Evidence map›Paper›PMID 31281930›Full record

ReviewGlycobiology2020

Monitoring of immunoglobulin N- and O-glycosylation in health and disease.

Noortje de Haan, David Falck, Manfred Wuhrer

Registry-linked trialOpen access · bronzeAbstract readReview
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. It is linked to trial NCT05301231 (Omics-based Predictors of NAFLD/Potential NASH), which is not on this map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.7field-weighted citation impact, top 3% 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.

NCT05301231 unknown statusnot on this mapstarted 2022, after this paper: background citation

Omics-based Predictors of NAFLD/Potential NASH: A New Era Towards Valid and Reliable Non-invasive Diagnosis and Personalized Therapy

Typeobservational_patient_registrySponsorNational Research Centre, EgyptRan2022 to 2024Enrolled450ConditionsNon-Alcoholic Fatty Liver Disease, Non Alcoholic SteatohepatitisArmsGenomics (DNA Extraction), Epi-genomics, Proteomics (Glycoproteomics), Salivary Metabolomics, Individualized counselling for behavioural modification
3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Article
  3. Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026
    Review
  4. Antibody glycosylation in neuroimmune diseases.Journal of translational medicine · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Glycosylation in Cancer.Handbook of experimental pharmacology · 2025
    Review
  13. Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025
    Review
  14. Frontiers in immunology · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

5 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

3 authors at 1 institution in 1 country.

Noortje de HaanCenter for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333ZA Leiden, The Netherlands.
David FalckCenter for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333ZA Leiden, The Netherlands.
Manfred WuhrerCenter for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333ZA Leiden, The Netherlands.
Leiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein N- and O-glycosylation are well known co- and post-translational modifications of immunoglobulins. Antibody glycosylation on the Fab and Fc portion is known to influence antigen binding and effector functions, respectively. To study associations between antibody glycosylation profiles and (patho) physiological states as well as antibody functionality, advanced technologies and methods are required. In-depth structural characterization of antibody glycosylation usually relies on the separation and tandem mass spectrometric (MS) analysis of released glycans. Protein- and site-specific information, on the other hand, may be obtained by the MS analysis of glycopeptides. With the development of high-resolution mass spectrometers, antibody glycosylation analysis at the intact or middle-up level has gained more interest, providing an integrated view of different post-translational modifications (including glycosylation). Alongside the in-depth methods, there is also great interest in robust, high-throughput techniques for routine glycosylation profiling in biopharma and clinical laboratories. With an emphasis on IgG Fc glycosylation, several highly robust separation-based techniques are employed for this purpose. In this review, we describe recent advances in MS methods, separation techniques and orthogonal approaches for the characterization of immunoglobulin glycosylation in different settings. We put emphasis on the current status and expected developments of antibody glycosylation analysis in biomedical, biopharmaceutical and clinical research.

Indexed as

Communicable DiseasesGlycosylationHumansImmunoglobulinsPolysaccharidesTandem Mass SpectrometryImmunoglobulinsPolysaccharidesantibodybiopharmaceuticalglycanglycoproteomicsmass spectrometry

Identifiers

PMID31281930
PMCPMC7225405
OpenAlexW2962516949

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

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.