Global profiling of crotonylation on non-histone proteins

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

Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902 · see citing works

Acetylation and deacetylation of non-histone proteins

Glozak, M. A., Sengupta, N., Zhang, X., & Seto, E. (2005) · Gene · doi:10.1016/j.gene.2005.09.010 · Cited by 1,584 · see citing works

Lysine Acetylation: Codified Crosstalk with Other Posttranslational Modifications

Yang, X.-J., & Seto, E. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.002 · Cited by 1,006 · see citing works

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

Sabari, B. R., Tang, Z., Huang, H., Yong-Gonzalez, V., Molina, H., Kong, H. E., Dai, L., Shimada, M., Cross, J. R., Zhao, Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.029 · Cited by 659 · see citing works

Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins

Feldman, J. L., Baeza, J., & Denu, J. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.511261 · Cited by 637 · see citing works

Cross-regulation of histone modifications

Latham, J. A., & Dent, S. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1307 · Cited by 406 · see citing works

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

Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324 · see citing works

YEATS2 is a selective histone crotonylation reader

Zhao, D. Y., Guan, H., Zhao, S., Mi, W., Wen, H., Li, Y., Zhao, Y., Allis, C. D., Shi, X., & Li, H. (2016) · Cell Research · doi:10.1038/cr.2016.49 · Cited by 224 · see citing works

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

Madsen, A. S., & Olsen, C. A. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203754 · Cited by 122 · see citing works

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

Fellows, R., Denizot, J., Stellato, C., Cuomo, A., Jain, P., Stoyanova, E., Balázsi, S., Hajnády, Z., Liebert, A., Kazakevych, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02651-5 · Cited by 568 · see citing works

iLearnPlus: a comprehensive and automated machine-learning platform for nucleic acid and protein sequence analysis, prediction and visualization

Chen, Z., Zhao, P., Li, C., Li, F., Xiang, D., Chen, Y., Akutsu, T., Daly, R. J., Webb, G. I., Zhao, Q., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab122 · Cited by 279 · see citing works

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

Wu, X., Xu, M., Geng, M., Chen, S., Little, P. J., Xu, S., & Weng, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01439-y · Cited by 290 · see citing works

Protein acylation: mechanisms, biological functions and therapeutic targets

Shang, S., Liu, J., & Hua, F. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01245-y · Cited by 247 · see citing works

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

Yuan, M., Yang, B., Rothschild, G., Mann, J. J., Sanford, L. D., Tang, X., Huang, C., Wang, C., & Zhang, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01519-z · Cited by 246 · see citing works

p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis

Huang, H., Tang, S., Ji, M. H., Tang, Z., Shimada, M., Liu, X., Qi, S., Locasale, J. W., Roeder, R. G., Zhao, Y., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.011 · Cited by 221 · see citing works

Beyond histone acetylation—writing and erasing histone acylations

Zhao, S., Zhang, X., & Li, H. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.10.001 · Cited by 207 · see citing works

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

Li, W., Li, F., Zhang, X., Lin, H., & Xu, C. S. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00825-8 · Cited by 203 · see citing works

Short-chain fatty acid, acylation and cardiovascular diseases

Chen, X., Chen, X., & Tang, X. (2020) · Clinical Science · doi:10.1042/cs20200128 · Cited by 186 · see citing works

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

Yu, H., Bu, C., Liu, Y., Gong, T., Liu, X., Liu, S., Peng, X., Zhang, W., Peng, Y., Yang, J., et al. (2020) · Science Advances · doi:10.1126/sciadv.aay4697 · Cited by 157 · see citing works

Functions and mechanisms of lysine crotonylation

Wan, J., Liu, H., Chu, J., & Zhang, H. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14650 · Cited by 138 · see citing works

Protein lysine crotonylation: past, present, perspective

Jiang, G., Li, C., Lü, M. K., Lu, K., & Li, H. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03987-z · Cited by 138 · see citing works

Lysine crotonylation is involved in hepatocellular carcinoma progression

Wan, J., Liu, H., & Ming, L. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.12.148 · Cited by 106 · see citing works

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

Yang, Y., Wen, R., Yang, N., Zhang, T., & Liu, C. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00684-9 · Cited by 102 · see citing works

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

Fu, Y., Yu, J., Li, F., & Ge, S. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02338-w · Cited by 96 · see citing works

