Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling

UCSF Chimera—A visualization system for exploratory research and analysis

Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047

Oxidants, oxidative stress and the biology of ageing

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Aging: a theory based on free radical and radiation chemistry

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AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

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A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine

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Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160

Mammalian Sirtuins: Biological Insights and Disease Relevance

Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085

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

Regulation of cellular metabolism by protein lysine acetylation

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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

Tetradecylthioacetic Acid Attenuates Inflammation and Has Antioxidative Potential During Experimental Colitis in Rats

Bjørndal, B., Grimstad, T., Cacabelos, D., Nylund, K., Aasprong, O. G., Omdal, R., Portero-Otín, M., Pamplona, R., Lied, G., Hausken, T., et al. (2012) · Digestive Diseases and Sciences · doi:10.1007/s10620-012-2321-2 · Cited by 15

Genetically Encoded Near-Infrared Photocatalysis for Proximity Labeling of Subcellular Proteome

Ren, T., Gong, J., Zheng, F., Long, J., Wang, H., He, J., Jiang, J., & Zou, P. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c01826 · Cited by 14

Discovery and characterization of small molecule SIRT3-specific inhibitors as revealed by mass spectrometry

Loharch, S., Chhabra, S., Kumar, A., Swarup, S., & Parkesh, R. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104768 · Cited by 14

The Role of Mitochondrial Metabolism, AMPK-SIRT Mediated Pathway, LncRNA and MicroRNA in Osteoarthritis

Liu, H.-Y., Chang, C., Lu, C., Wu, S., Huang, B., Cheng, T., Lin, S., Ho, C.-J., Lee, M., Yang, C., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10071477 · Cited by 15

Longitudinal in vivo metabolic labeling reveals tissue-specific mitochondrial proteome turnover rates and proteins selectively altered by parkin deficiency

Stauch, K. L., Totusek, S., Trease, A. J., Estrella, L. D., Emanuel, K. M., Fangmeier, A., & Fox, H. S. (2023) · Scientific Reports · doi:10.1038/s41598-023-38484-0 · Cited by 15

Colonic ketogenesis, a microbiota-regulated process, contributes to blood ketones and protects against colitis in mice

Bass, K. N., Sivaprakasam, S., Dharmalingam-Nandagopal, G., Thangaraju, M., & Ganapathy, V. (2024) · Biochemical Journal · doi:10.1042/bcj20230403 · Cited by 14

Grass carp (Ctenopharyngodon idella) SIRT3 enhances MAVS-mediated antiviral innate immunity in response to GCRV infection

Zhu, C., Liu, W., Jia, S., Sun, X., Wang, Z., Deng, H., Bai, Y., Xiao, W., & Liu, X. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.740871 · Cited by 13

Discovery of a novel small-molecule activator of SIRT3 that inhibits cell proliferation and migration by apoptosis and autophagy-dependent cell death pathways in colorectal cancer

Mou, Y., Chen, Y., Fan, Z., Ye, L., Hu, B., Han, B., & Wang, G. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107327 · Cited by 14

Regulated Cell Death Pathways in Pathological Cardiac Hypertrophy

Wu, S., Ding, D., & Wang, D. (2024) · Reviews in Cardiovascular Medicine · doi:10.31083/j.rcm2510366 · Cited by 14

Investigating the role of Sirtuins in cell reprogramming

Shin, J., Kim, J., Park, H., & Kim, J. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.10.172 · Cited by 14

Comparative transcriptome analysis in Chinese cabbage (Brassica rapa ssp. pekinesis) for DEGs of Ogura-, Polima-CMS and their shared maintainer

Wei, X., Lv, Y., Zhao, Y., Nath, U. K., Yuan, Y., Wang, Z., Yang, S., Jia, H., Wei, F., & Zhang, X. (2020) · Physiology and Molecular Biology of Plants · doi:10.1007/s12298-020-00775-5 · Cited by 14

Independent and additive effects of atenolol and methionine restriction on lowering rat heart mitochondria oxidative stress

Sánchez-Román, I., Gómez, A. G., Naudí, A., Jové, M., Gómez, J., Lopez‐Torres, M., Pamplona, R., & Barja, G. (2013) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-013-9535-7 · Cited by 14

A narrative review of the roles of the miR-15/107 family in heart disease: lessons and prospects for heart disease

