Evidence map›Paper›PMID 37904770›Full record

ArticleMagnetic resonance (Gottingen, Germany)2021

Small-molecule inhibitors of the PDZ domain of Dishevelled proteins interrupt Wnt signalling.

Nestor Kamdem, Yvette Roske, Dmytro Kovalskyy, Maxim O Platonov, Oleksii Balinskyi, Annika Kreuchwig, Jörn Saupe, Liang Fang, Anne Diehl, Peter Schmieder and 5 more

Open access · goldAbstract read
In one paragraph

Article in Magnetic resonance (Gottingen, Germany), 2021. 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
0.6field-weighted citation impact, top 34% 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.

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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

15 authors at 3 institutions in 2 countries.

Nestor KamdemLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Yvette RoskeMax Delbrück Center for Molecular Medicine, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Dmytro KovalskyyEnamine Ltd., Chervonotkatska Street 78, Kyiv 02094, Ukraine.
Maxim O PlatonovEnamine Ltd., Chervonotkatska Street 78, Kyiv 02094, Ukraine.
Oleksii BalinskyiEnamine Ltd., Chervonotkatska Street 78, Kyiv 02094, Ukraine.
Annika KreuchwigLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Jörn SaupeLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Liang FangInstitut für Chemie und Biochemie, Freie Universität Berlin, Takustraße 3, 14195 Berlin, Germany.
Anne DiehlLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Peter SchmiederLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Gerd KrauseLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Jörg RademannLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Udo HeinemannInstitut für Chemie und Biochemie, Freie Universität Berlin, Takustraße 3, 14195 Berlin, Germany.
Walter BirchmeierMax Delbrück Center for Molecular Medicine, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Hartmut OschkinatLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, 13125 Berlin, Germany.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DEMax Delbrück Center · DETaras Shevchenko National University of Kyiv · UA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dishevelled (Dvl) proteins are important regulators of the Wnt signalling pathway, interacting through their PDZ domains with the Wnt receptor Frizzled. Blocking the Dvl PDZ-Frizzled interaction represents a potential approach for cancer treatment, which stimulated the identification of small-molecule inhibitors, among them the anti-inflammatory drug Sulindac and Ky-02327. Aiming to develop tighter binding compounds without side effects, we investigated structure-activity relationships of sulfonamides. X-ray crystallography showed high complementarity of anthranilic acid derivatives in the GLGF loop cavity and space for ligand growth towards the PDZ surface. Our best binding compound inhibits Wnt signalling in a dose-dependent manner as demonstrated by TOP-GFP assays (IC

Identifiers

PMID37904770
PMCPMC10539800
OpenAlexW3132883020

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.