Evidence map›Paper›PMID 41112269›Full record

ReviewFrontiers in immunology2025

Role of novel protein acylation modifications in sepsis.

Jing Wang, Aifeng He, Lin Song, Wei Jiang, Lu Xu, Ruiqiang Zheng, Jiangquan Yu

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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.

Jing Wang *Northern Jiangsu People's Hospital Affiliated to Yangzhou University, Yangzhou, China.
Aifeng He *Binhai County People's Hospital, Yancheng, Jiangsu, China.
Lin SongNorthern Jiangsu People's Hospital Affiliated to Yangzhou University, Yangzhou, China.
Wei JiangNorthern Jiangsu People's Hospital Affiliated to Yangzhou University, Yangzhou, China.
Lu XuThe Yangzhou Clinical College of Xuzhou Medical University, Xuzhou, Jiangsu Province, China.
Ruiqiang ZhengNorthern Jiangsu People's Hospital Affiliated to Yangzhou University, Yangzhou, China.
Jiangquan YuNorthern Jiangsu People's Hospital Affiliated to Yangzhou University, Yangzhou, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sepsis is a life-threatening organ dysfunction caused by a dysregulated host response to infection, exhibiting high global morbidity and mortality. Accumulating evidence indicates that post-translational modifications (PTMs), as pivotal epigenetic mechanisms, play a crucial role in regulating diverse biological processes. The significance of PTMs in sepsis is increasingly recognized, as they may influence disease progression by modulating protein stability, activity, and localization. In recent years, advances in mass spectrometry have elucidated a series of novel PTMs, including succinylation (Ksucc), S-palmitoylation, lactylation (Kla), crotonylation (Kcr), 2-hydroxyisobutyrylation (Khib), β-hydroxybutyrylation (Kbhb), and malonylation (Kmal). This review presents the first comprehensive analysis of the characteristics, functions, and implications of these seven lysine acylation modifications in the pathogenesis and progression of sepsis, aiming to provide valuable insights for diagnosis and therapeutic intervention.

Indexed as

Protein Processing, Post-TranslationalSepsisAcylationAnimalsHumansLysineLysineacylationepigeneticsinflammationorgan dysfunctionsepsis

Identifiers

PMID41112269
PMCPMC12527872

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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.