Evidence map›Paper›PMID 35979853›Full record

ArticleChemMedChem2022

Synthesis, Biological Evaluation, and Binding Mode of a New Class of Oncogenic K-Ras4b Inhibitors.

Stephan Jeuken, Oleksandr Shkura, Marc Röger, Victoria Brickau, Axel Choidas, Carsten Degenhart, Daniel Gülden, Bert Klebl, Uwe Koch, Raphael Stoll and 1 more

Abstract read
In one paragraph

Article in ChemMedChem, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

11 authors.

Stephan JeukenFaculty of Mathematics and Natural Sciences, University of Wuppertal, Gaussstrasse 20, 42119, Wuppertal, Germany.
Oleksandr ShkuraFaculty of Chemistry and Biochemistry, Biomolecular Spectroscopy and RUBiospec | NMR, University of Bochum, Universitätsstrasse 150, 44780, Bochum, Germany.
Marc RögerFaculty of Mathematics and Natural Sciences, University of Wuppertal, Gaussstrasse 20, 42119, Wuppertal, Germany.
Victoria BrickauLead Discovery Center GmbH, Otto-Hahn-Strasse 15, 44227, Dortmund, Germany.
Axel ChoidasLead Discovery Center GmbH, Otto-Hahn-Strasse 15, 44227, Dortmund, Germany.
Carsten DegenhartLead Discovery Center GmbH, Otto-Hahn-Strasse 15, 44227, Dortmund, Germany.
Daniel GüldenFaculty of Mathematics and Natural Sciences, University of Wuppertal, Gaussstrasse 20, 42119, Wuppertal, Germany.
Bert KleblLead Discovery Center GmbH, Otto-Hahn-Strasse 15, 44227, Dortmund, Germany.
Uwe KochLead Discovery Center GmbH, Otto-Hahn-Strasse 15, 44227, Dortmund, Germany.
Raphael StollFaculty of Chemistry and Biochemistry, Biomolecular Spectroscopy and RUBiospec | NMR, University of Bochum, Universitätsstrasse 150, 44780, Bochum, Germany.
Jürgen ScherkenbeckFaculty of Mathematics and Natural Sciences, University of Wuppertal, Gaussstrasse 20, 42119, Wuppertal, Germany.ORCID 0000-0003-1321-0595

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ras proteins are implicated in some of the most common life-threatening cancers. Despite intense research during the past three decades, progress towards small-molecule inhibitors of mutant Ras proteins still has been limited. Only recently has significant progress been made, in particular with ligands for binding sites located in the switch II and between the switch I and switch II region of K-Ras4B. However, the structural diversity of inhibitors identified for those sites to date is narrow. Herein, we show that hydrazones and oxime ethers of specific bis(het)aryl ketones represent structurally variable chemotypes for new GDP/GTP-exchange inhibitors with significant cellular activity.

Indexed as

Ethersras ProteinsBinding SitesFungal ProteinsHydrazonesEthersFungal ProteinsHydrazonesras ProteinsGTPase; K-Ras4B.hydrazoneoxime etherRas/SOS inhibitor

Identifiers

PMID35979853
PMCPMC9826232

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.