ArticleThe Journal of biological chemistry2017
Allosteric mechanism of action of the therapeutic anti-IgE antibody omalizumab.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.
- The efficacy and safety of omalizumab in the treatment of asthma: an overview of systematic reviews and meta analyses.Frontiers in medicine · 2025Pooled it
- 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
- Review
- Toward personalized prediction: a multicenter machine learning model for omalizumab response duration in moderate-to-severe perennial allergic rhinitis.Frontiers in allergy · 2026Article
- Long-range allosteric communication within antibodies affects antigen-binding affinity.Frontiers in immunology · 2026Article
- Off-label applications of omalizumab: Current insights and perspectives.The World Allergy Organization journal · 2025Review
- Article
- Autoallergy and what the Allergist Needs to know.Current allergy and asthma reports · 2025Review
- LP-003, a novel high-affinity anti-IgE antibody for inadequately controlled seasonal allergic rhinitis: A multicenter, randomized, double-blind, placebo-controlled phase 2 clinical trial.Clinical and translational allergy · 2025Article
- Structural and Functional Insights Into IgE Receptor Interactions and Disruptive Inhibition.Immunological reviews · 2025Review
- The Crystal Structure of Human IgD-Fc Reveals Unexpected Differences With Other Antibody Isotypes.Proteins · 2025Article
- Emerging diagnostic and therapeutic opportunities in food allergy.Frontiers in immunology · 2025Review
- Therapeutic monoclonal antibodies in allergy: Targeting IgE, cytokine, and alarmin pathways.Immunological reviews · 2024Review
- Allosteric inhibition of IgE-FcεRI interactions by simultaneous targeting of IgE F(ab')2 epitopes.Communications biology · 2024Article
- Immunologic, genetic, and ecological interplay of factors involved in allergic diseases.Frontiers in allergy · 2023Review
- IgE Immune Complexes Mitigate Eosinophilic Immune Responses through NLRC4 Inflammasome.Mediators of inflammation · 2023Article
- New Mechanistic Advances in FcεRI-Mast Cell-Mediated Allergic Signaling.Clinical reviews in allergy & immunology · 2022Review
- 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
- Computational counterselection identifies nonspecific therapeutic biologic candidates.Cell reports methods · 2022Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 4 institutions in 1 country.
Funding
Abstract
Immunoglobulin E and its interactions with receptors FcϵRI and CD23 play a central role in allergic disease. Omalizumab, a clinically approved therapeutic antibody, inhibits the interaction between IgE and FcϵRI, preventing mast cell and basophil activation, and blocks IgE binding to CD23 on B cells and antigen-presenting cells. We solved the crystal structure of the complex between an omalizumab-derived Fab and IgE-Fc, with one Fab bound to each Cϵ3 domain. Free IgE-Fc adopts an acutely bent structure, but in the complex it is only partially bent, with large-scale conformational changes in the Cϵ3 domains that inhibit the interaction with FcϵRI. CD23 binding is inhibited sterically due to overlapping binding sites on each Cϵ3 domain. Studies of omalizumab Fab binding in solution demonstrate the allosteric basis for FcϵRI inhibition and, together with the structure, reveal how omalizumab may accelerate dissociation of receptor-bound IgE from FcϵRI, exploiting the intrinsic flexibility and allosteric potential of IgE.
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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.