Zheng, M.-N., & Wang, M. (2021) · Annals of Translational Medicine · doi:10.21037/atm-20-6073 · Cited by 13

Transcriptomic signals of mitochondrial dysfunction and OXPHOS dynamics in fast-growth chicken

Hubert, S. M., & Athrey, G. (2022) · PeerJ · doi:10.7717/peerj.13364 · Cited by 13

Elucidating the Role of Sirtuin 3 in Mammalian Oocyte Aging

Kordowitzki, P. (2024) · Cells · doi:10.3390/cells13181592 · Cited by 13

Changes in SIRT gene expression during odontoblastic differentiation of human dental pulp cells

Jang, Y.-E., Go, S.-H., Lee, B.-N., Chang, H.-S., Hwang, I., Oh, W., & Hwang, Y. (2015) · Restorative Dentistry & Endodontics · doi:10.5395/rde.2015.40.3.223 · Cited by 13

The effect of caloric restriction on genetical pathways

Karagöz, M. F., & Celep, G. S. (2023) · Food Science and Human Wellness · doi:10.1016/j.fshw.2023.02.007 · Cited by 15

New insights toward molecular and nanotechnological approaches to antidiabetic agents for Alzheimer’s disease

Pradhan, S. P., Sahu, P. K., & Behera, A. (2023) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-023-04696-1 · Cited by 14

Spermidine Enhances Mitochondrial Function and Mitigates Aortic Valve Calcification

Song, N., Ji, E., Yu, J. E., Choi, K., Kim, D., Song, J., Kang, D., Song, J., Yu, J., Kim, K., et al. (2025) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2024.11.011 · Cited by 12

Apple pomace and rosemary extract ameliorates hepatic steatosis in fructose-fed rats: Association with enhancing fatty acid oxidation and suppressing inflammation

Bai, R., Yuan, C., Wang, T., Liu, L., Li, J., Lai, Y., Li, H., Chen, Z., Li, C., Ke, D., et al. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8910 · Cited by 12

The Mitochondrial Italian Human Proteome Project Initiative (mt-HPP)

Urbani, A., & Canio, M. D. (2013) · Molecular BioSystems · doi:10.1039/c3mb70065h · Cited by 12

Hypoxia reverses the early anti-inflammatory microglial response to the β-amyloid peptide: mitochondrial involvement and beneficial roles of melatonin and naringenin

Lipari, C. L. R., Patti, A., Nibali, S. C., Messina, A. A., Magrì, A., Sortino, M. A., & Merlo, S. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07044-7 · Cited by 12

AAV-mediated upregulation of VDAC1 rescues the mitochondrial respiration and sirtuins expression in a SOD1 mouse model of inherited ALS

Magrì, A., Lipari, C. L. R., Caccamo, A., Battiato, G., Nibali, S. C., Pinto, V. D., Guarino, F., & Messina, A. A. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01949-w · Cited by 11

The role of mitochondrial remodeling in neurodegenerative diseases

Guan, D., Liang, C., Zheng, D., Liu, S., Luo, J., Cai, Z., Zhang, H., & Chen, J. (2025) · Neurochemistry International · doi:10.1016/j.neuint.2024.105927 · Cited by 11

SIRT3 deficiency reduces PFKFB3-driven T-cell glycolysis and promotes arthritic inflammation

Wang, T., Han, T., Xiao, X., Guo, D., Sun, X., Liu, Y., Zhao, L., Xu, H., Li, R., Jiang, L., et al. (2025) · Science China Life Sciences · doi:10.1007/s11427-024-2823-2 · Cited by 12

Cryptotanshinone attenuates lactate-induced nucleus pulposus cells injury by modulating the STAT3/SIRT3 signaling axis

Lu, J.-J., Zhang, Q., Chen, Y., Yuan, G.-C., Huang, Y.-K., Wu, T., Zhang, Q., Dong, J., Jiang, L., & Li, X. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157021 · Cited by 11

Proteomic Changes in the Monolayer and Spheroid Melanoma Cell Models of Acquired Resistance to BRAF and MEK1/2 Inhibitors

Martinez, R., Huang, W., Buck, H., Rea, S., Defnet, A. E., Kane, M. A., & Shapiro, P. (2022) · ACS Omega · doi:10.1021/acsomega.1c05361 · Cited by 11

Hyperglycemia induced C2C12 myoblast cell cycle arrest and skeletal muscle atrophy by modulating sirtuins gene expression in rats

