Global profiling of crotonylation on non-histone proteins

Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification

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Intracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation

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Cross-regulation of histone modifications

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Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach

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YEATS2 is a selective histone crotonylation reader

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Profiling of Substrates for Zinc‐dependent Lysine Deacylase Enzymes: HDAC3 Exhibits Decrotonylase Activity In Vitro

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Microbiota Derived Short Chain Fatty Acids Promote Histone Crotonylation in the Colon Through Histone Deacetylases

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Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies

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Protein acylation: mechanisms, biological functions and therapeutic targets

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Epigenetic regulation in major depression and other stress-related disorders: molecular mechanisms, clinical relevance and therapeutic potential

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p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis

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Beyond histone acetylation—writing and erasing histone acylations

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Insights into the post-translational modification and its emerging role in shaping the tumor microenvironment

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Short-chain fatty acid, acylation and cardiovascular diseases

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Global crotonylome reveals CDYL-regulated RPA1 crotonylation in homologous recombination–mediated DNA repair

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Functions and mechanisms of lysine crotonylation

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Protein lysine crotonylation: past, present, perspective

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Lysine crotonylation is involved in hepatocellular carcinoma progression

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Roles of protein post-translational modifications in glucose and lipid metabolism: mechanisms and perspectives

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Oncometabolites drive tumorigenesis by enhancing protein acylation: from chromosomal remodelling to nonhistone modification

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Global Involvement of Lysine Crotonylation in Protein Modification and Transcription Regulation in Rice

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Quantitative Crotonylome Analysis Expands the Roles of p300 in the Regulation of Lysine Crotonylation Pathway

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Research progress on post-translational modification of proteins and cardiovascular diseases

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Epigenetic effects of short-chain fatty acids from the large intestine on host cells

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Ultradeep Lysine Crotonylome Reveals the Crotonylation Enhancement on Both Histones and Nonhistone Proteins by SAHA Treatment

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An Expanding Repertoire of Protein Acylations

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A qualitative proteome-wide lysine crotonylation profiling of papaya (Carica papaya L.)

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The health benefits of dietary short-chain fatty acids in metabolic diseases

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Histone crotonylation-centric gene regulation

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A global view of the human post-translational modification landscape

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Transcriptional Regulation at DSBs: Mechanisms and Consequences

Machour, F. E., & Ayoub, N. (2020) · Trends in Genetics · doi:10.1016/j.tig.2020.01.001 · Cited by 68

Hypoxia-induced downregulation of PGK1 crotonylation promotes tumorigenesis by coordinating glycolysis and the TCA cycle

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Acox2 is a regulator of lysine crotonylation that mediates hepatic metabolic homeostasis in mice

Zhang, Y., Chen, Y., Zhang, Z., Tao, X., Xu, S., Zhang, X., Zurashvili, T., Lu, Z., Bayascas, J. R., Jin, L., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04725-9 · Cited by 68

Modulation of cellular metabolism by protein crotonylation regulates pancreatic cancer progression

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Upregulation of α enolase (ENO1) crotonylation in colorectal cancer and its promoting effect on cancer cell metastasis

Hou, J., Cao, J., Gao, L., Zhang, F., Shen, J., Zhou, L., Shi, J., Feng, Y., Yan, Z., Wang, D., et al. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.09.027 · Cited by 63

Improved Prediction Model of Protein Lysine Crotonylation Sites Using Bidirectional Recurrent Neural Networks

Tng, S. S., Le, N. Q. K., Yeh, H., & Chua, M. C. H. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00848 · Cited by 62

Plant Proteoforms Under Environmental Stress: Functional Proteins Arising From a Single Gene

Kosová, K., Vítámvás, P., Prášil, I., Klíma, M., & Renaut, J. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.793113 · Cited by 61

First profiling of lysine crotonylation of myofilament proteins and ribosomal proteins in zebrafish embryos

Kwon, O. K., Kim, S. J., & Lee, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-22069-3 · Cited by 59

Crotonylated BEX2 interacts with NDP52 and enhances mitophagy to modulate chemotherapeutic agent-induced apoptosis in non-small-cell lung cancer cells

Mu, N., Wang, Y., Li, X., Du, Z., Wu, Y., Su, M., Wang, Y., Sun, X., Su, L., & Liu, X. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06164-6 · Cited by 59

HDAC-dependent decrease in histone crotonylation during DNA damage

Abu‐Zhayia, E. R., Machour, F. E., & Ayoub, N. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz019 · Cited by 55

