The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 1,007
ATP-citrate lyase is essential for macrophage inflammatory response
Infantino, V., Iacobazzi, V., Palmieri, F., & Menga, A. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.09.037 · Cited by 274
Regulation of Stem Cell Aging by Metabolism and Epigenetics
Ren, R., Ocampo, A., Liu, G., & Belmonte, J. C. I. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.07.019 · Cited by 286
Tissue-specific metabolic reprogramming drives nutrient flux in diabetic complications
Sas, K. M., Kayampilly, P., Byun, J., Nair, V., Hinder, L. M., Hur, J., Zhang, H., Lin, C., Qi, N. R., Michailidis, G., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.86976 · Cited by 268
Sakr, S., Wang, M., Dédaldéchamp, F., Pérez-Garcia, M.-D., Ogé, L., Hamama, L., & Atanassova, R. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092506 · Cited by 273
Mitochondria, Energetics, Epigenetics, and Cellular Responses to Stress
Shaughnessy, D. T., McAllister, K. A., Worth, L., Haugen, A. C., Meyer, J. N., Domann, F. E., Houten, B. V., Mostoslavsky, R., Bultman, S. J., Baccarelli, A., et al. (2014) · Environmental Health Perspectives · doi:10.1289/ehp.1408418 · Cited by 272
A Metabolic Basis for Endothelial-to-Mesenchymal Transition
Xiong, J., Kawagishi, H., Yan, Y., Liu, J., Wells, Q. S., Edmunds, L. R., Fergusson, M. M., Yu, Z., Rovira, I. I., Brittain, E. L., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.010 · Cited by 266
Caloric restriction mimetics: towards a molecular definition
Madeo, F., Pietrocola, F., Eisenberg, T., & Kroemer, G. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4391 · Cited by 245
Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology
Kumar, S., & Lombard, D. B. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1458071 · Cited by 273
Reprogramming of basic metabolic pathways in microbial sepsis: therapeutic targets at last?
Wyngene, L. V., Vandewalle, J., & Libert, C. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708712 · Cited by 269
Ritterhoff, J., & Tian, R. (2023) · Nature Reviews Cardiology · doi:10.1038/s41569-023-00887-x · Cited by 265
Proteins of Diverse Function and Subcellular Location Are Lysine Acetylated in Arabidopsis
Finkemeier, I., Laxa, M., Miguet, L., Howden, A. J. M., & Sweetlove, L. J. (2011) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.171595 · Cited by 267
Interplay between epigenetics and metabolism in oncogenesis: mechanisms and therapeutic approaches
Wong, C. C., Qian, Y., & Yu, J. Q. (2017) · Oncogene · doi:10.1038/onc.2016.485 · Cited by 266
Eisenberg, T., Schroeder, S., Andryushkova, A., Pendl, T., Küttner, V., Bhukel, A., Mariño, G., Pietrocola, F., Harger, A., Zimmermann, A., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.02.010 · Cited by 256
Cellular metabolism regulates the differentiation and function of T-cell subsets
Ma, S., Ming, Y., Wu, J., & Cui, G. (2024) · Cellular and Molecular Immunology · doi:10.1038/s41423-024-01148-8 · Cited by 276
Li, L., & Li, W. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.01.004 · Cited by 257
Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism
Gomes, P., Outeiro, T. F., & Cavadas, C. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.001 · Cited by 259
Xu, D., Shao, F., Bian, X., Meng, Y., Liang, T., & Lu, Z. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2020.12.015 · Cited by 257
Targeting T cell metabolism for therapy
O’Sullivan, D., & Pearce, E. L. (2015) · Trends in Immunology · doi:10.1016/j.it.2014.12.004 · Cited by 261
Mitochondria: Their relevance during oocyte ageing
van der Reest, J., Cecchino, G. N., Haigis, M. C., & Kordowitzki, P. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101378 · Cited by 258
ATP-citrate lyase: A mini-review
Chypre, M., Zaidi, N., & Smans, K. A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.144 · Cited by 257
