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KAT2A coupled with the α-KGDH complex acts as a histone H3 succinyltransferase
Open accessAbstract
Histone modifications, such as the frequently occurring lysine succinylation, are central to the regulation of chromatin-based processes. However, the mechanism and functional consequences of histone succinylation are unknown. Here we show that the α-ketoglutarate dehydrogenase (α-KGDH) complex is localized in the nucleus in human cell lines and binds to lysine acetyltransferase 2A (KAT2A, also known as GCN5) in the promoter regions of genes. We show that succinyl-coenzyme A (succinyl-CoA) binds to KAT2A. The crystal structure of the catalytic domain of KAT2A in complex with succinyl-CoA at 2.3 Å resolution shows that succinyl-CoA binds to a deep cleft of KAT2A with the succinyl moiety pointing towards the end of a flexible loop 3, which adopts different structural conformations in succinyl-CoA-bound and acetyl-CoA-bound forms. Site-directed mutagenesis indicates that tyrosine 645 in this loop has an important role in the selective binding of succinyl-CoA over acetyl-CoA. KAT2A acts as a succinyltransferase and succinylates histone H3 on lysine 79, with a maximum frequency around the transcription start sites of genes. Preventing the α-KGDH complex from entering the nucleus, or expression of KAT2A(Tyr645Ala), reduces gene expression and inhibits tumour cell proliferation and tumour growth. These findings reveal an important mechanism of histone modification and demonstrate that local generation of succinyl-CoA by the nuclear α-KGDH complex coupled with the succinyltransferase activity of KAT2A is instrumental in histone succinylation, tumour cell proliferation, and tumour development.
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“In the vast majority of these studies to date, histone succinylation is associated with the opening of chromatin and increased gene transcription.”
From Loss of succinyl-CoA synthetase in mouse forebrain results in hypersuccinylation with perturbed neuronal transcription and metabolism (2023) · cites this paper as [42]
Experimental — accuracy not yet measuredIn the citing paper
“Under acidic conditions αKG is protonated and this promotes binding to LDHA and L-2HG production.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [52]
In the citing paper
“The authors demonstrate that this is independent of IDH1 and 2 and primarily mediated by LDHA and malate dehydrogenase (MDH) via “promiscuous” reduction of αKG and this is enhanced by acidic pH52.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [52]
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Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
Grant, P. A., Duggan, L. J., Côté, J., Roberts, S. M., Brownell, J. E., Candau, R., Ohba, R., Owen‐Hughes, T., Allis, C. D., Winston, F., et al. (1997) · Genes & Development · doi:10.1101/gad.11.13.1640 · Cited by 1,087
Nuclear PKM2 regulates β-catenin transactivation upon EGFR activation
Yang, W., Xia, Y., Ji, H., Zheng, Y., Liang, J., Huang, W., Gao, X., Aldape, K., & Lu, Z. (2011) · Nature · doi:10.1038/nature10598 · Cited by 1,051
Self-citationIdentification of lysine succinylation as a new post-translational modification
Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., & Zhao, Y. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.495 · Cited by 1,027
Weinert, B. T., Scholz, C. W., Wagner, S., Iešmantavičius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.024 · Cited by 774
NLStradamus: a simple Hidden Markov Model for nuclear localization signal prediction
Ba, A. N. N., Pogoutse, A. K., Provart, N. J., & Moses, A. M. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-202 · Cited by 697
Sutendra, G., Kinnaird, A. S., Dromparis, P., Paulin, R., Stenson, T. H., Haromy, A., Hashimoto, K., Zhang, N., Flaim, E., & Michelakis, E. D. (2014) · Cell · doi:10.1016/j.cell.2014.04.046 · Cited by 633
