Evidence map›Paper›PMID 31088911›Full record

ArticleThe Journal of biological chemistry2019

The solution structure of the human IgG2 subclass is distinct from those for human IgG1 and IgG4 providing an explanation for their discrete functions.

Gar Kay Hui, Antoni D Gardener, Halima Begum, Charles Eldrid, Konstantinos Thalassinos, Jayesh Gor, Stephen J Perkins

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Ex vivo comparison of ACU193 and lecanemab reveals binding differences in mouse brain.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. IgG subclass deposition in diabetic nephropathy.European journal of medical research · 2022
    Article
  7. Article
  8. Article
  9. Selectivity over coverage inChemical science · 2020
    Article
  10. Article
  11. 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

7 authors at 1 institution in 1 country.

Gar Kay HuiInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom.
Antoni D GardenerInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom.
Halima BegumInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom.
Charles EldridInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom.
Konstantinos ThalassinosInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom; Institute of Structural and Molecular Biology, Birkbeck College, University of London, London, WC1E 7HX, United Kingdom.
Jayesh GorInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom.
Stephen J PerkinsInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6BT, United Kingdom. Electronic address: s.perkins@ucl.ac.uk.
Institute of Structural and Molecular Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human IgG2 antibody displays distinct therapeutically-useful properties compared with the IgG1, IgG3, and IgG4 antibody subclasses. IgG2 is the second most abundant IgG subclass, being able to bind human FcγRII/FcγRIII but not to FcγRI or complement C1q. Structural information on IgG2 is limited by the absence of a full-length crystal structure for this. To this end, we determined the solution structure of human myeloma IgG2 by atomistic X-ray and neutron-scattering modeling. Analytical ultracentrifugation disclosed that IgG2 is monomeric with a sedimentation coefficient (

Indexed as

Carrier ProteinsHumansImmunoglobulin Fab FragmentsImmunoglobulin Fc FragmentsImmunoglobulin GModels, MolecularMolecular StructureNeutron DiffractionNeutronsProtein BindingProtein ConformationScattering, Small AngleUltracentrifugationX-Ray DiffractionX-RaysCarrier ProteinsImmunoglobulin Fab FragmentsImmunoglobulin Fc FragmentsImmunoglobulin Gprolactin-binding proteinanalytical ultracentrifugationantibodyimmunoglobulin G (IgG)molecular modelingneutron-scatteringsmall-angle X-ray scattering (SAXS)

Identifiers

PMID31088911
PMCPMC6635440
OpenAlexW2946393408

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.