ArticleMolecular immunology2013
Conformational plasticity at the IgE-binding site of the B-cell receptor CD23.
Article in Molecular immunology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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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
7 citing papers in PubMed, 17 citations in OpenAlex.
- 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
- Review
- Reviving lost binding sites: Exploring calcium-binding site transitions between human and murine CD23.FEBS open bio · 2021Article
- The structure-based cancer-related single amino acid variation prediction.Scientific reports · 2021Article
- IgE Antibodies: From Structure to Function and Clinical Translation.Antibodies (Basel, Switzerland) · 2019Review
- IgE binds asymmetrically to its B cell receptor CD23.Scientific reports · 2017Article
- A range of Cℇ3-Cℇ4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.Acta crystallographica. Section F, Structural biology communications · 2014Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, FcɛRI and CD23. Crosslinking of FcɛRI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding.
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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.