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ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation
Open accessAbstract
Chromatin Modifier Modulates Gene Expression: Modification of chromatin structure is usually thought of as a global, relatively nonspecific way of modulating gene expression. However, Wellen et al. (p. 1076 ; see the Perspective by Rathmell and Newgard ) demonstrate that such regulation helps link growth factor–stimulated increases in metabolism to appropriate changes in gene expression. Adenosine triphosphate (ATP)–citrate lyase (ACL), which converts citrate to acetyl–coenzyme A (CoA) in the mitochondria of mammalian cells during metabolism of glucose, was also found to be present in the nucleus, where it might regulate activity of histone acetyl transferases (HATs) by controlling the availability of acetyl-CoA. Indeed, depletion of ACL from cultured human colon carcinoma cells specifically decreased histone acetylation in the nucleus, but appeared not to affect the overall amount of acetylation of proteins in the cells. Loss of ACL in cultured mouse 3T3-L1 cells diminished the increase in histone acetylation normally associated with hormone-stimulated differentiation of these cells and inhibited the increase in expression of specific genes, such as that encoding the Glut4 glucose transporter. Thus, ACL may help cells link metabolic activity to changes in gene expression.
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In the citing paper
“the production of acetyl-CoA in HeLa cells necessary to drive histone acetylation has been attributed to the enzymatic conversion of citrate into oxaloacetate and acetyl-CoA via the ATP citrate lyase enzyme”
From Influence of Metabolism on Epigenetics and Disease (2013) · cites this paper as Wellen et al., 2009
In the citing paper
“the GCN5 histone acetyltransferase enzyme of the SAGA complex is of critical importance for histone acetylation in response to the combined provision of glucose and growth factors to otherwise quiescent cells.”
From Influence of Metabolism on Epigenetics and Disease (2013) · cites this paper as Wellen et al., 2009
In the citing paper
“cancer cells make acetyl-CoA via a fundamentally different pathway than prototrophic yeast”
From Influence of Metabolism on Epigenetics and Disease (2013) · cites this paper as Wellen et al., 2009
In the citing paper
“However, citrate export to the cytosol and subsequent cleavage by ACL provides a major source of cytosolic acetyl-CoA that is the obligate substrate for both de novo lipid synthesis and protein acetylation reactions (39, 187, 188).”
From Regulation and function of the mammalian tricarboxylic acid cycle (2023) · cites this paper as [39]
In the citing paper
“Furthermore, studies have shown that both the glucose- and oncogene-driven increases in global histone acetylation are blocked by ACLY inhibition (Lee et al., 2014; Wellen et al., 2009).”
From The emerging hallmarks of cancer metabolism (2016) · cites this paper as Wellen et al., 2009
In the citing paper
“Acetylation requires a pool of the metabolite acetyl-CoA in the nucleus.155”
From Epigenetic mechanisms of major depression: Targeting neuronal plasticity (2018) · cites this paper as [155]
In the citing paper
“Glucose availability and acetyl-CoA production can also influence epigenetics by regulating the cytosolic acetyl-CoA pools available for histone acetylation reactions (51), raising the prospect that glucose-dependent metabolic flux may help drive or reinforce T cell differentiation programs.”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [51]
In the citing paper
“The acetyl-CoA groups used to modify histones are predominantly produced by acetyl-CoA synthetase in yeast and ATP-citrate lyase in mammalian cells, both of which enter the nucleus to produce a localized acetyl-CoA pool for this purpose (Figure 2).”
From Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us? (2012) · cites this paper as Wellen et al., 2009
In the citing paper
“Loss of function of these enzymes reduces histone acetylation, with global consequences on gene expression (Takahashi et al., 2006; Wellen et al., 2009).”
From Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us? (2012) · cites this paper as Wellen et al., 2009
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Citations
Cites
The Role of Chromatin during Transcription
Li, B., Carey, M., & Workman, J. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.015 · Cited by 3,503
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924
Acetylation of Histones and Transcription-Related Factors
Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,824
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
ATP citrate lyase inhibition can suppress tumor cell growth
Hatzivassiliou, G., Zhao, F., Bauer, D. E., Andreadis, C., Shaw, A. N., Dhanak, D., Hingorani, S. R., Tuveson, D. A., & Thompson, C. B. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.09.008 · Cited by 1,086
Self-citationHistone deacetylases and cancer
Glozak, M. A., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210610 · Cited by 1,031
Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival
Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., Lamming, D. W., Souza-Pinto, N. C., Bohr, V. A., Rosenzweig, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.035 · Cited by 950
Paine, P. L., Moore, L. C., & Horowitz, S. B. (1975) · Nature · doi:10.1038/254109a0 · Cited by 824
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792
Histone acetylation and deacetylation in yeast
Kurdistani, S. K., & Grunstein, M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1075 · Cited by 677
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Folmes, C. D. L., Ma, H., Mitalipov, S. M., & Terzic, A. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.02.001 · Cited by 48
Biphasic Modeling of Mitochondrial Metabolism Dysregulation during Aging
Baker, D. J., & Peleg, S. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.06.005 · Cited by 48
Impact of nutrient overload on metabolic homeostasis
Qiu, H., & Schlegel, V. L. (2018) · Nutrition Reviews · doi:10.1093/nutrit/nuy023 · Cited by 51
Zhang, J., Fan, T., Mao, Y.-Z., Hou, J., Wang, M., Zhang, M., Lin, Y., Zhang, L., Yan, G., An, Y., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00405-8 · Cited by 48
Diabetes Primes Neutrophils for Neutrophil Extracellular Trap Formation through Trained Immunity
Shrestha, S., Lee, Y.-B., Lee, H., Choi, Y., Park, B.-Y., Kim, M. J., Youn, Y.-J., Kim, S.-H., Jung, S.-J., Song, D., et al. (2024) · Research · doi:10.34133/research.0365 · Cited by 50
A two-way relationship between histone acetylation and metabolism
Charidemou, E., & Kirmizis, A. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.10.005 · Cited by 49
Lactylation in cancer: metabolic mechanism and therapeutic strategies
Sui, Y., Shen, Z., Wang, Z., Feng, J., & Zhou, G. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02349-4 · Cited by 57
Concise Review: Energy Metabolites: Key Mediators of the Epigenetic State of Pluripotency
Moussaieff, A., Kogan, N. M., & Aberdam, D. (2015) · Stem Cells · doi:10.1002/stem.2041 · Cited by 47
Ge, Z., Zhang, C., Schatten, H., & Sun, Q. (2014) · Biology of Reproduction · doi:10.1095/biolreprod.114.118141 · Cited by 47
Imielinski, M. B., Cha, S., Rejtar, T., Richardson, E. A., Karger, B. L., & Sgroi, D. C. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014910 · Cited by 47
Mitochondrial regulation of hematopoietic stem cells
Snoeck, H. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.12.010 · Cited by 50
Wang, Y., Dong, C., & Zhou, B. P. (2019) · Genes & Diseases · doi:10.1016/j.gendis.2019.09.012 · Cited by 48
Dai, M., Yang, B., Chen, J., Liu, F., Zhou, Y., Zhou, Y., Xu, Q., Jiang, S., Zhao, S., Li, X., et al. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.04.024 · Cited by 49
Icard, P., Simula, L., Wu, Z., Berzan, D., Sogni, P., Dohan, A. J. J., Dautry, R., Coquerel, A., Lincet, H., Loi, M., et al. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100790 · Cited by 48
ATP-citrate lyase (ACLY) inhibitors as therapeutic agents: a patenting perspective
Granchi, C. (2022) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2022.2067478 · Cited by 47
Chen, Y., Qian, J., He, Q., Zhao, H., Toral‐Barza, L., Shi, C., Zhang, X., Wu, J., & Yu, K. (2016) · Oncotarget · doi:10.18632/oncotarget.8279 · Cited by 50
Castillo, J., López‐Rodas, G., & Franco, L. (2017) · Advances in experimental medicine and biology · doi:10.1007/5584_2017_58 · Cited by 48
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Godfrey, W. H., & Kornberg, M. D. (2020) · Metabolites · doi:10.3390/metabo10110426 · Cited by 50
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Li, Y., Xie, Z., Song, Q., & Li, J.-Y. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00864-z · Cited by 49
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Zhang, B., & Schroeder, F. C. (2025) · Nature Chemical Biology · doi:10.1038/s41589-024-01805-z · Cited by 46
José, C., Melser, S., Bénard, G., & Rossignol, R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4357 · Cited by 51
Systems analysis of metabolic phenotypes: what have we learnt?
