ArticleScientific reports2017
Effects of N-Glycan Composition on Structure and Dynamics of IgG1 Fc and Their Implications for Antibody Engineering.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Antibody-drug conjugate engineering: from design to efficacy and safety.Signal transduction and targeted therapy · 2026Review
- Molecular Basis of Core Fucosylation-Dependent Modulation of IgG1 Fc-CD16a Binding.bioRxiv : the preprint server for biology · 2026Article
- Platform-Specific FcAntibodies (Basel, Switzerland) · 2024Article
- Effects of glycans and hinge on dynamics in the IgG1 Fc.Journal of biomolecular structure & dynamics · 2024Article
- Chromatographic Analysis of theACS omega · 2023Article
- Extensive substrate recognition by the streptococcal antibody-degrading enzymes IdeS and EndoS.Nature communications · 2022Article
- Definition of IgG Subclass-Specific Glycopatterns in Idiopathic Membranous Nephropathy: Aberrant IgG Glycoforms in Blood.International journal of molecular sciences · 2022Article
- On the Use of Surface Plasmon Resonance Biosensing to Understand IgG-FcγR Interactions.International journal of molecular sciences · 2021Review
- Global variability of the human IgG glycome.Aging · 2020Article
- Biophysical characterization of dynamic structures of immunoglobulin G.Biophysical reviews · 2020Review
- A synopsis of recent developments defining how N-glycosylation impacts immunoglobulin G structure and function.Glycobiology · 2020Review
- Reprogramming the Constant Region of Immunoglobulin G Subclasses for Enhanced Therapeutic Potency against Cancer.Biomolecules · 2020Review
- Boosting therapeutic potency of antibodies by taming Fc domain functions.Experimental & molecular medicine · 2019Review
- Dynamic Views of the Fc Region of Immunoglobulin G Provided by Experimental and Computational Observations.Antibodies (Basel, Switzerland) · 2019Article
- CHARMM-GUI Glycan Modeler for modeling and simulation of carbohydrates and glycoconjugates.Glycobiology · 2019Article
- Intradomain Interactions in an NMDA Receptor Fragment Mediate N-Glycan Processing and Conformational Sampling.Structure (London, England : 1993) · 2019Article
- Article
- Predicting the Structures of Glycans, Glycoproteins, and Their Complexes.Chemical reviews · 2018Review
- Impact of Glycosylation on the Local Backbone Flexibility of Well-Defined IgG1-Fc Glycoforms Using Hydrogen Exchange-Mass Spectrometry.Journal of pharmaceutical sciences · 2018Article
- In Silico Methods in Antibody Design.Antibodies (Basel, Switzerland) · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Immunoglobulin G1 (IgG1), a subclass of human serum antibodies, is the most widely used scaffold for developing monoclonal antibodies to treat human diseases. The composition of asparagine(N)297-linked glycans can modulate the binding affinity of IgG1 Fc to Fc γ receptors, but it is unclear how the structural modifications of N-glycan termini, which are distal from the binding interface, contribute to the affinity. Through atomistic molecular dynamics simulations of a series of sequentially truncated high-mannose IgG1 Fc glycoforms, we found that the C'E loop and the Cγ2-Cγ3 orientation are highly dynamic, and changes in N-glycan composition alter their conformational ensembles. High-mannose glycoform preferentially samples conformations that are more competent to FcγRIIIa binding, compared to the truncated glycoforms, suggesting a role of IgG1 Fc N-glycan in optimizing the interface with the Fc receptor for efficient binding. The trajectory analyses also reveal that the N-glycan has large amplitude motions and the carbohydrate moiety interconverts between Fc-bound and unbound forms, enabling enzymatic modification of the glycan termini.
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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.