Granchi, C. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.09.001 · Cited by 251
Metabolic Regulation of the Immune Humoral Response
Boothby, M. R., & Rickert, R. C. (2017) · Immunity · doi:10.1016/j.immuni.2017.04.009 · Cited by 252
The carnitine system and cancer metabolic plasticity
Melone, M. A. B., Valentino, A., Margarucci, S., Galderisi, U., Giordano, A., & Peluso, G. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0313-7 · Cited by 260
Tricarboxylic Acid (TCA) Cycle Intermediates: Regulators of Immune Responses
Choi, I., Son, H., & Baek, J.-H. (2021) · Life · doi:10.3390/life11010069 · Cited by 262
Li, C., Zhu, B., Son, Y. M., Wang, Z., Jiang, L., Xiang, M., Ye, Z., Beckermann, K. E., Wu, Y., Jenkins, J. W., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.08.013 · Cited by 251
Hochrein, S. M., Wu, H., Eckstein, M., Arrigoni, L., Herman, J. S., Schumacher, F., Gerecke, C., Rosenfeldt, M. T., Grün, D., Kleuser, B., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.02.015 · Cited by 253
Liu, P.-S., Chen, Y.-T., Li, X., Hsueh, P., Tzeng, S., Chen, H., Shi, P.-Z., Xie, X., Parik, S., Planque, M., et al. (2023) · Nature Immunology · doi:10.1038/s41590-023-01430-3 · Cited by 243
Pleiotropic effects of mitochondria in aging
de Lima, T. I., Li, T. Y., Mottis, A., & Auwerx, J. H. (2022) · Nature Aging · doi:10.1038/s43587-022-00191-2 · Cited by 254
Berghe, W. V. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.03.007 · Cited by 245
Cancer metabolism: Key players in metabolic reprogramming
Soga, T. (2012) · Cancer Science · doi:10.1111/cas.12085 · Cited by 247
Pinkosky, S. L., Filippov, S. I., Srivastava, R. A. K., Hanselman, J. C., Bradshaw, C. D., Hurley, T. R., Cramer, C. T., Spahr, M. A., Brant, A. F., Houghton, J. L., et al. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m030528 · Cited by 241
Metabolism in physiological cell proliferation and differentiation
Agathocleous, M., & Harris, W. A. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.05.004 · Cited by 245
ATP citrate lyase: A central metabolic enzyme in cancer
Icard, P., Wu, Z., Fournel, L., Coquerel, A., Lincet, H., & Alifano, M. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.12.010 · Cited by 247
Mechanistic insights into the regulation of metabolic enzymes by acetylation
Xiong, Y., & Guan, K. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201202056 · Cited by 243
Targeting epigenetic mechanisms in diabetic wound healing
den Dekker, A. D., Davis, F. M., Kunkel, S. L., & Gallagher, K. A. (2018) · Translational research · doi:10.1016/j.trsl.2018.10.001 · Cited by 246
Heterogeneity in Cancer Metabolism: New Concepts in an Old Field
Gentric, G., Mieulet, V., & Mechta‐Grigoriou, F. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6750 · Cited by 248
Metabolic regulation of chromatin modifications and gene expression
Schvartzman, J. M., Thompson, C. B., & Finley, L. W. S. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201803061 · Cited by 233
Self-citationDistinct modes of mitochondrial metabolism uncouple T cell differentiation and function
Bailis, W., Shyer, J. A., Zhao, J., García‐Cañaveras, J. C., Khazal, F. J. A., Qu, R., Steach, H. R., Bielecki, P., Khan, O. M., Jackson, R. P., et al. (2019) · Nature · doi:10.1038/s41586-019-1311-3 · Cited by 243
ATP-citrate lyase (ACLY) in lipid metabolism and atherosclerosis: An updated review
Feng, X., Zhang, L., Xu, S., & Shen, A.-Z. (2019) · Progress in Lipid Research · doi:10.1016/j.plipres.2019.101006 · Cited by 242
Metabolic regulation of transcription through compartmentalized NAD + biosynthesis
Ryu, K. W., Nandu, T. S., Kim, J., Challa, S., DeBerardinis, R. J., & Kraus, W. L. (2018) · Science · doi:10.1126/science.aan5780 · Cited by 235
VDAC1 at the Intersection of Cell Metabolism, Apoptosis, and Diseases
