Evidence map›Paper›PMID 37095205›Full record

ArticleNature structural & molecular biology2023

Structural basis for Fc receptor recognition of immunoglobulin M.

Qu Chen, Rajesh P Menon, Laura Masino, Pavel Tolar, Peter B Rosenthal

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mass Photometry Analysis of Membrane Proteins in Detergent Micelles.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Defining the Features of Complement-Active IgM.Journal of molecular biology · 2025
    Article
  9. Integrated analysis of single-cell and bulk RNA-sequencing identifies a metastasis-related gene signature for predicting prognosis in lung adenocarcinoma.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2025
    Article
  10. Understanding IgM Structure and Biology to Engineer New Antibody Therapeutics.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. 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

5 authors at 1 institution in 1 country.

Qu ChenStructural Biology Science Technology Platform, The Francis Crick Institute, London, UK.ORCID 0000-0001-5921-8125
Rajesh P MenonImmune Receptor Activation Laboratory, The Francis Crick Institute, London, UK.
Laura MasinoStructural Biology Science Technology Platform, The Francis Crick Institute, London, UK.
Pavel TolarImmune Receptor Activation Laboratory, The Francis Crick Institute, London, UK. p.tolar@ucl.ac.uk.ORCID 0000-0003-4693-7299
Peter B RosenthalStructural Biology of Cells and Viruses Laboratory, The Francis Crick Institute, London, UK. Peter.Rosenthal@crick.ac.uk.ORCID 0000-0002-0387-2862
The Francis Crick Institute · GB

Funding

Cancer Research UK CC2006Cancer Research UK CC2106Medical Research Council CC2006Medical Research Council CC2106Wellcome Trust CC2006Wellcome Trust CC2106
6 · The paper itself

Abstract

Immunoglobulin Fc receptors are cell surface transmembrane proteins that bind to the Fc constant region of antibodies and play critical roles in regulating immune responses by activation of immune cells, clearance of immune complexes and regulation of antibody production. FcμR is the immunoglobulin M (IgM) antibody isotype-specific Fc receptor involved in the survival and activation of B cells. Here we reveal eight binding sites for the human FcμR immunoglobulin domain on the IgM pentamer by cryogenic electron microscopy. One of the sites overlaps with the binding site for the polymeric immunoglobulin receptor (pIgR), but a different mode of FcμR binding explains its antibody isotype specificity. Variation in FcμR binding sites and their occupancy reflects the asymmetry of the IgM pentameric core and the versatility of FcμR binding. The complex explains engagement with polymeric serum IgM and the monomeric IgM B-cell receptor (BCR).

Indexed as

B-LymphocytesReceptors, FcBinding SitesHumansImmunoglobulin Fc FragmentsImmunoglobulin MImmunoglobulin Fc FragmentsImmunoglobulin MReceptors, Fc

Identifiers

PMID37095205
PMCPMC7614769
OpenAlexW4366823233

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.