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 601–700 of 1,007
When Metabolism and Epigenetics Converge
Sassone‐Corsi, P. (2013) · Science · doi:10.1126/science.1233423 · Cited by 83
Gut, P., Matilainen, S., Meyer, J. G., Pällijeff, P., Richard, J., Carroll, C. J., Euro, L., Jackson, C. B., Isohanni, P., Minassian, B. A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19743-4 · Cited by 83
Interactions between epigenetics and metabolism in cancers
Yun, J., Johnson, J. L., Hanigan, C. L., & Locasale, J. W. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00163 · Cited by 82
Structure and inhibition mechanism of the human citrate transporter NaCT
Sauer, D. B., Song, J., Wang, B., Hilton, J. K., Karpowich, N. K., Mindell, J. A., Rice, W. J., & Wang, D. (2021) · Nature · doi:10.1038/s41586-021-03230-x · Cited by 82
Pouikli, A., Parekh, S., Maleszewska, M., Nikopoulou, C., Baghdadi, M., Tripodi, I. J., Folz‐Donahue, K., Hinze, Y., Mesaros, A., Hoey, D. A., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00105-8 · Cited by 84
Pyrimidines maintain mitochondrial pyruvate oxidation to support de novo lipogenesis
Sahu, U., Villa, E., Reczek, C. R., Zhao, Z., O’Hara, B. P., Torno, M. D., Mishra, R., Shannon, W. D., Asara, J. M., Gao, P., et al. (2024) · Science · doi:10.1126/science.adh2771 · Cited by 82
Kebede, A. F., Schneider, R., & Daujat, S. (2014) · FEBS Journal · doi:10.1111/febs.13047 · Cited by 89
Maternal diabetes and oocyte quality
Wang, Q., & Moley, K. H. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.03.002 · Cited by 82
Apicomplexan Energy Metabolism: Carbon Source Promiscuity and the Quiescence Hyperbole
Jacot, D., Waller, R. F., Soldati‐Favre, D., MacPherson, D. A., & MacRae, J. I. (2015) · Trends in Parasitology · doi:10.1016/j.pt.2015.09.001 · Cited by 82
Gene-Diet Interactions in Type 2 Diabetes: The Chicken and Egg Debate
Ortega, Á., Berná, G., Rojas, A., Martín, F., & Soria, B. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061188 · Cited by 87
The paradox of metabolism in quiescent stem cells
Coller, H. A. (2019) · FEBS Letters · doi:10.1002/1873-3468.13608 · Cited by 82
Metabolic Reprogramming in Mitochondria of Myeloid Cells
Zuo, H., & Wan, Y. (2019) · Cells · doi:10.3390/cells9010005 · Cited by 83
The Interplay Between Exercise Metabolism, Epigenetics, and Skeletal Muscle Remodeling
Seaborne, R. A. E., & Sharples, A. P. (2020) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000227 · Cited by 84
Mitochondria signaling to the epigenome: A novel role for an old organelle
Santos, J. H. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.11.016 · Cited by 84
The GCN5: its biological functions and therapeutic potentials
Haque, M. E., Jakaria, M., Akther, M., Cho, D.-Y., Kim, I., & Choi, D. (2021) · Clinical Science · doi:10.1042/cs20200986 · Cited by 83
Michniewicz, F., Saletta, F., Rouaen, J. R. C., Hewavisenti, R., Mercatelli, D., Cirillo, G., Giorgi, F. M., Trahair, T. N., Ziegler, D. S., & Vittorio, O. (2021) · ChemMedChem · doi:10.1002/cmdc.202100172 · Cited by 81
Compartmentalization of Mammalian Pantothenate Kinases
Alfonso-Pecchio, A. R., Garcia, M. R., Leonardi, R., & Jackowski, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049509 · Cited by 81
Metabolic regulation of neurodifferentiation in the adult brain
Maffezzini, C., Calvo‐Garrido, J., Wredenberg, A., & Freyer, C. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03430-9 · Cited by 86
GCN5 acetyltransferase in cellular energetic and metabolic processes
Mutlu, B., & Puigserver, P. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194626 · Cited by 82
Park, S., Baek, I., Ryu, J. H., Chun, C. H., & Jin, E. (2022) · Nature Communications · doi:10.1038/s41467-021-27738-y · Cited by 81
The Logic Linking Protein Acetylation and Metabolism
Guarente, L. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.007 · Cited by 79
The Yeast AMPK Homolog SNF1 Regulates Acetyl Coenzyme A Homeostasis and Histone Acetylation
Zhang, M., Galdieri, L. C., & Vančura, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00198-13 · Cited by 79
