Evidence map›Paper›PMID 34495537›Full record

ArticleAdvances in experimental medicine and biology2021

Glycosylation in Autoimmune Diseases.

Marta Ząbczyńska, Paweł Link-Lenczowski, Ewa Pocheć

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Advances in experimental medicine and biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
9.4field-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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. 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
  2. Article
  3. Glycosylation Regulation by TMEM230 in Aging and Autoimmunity.International journal of molecular sciences · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Age-Related Changes in SerumBiomolecules · 2023
    Article
  8. Review
  9. TheBiomolecules · 2023
    Article
  10. The Role of B Cell and T Cell Glycosylation in Systemic Lupus Erythematosus.International journal of molecular sciences · 2023
    Review
  11. Article
  12. The role ofFrontiers in immunology · 2023
    Review
  13. Article
  14. Changes of IgGFrontiers in immunology · 2022
    Article
  15. Review
  16. Review
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.

Marta ZąbczyńskaDepartment of Glycoconjugate Biochemistry, Institute of Zoology and Biomedical Research, Faculty of Biology, Jagiellonian University, Kraków, Poland.
Paweł Link-LenczowskiDepartment of Medical Physiology, Jagiellonian University Medical College, Kraków, Poland.
Ewa PochećDepartment of Glycoconjugate Biochemistry, Institute of Zoology and Biomedical Research, Faculty of Biology, Jagiellonian University, Kraków, Poland. ewa.pochec@uj.edu.pl.
Jagiellonian University · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autoimmune diseases are accompanied by changes in protein glycosylation, in both the immune system and target tissues. The best-studied alteration in autoimmunity is agalactosylation of immunoglobulin G (IgG), characterized primarily in rheumatoid arthritis (RA), and then detected also in systemic lupus erythematosus (SLE), inflammatory bowel disease (IBD), and multiple sclerosis (MS). The rebuilding of IgG N-glycans in RA correlates with the relapses and remissions of the disease, is associated with physiological states such as pregnancy but also depends on applied anti-inflammatory therapy. In turn, a decreased core fucosylation of the whole pool of IgG N-glycans is a serum glycomarker in autoimmune thyroid diseases (AITD) encompassing Hashimoto's thyroiditis (HT) and Grave's disease (GD). However, fucosylation of anti-thyroglobulin IgG (an immunological marker of HT) was elevated in HT serum. Core fucosylation of IgG oligosaccharides was also lowered in MS and SLE. In AITD and IBD, chronic inflammation T lymphocytes showed the reduced expression of MGAT5 gene encoding β1,6-N-acetylglucosaminyltransferase V (GnT-V) responsible for β1,6-branching of N-glycans, which is important for T cell receptor activation. Structural changes of glycans have a profound effect on the pro-inflammatory activity of immune cells and serum immune proteins, including IgG in autoimmunity.

Indexed as

Autoimmune DiseasesHashimoto DiseaseLupus Erythematosus, SystemicGlycosylationHumansImmunoglobulin GImmunoglobulin GAutoimmune diseasesCore fucosylationGalactosylationGlycosylationSialylationβ1,6-branching

Identifiers

PMID34495537
OpenAlexW3198870601

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.