Compartmentalised acyl-CoA metabolism and roles in chromatin regulation
Open accessAbstract
BACKGROUND: Many metabolites serve as important signalling molecules to adjust cellular activities and functions based on nutrient availability. Links between acetyl-CoA metabolism, histone lysine acetylation, and gene expression have been documented and studied over the past decade. In recent years, several additional acyl modifications to histone lysine residues have been identified, which depend on acyl-coenzyme A thioesters (acyl-CoAs) as acyl donors. Acyl-CoAs are intermediates of multiple distinct metabolic pathways, and substantial evidence has emerged that histone acylation is metabolically sensitive. Nevertheless, the metabolic sources of acyl-CoAs used for chromatin modification in most cases remain poorly understood. Elucidating how these diverse chemical modifications are coupled to and regulated by cellular metabolism is important in deciphering their functional significance. SCOPE OF REVIEW: In this article, we review the metabolic pathways that produce acyl-CoAs, as well as emerging evidence for functional roles of diverse acyl-CoAs in chromatin regulation. Because acetyl-CoA has been extensively reviewed elsewhere, we will focus on four other acyl-CoA metabolites integral to major metabolic pathways that are also known to modify histones: succinyl-CoA, propionyl-CoA, crotonoyl-CoA, and butyryl-CoA. We also briefly mention several other acyl-CoA species, which present opportunities for further research; malonyl-CoA, glutaryl-CoA, 3-hydroxybutyryl-CoA, 2-hydroxyisobutyryl-CoA, and lactyl-CoA. Each acyl-CoA species has distinct roles in metabolism, indicating the potential to report shifts in the metabolic status of the cell. For each metabolite, we consider the metabolic pathways in which it participates and the nutrient sources from which it is derived, the compartmentalisation of its metabolism, and the factors reported to influence its abundance and potential nuclear availability. We also highlight reported biological functions of these metabolically-linked acylation marks. Finally, we aim to illuminate key questions in acyl-CoA metabolism as they relate to the control of chromatin modification. MAJOR CONCLUSIONS: A majority of acyl-CoA species are annotated to mitochondrial metabolic processes. Since acyl-CoAs are not known to be directly transported across mitochondrial membranes, they must be synthesized outside of mitochondria and potentially within the nucleus to participate in chromatin regulation. Thus, subcellular metabolic compartmentalisation likely plays a key role in the regulation of histone acylation. Metabolite tracing in combination with targeting of relevant enzymes and transporters will help to map the metabolic pathways that connect acyl-CoA metabolism to chromatin modification. The specific function of each acyl-CoA may be determined in part by biochemical properties that affect its propensity for enzymatic versus non-enzymatic protein modification, as well as the various enzymes that can add, remove and bind each modification. Further, competitive and inhibitory effects of different acyl-CoA species on these enzymes make determining the relative abundance of acyl-CoA species in specific contexts important to understand the regulation of chromatin acylation. An improved and more nuanced understanding of metabolic regulation of chromatin and its roles in physiological and disease-related processes will emerge as these questions are answered.
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
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?
An emerging body of literature provides evidence for the presence of anaplerotic enzymes outside of the mitochondria, including SCS.
“an emerging body of literature provides evidence for the presence of anaplerotic enzymes outside of the mitochondria, including SCS.44,45”
From Loss of succinyl-CoA synthetase in mouse forebrain results in hypersuccinylation with perturbed neuronal transcription and metabolism (2023) · cites this paper as [44]
The Succinyl-CoA generation section (page unavailable) reports nuclear localization of the OGDH complex and discusses possible cytosolic succinyl-CoA production. But it describes succinyl-CoA synthase (SCS, termed SUCL in the paper) as acting in the mitochondrial TCA cycle; it does not provide evidence that SCS is present outside mitochondria. (LLM, conf=0.88)
Experimental — accuracy not yet measuredBy co-opting the production and localization of select TCA cycle metabolites, cells can modulate the activity of chromatin-modifying enzymes and exert control over gene expression and cell fate.
“By co-opting the production and localization of select TCA cycle metabolites, cells can modulate the activity of chromatin-modifying enzymes and exert control over gene expression and cell fate (158, 159, 160).”
From Regulation and function of the mammalian tricarboxylic acid cycle (2023) · cites this paper as [160]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
From Dietary Fiber to Host Physiology: Short-Chain Fatty Acids as Key Bacterial Metabolites
Koh, A., De Vadder, F., Kovatcheva-Datchary, P., & Bäckhed, F. (2016) · Cell · doi:10.1016/j.cell.2016.05.041 · Cited by 7,070 · see citing works
den Besten, G., van Eunen, K., Groen, A. K., Venema, K., Reijngoud, D.-J., & Bakker, B. M. (2013) · Journal of Lipid Research · doi:10.1194/jlr.r036012 · Cited by 5,048 · see citing works
Metabolic regulation of gene expression by histone lactylation
Zhang, D., Tang, Z., Huang, H., Zhou, G., Cui, C., Weng, Y., Liu, W., Kim, S., Lee, S., Perez-Neut, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1678-1 · Cited by 4,371 · see citing works
