ReviewJournal of translational medicine2026
Lactylation and acetylation: parallel paths, divergent deeds, and research dilemmas.
Review in Journal of translational medicine, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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.
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.
Who cites it
7 citing papers in PubMed.
- Lactylation in influenza a virus infection: Current evidence, knowledge gaps, and future perspectives.Virulence · 2026Review
- Review
- Lactylation Remodels Tumorigenesis, Immune Microenvironment, and Therapeutic Response.Current issues in molecular biology · 2026Review
- Roles of lactate and protein lactylation in neurogenesis and neurodegenerative disease.Journal of translational medicine · 2026Review
- Research progress of lactylation modification in tumors (Review).Experimental and therapeutic medicine · 2026Review
- Lactylation: A central metabolic-epigenetic driver of sepsis-associated acute kidney injury.Molecular biology reports · 2026Review
- Lactylation modification in extracellular vesicles: A key regulator of cellular communication.iScience · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
backgroundMetabolism-induced post-translational modifications (PTMs) are critical for the regulation of cellular activities. As important types of modifications, lactylation and acetylation play essential roles in health and disease. With the development of lactylation research, its regulatory mechanism has been revealed to be highly similar to that of acetylation. MAIN BODY: Most lactylated proteins are also acetylated. They share lysine modification sites and exert similar regulatory functions in gene transcription, DNA repair, signal transduction, autophagy, and metabolism, although certain differences exist. Both lactylation and acetylation regulate protein functions by affecting protein stability, enzyme activity, liquid-liquid phase separation, and crosstalk with other modifications. More importantly, the high similarity between their regulatory mechanisms brings challenges to their specific research and raises previously overlooked questions for published acetylation studies.
conclusionThis review discusses the regulatory mechanisms, functional differences, and research dilemmas of lactylation and acetylation.
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Identifiers
What OpenQuestion holds
Registered trials
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.