Evidence map›Paper›PMID 42305479›Full record

ArticleTranslational cancer research2026

Identification of protein lysine lactylation and potential targets in esophageal squamous cell carcinoma.

Hanlu Zhang, Xiuji Yan, Lucheng Xi, Sicheng Chen, Qixin Shang, Long-Qi Chen, Wen-Ping Wang

Abstract read
In one paragraph

Article in Translational cancer research, 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. 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

7 authors.

Hanlu Zhang *Department of Thoracic Surgery, West China Hospital of Sichuan University, Chengdu, China.
Xiuji Yan *Department of Plastic and Burns Surgery, West China Hospital of Sichuan University, Chengdu, China.
Lucheng XiDepartment of Thoracic Surgery, West China Hospital of Sichuan University, Chengdu, China.
Sicheng ChenDepartment of Thoracic Surgery, West China Hospital of Sichuan University, Chengdu, China.
Qixin ShangDepartment of Thoracic Surgery, West China Hospital of Sichuan University, Chengdu, China.
Long-Qi ChenDepartment of Thoracic Surgery, West China Hospital of Sichuan University, Chengdu, China.
Wen-Ping WangDepartment of Thoracic Surgery, West China Hospital of Sichuan University, Chengdu, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Esophageal squamous cell carcinoma (ESCC) is one of the most common malignancies with high morbidity and mortality. Exploring the molecular pathogenesis of ESCC is of pivotal importance to improve patients' prognosis. Lactate-mediated lysine lactylation (Kla) is a novel post-translational modification and critical for cancer progression. However, the role and mechanism of Kla in ESCC metastasis are poorly defined. Methods: A comparative lactylome analysis was carried out to assess proteins with significantly different lactylation between ESCC patients with and without lymph node metastasis (LNM). Furthermore, key findings of liquid chromatography-tandem mass spectrometry (LC-MS/MS) were verified using ESCC cell lines and primary ESCC specimens. Results: Global lactylome profiling revealed that many proteins were lactylated in ESCC samples. Substantial upregulation of Kla was observed in ESCC tissues with LNM compared to tissues without LNM. Forty-eight Kla sites in 29 proteins were substantially downregulated, whereas 91 Kla sites in 60 proteins were markedly upregulated in ESCC tissues with LNM compared to tissues without LNM. It was observed that about 46.07% of the differentially expressed lactylated proteins were localized in the cytoplasm, indicating that many non-histone proteins were lactylated in ESCC samples and Kla involvement in ESCC metastasis via multiple tumorigenic processes. We verified that the enolase 1 (ENO1) protein's Kla level in ESCC cells was positively correlated with cell migration ability. Using tyramide signal amplification (TSA) multiplex immunofluorescence staining, it was demonstrated that ESCC-LNM tissues had higher ENO1 Kla levels than ESCC-non-LNM tissues. Conclusions: The study found a positive correlation between Kla and ESCC metastasis. Furthermore, ENO1-Kla potentially promotes esophageal cancer (EC) metastasis and it may be a promising treatment target and a predictive biomarker of ESCC metastasis.

Indexed as

enolase 1 (ENO1)Esophageal squamous cell carcinoma (ESCC)lactylationmetastasis

Identifiers

PMID42305479
PMCPMC13265163

What OpenQuestion 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 OpenQuestion graph.