Parada Venegas, D., De la Fuente, M. K., Landskron, G., González, M. J., Quera, R., Dijkstra, G., Harmsen, H. J. M., Faber, K. N., & Hermoso, M. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00277 · Cited by 3,820 · see citing works
A guide to immunometabolism for immunologists
O'Neill, L. A. J., Kishton, R. J., & Rathmell, J. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.70 · Cited by 3,315 · see citing works
Short chain fatty acids in human large intestine, portal, hepatic and venous blood
Cummings, J. H., Pomare, E. W., Branch, W. J., Naylor, C. P., & Macfarlane, G. T. (1987) · Gut · doi:10.1136/gut.28.10.1221 · Cited by 3,119 · see citing works
Understanding the Intersections between Metabolism and Cancer Biology
Heiden, M. G. V., & DeBerardinis, R. J. (2017) · Cell · doi:10.1016/j.cell.2016.12.039 · Cited by 2,316 · see citing works
ATP-citrate lyase links cellular metabolism to histone acetylation
Wellen, K. E., Hatzivassiliou, G., Sachdeva, U. M., Bui, T. V., Cross, J. R., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1164097 · Cited by 2,298 · see citing works
Self-citationTan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902 · see citing works
Glucose feeds the TCA cycle via circulating lactate
Hui, S., Ghergurovich, J. M., Morscher, R. J., Jang, C., Teng, X., Lu, W., Esparza, L. A., Reya, T., Zhan, L., Yanxiang Guo, J., et al. (2017) · Nature · doi:10.1038/nature24057 · Cited by 1,721 · see citing works
Multi-dimensional Roles of Ketone Bodies in Fuel Metabolism, Signaling, and Therapeutics
Puchalska, P., & Crawford, P. A. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.12.022 · Cited by 1,617 · see citing works
Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429 · see citing works
Chambers, E. S., Viardot, A., Psichas, A., Morrison, D. J., Murphy, K. G., Zac-Varghese, S. E. K., MacDougall, K., Preston, T., Tedford, C., Finlayson, G. S., et al. (2015) · Gut · doi:10.1136/gutjnl-2014-307913 · Cited by 1,424 · see citing works
Acetyl Coenzyme A: A Central Metabolite and Second Messenger
Pietrocola, F., Galluzzi, L., Pedro, J. M. B., Madeo, F., & Kroemer, G. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.014 · Cited by 1,349 · see citing works
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324 · see citing works
Symbiotic gut microbes modulate human metabolic phenotypes
Li, M., Wang, B., Zhang, M., Rantalainen, M., Wang, S., Zhou, H., Zhang, Y., Shen, J., Pang, X., Zhang, M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712038105 · Cited by 1,144 · see citing works
Metabolic regulation of gene expression through histone acylations
Sabari, B. R., Zhang, D., Allis, C. D., & Zhao, Y. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.140 · Cited by 1,134 · see citing works
Identification 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 · see citing works
A general introduction to the biochemistry of mitochondrial fatty acid β‐oxidation
Houten, S. M., & Wanders, R. J. A. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9061-2 · Cited by 1,020 · see citing works
Branched-Chain Amino Acid Metabolism
Harper, A. E., Miller, R. H., & Block, K. P. (1984) · Annual Review of Nutrition · doi:10.1146/annurev.nu.04.070184.002205 · Cited by 1,011 · see citing works
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Park, J., Chen, Y., Tishkoff, D. X., Peng, C., Tan, M., Dai, L., Xie, Z., Zhang, Y., Zwaans, B. M. M., Skinner, M. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.001 · Cited by 1,000 · see citing works
Donohoe, D. R., Collins, L. B., Wali, A., Bigler, R., Sun, W., & Bultman, S. J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.033 · Cited by 993 · see citing works
Acetyl-CoA and the regulation of metabolism: mechanisms and consequences
Shi, L., & Tu, B. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.02.003 · Cited by 903 · see citing works
Scheiman, J., Luber, J. M., Chavkin, T. A., MacDonald, T., Tung, A., Pham, L.-D., Wibowo, M. C., Wurth, R. C., Punthambaker, S., Tierney, B. T., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0485-4 · Cited by 892 · see citing works
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.014 · Cited by 844 · see citing works
Paine, P. L., Moore, L. C., & Horowitz, S. B. (1975) · Nature · doi:10.1038/254109a0 · Cited by 824 · see citing works
Lysine propionylation and butyrylation are novel post-translational modifications in histones
Chen, Y., Sprung, R., Tang, Y., Ball, H., Sangras, B., Kim, S. C., Falck, J. R., Peng, J., Gu, W., & Zhao, Y. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700021-mcp200 · Cited by 764 · see citing works
Branched-Chain Amino Acid Metabolism
Yudkoff, M. (1999) · Cited by 763 · see citing works
The mitochondrial transporter family (SLC25): physiological and pathological implications
Palmieri, F. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1099-7 · Cited by 757 · see citing works
Microbiota-Produced Succinate Improves Glucose Homeostasis via Intestinal Gluconeogenesis
Vadder, F. D., Kovatcheva‐Datchary, P., Zitoun, C., Duchampt, A., Bäckhed, F., & Mithieux, G. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.013 · Cited by 756 · see citing works
The first identification of lysine malonylation substrates and its regulatory enzyme
Peng, C., Lu, Z., Xie, Z., Cheng, Z., Chen, Y., Tan, M., Luo, H., Zhang, Y., He, W., Yang, K., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.012658 · Cited by 751 · see citing works
Metabolic Regulation of Gene Expression by Histone Lysine β-Hydroxybutyrylation
Xie, Z., Zhang, D., Chung, D., Tang, Z., Huang, H., Dai, L., Qi, S., Li, J., Colak, G., Chen, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.036 · Cited by 744 · see citing works
The Colonic Crypt Protects Stem Cells from Microbiota-Derived Metabolites
Kaiko, G. E., Ryu, H., Koues, O. I., Collins, P. L., Solnica‐Krezel, L., Pearce, E. J., Pearce, E. L., Oltz, E. M., & Stappenbeck, T. S. (2016) · Cell · doi:10.1016/j.cell.2016.05.018 · Cited by 738 · see citing works
