Evidence map›Paper›PMID 41924730›Full record

ArticleFrontiers in medicine2026

Lactylation omics of rabbit rotator cuff tear reveals differentially modified proteins and metabolic relating therapy targets.

Tong Pan, Zhenlong Liu

Abstract read
In one paragraph

Article in Frontiers in medicine, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Tong PanDepartment of Sports Medicine, Peking University Third Hospital, Institute of Sports Medicine of Peking University, Beijing, China.
Zhenlong LiuDepartment of Sports Medicine, Peking University Third Hospital, Institute of Sports Medicine of Peking University, Beijing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins exert biological functions not only depending on abundance but also on regulation. Lactylation, a novel post-translational modification, can mediate metabolic reprogramming and epigenetic regulation, playing a crucial role in signal transduction, gene expression and cellular metabolism. Lactylation is also involved in various diseases, such as tumors, Alzheimer's disease, heart failure and myocardial infarction. However, there is little research in musculoskeletal system. In this study, we conducted lactylation omics on rabbit rotator cuff tear samples and identified 2,624 modification sites on 851 proteins. We obtained results on subcellular localization, differentially modified proteins and functional pathway enrichment. Basing on motif, we proposed the "lysine co-lactylation modification effect" concept. Overall, lactylation mainly localized in cytoplasm, mitochondria and nucleus, with its functions enriching in RNA processing, DNA processing and cellular metabolism. Considering that lactylation is widely present and significantly occurs in rotator cuff tears, we aim to identify the key targets through which lactylation exerts its effects and to intervene it, ultimately providing new insights and therapeutic approaches for clinic therapy.

Indexed as

functional enrichmentlactatelactylationmodification sitesmotifomics

Identifiers

PMID41924730
PMCPMC13037487

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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.