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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Acetylation and deacetylation of non-histone proteins

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Lysine Acetylation: Codified Crosstalk with Other Posttranslational Modifications

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

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

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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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Dihydrolipoyl dehydrogenase promotes white adipocytes browning by activating the RAS/ERK pathway and undergoing crotonylation modification

Liu, Y., Liang, J., Liu, Z., Tian, X., & Sun, C. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.130816 · Cited by 15

Protein Post-Translational Modifications Based on Proteomics: A Potential Regulatory Role in Animal Science

Fan, S., Kong, C., Zhou, R., Zheng, X., Ren, D., & Yin, Z. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c08332 · Cited by 17

Development and Validation of a Prognostic Signature Based on the Lysine Crotonylation Regulators in Head and Neck Squamous Cell Carcinoma

Jiang, L., Yin, X., Zhang, H., Zhang, X., Cao, Z., Zhou, M., & Xu, W. (2023) · BioMed Research International · doi:10.1155/2023/4444869 · Cited by 14

Single-step fluorescent probes to detect decrotonylation activity of HDACs through intramolecular reactions

Xie, Y., Yang, L., Chen, Q., Zhang, J., Feng, L., Chen, J. L., Hao, Q., Zhang, L. N., & Sun, H. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113120 · Cited by 14

Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense

Wu, J. T., Meng, X., Jiang, W., Wang, Z., Zhang, J., Meng, F., Yao, X., Ye, M., Yao, L., Wang, L., et al. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.822374 · Cited by 14

Crotonylation modification and its role in diseases

Guo, Y., Li, J., & Zhang, K. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1492212 · Cited by 15

Fluoride induces immune-inflammatory disorder in the kidneys via histone lysine crotonylation in vivo

Zheng, J., Wang, Q., Xu, K., Ma, M., Wang, Z., Sun, Z., Yang, S. C., Wang, X., Yan, N., & Duan, X. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.117385 · Cited by 14

Crotonylation of IDH1 alleviates MASLD progression by enhancing the TCA cycle

Liu, S., Ji, Y., Wei, L., Zhang, Y., Zeng, L., Min, Y., Yin, D., Liu, K., Guan, C., Liu, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62731-9 · Cited by 13

YjgM is a crotonyltransferase critical for polymyxin resistance of Escherichia coli

Zhuang, J., Liu, S., Du, G., Fang, Z., Wu, J., Li, N., Zhong, T., Xu, J., He, Q., & Sun, X. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114161 · Cited by 13

p53 deficiency mediates cisplatin resistance by upregulating RRM2 and crotonylation of RRM2K283 through the downregulation of SIRT7

Sun, L., Li, Y., Wang, M., Luo, L., Sun, R., Yang, C., Bai, Y., Ding, C., & Wang, Y. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1423594 · Cited by 13

Potential functions and mechanisms of lysine crotonylation modification (Kcr) in tumorigenesis and lymphatic metastasis of papillary thyroid cancer (PTC)

Li, Z., Li, J., Li, F., Han, L., Sui, C., Zhou, L., Zhang, D., Fu, Y., Du, R., Kou, J., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05651-4 · Cited by 13

TaHSP18.6 and TaSRT1 interact to confer resistance to Fusarium crown rot by regulating the auxin content in common wheat

Zhang, N., Liu, L., Li, S., Wei, Y., Ren, W., Li, M., Zhao, S., Sun, Z., Yang, X., Ren, Y. N., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2500029122 · Cited by 12

Decrotonylation of cGAS K254 prompts homologous recombination repair by blocking its DNA binding and releasing PARP1

Guo, H., Han, Y., Yao, S., Chen, B., Zhao, H., Jin, J., Chen, S., Liu, Y., Gao, S., Guan, H., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107554 · Cited by 13

Novel post-translational modifications in the kidneys for human health and diseases

Xiang, T., Zhao, S., Wu, Y., Li, L., Fu, P., & Ma, L. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.121188 · Cited by 13

Function and mechanism of lysine crotonylation in health and disease

Hou, L., Chen, Y. J., Zhong, Q., Pei, J., Liu, L., Pi, H., Xie, M., & Zhao, G. (2024) · QJM · doi:10.1093/qjmed/hcae034 · Cited by 11