Sweetlove, L. J., Obata, T., & Fernie, A. R. (2013) · Trends in Plant Science · doi:10.1016/j.tplants.2013.09.005 · Cited by 46
Wen, S., Wang, J., Liu, P., Li, Y., Lu, W., Hu, Y., Liu, J., He, Z., & Huang, P. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.10.015 · Cited by 47
Regulation of inflammation in diabetes: From genetics to epigenomics evidence
Diedisheim, M., Carcarino, E., Vandiedonck, C., Roussel, R., Gautier, J., & Venteclef, N. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101041 · Cited by 48
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Giblin, W., Bringman, L. R., Guo, A. H., Kumar, S., Monovich, A. C., Mostafa, A. M., Skinner, M. E., Azar, M., Mady, A. S. A., Chung, C. H., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci138926 · Cited by 47
Cancer cell metabolism connects epigenetic modifications to transcriptional regulation
Morrison, A. J. (2021) · FEBS Journal · doi:10.1111/febs.16032 · Cited by 47
An extended Myc network contributes to glucose homeostasis in cancer and diabetes
Christopher, W. P. (2011) · Frontiers in bioscience · doi:10.2741/3848 · Cited by 48
Rodrigues, M. F., Carvalho, É., Pezzuto, P., Rumjanek, F. D., & Amoêdo, N. D. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25036 · Cited by 48
Inflammation driven metabolic regulation and adaptation in macrophages
Gupta, S., & Sarangi, P. P. (2022) · Clinical Immunology · doi:10.1016/j.clim.2022.109216 · Cited by 46
Metabolic regulation of the plant epigenome
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
ACL and HAT1 form a nuclear module to acetylate histone H4K5 and promote cell proliferation
Xu, Q., Yue, Y., Liu, B., Chen, Z., Ma, X., Wang, J., Zhao, Y. J., & Zhou, D. (2023) · Nature Communications · doi:10.1038/s41467-023-39101-4 · Cited by 45
The role of epigenetics in women’s reproductive health: the impact of environmental factors
Yu, X., Xu, J., Song, B., Zhu, R., Liu, J., Liu, Y. F., & Ma, Y. J. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1399757 · Cited by 47
Gao, S., Sun, H., Jiang, H., Li, L., Hu, X., Xu, X., & Jin, W. (2015) · Oncotarget · doi:10.18632/oncotarget.6222 · Cited by 45
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Munakata, Y., Ichinose, T., Ogawa, K., Itami, N., Tasaki, H., Shirasuna, K., Kuwayama, T., & Iwata, H. (2016) · Theriogenology · doi:10.1016/j.theriogenology.2016.05.036 · Cited by 45
Vidimar, V., Gius, D. R., Chakravarti, D., Bulun, S. E., Wei, J., & Kim, J. J. (2016) · Science Advances · doi:10.1126/sciadv.1601132 · Cited by 45
Wellen, K. E., & Snyder, N. W. (2019) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000580 · Cited by 48
Self-citationJiang, Y., Hu, T., Wang, T., Shi, X. E., Kitano, A., Eagle, K., Hoegenauer, K. A., Konopleva, M. Y., Lin, C. Y., Young, N. L., et al. (2019) · Blood · doi:10.1182/blood.2019001076 · Cited by 47
The therapeutic potential of epigenetic manipulation during infectious diseases
Cole, J., Morris, P., Dickman, M. J., & Dockrell, D. H. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.07.013 · Cited by 49
Anti-Inflammatory Effects of Spirulina platensis Extract via the Modulation of Histone Deacetylases
Pham, T., Park, Y.-K., & Lee, J.-Y. (2016) · Nutrients · doi:10.3390/nu8060381 · Cited by 44
