Evidence map›Paper›PMID 38812044›Full record

ReviewClinical epigenetics2024

Lactylation: the novel histone modification influence on gene expression, protein function, and disease.

Yue Hu, Zhenglin He, Zongjun Li, Yihan Wang, Nan Wu, Hongyan Sun, Zilong Zhou, Qianying Hu, Xianling Cong

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Clinical epigenetics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.

0numbers the graph read from it
0cells of the map it votes in
135citing 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

135 citing papers in PubMed.

  1. Review
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  5. Review
  6. WTAP Histone Lactylation Drives the YTHDF1/ALOX15 Axis to Regulate Ferroptosis in Myocardial Ischemia-Reperfusion Injury.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  7. Article
  8. Review
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  10. HSP90α lactylation orchestrates PGC1α and LRPGC1 nuclear translocation driving mitochondrial biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Brain-muscle axis regulation of neuroinflammation and sarcopenia in Parkinson's disease: the bridging role of lactylation.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review

75 more citing papers are in PubMed but not listed here.

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.

Yue HuDepartment of Tissues Bank, China-Japan Union Hospital of Jilin University, Changchun, 130033, China.
Zhenglin HeChina-Japan Union Hospital of Jilin University, Jilin University, Changchun, 130033, China.
Zongjun LiChina-Japan Union Hospital of Jilin University, Jilin University, Changchun, 130033, China.
Yihan WangChina-Japan Union Hospital of Jilin University, Jilin University, Changchun, 130033, China.
Nan WuDepartment of Tissues Bank, China-Japan Union Hospital of Jilin University, Changchun, 130033, China.
Hongyan SunDepartment of Tissues Bank, China-Japan Union Hospital of Jilin University, Changchun, 130033, China.
Zilong ZhouDepartment of Tissues Bank, China-Japan Union Hospital of Jilin University, Changchun, 130033, China.
Qianying HuDepartment of Tissues Bank, China-Japan Union Hospital of Jilin University, Changchun, 130033, China.
Xianling CongDepartment of Tissues Bank, China-Japan Union Hospital of Jilin University, Changchun, 130033, China. congxl@jlu.edu.cn.

Funding

Bethune Project of Jilin University 2023B21Science and Technology Development Project of Jilin Province 20210402030GHScience and Technology Development Project of Jilin Province 20220402071GHScience and Technology Development Project of Jilin Province 20230402001GHthe Health Talent Project of Jilin Province department of Finance 2023SCZ18
6 · The paper itself

Abstract

Lactic acid, traditionally considered as a metabolic waste product arising from glycolysis, has undergone a resurgence in scientific interest since the discovery of the Warburg effect in tumor cells. Numerous studies have proved that lactic acid could promote angiogenesis and impair the function of immune cells within tumor microenvironments. Nevertheless, the precise molecular mechanisms governing these biological functions remain inadequately understood. Recently, lactic acid has been found to induce a posttranslational modification, lactylation, that may offer insight into lactic acid's non-metabolic functions. Notably, the posttranslational modification of proteins by lactylation has emerged as a crucial mechanism by which lactate regulates cellular processes. This article provides an overview of the discovery of lactate acidification, outlines the potential "writers" and "erasers" responsible for protein lactylation, presents an overview of protein lactylation patterns across different organisms, and discusses the diverse physiological roles of lactylation. Besides, the article highlights the latest research progress concerning the regulatory functions of protein lactylation in pathological processes and underscores its scientific significance for future investigations.

Indexed as

Protein Processing, Post-TranslationalAnimalsEpigenesis, GeneticHistone CodeHistonesHumansLactic AcidNeoplasmsHistonesLactic AcidDiseaseLactic acidLactylationMetabolismProtein posttranslational modifications

Identifiers

PMID38812044
PMCPMC11138093

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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.