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Self-citationSuccinate-loaded tumor cell–derived microparticles reprogram tumor-associated macrophage metabolism
Lu, S., Li, J., Li, Y., Liu, S., Liu, Y., Liang, Y., Zheng, X., Chen, Y., Deng, J., Zhang, H., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adr4458 · Cited by 70
Self-citationLiao, W., Xu, N., Zhang, H., Liao, W., Wang, Y., Wang, S., Zhang, S., Jiang, Y., Xie, W., & Zhang, Y. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.699 · Cited by 65
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Gao, J., Shao, K., Chen, X., Li, Z., Liu, Z., Yu, Z., Aung, L. H. H., Wang, Y., & Li, P. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.11.146 · Cited by 62
Self-citationNonmetabolic functions of metabolic enzymes in cancer development
Lu, S., & Wang, Y. (2018) · 癌症：英文版 · doi:10.1186/s40880-018-0336-6 · Cited by 64
Self-citationJing, Y., Ding, D., Tian, G., Kwan, K. C. J., Liu, Z., Ishibashi, T., & Li, X. D. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa663 · Cited by 62
Self-citationDelaney, K., Tan, M., Zhu, Z., Gao, J., Dai, L., Kim, S., Ding, J., He, M., Halabelian, L., Yang, L., et al. (2021) · Cell Discovery · doi:10.1038/s41421-021-00344-4 · Cited by 60
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Wu, J., Liu, N., Chen, J., Tao, Q., Li, Q., Li, J., Chen, X., & Peng, C. (2024) · Research · doi:10.34133/research.0351 · Cited by 57
Wang, X., Luo, X., Xiao, R., Liu, X., Zhou, F., Jiang, D., Bai, J., Cui, M., You, L., & Yupei, Z. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02334-4 · Cited by 59
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Liu, Q., Wang, H., Zhang, H., Sui, L., Li, L., Xu, W., Du, S., Hao, P., Jiang, Y., Chen, J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2123065119 · Cited by 53
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Shao, F., Yang, X., Wang, W., Wang, J., Guo, W., Feng, X., Shi, S., Xue, Q., Gao, S., Gao, Y., et al. (2019) · 癌症：英文版 · doi:10.1186/s40880-019-0401-9 · Cited by 52
Self-citationLu, D., Song, Y., Yu, Y., Wang, D., Liu, B., Chen, L., Li, X., Li, Y., Cheng, L., Lv, F., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04077-w · Cited by 51
Self-citationDevelopmental origins and oncogenic pathways in malignant brain tumors
Lu, Q. R., Qian, L., & Zhou, X. (2019) · Wiley Interdisciplinary Reviews Developmental Biology · doi:10.1002/wdev.342 · Cited by 55
Wu, T., Zhao, Y., Zhang, X., Wang, Y., Chen, Q., Zhang, M., Sheng, H., Zhang, Y., Guo, J., Li, J., et al. (2025) · 癌症：英文版 · doi:10.1002/cac2.70048 · Cited by 50
Self-citationSupramolecular assembly of KAT2A with succinyl-CoA for histone succinylation
Wang, Y., Guo, Y. R., Xing, D., Tao, Y. J., & Lu, Z. (2018) · Cell Discovery · doi:10.1038/s41421-018-0048-8 · Cited by 51
Self-citationPhenylalanine diminishes M1 macrophage inflammation
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Self-citationDeciphering functional roles of protein succinylation and glutarylation using genetic code expansion
Weyh, M., Jokisch, M., Nguyen, T., Fottner, M., & Lang, K. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01500-5 · Cited by 49
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Ning, W., Xu, H., Jiang, P., Cheng, H., Deng, W., Guo, Y., & Xue, Y. (2020) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2019.11.010 · Cited by 47
Self-citationMechanisms of metabolism-coupled protein modifications
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Jia, H., Jiang, L., Shen, X., Ye, H., Li, X., Zhang, L., Hu, Y., Song, D., Jia, H., & Wang, Z. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02397-5 · Cited by 49
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Lu, Y., Bu, Q., Chuan, M., Cui, X., Zhao, Y. J., & Zhou, D. (2023) · The Plant Journal · doi:10.1111/tpj.16122 · Cited by 47
Yang, Z., He, M., Austin, J., Sayed, D. H., & Abdellatif, M. (2023) · Journal of Clinical Investigation · doi:10.1172/jci169399 · Cited by 45
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Liu, Z., Wang, R., Wang, Y., Duan, Y., & Zhan, H. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115713 · Cited by 43