Unraveling the intricate relationship between lipid metabolism and oncogenic signaling pathways
Khan, F., Elsori, D. H., Verma, M., Pandey, S., Rab, S. O., Siddiqui, S., Alabdallah, N. M., Saeed, M., & Pandey, P. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1399065 · Cited by 45
Lazaropoulos, M. P., Gibb, A., Chapski, D. J., Nair, A. A., Reiter, A. N., Roy, R., Eaton, D., Bedi, K. C., Margulies, K. B., Wellen, K. E., et al. (2024) · Nature Cardiovascular Research · doi:10.1038/s44161-024-00502-3 · Cited by 44
Self-citationWu, S., Bi, J., Cloughesy, T. F., Cavenee, W. K., & Mischel, P. S. (2014) · PubMed · doi:10.7497/j.issn.2095-3941.2014.04.004 · Cited by 44
Cui, M., Wang, X.-L., Tang, D., Zhang, J., Liu, Y., & Zeng, S. (2010) · Theriogenology · doi:10.1016/j.theriogenology.2010.09.031 · Cited by 45
Friis, R. M. N., Glaves, J. P., Huan, T., Li, L., Sykes, B. D., & Schultz, M. C. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.029 · Cited by 44
Sasaki, C. Y., Chen, G., Munk, R. B., Eitan, E., Martindale, J. L., Longo, D. L., & Ghosh, P. (2015) · European Journal of Immunology · doi:10.1002/eji.201445422 · Cited by 45
Defining the Orphan Functions of Lysine Acetyltransferases
Montgomery, D. C., Sorum, A. W., & Meier, J. L. (2015) · ACS Chemical Biology · doi:10.1021/cb500853p · Cited by 44
Badur, M. G., & Metallo, C. M. (2017) · Metabolic Engineering · doi:10.1016/j.ymben.2017.11.013 · Cited by 44
Genetics of lipid metabolism in prostate cancer
Poulose, N., Amoroso, F., Steele, R. E., Singh, R., Ong, C. W., & Mills, I. G. (2018) · Nature Genetics · doi:10.1038/s41588-017-0037-0 · Cited by 44
Assante, G., Chandrasekaran, S., Ng, S., Tourna, A., Chung, C. H., Isse, K. A., Banks, J. L., Soffientini, U., Filippi, C., Dhawan, A. K., et al. (2022) · Genome Medicine · doi:10.1186/s13073-022-01071-5 · Cited by 43
Fan, S., Wang, W., Che, W., Xu, Y., Jin, C., Dong, L., & Xia, Q. (2025) · Metabolites · doi:10.3390/metabo15030201 · Cited by 43
Responses of the embryonic epigenome to maternal diabetes
Salbaum, J. M., & Kappen, C. (2012) · Birth Defects Research Part A Clinical and Molecular Teratology · doi:10.1002/bdra.23035 · Cited by 43
Physiological characterization of ATP-citrate lyase in Aspergillus niger
Chen, H., He, X., Geng, H., & Liu, H. (2014) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-014-1418-3 · Cited by 43
ACLY and ACC1 Regulate Hypoxia-Induced Apoptosis by Modulating ETV4 via α-ketoglutarate
Keenan, M. M., Liu, B., Tang, X., Wu, J., Cyr, D. D., Stevens, R. D., Ilkayeva, O., Huang, Z., Tollini, L. A., Murphy, S. K., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005599 · Cited by 43
Singh, K., Krug, L., Basu, A., Meyer, P., Treiber, N., Beken, S. V., Wlaschek, M., Kochanek, S., Bloch, W., Geiger, H., et al. (2017) · Stem Cells · doi:10.1002/stem.2629 · Cited by 44
Metabolic Signaling to Epigenetic Alterations in Cancer
Kim, J., & Yeom, Y. I. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2017.185 · Cited by 45
Molusky, M. M., Hsieh, J., Lee, S. X., Ramakrishnan, R., Tascau, L., Haeusler, R. A., Accili, D., & Tall, A. R. (2018) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.311212 · Cited by 45
