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Lysine Glutarylation Is a Protein Posttranslational Modification Regulated by SIRT5
Open accessAbstract
We report the identification and characterization of a five-carbon protein posttranslational modification (PTM) called lysine glutarylation (Kglu). This protein modification was detected by immunoblot and mass spectrometry (MS), and then comprehensively validated by chemical and biochemical methods. We demonstrated that the previously annotated deacetylase, sirtuin 5 (SIRT5), is a lysine deglutarylase. Proteome-wide analysis identified 683 Kglu sites in 191 proteins and showed that Kglu is highly enriched on metabolic enzymes and mitochondrial proteins. We validated carbamoyl phosphate synthase 1 (CPS1), the rate-limiting enzyme in urea cycle, as a glutarylated protein and demonstrated that CPS1 is targeted by SIRT5 for deglutarylation. We further showed that glutarylation suppresses CPS1 enzymatic activity in cell lines, mice, and a model of glutaric acidemia type I disease, the last of which has elevated glutaric acid and glutaryl-CoA. This study expands the landscape of lysine acyl modifications and increases our understanding of the deacylase SIRT5.
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“This work resulted in the identification of novel modifications targeted by SIRT5: succinylation, malonylation and glutarylation as described in details below ((Du et al. 2011{Zhang, 2011 #16);(Peng et al. 2011);(Tan et al. 2014)}.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“SIRT5 positively regulates CPS1 activity by mediating desuccinylation, deglutarylation and possibly by deacetylation across multiple sites ((Du et al. 2011))((Tan et al. 2014))((Nakagawa et al. 2009)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Mice lacking SIRT5 fail to upregulate CPS1 activity and show elevated blood ammonia under these conditions ((Nakagawa et al. 2009))((Tan et al. 2014)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Moreover, HMGCS2 is also subject to glutarylation and malonylation ((Tan et al. 2014))((Nishida et al. 2015)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Interestingly, lysine 88 is also a target of succinylation and glutarylation ((Rardin, He, et al. 2013))((Tan et al. 2014)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Both MnSOD and the various mitochondrial superoxide sources are acylated ((Rardin, Newman, et al. 2013), (Rardin, He, et al. 2013);(Tan et al. 2014)); MnSOD also carries glutarylation, succinylation, and acetylation at functionally required lysine residues near its active site, K122 in particular bears all three modifications ((Tao et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Mass-spectrometry data has shown that there are an abundance of histone crotonylation sites in all four core histones22,40.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [40]
In the citing paper
“For example, SIRT5 exhibits efficient activity to lysine desuccinylation, demalonylation and glutarylation12-14”
From HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine (2016) · cites this paper as [14]
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Citations
Cites
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MethodThe metabolic and molecular bases of inherited disease
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Self-citationAMPK: a nutrient and energy sensor that maintains energy homeostasis
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“In addition to histones, PTM-regulatory enzymes, such as AMP-activated protein kinase (AMPK) and lysine deacetylases (KDACs or HDACs), can control activity of their substrates (Chalkiadaki and Guarente, 2012; Hardie et al., 2012), many of which are metabolic enzymes.”
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BackgroundInfluentialThe complex language of chromatin regulation during transcription
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“These PTM enzymes have important roles in modulation of chromatin structure and transcriptional regulation (Berger, 2007; Chi et al., 2010).”
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“For example, acetyl-CoA, SAM, NAD+, and a-ketoglutarate are donors/substrates or cofactors for histone lysine-modifying enzymes, i.e., those modulating levels of acetylation and methylation (Imai et al., 2000; Takahashi et al., 2006; Tsukada et al., 2006; Wellen et al., 2009).”
BackgroundHistone demethylation by a family of JmjC domain-containing proteins
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“For example, acetyl-CoA, SAM, NAD+, and a-ketoglutarate are donors/substrates or cofactors for histone lysine-modifying enzymes, i.e., those modulating levels of acetylation and methylation (Imai et al., 2000; Takahashi et al., 2006; Tsukada et al., 2006; Wellen et al., 2009).”