Protein crotonylation: An emerging regulator in DNA damage response

Ji, P., Zhang, G., Guo, Y., Song, H., Yuan, X., Hu, X., Guo, Z., Xia, P., Shen, R., & Wang, D. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122059 · Cited by 11

Differential Expression Study of Lysine Crotonylation and Proteome for Chronic Obstructive Pulmonary Disease Combined with Type II Respiratory Failure

Gan, Q. Y., Tang, D., Yan, Q., Chen, J., Xu, Y. J., Xue, W., Xiao, L., Zheng, F., Xu, H., Fu, Y., et al. (2021) · Canadian Respiratory Journal · doi:10.1155/2021/6652297 · Cited by 11

Mechanistic insights into post-translational modifications in hepatic fibrosis: pathogenic roles and therapeutic potentials

Bai, X., Liu, Z., Li, X., Sun, R., & Yu, Z. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07037-6 · Cited by 10

Protein lysine four‐carbon acylations in health and disease

Fang, Y., & Li, X. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.30981 · Cited by 10

Regulation of endothelial-to-mesenchymal transition by histone deacetylase 3 posttranslational modifications in neointimal hyperplasia

Chen, L., He, J., Zhang, Y., Li, Y., Zhang, T., Wang, R., Bai, L., Zhao, S., Liu, E., & Wang, W. (2023) · Annals of Translational Medicine · doi:10.21037/atm-22-4371 · Cited by 10

PlantNh-Kcr: a deep learning model for predicting non-histone crotonylation sites in plants

Jiang, Y., Yan, R., & Wang, X. (2024) · Plant Methods · doi:10.1186/s13007-024-01157-8 · Cited by 10

Global proteomic analyses of lysine acetylation, malonylation, succinylation, and crotonylation in human sperm reveal their involvement in male fertility

Tian, Y., Wang, H., Pan, T., Hu, X.-N., Ding, J., Chen, Y., Li, J. X., Chen, H., & Luo, T. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105213 · Cited by 10

Application of crotonylation modification in pan-vascular diseases

Yan, W., Zhang, Y., Dai, Y., & Ge, J. (2024) · Journal of drug targeting · doi:10.1080/1061186x.2024.2372316 · Cited by 10

Crotonylation versus acetylation in petunia corollas with reduced acetyl‐CoA due to PaACL silencing

Yang, W., Li, X., Jiang, G., Yu, L., Li, H., Yu, S., Zhao, H., & Liu, J. (2022) · Physiologia Plantarum · doi:10.1111/ppl.13794 · Cited by 10

Crotonylation of GAPDH regulates human embryonic stem cell endodermal lineage differentiation and metabolic switch

Zhang, J., Shi, G. W., Pang, J., Zhu, X. Q., Feng, Q., Na, J., Ma, W., Liu, D., & Songyang, Z. (2023) · Stem Cell Research & Therapy · doi:10.1186/s13287-023-03290-y · Cited by 10

Lactate Dehydrogenase A Crotonylation and Mono‐Ubiquitination Maintains Vascular Smooth Muscle Cell Growth and Migration and Promotes Neointima Hyperplasia

Chen, Z., Cao, S., Ren, Z., Zhang, T., Jiang, H., Hu, Z., & Dong, L. (2025) · Journal of the American Heart Association · doi:10.1161/jaha.124.036377 · Cited by 9

Histone crotonylation in tumors (Review)

Wang, X., Qu, Y., Li, Z., & Xia, Q. (2025) · Molecular and Clinical Oncology · doi:10.3892/mco.2025.2834 · Cited by 10

Sirtuin‐Derived Covalent Binder for the Selective Recognition of Protein Crotonylation

Ji, Y., Sun, L., Chen, Y., Qin, H., & Xuan, W. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202205522 · Cited by 9

Crotonate suppresses breast cancer metastasis and promotes immunotherapy response by inducing ACSS2-mediated EZH2-K348 crotonylation

Liu, B., Duan, X., Wang, G., Tang, Y., Zhou, K., Zhang, J. Q., Yu, Y., & Zhang, H. (2026) · Science Advances · doi:10.1126/sciadv.aea9892 · Cited by 8