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Li, J., Yan, C., Wang, Y., Chen, C., Yu, H., Liu, D., Huang, K., & Han, Y. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04881-y · Cited by 41
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Yu, W., Zhou, R., Li, N., Lei, Z.-C., Guo, D., Peng, F., Li, Y., Bai, X., Feng, S., Wang, Y., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01267-9 · Cited by 40
Self-citationOXCT1 succinylation and activation by SUCLA2 promotes ketolysis and liver tumor growth
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Lü, W., Che, X., Qu, X., Zheng, C., Yang, X., Bao, B., Li, Z., Wang, D., Jin, Y., Wang, Y., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.622198 · Cited by 40
Self-citationYang, Z., He, M., Austin, J., Pfleger, J. M., & Abdellatif, M. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101249 · Cited by 40
Hu, J., Chen, J., Hou, Q., Xu, X., Ren, J., Ma, L., & Yan, X. (2023) · Microbiome · doi:10.1186/s40168-023-01468-3 · Cited by 41
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
Histone malonylation is regulated by SIRT5 and KAT2A
Zhang, R., Bons, J., Scheidemantle, G. M., Liu, X., Bielska, O., Carrico, C., Rose, J., Heckenbach, I., Scheibye‐Knudsen, M., Schilling, B., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106193 · Cited by 40
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Acker, H. H. V., Ma, S., Scolaro, T., Kaech, S. M., & Mazzone, M. (2021) · Trends in Immunology · doi:10.1016/j.it.2021.03.006 · Cited by 39
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Sun, X., Zhang, Y., Chen, X., & Tang, X. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104418 · Cited by 38
Post-translational acylation of proteins in cardiac hypertrophy
Liu, Y., Yang, Q., & He, G. (2025) · Nature Reviews Cardiology · doi:10.1038/s41569-025-01150-1 · Cited by 38
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Wang, Y., Zhang, J., Li, B., & He, Q. (2019) · Small Methods · doi:10.1002/smtd.201900041 · Cited by 38
Self-citationZhao, X., Yang, X., Du, C., Huimin, H., Liu, S., Liu, G., Zhang, G., Fan, K., & Ma, J. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03284-4 · Cited by 38
Regulation of tumor metabolism by post translational modifications on metabolic enzymes
Dessai, A. S., Kalhotra, P., Novickis, A. T., & Dasgupta, S. (2022) · Cancer Gene Therapy · doi:10.1038/s41417-022-00521-x · Cited by 38
Zhang, C., & Huang, Z.-H. (2023) · Molecular Biotechnology · doi:10.1007/s12033-023-00778-z · Cited by 36
Ishiguro, T., Tanabe, K., Kobayashi, Y., Mizumoto, S., Kanai, M., & Kawashima, S. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-26114-z · Cited by 38
The Growing Landscape of Succinylation Links Metabolism and Heart Disease
Yang, L., Miao, S., Zhang, J., Wang, P., Liu, G., & Wang, J. (2021) · Epigenomics · doi:10.2217/epi-2020-0273 · Cited by 39
Zhang, Y., Ma, S., Nie, J., Liu, Z., Chen, F., Li, A., & Pei, D. (2023) · Small · doi:10.1002/smll.202207951 · Cited by 35
Crespo, M., Damont, A., Blanco, M., Lastrucci, E., Kennani, S. E., Ialy‐Radio, C., Khattabi, L. E., Terrier, S., Louwagie, M., Kieffer‐Jaquinod, S., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa163 · Cited by 43
Succinylation modification: a potential therapeutic target in stroke
Lian, J., Liu, W., Hu, Q., & Zhang, X. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382229 · Cited by 36
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Nickel, G. A., Pederson, N. J., Faheem, F., Yang, Z., Bulf, J., & Diehl, K. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110795 · Cited by 37
Succinylation and redox status in cancer cells
Dai, X., Zhou, Y., Han, F., & Li, J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1081712 · Cited by 37
Qin, Y.-P., Yu, H., Yuan, S.-Y., Yang, Z., Ren, F., Wang, Q., Li, F., Ren, J., Cheng, S., Zhou, Y.-J., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.795388 · Cited by 33