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Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
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Movement Disorders and Inherited Metabolic Disorders
(2020) · Cambridge University Press eBooks · doi:10.1017/9781108556767 · Cited by 6
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“…records of 9 novel modifications emerging in the recent years are also identified, including crotonylation [21], dopaminylation [22], glutarylation [23], β -hydroxybutyrylation [24], 2-hydroxyiso-Int butyrylation [25], lactylation [26], malonylation [27], succinylation [28], and UFMylation [29].”
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Lysine β-hydroxybutyrylation in metabolic plasticity and disease pathogenesis
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Self-citationThe role of acetylation in obesity-induced cardiac metabolic alterations
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“Some studies suggest that HATs, such as p300/CBP families, may shuttle between the nucleus and cytoplasm and regulate the cytoplasmic acetylation processes [63, 103, 104].”
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The Role of the Sirtuin Family Histone Deacetylases in Acute Myeloid Leukemia—A Promising Road Ahead
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Native chemical ligation approach to sensitively probe tissue acyl-CoA pools
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“1232 Cell Chemical Biology 29, 1232–1244, July 21, 2022 a 2022 The This is an open access article under the CC BY license (http://creative shown to generate N-linked modifications on lysines in vivo (Weinert et al., 2013; Peng et al., 2011; Tan et al., 2014).”
BackgroundQiao, N., Qi, Z., Wang, Y., Deng, A., & Chen, C. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac421 · Cited by 5
Umezawa, K., Tsumoto, H., Kawakami, K., & Miura, Y. (2022) · The Analyst · doi:10.1039/d2an01370c · Cited by 5
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“SIRT5 is primarily localized in the mitochondria and has been shown to orchestrate diverse metabolic processes through its multifaceted enzymatic activities, including the deacetylation [11], decarbonylation, desuc-cinylation [12], and deglutarylation [13] of key metabolic proteins.”
BackgroundHistone deacetylases: potential therapeutic targets in cisplatin-induced acute kidney injury
Guo, S., Zhao, J., Zhang, Y., Qin, Y., Yuan, J., Yu, Z., Xing, Y., Zhang, Y., Hui, Y., Wang, A., et al. (2024) · Annals of Medicine · doi:10.1080/07853890.2024.2418958 · Cited by 5
“SIRT5, as the exclusive sirtuin that prefers malonyllysine, glutaryllysine, and succinyllysine as substrates, primarily resides in mitochondria and is involved in various biological processes during cisplatin treatment, such as reactive oxygen defense, apoptosis, and fatty acid metabolism [74,75].”
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Analysis of Lysine Acetylation and Acetylation‐like Acylation In Vitro and In Vivo
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“…2007), butyrylation (Chen et al., 2007), crotonylation (Tan et al., 2011), 2-hydroxyisobutyrylation (Dai et al., 2014), malonylation (Xie et al., 2012), succinylation (Xie et al., 2012), glutarylation (Tan et al., 2014), benzoylation (Huang et al., 2018) and lactylation (Zhang et al., 2019) (Fig.”
BackgroundEvolvierte, selektive Eraser für spezifische Lysinacylierungen
Spinck, M., Neumann‐Staubitz, P., Ecke, M., Gasper, R., & Neumann, H. (2020) · Angewandte Chemie · doi:10.1002/ange.202002899 · Cited by 5
Glutarate regulates T cell function and metabolismPreprint
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“Glutarate in its CoA form, glutaryl-CoA, acts as a substrate for the recently discovered PTM glutarylation (Tan et al., 2014).”
BackgroundMethodInfluentialLipoyl deglutarylation by ABHD11 regulates mitochondrial and T cell metabolism
Grice, G. L., Minogue, E., Coates, H. W., Debela, M., Stopforth, R. J., Wit, N., Li, Z., Crowley, J. P., Kaser, A., Kaneider-Kaser, N., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01965-6 · Cited by 5
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Structural basis of SIRT2 pre-catalysis NAD + binding dynamics and mechanism
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Unveiling the importance of SIRT5 for cardiac health and disease in an era of increasing longevity
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Sirtuins and tumor immunity: mechanistic insights, immunotherapy prospects, and therapeutic horizons
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Histone lactylation: A sensor of epigenetic reprogramming mediated by cellular metabolism
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“SIRT3 functions as the primary mitochondrial deacetylase [226,234], while SIRT5 preferentially removes acidic acyl modifications, such as lysine malonyla-tion [235], succinylation [236], and glutarylation [237].”