SIRT5 Regulates the Mitochondrial Lysine Succinylome and Metabolic Networks
Rardin, M. J., He, W., Nishida, Y., Newman, J. C., Carrico, C., Danielson, S. R., Guo, A., Gut, P., Sahu, A. K., Li, B., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.013 · Cited by 711 · see citing works
Intracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation
Sabari, B. R., Tang, Z., Huang, H., Yong-Gonzalez, V., Molina, H., Kong, H. E., Dai, L., Shimada, M., Cross, J. R., Zhao, Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.029 · Cited by 659 · see citing works
Isolation of an archaeon at the prokaryote–eukaryote interface
Imachi, H., Nobu, M. K., Nakahara, N., Morono, Y., Ogawara, M., Takaki, Y., Takano, Y., Uematsu, K., Ikuta, T., Ito, M., et al. (2020) · Nature · doi:10.1038/s41586-019-1916-6 · Cited by 624 · see citing works
Lysine succinylation and lysine malonylation in histones
Xie, Z., Dai, J., Dai, L., Tan, M., Cheng, Z., Wu, Y., Boeke, J. D., & Zhao, Y. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015875 · Cited by 613 · see citing works
Fellows, R., Denizot, J., Stellato, C., Cuomo, A., Jain, P., Stoyanova, E., Balázsi, S., Hajnády, Z., Liebert, A., Kazakevych, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02651-5 · Cited by 568 · see citing works
KAT2A coupled with the α-KGDH complex acts as a histone H3 succinyltransferase
Wang, Y., Guo, Y. R., Liu, K., Yin, Z., Liu, R., Xia, Y., Tan, L., Yang, P., Lee, J.-H., Li, X.-J., et al. (2017) · Nature · doi:10.1038/nature25003 · Cited by 567 · see citing works
Akt-dependent metabolic reprogramming regulates tumor cell histone acetylation
Lee, J. V., Carrer, A., Shah, S., Snyder, N. W., Wei, S., Venneti, S., Worth, A. J., Yuan, Z.-F., Lim, H.-W., Liu, S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.004 · Cited by 563 · see citing works
Accumulation of succinate controls activation of adipose tissue thermogenesis
Mills, E. L., Pierce, K. A., Jedrychowski, M. P., Garrity, R., Winther, S., Vidoni, S., Yoneshiro, T., Spinelli, J. B., Lu, G. Z., Kazak, L., et al. (2018) · Nature · doi:10.1038/s41586-018-0353-2 · Cited by 539 · see citing works
Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery
Tong, L. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5121-4 · Cited by 519 · see citing works
Wagner, G. R., & Payne, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.486753 · Cited by 490 · see citing works
Nishida, Y., Rardin, M. J., Carrico, C., He, W., Sahu, A. K., Gut, P., Najjar, R., Fitch, M., Hellerstein, M., Gibson, B. W., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.022 · Cited by 481 · see citing works
Branched-chain amino acid catabolism fuels adipocyte differentiation and lipogenesis
Green, C. R., Wallace, M., Divakaruni, A. S., Phillips, S. A., Murphy, A. N., Ciaraldi, T. P., & Metallo, C. M. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.1961 · Cited by 471 · see citing works
Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark
Dai, L., Peng, C., Montellier, E., Lu, Z., Chen, Y., Ishii, H., Debernardi, A., Buchou, T., Rousseaux, S., Jin, F., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1497 · Cited by 460 · see citing works
Acyl-CoA Metabolism and Partitioning
Grevengoed, T. J., Klett, E. L., & Coleman, R. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071813-105541 · Cited by 444 · see citing works
Takahashi, H., McCaffery, J. M., Irizarry, R. A., & Boeke, J. D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.040 · Cited by 438 · see citing works
Non-enzymatic Lysine Lactoylation of Glycolytic Enzymes
Gaffney, D. O., Jennings, E. Q., Anderson, C. C., Marentette, J., Shi, T., Oxvig, A.-M. S., Streeter, M. D., Johannsen, M., Spiegel, D. A., Chapman, E., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.11.005 · Cited by 430 · see citing works
Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation
Hirschey, M. D., & Zhao, Y. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r114.046664 · Cited by 423 · see citing works
The nexus of chromatin regulation and intermediary metabolism
Gut, P., & Verdin, E. M. (2013) · Nature · doi:10.1038/nature12752 · Cited by 419 · see citing works
Bartlett, K., & Eaton, S. D. (2004) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03947.x · Cited by 411 · see citing works
Coupling Krebs cycle metabolites to signalling in immunity and cancer
Ryan, D. G., Murphy, M. P., Frezza, C., Prag, H. A., Chouchani, E. T., O’Neill, L. A., & Mills, E. L. (2018) · Nature Metabolism · doi:10.1038/s42255-018-0014-7 · Cited by 398 · see citing works
Srere, P. A. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69735-2 · Cited by 394 · see citing works
Li, L., Shi, L., Yang, S., Yan, R., Zhang, D., Yang, J., He, L., Li, W., Yi, X., Sun, L., et al. (2016) · Nature Communications · doi:10.1038/ncomms12235 · Cited by 392 · see citing works
Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain
Li, Y., Sabari, B. R., Panchenko, T., Wen, H., Zhao, D., Guan, H., Wan, L., Huang, H., Tang, Z., Zhao, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.028 · Cited by 384 · see citing works
Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome
Watkins, P. A., Maiguel, D. A., Jia, Z., & Pevsner, J. (2007) · Journal of Lipid Research · doi:10.1194/jlr.m700378-jlr200 · Cited by 378 · see citing works
Sadhukhan, S., Liu, X., Ryu, D., Nelson, O. D., Stupinski, J. A., Li, Z., Chen, W., Zhang, S., Weiss, R. S., Locasale, J. W., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519858113 · Cited by 376 · see citing works
Quantitative Proteomic Analysis of Histone Modifications
Huang, H., Lin, S., Garcia, B. A., & Zhao, Y. (2015) · Chemical Reviews · doi:10.1021/cr500491u · Cited by 372 · see citing works
