ReviewBiochemistry and biophysics reports2024
Protein crotonylation: Basic research and clinical diseases.
Review in Biochemistry and biophysics reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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
8 citing papers in PubMed.
- MOF promotes venous thromboembolism in lung cancer by activating the YBX1-MALT1-NF-κB-PAI-1 axis, possibly through histone crotonylation.The Journal of biological chemistry · 2026Article
- Chemical Proteomics Identifies Ketogenesis-Mediated Cysteine Modifications Regulating Redox Function.Angewandte Chemie (International ed. in English) · 2026Article
- Review
- Post-translational modifications at the crossroads of cancer metabolism and immune regulation: therapeutic opportunities and challenges.International journal of surgery (London, England) · 2026Review
- HDAC1-mediated CDK1 decrotonylation inhibits colorectal cancer proliferation by regulating cell cycle and apoptosis.Frontiers in oncology · 2026Article
- Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post-Translational Modification.Chembiochem : a European journal of chemical biology · 2025Review
- Novel protein acylations in ferroptosis: decoding the regulatory roles of lactylation, crotonylation, succinylation, and β-hydroxybutyrylation.Frontiers in pharmacology · 2025Review
- Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crotonylation is an importantly conserved post-translational modification, which is completely different from acetylation. In recent years, it has been confirmed that crotonylation occurs on histone and non-histone. Crotonylated Histone primarily affects gene expression through transcriptional regulation, while non-histone Crotonylation mainly regulates protein functions including protein activity, localization, and stability, as well as protein-protein interactions. The change in protein expression and function will affect the physiological process of cells and even cause disease. Reviewing previous studies, this article summarizes the mechanisms of histone and non-histone crotonylation in regulating diseases and cellular physiological processes to explore the possibility of precise regulation of crotonylation sites as potential targets for disease treatment.
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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.