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Revealing chromatin-specific functions of histone deacylases
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The crotonylated and succinylated proteins of jujube involved in phytoplasma-stress responses
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Self-citationMechanism-based inactivators of sirtuin 5: A focused structure–activity relationship study
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Self-citationCircadian Rhythms and Lung Cancer in the Context of Aging: A Review of Current Evidence
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“[4] This system is responsible for many aspects of the molecular function of cells, respiration system of cells, amino acid and fatty acid metabolism, etc. Abnormal glutarylation status also responsible for many diseases.”
BackgroundRajabi, N., Hansen, T. N., Nielsen, A. L., Nguyen, H. T., Bæk, M., Bolding, J. E., Bahlke, O. Ø., Petersen, S. E. G., Bartling, C. R. O., Strømgaard, K., et al. (2022) · Angewandte Chemie · doi:10.1002/ange.202115805 · Cited by 5
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“It is also stated diabetes, neurodegenerative diseases are also caused for glutarylation [8], [9].”
BackgroundGlutaric Acid Neurotoxicity: Mechanisms and Actions
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Roles for Sirtuins in Cardiovascular Biology
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Self-citationHuman SIRT5 variants with reduced stability and activity do not cause neuropathology in mice
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Self-citationThe metabolic profiles of cancer stem cells
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“About 20 different lysine acylations have been discovered, including acetylation [196, 197], propionylation [198], butyrylation [199], crotonylation [200], succinyl-ation [201], malonylation [202], and glutarylation [203].”
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Lysine acylation causes collateral damage in inborn errors of metabolism
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“Ongoing research has revealed a spectrum of modifications, including lactation, phosphorylation, methylation, propionylation, butyrylation, suc-cinylation, malonylation, glutarylation, and crotonylation 4–10 .”
BackgroundDecoding Ubiquitin Modifications by Mass Spectrometry
Gong, Y., & Dai, L. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-981-97-7288-9_1 · Cited by 3
Self-citationCharacterization of acidic lysine acylations in mycobacteria
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Self-citationDeacetylation by SIRT3 Relieves Inhibition of Mitochondrial Protein Function
Chhoy, P., Anderson, K. A., Hershberger, K. A., Huynh, F. K., Martin, A. S., McDonnell, E., Peterson, B. S., Starzenski, L. A., Backos, D. S., Fritz, K. S., et al. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_5 · Cited by 3
Self-citationCycling around Lysine Modifications
Kumar, S., & Lombard, D. B. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.05.006 · Cited by 3
“Although previous studies had demonstrated that inborn errors of metabolism can provoke altered cellular protein acylation [9, 10], the studies of Wagner et al.”
ResultSelf-citationMethods for studying human sirtuins with activity-based chemical probes
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“For example, in addition to being a weak deacetylase, SIRT5 also harbors robust desuccinylase, demalonylase, and deglutarylase activities (Du et al., 2011; Tan et al., 2014).”
BackgroundSirtuins and cellular metabolism in cancers
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“The transient nature and organ-specificity of protein glutarylation [1,6,10], potential competition between glutarylation and other modifications of lysine residues in proteins (acetylation, succinylation) [5–8,14,15] suggest glutarylation to be an important component of metabolic regulation.”
InfluentialReyes, A., Hatcher, J. D., Salazar, E., Galan, J. A., Iliuk, A. B., Sanchez, E. E., & Suntravat, M. (2023) · Toxins · doi:10.3390/toxins15070434 · Cited by 3
“It is known that Gcdh degrades glutaryl-CoA, thereby reducing the lysine glutarylation (Kglu) level of the protein [101].”
BackgroundLiu, X., Zhu, B. T., Dai, X.-W., Xu, Z.-A., Li, R., Qian, Y., Lu, Y., Zhang, W., Liu, Y. U., & Zheng, J. (2023) · BMC Genomics · doi:10.1186/s12864-023-09834-z · Cited by 3
“Lysine glutarylation (Kglu) was first reported by Tan et al. in 2014 [1], which refers to the process of covalently binding glutaryl groups (such as glutaryl-CoA and other donors) to lysine residues of substrate proteins under the catalysis of enzymes.”