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

Liu, S., Xue, C., Fang, Y., Chen, G., Peng, X., Zhou, Y., Chen, C., Liu, G., Gu, M., Wang, K., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000640 · Cited by 88 · see citing works

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

Huang, H., Wang, D., & Zhao, Y. (2018) · PROTEOMICS · doi:10.1002/pmic.201700230 · Cited by 83 · see citing works

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

Cheng, X., Wang, K., Zhao, Y., & Wang, K. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01560-5 · Cited by 86 · see citing works

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

Stein, R. A., & Riber, L. (2023) · microLife · doi:10.1093/femsml/uqad032 · Cited by 81 · see citing works

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

Wu, Q., Li, W., Wang, C., Fan, P., Cao, L., Wu, Z., & Wang, F. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00380 · Cited by 78 · see citing works

An Expanding Repertoire of Protein Acylations

Xu, Y., Shi, Z., & Bao, L. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100193 · Cited by 78 · see citing works

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

Liu, K., Yuan, C., Li, H., Kunyan, C., Lu, L., Shen, C., & Zheng, X. (2018) · Scientific Reports · doi:10.1038/s41598-018-26676-y · Cited by 76 · see citing works

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

Tao, Z., & Wang, Y. (2024) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2297811 · Cited by 78 · see citing works

Histone crotonylation-centric gene regulation

Li, K., & Wang, Z. (2021) · Epigenetics & Chromatin · doi:10.1186/s13072-021-00385-9 · Cited by 73 · see citing works

A global view of the human post-translational modification landscape

Kitamura, N., & Galligan, J. J. (2023) · Biochemical Journal · doi:10.1042/bcj20220251 · Cited by 70 · see citing works

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 69 · see citing works

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

Guo, Z., Zhang, Y., Wang, H., Liao, L., Ma, L., Zhao, Y., Yang, R., Li, X., Niu, J., Chu, Q., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51232-w · Cited by 69 · see citing works

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 66 · see citing works

Modulation of cellular metabolism by protein crotonylation regulates pancreatic cancer progression

Zheng, Y., Le, Z., Qin, Z., Guo, Y., Wang, S., Xue, M., Shen, K.-Y., Hu, B., Wang, X., Wang, C., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112666 · Cited by 67 · see citing works

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 · see citing works

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 61 · see citing works

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 · see citing works

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 58 · see citing works

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 57 · see citing works

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 · see citing works

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 54 · see citing works

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 · see citing works

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 · see citing works

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 53 · see citing works

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 · see citing works

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 51 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 39 · see citing works

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 38 · see citing works

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 39 · see citing works

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 39 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 35 · see citing works

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 · see citing works

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 34 · see citing works

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 35 · see citing works

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 32 · see citing works

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 31 · see citing works

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 · see citing works

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 · see citing works

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

Stastna, M. (2024) · The FEBS Journal · doi:10.1111/febs.17108 · Cited by 28 · see citing works

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 29 · see citing works

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 · see citing works

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 29 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 24 · see citing works

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 · see citing works

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

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

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 23 · see citing works

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 21 · see citing works

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 20 · see citing works

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 · see citing works

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 · see citing works

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

Song, H., Guo, Z., Xie, K., Liu, X., Yang, X., Shen, R., & Wang, D. (2024) · Cell Proliferation · doi:10.1111/cpr.13759 · Cited by 20 · see citing works

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

Wang, X., Guo, Y., Fu, Y., Zhang, C., Chen, W., Tang, X. T., Yu, Y., Chen, Y., Ding, G., & Zhang, J. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02535-4 · Cited by 20 · see citing works

The role of post-translational modifications in driving abnormal cardiovascular complications at high altitude

Hou, J., Wen, X., Long, P., Xiong, S., Liu, H., Cai, L., Deng, H., & Zhang, Z. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.886300 · Cited by 18 · see citing works

Lysine Crotonylation: An Emerging Player in DNA Damage Response

Zhao, Y., Hao, S., Wu, W., Li, Y., Hou, K., Liu, Y., Cui, W., Xu, X., & Wang, H. (2022) · Biomolecules · doi:10.3390/biom12101428 · Cited by 21 · see citing works

CapsNh-Kcr: Capsule network-based prediction of lysine crotonylation sites in human non-histone proteins

