Evidence map›Paper›PMID 41823547›Full record

ReviewInternational journal of oncology2026

Enolase 1: A paradigm of metabolic enzyme moonlighting in tumorigenesis (Review).

Xiaochen Ni, Mingsi Zhang, Kaiyuan Zhang, Chuhang Wang, Jianing Guo, Wei Fan, Linfeng Zheng, Tao Jiang, Guangji Zhang

Abstract readReview
In one paragraph

Review in International journal of oncology, 2026. 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. Review
  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

9 authors.

Xiaochen NiSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.
Mingsi ZhangSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.
Kaiyuan ZhangSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.
Chuhang WangSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.
Jianing GuoSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.
Wei FanSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.
Linfeng ZhengSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.
Tao JiangSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.
Guangji ZhangSchool of Basic Medical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang 310053, P.R. China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enolase 1 (ENO1) plays a pivotal role in tumor development, recognized as a multifunctional oncogene across diverse cancers. Initially known for its central role in glycolysis, where it catalyzes the conversion of 2‑phosphoglycerate to phosphoenolpyruvate, the influence of ENO1 extends far beyond. Recent studies have unveiled its additional roles in promoting tumor progression through plasminogen receptor activity, nucleic acid binding activity and signaling functions. The function of ENO1 is intricately regulated by a wide array of post‑translational modifications, such as phosphorylation, ubiquitination, acetylation, methylation, succinylation and glycosylation. These modifications fine‑tune its enzymatic activity, stability and subcellular localization, thereby affecting tumor behavior. ENO1 holds significant diagnostic and prognostic value, with its expression levels closely linked to tumor malignancy and patient survival outcomes. In preclinical models, multiple therapeutic approaches targeting ENO1 have demonstrated tumor progression‑inhibiting effects. Consequently, drug development efforts centered on ENO1 are gaining momentum, with anticancer agents targeting this protein showing promising potential. As ENO1 emerges as a novel therapeutic target in oncology, the present review summarizes the latest research progress on ENO1 in the field of cancer.

Indexed as

Biomarkers, TumorCarcinogenesisDNA-Binding ProteinsNeoplasmsPhosphopyruvate HydrataseTumor Suppressor ProteinsAnimalsGene Expression Regulation, NeoplasticGlycolysisHumansPrognosisProtein Processing, Post-TranslationalBiomarkers, TumorDNA-Binding ProteinsENO1 protein, humanPhosphopyruvate HydrataseTumor Suppressor Proteinsenolase 1glycolysismoonlighting proteinpost‑translational modificationstumorigenesis

Identifiers

PMID41823547
PMCPMC13004432

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.