ArticleProceedings of the National Academy of Sciences of the United States of America2025
Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 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
6 citing papers in PubMed.
- Chemoenzymatic synthesis of unusual antibody glycoforms using E. coli expressed human and bovine β-1,4-galactosyltransferase and their mutants.Carbohydrate research · 2026Article
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- The impact of glycosylation on the conformational ensembles of β-, δ-, and γ-sarcoglycans.Biophysical journal · 2026Article
- Selective fluorination of Fc glycans enhances antibody-mediated effector functions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Unlabeled NMR Approach with Site-Specific Methyl Assignments for Structural Evaluation of the IgG1 Fc Region.Journal of the American Chemical Society · 2026Article
- Key Role of Pro230 in the Hinge Region on the Architecture and Function of IgG1.Journal of medicinal chemistry · 2026Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors.
Funding
Abstract
We investigate the impact of glycoform alterations on the dynamic structure of the human immunoglobulin G1 (IgG1) Fc region using integrated computational and experimental approaches. Four distinct IgG1-Fc glycoforms, varying in core fucosylation and nonreducing terminal galactosylation, were generated through a combination of cell engineering and in vitro enzymatic reactions. Stable-isotope-assisted NMR spectroscopy, incorporating both glycan and protein signals, revealed that galactosylation induces chemical shift perturbations extending from the glycan-protein interface to the C
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Registered trials
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