Wanders, R. J. A., Waterham, H. R., & Ferdinandusse, S. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00083 · Cited by 366 · see citing works
Malonyl-CoA: the regulator of fatty acid synthesis and oxidation
Foster, D. W. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63967 · Cited by 358 · see citing works
Spatiotemporal Control of Acetyl-CoA Metabolism in Chromatin Regulation
Sivanand, S., Viney, I. A., & Wellen, K. E. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.11.004 · Cited by 356 · see citing works
Self-citationMetabolism as a guiding force for immunity
Jung, J., Zeng, H., & Horng, T. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0217-x · Cited by 345 · see citing works
Carrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331 · see citing works
Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324 · see citing works
Short‐Chain Fatty Acid Transporters: Role in Colonic Homeostasis
Sivaprakasam, S., Bhutia, Y. D., Yang, S., & Ganapathy, V. (2017) · Comprehensive physiology · doi:10.1002/cphy.c170014 · Cited by 321 · see citing works
Wei, W., Liu, X., Chen, J., Gao, S., Lu, L., Zhang, H., Ding, G., Wang, Z., Chen, Z., Shi, T., et al. (2017) · Cell Research · doi:10.1038/cr.2017.68 · Cited by 304 · see citing works
Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism
Walsh, C. T., Tu, B. P., & Tang, Y. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00510 · Cited by 302 · see citing works
Tirosh, A., Calay, E. S., Tuncman, G., Claiborn, K. C., Inouye, K., Eguchi, K., Alcala, M., RATHAUS, M., Hollander, K. S., Ron, I., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aav0120 · Cited by 297 · see citing works
Impairment of Angiogenesis by Fatty Acid Synthase Inhibition Involves mTOR Malonylation
Brüning, U., Morales-Rodriguez, F., Kalucka, J. M., Goveia, J., Taverna, F., Queiroz, K. C. S., Dubois, C., Cantelmo, A. R., Chen, R., Loroch, S., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.019 · Cited by 278 · see citing works
Colak, G., Xie, Z., Zhu, A. Y., Dai, L., Lu, Z., Zhang, Y., Wan, X., Chen, Y., Cha, Y. H., Lin, H., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031567 · Cited by 273 · see citing works
Luong, A., Hannah, V. C., Brown, M. S., & Goldstein, J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004160200 · Cited by 266 · see citing works
Goudarzi, A., Zhang, D., Huang, H., Barral, S., Kwon, O. K., Qi, S., Tang, Z., Buchou, T., Vitte, A.-L., Tie-ming, H., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.014 · Cited by 264 · see citing works
Citrate and the Conversion of Carbohydrate into Fat
Watson, J. A., & Lowenstein, J. M. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62653-5 · Cited by 262 · see citing works
A Class of Reactive Acyl-CoA Species Reveals the Non-enzymatic Origins of Protein Acylation
Wagner, G. R., Bhatt, D. P., O’Connell, T. M., Thompson, J. W., Dubois, L. G., Backos, D. S., Yang, H., Mitchell, G. A., Ilkayeva, O. R., Stevens, R. D., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.03.006 · Cited by 258 · see citing works
Liu, S., Yu, H., Liu, Y., Liu, X., Zhang, Y., Bu, C., Yuan, S., Chen, Z., Xie, G., Li, W., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.011 · Cited by 258 · see citing works
Metabolite exchange between mammalian organs quantified in pigs
Jang, C., Hui, S., Zeng, X., Cowan, A. J., Wang, L., Chen, L., Morscher, R. J., Reyes, J., Frezza, C., Hwang, H. Y., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.06.002 · Cited by 256 · see citing works
Gut microbiome-derived metabolites characterize a peculiar obese urinary metabotype
Calvani, R., Miccheli, A., Capuani, G., Tomassini Miccheli, A., Puccetti, C., Delfini, M., Iaconelli, A., Nanni, G., & Mingrone, G. (2010) · International Journal of Obesity · doi:10.1038/ijo.2010.44 · Cited by 241 · see citing works
The Taf14 YEATS domain is a reader of histone crotonylation
Andrews, F. H., Shinsky, S. A., Shanle, E. K., Bridgers, J. B., Gest, A. M. M., Tsun, I. K., Krajewski, K., Shi, X., Strahl, B. D., & Kutateladze, T. G. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2065 · Cited by 239 · see citing works
Characterization of histone acylations links chromatin modifications with metabolism
Simithy, J., Sidoli, S., Yuan, Z., Coradin, M., Bhanu, N. V., Marchione, D. M., Klein, B. J., Bazilevsky, G. A., McCullough, C. E., Magin, R. S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01384-9 · Cited by 226 · see citing works
Self-citationYEATS2 is a selective histone crotonylation reader
Zhao, D. Y., Guan, H., Zhao, S., Mi, W., Wen, H., Li, Y., Zhao, Y., Allis, C. D., Shi, X., & Li, H. (2016) · Cell Research · doi:10.1038/cr.2016.49 · Cited by 224 · see citing works
METABOLISM OF PROPIONIC ACID IN ANIMAL TISSUES
Flavin, M., & Ochoa, S. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63700-2 · Cited by 222 · see citing works
Flynn, E. M., Huang, O. W., Poy, F., Oppikofer, M., Bellon, S. F., Tang, Y., & Cochran, A. G. (2015) · Structure · doi:10.1016/j.str.2015.08.004 · Cited by 222 · see citing works
p300-Mediated Lysine 2-Hydroxyisobutyrylation Regulates Glycolysis
Huang, H., Tang, S., Ji, M. H., Tang, Z., Shimada, M., Liu, X., Qi, S., Locasale, J. W., Roeder, R. G., Zhao, Y., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.011 · Cited by 221 · see citing works
Dalby, M. J., Ross, A., Walker, A. W., & Morgan, P. J. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.056 · Cited by 214 · see citing works
Regulation of UCP1 and Mitochondrial Metabolism in Brown Adipose Tissue by Reversible Succinylation
Wang, G., Meyer, J. G., Cai, W., Softic, S., Li, M. E., Verdin, E. M., Newgard, C. B., Schilling, B., & Kahn, C. R. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.021 · Cited by 213 · see citing works
Kinetic Study of the Tricarboxylate Carrier in Rat Liver Mitochondria
