Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation
Open accessAbstract
Lysine acetylation is rapidly becoming established as a key post-translational modification for regulating mitochondrial metabolism. Nonetheless, distinguishing regulatory sites from among the thousands identified by mass spectrometry and elucidating how these modifications alter enzyme function remain primary challenges. Here, we performed multiplexed quantitative mass spectrometry to measure changes in the mouse liver mitochondrial acetylproteome in response to acute and chronic alterations in nutritional status, and integrated these data sets with our compendium of predicted Sirt3 targets. These analyses highlight a subset of mitochondrial proteins with dynamic acetylation sites, including acetyl-CoA acetyltransferase 1 (Acat1), an enzyme central to multiple metabolic pathways. We performed in vitro biochemistry and molecular modeling to demonstrate that acetylation of Acat1 decreases its activity by disrupting the binding of coenzyme A. Collectively, our data reveal an important new target of regulatory acetylation and provide a foundation for investigating the role of select mitochondrial protein acetylation sites in mediating acute and chronic metabolic transitions. Background: Lysine acetylation, a prevalent post-translational modification, alters mitochondrial metabolism in response to nutrient changes. Results: Quantitative proteomics distinguishes dynamic and static acetylation sites, highlighting 48 likely regulatory sites of thousands identified. Conclusion: Acetylation of Acat1 lysine 260, a highly dynamic site, reversibly inhibits enzyme activity. Significance: Quantitative, state-specific proteomic analyses accelerate the functional characterization of acetylation in mitochondrial remodeling.
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?
Many mitochondrial proteins are hyperacetylated during fasting.
“Mitochondrial hyperacetylation thus tends to limit the metabolic adaptations necessary for proper function during fasting; SIRT3 is upregulated during fasting to combat this process (Hirschey et al. 2010), and many mitochondrial proteins are hyperacetylated during fasting (Still et al. 2013).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Still et al. 2013
Obesity from hypernutrition predominantly decreases mitochondrial acetylation in liver.
“In contrast to fasting and calorie restriction, hypernutrition to the point of obesity has been shown to predominantly decrease mitochondrial acetylation in liver (Still et al. 2013).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Still et al. 2013
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
Electrostatics of nanosystems: Application to microtubules and the ribosome
Baker, N., Sept, D., Joseph, S., Holst, M., & McCammon, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181342398 · Cited by 7,125 · see citing works
Open source clustering software
de Hoon, M., Imoto, S., Nolan, J., & Miyano, S. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth078 · Cited by 3,043 · see citing works
Java Treeview—extensible visualization of microarray data
Saldanha, A. J. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth349 · Cited by 2,991 · see citing works
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,649 · see citing works
A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994 · see citing works
Self-citationRegulation of cellular metabolism by protein lysine acetylation
Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., et al. (2010) · Science · doi:10.1126/science.1179689 · Cited by 1,910 · see citing works
Williamson, D., Lund, P., & Krebs, H. (1967) · Biochemical Journal · doi:10.1042/bj1030514 · Cited by 1,871 · see citing works
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687 · see citing works
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487 · see citing works
Regulation of hepatic fatty acid oxidation and ketone body production
McGarry, J. D., & Foster, D. W. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.002143 · Cited by 1,460 · cited 2× · see citing works
“Three of these processes, branched chain amino acid metabolism, fatty acid catabolism, and ketogenesis, exhibit acetylation changes in many pathway members and have in common a single enzyme: acetyl-coenzyme A acetyltransferase 1 (Acat1, NCBI gene ID 110446) (56, 57).”