Surinlert, P., Thitiphatphuvanon, T., Khimmaktong, W., Pholpramool, C., & Tipbunjong, C. (2021) · Polish Journal of Veterinary Sciences · doi:10.24425/pjvs.2021.139981 · Cited by 11

Effects of Deacetylase Inhibition on the Activation of the Antioxidant Response and Aerobic Metabolism in Cellular Models of Fanconi Anemia

Bertola, N., Regis, S., Bruno, S., Mazzarello, A. N., Serra, M., Lupia, M., Sabatini, F., Corsolini, F., Ravera, S., & Cappelli, E. (2023) · Antioxidants · doi:10.3390/antiox12051100 · Cited by 11

Mitochondrial dysfunction is implicated in retinoic acid‐induced spina bifida aperta in rat fetuses

Xue, J., Gu, H., Liu, D., Ma, W., Wei, X., Zhao, L., Liu, Y., Zhang, C., & Yuan, Z. (2018) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2018.04.003 · Cited by 11

Mitochondrial Sirt3 serves as a biomarker for sepsis diagnosis and mortality prediction

Liu, J., Zhou, G., Chen, R., Tong, Z., Zhang, H., Wang, X., & Liu, D. (2022) · Scientific Reports · doi:10.1038/s41598-022-14365-w · Cited by 11

Characterization of novel mechanisms for steatosis from global protein hyperacetylation in ethanol-induced mouse hepatocytes

Kim, S., Kwon, O. K., Ki, S. H., Jeong, T. C., & Lee, S. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.04.154 · Cited by 11

Molecular Characterization of PGC-1β (PPAR Gamma Coactivator 1β) and its Roles in Mitochondrial Biogenesis in Blunt Snout Bream (Megalobrama amblycephala)

Lu, K., Policar, T., Song, X., & Rahimnejad, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21061935 · Cited by 11

Sirt3 promotes hepatocellular carcinoma cells sensitivity to regorafenib through the acceleration of mitochondrial dysfunction

Wang, R., Liu, Y., Mi, X., Chen, Q., Jiang, P., Hou, J., Lin, Y., Li, S., Ji, B., & Fang, Y. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108415 · Cited by 11

Emerging regulatory roles of mitochondrial sirtuins on pyruvate dehydrogenase complex and the related metabolic diseases: Review

Nasiri, A., Sadeghi, M., Vaisi‐Raygani, A., Kiani, S., Aghelan, Z., & Khodarahmi‬, R. (2020) · Biomedical Research and Therapy · doi:10.15419/bmrat.v7i2.591 · Cited by 11

Pistacia lentiscus extract enhances mammary epithelial cells’ productivity by modulating their oxidative status

Hadaya, O., Bransi-Nicola, R., Shalev, Y., Azaizeh, H., Roth, Z., Muklada, H., Deutch, T., Landau, S. Y., & Argov-Argaman, N. (2020) · Scientific Reports · doi:10.1038/s41598-020-78065-z · Cited by 10

SIRT4 regulates rat dental papilla cell differentiation by promoting mitochondrial functions

Chen, H., Kang, J., Zhang, F., Yan, T., Fan, W., He, H., & Huang, F. P. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.105962 · Cited by 10

Mitochondrial Effects in the Liver of C57BL/6 Mice by Low Dose, High Energy, High Charge Irradiation

Barnette, B. L., Yu, Y., Ullrich, R. L., & Emmett, M. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111806 · Cited by 10

Overexpression of SIRT3 disrupts mitochondrial proteostasis and cell cycle progression

Wang, X., Tang, H., Chen, Y., Chi, B., Wang, S., Lv, Y., Wu, D., Ge, R., & Deng, H. (2016) · Protein & Cell · doi:10.1007/s13238-016-0251-z · Cited by 10

Label-free quantitative proteomic analysis of M. longissimus dorsi from cattle during dietary restriction and subsequent compensatory growth

Mullins, Y., Keogh, K. A., Kenny, D. A., Kelly, A. K., Boyle, P. O., & Waters, S. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-59412-6 · Cited by 9

Activation of Sirtuin 2 Inhibitors Employing Photoswitchable Geometry and Aqueous Solubility

Grathwol, C. W., Wössner, N., Behnisch‐Cornwell, S., Schulig, L., Zhang, L., Einsle, O., Jung, M., & Link, A. (2020) · ChemMedChem · doi:10.1002/cmdc.202000148 · Cited by 10

