Mechanistic Role of the Mdm2/MdmX Lid Domain in Regulating Their Interactions with p53.

Qiuyin Wei, Chenqi Li, Yibing Tang, Jinping Bai, Wang Li, Jidong Liu, Zhengding Su, Xiyao Cheng

Abstract readReview

In one paragraph

Review in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Effect of TP53 mutation, expression and polymorphism on the survival, immune infiltration and ferroptosis in patients with prostate cancer.Oncology letters · 2025
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

8 authors.

Qiuyin WeiInstitute of Modern Fermentation Engineering and Future Foods, School of Light Industry and Food Engineering, Guangxi University, No. 100, Daxuedong Road, Nanning 530004, China.

Chenqi LiInstitute of Modern Fermentation Engineering and Future Foods, School of Light Industry and Food Engineering, Guangxi University, No. 100, Daxuedong Road, Nanning 530004, China.

Yibing TangInstitute of Modern Fermentation Engineering and Future Foods, School of Light Industry and Food Engineering, Guangxi University, No. 100, Daxuedong Road, Nanning 530004, China.

Jinping BaiInstitute of Modern Fermentation Engineering and Future Foods, School of Light Industry and Food Engineering, Guangxi University, No. 100, Daxuedong Road, Nanning 530004, China.

Wang LiInstitute of Modern Fermentation Engineering and Future Foods, School of Light Industry and Food Engineering, Guangxi University, No. 100, Daxuedong Road, Nanning 530004, China.

Jidong LiuInstitute of Modern Fermentation Engineering and Future Foods, School of Light Industry and Food Engineering, Guangxi University, No. 100, Daxuedong Road, Nanning 530004, China.ORCID 0000-0003-3269-1240

Zhengding SuSchool of Pharmaceutical Sciences and Institute of Materia Medica, Xinjiang University, Urumqi 830017, China.ORCID 0000-0003-3558-001X

Xiyao ChengInstitute of Modern Fermentation Engineering and Future Foods, School of Light Industry and Food Engineering, Guangxi University, No. 100, Daxuedong Road, Nanning 530004, China.ORCID 0000-0003-2161-1743

Funding

National Natural Science Foundation of China 32301020National Natural Science Foundation of China 32471260Natural Science Foundation of Guangxi Province 2024GXNSFBA010080

6 · The paper itself

Abstract

p53 functions as a critical guardian of the genome, orchestrating tumor suppression pathways and ensuring the integrity of chromosomal stability. Mdm2 and MdmX, homologous proteins, serve as negative feedback regulators of p53. In approximately half of tumor cases, overexpression of Mdm2/MdmX results in the inhibition of p53 activity. Current research focuses on designing Mdm2 and MdmX inhibitors based on the structure of lidless N-terminal forms of these proteins. However, growing evidence suggests that the lid of Mdm2 and MdmX plays a key role in the selective binding of p53 and inhibitors. Therefore, targeting the lid in the screening and design of Mdm2/MdmX inhibitors may offer a novel strategy for developing anti-cancer drugs. This review examines the impact of the Mdm2/MdmX lid on ligand binding, providing valuable insights for future research and guiding new approaches to the screening and design of innovative anti-cancer therapeutics.

Indexed as

Nuclear ProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p53AnimalsCell Cycle ProteinsHumansNeoplasmsProtein BindingProtein DomainsCell Cycle ProteinsMDM2 protein, humanMDM4 protein, humanNuclear ProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p53LidMdm2MdmXtumor suppressor protein p53

Identifiers

PMID40427535

DOI10.3390/biom15050642

PMCPMC12109074

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.