Evidence map›Paper›PMID 37973560›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2023

PRMT3-Mediated Arginine Methylation of METTL14 Promotes Malignant Progression and Treatment Resistance in Endometrial Carcinoma.

Yiru Wang, Can Wang, Xue Guan, Ying Ma, Shijie Zhang, Fei Li, Yue Yin, Zhenxing Sun, Xiuwei Chen, Hang Yin

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
8.9field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
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  3. RNA modifications and cancer ferroptosis.Cancer cell international · 2026
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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 2 institutions in 2 countries.

Yiru WangDepartment of Gynecologic Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.ORCID 0000-0002-8145-4199
Can WangDepartment of Gynecologic Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.
Xue GuanAnimal Laboratory Center, The Second Affiliated Hospital of Harbin Medical University, Harbin, Heilongjiang, 150000, China.
Ying MaDepartment of Gynecologic Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.
Shijie ZhangDepartment of Radiation Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.
Fei LiDepartment of Gynecologic Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.
Yue YinDepartment of Gynecologic Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.
Zhenxing SunDepartment of Gynecologic Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.
Xiuwei ChenDepartment of Gynecologic Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.ORCID 0000-0002-5771-6662
Hang YinDepartment of Radiation Oncology, Harbin Medical University Cancer Hospital, Harbin, Heilongjiang, 150000, China.
Harbin Medical University · CNHong Kong Polytechnic University · HK

Funding

Hong Kong Scholars Program XJ2022049National Natural Science Foundation of China 82073239National Natural Science Foundation of China 82272730
6 · The paper itself

Abstract

Protein arginine methyltransferase (PRMT) plays essential roles in tumor initiation and progression, but its underlying mechanisms in the treatment sensitivity of endometrial cancer (EC) remain unclear and warrant further investigation. Here, a comprehensive analysis of the Cancer Genome Atlas database and Clinical Proteomic Tumor Analysis Consortium database identifies that PRMT3 plays an important role in EC. Specifically, further experiments show that PRMT3 inhibition enhances the susceptibility of EC cells to ferroptosis. Mechanistically, PRMT3 interacts with Methyltransferase 14 (METTL14) and is involved in its arginine methylation. In addition, PRMT3 inhibition-mediated METTL14 overexpression promotes methylation modification via an m

Indexed as

ArginineEndometrial NeoplasmsFemaleHumansMethylationMethyltransferasesProtein-Arginine N-MethyltransferasesProteomicsArginineMethyltransferasesMETTL14 protein, humanPRMT3 protein, humanProtein-Arginine N-Methyltransferasesendometrial cancerferroptosisMETTL14PRMT3therapeutic resistance

Identifiers

PMID37973560
PMCPMC10754120
OpenAlexW4388774630

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.