Evidence map›Paper›PMID 39925738›Full record

ReviewFrontiers in cell and developmental biology2025

Non-histone lactylation: unveiling its functional significance.

Pusong Shi, Yongjie Ma, Shaolu Zhang

Erratum issuedAbstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Review
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  3. 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
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Pusong ShiSchool of Integrative Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin, China.
Yongjie MaLaboratory of Cancer Cell Biology, Tianjin Medical University Cancer Institute and Hospital, National Clinical Research Center for Cancer, Tianjin, China.
Shaolu ZhangLaboratory of Cancer Cell Biology, Tianjin Medical University Cancer Institute and Hospital, National Clinical Research Center for Cancer, Tianjin, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactylation, a newly discovered protein posttranslational modification (PTM) in 2019, primarily occurs on lysine residues. Lactylation of histones was initially identified, and subsequent studies have increasingly demonstrated its widespread presence on non-histone proteins. Recently, high-throughput proteomics studies have identified a large number of lactylated proteins and sites, revealing their global regulatory role in disease development. Notably, this modification is catalyzed by lactyltransferase and reversed by delactylase, with numerous new enzymes, such as AARS1/2, reported to be involved. Specifically, these studies have revealed how lactylation exerts its influence through alterations in protein spatial conformation, molecular interactions, enzyme activity and subcellular localization. Indeed, lactylation is implicated in various physiological and pathological processes, including tumor development, cardiovascular and cerebrovascular diseases, immune cell activation and psychiatric disorders. This review provides the latest advancements in research on the regulatory roles of non-histone protein lactylation, highlighting its crucial scientific importance for future studies.

Indexed as

lactylationlysinemetabolismnon-histoneposttranslational modification

Identifiers

PMID39925738
PMCPMC11802821

What OpenQuestion holds

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Registered trials

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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.