Khanal, J., Kandel, J., Tayara, H., & Chong, K. T. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.11.056 · Cited by 19 · see citing works

Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

Gao, Y., Lee, H., Kwon, O. K., Tan, M., Kim, K., & Lee, S. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00462 · Cited by 18 · see citing works

Lysine crotonylation in disease: mechanisms, biological functions and therapeutic targets

Ji, Y., Liu, S., Zhang, Y., Min, Y., Wei, L., Guan, C., Yu, H., & Zhang, Z. (2025) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00577-7 · Cited by 18 · see citing works

Lysine crotonylation: A challenging new player in the epigenetic regulation of plants

la Rosa, P. A. C.-D., Aragón-Rodríguez, C., Ceja-López, J. A., García-Arteaga, K. F., & De‐la‐Peña, C. (2022) · Journal of Proteomics · doi:10.1016/j.jprot.2022.104488 · Cited by 18 · see citing works

Dynamic post‐translational modifications in obesity

Yang, H., Yang, K., Gu, H., & Sun, C. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14889 · Cited by 18 · see citing works

DeepKcrot: A Deep-Learning Architecture for General and Species-Specific Lysine Crotonylation Site Prediction

Wei, X., Sha, Y., Zhao, Y., He, N., & Li, L. (2021) · IEEE Access · doi:10.1109/access.2021.3068413 · Cited by 18 · see citing works

Protein Crotonylation Promotes Osteogenic Differentiation of Periodontal Ligament Stem Cells via the PI3K-AKT Pathway

Han, R., Dang, R., Liu, F., Nie, S., Tao, S., Xing, L., Yang, T., Hu, M., & Liu, D. (2024) · Stem Cells · doi:10.1093/stmcls/sxae018 · Cited by 17 · see citing works

PKM2 crotonylation reprograms glycolysis in VSMCs, contributing to phenotypic switching

Cao, S., Ma, R.-Y., Cao, T., Hu, T., Yang, S., Ren, Z., Niu, J.-L., Zheng, M.-Q., Han, M., & Dong, L. (2025) · Oncogene · doi:10.1038/s41388-025-03353-9 · Cited by 17 · see citing works

Global Lysine Crotonylation Alterations of Host Cell Proteins Caused by Brucella Effector BspF

Zhu, J., Dong, Q., Dong, C., Zhang, X., Zhang, H., & Chen, Z. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.603457 · Cited by 17 · see citing works

Global Profiling of the Lysine Crotonylome in Different Pluripotent States

Lv, Y., Bu, C., Meng, J., Ward, C., Volpe, G., Hu, J., Jiang, M., Guo, L., Chen, J., Esteban, M. A., et al. (2021) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2021.01.004 · Cited by 17 · see citing works

Protein lysine crotonylation in cellular processions and disease associations

Zhao, H., Han, Y., Zhou, P., Guan, H., & Gao, S. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.06.029 · Cited by 17 · see citing works

Dynamic Responses of Barley Root Succinyl-Proteome to Short-Term Phosphate Starvation and Recovery

Wang, J., Ma, Z., Li, C., Ren, P., Yao, L., Li, B., Meng, Y., Ma, X., Si, E., Yang, K., et al. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.649147 · Cited by 16 · see citing works

Crotonylation of PRKACA enhances PKA activity and promotes colorectal cancer development via the PKA-FAK-AKT pathway

Hou, J., Gao, L., Shen, J., Zhou, L., Shi, J., Sun, T., Hao, S., Wang, D., & Cao, J. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.02.018 · Cited by 15 · see citing works

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 54 · see citing works

Protein crotonylation: Basic research and clinical diseases

Li, D., Lin, L., Xu, F., Feng, T., Tao, Y., Miao, H., & Yang, F. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101694 · Cited by 8 · see citing works

Large-Scale Identification of Protein Crotonylation Reveals Its Role in Multiple Cellular Functions

Wei, W., Mao, A., Tang, B., Zeng, Q., Gao, S., Liu, X., Lu, L., Li, W., Du, J. X., Li, J., et al. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00012 · Cited by 163 · see citing works

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 · see citing works

Research Progress on Crotonylation in Malignant Tumor

Fangyuan, L., & Su, L. (2023) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.3971/j.issn.1000-8578.2023.22.0770