Evidence map›Paper›PMID 37283747›Full record

ArticleFrontiers in immunology2023

C4b-binding protein inhibits particulate- and crystalline-induced NLRP3 inflammasome activation.

Damien Bierschenk, Nikolina Papac-Milicevic, Ian P Bresch, Valentina Kovacic, Serena Bettoni, Mateusz Dziedzic, Rick A Wetsel, Susanne Eschenburg, Christoph J Binder, Anna M Blom and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in immunology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
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  5. Article
  6. Diverse Functions of C4b-Binding Protein in Health and Disease.Journal of immunology (Baltimore, Md. : 1950) · 2023
    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

11 authors at 4 institutions in 4 countries.

Damien BierschenkDivision of Medical Protein Chemistry, Department of Translational Medicine, Lund University, Malmö, Sweden.
Nikolina Papac-MilicevicDepartment of Laboratory Medicine, Medical University of Vienna, Vienna, Austria.
Ian P BreschInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Valentina KovacicDepartment of Laboratory Medicine, Medical University of Vienna, Vienna, Austria.
Serena BettoniDivision of Medical Protein Chemistry, Department of Translational Medicine, Lund University, Malmö, Sweden.
Mateusz DziedzicDivision of Medical Protein Chemistry, Department of Translational Medicine, Lund University, Malmö, Sweden.
Rick A WetselResearch Center for Immunology and Autoimmune Diseases, Brown Foundation Institute of Molecular Medicine, McGovern Medical School, University of Texas Health Science Center at Houston, Houston, TX, United States.
Susanne EschenburgInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Christoph J BinderDepartment of Laboratory Medicine, Medical University of Vienna, Vienna, Austria.
Anna M BlomDivision of Medical Protein Chemistry, Department of Translational Medicine, Lund University, Malmö, Sweden.
Ben C KingDivision of Medical Protein Chemistry, Department of Translational Medicine, Lund University, Malmö, Sweden.
Lund University · SEMedical University of Vienna · ATMedizinische Hochschule Hannover · DEBrown Foundation · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dysregulated NLRP3 inflammasome activation drives a wide variety of diseases, while endogenous inhibition of this pathway is poorly characterised. The serum protein C4b-binding protein (C4BP) is a well-established inhibitor of complement with emerging functions as an endogenously expressed inhibitor of the NLRP3 inflammasome signalling pathway. Here, we identified that C4BP purified from human plasma is an inhibitor of crystalline- (monosodium urate, MSU) and particulate-induced (silica) NLRP3 inflammasome activation. Using a C4BP mutant panel, we identified that C4BP bound these particles

Indexed as

InflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinAnimalsComplement C4b-Binding ProteinHistocompatibility AntigensHumansMacrophagesMiceSilicon DioxideC4bp protein, mouseComplement C4b-Binding ProteinHistocompatibility AntigensInflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinSilicon DioxideC4BPcytokinegoutinflammasomeMSUpyroptosissilica

Identifiers

PMID37283747
PMCPMC10239802
OpenAlexW4377205893

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.