Qualitative Proteome-wide Lysine Crotonylation Profiling Reveals Protein Modification Alteration in the Leukocyte Extravasation Pathway in Systemic Lupus Erythematosus

Zeng, H., Li, D., Dong, J., Zhou, X., Ou, M., Xue, W., Zhang, R., Zou, Y., Tang, D., Yin, L., et al. (2023) · ACS Omega · doi:10.1021/acsomega.3c06293 · Cited by 8

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

Lysine crotonylation is widespread on proteins of diverse functions and localizations in Toxoplasma gondii

Li, F.-C., Nie, L.-B., Elsheikha, H. M., Yin, F.-Y., & Zhu, X. (2021) · Parasitology Research · doi:10.1007/s00436-021-07057-3 · Cited by 8

Protein Crotonylation Expert Review: A New Lens to Take Post-Translational Modifications and Cell Biology to New Heights

Subba, P., & Prasad, T. S. K. (2021) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2021.0132 · Cited by 8

A novel strategy of gene screen based on multi-omics in Streptomyces roseosporus

Xu, W., Fang, J.-L., Bu, Q., Lyu, Z.-Y., Zhu, C., Sun, C., Zhao, Q., & Li, Y. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11904-3 · Cited by 8

Large-Scale Identification of Lysine Crotonylation Reveals Its Potential Role in Oral Squamous Cell Carcinoma

Yin, X., Hongbo, Z., Wei, Z., Wang, Y., Han, S., Zhou, M., Xu, W., & Han, W. (2023) · Cancer Management and Research · doi:10.2147/cmar.s424422 · Cited by 9

Emerging posttranslational modifications and their roles in DNA damage response

Wu, Z., Liu, Y., Zhang, M., & Wang, D. (2023) · Genome Instability & Disease · doi:10.1007/s42764-023-00115-3 · Cited by 8

MVNN-HNHC:A multi-view neural network for identification of human non-histone crotonylation sites

Gao, J., Zhao, Y., Chen, C., & Qiao, N. (2023) · Analytical Biochemistry · doi:10.1016/j.ab.2023.115426 · Cited by 7

Global crotonylome identifies EP300-regulated ANXA2 crotonylation in cumulus cells as a regulator of oocyte maturation

Zhou, C., Zeng, H., Xiao, X., Wang, L., Jia, L., Shi, Y., Zhang, M., Fang, C., Zeng, Y., Wu, T., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.129149 · Cited by 7

Protein post-translational modification crotonylation of TXN and GLO1 in artery and vein grafts for coronary artery surgery

Sun, W., Chen, H., Hou, H., Xue, H., Yang, Q., & He, G. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103608 · Cited by 7

Proteome-Wide Identification and Functional Analysis of Lysine Crotonylation in Trichophyton rubrum Conidial and Mycelial Stages

Xu, X., Hu, X., Dong, J., Xue, Y., Liu, T., & Jin, Q. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.832668 · Cited by 7

Recent progress in histone post-translational modifications as regulators of metabolic diseases: A review

Zhu, A., Ye, T., Tan, M., & Xu, J. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147964 · Cited by 7

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 · doi:10.1002/ange.202200303 · Cited by 6

Glycometabolism change during Burkholderia pseudomallei infection in RAW264.7 cells by proteomic analysis

Li, X., Zeng, Y., Guo, S., Chen, C., Liu, L., & Xia, Q. (2022) · Scientific Reports · doi:10.1038/s41598-022-16716-z · Cited by 6

Using ATCLSTM-Kcr to predict and generate the human lysine crotonylation database

Yang, Y., Wu, S., Kong, J., Zhu, Y., Liu, J.-F., & Yang, J. (2023) · Journal of Proteomics · doi:10.1016/j.jprot.2023.104905 · Cited by 7

Identification of Crotonylation Metabolism Signature Predicting Overall Survival for Clear Cell Renal Cell Carcinoma

Zheng, J., Liu, Y., Wei, K., Shi, J., Li, L., Jiang, X., & Tao, L. (2023) · International Journal of Clinical Practice · doi:10.1155/2023/5558034 · Cited by 6

