Evidence map›Paper›PMID 29960887›Full record

ArticleCell systems2018

Dissecting FcγR Regulation through a Multivalent Binding Model.

Ryan A Robinett, Ning Guan, Anja Lux, Markus Biburger, Falk Nimmerjahn, Aaron S Meyer

Open access · bronzeAbstract read
In one paragraph

Article in Cell systems, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025
    Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Immunoglobulin G subclasses confer protection againstProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. A quantitative view of strategies to engineer cell-selective ligand binding.Integrative biology : quantitative biosciences from nano to macro · 2021
    Article
  16. Article
  17. Article
  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

6 authors at 3 institutions in 2 countries.

Ryan A RobinettKoch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Ning GuanKoch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Anja LuxDivision of Genetics, Department of Biology, Friedrich-Alexander-University of Erlangen-Nürnberg, Erlangen 91058, Germany.
Markus BiburgerDivision of Genetics, Department of Biology, Friedrich-Alexander-University of Erlangen-Nürnberg, Erlangen 91058, Germany.
Falk NimmerjahnDivision of Genetics, Department of Biology, Friedrich-Alexander-University of Erlangen-Nürnberg, Erlangen 91058, Germany.
Aaron S MeyerDepartment of Bioengineering, Jonsson Comprehensive Cancer Center, Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, University of California, Los Angeles, Los Angeles, CA 90095, USA. Electronic address: ameyer@asmlab.org.
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEMassachusetts Institute of Technology · USUniversity of California, Los Angeles · US

Funding

Women's CancersP30CA016042 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Beth A. Glenn · 1985 to 2026
$134.5M
Adapter-Layer RTK Signaling: Basic Understanding & Targeted DrugResistanceDP5OD019815 · OD · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MEYER, AARON SAMUEL · 2014 to 2018
$2.0M
NCI NIH HHS P30 CA016042NIH HHS DP5 OD019815
6 · The paper itself

Abstract

Many immune receptors transduce activation across the plasma membrane through their clustering. With Fcγ receptors (FcγRs), this clustering is driven by binding to antibodies of differing affinities that are in turn bound to multivalent antigen. As a consequence of this activation mechanism, accounting for and rationally manipulating immunoglobulin (Ig)G effector function is complicated by, among other factors, differing affinities between FcγR species and changes in the valency of antigen binding. In this study, we show that a model of multivalent receptor-ligand binding can effectively account for the contribution of IgG-FcγR affinity and immune complex valency. This model in turn enables us to make specific predictions about the effect of immune complexes of defined composition. In total, these results enable both rational immune complex design for a desired IgG effector function and the deconvolution of effector function by immune complexes.

Indexed as

AnimalsAntibodiesAntibodies, MonoclonalAntibody AffinityAntigen-Antibody ComplexB-Lymphocyte SubsetsCarrier ProteinsCell MembraneCHO CellsCricetulusHumansImmune System PhenomenaImmunoglobulin Fc FragmentsImmunoglobulin GMiceMice, Inbred C57BLAntibodiesAntibodies, MonoclonalAntigen-Antibody ComplexCarrier ProteinsImmunoglobulin Fc FragmentsImmunoglobulin GReceptors, IgGantibodiescell specificityeffector functionFcγR receptorsimmunology

Identifiers

PMID29960887
PMCPMC6062446
OpenAlexW2774160955

What OpenQuestion holds

Textmetadata
LicenceTDM
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.