Evidence map›Paper›PMID 27796794›Full record

ReviewCurrent allergy and asthma reports2016

Immunoglobulin Glycosylation Effects in Allergy and Immunity.

Alexandra Epp, Kathryn C Sullivan, Andrew B Herr, Richard T Strait

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current allergy and asthma reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Total IgE as a Marker for Chronic Spontaneous Urticaria.Allergy, asthma & immunology research · 2021
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. IgE Antibodies against Cancer: Efficacy and Safety.Antibodies (Basel, Switzerland) · 2020
    Review
  18. Article
  19. Clinical application of quantitative glycomics.Expert review of proteomics · 2018
    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

4 authors at 3 institutions in 2 countries.

Alexandra EppInstitute for Systemic Inflammation Research, University of Lübeck, Lübeck, Germany.
Kathryn C SullivanImmunology Graduate Program, Cincinnati Children's Hospital Medical Center and the University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Andrew B HerrDivision of Immunobiology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, USA.
Richard T StraitDepartment of Pediatrics, College of Medicine, University of Cincinnati, Cincinnati, OH, USA. rick.strait@cchmc.org.
University of Cincinnati Medical Center · USUniversity of Cincinnati · USUniversity of Lübeck · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purpose of reviewThe aim of this review will be to familiarize the reader with the general area of antibody (Ab) glycosylation and to summarize the known functional roles of glycosylation and how glycan structure can contribute to various disease states with emphasis on allergic disease. RECENT

findingsBoth immunoglobulin (Ig) isotype and conserved Fc glycosylation sites often dictate the downstream activity of an Ab where complexity and degree of glycosylation contribute to its ability to bind Fc receptors (FcRs) and activate complement. Most information on the effects of glycosylation center on IgG in cancer therapy and autoimmunity. In cancer therapy, glycosylation modifications that enhance affinity for activating FcRs are utilized to facilitate immune-mediated tumor cell killing. In autoimmunity, disease severity has been linked to alterations in the presence, location, and composition of Fc glycans. Significantly less is understood about the role of glycosylation in the setting of allergy and asthma. However, recent data demonstrate that glycosylation of IgE at the asparagine-394 site of Cε3 is necessary for IgE interaction with the high affinity IgE receptor but, surprisingly, glycosylation has no effect on IgE interaction with its low-affinity lectin receptor, CD23. Variations in the specific glycoform may modulate the interaction of an Ig with its receptors. Significantly more is known about the functional effects of glycosylation of IgG than for other Ig isotypes. Thus, the role of glycosylation is much better understood in the areas of autoimmunity and cancer therapy, where IgG is the dominant isotype, than in the field of allergy, where IgE predominates. Further work is needed to fully understand the role of glycan variation in IgE and other Ig isotypes with regard to the inhibition or mediation of allergic disease.

Indexed as

GlycosylationHumansHypersensitivityImmunoglobulinsImmunoglobulinsAllergyAsthmaImmunoglobulin glycosylationSialylation

Identifiers

PMID27796794
OpenAlexW2542865440

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.