Shoshan‐Barmatz, V., Shteinfer‐Kuzmine, A., & Verma, A. (2020) · Biomolecules · doi:10.3390/biom10111485 · Cited by 246
Grasso, D., Zampieri, L. X., Capelôa, T., de Velde, J. A. V., & Sonveaux, P. (2020) · Cell Stress · doi:10.15698/cst2020.06.221 · Cited by 239
Acetate Metabolism in Physiology, Cancer, and Beyond
Bose, S., Ramesh, V., & Locasale, J. W. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.05.005 · Cited by 236
Crossing epigenetic frontiers: the intersection of novel histone modifications and diseases
Yao, W., Hu, X., & Wang, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01918-w · Cited by 257
Barnes, C. E., English, D. M., & Cowley, S. M. (2019) · Essays in Biochemistry · doi:10.1042/ebc20180061 · Cited by 249
Acetyl-CoA Carboxylase Regulates Global Histone Acetylation
Galdieri, L. C., & Vančura, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380519 · Cited by 232
Lysine benzoylation is a histone mark regulated by SIRT2
Huang, H., Zhang, D., Wang, Y., Perez‐Neut, M., Han, Z. H., Zheng, Y. G., Hao, Q., & Zhao, Y. (2018) · Nature Communications · doi:10.1038/s41467-018-05567-w · Cited by 229
Saunier, E. F., Benelli, C., & Bortoli, S. (2015) · International Journal of Cancer · doi:10.1002/ijc.29564 · Cited by 217
Immunometabolic circuits in trained immunity
Arts, R. J. W., Joosten, L. A. B., & Netea, M. G. (2016) · Seminars in Immunology · doi:10.1016/j.smim.2016.09.002 · Cited by 228
Trained immunity: adaptation within innate immune mechanisms
Domínguez‐Andrés, J., dos Santos, J. C., Bekkering, S., Mulder, W. J. M., van der Meer, J. W. M., Riksen, N. P., Joosten, L. A. B., & Netea, M. G. (2022) · Physiological Reviews · doi:10.1152/physrev.00031.2021 · Cited by 227
The engine driving the ship: metabolic steering of cell proliferation and death
Buchakjian, M. R., & Kornbluth, S. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2972 · Cited by 228
Chen, T., Xu, Z., Luo, J., Manne, R., Wang, Z., Hsu, C.-C., Pan, B., Cai, Z., Tsai, P., Tsai, Y.-S., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.07.009 · Cited by 223
Undercover: gene control by metabolites and metabolic enzymesPreprint
van der Knaap, J. A., & Verrijzer, C. P. (2016) · Genes & Development · doi:10.1101/gad.289140.116 · Cited by 222
Birkenfeld, A. L., Lee, H., Guebre‐Egziabher, F., Alves, T. C., Jurczak, M. J., Jornayvaz, F. R., Zhang, D., Hsiao, J. J., Martín‐Montalvo, A., Fischer‐Rosinsky, A., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.06.009 · Cited by 217
Pluripotent stem cell energy metabolism: an update
TeSlaa, T. A., & Teitell, M. A. (2014) · The EMBO Journal · doi:10.15252/embj.201490446 · Cited by 221
Metabolic Pathways Involved in Regulatory T Cell Functionality
Kempkes, R. W. M., Joosten, I., Koenen, H. J. P. M., & He, X. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02839 · Cited by 220
Glucose and Insulin Induction of Bile Acid Synthesis
Li, T., Ferrell, J. M., Boehme, S., Ochoa, A., Zhang, Y., Klaassen, C. D., Erickson, S. K., & Chiang, J. Y. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.305789 · Cited by 219
MYST-family histone acetyltransferases: beyond chromatin
Sapountzi, V., & Côté, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0599-9 · Cited by 220
Energy Metabolism Regulates Stem Cell Pluripotency
Tsogtbaatar, E., Landin, C., Minter‐Dykhouse, K., & Folmes, C. D. L. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00087 · Cited by 213
Ge, T., Gu, X., Jia, R., Ge, S., Chai, P., Zhuang, A., & Fan, X. (2022) · 癌症：英文版 · doi:10.1002/cac2.12374 · Cited by 220
Metabolic Regulation of Protein N-Alpha-Acetylation by Bcl-xL Promotes Cell Survival
Yi, C. H., Pan, H., Seebacher, J., Jang, I. H., Hyberts, S. G., Heffron, G. J., Heiden, M. G. V., Yang, R., Li, F., Locasale, J. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.050 · Cited by 212
Myc Regulates Chromatin Decompaction and Nuclear Architecture during B Cell Activation