Identification and validation of crotonylation-related diagnostic markers for lung adenocarcinoma via weighted correlation network analysis and machine learning

Hu, B., Chen, X., Zou, D., Du, X., Feng, S., Shen, Y., Sha, X., Jiang, F., Zhou, G., Lin, F., et al. (2025) · Translational Lung Cancer Research · doi:10.21037/tlcr-2025-204 · Cited by 5

The role of CddA and cGNAT2 in crotonylation of proteins in cyanobacteria

Lin, J., Li, Q., Liu, X., Zhan, J., Yuan, L., Yang, M., & Ge, F. (2025) · New Phytologist · doi:10.1111/nph.70310 · Cited by 5

Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post‐Translational Modification

Westerveld, M., Besermenji, K., Aidukas, D., Ostrovitsa, N., & Petracca, R. (2024) · ChemBioChem · doi:10.1002/cbic.202400639 · Cited by 6

Proteomic Analysis of Histone Crotonylation Suggests Diverse Functions in Myzus persicae

Xu, M., Xie, Y., Li, Y., Shen, L., Huang, K., Lin, Z., Li, B., Xia, C., Zhang, X., Chi, Y., et al. (2021) · ACS Omega · doi:10.1021/acsomega.1c01194 · Cited by 5

Crotonyl-coenzyme A (crotonyl-CoA)

Wang, Y., Chen, H., & Tang, X. (2025) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2025.03.004 · Cited by 4

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

Mo, W., Wei, S., Xie, X., Liu, T., & Deng, J. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1688548 · Cited by 4

Qualitative lysine crotonylation and 2-hydroxyisobutyrylation analysis in the ovarian tissue proteome of piglets

Yang, D., Li, X., Yu, B., & Peng, H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1176212 · Cited by 4

Global profiling of the crotonylome in Small Cell Lung CancerPreprint

Guo, Z., Gu, M., Huang, J., Zhou, P., & Ma, T. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.29.175877 · Cited by 4

Integrative analysis of crotonylation-associated genes reveals prognostic and therapeutic targets in gliomas

Yin, B., Fan, Z., Yu, P., Li, J., Wang, Y., & Shu, M. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1573997 · Cited by 3

Lactylation, Crotonylation and Succinylation: Decoding Their Roles in the Progression of Cardiovascular Disease

Xuchao, H., Zhang, Y., Zhao, Q., Li, Y., & Wu, X. (2026) · Reviews in Cardiovascular Medicine · doi:10.31083/rcm45696 · Cited by 3

High histone crotonylation modification in bovine fibroblasts promotes cell proliferation and the developmental efficiency of preimplantation nuclear transfer embryos

Zhao, X., Du, M., Wu, S., Du, Z., Liu, S., Yang, L., Ma, H., Zhang, L., Song, L., Bai, C., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-61148-6 · Cited by 5

Key Regulators of Parasite Biology Viewed Through a Post‐Translational Modification Repertoire

Zhang, N., Jiang, N., & Chen, Q. (2024) · PROTEOMICS · doi:10.1002/pmic.202400120 · Cited by 3

Genetically encoding ε-N-methacryllysine into proteins in live cells

Zhu, T.-Y., Chen, S., Zhang, M., Li, H., Wu, T., Ajiboye, E. G., Wang, J. W., Jin, B., Liu, D., Zhou, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57969-2 · Cited by 3

A Prognostic Lysine Crotonylation Signature Shapes the Immune Microenvironment in Hepatocellular Carcinoma

Su, W., Kang, K., Li, X., & Huang, H. (2025) · Current Medicinal Chemistry · doi:10.2174/0109298673381518250529110617 · Cited by 3

Large-scale lysine crotonylation analysis reveals the role of TRAF6-Ecsit complex in endoplasmic reticulum stress in mud crab (Scylla paramamosain)

Zhang, Y., Ji, P., Zhang, M., Tran, N. T., & Li, S. (2023) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2023.104898 · Cited by 4

Acetylated Histone Modifications: Intersection of Diabetes and Atherosclerosis

Liu, R., Li, L., Wang, Z., Zhu, J., & Ji, Y. (2023) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001516 · Cited by 4