Bae, S., Park, P. S. U., Lee, Y., Mun, S. H., Γιαννοπούλου, Ε., Fujii, T., Lee, K. P., Violante, S. N., Cross, J. R., & Park‐Min, K. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109264 · Cited by 81
Self-citationAcetate metabolism and aging: An emerging connection
Shimazu, T., Hirschey, M. D., Huang, J.-Y., Ho, L., & Verdin, E. M. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.05.001 · Cited by 80
Tang, S., Fang, Y., Huang, G., Xu, X., Padilla‐Banks, E., Fan, W., Xu, Q., Sanderson, S. M., Foley, J. F., Dowdy, S., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796708 · Cited by 81
Herr, D. J., Baarine, M., Aune, S. E., Li, X., Ball, L. E., Lemasters, J. J., Beeson, C., Chou, C. J., & Menick, D. R. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.12.004 · Cited by 78
Li, H., Song, J., He, Y., Liu, Y., Liu, Z., Sun, W., Hu, W., Lei, Q., Hu, X., Chen, Z., et al. (2022) · Advanced Science · doi:10.1002/advs.202105126 · Cited by 83
Activation of diverse signalling pathways by oncogenic PIK3CA mutations
Wu, X., Renuse, S., Sahasrabuddhe, N. A., Zahari, M. S., Chaerkady, R., Kim, M., Nirujogi, R. S., Mohseni, M., Kumar, P., Raju, R., et al. (2014) · Nature Communications · doi:10.1038/ncomms5961 · Cited by 80
Androgen-regulated metabolism and biosynthesis in prostate cancer
Barfeld, S. J., Itkonen, H. M., Urbanucci, A., & Mills, I. G. (2014) · Endocrine Related Cancer · doi:10.1530/erc-13-0515 · Cited by 78
Glucose stimulates cholesterol 7α-hydroxylase gene transcription in human hepatocytes
Li, T., Chanda, D., Zhang, Y., Choi, H., & Chiang, J. Y. L. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m002782 · Cited by 80
Energy metabolism in cancer cells: How to explain the Warburg and Crabtree effects?
Antone, P. D. (2012) · Medical Hypotheses · doi:10.1016/j.mehy.2012.06.002 · Cited by 81
Dietary Regulation of Histone Acetylases and Deacetylases for the Prevention of Metabolic Diseases
Pham, T. X., & Lee, J. (2012) · Nutrients · doi:10.3390/nu4121868 · Cited by 78
Changing the Selectivity of p300 by Acetyl-CoA Modulation of Histone Acetylation
Henry, R. A., Kuo, Y., Bhattacharjee, V., Yen, T. J., & Andrews, A. J. (2014) · ACS Chemical Biology · doi:10.1021/cb500726b · Cited by 78
ACSS2-mediated acetyl-CoA synthesis from acetate is necessary for human cytomegalovirus infection
Vysochan, A., Sengupta, A., Weljie, A. M., Alwine, J. C., & Yu, Y. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614268114 · Cited by 86
C57BL/6J mice as a polygenic developmental model of diet-induced obesity
Chu, D., Malinowska, E., Jura, M., & Kozak, L. P. (2017) · Physiological Reports · doi:10.14814/phy2.13093 · Cited by 78
Metabolic Switches Linked to Pluripotency and Embryonic Stem Cell Differentiation
Shyh‐Chang, N., & Daley, G. Q. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.02.011 · Cited by 77
Neto, H. A. P., Ausina, P., Gomez, L. S., Leandro, J. G. B., Zancan, P., & Sola‐Penna, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01478 · Cited by 81
Sirtuins in Metabolic and Epigenetic Regulation of Stem Cells
Fang, Y., Tang, S., & Li, X. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2018.12.002 · Cited by 79
Fernandez, S., Viola, J. M., Torres, A., Wallace, M., Trefely, S., Zhao, S., Affronti, H. C., Gengatharan, J. M., Guertin, D. A., Snyder, N. W., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.112 · Cited by 80
Self-citationChromatin as a key consumer in the metabolite economy
Diehl, K. L., & Muir, T. W. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0517-x · Cited by 82
Fatty Acid Synthesis Is Indispensable for Survival of Human Pluripotent Stem Cells
Tanosaki, S., Tohyama, S., Fujita, J., Someya, S., Hishiki, T., Matsuura, T., Nakanishi, H., Ohto‐Nakanishi, T., Akiyama, T., Morita, Y., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101535 · Cited by 78
Mitochondrial control of innate immune responses
Chen, S., Liao, Z., & Xu, P. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1166214 · Cited by 87
Citrate induces apoptotic cell death: a promising way to treat gastric carcinoma?
