Evidence map›Paper›PMID 27639381›Full record

ReviewCellular and molecular life sciences : CMLS2017

Regulation of antibody effector functions through IgG Fc N-glycosylation.

Isaak Quast, Benjamin Peschke, Jan D Lünemann

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. 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
  7. Article
  8. Review
  9. Characterization ofPharmaceuticals (Basel, Switzerland) · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Introduction of Carbonyl Groups into Antibodies.Molecules (Basel, Switzerland) · 2023
    Review
  15. Article
  16. Article
  17. TheBiomolecules · 2023
    Article
  18. Article
  19. Review
  20. Article
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

3 authors at 1 institution in 1 country.

Isaak QuastLaboratory of Neuroinflammation, Department of Neuroinflammation, Institute of Experimental Immunology, University of Zürich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Benjamin PeschkeLaboratory of Neuroinflammation, Department of Neuroinflammation, Institute of Experimental Immunology, University of Zürich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
Jan D LünemannLaboratory of Neuroinflammation, Department of Neuroinflammation, Institute of Experimental Immunology, University of Zürich, Winterthurerstrasse 190, 8057, Zurich, Switzerland. jan.luenemann@uzh.ch.ORCID 0000-0002-3007-708X
University of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Immunoglobulin gamma (IgG) antibodies are key effector proteins of the immune system. They recognize antigens with high specificity and are indispensable for immunological memory following pathogen exposure or vaccination. The constant, crystallizable fragment (Fc) of IgG molecules mediates antibody effector functions such as complement-dependent cytotoxicity, antibody-mediated cellular cytotoxicity, and antibody-dependent cell-mediated phagocytosis. These functions are regulated by a single N-linked, biantennary glycan of the heavy chain, which resides just below the hinge region, and the presence of specific sugar moieties on the glycan has profound implications on IgG effector functions. Emerging knowledge of how Fc glycans contribute to IgG structure and functions has opened new avenues for the therapeutic exploitation of defined antibody glycoforms in the treatment of cancer and autoimmune diseases. Here, we review recent advances in understanding proinflammatory IgG effector functions and their regulation by Fc glycans.

Indexed as

AnimalsComplement System ProteinsGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GPolysaccharidesComplement System ProteinsImmunoglobulin Fc FragmentsImmunoglobulin GPolysaccharidesAntibodyGlycanGlycobiologyImmunoglobulinImmunologyImmunotherapy

Identifiers

PMID27639381
PMCPMC11107549
OpenAlexW2520002898

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.