Palmieri, F., Stipani, I., Quagliariello, E., et al. (1972) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1972.tb01801.x · Cited by 211 · see citing works
Butyrate Histone Deacetylase Inhibitors
Steliou, K., Boosalis, M. S., Perrine, S. P., Sangerman, J., & Faller, D. V. (2012) · BioResearch open access · doi:10.1089/biores.2012.0223 · Cited by 208 · see citing works
Urinary metabolic signatures of human adiposity
Elliott, P., Posma, J. M., Chan, Q. M., García‐Pérez, I., Wijeyesekera, A., Bictash, M., Ebbels, T. M. D., Ueshima, H., Zhao, L., Horn, L. V., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa5680 · Cited by 207 · see citing works
Enzyme promiscuity drives branched-chain fatty acid synthesis in adipose tissues
Wallace, M., Green, C. R., Roberts, L. S., Lee, Y. M., McCarville, J. L., Sánchez-Gurmaches, J., Meurs, N., Gengatharan, J. M., Hover, J. D., Phillips, S. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0132-2 · Cited by 207 · see citing works
N-Lysine Propionylation Controls the Activity of Propionyl-CoA Synthetase
Garrity, J., Gardner, J. G., Hawse, W. F., Wolberger, C., & Escalante‐Semerena, J. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704409200 · Cited by 203 · see citing works
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 203 · see citing works
Hunt, M. C., Siponen, M. I., & Alexson, S. E. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.03.009 · Cited by 196 · see citing works
Histone lactylation links metabolism and gene regulation
Izzo, L., & Wellen, K. E. (2019) · Nature · doi:10.1038/d41586-019-03122-1 · Cited by 195 · see citing works
Self-citationCrown, S. B., Marze, N. A., & Antoniewicz, M. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145850 · Cited by 194 · see citing works
Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2
Xiong, X., Panchenko, T., Yang, S., Zhao, S., Yan, P., Zhang, W., Xie, W., Li, Y., Zhao, Y., Allis, C. D., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2218 · Cited by 192 · see citing works
Colak, G., Pougovkina, O., Dai, L., Tan, M., Brinke, H. T., Huang, H., Cheng, Z., Park, J.-S., Wan, X., Liu, X., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.048850 · Cited by 186 · see citing works
Carnitine Palmitoyltransferase 1A Has a Lysine Succinyltransferase Activity
Kurmi, K., Hitosugi, S., Wiese, E. K., Boakye‐Agyeman, F., Gonsalves, W. I., Lou, Z., Karnitz, L. M., Goetz, M. P., & Hitosugi, T. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.030 · Cited by 186 · see citing works
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 182 · see citing works
Self-citationThe role of mitochondrial sirtuins in health and disease
Osborne, B., Bentley, N. L., Montgomery, M. K., & Turner, N. A. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.197 · Cited by 179 · see citing works
Bracher, P. J., Snyder, P. W., Bohall, B. R., & Whitesides, G. M. (2011) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-011-9243-4 · Cited by 174 · see citing works
Structure of p300 in complex with acyl-CoA variants
Kaczmarska, Z., Ortega, E. M., Goudarzi, A., Huang, H., KIM, S. ‐., Márquez, J. A., Zhao, Y., Khochbin, S., & Panne, D. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2217 · Cited by 174 · see citing works
Kushnir, M. M., Komaromy-Hiller, G., Shushan, B. I., Urry, F. M., & Roberts, W. L. (2001) · Clinical Chemistry · doi:10.1093/clinchem/47.11.1993 · Cited by 170 · see citing works
Metabolomics Identifies Perturbations in Human Disorders of Propionate Metabolism
Wikoff, W. R., Gangoiti, J. A., Barshop, B. A., & Siuzdak, G. E. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2007.089011 · Cited by 170 · see citing works
Site-Specific Reactivity of Nonenzymatic Lysine Acetylation
Baeza, J., Smallegan, M. J., & Denu, J. M. (2015) · ACS Chemical Biology · doi:10.1021/cb500848p · Cited by 169 · see citing works
Molecular Characterization of Propionyllysines in Non-histone Proteins
Cheng, Z., Tang, Y., Chen, Y., Kim, S., Liu, H., Li, S. S. ‐., Gu, W. J., & Zhao, Y. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800224-mcp200 · Cited by 167 · see citing works
Circulating Succinate is Elevated in Rodent Models of Hypertension and Metabolic Disease
Sadagopan, N., Li, W., Roberds, S. L., Major, T. C., Preston, G. M., Yu, Y., & Tones, M. A. (2007) · American Journal of Hypertension · doi:10.1016/j.amjhyper.2007.05.010 · Cited by 164 · see citing works
Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics
Bao, X., Liu, Z., Zhang, W., Gladysz, K., Fung, Y. M. E., Tian, G., Xiong, Y., Wong, J. W. H., Yuen, K. W. Y., & Li, X. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.018 · Cited by 164 · see citing works
Natural history of propionic acidemia
Peña, L., Franks, J., Chapman, K. A., et al. (2011) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2011.09.022 · Cited by 159 · see citing works
Histone lysine crotonylation during acute kidney injury in mice
Ruiz‐Andrés, O., Sánchez-Niño, M. D., Cannata‐Ortiz, P., Ruiz‐Ortega, M., Egido, J., Ortíz, A., & Sanz, A. B. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.024455 · Cited by 158 · see citing works
Liu, X., Wei, W., Liu, Y., Yang, X., Wu, J., Zhang, Y., Zhang, Q., Shi, T., Du, J. X., Zhao, Y., et al. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.16 · Cited by 158 · see citing works
Impact of a High-fat Diet on Tissue Acyl-CoA and Histone Acetylation Levels
Carrer, A., Parris, J. L. D., Trefely, S., Henry, R. A., Montgomery, D. C., Torres, A., Viola, J. M., Kuo, Y., Blair, I. A., Meier, J. L., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.750620 · Cited by 156 · see citing works
Self-citationSmestad, J. A., Erber, L. N., Chen, Y., & Maher, L. J. (2018) · iScience · doi:10.1016/j.isci.2018.03.012 · Cited by 153 · see citing works
Transfer of metabolites across the peroxisomal membrane.
