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Biotin starvation causes mitochondrial protein hyperacetylation and partial rescue by the SIRT3-like deacetylase Hst4p

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Sirtuin 3 (SIRT3) Regulates α-Smooth Muscle Actin (α-SMA) Production through the Succinate Dehydrogenase-G Protein-coupled Receptor 91 (GPR91) Pathway in Hepatic Stellate Cells

Li, Y. H., Choi, D. H., Lee, E. H., Seo, S. R., Lee, S., & Cho, E.-H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.692244 · Cited by 62 · see citing works

Gestational Leucylation Suppresses Embryonic T‐Box Transcription Factor 5 Signal and Causes Congenital Heart Disease

Zhang, X., Liu, L., Chen, W., Wang, F., Cheng, Y., Liu, Y., Lai, Y., Zhang, R., Qiao, Y., Yuan, Y.-Y., et al. (2022) · Advanced Science · doi:10.1002/advs.202201034 · Cited by 61 · see citing works

Acetate as a Metabolic and Epigenetic Modifier of Cancer Therapy

Jaworski, D. M., Namboodiri, A. M. A., & Moffett, J. R. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25305 · Cited by 63 · see citing works

Metabolic changes associated with the long winter fast dominate the liver proteome in 13-lined ground squirrels

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Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis

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Metabolic inflexibility and protein lysine acetylation in heart mitochondria of a chronic model of Type 1 diabetes

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Dysregulation of mitochondrial function and biogenesis modulators in adipose tissue of obese children

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Early mitochondrial dysfunction in glycolytic muscle, but not oxidative muscle, of the fructose-fed insulin-resistant rat

Warren, B. E., Lou, P., Lucchinetti, E., Zhang, L., Clanachan, A. S., Affolter, A., Hersberger, M., Zaugg, M., & Lemieux, H. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00511.2013 · Cited by 55 · see citing works

Mitochondrial Dynamics Is Linked to Longevity and Protects from End-Organ Injury: The Emerging Role of Sirtuin 3

Benigni, A., Perico, L., & Macconi, D. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6682 · Cited by 58 · see citing works

Targeting a Sirt5-Positive Subpopulation Overcomes Multidrug Resistance in Wild-Type Kras Colorectal Carcinomas

Du, Z., Liu, X., Chen, T., Gao, W., Wu, Z., Hu, Z., Wei, D., Gao, C., & Li, Q. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.037 · Cited by 56 · see citing works

Emerging Metabolic Therapies in Pulmonary Arterial Hypertension

Harvey, L. D., & Chan, S. Y. (2017) · Journal of Clinical Medicine · doi:10.3390/jcm6040043 · Cited by 56 · see citing works

Myricetin Exerts Anti-Obesity Effects through Upregulation of SIRT3 in Adipose Tissue

Akindehin, S., Jung, Y.-S., Kim, S.-N., Son, Y.-H., Lee, I., Seong, J. K., Jeong, H. W., & Lee, Y.-H. (2018) · Nutrients · doi:10.3390/nu10121962 · Cited by 56 · see citing works

Nicotinamide Phosphoribosyl Transferase (Nampt) Is Required for De Novo Lipogenesis in Tumor Cells

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SIRT3 controls brown fat thermogenesis by deacetylation regulation of pathways upstream of UCP1

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Advances in characterization of SIRT3 deacetylation targets in mitochondrial function

Wang, S., Zhang, J., Deng, X., Zhao, Y., & Xu, K. (2020) · Biochimie · doi:10.1016/j.biochi.2020.08.021 · Cited by 53 · see citing works

Aberrant methylmalonylation underlies methylmalonic acidemia and is attenuated by an engineered sirtuin

Head, P. E., Myung, S., Chen, Y., Schneller, J. L., Wang, C., Duncan, N., Hoffman, P., Chang, D., Gebremariam, A., Gucek, M., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn4772 · Cited by 52 · see citing works

Minocycline reduces inflammatory response and cell death in a S100B retina degeneration model

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NAD + acts on mitochondrial SirT3 to prevent axonal caspase activation and axonal degeneration

Magnifico, S., Saïas, L., Deleglise, B., Duplus, E., Kilinc, D., Miquel, M., Viovy, J., Brugg, B., & Peyrin, J. (2013) · The FASEB Journal · doi:10.1096/fj.13-229781 · Cited by 51 · see citing works

Epigenetic Regulation of Metabolism and Inflammation by Calorie Restriction

Hernández‐Saavedra, D., Moody, L., Xu, G. B., Chen, H., & Pan, Y. (2018) · Advances in Nutrition · doi:10.1093/advances/nmy129 · Cited by 51 · see citing works

Exogenous H2S reduces the acetylation levels of mitochondrial respiratory enzymes via regulating the NAD+-SIRT3 pathway in cardiac tissues of db/db mice

