Evidence map›Paper›PMID 26497531›Full record

ReviewImmunological reviews2015

TRIM21: a cytosolic Fc receptor with broad antibody isotype specificity.

Stian Foss, Ruth Watkinson, Inger Sandlie, Leo C James, Jan Terje Andersen

Open 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. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.2field-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

59 citing papers in PubMed, 104 citations in OpenAlex.

  1. Trial
  2. UBE2C-TRIM21-driven NOS2 degradation stabilizes Tregs and suppresses pyroptotic signaling in thyrocytes in Hashimoto's thyroiditis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Tripartite motif containing 21 autoimmunity primes CD8Arthritis research & therapy · 2026
    Article
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  11. Article
  12. Article
  13. Review
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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

5 authors at 4 institutions in 2 countries.

Stian FossCentre for Immune Regulation (CIR) and Department of Biosciences, University of Oslo, Oslo, Norway.
Ruth WatkinsonProtein and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Inger SandlieCentre for Immune Regulation (CIR) and Department of Biosciences, University of Oslo, Oslo, Norway.
Leo C JamesProtein and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Jan Terje AndersenCIR and Department of Immunology, Oslo University Hospital Rikshospitalet and University of Oslo, Oslo, Norway.
Oslo University Hospital · NOMedical Research Council · GBMRC Laboratory of Molecular Biology · GBUniversity of Oslo · NO

Funding

European Research Council 281627Medical Research Council MC_U105181010Medical Research Council U105181010
6 · The paper itself

Abstract

Antibodies are key molecules in the fight against infections. Although previously thought to mediate protection solely in the extracellular environment, recent research has revealed that antibody-mediated protection extends to the cytosolic compartment of cells. This postentry viral defense mechanism requires binding of the antibody to a cytosolic Fc receptor named tripartite motif containing 21 (TRIM21). In contrast to other Fc receptors, TRIM21 shows remarkably broad isotype specificity as it does not only bind IgG but also IgM and IgA. When viral pathogens coated with these antibody isotypes enter the cytosol, TRIM21 is rapidly recruited and efficient neutralization occurs before the virus has had the time to replicate. In addition, inflammatory signaling is induced. As such, TRIM21 acts as a cytosolic sensor that engages antibodies that have failed to protect against infection in the extracellular environment. Here, we summarize our current understanding of how TRIM21 orchestrates humoral immunity in the cytosolic environment.

Indexed as

AnimalsAntibodies, NeutralizingAntibody SpecificityCytosolEnzyme ActivationHost-Pathogen InteractionsHumansImmunityImmunoglobulin AImmunoglobulin Fc FragmentsImmunoglobulin GImmunoglobulin IsotypesImmunoglobulin MModels, MolecularProtein BindingProtein ConformationAntibodies, NeutralizingImmunoglobulin AImmunoglobulin Fc FragmentsImmunoglobulin GImmunoglobulin IsotypesImmunoglobulin MRibonucleoproteinsSS-A AntigenUbiquitin-Protein LigasesantibodiesFc-receptorintracellular immunityisotypeTRIM21virus

Identifiers

PMID26497531
PMCPMC4670481
OpenAlexW1888221672

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.