ArticleMolecular medicine reports2020
Quantitative analysis of protein crotonylation identifies its association with immunoglobulin A nephropathy.
Article in Molecular medicine reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Sodium Crotonate Alleviates Diabetic Kidney Disease Partially Via the Histone Crotonylation Pathway.Inflammation · 2025Article
- Protein lysine crotonylation in cellular processions and disease associations.Genes & diseases · 2024Review
- Protein crotonylation: Basic research and clinical diseases.Biochemistry and biophysics reports · 2024Review
- Inhibition of ACSS2-mediated histone crotonylation alleviates kidney fibrosis via IL-1β-dependent macrophage activation and tubular cell senescence.Nature communications · 2024Article
- The mechanisms, regulations, and functions of histone lysine crotonylation.Cell death discovery · 2024Review
- Systematic proteomics profiling of lysine crotonylation of the lung at Pseudoglandular and Canalicular phases in human fetus.Proteome science · 2023Article
- Histone crotonylation of peripheral blood mononuclear cells is a potential biomarker for diagnosis of colorectal cancer.Epigenetics & chromatin · 2023Article
- Lysine Crotonylation: An Emerging Player in DNA Damage Response.Biomolecules · 2022Review
- Identification of blood-based key biomarker and immune infiltration in Immunoglobulin A nephropathy by comprehensive bioinformatics analysis and a cohort validation.Journal of translational medicine · 2022Article
- Protein lysine crotonylation: past, present, perspective.Cell death & disease · 2021Review
- Emerging roles of non-histone protein crotonylation in biomedicine.Cell & bioscience · 2021Review
- The Function and related Diseases of Protein Crotonylation.International journal of biological sciences · 2021Review
- The Contribution of Histone Crotonylation to Tissue Health and Disease: Focus on Kidney Health.Frontiers in pharmacology · 2020Review
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Posttranslational modifications (PTMs) to histones such as lysine crotonylation are classified as epigenetic changes. Lysine crotonylation participates in various cellular processes and occurs in active promoters, directly accelerating transcription. The present study performed a proteomics analysis of crotonylation between healthy controls and patients with immunoglobulin A (IgA) nephropathy using tandem mass spectrometry and high‑resolution liquid chromatography. The present results identified 353 crotonylated proteins and 770 modification sites, including 155 upregulated and 198 downregulated crotonylated proteins. In total, seven conserved motifs were identified in the present study. The present bioinformatics analysis results suggested a number of the crotonylated proteins exhibited various subcellular localization patterns, such as in the cytoplasm. Protein domains, including thioredoxin, moesin tail and myosin like IQ motif domains were markedly enriched in crotonylated proteins. Kyoto Encyclopedia of Genes and Genomes and functional enrichment analyses suggested significant enrichment of crotonylated proteins in complement and coagulation cascades, and antigen processing and presentation pathways displaying important relationships with IgA nephropathy. The present results suggested that crotonylation occurred in numerous proteins and may play key regulatory roles in IgA nephropathy.
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