The Function and related Diseases of Protein Crotonylation

Wang, S., Mu, G., Qiu, B., Wang, M., Yu, Z., Wang, W., Wang, J., & Yang, Y. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.58872 · Cited by 53

nhKcr: a new bioinformatics tool for predicting crotonylation sites on human nonhistone proteins based on deep learning

Chen, Y., Wang, Z., Wang, Y., Ying, G., Chen, Z., & Song, J. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab146 · Cited by 54

Global crotonylome reveals hypoxia-mediated lamin A crotonylation regulated by HDAC6 in liver cancer

Zhang, D., Tang, J. P., Xu, Y., Huang, X., Wang, Y., Jin, X., Wu, G., & Liu, P. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05165-1 · Cited by 54

Effects of Histone Modification in Major Depressive Disorder

Wu, M.-S., Li, X., Liu, C., Xu, Q., Huang, J., Gu, S., & Chen, J. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210922150043 · Cited by 56

DeepCap-Kcr: accurate identification and investigation of protein lysine crotonylation sites based on capsule network

Khanal, J., Tayara, H., Zou, Q., & Chong, K. T. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab492 · Cited by 51

The mechanisms, regulations, and functions of histone lysine crotonylation

Xie, J., Ju, J., Zhou, P., Chen, H., Wang, S., Wang, K., Wang, T., Chen, Y.-C., Chen, Y.-C., & Wang, K. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01830-w · Cited by 55

Crotonylation of key metabolic enzymes regulates carbon catabolite repression in Streptomyces roseosporus

Sun, C., Xu, W., Zhao, Q.-W., Luo, S., Chen, X.-A., Li, Y., & Mao, X. (2020) · Communications Biology · doi:10.1038/s42003-020-0924-2 · Cited by 50

Global Lysine Crotonylation and 2-Hydroxyisobutyrylation in Phenotypically Different Toxoplasma gondii Parasites

Yin, D., Jiang, N., Zhang, Y., Wang, D., Sang, X., Feng, Y., Chen, R., Wang, X., Yang, N., & Chen, Q. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001611 · Cited by 49

SIRT7-Induced PHF5A Decrotonylation Regulates Aging Progress Through Alternative Splicing-Mediated Downregulation of CDK2

Yu, A. Q., Wang, J., Jiang, S. T., Yuan, L. Q., Ma, H. Y., Hu, Y., Han, X. M., Tan, L. M., & Wang, Z. X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.710479 · Cited by 45

Emerging roles of non-histone protein crotonylation in biomedicine

Hou, J., Zhou, L., Li, J., Wang, D., & Cao, J. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00616-2 · Cited by 44

Crotonylation at serine 46 impairs p53 activity

Liao, P., Bhattarai, N., Cao, B., Zhou, X. Y., Jung, J. H., Damera, K., Fuselier, T. T., Thareja, S., Wimley, W. C., Wang, B., et al. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.152 · Cited by 43

The Contribution of Histone Crotonylation to Tissue Health and Disease: Focus on Kidney Health

Martinez-Moreno, J. M., Fontecha‐Barriuso, M., Martín‐Sánchez, D., Sánchez-Niño, M. D., Ruiz‐Ortega, M., Sanz, A. B., & Ortíz, A. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00393 · Cited by 41

Lysine crotonylation of DgTIL1 at K72 modulates cold tolerance by enhancing DgnsLTP stability in chrysanthemum

Huang, Q., Liao, X., Yang, X., Luo, Y., Lin, P., Zeng, Q.-H., Bai, H., Jiang, B., Pan, Y., Zhang, F., et al. (2020) · Plant Biotechnology Journal · doi:10.1111/pbi.13533 · Cited by 41

CDYL1-dependent decrease in lysine crotonylation at DNA double-strand break sites functionally uncouples transcriptional silencing and repair

Abu‐Zhayia, E. R., Bishara, L. A., Machour, F. E., Barisaac, A. S., Ben‐Oz, B. M., & Ayoub, N. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.031 · Cited by 40

The decrotonylase FoSir5 facilitates mitochondrial metabolic state switching in conidial germination of Fusarium oxysporum

Zhang, N., Song, L., Xu, Y., Pei, X.-Y., Luisi, B. F., & Liang, W. (2021) · eLife · doi:10.7554/elife.75583 · Cited by 40

Targeting the transmembrane cytokine co-receptor neuropilin-1 in distal tubules improves renal injury and fibrosis

Li, Y., Wang, Z., Xu, H., Hong, Y., Shi, M., Hu, B., Wang, X., Ma, S., Wang, M., Cao, C., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50121-6 · Cited by 40

Crotonylation and disease: Current progress and future perspectives

Yang, P., Qin, Y., Zeng, L., He, Y., Xie, Y., Cheng, X., Huang, W. G., & Cao, L. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115108 · Cited by 42

