Evidence map›Paper›PMID 40185947›Full record

ReviewNature cell biology2025

Emerging roles of lysine lactyltransferases and lactylation.

Zhi Zong, Jiang Ren, Bing Yang, Long Zhang, Fangfang Zhou

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
–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

67 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Scleral Postn Drives Myopia via Promoting Myofibroblast Transdifferentiation.Investigative ophthalmology & visual science · 2026
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Targeting Lactate and Lactylation in Cancer Metabolism and Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  17. Review
  18. Article
  19. Review
  20. Review

7 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

5 authors.

Zhi Zong *The First Affiliated Hospital of Soochow University, Suzhou, China.ORCID http://orcid.org/0009-0004-4375-8548
Jiang Ren *MOE Basic Research and Innovation Center for the Targeted Therapeutics of Solid Tumors, Institute of Biomedical Innovation, School of Basic Medical Sciences, Jiangxi Medical College, Nanchang University, Nanchang, China.
Bing YangState Key Laboratory of Transvascular Implantation Devices of the Second Affiliated Hospital of the Zhejiang University School of Medicine, Zhejiang University, Hangzhou, China. bingyang@zju.edu.cn.ORCID http://orcid.org/0000-0001-6739-2932
Long ZhangMOE Basic Research and Innovation Center for the Targeted Therapeutics of Solid Tumors, Institute of Biomedical Innovation, School of Basic Medical Sciences, Jiangxi Medical College, Nanchang University, Nanchang, China. L_Zhang@zju.edu.cn.ORCID http://orcid.org/0000-0001-8139-0474
Fangfang ZhouThe First Affiliated Hospital of Soochow University, Suzhou, China. zhoufangfang@suda.edu.cn.ORCID http://orcid.org/0000-0003-1870-7584

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Given its various roles in cellular functions, lactate is no longer considered a waste product of metabolism and lactate sensing is a pivotal step in the transduction of lactate signals. Lysine lactylation is a recently identified post-translational modification that serves as an intracellular mechanism of lactate sensing and transfer. Although acetyltransferases such as p300 exhibit general acyl transfer activity, no bona fide lactyltransferases have been identified. Recently, the protein synthesis machinery, alanyl-tRNA synthetase 1 (AARS1), AARS2 and their Escherichia coli orthologue AlaRS, have been shown to be able to sense lactate and mediate lactyl transfer and are thus considered pan-lactyltransferases. Here we highlight the mechanisms and functions of these lactyltransferases and discuss potential strategies that could be exploited for the treatment of human diseases.

Indexed as

AminoacyltransferasesLysineProtein Processing, Post-TranslationalAmino Acyl-tRNA SynthetasesAnimalsHumansAminoacyltransferasesAmino Acyl-tRNA SynthetasesLysine

Identifiers

What OpenQuestion holds

Textmetadata
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.