Antonenkov, V. D., & Hiltunen, J. (2012) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2011.12.011 · Cited by 152 · see citing works
Nonenzymatic acetylation of histones with acetyl-CoA
Paik, W. K., Pearson, D., Lee, H. W., & Kim, S. (1970) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(70)90058-4 · Cited by 151 · see citing works
Isolation of an archaeon at the prokaryote-eukaryote interfacePreprint
Imachi, H., Nobu, M. K., Nakahara, N., Morono, Y., Ogawara, M., Takaki, Y., Takano, Y., Uematsu, K., Ikuta, T., Ito, M., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/726976 · Cited by 150 · see citing works
Mitochondrial acetylcarnitine provides acetyl groups for nuclear histone acetylation
Madiraju, P., Pande, S. V., Prentki, M., & Madiraju, S. R. M. (2009) · Epigenetics · doi:10.4161/epi.4.6.9767 · Cited by 147 · see citing works
Zhang, K., Chen, Y., Zhang, Z., & Zhao, Y. (2008) · Journal of Proteome Research · doi:10.1021/pr8005155 · Cited by 147 · see citing works
Identification and Characterization of Propionylation at Histone H3 Lysine 23 in Mammalian Cells
Liu, B., Lin, Y.-H., Darwanto, A., Song, X., Xu, G., & Zhang, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045856 · Cited by 145 · see citing works
Phytanic acid metabolism in health and disease
Wanders, R. J. A., Komen, J. C., & Ferdinandusse, S. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.06.006 · Cited by 143 · see citing works
Yang, W., & Drueckhammer, D. G. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010726a · Cited by 139 · see citing works
Acetyl-lysine Analog Peptides as Mechanistic Probes of Protein Deacetylases
Smith, B. C., & Denu, J. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707878200 · Cited by 139 · see citing works
Gibson, G. E., Xu, H., Chen, H., Chen, W., Denton, T. T., & Zhang, S. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13096 · Cited by 137 · see citing works
Fiermonte, G., Palmieri, L., Dolce, V., Lasorsa, F. M., Palmieri, F., Runswick, M. J., & Walker, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.38.24754 · Cited by 135 · see citing works
Diurnal rhythms in the human urine metabolome during sleep and total sleep deprivation
Giskeødegård, G. F., Davies, S. K., Revell, V. L., Keun, H., & Skene, D. J. (2015) · Scientific Reports · doi:10.1038/srep14843 · Cited by 135 · cited 1× · see citing works
“2-HIB levels in urine were increased in obesity in humans [163e165], decreased in sleep deprivation in humans [166], and varied according to gender in obese mouse models [167].”
BackgroundMolecular basis for hierarchical histone de-β-hydroxybutyrylation by SIRT3
Zhang, X., Cao, R., Niu, J., Yang, S., Ma, H., Zhao, S., & Li, H. (2019) · Cell Discovery · doi:10.1038/s41421-019-0103-0 · Cited by 124 · see citing works
Peroxisomes in human fibroblasts have a basic pH
Dansen, T. B., WIRTZ, K. W. A., Wanders, R. J. A., & Pap, E. H. W. (1999) · Nature Cell Biology · doi:10.1038/71375 · Cited by 123 · see citing works
Wang, H., Fei, Y.-J., Kekuda, R., et al. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.278.5.c1019 · Cited by 122 · see citing works
Metabolic and Tissue-Specific Regulation of Acyl-CoA Metabolism
Ellis, J. M., Bowman, C. E., & Wolfgang, M. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116587 · Cited by 112 · see citing works
The Landscape of Histone Modifications in a High-Fat Diet-Induced Obese (DIO) Mouse Model
Nie, L., Shuai, L., Zhu, M., Liu, P., Xie, Z., Jiang, S., Jiang, H., Li, J., Zhao, Y., Li, J.-Y., et al. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m117.067553 · Cited by 109 · see citing works
Liu, X., Sadhukhan, S., Sun, S., Wagner, G. R., Hirschey, M. D., Qi, L., Lin, H., & Locasale, J. W. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.044859 · Cited by 108 · see citing works
Molecular and functional analysis of SDCT2, a novel rat sodium-dependent dicarboxylate transporter
Chen, X., Tsukaguchi, H., Chen, X., Berger, U. V., & Hediger, M. A. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5392 · Cited by 105 · see citing works
Violante, S. N., IJlst, L., Ruiter, J. P. N., Koster, J., van LENTHE, H., Durán, M., de Almeida, I. T., Wanders, R. J. A., Houten, S. M., & Ventura, F. V. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.02.012 · Cited by 102 · see citing works
Bowman, C. E., Rodriguez, S., Alpergin, E. S. S., Acoba, M. G., Zhao, L., Härtung, T., Claypool, S. M., Watkins, P. A., & Wolfgang, M. J. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.04.009 · Cited by 100 · see citing works
Westin, M. A. K., Hunt, M. C., & Alexson, S. E. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508479200 · Cited by 98 · see citing works
Discovering Targets of Non-enzymatic Acylation by Thioester Reactivity Profiling
Kulkarni, R. A., Worth, A. J., Zengeya, T. T., Shrimp, J. H., Garlick, J. M., Roberts, A. M., Montgomery, D. C., Sourbier, C., Gibbs, B. K., Mesaros, C., et al. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.01.002 · Cited by 94 · see citing works
Self-citationShort-Chain Acyl-Coenzyme A Dehydrogenase Deficiency in Mice
Wood, P. A., Amendt, B. A., Rhead, W. J., et al. (1989) · Pediatric Research · doi:10.1203/00006450-198901000-00010 · Cited by 90 · see citing works
Regulation of peroxisomal lipid metabolism: The role of acyl-CoA and coenzyme A metabolizing enzymes
Hunt, M. C., Tillander, V., & Alexson, S. E. H. (2014) · Biochimie · doi:10.1016/j.biochi.2013.12.018 · Cited by 87 · see citing works
Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation
Wang, Y., Jin, J., Chung, M. W. H., Feng, L., Sun, H., & Hao, Q. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717664115 · Cited by 82 · see citing works
Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism
Pougovkina, O., te Brinke, H., Wanders, R. J. A., Houten, S. M., & de Boer, V. C. J. (2014) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-014-9684-9 · Cited by 80 · see citing works
Interaction of Propionylated and Butyrylated Histone H3 Lysine Marks with Brd4 Bromodomains
Vollmuth, F., & Geyer, M. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201002724 · Cited by 79 · see citing works
Propionate increases hepatic pyruvate cycling and anaplerosis and alters mitochondrial metabolism
Perry, R. J., Borders, C. B., Cline, G. W., Zhang, X.-M., Alves, T. C., Petersen, K. F., Rothman, D. L., Kibbey, R. G., & Shulman, G. I. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.720631 · Cited by 78 · see citing works
The Human Histone Acetyltransferase P/CAF is a Promiscuous Histone Propionyltransferase
Leemhuis, H., Packman, L. C., Nightingale, K. P., & Hollfelder, F. (2008) · ChemBioChem · doi:10.1002/cbic.200700556 · Cited by 77 · see citing works
Comparative aspects of propionate metabolism
Halarnkar, P. P., & Blomquist, G. J. (1989) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(89)90270-8 · Cited by 76 · see citing works
Coupling of the de Novo Fatty Acid Biosynthesis and Lipoylation Pathways in Mammalian Mitochondria
Witkowski, A., Joshi, A. K., & Smith, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701486200 · Cited by 75 · see citing works
Han, Z. H., Wu, H., KIM, S. ‐., Yang, X., Li, Q., Huang, H., Cai, H., Bartlett, M. G., Dong, A., Zeng, H., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000529 · Cited by 68 · see citing works
Purification and properties of acetyl coenzyme A synthetase from bakers' yeast.