BackgroundMethodDeep Learning and Blockchain Applications in Healthcare Sector Using Imaging Data
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Lithocholic acid targets TULP3 to activate sirtuins and AMPK to retard ageingPreprint
Qu, Q., Chen, Y., Wang, Y., Long, S., Wang, W., Yang, H.-Y., Wu, J., Li, M., Tian, X., Wei, X., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.07.570558 · Cited by 3
Self-citationSirt5 preserves cardiac function in ischemia-reperfusion injury by inhibiting ANT2 lactylationPreprint
Li, S., Shen, S., Hong, Y., Ding, K., Chen, S., Chen, J., Wang, C., Wen, Y., Mo, G., Yu, L., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.25.625148 · Cited by 3
Yokoyama, T., Takayama, Y., Mizuguchi, M., Nabeshima, Y., & Kusaka, K. (2024) · FEBS Letters · doi:10.1002/1873-3468.14961 · Cited by 2
Ju, Z., & Zhang, Q.-B. (2024) · Analytical Biochemistry · doi:10.1016/j.ab.2024.115715 · Cited by 2
Fadaei, R., Bernstein, A., Jenkins, A. N., Pickens, A. G., Zarrow, J. E., Alli-Oluwafuyi, A., Tallman, K. A., & Davies, S. S. (2025) · Journal of Lipid Research · doi:10.1016/j.jlr.2025.100831 · Cited by 2
Succinate reduces biological activity and mitochondrial function of human adipose-derived stem cells
Wang, B., Wang, X., Guo, M., & Xu, H. (2025) · Cell Cycle · doi:10.1080/15384101.2025.2508109 · Cited by 2
Mitochondrial sirtuins sir-2.2 and sir-2.3 regulate lifespan in C. elegans
Chang, S. M., Franklin, L. P., Sattar, S., Moro, C. A., DeGennaro, M. V., LaGanke, N. G., & Hanna‐Rose, W. (2025) · Genetics · doi:10.1093/genetics/iyaf185 · Cited by 2
Protein crotonylation in cancer: mechanisms, functions, and therapeutic potential
Han, F., Shen, W., Zhang, X., Du, M., Ye, Q., Ma, J., & Hu, L.-P. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-025-10130-7 · Cited by 2
Zhu, Z., Mao, P.-Z., Tarn, C., & Cao, Y. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01826-2 · Cited by 2
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Ion Mobility Separation of Isomeric Acyl-lysine Marks in Peptides
Berthias, F., Bilgin, N., Cooper-Shepherd, D. A., Hammami, N., Langridge, J., Mecinović, J., & Jensen, O. N. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c06460 · Cited by 3
The neuropathological mechanisms underlying the inborn errors of lysine metabolism
Guo, Y., Wu, J., & Guo, W. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107315 · Cited by 2
Wang, P., Li, Y., He, Z., Duan, X., He, L., Wang, P., Pan, C., Xu, L., Ma, X., Chen, T., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c20947 · Cited by 3
An Update on the Role of Sirtuins in the Prevention of the Aging Process: A Narrative Review
Lucà, F., Fioravanti, L., Scevola, S., Arpino, A., Saler, M., & Nicoletti, G. J. (2026) · Journal of Gerontology and Geriatrics · doi:10.3390/jgg74010006 · Cited by 2
“In humans, the sirtuin family comprises seven isoforms (SIRT1–SIRT7), each with specific substrate preferences and primarily, but not exclusively, localized in the nucleus (SIRT1, SIRT6, and SIRT7), cytoplasm (SIRT2), and mitochondria (SIRT3, SIRT4, and SIRT5) [4,6,17–22].”