Role of succinylation modification in central nervous system diseases
Wang, C., Cui, W., Yu, B., Zhou, H., Cui, Z., Pin, G., Yu, T., & Feng, Y. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102242 · Cited by 32
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Wu, J., Chen, X.-W., Liu, Y., Wu, J.-Y., Chen, Z., & Peng, B. (2025) · Science Advances · doi:10.1126/sciadv.adu2856 · Cited by 33
Wu, G., Fan, X., Cheng, L., Chen, Z., Yi, Y., Liang, J., Huang, X., Yang, N., Yin, J., Guo, W., et al. (2025) · Science Advances · doi:10.1126/sciadv.adx6489 · Cited by 37
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A glimpse into novel acylations and their emerging role in regulating cancer metastasis
Shi, H., Cui, W., Qin, Y., Chen, L., Yu, T., & Lv, J. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05104-z · Cited by 35
Epigenetic modification of hepatitis B virus infection and related hepatocellular carcinoma
Zhang, Y., Cao, W., Wang, S., Zhang, L., Li, X., Zhang, Z., Xie, Y., & Li, M. (2024) · Virulence · doi:10.1080/21505594.2024.2421231 · Cited by 32
Self-citationCatalysis by protein acetyltransferase Gcn5
Albaugh, B. N., & Denu, J. M. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194627 · Cited by 33
Metabolic Fuel for Epigenetic: Nuclear Production Meets Local Consumption
Boon, R. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.768996 · Cited by 35
Shteinfer‐Kuzmine, A., Verma, A., Arif, T., Aizenberg, O., Paul, A., & Shoshan‐Barmatz, V. (2020) · IUBMB Life · doi:10.1002/iub.2407 · Cited by 31
Zhang, X., Liu, J., Cheng, Y., Chen, K., Chen, Y., Zhu, H., Li, Z., Liu, S., & Cao, X. (2023) · Journal of Autoimmunity · doi:10.1016/j.jaut.2023.103048 · Cited by 31
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Dashti, P., Lewallen, E. A., Gordon, J. A. R., Montecino, M. A., Davie, J., Stein, G. S., van Leeuwen, J. P. T. M., van der Eerden, B. C. J., & van Wijnen, A. J. (2024) · Bone · doi:10.1016/j.bone.2024.117043 · Cited by 32
The Mitochondrial Protein VDAC1 at the Crossroads of Cancer Cell Metabolism: The Epigenetic Link
Amsalem, Z., Arif, T., Shteinfer‐Kuzmine, A., Caspi, V. C., & Shoshan‐Barmatz, V. (2020) · Cancers · doi:10.3390/cancers12041031 · Cited by 30
He, D., Zhang, X., & Tu, J. (2020) · Cancer Medicine · doi:10.1002/cam4.3486 · Cited by 30
Guo, Y., Liu, B., Liu, Y., Sun, W., Gao, W., Mao, S., & Chen, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.690796 · Cited by 30
Self-citationRegulation of proteostasis and innate immunity via mitochondria-nuclear communication
Kim, S., Ramalho, T. R. D. O., & Haynes, C. M. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202310005 · Cited by 30
High Sugar Induced RCC2 Lactylation Drives Breast Cancer Tumorigenicity Through Upregulating MAD2L1
Zheng, B., Pan, Y., Qian, F., Liu, D., Ye, D., Yu, B., Zhong, S., Zheng, W., Wang, X., Zhou, B., et al. (2025) · Advanced Science · doi:10.1002/advs.202415530 · Cited by 29
Self-citationXue, 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
Self-citationChemical 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
Targeting 2-oxoglutarate dehydrogenase for cancer treatment.
Chang, L., Chiang, S.-K., Chen, S., & Hung, M. (2022) · PubMed Central · Cited by 29
Li, H., Wan, X., Wu, Z., Zhou, Y., Chen, R., Xu, W., Zhang, J., Yang, Z., Bai, L., Zhang, J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111724 · Cited by 29
Self-citationXu, Y., Ye, X., Zhou, Y., Cao, X., Peng, S., Peng, Y., Zhang, X., Sun, Y., Jiang, H., Huang, W., et al. (2023) · Frontiers of Medicine · doi:10.1007/s11684-022-0943-0 · Cited by 29
Zhang, H., Li, P., Ren, S., Cheng, Z., Zhao, G., & Zhao, W. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.001298 · Cited by 29
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Zhang, R., Fang, J., Xie, X., Carrico, C., Meyer, J. G., Wei, L., Bons, J., Rose, J., Riley, R. R., Kwok, R., et al. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01005-y · Cited by 29
Zhu, Y., & Lu, F. (2024) · BMC Cancer · doi:10.1186/s12885-024-12438-9 · Cited by 28
