ArticlemAbs2025
IL-17A complexes with therapeutic antibodies exhibit distinct size distributions, potentially contributing to clinically observed immunogenicity.
Article in mAbs, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- De novo epitope-specific antibody design via time-dependent guidance.Bioinformatics (Oxford, England) · 2026Article
- Interleukin-17 in disease pathogenesis and therapy: recent advances in targeted drug design and medicinal chemistry.Frontiers in pharmacology · 2026Review
- Evaluating Drug-Target Complexes in Therapeutic Monoclonal Antibodies Using A4F-MALS: Implications for Drug Development and Clinical Design.Journal of immunology research · 2026Article
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Authors and funding
9 authors.
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Abstract
Monoclonal antibodies are well established as promising treatment options for a broad range of patients with severe diseases. In some cases, the formation of anti-drug antibodies (ADA) may limit their clinical use and potentially affect safety and efficacy for patients. Despite extensive research, some factors contributing to the immunogenicity of therapeutic antibodies remain poorly understood. In particular, the immunogenicity potential associated with multivalent antibody formats targeting oligomeric protein antigens has thus far received insufficient attention. Large, target-related immune complexes (TRICs) may be formed that can trigger Fc-mediated downstream effects and have the potential to contribute to the development of an ADA response. Here, we present experimental evidence highlighting the roles of epitope, paratope, and binding geometry in defining the composition and size distribution of TRICs formed by IL-17A, a homodimeric cytokine, with four clinical anti-IL-17 antibodies, secukinumab (Cosentyx
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