ArticleCommunications biology2023
Effect of Fc core fucosylation and light chain isotype on IgG1 flexibility.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Characterization of Full-Length Antibody Complexes Through HDX-Mass Spectrometry Coupled With NMR Spectroscopy: New Insight Into Avelumab/PD-L1 Interaction.Angewandte Chemie (International ed. in English) · 2026Article
- Molecular Basis of Core Fucosylation-Dependent Modulation of IgG1 Fc-CD16a Binding.bioRxiv : the preprint server for biology · 2026Article
- A Chemoenzymatic Method To Systematically Quantify Core Fucosylation Stoichiometry of Glycoproteins and Reveal Its Roles in EMT and Embryonic Development.Analytical chemistry · 2026Article
- A versatile platform for sequential glyco-, phospho-, and proteomics with multi-PTMs integration.Nature communications · 2026Article
- Light Chain Isotype and Antibody-Specificity Impact on Virus Neutralization.Antibodies (Basel, Switzerland) · 2025Article
- Antigen binding triggers long-range conformational changes in monoclonal antibodies.Frontiers in immunology · 2025Article
- Refined Protein-Sugar Interactions in the Martini Force Field.Journal of chemical theory and computation · 2024Article
- Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
N-glycosylation plays a key role in modulating the bioactivity of monoclonal antibodies (mAbs), as well as the light chain (LC) isotype can influence their physicochemical properties. However, investigating the impact of such features on mAbs conformational behavior is a big challenge, due to the very high flexibility of these biomolecules. In this work we investigate, by accelerated molecular dynamics (aMD), the conformational behavior of two commercial immunoglobulins G1 (IgG1), representative of κ and λ LCs antibodies, in both their fucosylated and afucosylated forms. Our results show, through the identification of a stable conformation, how the combination of fucosylation and LC isotype modulates the hinge behavior, the Fc conformation and the position of the glycan chains, all factors potentially affecting the binding to the FcγRs. This work also represents a technological enhancement in the conformational exploration of mAbs, making aMD a suitable approach to clarify experimental results.
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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.