Kieffer-Kwon, K.-R., Nimura, K., Rao, S. S. P., Xu, J., Jung, S., Pękowska, A., Dose, M., Stevens, E., Mathé, E. A., Dong, P., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.013 · Cited by 210
Sirtuins, Aging, and MetabolismPreprint
Guarente, L. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010629 · Cited by 213
Snail1 is stabilized by O‐GlcNAc modification in hyperglycaemic condition
Park, S., Kim, H. S., Kim, N. H., Ji, S., Cha, S. Y., Kang, J. G., Ota, I., Shimada, K., Konishi, N., Nam, H. W., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.254 · Cited by 210
D-beta-hydroxybutyrate extends lifespan in C. elegans
Edwards, C., Canfield, J., Copes, N., Rehan, M., Lipps, D., & Bradshaw, P. C. (2014) · Aging · doi:10.18632/aging.100683 · Cited by 209
Histone propionylation is a mark of active chromatin
Kebede, A. F., Nieborak, A., Shahidian, L. Z., Gras, S. L., Richter, F. M., Aguilar‐Gómez, D., Baltissen, M. P. A., Mészáros, G., Magliarelli, H. D. F., Taudt, A., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3490 · Cited by 215
Sutendra, G., Dromparis, P., Paulin, R., Zervopoulos, S. D., Haromy, A., Nagendran, J., & Michelakis, E. D. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1059-4 · Cited by 209
Wang, T., Zeng, Y., Li, Z., Jing, D., Fan, G., Liu, M., Zhuo, Q., Ji, S., Yu, X., Xu, X., et al. (2023) · Cell Proliferation · doi:10.1111/cpr.13478 · Cited by 217
Ketogenesis prevents diet-induced fatty liver injury and hyperglycemia
Cotter, D. G., Erçal, B., Huang, X., Leid, J. M., d’Avignon, D. A., Graham, M. J., Dietzen, D. J., Brunt, E. M., Patti, G. J., & Crawford, P. A. (2014) · Journal of Clinical Investigation · doi:10.1172/jci76388 · Cited by 211
Chen, J., Guccini, I., Mitri, D. D., Brina, D., Revandkar, A., Sarti, M., Pasquini, E., Alajati, A., Pinton, S., Losa, M., et al. (2018) · Nature Genetics · doi:10.1038/s41588-017-0026-3 · Cited by 202
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle
Verschueren, K. H. G., Blanchet, C. E., Félix, J., Dansercoer, A., Vos, D. E. D., Bloch, Y., BEEUMEN, J. V., Svergun, D. I., Gutsche, I., Savvides, S. N., et al. (2019) · Nature · doi:10.1038/s41586-019-1095-5 · Cited by 205
Brain glucose sensing and neural regulation of insulin and glucagon secretion
Thorens, B. (2011) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2011.01453.x · Cited by 198
Sugar-free approaches to cancer cell killing
Mjiyad, N. E., Caro‐Maldonado, A., Ramírez‐Peinado, S., & Muñoz‐Pinedo, C. (2010) · Oncogene · doi:10.1038/onc.2010.466 · Cited by 198
Gouw, A. M., Margulis, K., Liu, N. S., Raman, S. J., Mancuso, A., Toal, G. G., Tong, L., Mosley, A. R., Hsieh, A. L., Sullivan, D. K., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.07.012 · Cited by 195
Roze, L. V., Chanda, A., & Linz, J. E. (2010) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2010.05.006 · Cited by 194
Moonlighting functions of metabolic enzymes and metabolites in cancer
Pan, C., Li, B., & Simon, M. C. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.031 · Cited by 198
vel Szic, K. S., Declerck, K., Vidaković, M., & Vanden Berghe, W. (2015) · Clinical Epigenetics · doi:10.1186/s13148-015-0068-2 · Cited by 192
Yu, Y., Clippinger, A. J., & Alwine, J. C. (2011) · Trends in Microbiology · doi:10.1016/j.tim.2011.04.002 · Cited by 199
Janke, R., Dodson, A. E., & Rine, J. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100814-125544 · Cited by 199
A key role of the mitochondrial citrate carrier (SLC25A1) in TNFα- and IFNγ-triggered inflammation
Infantino, V., Iacobazzi, V., Menga, A., Avantaggiati, M. L., & Palmieri, F. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.07.013 · Cited by 191
Jeninga, E. H., Schoonjans, K., & Auwerx, J. H. (2010) · Oncogene · doi:10.1038/onc.2010.206 · Cited by 197