Combination of sirtuin 3 and hyperoxia diminishes tumorigenic properties of MDA-MB-231 cells

Podgorski, I. I., Pinterić, M., Marčinko, D., Hadžija, M. P., Filić, V., Ciganek, I., Pleše, D., Balog, T., & Sobočanec, S. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117812 · Cited by 10

Multi-Omics Comparison of the Spontaneous Diabetes Mellitus and Diet-Induced Prediabetic Macaque Models

Yang, Z., Yang, D., Tan, F., Wong, C. W., Yang, J. Y., Zhou, D., Cai, Z., & Lin, S. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.784231 · Cited by 10

SGLT2 inhibitors: how do they affect the cardiac cells

Erdoğan, B. R., & Arioglu‐Inan, E. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05084-z · Cited by 9

Targeting the SIRT3/MnSOD and JNK/HMGB1/Beclin 1 Axes: Role of Apigenin in Multifaceted Metabolic Intervention in Colorectal Cancer

Abdelmaksoud, N. M., Abulsoud, A. I., Abdelghany, T. M., Elshaer, S. S., Samaha, A., Maurice, N. W., Rizk, S. M., & Senousy, M. A. (2024) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70095 · Cited by 9

Nano-Drug Delivery System Targeting the Oxidative Stress Microenvironment: A Prospective Strategy for Intervertebral Disc Degeneration Treatment

Wang, Y., Wen, P., Zhang, B.-F., Hu, S., & Yang, Z. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s529127 · Cited by 9

Sirtuins in Brain and Neurodegenerative Disease

Szegő, É. M., Outeiro, T. F., & Kazantsev, A. G. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00013-7 · Cited by 9

MGARP is ultrastructurally located in the inner faces of mitochondrial membranes

Zhang, S. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.06.028 · Cited by 9

Diisononyl Phthalate Differentially Affects Sirtuin Expression in the HepG2 Cell Line

Gutiérrez-García, A. K., Choudhury, M., & León‐Rodríguez, A. D. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00206 · Cited by 9

LncRNA DLEU2 regulates sirtuins and mitochondrial respiratory chain complex IV: a novel pathway in obesity and offspring’s health

Zhang, J., Kay, M., Park, M. H., Meruvu, S., Powell, C. A., & Choudhury, M. (2022) · International Journal of Obesity · doi:10.1038/s41366-022-01075-6 · Cited by 9

Molecular genetic mechanisms of teratozoospermia

Chang, Y., Jiang, X., Liu, W., Zhang, D., Yang, S., & Zhao, D. (2023) · Zygote · doi:10.1017/s0967199422000594 · Cited by 9

PGC1α is required for the induction of contact inhibition by suppressing ROS

Yang, S., Hwang, S., Jang, J., Kim, M., Gwak, J., & Jeong, S. M. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.05.059 · Cited by 9

Training state and fasting-induced PDH regulation in human skeletal muscle

Gudiksen, A., Bertholdt, L., Stankiewicz, T., Villesen, I. F., Bangsbo, J., Plomgaard, P., & Pilegaard, H. (2018) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-018-2164-6 · Cited by 9

Dicationic π-conjugated triphenylamine fluorescent ligands target mitochondrial DNA G‑quadruplexes and inhibit triple-negative breast cancer growth

Wang, X.-D., Li, Z.-M., Liu, X.-Z., & Hu, M.-H. (2025) · Sensors and actuators. B, Chemical · doi:10.1016/j.snb.2025.138696 · Cited by 9

Role of NAD+ and FAD in Ischemic Stroke Pathophysiology: An Epigenetic Nexus and Expanding Therapeutic Repertoire

Narne, P., & Phanithi, P. B. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01287-4 · Cited by 9

Unveiling the dynamics of acetylation and phosphorylation in SGBS and 3T3-L1 adipogenesis

Aldehoff, A. S., Karkossa, I., Goerdeler, C., Krieg, L., Schor, J., Engelmann, B., Wabitsch, M., Landgraf, K., Hackermüller, J., Körner, A., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109711 · Cited by 8

Sirtuin 3 drives sex-specific responses to age-related changes in mouse embryonic fibroblasts

Šimunić, E., Podgorski, I. I., Pinterić, M., Hadžija, M. P., Belužić, R., Paradžik, M., Dončević, L., Balog, T., Kaloper, M., Habisch, H., et al. (2024) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2024.111996 · Cited by 8

