Evidence map›Paper›PMID 42859251›Full record

ReviewMolecular biology reports2026

E3 ubiquitin ligase-mediated necroptosis: regulatory mechanisms and therapeutic implication in cancer.

Mingzhen Wei, Aiqin Sun

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 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

2 authors.

Mingzhen WeiSchool of Clinical Medicine & Laboratory Medicine, Jiangsu University, 301 Xuefu Road, Zhenjiang, 212013, Jiangsu, China.
Aiqin SunSchool of Clinical Medicine & Laboratory Medicine, Jiangsu University, 301 Xuefu Road, Zhenjiang, 212013, Jiangsu, China. aiqinsun@ujs.edu.cn.ORCID https://orcid.org/0000-0002-3081-7893

Funding

National Natural Science Foundation of China 82002581
6 · The paper itself

Abstract

Necroptosis, a form of regulated cell death, has attracted significant attention as a potential therapeutic target for cancer. Although necroptosis is regulated at various levels, ubiquitination is key to post-translational regulation of necroptotic cell death. E3 ubiquitin ligases are the most remarkable enzymes in the ubiquitination modification, responsible for recognizing and ubiquitinating specific substrates. In this review article, we will explain how E3 ubiquitin ligases influences necroptosis, as well as to discuss what is the present state of the knowledge about the role of E3 ubiquitin ligase-mediated necroptosis in cancer development, and in response to therapy.

Indexed as

NecroptosisNeoplasmsUbiquitin-Protein LigasesAnimalsApoptosisHumansUbiquitinationUbiquitin-Protein LigasesCancersCancer therapyE3 ubiquitin ligasesNecroptosisUbiquitination

Identifiers

What OpenQuestion holds

Textmetadata
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.