Evidence map›Paper›PMID 41480383›Full record

ReviewFrontiers in pharmacology2025

Novel protein acylations in ferroptosis: decoding the regulatory roles of lactylation, crotonylation, succinylation, and β-hydroxybutyrylation.

Meiquan Wei, Shiming Wei, Xuhua Xie, Taotao Liu, Jun Deng

Abstract readReview
In one paragraph

Review in Frontiers in pharmacology, 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

5 authors.

Meiquan WeiDepartment of Pharmacy, The First Affiliated Hospital of Guangxi Medical University, Nanning, China.
Shiming WeiThe First Clinical Hospital, The First Affiliated Hospital of Guangxi Medical University, Nanning, China.
Xuhua XieDepartment of Pharmacy, The First Affiliated Hospital of Guangxi Medical University, Nanning, China.
Taotao LiuDepartment of Pharmacy, The First Affiliated Hospital of Guangxi Medical University, Nanning, China.
Jun DengDepartment of Pharmacy, The First Affiliated Hospital of Guangxi Medical University, Nanning, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ferroptosis is a unique form of iron-dependent programmed cell death, characterized by the abnormal accumulation of lipid peroxides, which plays a important role in various physiological and pathological processes. Crucially, the activity and stability of core ferroptosis regulators (including GPX4, ACSL4, FSP1, and iron/lipid metabolism proteins) are dynamically controlled by diverse post-translational modifications (PTMs), positioning PTMs as central molecular switches modulating cellular ferroptotic susceptibility across pathophysiological contexts. Elucidating the regulatory mechanisms of PTMs in ferroptosis is of great significance for understanding the complex network of cell death and providing new perspectives for disease treatment and diagnosis. This review focuses on four emerging PTMs-lactylation, crotonylation, succinylation, and β-hydroxybutyrylation-and their roles in promoting ferroptosis progression via protein regulatory systems. Additionally, it explores their clinical potential as therapeutic targets and diagnostic biomarkers. The definitions, functional mechanisms, and enzymatic regulation of these PTMs are systematically elucidated.

Indexed as

crotonylationferroptosisLactylationnovel protein modificationssuccinylationβ-hydroxybutyrylation

Identifiers

PMID41480383
PMCPMC12754016

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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.