Evidence map›Paper›PMID 40057816›Full record

ReviewExperimental hematology & oncology2025

Lactylation modification in cancer: mechanisms, functions, and therapeutic strategies.

Mengqi Lv, Yefei Huang, Yansu Chen, Kun Ding

Abstract readReview
In one paragraph

Review in Experimental hematology & oncology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Review
  2. Lactate-Mediated Lysine Lactylation in Renal Fibrosis: Current Progress and Challenges.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  3. Review
  4. Lactylation: a novel post-translational modification for cGAS-STING pathway.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Role of histone modifications in gastric cancer (Review).International journal of oncology · 2026
    Review
  12. Review
  13. H4K5 lactylation - ENO2 loop drives glycolysis and HCC progression.JHEP reports : innovation in hepatology · 2026
    Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. 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

4 authors.

Mengqi LvSchool of Public Health, Xuzhou Medical University, Xuzhou, 221004, Jiangsu, China.
Yefei Huang *School of Public Health, Xuzhou Medical University, Xuzhou, 221004, Jiangsu, China. huangyefei@xzhmu.edu.cn.
Yansu Chen *School of Public Health, Xuzhou Medical University, Xuzhou, 221004, Jiangsu, China. chenyansu@xzhmu.edu.cn.
Kun Ding *School of Public Health, Xuzhou Medical University, Xuzhou, 221004, Jiangsu, China. dingkun1995@163.com.

Funding

the natural science foundation of Jiangsu Province, China BK20241038the Natural Science Fund for Colleges and Universities in Jiangsu Province 24KJD320005the Outstanding Talent Research Initiation Foundation of Xuzhou Medical University D2023021
6 · The paper itself

Abstract

Cancer remains the leading cause of mortality worldwide, and the emergence of drug resistance has made the identification of new therapeutic targets imperative. Lactate, traditionally viewed as a byproduct of glycolysis with limited ATP-producing capacity, has recently gained recognition as a critical signaling molecule. It plays a key role not only in cancer cell metabolism but also in shaping the tumor microenvironment (TME). Histone lysine lactylation, a newly identified post-translational modification, has been shown to influence a range of cellular processes in cancer. Current research focuses on the mechanisms and functions of histone lactylation in cancer, including its role in gene expression regulation, signal transduction, and protein synthesis. However, despite these advancements, there are still plenty of barriers in the quest to unravel the mechanisms of lactylation modification. The emergence of single-cell and spatial transcriptomics may offer valuable insights for selecting targets. This review provides a comprehensive summary of the mechanisms and the applications of lactylation modification in clinical settings. Through a detailed analysis, we identify the key challenges and limitations that exist in the current research landscape. These insights lay the groundwork for future studies by highlighting promising research directions.

Indexed as

CancerLactylationMetabolic reprogrammingMetastasisTherapy

Identifiers

PMID40057816
PMCPMC11889934

What OpenQuestion holds

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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.