Lu, Y., Zhang, X., Zhang, H., Lan, J. X., Huang, G., Varin, E., Lincet, H., Poulain, L., & Icard, P. (2011) · PubMed · Cited by 77
Metabolic regulation of stem cell function
Burgess, R., Agathocleous, M., & Morrison, S. J. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12247 · Cited by 81
Liu, H., Marsafari, M., Deng, L., & Xu, P. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-09664-8 · Cited by 77
TIGAR promotes neural stem cell differentiation through acetyl-CoA-mediated histone acetylation
Zhou, W., Zhao, T., Du, J., Ji, G., Li, X., Ji, S., Tian, W., Wang, X., & Hao, A. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1434-3 · Cited by 80
NADPH levels affect cellular epigenetic state by inhibiting HDAC3–Ncor complex
Li, W., Kou, J., Qin, J., Li, L., Zhang, Z., Pan, Y., Xue, Y., & Du, W. (2021) · Nature Metabolism · doi:10.1038/s42255-020-00330-2 · Cited by 79
Cell cycle progression is regulated by intertwined redox oscillators
Moreira, J. D. V., Pérès, S., Steyaert, J., Bigan, E., Paulevé, L., Lévy, M., & Schwartz, L. H. (2015) · Theoretical Biology and Medical Modelling · doi:10.1186/s12976-015-0005-2 · Cited by 80
The Acetate/ACSS2 Switch Regulates HIF-2 Stress Signaling in the Tumor Cell Microenvironment
Chen, R., Xu, M., Nagati, J. S., Hogg, R. T., Das, A., Gerard, R. D., & Garcia, J. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116515 · Cited by 76
PPARγ maintains ERBB2-positive breast cancer stem cells
Wang, X., Sun, Y., Wong, J. A., & Conklin, D. S. (2013) · Oncogene · doi:10.1038/onc.2013.217 · Cited by 76
A Tale of Metabolites: The Cross-Talk between Chromatin and Energy Metabolism
Martínez-Pastor, B., Cosentino, C., & Mostoslavsky, R. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0059 · Cited by 76
The Regulatory Effects of Acetyl-CoA Distribution in the Healthy and Diseased Brain
Ronowska, A., Szutowicz, A., Bielarczyk, H., Gul‐Hinc, S., Klimaszewska‐Łata, J., Dyś, A., Zyśk, M., & Jankowska-Kulawy, A. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00169 · Cited by 76
Mitochondrial dynamics in cancer stem cells
Sessions, D. T., & Kashatus, D. F. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03773-2 · Cited by 75
Exploring the Role of ATP-Citrate Lyase in the Immune System
Dominguez, M., Brüne, B., & Namgaladze, D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.632526 · Cited by 79
Operation of a TCA cycle subnetwork in the mammalian nucleus
Kafkia, E., Andrés‐Pons, A., Ganter, K., Seiler, M., Smith, T. S., Andrejeva, A., Jouhten, P., Pereira, F. M., Franco, C., Kuroshchenkova, A., et al. (2022) · Science Advances · doi:10.1126/sciadv.abq5206 · Cited by 76
Emerging Roles of SIRT5 in Metabolism, Cancer, and SARS-CoV-2 Infection
Fabbrizi, E., Fiorentino, F., Carafa, V., Altucci, L., Mai, A., & Rotili, D. (2023) · Cells · doi:10.3390/cells12060852 · Cited by 77
Epigenetic Regulation of Chondrocyte Catabolism and Anabolism in Osteoarthritis
Kim, H., Kang, D., Cho, Y., & Kim, J. (2015) · Molecules and Cells · doi:10.14348/molcells.2015.0200 · Cited by 76
Epigenetics: deciphering how environmental factors may modify autoimmune type 1 diabetes
MacFarlane, A. J., Strom, A., & Scott, F. W. (2009) · Mammalian Genome · doi:10.1007/s00335-009-9213-6 · Cited by 78
Nutrition, metabolism, and epigenetics: pathways of circadian reprogramming
Sato, T., & Sassone‐Corsi, P. (2022) · EMBO Reports · doi:10.15252/embr.202152412 · Cited by 77
Epigenetic regulation of tumor immunity
Pang, L., Zhou, F., Liu, Y., Ali, H. A., Khan, F., Heimberger, A. B., & Chen, P. (2024) · Journal of Clinical Investigation · doi:10.1172/jci178540 · Cited by 75