Polarization of Human Macrophages by Interleukin-4 Does Not Require ATP-Citrate Lyase
Namgaladze, D., Zukunft, S., Schnütgen, F., Kurrle, N., Fleming, I., Fuhrmann, D. C., & Brüne, B. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02858 · Cited by 44
The role of epigenetics in hypothalamic energy balance control: implications for obesity
Obri, A., & Claret, M. (2019) · Cell Stress · doi:10.15698/cst2019.07.191 · Cited by 46
Huang, T., Ying, S.-H., Li, J.-Y., Chen, H., Zang, Y., Wang, W., Li, J. X., Xiong, J., & Hu, J. (2019) · Phytochemistry · doi:10.1016/j.phytochem.2019.112184 · Cited by 43
Acevedo, O. A., Berríos-Rojas, R. V., Rodríguez‐Guilarte, L., Lillo-Dapremont, B., & Kalergis, A. M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.745332 · Cited by 45
Zhao, X. L., & Karpac, J. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.10.003 · Cited by 45
Cancer metabolism and dietary interventions
Qian, L., Zhang, F., Yin, M., & Lei, Q. (2021) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2021.0461 · Cited by 40
Csanádi, Á., Kayser, C., Donauer, M., Gumpp, V., Aumann, K., Rawluk, J. K., Prasse, A., Hausen, A. Z., Wiesemann, S. D., Werner, M., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126357 · Cited by 44
Goretzki, A., Lin, Y., & Schülke, S. (2021) · Allergy · doi:10.1111/all.14843 · Cited by 42
Sowers, M. L., Tang, H. R., Singh, V. K., Khan, A., Mishra, A., Restrepo, B. I., Jagannath, C., & Zhang, K. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102418 · Cited by 45
Subcellular one carbon metabolism in cancer, aging and epigenetics
Bernasocchi, T., & Mostoslavsky, R. (2024) · Frontiers in Epigenetics and Epigenomics · doi:10.3389/freae.2024.1451971 · Cited by 44
Sanders, E. B., & Diehl, S. (2015) · Oncoscience · doi:10.18632/oncoscience.128 · Cited by 43
Chemical Biology Approaches for Investigating the Functions of Lysine Acetyltransferases
He, M., Han, Z. H., Liu, L., & Zheng, Y. G. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201704745 · Cited by 43
Ramaiyan, B., & Talahalli, R. R. (2018) · Lipids · doi:10.1002/lipd.12074 · Cited by 42
ATP‐citrate lyase is an epigenetic regulator to promote obesity‐related kidney injury
Chen, Y., Deb, D. K., Fu, X., Yi, B., Liang, Y., Du, J., He, L., & Li, Y. C. (2019) · The FASEB Journal · doi:10.1096/fj.201900213r · Cited by 43
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Haferkamp, S., Drexler, K., Federlin, M., Schlitt, H. J., Berneburg, M., Adamski, J., Gaumann, A. K. A., Geissler, E. K., Ganapathy, V., Parkinson, E. K., et al. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.602476 · Cited by 44
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Jiang, X., Deng, X., Wang, J., Mo, Y., Shi, L., Fang, W., Zhang, S., Gong, Z., He, Y., Xiong, F., et al. (2021) · Oncogene · doi:10.1038/s41388-021-02079-8 · Cited by 42
Li, R., Meng, M., Chen, Y., Pan, T., Li, Y., Deng, Y., Zhang, R., Tian, R., Xu, W., Zheng, X., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05932-8 · Cited by 41
Yu, Y., Zhao, F., Yue, Y., Zhao, Y. J., & Zhou, D. (2024) · Nature Plants · doi:10.1038/s41477-024-01623-0 · Cited by 42
Multifunctional Biocatalysts for Organic Synthesis
Thorpe, T. W., Marshall, J. R., & Turner, N. J. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c09542 · Cited by 41
