Evidence map›Paper›PMID 33668313›Full record

ArticleBiosensors2021

Novel Method for Quantifying AhR-Ligand Binding Affinities Using Microscale Thermophoresis.

Anne Stinn, Jens Furkert, Stefan H E Kaufmann, Pedro Moura-Alves, Michael Kolbe

Open access · goldAbstract read
In one paragraph

Article in Biosensors, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. The role of the AHR in host-pathogen interactions.Nature reviews. Immunology · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
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 5 institutions in 3 countries.

Anne StinnDepartment of Immunology, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.ORCID 0000-0001-9889-7853
Jens FurkertLeibniz-Institut für Molekulare Pharmakologie (FMP), Robert-Rössle-Strasse 10, 13125 Berlin, Germany.
Stefan H E KaufmannDepartment of Immunology, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.
Pedro Moura-AlvesDepartment of Immunology, Max Planck Institute for Infection Biology, Charitéplatz 1, 10117 Berlin, Germany.ORCID 0000-0003-4337-9113
Michael KolbeDepartment of Structural Infection Biology, Center for Structural Systems Biology (CSSB), Helmholtz-Center for Infection Research (HZI), Notkestrasse 85, 22607 Hamburg, Germany.
Institute for Advanced Study · USLeibniz-Forschungsinstitut für Molekulare Pharmakologie · DEMax Planck Institute for Infection Biology · DEUniversität Hamburg · DEUniversity of Oxford · GB

Funding

iNEXT 653706International Max Planck Research School for Infectious Diseases and Immunology PhD fellowshipMax-Planck-Gesellschaft Intramural Funding
6 · The paper itself

Abstract

The aryl hydrocarbon receptor (AhR) is a highly conserved cellular sensor of a variety of environmental pollutants and dietary-, cell- and microbiota-derived metabolites with important roles in fundamental biological processes. Deregulation of the AhR pathway is implicated in several diseases, including autoimmune diseases and cancer, rendering AhR a promising target for drug development and host-directed therapy. The pharmacological intervention of AhR processes requires detailed information about the ligand binding properties to allow specific targeting of a particular signaling process without affecting the remaining. Here, we present a novel microscale thermophoresis-based approach to monitoring the binding of purified recombinant human AhR to its natural ligands in a cell-free system. This approach facilitates a precise identification and characterization of unknown AhR ligands and represents a screening strategy for the discovery of potential selective AhR modulators.

Indexed as

Basic Helix-Loop-Helix ProteinsHumansLigandsNeoplasmsProtein BindingReceptors, Aryl HydrocarbonSignal TransductionAHR protein, humanBasic Helix-Loop-Helix ProteinsLigandsReceptors, Aryl HydrocarbonAhRhigh-throughput screeningligand bindingMSTrecombinant expression

Identifiers

PMID33668313
PMCPMC7996170
OpenAlexW3124013764

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.