BackgroundA role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291 · see citing works
Interplay between lipids and branched-chain amino acids in development of insulin resistance
Newgard, C. B. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.024 · Cited by 1,080 · 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
Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899 · see citing works
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 · see citing works
Self-citationHirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · see citing works
Kim, H.-S., Patel, K., Muldoon-Jacobs, K., Bisht, K. S., Aykin-Burns, N., Pennington, J. D., van der Meer, R., Nguyen, P., Savage, J., Owens, K. M., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.11.023 · Cited by 785 · see citing works
Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., Carson, J. J., Tonelli, M., Balloon, A. J., Higbee, A. J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.024 · Cited by 636 · see citing works
Self-citationGenetically encoding Nε-acetyllysine in recombinant proteins
Neumann, H., Peak‐Chew, S., & Chin, J. W. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.73 · Cited by 593 · see citing works
Lundby, A., Lage, K., Weinert, B. T., Bekker‐Jensen, D. B., Secher, A., Skovgaard, T., Kelstrup, C. D., Dmytriyev, A., Choudhary, C., Lundby, C., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.07.006 · Cited by 544 · see citing works
Disorders of carnitine transport and the carnitine cycle
Longo, N., Amat di San Filippo, C., & Pasquali, M. (2006) · American Journal of Medical Genetics Part C: Seminars in Medical Genetics · doi:10.1002/ajmg.c.30087 · Cited by 543 · see citing works
The dynamic regulation of NAD metabolism in mitochondria
Stein, L. R., & Imai, S. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.06.005 · Cited by 529 · see citing works
The presence of acetyl groups in histones
PHILLIPS, D. (1963) · Biochemical Journal · doi:10.1042/bj0870258 · Cited by 506 · see citing works
Neumann, H., Hancock, S. M., Buning, R., Routh, A. L., Chapman, L., Somers, J., Owen‐Hughes, T., van Noort, J., Rhodes, D., & Chin, J. W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.027 · Cited by 498 · see citing works
Shimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., Li, Y., Bunkenborg, J., Alt, F. W., Denu, J. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.003 · Cited by 484 · see citing works
Self-citationRegulation of Succinate Dehydrogenase Activity by SIRT3 in Mammalian Mitochondria
Çimen, H., Han, M., Yang, Y., Tong, Q., Koc, H., & Koc, E. C. (2009) · Biochemistry · doi:10.1021/bi901627u · Cited by 478 · see citing works
Rogers, G. W., Brand, M. D., Petrosyan, S., Ashok, D., Elorza, Á. A., Ferrick, D. A., & Murphy, A. N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021746 · Cited by 474 · see citing works
Metabolic flux and the regulation of mammalian cell growth
Locasale, J. W., & Cantley, L. C. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.014 · Cited by 449 · see citing works
Rardin, M. J., Newman, J. C., Held, J. M., Cusack, M. P., Sorensen, D. J., Li, B., Schilling, B., Mooney, S. D., Kahn, C. R., Verdin, E. M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302961110 · Cited by 446 · see citing works
Yu, W., Dittenhafer‐Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355206 · Cited by 445 · see citing works
Self-citationSystematic Functional Prioritization of Protein Posttranslational Modifications
Beltrão, P., Albanèse, V., Kenner, L., Swaney, D. L., Burlingame, A. L., Villén, J., Lim, W. A., Fraser, J. S., Frydman, J., & Krogan, N. J. (2012) · Cell · doi:10.1016/j.cell.2012.05.036 · Cited by 425 · see citing works
Fatty liver is associated with reduced SIRT3 activity and mitochondrial protein hyperacetylation
Kendrick, A. A., Choudhury, M., Rahman, S. M., McCurdy, C. E., Friederich, M., Van Hove, J. L. K., Watson, P. A., Birdsey, N., Bao, J., Gius, D., et al. (2011) · Biochemical Journal · doi:10.1042/bj20100791 · Cited by 382 · see citing works
Keller, M. P., Choi, Y., Wang, P., Belt Davis, D., Rabaglia, M. E., Oler, A. T., Stapleton, D. S., Argmann, C., Schueler, K. L., Edwards, S., et al. (2008) · Genome Research · doi:10.1101/gr.074914.107 · Cited by 377 · see citing works
Self-citationSuccinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity
Finley, L. W. S., Haas, W., Desquiret‐Dumas, V., Wallace, D. C., Procaccio, V., Gygi, S. P., & Haigis, M. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023295 · Cited by 364 · see citing works
Regulation of intermediary metabolism by protein acetylation
Guan, K., & Xiong, Y. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.003 · Cited by 353 · see citing works
Genetic Analysis of Histone H4: Essential Role of Lysines Subject to Reversible Acetylation
Megee, P. C., Morgan, B. A., Mittman, B. A., & Smith, M. M. (1990) · Science · doi:10.1126/science.2106160 · Cited by 349 · see citing works