A transient ischemic environment induces reversible compaction of chromatin
Kirmes, I., Szczurek, A., Prakash, K., Charapitsa, I., Heiser, C., Musheev, M. U., Schock, F., Fornalczyk, K., Ma, D., Birk, U. J., et al. (2015) · Genome biology · doi:10.1186/s13059-015-0802-2 · Cited by 73
Han, Q., Chen, C.-A., Yang, W. K., Liang, D., Lv, H., Lv, G., Zong, Q.-N., & Wang, H. (2020) · Hepatobiliary & pancreatic diseases international · doi:10.1016/j.hbpd.2020.05.010 · Cited by 73
Regulation of autophagy and mitophagy by nutrient availability and acetylation
Webster, B. R., Scott, I., Traba, J., Han, K., & Sack, M. N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.02.001 · Cited by 75
Early environmental factors, alteration of epigenetic marks and metabolic disease susceptibility
Portha, B., Fournier, A., Kioon, M. D. A., Mezger, V., & Movassat, J. (2013) · Biochimie · doi:10.1016/j.biochi.2013.10.003 · Cited by 79
Metabolic Mechanisms of Epigenetic Regulation
Meier, J. L. (2013) · ACS Chemical Biology · doi:10.1021/cb400689r · Cited by 75
Qu, J., Sun, W., Zhong, J., Lv, H., Zhu, M., Xu, J., Jin, N., Xie, Z., Tan, M., Lin, S., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201607008 · Cited by 74
CAB39L elicited an anti-Warburg effect via a LKB1-AMPK-PGC1α axis to inhibit gastric tumorigenesis
Li, W., Wong, C. C., Zhang, X., Kang, W., Nakatsu, G., Zhao, Q., Chen, H., Go, M. Y. Y., Chiu, P. W. Y., Wang, X., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0402-1 · Cited by 74
The adjustable nucleosome: an epigenetic signaling module
Turner, B. M. (2012) · Trends in Genetics · doi:10.1016/j.tig.2012.04.003 · Cited by 75
Shan, C., Lu, Z., Li, Z., Sheng, H., Fan, J., Qi, Q., Liu, S., & Zhang, S. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1756-1 · Cited by 72
Lei, I., Tian, S., Gao, W., Liu, L., Guo, Y., Tang, P., Chen, E., & Wang, Z. (2021) · eLife · doi:10.7554/elife.60311 · Cited by 72
Wang, Y., Yang, H., Geerts, C., Fürtös, A., Waters, P. J., Cyr, D., Wang, S., & Mitchell, G. A. (2022) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2022.106966 · Cited by 74
Sahar, S., Masubuchi, S., Eckel‐Mahan, K. L., Vollmer, S., Galla, L., Ceglia, N., Masri, S., Barth, T. K., Grimaldi, B., Oluyemi, O. I., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.537191 · Cited by 74
The biology of lysine acetylation integrates transcriptional programming and metabolism
Patel, J. A., Pathak, R. R., & Mujtaba, S. (2011) · Nutrition & Metabolism · doi:10.1186/1743-7075-8-12 · Cited by 76
Qian, X., Hu, J., Zhao, J., & Chen, H. (2015) · Europe PMC (PubMed Central) · Cited by 72
Peruzzotti‐Jametti, L., & Pluchino, S. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.07.007 · Cited by 75
Interactions between metabolism and chromatin in plant models
Lindermayr, C., Rudolf, E. E., Durner, J., & Groth, M. Z. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.01.015 · Cited by 72
Reynolds, J. A., Bautista-Jimenez, R., & Denlinger, D. L. (2016) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2016.06.012 · Cited by 71
Zhou, L., He, B., Deng, J., Pang, S., & Tang, H. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008122 · Cited by 73
Chromatin dynamics and histone modifications in intestinal microbiota-host crosstalk
Fellows, R., & Varga‐Weisz, P. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.12.005 · Cited by 77
Metabolic acetate therapy improves phenotype in the tremor rat model of Canavan disease
Arun, P., Madhavarao, C. N., Moffett, J. R., Hamilton, K. R., Grunberg, N. E., Ariyannur, P. S., Gahl, W. A., Anikster, Y., Mog, S. R., Hallows, W. C., et al. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9100-z · Cited by 71