Mitochondria Lysine Acetylation and Phenotypic Control

Ciregia, F. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8367-0_4 · Cited by 8

Nutraceuticals for Promoting Longevity

Pavlović, I., Khateb, S., Milisav, I., & Mahajna, J. A. (2020) · Current Nutraceuticals · doi:10.2174/2665978601666200213121512 · Cited by 8

Bone marrow-derived humoral factors suppress oxidative phosphorylation, upregulate TSG-6, and improve therapeutic effects on liver injury of mesenchymal stem cells

Miyaji, T., Takami, T., Fujisawa, K., Matsumoto, T., Yamamoto, N., & Sakaida, I. (2020) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.19-125 · Cited by 8

Physiological profile regulation during weight gain and loss by ovariectomized females: importance of SIRT1 and SIRT4

Camargo, T. F., Zanesco, A. M., Pacher, K. A. S., de Andrade, T. A. M., Alves, A. A., & do Amaral, M. E. C. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00465.2019 · Cited by 8

Changes in Biceps femoris Transcriptome along Growth in Iberian Pigs Fed Different Energy Sources and Comparative Analysis with Duroc Breed

Benítez, R., Núñez, Y., Ayuso, M., Isabel, B., Fernández‐Barroso, M. Á., de Mercado, E., Gómez-Izquierdo, E., Casco, J. M. G., López-Bote, C. J., & Óvilo, C. (2021) · Animals · doi:10.3390/ani11123505 · Cited by 8

Autophagy-inducing nutritional interventions in experimental and clinical oncology

Hofer, S. J., Kroemer, G., & Kepp, O. (2022) · International review of cytology · doi:10.1016/bs.ircmb.2022.08.003 · Cited by 8

C/EBPβ-LIP mediated activation of the malate-aspartate shuttle sensitizes cells to glycolysis inhibition

Ackermann, T., Zuidhof, H. R., Müller, C., Kortman, G., Rutten, M. G. S., Broekhuis, M., Zaini, M. A., Hartleben, G., & Calkhoven, C. F. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101726 · Cited by 9

Corn Oligopeptide Alleviates Nonalcoholic Fatty Liver Disease by Regulating the Sirtuin Signaling Pathway

Xu, Y., Su, T., Mishra, H., Ando, R., Furutani, Y., Lu, J., Cai, M., Suzuki, H., Yu, W., & Qin, X. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c09058 · Cited by 8

2,3,7,8-Tetrachlorodibenzo-p-dioxin influences bovine herpesvirus 1 replication through upregulation of SIRT3 and cytoskeletal reorganization

Fiorito, F., Iovane, V., Marullo, A., Costagliola, A., Granato, G. E., & Martino, L. D. (2017) · Veterinary Research Communications · doi:10.1007/s11259-017-9701-1 · Cited by 8

Development of Second Generation Activity-Based Chemical Probes for Sirtuins

Curry, A. M., Barton, E. E., Kang, W., Mongeluzi, D. V., & Cen, Y. (2020) · Molecules · doi:10.3390/molecules26010011 · Cited by 8

DIA-Based Proteomics Identifies IDH2 as a Targetable Regulator of Acquired Drug Resistance in Chronic Myeloid Leukemia

Liu, W., Sun, Y., Ge, W., Zhang, F., Gan, L., Zhu, Y., Guo, T., & Liu, K. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100187 · Cited by 8

Altered sirtuins 1 and 2 expression in the brain of rats induced by experimental diabetes and the ways of its correction

Guzyk, M. M., Tykhonenko, T., Dyakun, K., Yanitska, L. V., Pryvrotska, I. B., & Kuchmerovska, T. M. (2019) · The Ukrainian Biochemical Journal · doi:10.15407/ubj91.01.021 · Cited by 8

Dose-related effects of eugenol: Exploring renal functionality and morphology in healthy Wistar rats

Carvalho, R. P. R., da Costa, R. V., de Carvalho, I. R., Viana, A. G. A., Lopez, C. R., Oliveira, M., Guimarães‐Ervilha, L. O., de Sousa, W. V., Bastos, D. S. S., de Miranda, E. V. C., et al. (2025) · Food and Chemical Toxicology · doi:10.1016/j.fct.2025.115244 · Cited by 7

Polyphenols and Exercise in Mitochondrial Biogenesis: Focus on Age-Related CNS Disorders

