Evidence map›Paper›PMID 31504525›Full record

ReviewGlycobiology2020

The history of IgG glycosylation and where we are now.

Brian A Cobb

Abstract readHistorical ArticleReview
In one paragraph

Review in Glycobiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
–field-weighted citation impact
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

111 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Selective fluorination of Fc glycans enhances antibody-mediated effector functions.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Review
  12. Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026
    Review
  13. Not all antibodies are created equal: total IgG glycosylation and severity of antibody-mediated rejection in kidney transplantation.Transplant international : official journal of the European Society for Organ Transplantation · 2026
    Article
  14. Article
  15. Immunoglobulin G in aging and cancer.Frontiers in immunology · 2026
    Review
  16. Endothelial cells sialylate IgG within the FcRn-mediated recycling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article

51 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

1 author.

Brian A CobbDepartment of Pathology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106, USA.

Funding

Regulatory Mechanisms of Glycoprotein SialylationR01GM115234 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI Brian A Cobb · 2016 to 2026
$5.1M
NIGMS NIH HHS R01 GM115234
6 · The paper itself

Abstract

IgG glycosylation is currently at the forefront of both immunology and glycobiology, likely due in part to the widespread and growing use of antibodies as drugs. For over four decades, it has been recognized that the conserved N-linked glycan on asparagine 297 found within the second Ig domain of the heavy chain (CH2) that helps to comprise Fc region of IgG plays a special role in IgG structure and function. Changes in galactosylation, fucosylation and sialylation are now well-established factors, which drive differential IgG function, ranging from inhibitory/anti-inflammatory to activating complement and promoting antibody-dependent cellular cytotoxicity. Thus, if we are to truly understand how to design and deploy antibody-based drugs with maximal efficacy and evaluate proper vaccine responses from a protective and functional perspective, a deep understanding of IgG glycosylation is essential. This article is intended to provide a comprehensive review of the IgG glycosylation field and the impact glycans have on IgG function, beginning with the earliest findings over 40 years ago, in order to provide a robust foundation for moving forward.

Indexed as

AnimalsGlycosylationHistory, 20th CenturyHistory, 21st CenturyHumansImmunoglobulin GPolysaccharidesImmunoglobulin GPolysaccharidesglycanglycosylationIgGsialylation

Identifiers

PMID31504525
PMCPMC7109348

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.