Pan, J.-J., Xie, S., Zheng, X. M., Xu, J., Xu, H. Y., Yin, R.-Q., Luo, Y., Li, S., Chen, Z.-R., Chen, Y.-R., et al. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216903 · Cited by 42
Grobs, Y., Romanet, C., Lemay, S.-E. S., Bourgeois, A., Voisine, P., Théberge, C., Sauvaget, M., Breuils‐Bonnet, S., Martineau, S., Kabbout, R. E., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.ado7824 · Cited by 42
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Martín-Martín, N., Carracedo, A., & Torrano, V. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00119 · Cited by 43
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Harachi, M., Masui, K., Okamura, Y., Tsukui, R., Mischel, P. S., & Shibata, N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103267 · Cited by 43
Khoury, N., Xu, J., Stegelmann, S. D., Jackson, C. W., Koronowski, K. B., Dave, K. R., Young, J. I., & Pérez‐Pinzón, M. A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1380-6 · Cited by 41
Zhou, W., Niu, Y., Nie, Z., Kim, J., Xu, Y., Yan, C., & Cui, X. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118648 · Cited by 42
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Zhang, Z., Miao, J., & Wang, Y. (2022) · Reproduction · doi:10.1530/rep-21-0431 · Cited by 41
Hullinger, R., Li, M., Wang, J., Peng, Y., Dowell, J. A., Bomba-Warczak, E. K., Mitchell, H. A., Bürger, C., Chapman, E. R., Denu, J. M., et al. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151776 · Cited by 42
Deb, D. K., Chen, Y., Sun, J. H., Wang, Y., & Li, Y. C. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00029.2017 · Cited by 41
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Metadata
- Authors
- Wellen, K. E., Hatzivassiliou, G., Sachdeva, U. M., Bui, T. V., Cross, J. R., & Thompson, C. B.
- Affiliations
- University of Pennsylvania (US)
- Venue
- Science
- Published
- 2009-05-22
- Volume
- 324
- Issue
- 5930
- Pages
- 1076-1080
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2746744
- OpenAlex
- W2144575277
- Cited by
- 2,298
- References
- 32
- Citations by year
- 2026: 194 · 2025: 158 · 2024: 150 · 2023: 169 · 2022: 167 · 2021: 185 · 2020: 149 · 2019: 163 · 2018: 131 · 2017: 122 · 2016: 111 · 2015: 131 · 2014: 118 · 2013: 87 · 2012: 96
- FWCI
- 35.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (T32-HL07439-27, T32HL007439)
- National Cancer Institute (R01CA092660, R01CA105463)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- ATP citrate lyase, histone acetylation, histone acetyltransferase, chromatin modification, gene expression regulation, cellular metabolism, glucose metabolism, 3T3-L1 adipocytes, adipogenesis, colon cancer cells, growth factor signaling
- MeSH terms
- Acetyl Coenzyme A, Acetate-CoA Ligase, Acetylation, Animals, ATP Citrate (pro-S)-Lyase, Cell Differentiation, Cell Line, Cell Nucleus, Cytoplasm, Gene Expression Regulation, Glucose, Glycolysis, Histone Deacetylases, Histones, Humans, Interleukin-3, Transcription, Genetic, 3T3 Cells, Adipocytes, Citric Acid, RNA Interference, Intercellular Signaling Peptides and Proteins, Cell Line, Tumor, Cell Proliferation, Mice, Histone Deacetylase Inhibitors
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