Evidence map›Paper›PMID 39394602›Full record

ArticleBiology direct2024

Deciphering the role of SAMHD1 in endometrial cancer progression.

Ping Qiang, Ying Chen, Yang Shao, Qicheng Deng, Songyuan Xu, Weipei Zhu

Abstract read
In one paragraph

Article in Biology direct, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

6 authors.

Ping QiangDepartment of Obstetrics and Gynecology, The First People's Hospital of Zhangjiagang City, The Zhangjiagang Affiliated Hospital of Soochow University, Suzhou, 215600, China.
Ying ChenDepartment of Obstetrics and Gynecology, The Second Affiliated Hospital of Soochow University, No. 1055, Sanxiang Road, Suzhou, Jiangsu Province, 215000, China.
Yang ShaoDepartment of Obstetrics and Gynecology, The First People's Hospital of Zhangjiagang City, The Zhangjiagang Affiliated Hospital of Soochow University, Suzhou, 215600, China.
Qicheng DengDepartment of Obstetrics and Gynecology, The Second Affiliated Hospital of Soochow University, No. 1055, Sanxiang Road, Suzhou, Jiangsu Province, 215000, China.
Songyuan XuDepartment of Obstetrics and Gynecology, The First People's Hospital of Zhangjiagang City, The Zhangjiagang Affiliated Hospital of Soochow University, Suzhou, 215600, China.
Weipei ZhuDepartment of Obstetrics and Gynecology, The Second Affiliated Hospital of Soochow University, No. 1055, Sanxiang Road, Suzhou, Jiangsu Province, 215000, China. zwp3333@suda.edu.cn.

Funding

the project of Jiangsu Maternal and Child Health F201843
6 · The paper itself

Abstract

backgroundEndometrial cancer (EC) presents significant clinical challenges due to its heterogeneity and complex pathophysiology. SAMHD1, known for its role as a deoxynucleotide triphosphate triphosphohydrolase, has been implicated in the progression of various cancers, including EC. This study focuses on elucidating the role of SAMHD1 in EC through its impact on TRIM27-mediated PTEN ubiquitination.

resultsUtilizing a combination of bioinformatics and cellular biology techniques, we investigated the interactions among SAMHD1, TRIM27, and PTEN. Our findings reveal that SAMHD1 modulates PTEN ubiquitination via TRIM27, impacting key pathways involved in EC pathogenesis. These interactions suggest a critical mechanism by which SAMHD1 could influence tumor behavior and progression in EC.

conclusionsThe results from this study underscore the potential of targeting the SAMHD1-TRIM27-PTEN axis as a therapeutic strategy in EC. By providing new insights into the molecular mechanisms underlying EC progression, our research supports the development of novel therapeutic approaches that could contribute to improve treatment strategies for patients with EC.

Indexed as

Disease ProgressionEndometrial NeoplasmsPTEN PhosphohydrolaseSAM Domain and HD Domain-Containing Protein 1Cell Line, TumorFemaleHumansTripartite Motif ProteinsUbiquitinationPTEN PhosphohydrolasePTEN protein, humanSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, humanTripartite Motif ProteinsdNTP hydrolysis enzymePI3K/AKT signaling pathwayPTENSAMHD1TRIM27Ubiquitination

Identifiers

PMID39394602
PMCPMC11468744

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Registered trials

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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.