Evidence map›Paper›PMID 37252102›Full record

ArticleRSC medicinal chemistry2023

Identification of ARUK2002821 as an isoform-selective PI5P4Kα inhibitor.

Henriëtte M G Willems, Simon Edwards, Helen K Boffey, Stephen J Chawner, Christopher Green, Tamara Romero, David Winpenny, John Skidmore, Jonathan H Clarke, Stephen P Andrews

Open access · hybridAbstract read
In one paragraph

Article in RSC medicinal chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Structural basis for high-affinity inhibitor binding to lipid kinases PIP4K2A and PIP4K2B.Acta crystallographica. Section D, Structural biology · 2026
    Article
  3. Article
  4. Review
  5. 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

10 authors at 1 institution in 1 country.

Henriëtte M G WillemsThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.ORCID https://orcid.org/0000-0001-7196-5975
Simon EdwardsThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.
Helen K BoffeyThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.ORCID https://orcid.org/0000-0001-5088-4615
Stephen J ChawnerThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.ORCID https://orcid.org/0000-0001-9254-9532
Christopher GreenThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.ORCID https://orcid.org/0000-0002-4690-7594
Tamara RomeroThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.
David WinpennyThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.
John SkidmoreThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.ORCID https://orcid.org/0000-0001-9108-7858
Jonathan H ClarkeThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.ORCID https://orcid.org/0000-0002-4079-5333
Stephen P AndrewsThe ALBORADA Drug Discovery Institute, University of Cambridge Island Research Building, Cambridge Biomedical Campus, Hills Road Cambridge CB2 0AH UK spa26@cam.ac.uk.ORCID https://orcid.org/0000-0001-6021-6899
University of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The phosphatidylinositol 5-phosphate 4-kinases (PI5P4Ks) play a central role in regulating cell signalling pathways and, as such, have become therapeutic targets for diseases such as cancer, neurodegeneration and immunological disorders. Many of the PI5P4Kα inhibitors that have been reported to date have suffered from poor selectivity and/or potency and the availability of better tool molecules would facilitate biological exploration. Herein we report a novel PI5P4Kα inhibitor chemotype that was identified through virtual screening. The series was optimised to deliver ARUK2002821 (36), a potent PI5P4Kα inhibitor (pIC

Identifiers

PMID37252102
PMCPMC10211317
OpenAlexW4366208615

What Socratic 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 Socratic graph.