologics.Allergy · 2020Review
- Immunoglobulins or Antibodies: IMGTBiomedicines · 2020Review
- NMR backbone assignment of the Cε4 domain of immunoglobulin E.Biomolecular NMR assignments · 2020Article
- Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Identification of Amino Acid Residues in Human IgM Fc Receptor (FcµR) Critical for IgM Binding.Frontiers in immunology · 2020Article
- Article
- Sex difference in IgE sensitization associated with alcohol consumption in the general population.Scientific reports · 2019Article
- IgE Antibodies: From Structure to Function and Clinical Translation.Antibodies (Basel, Switzerland) · 2019Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
Abstract
Immunoglobulin E (IgE) antibodies play a central role in the allergic response: interaction with FcεRI on mast cells and basophils leads to immediate hypersensitivity reactions upon allergen challenge, while interaction with CD23/FcεRII, expressed on a variety of cells, regulates IgE synthesis among other activities. The receptor-binding IgE-Fc region has recently been found to display remarkable flexibility, from acutely bent to extended conformations, with allosteric communication between the distant FcεRI and CD23 binding sites. We report the structure of an anti-IgE antibody Fab (8D6) bound to IgE-Fc through a mixed protein-carbohydrate epitope, revealing further flexibility and a novel extended conformation with potential relevance to that of membrane-bound IgE in the B cell receptor for antigen. Unlike the earlier, clinically approved anti-IgE antibody omalizumab, 8D6 inhibits binding to FcεRI but not CD23; the structure reveals how this discrimination is achieved through both orthosteric and allosteric mechanisms, supporting therapeutic strategies that retain the benefits of CD23 binding.
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What OpenQuestion holds
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.