Evidence map›Paper›PMID 41285721›Full record

ReviewCell death & disease2025

Lysine lactylation in diseases: beyond histone lactylation.

Yiming Liu, Xuan Guo, Xinyang Hu, Sining Zhou, Qi Yang, Pingping Feng, Linghui Zeng

Abstract readReview
In one paragraph

Review in Cell death & disease, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

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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.

Yiming LiuHangzhou Lin'an Traditional Chinese Medicine Hospital, Affiliated Hospital, Hangzhou City University, Hangzhou, 311300, China.
Xuan GuoKey Laboratory of Novel Targets and Drug Study for Neural Repair of Zhejiang Province, Hangzhou City University School of Medicine, Hangzhou, 310015, China.
Xinyang HuLaboratory of Cancer Biology, Key Laboratory of Biotherapy of Zhejiang Province, Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310017, China.
Sining ZhouLife Sciences Institute, Zhejiang University, Hangzhou, 310058, China.
Qi YangKey Laboratory of Novel Targets and Drug Study for Neural Repair of Zhejiang Province, Hangzhou City University School of Medicine, Hangzhou, 310015, China.
Pingping FengHangzhou Lin'an Traditional Chinese Medicine Hospital, Affiliated Hospital, Hangzhou City University, Hangzhou, 311300, China.
Linghui ZengHangzhou Lin'an Traditional Chinese Medicine Hospital, Affiliated Hospital, Hangzhou City University, Hangzhou, 311300, China. zenglh@hzcu.edu.cn.ORCID http://orcid.org/0000-0002-3758-0366

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactylation, a recently identified post-translational modification, was initially characterized as lysine residue modification in histone subunits that regulates gene transcription via epigenetic mechanisms. Elevated intracellular lactate has been shown to drive histone lysine lactylation (Kla), establishing its association with disease pathogenesis. Emerging evidence reveals that Kla modifications extend beyond histones to transcriptional regulators and cytoplasmic functional proteins. Unlike the broad transcriptional regulation mediated by histone lactylation, Kla modifications of functional proteins exert regulatory effects through both specific transcriptional modulation and direct functional alteration of target proteins, thereby precisely controlling biological processes. This review systematically examines the pathological implications of Kla modifications of functional proteins across multiple disease contexts, including inflammatory disorders, infectious diseases, neurological or cardiovascular pathologies, and oncological conditions. Our synthesis provides mechanistic insights into disease-associated Kla networks, facilitating therapeutic target discovery and pharmacological intervention strategies.

Indexed as

HistonesLysineProtein Processing, Post-TranslationalAnimalsHumansHistonesLysine

Identifiers

PMID41285721
PMCPMC12824173

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.