Evidence map›Paper›PMID 26211613›Full record

ArticleStructure (London, England : 1993)2015

The Structural Role of Antibody N-Glycosylation in Receptor Interactions.

Ganesh P Subedi, Adam W Barb

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed, 1 pooled it
14.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

132 citing papers in PubMed, 1 synthesis or guideline pooled it, 202 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026
    Review
  14. Antibody glycosylation in neuroimmune diseases.Journal of translational medicine · 2025
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

72 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Ganesh P SubediRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, 2214 Molecular Biology Building, Ames, IA 50011, USA.
Adam W BarbRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, 2214 Molecular Biology Building, Ames, IA 50011, USA. Electronic address: abarb@iastate.edu.
Iowa State University · US

Funding

NMR Studies on the Role of the Essential IgG N-Glycan in Immune System ActivationK22AI099165 · NIAID · IOWA STATE UNIVERSITY · PI BARB, ADAM WESLEY · 2013 to 2014
$267k
NIAID NIH HHS K22 AI099165
6 · The paper itself

Abstract

Asparagine(N)297-linked glycosylation of immunoglobulin G (IgG) Fc is required for binding to FcγRIIa, IIb, and IIIa, although it is unclear how it contributes. We found the quaternary structure of glycosylated Fc was indistinguishable from aglycosylated Fc, indicating that N-glycosylation does not maintain relative Fc Cγ2/Cγ3 domain orientation. However, the conformation of the C'E loop, which contains N297, was significantly perturbed in the aglycosylated Fc variant. The conformation of the C'E loop as measured with a range of Fc variants shows a strong correlation with FcγRIIIa affinity. These results indicate that the primary role of the IgG1 Fc N-glycan is to stabilize the C'E loop through intramolecular interactions between carbohydrate and amino acid residues, and preorganize the FcγRIIIa interface for optimal binding affinity. The features that contribute to the capacity of the IgG1 Fc N-glycan to restrict protein conformation and tune binding affinity are conserved in other antibodies including IgG2-IgG4, IgD, IgE, and IgM.

Indexed as

AsparagineCrystallography, X-RayGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GModels, MolecularProtein BindingProtein Structure, QuaternaryAsparagineImmunoglobulin Fc FragmentsImmunoglobulin G

Identifiers

PMID26211613
PMCPMC4558368
OpenAlexW1929486047

What OpenQuestion holds

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Registered trials

None linked

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.