Evidence map›Paper›PMID 42441110›Full record

ReviewRSC advances2026

Disrupting the tumor-associated TNKS-USP25 protein-protein interface in cancer: structural basis, druggability, and therapeutic opportunities.

Emadeldin M Kamel, Sally Mostafa Khadrawy, Mohamed A M Ali, Noha A Ahmed, Saleh Alkhedhairi, Faris F Aba Alkhayl, Al Mokhtar Lamsabhi

Abstract readReview
In one paragraph

Review in RSC advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Emadeldin M KamelChemistry Department, Faculty of Science, Beni-Suef University Beni-Suef 62514 Egypt drnohascience@science.bsu.edu.eg.ORCID https://orcid.org/0000-0002-1279-9564
Sally Mostafa KhadrawyDepartment of Biology, College of Science, Imam Mohammad Ibn Saud Islamic University (IMSIU) Riyadh 11623 Saudi Arabia.
Mohamed A M AliDepartment of Biology, College of Science, Imam Mohammad Ibn Saud Islamic University (IMSIU) Riyadh 11623 Saudi Arabia.ORCID https://orcid.org/0000-0001-8217-0262
Noha A AhmedPhysiology Division, Zoology Department, Faculty of Science, Beni-Suef University P.O. Box 62521 Beni-Suef Egypt.ORCID https://orcid.org/0000-0002-5080-0933
Saleh AlkhedhairiDepartment of Medical Biosciences, College of Veterinary Medicine, Qassim University P.O. Box 6622 Buraydah 51452 Saudi Arabia.
Faris F Aba AlkhaylDepartment of Medical Laboratories, College of Applied Medical Sciences, Qassim University Buraydah 51452 Saudi Arabia.
Al Mokhtar LamsabhiDepartamento de Química and Institute for Advanced Research in Chemical Science (IAdChem), Facultad de Ciencias, Módulo 13, Universidad Autónoma de Madrid 28049 Madrid Spain.ORCID https://orcid.org/0000-0002-1509-2513

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tankyrases (TNKS1/2) are multi-domain poly(ADP-ribose) polymerases that regulate Wnt/β-catenin signaling and broader cellular programs through both catalytic activity and extensive protein-protein interaction (PPI) networks. While most tankyrase-directed drug discovery has focused on inhibiting the PARP catalytic site, an emerging alternative is to target tankyrase stability by disrupting its interaction with the deubiquitinase USP25. USP25 functions as a positive regulator of tankyrase abundance by counteracting ubiquitin-dependent turnover; consequently, blocking the TNKS-USP25 PPI can reduce tankyrase levels, stabilize pathway antagonists such as AXIN, and dampen Wnt transcriptional output. In this review, we discuss current understanding of tankyrase domain architecture with emphasis on ankyrin repeat clusters (ARC1/2/4/5) that recognize short tankyrase-binding motifs (TBMs), and we highlight why ARC5 is a particularly actionable node for intervention in the TNKS-USP25 axis. We summarize the structural basis of USP25 recruitment

Identifiers

PMID42441110
PMCPMC13335189

What OpenQuestion holds

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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.