Evidence map›Paper›PMID 31616919›Full record

ReviewGlycobiology2020

On enzymatic remodeling of IgG glycosylation; unique tools with broad applications.

Jonathan Sjögren, Rolf Lood, Andreas Nägeli

Open access · hybridAbstract 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. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026
    Review
  5. Review
  6. Review
  7. TREK2 Lipid Binding Preferences Revealed by Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  8. Increasing Rate of FatalMicroorganisms · 2024
    Article
  9. Article
  10. Platform-Specific FcAntibodies (Basel, Switzerland) · 2024
    Article
  11. Immunomodulating Enzymes fromMicroorganisms · 2024
    Review
  12. Article
  13. Introduction of Carbonyl Groups into Antibodies.Molecules (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Article
  16. Recombinant mucin biotechnology and engineering.Advanced drug delivery reviews · 2023
    Review
  17. Review
  18. Article
  19. Article
  20. 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.

Jonathan SjögrenGenovis AB, Scheelevägen 2, 223 63 Lund, Sweden.
Rolf LoodGenovis AB, Scheelevägen 2, 223 63 Lund, Sweden.
Andreas NägeliGenovis AB, Scheelevägen 2, 223 63 Lund, Sweden.
Genovis (Sweden) · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The importance of IgG glycosylation has been known for many years not only by scientists in glycobiology but also by human pathogens that have evolved specific enzymes to modify these glycans with fundamental impact on IgG function. The rise of IgG as a major therapeutic scaffold for many cancer and immunological indications combined with the availability of unique enzymes acting specifically on IgG Fc-glycans have spurred a range of applications to study this important post-translational modification on IgG. This review article introduces why the IgG glycans are of distinguished interest, gives a background on the unique enzymatic tools available to study the IgG glycans and finally presents an overview of applications utilizing these enzymes for various modifications of the IgG glycans. The applications covered include site-specific glycan transglycosylation and conjugation, analytical workflows for monoclonal antibodies and serum diagnostics. Additionally, the review looks ahead and discusses the importance of O-glycosylation for IgG3, Fc-fusion proteins and other new formats of biopharmaceuticals.

Indexed as

AnimalsGlycoproteinsGlycoside HydrolasesHumansImmunoglobulin GPolysaccharidesGlycoproteinsGlycoside Hydrolasesglycosylated IgGImmunoglobulin GPolysaccharidesAntibodiesEndoglycosidasesEndoSEnzymatic tools/IgG glycosylation

Identifiers

PMID31616919
PMCPMC7109354
OpenAlexW2980651327

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.