Frenkel, E. P., & Kitchens, R. L. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32745-x · Cited by 63 · see citing works
Bernauer, U., Amberg, A., Scheutzow, D., et al. (1998) · Chemical Research in Toxicology · doi:10.1021/tx970215v · Cited by 62 · see citing works
Tertiary-Butanol: A toxicological review
McGregor, D. B. (2010) · Critical Reviews in Toxicology · doi:10.3109/10408444.2010.494249 · Cited by 62 · see citing works
Intracellular iron and heme trafficking and metabolism in developing erythroblasts
Kafina, M. D., & Paw, B. H. (2017) · Metallomics · doi:10.1039/c7mt00103g · Cited by 62 · see citing works
Won, E.-Y., Yoon, M., Kim, S. W., Jung, Y., Bae, H.-W., Lee, D., Park, S. G., Lee, C., Hwang, G., & Chi, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075998 · Cited by 61 · see citing works
13C isotopomer model for estimation of anaplerotic substrate oxidation via acetyl-CoA
Jeffrey, F. M. H., Storey, C. J., Sherry, A. D., et al. (1996) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1996.271.4.e788 · Cited by 61 · see citing works
Structural basis for acyl-group discrimination by human Gcn5L2
Ringel, A. E., & Wolberger, C. (2016) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798316007907 · Cited by 61 · see citing works
The mitochondrial oxoglutarate carrier: from identification to mechanism
Monné, M., Miniero, D. V., Bisaccia, F., & Fiermonte, G. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9475-7 · Cited by 58 · see citing works
Burckhardt, B. C., Lorenz, J., Kobbe, C., et al. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00360.2004 · Cited by 57 · see citing works
Reszko, A. E., Kasumov, T., Pierce, B. A., David, F., Hoppel, C. L., Stanley, W. C., Rosiers, C. D., & Brunengraber, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302013200 · Cited by 55 · see citing works
Substrate specificity of acetyl coenzyme A synthetase.
Patel, S. S., & Walt, D. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48214-2 · Cited by 55 · see citing works
Kawai, Y., Fujii, H., Okada, M., Tsuchie, Y., Uchida, K., & Osawa, T. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600091-jlr200 · Cited by 53 · see citing works
Propionate alleviates high-fat diet-induced lipid dysmetabolism by modulating gut microbiota in mice
Song, B., Zhong, Y. Z., Zheng, C. B., Li, F. N., Duan, Y., & Deng, J. (2019) · Journal of Applied Microbiology · doi:10.1111/jam.14389 · Cited by 52 · see citing works
Yoshimura, Y., Araki, A., Maruta, H., Takahashi, Y., & Yamashita, H. (2016) · The Journal of Biochemistry · doi:10.1093/jb/mvw067 · Cited by 49 · see citing works
Nochi, Z., Olsen, R. K. J., & Gregersen, N. (2017) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-017-0047-1 · Cited by 49 · see citing works
Meyer, J. G., Softic, S., Basisty, N., Rardin, M. J., Verdin, E. M., Gibson, B. W., Ilkayeva, O., Newgard, C. B., Kahn, C. R., & Schilling, B. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208973 · Cited by 49 · see citing works
Fisher‐Wellman, K. H., Draper, J. A., Davidson, M. T., Williams, A. S., Narowski, T. M., Slentz, D. H., Ilkayeva, O., Stevens, R. D., Wagner, G. R., Najjar, R. S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.057 · Cited by 49 · see citing works
Mild metabolic perturbations alter succinylation of mitochondrial proteins
Chen, H., Xu, H., Potash, S., Starkov, A. A., Belousov, V. V., Bilan, D. S., Denton, T. T., & Gibson, G. E. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24103 · Cited by 45 · see citing works
Nonenzymatic Protein Acetylation Detected by NAPPA Protein Arrays
Olia, A. S., Barker, K., McCullough, C. E., Tang, H., Speicher, D. W., Qiu, J., LaBaer, J., & Marmorstein, R. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00342 · Cited by 44 · see citing works
Kerner, J., & Hoppel, C. (2002) · Analytical Biochemistry · doi:10.1006/abio.2002.5696 · Cited by 33 · see citing works
Short-Term Changes of the Urine Metabolome After Bariatric Surgery
Friedrich, N., Budde, K., Wolf, T., Jungnickel, A., Grotevendt, A., Dreßler, M., Völzke, H., Blüher, M., Nauck, M. A., Lohmann, T., et al. (2012) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2012.0066 · Cited by 33 · see citing works
Isolation of an archaeon at the prokaryote-eukaryote interface
Dey, G. K. (2019) · doi:10.1242/prelights.13336 · Cited by 32 · see citing works
Palladino, A., Chen, J., Kallish, S., et al. (2012) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2012.10.007 · Cited by 31 · see citing works
Han, A., Bennett, N. E., MacDonald, A., Johnstone, M. E., Whelan, J. N., & Donohoe, D. R. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25287 · Cited by 31 · see citing works
Meijer-Severs, G. J., & van Santen, E. (1987) · Scandinavian Journal of Gastroenterology · doi:10.3109/00365528709011141 · Cited by 30 · see citing works
