Evidence map›Paper›PMID 30833543›Full record

ArticleCell death & disease2019

TNFRSF receptor-specific antibody fusion proteins with targeting controlled FcγR-independent agonistic activity.

Juliane Medler, Johannes Nelke, Daniela Weisenberger, Tim Steinfatt, Moritz Rothaug, Susanne Berr, Thomas Hünig, Andreas Beilhack, Harald Wajant

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 34 citations in OpenAlex.

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  13. Targeting Co-Stimulatory Receptors of the TNF Superfamily for Cancer Immunotherapy.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023
    Review
  14. FcγRs and Their Relevance for the Activity of Anti-CD40 Antibodies.International journal of molecular sciences · 2022
    Review
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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

9 authors at 2 institutions in 1 country.

Juliane MedlerDivision of Molecular Internal Medicine, Department of Internal Medicine II, University Hospital Würzburg, Auvera Haus Grombühlstraße 12, 97080, Würzburg, Germany.
Johannes NelkeDivision of Molecular Internal Medicine, Department of Internal Medicine II, University Hospital Würzburg, Auvera Haus Grombühlstraße 12, 97080, Würzburg, Germany.ORCID http://orcid.org/0000-0003-4333-0299
Daniela WeisenbergerDivision of Molecular Internal Medicine, Department of Internal Medicine II, University Hospital Würzburg, Auvera Haus Grombühlstraße 12, 97080, Würzburg, Germany.
Tim SteinfattDepartment of Internal Medicine II, University Hospital of Würzburg, Zinklesweg 10, 97078, Würzburg, Germany.
Moritz RothaugDivision of Molecular Internal Medicine, Department of Internal Medicine II, University Hospital Würzburg, Auvera Haus Grombühlstraße 12, 97080, Würzburg, Germany.
Susanne BerrInstitute of Virology and Immunobiology, University of Würzburg, Versbacher Str. 7, 97078, Würzburg, Germany.
Thomas HünigInstitute of Virology and Immunobiology, University of Würzburg, Versbacher Str. 7, 97078, Würzburg, Germany.
Andreas BeilhackDepartment of Internal Medicine II, University Hospital of Würzburg, Zinklesweg 10, 97078, Würzburg, Germany.
Harald WajantDivision of Molecular Internal Medicine, Department of Internal Medicine II, University Hospital Würzburg, Auvera Haus Grombühlstraße 12, 97080, Würzburg, Germany. harald.wajant@mail.uni-wuerzburg.de.ORCID http://orcid.org/0000-0002-2005-3949
Universitätsklinikum Würzburg · DEUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies specific for TNFRSF receptors that bind soluble ligands without getting properly activated generally act as strong agonists upon FcγR binding. Systematic analyses revealed that the FcγR dependency of such antibodies to act as potent agonists is largely independent from isotype, FcγR type, and of the epitope recognized. This suggests that the sole cellular attachment, achieved by Fc domain-FcγR interaction, dominantly determines the agonistic activity of antibodies recognizing TNFRSF receptors poorly responsive to soluble ligands. In accordance with this hypothesis, we demonstrated that antibody fusion proteins harboring domains allowing FcγR-independent cell surface anchoring also act as strong agonist provided they have access to their target. This finding defines a general possibility to generate anti-TNFRSF receptor antibodies with FcγR-independent agonism. Moreover, anti-TNFRSF receptor antibody fusion proteins with an anchoring domain promise superior applicability to conventional systemically active agonists when an anchoring target with localized disease associated expression can be addressed.

Indexed as

AnimalsAntigen-Antibody ReactionsEpitopesHEK293 CellsHeLa CellsHT29 CellsHumansImmunoglobulin Fc FragmentsJurkat CellsMiceReceptors, IgGReceptors, Tumor Necrosis FactorEpitopesFcgr2b protein, mouseImmunoglobulin Fc FragmentsReceptors, IgGReceptors, Tumor Necrosis Factor

Identifiers

PMID30833543
PMCPMC6399339
OpenAlexW2919758335

What OpenQuestion holds

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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.