Substrate and Functional Diversity of Protein Lysine Post-translational Modifications

Hao, B., Chen, K., Zhai, L., Liu, M., Liu, B., & Tan, M. (2024) · Genomics Proteomics & Bioinformatics · doi:10.1093/gpbjnl/qzae019 · Cited by 41

Novel histone modifications and liver cancer: emerging frontiers in epigenetic regulation

Wang, Z., Liu, Z., Lv, M., Luan, Z., Li, T., & Hu, J. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-01838-8 · Cited by 40

Proteome-wide and lysine crotonylation profiling reveals the importance of crotonylation in chrysanthemum (Dendranthema grandiforum) under low-temperature

Lin, P., Bai, H., He, L., Huang, Q., Zeng, Q.-H., Pan, Y., Jiang, B., Zhang, F., Zhang, L., & Liu, Q. (2021) · BMC Genomics · doi:10.1186/s12864-020-07365-5 · Cited by 37

SEPT2 crotonylation promotes metastasis and recurrence in hepatocellular carcinoma and is associated with poor survival

Zhang, X., Liu, Z., Zhang, Y., Xu, L., Chen, M., Zhou, Y.-F., Yu, J. Q., Li, X., & Zhang, N. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00996-7 · Cited by 37

Lysine crotonylation regulates leucine-deprivation-induced autophagy by a 14-3-3ε-PPM1B axis.

Zheng, Z., Yan, G., Li, X., Fei, Y.-K., Sun, L.-L., Yu, H.-N., Niu, Y.-R., Gao, W.-H., Zhong, Q., & Yan, X.-H. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111850 · Cited by 29

Maternal exposure to dibutyl phthalate regulates MSH6 crotonylation to impair homologous recombination in fetal oocytes

Ma, Y., Mu, X., Gao, R., Zhang, Y., Geng, Y., Chen, X., Yin, X. H., Li, F., & He, J. (2023) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2023.131540 · Cited by 36

Lysine crotonylation of SERCA2a correlates to cardiac dysfunction and arrhythmia in Sirt1 cardiac-specific knockout mice

Chen, H., Wang, X.-C., Hou, H., Wang, J., Yang, Q., Chen, Y.-L., Chen, H., & He, G. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125151 · Cited by 35

P300 regulates histone crotonylation and preimplantation embryo development

Gao, D., Li, C., Liu, S., Xu, T., Lin, X., Tan, Y.-P., Gao, F.-M., Yi, L.-T., Zhang, J. V., Ma, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50731-0 · Cited by 44

Global Analysis of Lysine 2-Hydroxyisobutyrylome upon SAHA Treatment and Its Relationship with Acetylation and Crotonylation

Wu, Q., Li, K., Wang, C., Fan, P., Wu, Z., & Xu, X. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00289 · Cited by 36

Toxoplasma gondii Infection Inhibits Histone Crotonylation to Regulate Immune Response of Porcine Alveolar Macrophages

Yang, J., He, Z., Chen, C., Li, S., Qian, J., Zhao, J., & Fang, R. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.696061 · Cited by 33

KAT7-mediated CANX (calnexin) crotonylation regulates leucine-stimulated MTORC1 activity

Yan, G., Li, X., Zheng, Z., Gao, W., Chen, C., Wang, X., Cheng, Z., Yu, J., Zou, G., Farooq, M. Z., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2047481 · Cited by 30

Decrotonylation of AKT1 promotes AKT1 phosphorylation and activation during myogenic differentiation

Qian, Z., Ye, J., Li, J., Che, Y., Yu, W., Xu, P., Lin, J., Ye, F., Xu, X., Su, Z., et al. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.10.005 · Cited by 30

Analysis of the chloroplast crotonylome of wheat seedling leaves reveals the roles of crotonylated proteins involved in salt-stress responses

Zhu, D. Z., Liu, J., Duan, W., Sun, H., Zhang, L., & Yan, Y. (2023) · Journal of Experimental Botany · doi:10.1093/jxb/erad006 · Cited by 29

Post‐translational modifications of proteins in cardiovascular diseases examined by proteomic approaches

Št́astná, M. (2024) · FEBS Journal · doi:10.1111/febs.17108 · Cited by 32

Proteome-Wide Analyses Reveal the Diverse Functions of Lysine 2-Hydroxyisobutyrylation in Oryza sativa

Xue, C., Qiao, Z., Chen, X., Cao, P., Liu, K., Liu, S., Lu, Y., & Gong, Z. (2020) · Rice · doi:10.1186/s12284-020-00389-1 · Cited by 30

