Evidence map›Paper›PMID 26497518›Full record

ReviewImmunological reviews2015

Human IgG4: a structural perspective.

Anna M Davies, Brian J Sutton

Registry-linked trialOpen access · hybridAbstract readReview
In one paragraph

Review in Immunological reviews, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02654288 (Dynamic Changes of the Serum Level of Immunoglobulin G4), which is not on this map. Cited by 97 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed, 1 pooled it
10.3field-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.

NCT02654288 unknown statusnot on this mapstarted 2016, after this paper: background citation

Dynamic Changes of the Serum Level of Immunoglobulin G4(IgG4) and Interleukin-10(IL-10) in the Patients of Pancreatic Cancer After Gemcitabine-based Chemotherapy

TypeobservationalSponsorPeking Union Medical College HospitalRan2016 to 2019Enrolled300ConditionsPancreatic Neoplasms, InflammationArmsgemcitabine-based chemotherapy
3 · Its place in the literature

Who cites it

97 citing papers in PubMed, 1 synthesis or guideline pooled it, 166 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
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  6. Article
  7. Article
  8. Article
  9. Tumors in the setting of dupilumab use: A review of the literature.The World Allergy Organization journal · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. A Bispecific, Tetravalent Antibody Targeting Inflammatory and Pruritogenic Pathways in Atopic Dermatitis.JID innovations : skin science from molecules to population health · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. Serum immunoglobulin and the threshold of Fc receptor-mediated immune activation.Biochimica et biophysica acta. General subjects · 2023
    Review
  19. Review
  20. Article

37 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

2 authors at 2 institutions in 1 country.

Anna M DaviesRandall Division of Cell and Molecular Biophysics, King's College London, London, UK.
Brian J SuttonRandall Division of Cell and Molecular Biophysics, King's College London, London, UK.
Asthma UK · GBMedical Research Council · GB

Funding

Medical Research Council G0501494Medical Research Council G1100090
6 · The paper itself

Abstract

IgG4, the least represented human IgG subclass in serum, is an intriguing antibody with unique biological properties, such as the ability to undergo Fab-arm exchange and limit immune complex formation. The lack of effector functions, such as antibody-dependent cell-mediated cytotoxicity and complement-dependent cytotoxicity, is desirable for therapeutic purposes. IgG4 plays a protective role in allergy by acting as a blocking antibody, and inhibiting mast cell degranulation, but a deleterious role in malignant melanoma, by impeding IgG1-mediated anti-tumor immunity. These findings highlight the importance of understanding the interaction between IgG4 and Fcγ receptors. Despite a wealth of structural information for the IgG1 subclass, including complexes with Fcγ receptors, and structures for intact antibodies, high-resolution crystal structures were not reported for IgG4-Fc until recently. Here, we highlight some of the biological properties of human IgG4, and review the recent crystal structures of IgG4-Fc. We discuss the unexpected conformations adopted by functionally important Cγ2 domain loops, and speculate about potential implications for the interaction between IgG4 and FcγRs.

Indexed as

AnimalsAntibody AffinityAntibody SpecificityBinding SitesComplement C1qGlycosylationHumansHypersensitivityImmunoglobulin Fab FragmentsImmunoglobulin GModels, MolecularNeoplasmsProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein MultimerizationComplement C1qImmunoglobulin Fab FragmentsImmunoglobulin GReceptors, IgGantibodyFc receptorIgG1IgG4immunoglobulin

Identifiers

PMID26497518
PMCPMC4670484
OpenAlexW1895658925

What OpenQuestion holds

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LicenceCC BY
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.