Bantug, G. R., Fischer, M., Grählert, J., Balmer, M. L., Unterstab, G., Develioglu, L., Steiner, R., Zhang, L., Costa, A. S. H., Gubser, P. M., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.02.012 · Cited by 196
Metabolic Stress in Autophagy and Cell Death PathwaysPreprint
Altman, B. J., & Rathmell, J. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008763 · Cited by 204
HDAC inhibitor–dependent transcriptome and memory reinstatement in cognitive decline models
Benito, E., Urbanke, H., Ramachandran, B., Barth, J., Halder, R., Awasthi, A., Jain, G., Capece, V., Burkhardt, S., Navarro-Sala, M., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci79942 · Cited by 197
Mitochondria and the dynamic control of stem cell homeostasis
Lisowski, P., Kannan, P., Mlody, B., & Prigione, A. (2018) · EMBO Reports · doi:10.15252/embr.201745432 · Cited by 191
Short‐chain fatty acids: Bacterial messengers modulating the immunometabolism of T cells
Luu, M., & Visekruna, A. (2019) · European Journal of Immunology · doi:10.1002/eji.201848009 · Cited by 187
Methionine adenosyltransferase II serves as a transcriptional corepressor of Maf oncoprotein
Katoh, Y., Ikura, T., Hoshikawa, Y., Tashiro, S., Ito, T., Ohta, M., Kera, Y., Noda, T., & Igarashi, K. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.018 · Cited by 185
Mitochondrially derived peptides as novel regulators of metabolism
Kim, S., Xiao, J., Wan, J., Cohen, P., & Yen, K. (2017) · The Journal of Physiology · doi:10.1113/jp274472 · Cited by 185
An allosteric mechanism for potent inhibition of human ATP-citrate lyase
Jia, W., Leit, S. M., Kuai, J., Therrien, É., Rafi, S. B., Harwood, H. J., DeLaBarre, B., & Tong, L. (2019) · Nature · doi:10.1038/s41586-019-1094-6 · Cited by 186
Metabolites Regulate Cell Signaling and Growth via Covalent Modification of Proteins
Figlia, G., Willnow, P., & Teleman, A. A. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.036 · Cited by 185
Acetyl-CoA Metabolism and Histone Acetylation in the Regulation of Aging and Lifespan
Bradshaw, P. C. (2021) · Antioxidants · doi:10.3390/antiox10040572 · Cited by 189
Moffett, J. R., Arun, P., Ariyannur, P. S., & Namboodiri, A. M. A. (2013) · Frontiers in Neuroenergetics · doi:10.3389/fnene.2013.00011 · Cited by 183
Aberrant lipid metabolism as a therapeutic target in liver cancer
Pope, E. D., Kimbrough, E. O., Vemireddy, L. P., Surapaneni, P. K., Copland, J. A., & Mody, K. (2019) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1615883 · Cited by 186
Up-regulation of glycolytic metabolism is required for HIF1α-driven bone formation
Regan, J. N., Lim, J., Shi, Y., Joeng, K. S., Arbeit, J. M., Shohet, R. V., & Long, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324290111 · Cited by 184
Metabolic Signaling to the Nucleus in Cancer
Campbell, S. L., & Wellen, K. E. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.015 · Cited by 186
Self-citationMoffett, J. R., Puthillathu, N., Vengilote, R., Jaworski, D. M., & Namboodiri, A. M. A. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.580167 · Cited by 190
The role and mechanism of histone lactylation in health and diseases
Xie, Y., Hu, H., Liu, M., Zhou, T., Cheng, X., Huang, W. G., & Cao, L. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.949252 · Cited by 189
Epigenetic mechanisms of major depression: Targeting neuronal plasticity
Uchida, S., Yamagata, H., Seki, T., & Watanabe, Y. (2018) · Psychiatry and Clinical Neurosciences · doi:10.1111/pcn.12621 · Cited by 181
Krüger, A., Grüning, N., Wamelink, M. M. C., Kerick, M., Kirpy, A., Parkhomchuk, D., Bluemlein, K., Schweiger, M. R., Soldatov, A. V., Lehrach, H. R., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3797 · Cited by 181
Shi, W., Cassmann, T. J., Bhagwate, A. V., Hitosugi, T., & Ip, W. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113746 · Cited by 186
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