Das, S. K., Morvan, F., Morozzi, G., Jourde, B., Minetti, G., Kahle, P., Rivet, H., Brebbia, P., Toussaint, G., Glass, D. J., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.038 · Cited by 71
The contributions of cancer cell metabolism to metastasis
Pascual, G., Domínguez, D., & Benitah, S. A. (2018) · Disease Models & Mechanisms · doi:10.1242/dmm.032920 · Cited by 74
Mechanisms of the Metabolic Shift during Somatic Cell Reprogramming
Nishimura, K., Fukuda, A., & Hisatake, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092254 · Cited by 71
Lee, W. D., Mukha, D., Aizenshtein, E., & Shlomi, T. (2019) · Nature Communications · doi:10.1038/s41467-019-09352-1 · Cited by 70
Johswich, A., Longuet, C., Pawling, J., Rahman, A. M. A., Ryczko, M. C., Drucker, D. J., & Dennis, J. W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563734 · Cited by 71
Posttranslational regulation of PGC‐1α and its implication in cancer metabolism
Luo, X., Liao, C., Quan, J., Cheng, C., Zhao, X., Bode, A. M., & Cao, Y. (2019) · International Journal of Cancer · doi:10.1002/ijc.32253 · Cited by 75
Han, J. H., Kim, Y. K., Kim, H., Lee, J., Oh, M. J., Kim, M., Kim, K. H., Kim, K. H., Yoon, H. J., Lee, M., et al. (2022) · 癌症：英文版 · doi:10.1002/cac2.12332 · Cited by 73
The biochemistry and physiology of long-chain dicarboxylic acid metabolism
Ranea‐Robles, P., & Houten, S. M. (2023) · Biochemical Journal · doi:10.1042/bcj20230041 · Cited by 77
Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells
Cheng, Z., Huang, H., Li, M., & Chen, Y. (2023) · iScience · doi:10.1016/j.isci.2023.108645 · Cited by 70
Epigenomic regulation of host–microbiota interactions
Alenghat, T., & Artis, D. (2014) · Trends in Immunology · doi:10.1016/j.it.2014.09.007 · Cited by 72
Schwartz, S. (2010) · Oncology Reports · doi:10.3892/or_00000778 · Cited by 71
Chemical signaling between gut microbiota and host chromatin: What is your gut really saying?
Krautkramer, K. A., Rey, F. E., & Denu, J. M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.761577 · Cited by 70
Lysine Deacetylases and Regulated Glycolysis in Macrophages
Shakespear, M. R., Iyer, A., Cheng, C. Y., Gupta, K. D., Singhal, A., Fairlie, D. P., & Sweet, M. J. (2018) · Trends in Immunology · doi:10.1016/j.it.2018.02.009 · Cited by 70
Imaging Cancer Metabolism: Underlying Biology and Emerging Strategies
Pantel, A. R., Ackerman, D., Lee, S., Mankoff, D. A., & Gade, T. P. F. (2018) · Journal of Nuclear Medicine · doi:10.2967/jnumed.117.199869 · Cited by 70
Navarro, E., Funtikova, A. N., Fitó, M., & Schröder, H. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.03.012 · Cited by 72
Porta, C., Sica, A., & Riboldi, E. (2017) · FEBS Journal · doi:10.1111/febs.14288 · Cited by 70
Circadian rhythms affect bone reconstruction by regulating bone energy metabolism
Luo, B., Zhou, X., Tang, Q., Yin, Y., Feng, G., Li, S., & Chen, L. (2021) · Journal of Translational Medicine · doi:10.1186/s12967-021-03068-x · Cited by 72
Ewald, J. C., Reich, S., Baumann, S., Frommer, W. B., & Zamboni, N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028245 · Cited by 69
Shao, J., Xu, D., Hu, L., Kwan, Y. W., Wang, Y., Kong, X., & Ngai, S. M. (2012) · Molecular BioSystems · doi:10.1039/c2mb25251a · Cited by 69
Tricarboxylates Induce Defense Priming Against Bacteria in Arabidopsis thaliana
Balmer, A., Pastor, V., Glauser, G., & Mauch‐Mani, B. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.01221 · Cited by 69
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
