Evidence map›Paper›PMID 33172893›Full record

ReviewThe Journal of biological chemistry

Fc γ receptor compositional heterogeneity: Considerations for immunotherapy development.

Adam W Barb

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
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  11. Review
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  13. Article
  14. Serum immunoglobulin and the threshold of Fc receptor-mediated immune activation.Biochimica et biophysica acta. General subjects · 2023
    Review
  15. Article
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  17. Article
  18. Role ofFrontiers in immunology · 2022
    Article
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  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

1 author at 1 institution in 1 country.

Adam W BarbDepartment of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA. Electronic address: abarb@uga.edu.
University of Georgia · US

Funding

Mechanism and engineering of IgG-based monoclonal antibody/receptor interactionsR01GM115489 · NIGMS · UNIVERSITY OF GEORGIA · PI BARB, ADAM WESLEY · 2015 to 2019
$1.4M
Post-translational modification of cell-activating antibody receptors from primary human leukocytesR21AI142122 · NIAID · UNIVERSITY OF GEORGIA · PI BARB, ADAM WESLEY · 2019 to 2020
$415k
NIAID NIH HHS R21 AI142122NIGMS NIH HHS R01 GM115489
6 · The paper itself

Abstract

The antibody-binding crystallizable fragment (Fc) γ receptors (FcγRs) are expressed by leukocytes and activate or suppress a cellular response once engaged with an antibody-coated target. Therapeutic mAbs that require FcγR binding for therapeutic efficacy are now frontline treatments for multiple diseases. However, substantially fewer development efforts are focused on the FcγRs, despite accounting for half of the antibody-receptor complex. The recent success of engineered cell-based immunotherapies now provides a mechanism to introduce modified FcγRs into the clinic. FcγRs are highly heterogeneous because of multiple functionally distinct alleles for many genes, the presence of membrane-tethered and soluble forms, and a high degree of post-translational modification, notably asparagine-linked glycans. One significant factor limiting FcγR improvement is the fundamental lack of knowledge regarding endogenous receptor forms present in the human body. This review describes the composition of FcγRs isolated from primary human leukocytes, summarizes recent efforts to engineer FcγRs, and concludes with a description of potential FcγR features to enrich for enhanced function. Further understanding FcγR biology could accelerate the development of new clinical therapies targeting immune-related disease.

Indexed as

AllelesAnimalsAntibodies, MonoclonalAntigens, CDCytotoxicity, ImmunologicHumansImmunoglobulin Fc FragmentsImmunotherapyKiller Cells, NaturalReceptors, Chimeric AntigenReceptors, IgGAntibodies, MonoclonalAntigens, CDImmunoglobulin Fc FragmentsReceptors, Chimeric AntigenReceptors, IgGantibodyFc receptorglycobiologyglycoproteinimmunotherapy

Identifiers

PMID33172893
PMCPMC7948983
OpenAlexW3099607932

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.