Zhang, L., Yang, Y., Li, Y., Wang, C., Bian, C., Wang, H., & Wang, F. (2025) · Biomarker Research · doi:10.1186/s40364-025-00788-w · Cited by 28
Li, X., Long, Y.-Q., Zhu, Y., Gu, J., Zhou, P., & Miao, C. (2025) · Advanced Science · doi:10.1002/advs.202506209 · Cited by 28
Self-citationT herapeutic targeting of chromatin: status and opportunities
Siklos, M. I., & Kubicek, S. (2021) · FEBS Journal · doi:10.1111/febs.15966 · Cited by 28
Mailloux, R. J. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103155 · Cited by 30
Arede, L., & Pina, C. (2020) · Experimental Hematology · doi:10.1016/j.exphem.2020.10.003 · Cited by 27
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Pallett, L. J., Dimeloe, S., Sinclair, L. V., Byrne, A. J., & Schurich, A. (2021) · Immunotherapy Advances · doi:10.1093/immadv/ltab010 · Cited by 28
Zhou, J., Yang, L., Ozohanics, O., Zhang, X., Wang, J., Ambrus, A., Arjunan, P., Brukh, R., Nemeria, N. S., Furey, W. F., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005432 · Cited by 27
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Nemeria, N. S., Zhang, X., Leandro, J., Zhou, J., Yang, L., Houten, S. M., & Jordan, F. (2021) · Life · doi:10.3390/life11050407 · Cited by 28
Ren, C., Wu, Q., Xiao, R., Ji, Y., Yang, X., Zhang, Z., Qin, H., Ma, J., & Xuan, W. (2022) · ChemBioChem · doi:10.1002/cbic.202200302 · Cited by 26
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Arede, L., Foerner, E., Wind, S., Kulkarni, R., Domingues, A. F., Giotopoulos, G., Kleinwaechter, S., Mollenhauer-Starkl, M., Davison, H., Chandru, A., et al. (2022) · Blood Advances · doi:10.1182/bloodadvances.2020002842 · Cited by 25
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Mancini, C., Lori, G., Pranzini, E., & Taddei, M. L. (2023) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2023.11.005 · Cited by 25
Qin, Y., Yang, P. C., He, W., Li, D., Zeng, L., Li, J., Zhou, T., Peng, J., Cao, L., & Huang, W. G. (2024) · Clinical Epigenetics · doi:10.1186/s13148-024-01650-w · Cited by 26
Self-citation
Metadata
- Authors
- Wang, Y., Guo, Y. R., Liu, K., Yin, Z., Liu, R., Xia, Y., Tan, L., Yang, P., Lee, J.-H., Li, X.-J., Hawke, D., Zheng, Y., Qian, X., Lyu, J., He, J., Xing, D., Tao, Y. J., & Lu, Z.
- Affiliations
- The University of Texas MD Anderson Cancer Center (US)
- Rice University (US)
- University of California, Berkeley (US)
- Houston Methodist (US)
- Hangzhou Medical College (CN)
- Wenzhou Medical University (CN)
- Affiliated Hospital of Qingdao University (CN)
- Corresponding author
- Xing, Dongming
- Tao, Yizhi Jane
- Lu, Zhimin
- ORCID
- Venue
- Nature
- Published
- 2017-12
- Volume
- 552
- Issue
- 7684
- Pages
- 273-277
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5841452
- OpenAlex
- W2773645338
- Cited by
- 567
- References
- 20
- Citations by year
- 2026: 84 · 2025: 123 · 2024: 77 · 2023: 61 · 2022: 55 · 2021: 60 · 2020: 47 · 2019: 33 · 2018: 26
- FWCI
- 12.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Rice Research Repository (Rice University) (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Human Genome Research Institute (U54HG007990)
- National Cancer Institute (R01CA109035, R01CA169603, P30CA016672, P50CA127001)
- National Institute of Neurological Disorders and Stroke (R01NS089754)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- GCN5, alpha-ketoglutarate dehydrogenase complex, succinyl-CoA, transcription start sites, gene expression regulation, chromatin modification, tumor cell proliferation
- MeSH terms
- Protein Domains, p300-CBP-Associated Factor, Acetyl Coenzyme A, Acyl Coenzyme A, Animals, Cell Nucleus, Female, Gene Expression Regulation, Histones, Humans, Ketoglutarate Dehydrogenase Complex, Lysine, Models, Molecular, Neoplasms, Protein Binding, Tyrosine, Mutagenesis, Site-Directed, Crystallography, X-Ray, Transcription Initiation Site, Cell Line, Tumor, Cell Proliferation, Mice, Histone Acetyltransferases
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