Mitochondrial sirtuins: regulators of protein acylation and metabolism
He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262 · see citing works
Mitochondrial protein acetylation regulates metabolism
Anderson, K. A., & Hirschey, M. D. (2012) · Essays in Biochemistry · doi:10.1042/bse0520023 · Cited by 249 · see citing works
Sirtuin catalysis and regulation
Feldman, J. L., Dittenhafer-Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.378877 · Cited by 248 · see citing works
Self-citationGas-phase purification enables accurate, multiplexed proteome quantification with isobaric tagging
Wenger, C. D., Lee, M. V., Hebert, A. S., McAlister, G. C., Phanstiel, D. H., Westphall, M. S., & Coon, J. J. (2011) · Nature Methods · doi:10.1038/nmeth.1716 · Cited by 244 · see citing works
Self-citationMechanistic 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 238 · see citing works
Oxenkrug, G. F. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05356.x · Cited by 221 · see citing works
Tanner, K. G., Trievel, R. C., Kuo, M., Howard, R. M., Berger, S. L., Allis, C. D., Marmorstein, R., & Denu, J. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.26.18157 · Cited by 221 · see citing works
Self-citationScott, I., Webster, B. R., Li, J. H., & Sack, M. N. (2012) · Biochemical Journal · doi:10.1042/bj20120118 · Cited by 214 · see citing works
Newman, J. C., He, W., & Verdin, E. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.404863 · Cited by 207 · see citing works
Popov, K. M., Zhao, Y., Shimomura, Y., Kuntz, M. J., & Harris, R. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42179-5 · Cited by 177 · see citing works
Blommel, P. G., Becker, K. J., Duvnjak, P., & Fox, B. G. (2007) · Biotechnology Progress · doi:10.1021/bp070011x · Cited by 171 · see citing works
Insulin resistance and the metabolism of branched-chain amino acids in humans
Adeva‐Andany, M. M., Calviño, J., Souto, G., & Donapetry, C. (2011) · Amino Acids · doi:10.1007/s00726-011-1088-7 · Cited by 158 · see citing works
SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity
Bao, J., Scott, I., Lu, Z., Pang, L., Dimond, C. C., Gius, D., & Sack, M. N. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.07.009 · Cited by 157 · see citing works
Grimsrud, P. A., Carson, J. J., Hebert, A. S., Hubler, S. L., Niemi, N. M., Bailey, D. J., Jochem, A., Stapleton, D. S., Keller, M. P., Westphall, M. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.004 · Cited by 155 · see citing works
Self-citationCOMPASS: A suite of pre‐ and post‐search proteomics software tools for OMSSA
Wenger, C. D., Phanstiel, D. H., Lee, M. V., Bailey, D. J., & Coon, J. J. (2011) · PROTEOMICS · doi:10.1002/pmic.201000616 · Cited by 152 · see citing works
Self-citationNonenzymatic 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
Obesity and genetics regulate microRNAs in islets, liver, and adipose of diabetic mice
Zhao, E., Keller, M. P., Rabaglia, M. E., Oler, A. T., Stapleton, D. S., Schueler, K. L., Neto, E. C., Moon, J., Wang, P., Wang, I., et al. (2009) · Mammalian Genome · doi:10.1007/s00335-009-9217-2 · Cited by 148 · see citing works
Self-citationMitochondrial Sirtuins in the Regulation of Mitochondrial Activity and Metabolic Adaptation
Lombard, D. B., Tishkoff, D. X., & Bao, J. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_8 · Cited by 124 · see citing works
Haapalainen, A. M., Meriläinen, G., Pirilä, P., Kondo, N., Fukao, T., & Wierenga, R. K. (2007) · Biochemistry · doi:10.1021/bi6026192 · Cited by 100 · see citing works
Cardiac mitochondrial matrix and respiratory complex protein phosphorylation
Covián, R., & Balaban, R. S. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00077.2012 · Cited by 99 · see citing works
Evolutionary Constraints of Phosphorylation in Eukaryotes, Prokaryotes, and Mitochondria
Gnad, F., Forner, F., Zielinska, D. F., Birney, E., Gunawardena, J., & Mann, M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.001594 · Cited by 97 · see citing works
Han, Q., Cai, T., Tagle, D. A., Robinson, H. H., & Li, J. (2008) · Bioscience Reports · doi:10.1042/bsr20080085 · Cited by 84 · see citing works
Boekhorst, J., van Breukelen, B., Heck, A. J. R., & Snel, . (2008) · Genome biology · doi:10.1186/gb-2008-9-10-r144 · Cited by 83 · see citing works
Inborn errors of isoleucine degradation: A review
Korman, S. H. (2006) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2006.07.010 · Cited by 82 · see citing works
Middleton, B. S. (1973) · Biochemical Journal · doi:10.1042/bj1320731 · Cited by 79 · see citing works
Norvell, A., & McMahon, S. B. (2010) · Science · doi:10.1126/science.1187159 · Cited by 69 · see citing works
Peroxisomal-mitochondrial oxidation in a rodent model of obesity-associated insulin resistance
Noland, R. C., Woodlief, T., Whitfield, B. R., Manning, S. M., Evans, J. R., Dudek, R. W., Lust, R. M., & Cortright, R. N. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00399.2006 · Cited by 68 · see citing works