Short chain acyl-CoA synthetases in ovine rumen epithelium
Scaife, J. R., & Tichivangana, J. Z. (1980) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(80)90097-1 · Cited by 27 · see citing works
Kinetic Mechanism of Glutaryl-CoA Dehydrogenase
Rao, K. S., Albro, M., Dwyer, T. M., et al. (2006) · Biochemistry · doi:10.1021/bi0609016 · Cited by 25 · see citing works
Quantifying Competition among Mitochondrial Protein Acylation Events Induced by Ethanol Metabolism
Ali, H., Assiri, M. A., Harris, P. S., Michel, C. R., Yun, Y., Marentette, J., Huynh, F. K., Orlicky, D. J., Shearn, C. T., Saba, L. M., et al. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00800 · Cited by 23 · see citing works
Studies on the extra-mitochondrial CoA-ester formation of valproic and Δ4-valproic acids
Aires, C., Ruiter, J., Luis, P. B., et al. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.01.010 · Cited by 22 · see citing works
Quantitation of Reactive Acyl-CoA Species Mediated Protein Acylation by HPLC–MS/MS
Baldensperger, T., Sanzo, S. D., Ori, A., & Glomb, M. A. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b02656 · Cited by 21 · see citing works
Rizzo, C., Boenzi, S., Inglese, R., et al. (2013) · Clinica Chimica Acta · doi:10.1016/j.cca.2013.11.016 · Cited by 20 · see citing works
Radioassay of acetyl-CoA synthetase, propionyl-CoA synthetase and butyryl-CoA synthetase in brain
Reijnierse, G. L. A., Veldstra, H., & den Berg, C. J. V. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90574-1 · Cited by 16 · see citing works
Biochemical Analysis of Histone Succinylation
Yokoyama, A., Katsura, S., & Sugawara, A. (2017) · Biochemistry Research International · doi:10.1155/2017/8529404 · Cited by 14 · see citing works
Su, H., Lou, Y., Fu, Y., Zhang, Y., Liu, N., Liu, Z., Zhou, Y., & Kong, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-14477-8 · Cited by 13 · see citing works
Energy Conservation via Thioesters in a Non-Enzymatic Metabolism-like Reaction NetworkPreprint
Chevallot-Béroux, E., Gorges, J., & Moran, J. (2019) · ChemRxiv · doi:10.26434/chemrxiv.8832425.v1 · Cited by 10 · see citing works
Non‐Enzymatic Lysine Lactoylation of Glycolytic Enzymes
Galligan, J. J., Gaffney, D. O., Jennings, E. Q., et al. (2020) · The FASEB Journal · doi:10.1096/fasebj.2020.34.s1.02010 · Cited by 5 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Regulation and function of the mammalian tricarboxylic acid cycle
Arnold, P. K., & Finley, L. W. S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102838 · Cited by 535 · see citing works
“By co-opting the production and localization of select TCA cycle metabolites, cells can modulate the activity of chromatinmodifying enzymes and exert control over gene expression and cell fate (Reid et al., 2017; Schvartzman et al., 2018; Trefely et al., 2020).”
BackgroundZhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works
Acetyl-CoA metabolism in cancer
Guertin, D. A., & Wellen, K. E. (2023) · Nature Reviews Cancer · doi:10.1038/s41568-022-00543-5 · Cited by 303 · see citing works
Self-citationSuccinylation of H3K122 destabilizes nucleosomes and enhances transcription
Zorro Shahidian, L., Haas, M., Le Gras, S., Nitsch, S., Mourão, A., Geerlof, A., Margueron, R., Michaelis, J., Daujat, S., & Schneider, R. (2021) · The EMBO Reports · doi:10.15252/embr.202051009 · Cited by 92 · see citing works
Lancaster, M. S., Kim, B., Doud, E. H., Tate, M. D., Sharify, A. D., Gao, H., Chen, D., Simpson, E., Gillespie, P., Chu, X., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113241 · Cited by 24 · see citing works
- Authors
- Trefely, S., Lovell, C. D., Snyder, N. W., & Wellen, K. E.
- Affiliations
- Abramson Cancer Center (US)
- Temple University (US)
- Corresponding author
- Snyder, Nathaniel W.
- Wellen, Kathryn E.
- Venue
- Molecular Metabolism
- Publisher
- Elsevier BV
- Published
- 2020-08
- Volume
- 38
- Pages
- 100941
- ISSN
- 2212-8778 (ISSN-L)
- PMC
- PMC7300382
- OpenAlex
- W3006138245
- Cited by
- 272
- References
- 182
- Citations by year
- 2026: 45 · 2025: 54 · 2024: 35 · 2023: 48 · 2022: 36 · 2021: 37 · 2020: 14 · 2019: 1
- FWCI
- 3.23
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecular Metabolism (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases
- National Cancer Institute
- National Institute of General Medical Sciences
- 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 › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- acyl-CoA metabolism, chromatin regulation, succinyl-CoA, propionyl-CoA, butyryl-CoA, malonyl-CoA, glutaryl-CoA, 3-hydroxybutyryl-CoA, mitochondrial metabolism
- MeSH terms
- Acetyl Coenzyme A, Acetylation, Acyl Coenzyme A, Animals, Chromatin, Histones, Humans, Lysine, Gene Expression
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