Sun, Y., Teng, Z., Sun, X., Zhang, L., Chen, J., Wang, B., Lu, F., Liu, N., Yu, M., Peng, S., et al. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00326.2018 · Cited by 46 · see citing works

Mitochondrion as a Target for Heart Failure Therapy – Role of Protein Lysine Acetylation –

Lee, C. F., & Tian, R. (2015) · Circulation Journal · doi:10.1253/circj.cj-15-0742 · Cited by 44 · see citing works

Multi-targeted Effect of Nicotinamide Mononucleotide on Brain Bioenergetic Metabolism

Klimova, N., & Kristián, T. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02729-0 · Cited by 42 · see citing works

Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective

Lammers, M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.757179 · Cited by 41 · see citing works

Sirtuins as modifiers of Parkinson's disease pathology

Tang, B. L. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23806 · Cited by 40 · see citing works

Acetylation of conserved lysines fine‐tunes mitochondrial malate dehydrogenase activity in land plants

Balparda, M., Elsässer, M., Badia, M. B., Giese, J., Bovdilova, A., Hüdig, M., Reinmuth, L., Eirich, J., Schwarzländer, M., Finkemeier, I., et al. (2021) · The Plant Journal · doi:10.1111/tpj.15556 · Cited by 38 · see citing works

Post-translational modifications by SIRT3 de-2-hydroxyisobutyrylase activity regulate glycolysis and enable nephrogenesis

Perico, L., Morigi, M., Pezzotta, A., Corna, D., Brizi, V., Conti, S., Zanchi, C., Sangalli, F., Trionfini, P., Buttò, S., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-03039-8 · Cited by 40 · see citing works

Bovine serum albumin and skim-milk improve boar sperm motility by enhancing energy metabolism and protein modifications during liquid storage at 17 °C

Fu, J., Li, Y., Wang, L., Zhen, L., Yang, Q., Li, P., & Li, X. (2017) · Theriogenology · doi:10.1016/j.theriogenology.2017.07.020 · Cited by 39 · see citing works

New insights into the pathophysiology of methylmalonic acidemia

Head, P. E., Meier, J. L., & Venditti, C. P. (2023) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12617 · Cited by 40 · see citing works

Relevance of a Hypersaline Sodium-Rich Naturally Sparkling Mineral Water to the Protection against Metabolic Syndrome Induction in Fructose-Fed Sprague-Dawley Rats: A Biochemical, Metabolic, and Redox Approach

Pereira, C., Severo, M., Araújo, J. R., Guimarães, J. T., Pestana, D., Santos, A., Ferreira, R. M., Ascensão, A. A. M. R., Magalhães, J., Azevedo, I., et al. (2014) · International Journal of Endocrinology · doi:10.1155/2014/384583 · Cited by 38 · see citing works

Sirtuin-3 (SIRT3) protects pancreatic β-cells from endoplasmic reticulum (ER) stress-induced apoptosis and dysfunction

Zhang, H., Ma, X., Wu, L., Zhao, Y., Zhang, P.-Y., Zhang, Y., Shao, M., Liu, F., Li, F., & Qin, G.-J. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2771-5 · Cited by 36 · see citing works

Sirtuins as emerging anti-parasitic targets

Zheng, W. (2012) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.11.014 · Cited by 37 · see citing works

Post-translational Acetylation Control of Cardiac Energy Metabolism

Ketema, E. B., & Lopaschuk, G. D. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.723996 · Cited by 37 · see citing works

Mito-Nuclear Communication in Hepatocellular Carcinoma Metabolic Rewiring

Mello, T., Simeone, I., & Galli, A. (2019) · Cells · doi:10.3390/cells8050417 · Cited by 33 · see citing works

Androgen-Regulated Cardiac Metabolism in Aging Men

Barrientos, G. C., Llanos, P., Basualto-Alarcón, C., & Estrada, M. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00316 · Cited by 34 · see citing works

In Utero Alcohol Exposure and the Alteration of Histone Marks in the Developing Fetus: An Epigenetic Phenomenon of Maternal Drinking

Mandal, C., Halder, D., Jung, K. H., & Chai, Y. G. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.21047 · Cited by 31 · see citing works

Mitochondrial Protein Acylation and Intermediary Metabolism: Regulation by Sirtuins and Implications for Metabolic Disease

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

Chapter 8 Acetylation of Mitochondrial Proteins

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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

Mitochondrial sirtuins: regulators of protein acylation and metabolism

He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology &amp; Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262 · see citing works

SIRT3, a pivotal actor in mitochondrial functions: metabolism, cell death and aging

Giralt, A., & Villarroya, F. (2012) · Biochemical Journal · doi:10.1042/bj20120030 · Cited by 253 · see citing works