EDS-Kcr: deep supervision based on large language model for identifying protein lysine crotonylation sites across multiple species

Zhang, H., Lin, X., Wang, Y., Pei, W.-F., Ma, G., Zhou, Z. H., Deng, K., Yan, D., & Liu, T. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf249 · Cited by 2

Fungi-Kcr: a language model for predicting lysine crotonylation in pathogenic fungal proteins

Chen, Y., Wang, X., Wang, Z., & Li, H. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1615443 · Cited by 2

DDX1 crotonylation mediates ACOX1 alternative splicing through HNRNPK to increase peroxisomal oxidative damage

Liu, J., Wang, S., Tao, C., Liu, H., Mao, Y., Zhao, X., Cheng, K., Mu, G., Wang, M., Wang, W., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.11.004 · Cited by 2

Novel insights in the diagnosis and treatment of non-small cell lung cancer: Post-translational modification of proteins

Sun, Y., Kong, W., Zhu, X., Chu, X., Wang, X., Zhu, G., He, X., & Li, J. (2025) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2025.189507 · Cited by 2

Protein crotonylation in cancer: mechanisms, functions, and therapeutic potential

Han, F., Shen, W., Zhang, X., Du, M., Ye, Q., Ma, J., & Hu, L.-P. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-025-10130-7 · Cited by 2

DeepNhKcr: Explainable Deep Learning Framework for the Prediction of Crotonylation Sites of Non-Histone Lysine in Plants Based on Pre-Trained Protein Language Model

Wang, J., Luo, Z., Geng, A., Xu, J., Meng, Y., Yan, S., Wei, L., Zhang, Z., Zhang, Q., Zou, Q., et al. (2025) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbbio.2025.3643930 · Cited by 2

MPA-KCro: Antibody-Free Crotonylome Profiling via 2-Mercaptophosphonic Acid Michael Addition and Titanium(IV)-Immobilized Metal Affinity Chromatography Enrichment

Yue, X., Zhang, Z., Miao, E., Liu, L., Song, X., Liu, X., Dai, M., Wang, Y., Ye, M., & Qin, H. (2026) · JACS Au · doi:10.1021/jacsau.5c01630 · Cited by 2

Crotonylation deficiency of S100A7 K49 promotes psoriatic keratinocyte proliferation through enhanced interaction with RAGE

Liang, H., Wang, Y., Li, J., & Zhang, K. (2025) · Scientific Reports · doi:10.1038/s41598-025-96874-y · Cited by 2

Global lysine crotonylation profiling reveals metabolic and stress-responsive mechanisms in Reynoutria japonica

You, L., Zhang, P., Cheng, H., Deng, Y., Xiong, H., Zhang, J., Ye, Z., Zhang, Z., Li, C., Espinosa, V. M. M., et al. (2025) · Journal of Plant Physiology · doi:10.1016/j.jplph.2025.154686 · Cited by 1

XAB2: a link between RNA metabolism, DNA damage repair, and human health

Pulzová, L., Sabo, M., & Chovanec, M. (2026) · Transcription · doi:10.1080/21541264.2026.2638065 · Cited by 1

Coming to light: the transcriptional regulatory roles of histone lysine crotonylation in health and disease

Dai, S., Ren, N., Liu, C.-M., & Yang, F. (2026) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-026-00935-7 · Cited by 1

Crotonylation: A novel layer of the epigenetic landscape in disease

Ma, Y., Zhang, Y., Cao, L., & Ren, H. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218579 · Cited by 1

Metabolic Fuel, Molecular Code: How Cancer Rewires Metabolite-Driven Post-Translational Modifications to Shape Tumor Fate

Wang, Y., Li, C., Liu, B., & Chen, X. (2026) · Cancer Bioscience · doi:10.1016/j.cbs.2026.100005 · Cited by 1

Post-translational modifications as hubs of amino acid metabolism in cancer: From oncogenic signaling to therapeutic targeting

Xu, N., Shao, J., Jiang, L., Zhao, H., & Zheng, W. (2026) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2026.189653 · Cited by 2

Sirtuin‐Derived Covalent Binder for the Selective Recognition of Protein Crotonylation