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Wu, M., Tan, J. Y., Zhou, W., Zhang, Z., Gao, Q., Cai, Y., Liao, G., Cao, Z., Zeng, C.-R., Zhang, Y., et al. (2026) · Circulation · doi:10.1161/circulationaha.125.077756 · Cited by 2
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Self-citationThe Sirtuin Network: Linking NAD + Metabolism, Mitochondrial Function, and Metabolic Homoeostasis
Szczęsny-Małysiak, E., Schiavoni, V., Rotondo, R., Zeppa, S. D., Vignini, A., Moriconi, E., Cecati, M., Armani, A., Gorini, S., Campagna, R., et al. (2026) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.70201 · Cited by 3
“These post‐translational modifications affect key pathways such as fatty acid oxidation, the tricarboxylic acid cycle, and mitochondrial respiration, thereby supporting lipid metabolic homoeostasis [74, 75].”
Sirtuin 5 is Dispensable for CD8+ T Cell Effector and Memory Differentiation
Duan, Q., Ding, J., Li, F., Liu, X., Zhao, Y., Yu, H., Liu, Y. U., & Zhang, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.761193 · Cited by 2
“Sirtuin 5 (SIRT5) is a unique member amongst the seven sirtuins, because it not only has deacetylase activity but also possesses stronger demalonylase, desuccinylase, and deglutarylase functions (Du et al., 2011; Tan et al., 2014; Wang et al., 2017; Kumar and Lombard, 2018).”
BackgroundSelf-citationReversing the charge of lysine by genetic code expansion
Danková, D., & Olsen, C. A. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01536-7 · Cited by 2
Self-citationMass spectrometry-based technologies for histone PTM analysis and novel PTM discovery
Chen, K., Zhao, W., Zhang, J., Zhao, S., Li, H., & Tan, M. (2025) · Scientia Sinica Chimica · doi:10.1360/ssc-2025-0043 · Cited by 2
Self-citationAlmusawi, M., Bhatt, N., Kaur, K., Kumar, A., Kishore, V. R., & Kandpal, V. (2024) · International Conference on Communication, Computing and Energy Efficient Technologies (I3CEET) · doi:10.1109/i3ceet61722.2024.10993866 · Cited by 2
Global Profiling of Protein β-hydroxybutyrylome in Porcine Liver
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Byrne, N. J., Koentges, C., Pfeil, K., Lueg, J. C., Bakshi, S., Tarkhnishvili, A., Vosko, I., Gollmer, J., Birkle, L. C., Rathner, T., et al. (2025) · Acta Physiologica · doi:10.1111/apha.70120 · Cited by 2
“Whereas SIRT3 has primarily deacetylase activity [3], SIRT5 is shown to remove other acyl groups from lysine residues, particularly malonyl [4], suc-cinyl [5] and glutaryl [6].”
Acylated peptide enrichment utilizing lysine deacylases for lysine acylomics
Tsumagari, K., & Ishihama, Y. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.05.077 · Cited by 2
Glutaric Acid Neurotoxicity: Mechanisms and Actions
Amaral, A. U., Ferreira, G. C., Seminotti, B., Leipnitz, G., & Wajner, M. (2022) · Springer eBooks · doi:10.1007/978-3-031-15080-7_186 · Cited by 3
Protein Lysine Acylation: Abundance, Dynamics and Function
Pougovkina, O., & de Boer, V. C. J. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_3 · Cited by 2
Dual role of sirtuins in cancer
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Epigenetic role of sirtuins in neurodegenerative brain disorders
Khanna, A., Anamika, A., & Trigun, S. K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814118-2.00009-4 · Cited by 3
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Qiao, N., & Qi, Z. (2024) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2024.109328 · Cited by 4
The Controversy Around Sirtuins and Their Functions in Aging
Sun, Y., & Dang, W. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801816-3.00017-0 · Cited by 2
Identification of Histone Lysine Glutarylation
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Predicting Lysine Glutarylation Sites by Combining Multiple Feature Selection Methods
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“A total of 3115 features were constructed with the aggregate of AAF, BE, and CKSAAP encoding methods.”