Chemical Biology Tools for Protein Lysine Acylation

Xie, Y., Du, S., Liu, Z., Liu, M., Xu, Z., Wang, X., Kee, J. X., Yi, F., Sun, H., & Yao, S. Q. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202200303 · Cited by 29

Reduction of H3K27cr Modification During DNA Damage in Colon Cancer

Liao, M., Chu, W., Sun, X., Zheng, W., Gao, S., Li, D., & Pei, D. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.924061 · Cited by 30

Crotonylation of NAE1 Modulates Cardiac Hypertrophy via Gelsolin Neddylation

Ju, J., Wang, K., Liu, F., Liu, C.-Y., Wang, Y.-H., Wang, S.-C., Zhou, L., Li, X., Wang, Y.-Q., Chen, X., et al. (2024) · Circulation Research · doi:10.1161/circresaha.124.324733 · Cited by 28

PTBP1 crotonylation promotes colorectal cancer progression through alternative splicing-mediated upregulation of the PKM2 gene

Hou, J., Wang, X., Chang, H.-J., Wang, X., Hao, S., Gao, Y., Li, G., Gao, L., Zhang, F.-P., Wang, Z., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05793-5 · Cited by 31

Genetically Encoded Benzoyllysines Serve as Versatile Probes for Interrogating Histone Benzoylation and Interactions in Living Cells

Tian, H., Yang, J., Guo, A., Ran, Y., Yang, Y., Yang, B., Huang, R., Liu, H., & Chen, X. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00614 · Cited by 27

Global Proteomic Analysis of Lysine Crotonylation in the Plant Pathogen Botrytis cinerea

Zhang, N., Yang, Z., Liang, W., & Liu, M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.564350 · Cited by 26

Regulatory Mechanism of Protein Crotonylation and Its Relationship with Cancer

Yang, S., Fan, X., & Yu, W. (2024) · Cells · doi:10.3390/cells13211812 · Cited by 27

Conversion of Ku80 K568 crotonylation to SUMOylation facilitates DNA non-homologous end joining and cancer radioresistance

Zhao, H., Gao, S., Han, Y., Xie, D., Xuan, L., Huang, X., Luo, J., Ran, Q., Li, G., Guo, H., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02210-1 · Cited by 28

Metabolites-mediated posttranslational modifications in cardiac metabolic remodeling: Implications for disease pathology and therapeutic potential

Guo, L., Du, Y., Li, H., He, T., Yao, L., Yang, G., & Yang, X. (2025) · Metabolism · doi:10.1016/j.metabol.2025.156144 · Cited by 25

Global Lysine Crotonylation Profiling of Mouse Liver

Liu, J., Wu, S., Liu, S., Sun, X., Wang, X., Xu, P., Chen, H., & Yang, J. (2020) · PROTEOMICS · doi:10.1002/pmic.202000049 · Cited by 23

Modulation of Gene Expression in Actinobacteria by Translational Modification of Transcriptional Factors and Secondary Metabolite Biosynthetic Enzymes

Martı́n, J. F., Liras, P., & Sánchez, S. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.630694 · Cited by 23

iKcr_CNN: A novel computational tool for imbalance classification of human nonhistone crotonylation sites based on convolutional neural networks with focal loss

Dou, L., Zhang, Z., Xu, L., & Zou, Q. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.06.032 · Cited by 24

Dynamics and Functional Interplay of Nonhistone Lysine Crotonylome and Ubiquitylome in Vascular Smooth Muscle Cell Phenotypic Remodeling

Cao, S., Chen, Z., Yue, L., Jiang, H., Ma, R.-Y., & Dong, L. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.783739 · Cited by 22

Chromatin lysine acylation: On the path to chromatin homeostasis and genome integrity

Chen, F., He, X., Xu, W., Zhou, L., Liu, Q., Chen, W., Zhu, W., & Zhang, J. (2024) · Cancer Science · doi:10.1111/cas.16321 · Cited by 21

Sorafenib Attenuates Fibrotic Hepatic Injury Through Mediating Lysine Crotonylation

Chen, X., & Ji, S. (2022) · Drug Design Development and Therapy · doi:10.2147/dddt.s368306 · Cited by 21

Novel post-translational modifications of protein by metabolites with immune responses and immune-related molecules in cancer immunotherapy

Chen, L., Huang, L., Gu, Y., Li, C., Sun, P., & Xiang, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133883 · Cited by 21

Crotonylation of MCM6 enhances chemotherapeutics sensitivity of breast cancer via inducing DNA replication stress

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Acyl post-translational modification of proteins by metabolites in cancer cells

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