Ji, Y., Sun, L., Chen, Y., Qin, H., & Xuan, W. (2022) · Angewandte Chemie · doi:10.1002/ange.202205522 · Cited by 1

Deep Crotonylproteomics Analysis of High-Altitude Exposure Hearts in Mice

Yue, T., Yang, J., He, J., Xiong, S., Gao, H. J., Qin, S., Danzeng, D., Xu, J., & Hou, J. (2024) · ACS Omega · doi:10.1021/acsomega.4c05818 · Cited by 1

Chromatin, histones, and histone modifications in health and disease

Shah, S. G., Rashid, M., Verma, T., & Gupta, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817819-5.00008-5 · Cited by 2

Qualitative lysine crotonylome analysis in the ovarian tissue of Harmonia axyridis (Pallas)

Zheng, C., & Sun, L. (2021) · PLoS ONE · doi:10.1371/journal.pone.0258371 · Cited by 1

LDHA maintains the growth and migration of vascular smooth muscle cells and promotes neointima formation via crosstalk between K5 crotonylation and K76 mono-ubiquitinationPreprint

Chen, Z., Cao, S., Ren, Z., Jiang, H., Hu, Z.-K., & Dong, L. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.28.530389 · Cited by 1

Global Profiling of Lysine Crotonylation in Vascular Smooth Muscle Cell Phenotypic RemodelingPreprint

Cao, S., Yue, L., & Dong, L. (2021) · Research Square · doi:10.21203/rs.3.rs-504286/v1

Systematic identification of a CDYL1-dependent decrease in lysine crotonylation at DNA double-strand break sites functionally uncouples transcriptional silencing and repairPreprint

Abu‐Zhayia, E. R., Machour, F. E., Bishara, L. A., Ben‐Oz, B. M., & Ayoub, N. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.31.446417

Crotonylation promotes human embryonic stem cell endodermal lineage differentiation and metabolic switchPreprint

Songyang, Z., Zhang, J., Shi, G. W., Pang, J., Zhu, X. Q., Ma, W., & Liu, D. (2021) · Research Square · doi:10.21203/rs.3.rs-618212/v1

Quantitative Crotonylome Analysis Reveals the Mechanism of Shenkang Injection on Diabetic Nephropathy

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Additional file 4 of 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) · Figshare · doi:10.6084/m9.figshare.12544355

Additional file 3 of 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) · Figshare · doi:10.6084/m9.figshare.13578660

Additional file 10 of 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) · Figshare · doi:10.6084/m9.figshare.13578636

Additional file 11 of 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) · Figshare · doi:10.6084/m9.figshare.13578639

Additional file 6 of 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) · Figshare · doi:10.6084/m9.figshare.13578669

Additional file 14 of 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) · Figshare · doi:10.6084/m9.figshare.13578648

Additional file 2 of 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) · Figshare · doi:10.6084/m9.figshare.12544346

Additional file 13 of 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) · Figshare · doi:10.6084/m9.figshare.13578645

Additional file 7 of 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) · Figshare · doi:10.6084/m9.figshare.13578672

Additional file 2 of Crotonylation of GAPDH regulates human embryonic stem cell endodermal lineage differentiation and metabolic switch

Zhang, J., Shi, G. W., Pang, J., Zhu, X. Q., Feng, Q., Na, J., Ma, W., Liu, D., & Songyang, Z. (2023) · Figshare · doi:10.6084/m9.figshare.22621468

Additional file 8 of Proteome-wide and lysine crotonylation profiling reveals the importance of crotonylation in chrysanthemum (Dendranthema grandiforum) under low-temperature

Lin, P. C., Bai, H., He, L., Huang, Q., Zeng, Q.-H., Pan, Y., Jiang, B., Zhang, F., Zhang, L., & Liu, Q. (2021) · Figshare · doi:10.6084/m9.figshare.13578675

Additional file 9 of 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) · Figshare · doi:10.6084/m9.figshare.13578678

Additional file 5 of 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) · Figshare · doi:10.6084/m9.figshare.13578666

Additional file 4 of 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) · Figshare · doi:10.6084/m9.figshare.13578663

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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

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