MethodInfluentialMitochondrial sirtuins at the crossroads of energy metabolism and oncogenic transformation
Grabacka, M., & Plonka, P. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00001-2 · Cited by 3
Sirtuins, mitochondria, and exercise in health and disease
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The bifunctional roles of sirtuins and their therapeutic potential in cancer
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Regulation of urea cycle related enzymes in response to freezing in the wood frog, Rana sylvatica
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Deglutarylation of GCDH by SIRT5 controls lysine metabolism in micePreprint
Bhatt, D. P., Mills, C. A., Anderson, K. A., Henriques, B. J., Lucas, T. G., Francisco, S., Liu, J., Ilkayeva, O., Adams, A. E., Kulkarni, S. R., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.28.176677 · Cited by 2
“We previously showed that mice lacking SIRT5 have hyperglutarylated mitochondrial proteins (9), which play a key role in regulating the enzyme CPS1 in ammonia detoxification and the urea cycle (10).”
BackgroundSelf-citationNielsen, A. L., Rajabi, N., Kudo, N., Larsen, K. L., Fontenas, M., Lucidi, A., Madsen, A. S., Yoshida, M., & Olsen, C. A. (2020) · Research at the University of Copenhagen (University of Copenhagen) · doi:10.1101/2020.03.20.000380 · Cited by 2
Self-citation
Metadata
- Authors
- Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., Ro, J., Wagner, G. R., Green, M. F., Madsen, A. S., Schmiesing, J., Peterson, B. S., Xu, G., Ilkayeva, O. R., Muehlbauer, M. J., Braulke, T., Mühlhausen, C., Backos, D. S., Olsen, C. A., McGuire, P. J., Pletcher, S. D., Lombard, D. B., Hirschey, M. D., & Zhao, Y.
- Affiliations
- Chinese Academy of Sciences (CN)
- University of Chicago (US)
- Duke University (US)
- University of Michigan (US)
- Technical University of Denmark (DK)
- University Medical Center Hamburg-Eppendorf (DE)
- University of Colorado Anschutz (US)
- National Institutes of Health (US)
- Corresponding author
- Hirschey, Matthew D.
- Zhao, Yingming
- ORCID
- Tan, Minjia
- Peng, Chao
- Chhoy, Peter
- Xie, Zhongyu
- Dai, Lunzhi
- Huang, He
- Zhang, Yi
- Ro, Jennifer
- Green, Michelle F.
- Madsen, Andreas S.
- Xu, Guofeng
- Ilkayeva, Olga R.
- Muehlbauer, Michael J.
- Braulke, Thomas
- Mühlhausen, Chris
- Backos, Donald S.
- Olsen, Christian A.
- McGuire, Peter J.
- Pletcher, Scott D.
- Lombard, David B.
- Hirschey, Matthew D.
- Zhao, Yingming
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2014-04
- Volume
- 19
- Issue
- 4
- Pages
- 605-617
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4108075
- OpenAlex
- W2088511656
- Cited by
- 844
- References
- 45
- Citations by year
- 2026: 49 · 2025: 63 · 2024: 86 · 2023: 50 · 2022: 79 · 2021: 106 · 2020: 67 · 2019: 74 · 2018: 80 · 2017: 53 · 2016: 70 · 2015: 50 · 2014: 16
- FWCI
- 32.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) (submittedVersion)
- Funders
- Lundbeckfonden (R52-2010-5054)
- National Institutes of Health (UL1TR000430)
- National Institute on Alcohol Abuse and Alcoholism (AA022146, R01AA022146)
- National Institute on Aging (F31AG047696, R01AG045351, AG045351, P30AG013283, T32AG000114)
- National Cancer Institute (R21CA177925, CA160036, CA059365-19, U24CA160036, T32CA059365, CA177925)
- National Institute of General Medical Sciences (GM105933, T32GM007105, GM101171, T32GM007315, R01GM101171, R01GM105933)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK096493, P30DK020572)
- National Center for Research Resources (RR020839, U54RR020839)
- National Center for Advancing Translational Sciences
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- SIRT5, protein posttranslational modification, urea cycle, glutaric aciduria type I, glutaryl-CoA, mitochondrial proteins, metabolic enzymes
- MeSH terms
- Acyl Coenzyme A, Animals, Carbamoyl-Phosphate Synthase (Ammonia), Lysine, Models, Biological, Protein Processing, Post-Translational, Mass Spectrometry, Immunoblotting, Molecular Structure, Sirtuins, Proteomics, Mice
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