Evidence map›Paper›PMID 36459434›Full record

ArticleJournal of medicinal chemistry2022

The Highly Potent AhR Agonist Picoberin Modulates Hh-Dependent Osteoblast Differentiation.

Jana Flegel, Saad Shaaban, Zhi Jun Jia, Britta Schulte, Yilong Lian, Adrian Krzyzanowski, Malte Metz, Tabea Schneidewind, Fabian Wesseler, Anke Flegel and 17 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
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  4. Article
  5. The role of the AHR in host-pathogen interactions.Nature reviews. Immunology · 2025
    Review
  6. Article
  7. Article
  8. Article
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  10. 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

27 authors at 7 institutions in 5 countries.

Jana FlegelDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Saad ShaabanDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Zhi Jun JiaDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Britta SchulteDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Yilong LianLudwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom.
Adrian KrzyzanowskiDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Malte MetzDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Tabea SchneidewindDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Fabian WesselerDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Anke FlegelDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Alisa ReichDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Alexandra BrauseDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Gang XueDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Minghao ZhangNuffield Department of Medicine, Target Discovery Institute, University of Oxford, Oxford, OX3 7FZ, UK.
Lara DötschDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.ORCID 0000-0001-8100-5636
Isabelle D StenderProtein Chemistry Facility, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Jan-Erik HoffmannProtein Chemistry Facility, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Rebecca ScheelFaculty of Chemistry, Inorganic Chemistry, Technical University Dortmund, Dortmund 44227, Germany.
Petra JanningDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Fraydoon RastinejadNuffield Department of Medicine, Target Discovery Institute, University of Oxford, Oxford, OX3 7FZ, UK.
Dennis SchadeDept. of Pharmaceutical & Medicinal Chemistry, Institute of Pharmacy, Christian-Albrechts-University of Kiel, Kiel 24118, Germany.ORCID 0000-0002-5515-1821
Carsten StrohmannFaculty of Chemistry, Inorganic Chemistry, Technical University Dortmund, Dortmund 44227, Germany.
Andrey P AntonchickDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.ORCID 0000-0003-0435-9443
Sonja SieversDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.
Pedro Moura-AlvesLudwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom.
Slava ZieglerDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.ORCID 0000-0003-4398-7741
Herbert WaldmannDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund 44227, Germany.ORCID 0000-0002-9606-7247
Max Planck Institute of Molecular Physiology · DETU Dortmund University · DEUniversity of Oxford · GBChristian-Albrechts-Universität zu Kiel · DESichuan University · CNUniversidade do Porto · PTUniversity of Vienna · AT

Funding

Wellcome Trust 210664/Z/18/Z
6 · The paper itself

Abstract

Identification and analysis of small molecule bioactivity in target-agnostic cellular assays and monitoring changes in phenotype followed by identification of the biological target are a powerful approach for the identification of novel bioactive chemical matter in particular when the monitored phenotype is disease-related and physiologically relevant. Profiling methods that enable the unbiased analysis of compound-perturbed states can suggest mechanisms of action or even targets for bioactive small molecules and may yield novel insights into biology. Here we report the enantioselective synthesis of natural-product-inspired 8-oxotetrahydroprotoberberines and the identification of Picoberin, a low picomolar inhibitor of Hedgehog (Hh)-induced osteoblast differentiation. Global transcriptome and proteome profiling revealed the aryl hydrocarbon receptor (AhR) as the molecular target of this compound and identified a cross talk between Hh and AhR signaling during osteoblast differentiation.

Indexed as

Hedgehog ProteinsReceptors, Aryl HydrocarbonCell DifferentiationOsteoblastsSignal TransductionHedgehog ProteinsReceptors, Aryl Hydrocarbon

Identifiers

PMID36459434
PMCPMC9791665
OpenAlexW4310602458

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.