Benovic, J., Tillman, T. S., Cudd, A., & Fridovich, I. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90151-0 · Cited by 60 · see citing works
Vadvalkar, S. S., Baily, C. N., Matsuzaki, S., West, M. S., Tesiram, Y. A., & Humphries, K. M. (2012) · Biochemical Journal · doi:10.1042/bj20121038 · Cited by 59 · see citing works
Rossi, F., Garavaglia, S., Montalbano, V., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707925200 · Cited by 55 · see citing works
Crystal Structure of Human Kynurenine Aminotransferase II
Han, Q., Robinson, H. H., & Li, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708358200 · Cited by 50 · see citing works
Buchner, D. A., Yazbek, S. N., Solinas, P., Burrage, L. C., Morgan, M. G., Hoppel, C. L., & Nadeau, J. H. (2010) · Obesity · doi:10.1038/oby.2010.214 · Cited by 45 · see citing works
Regulation and protection of mitochondrial physiology by sirtuins
Pereira, C. V., Lebiedzińska, M., Wieckowski, M. R., & Oliveira, P. J. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.07.003 · Cited by 45 · see citing works
Metabolic adaptations of liver mitochondria during restricted feeding schedules
Báez‐Ruíz, A., Escobar, C., Aguilar‐Roblero, R. A., Martínez, O. V., & Díaz‐Muñoz, M. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00488.2004 · Cited by 44 · see citing works
Vaitheesvaran, B., Yang, L., Hartil, K., Glaser, S. T., Yazulla, S., Bruce, J. E., & Kurland, I. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033717 · Cited by 29 · see citing works
Internal standards in the estimation of acetyl-CoA in liver extracts
Herrera, E., & Freinkel, N. (1967) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38912-4 · Cited by 27 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
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
SIRT3 regulates progression and development of diseases of aging
McDonnell, E., Peterson, B. S., Bomze, H. M., & Hirschey, M. D. (2015) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2015.06.001 · Cited by 217 · see citing works
Song, B.-J., Akbar, M., Abdelmegeed, M. A., Byun, K., Lee, B., Yoon, S. K., & Hardwick, J. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.10.004 · Cited by 123 · see citing works
Meyer, J. G., D’Souza, A. K., Sorensen, D. J., Rardin, M. J., Wolfe, A. J., Gibson, B. W., & Schilling, B. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1476-z · Cited by 79 · see citing works
Liu, R., Zeng, L.-W., Gong, R., Yuan, F., Shu, H.-B., & Li, S. (2021) · Nature Communications · doi:10.1038/s41467-021-24321-3 · Cited by 67 · see citing works
Nutrient sensing and utilization: getting to the heart of metabolic flexibility
Griffin, T. M., Humphries, K. M., Kinter, M., Lim, H.-Y., & Szweda, L. I. (2016) · Biochimie · doi:10.1016/j.biochi.2015.10.013 · Cited by 36 · see citing works
Global profiling of lysine acetylation in human histoplasmosis pathogen Histoplasma capsulatum
Xie, L., Fang, W., Deng, W., Yu, Z., Li, J., Chen, M., Liao, W., Xie, J., & Pan, W. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.01.008 · Cited by 16 · see citing works
- Authors
- Still, A. J., Floyd, B. J., Hebert, A. S., Bingman, C. A., Carson, J. J., Gunderson, D. R., Dolan, B. K., Grimsrud, P. A., Dittenhafer-Reed, K. E., Stapleton, D. S., Keller, M. P., Westphall, M. S., Denu, J. M., Attie, A. D., Coon, J. J., & Pagliarini, D. J.
- Affiliations
- University of Wisconsin–Madison (US)
- Corresponding author
- Pagliarini, David J.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 288
- Issue
- 36
- Pages
- 26209-26219
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3764825
- OpenAlex
- W2037959732
- Cited by
- 123
- References
- 72
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 4 · 2023: 6 · 2022: 11 · 2021: 8 · 2020: 5 · 2019: 8 · 2018: 9 · 2017: 12 · 2016: 16 · 2015: 18 · 2014: 15 · 2013: 4
- FWCI
- 7.95
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (1256259, DK066369)
- American Heart Association (T32GM008692)
- Glenn Foundation for Medical Research
- National Institutes of Health (DGE-1256259)
- National Institute on Aging (R01AG038679, AG038679)
- National Cancer Institute (P30CA014520)
- National Institute of General Medical Sciences (R01GM080148, GM-065386, U01GM094622, T32GM008349, R01GM065386, T32GM007215, R37GM059785, T32GM008692)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-066369, RC1DK086410, F32DK091049, R01DK066369, DK058037, R01DK058037, T32DK007665, R01DK098672)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- lysine acetylation, ACAT1, SIRT3, coenzyme A binding, enzyme inhibition, post-translational modification, mitochondrial metabolism, liver, nutritional status, quantitative proteomics
- MeSH terms
- Acetyl-CoA C-Acetyltransferase, Acetyl Coenzyme A, Acetylation, Animals, Mice, Obese, Mitochondria, Liver, Proteome, Mice, Sirtuin 3
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