Tu, J. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05121-y · Cited by 11

The crosstalk between MicroRNAs and sirtuins: a bit unexpected therapeutic target for cardiovascular diseases

Kamvar, R., Barjasteh, A. H., Omouri‐Kharashtomi, M., Roumiani, P. H., Beheshtirooy, A., Adib-Hajbagheri, P., Rezaei, P., Shokraei, R., & Pourhanifeh, M. H. (2025) · European journal of medical research · doi:10.1186/s40001-025-03235-6 · Cited by 7

Role of the circRNA_34414/ miR ‐6960a‐5p/ SIRT3 axis in postoperative delirium via CA1 Vglut1+ neurons in older mice

Wang, H., Liu, Q., Liu, Y., Dong, W., Wan, J., Jiao, X., Wu, Y., Li, T., & Miao, H. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14902 · Cited by 6

Sirtuins Affect Cancer Stem Cells via Epigenetic Regulation of Autophagy

Sípos, F., & Műzes, G. (2024) · Biomedicines · doi:10.3390/biomedicines12020386 · Cited by 7

Assembly and analysis of the complete mitochondrial genome of Leonurus japonicus (Lamiaceae)

Hu, Q., Li, Q., Mao, Y., Luo, Y., Deng, Z., & Zhang, W. (2025) · Scientific Reports · doi:10.1038/s41598-025-97594-z · Cited by 6

PKM2 Drives Lactate-mediated Fibrosis in Liver Transplantation

Liu, J.-Y., Liao, W., Chen, Z.-Y., Liu, T., Wang, R., Gong, J.-P., Xu, X.-S., & Wu, H. (2025) · Transplantation · doi:10.1097/tp.0000000000005461 · Cited by 6

Identification of Hypoxia and Mitochondrial-related Gene Signature and Prediction of Prognostic Model in Lung Adenocarcinoma

Zhao, W., Huang, H., Zhao, Z., Ding, C., Jia, C., Wang, Y., Wang, G., Li, Y., Liu, H., & Chen, J. (2024) · Journal of Cancer · doi:10.7150/jca.97374 · Cited by 6

Metabolically Relevant Cell Biology – Role of Intracellular Organelles for Cardiac Metabolism

Niemann, B., & Rohrbach, S. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-802394-5.00003-0 · Cited by 9

Sirtuins, NAD + , Aging, and Disease

Guarente, L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00001-0 · Cited by 6

Implications of altered sirtuins in metabolic regulation and oral cancer

Xu, Q., Xin, Y., Wang, H., Sun, Y., Chen, C., & Zhang, J. (2023) · PeerJ · doi:10.7717/peerj.14752 · Cited by 6

Role of Epigenetics in Neural Differentiation: Implications for Health and Disease

Toraño, E. G., Fernández, A. F., Urdinguio, R. G., & Fraga, M. F. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0706-9_2 · Cited by 6

The Enzymatic Activities of Sirtuins

Lin, H. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00004-6 · Cited by 6

Modulation of the Activity of Succinate Dehydrogenase by Acetylation with Chemicals, Drugs, and Microbial Metabolites

Fedotcheva, N. I., Kondrashova, M. N., Litvinova, E. G., Zakharchenko, M. V., Khunderyakova, N. V., & Nv, B. (2018) · BIOPHYSICS · doi:10.1134/s0006350918050081 · Cited by 6

Rosuvastatin Modulates the Post-Translational Acetylome in Endothelial Cells.

Lin, M. C., Hsing, C., Li, F., Wu, C. H., Fu, Y., Cheng, J. K., & Huang, B. (2014) · Europe PMC (PubMed Central) · Cited by 6

Plausible Links Between Metabolic Networks, Stem Cells, and Longevity

Kucia, M., & Ratajczak, M. Z. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-31206-0_15 · Cited by 6

Metabolism Meets Epigenetics: β-Hydroxybutyrate–Driven Lysine β-Hydroxybutyrylation Bridging Energy Metabolism With Transcription and Protein Functional Remodeling

Cheng, S., Cheng, C., Zhou, J., Ji, Y. S., Liu, Y., Jiang, W., Liu, C., & Wang, H. (2025) · Nutrition Reviews · doi:10.1093/nutrit/nuaf258 · Cited by 7

Targeting frataxin deficiency in DRG neurons and fibroblasts: omaveloxolone restores metabolic and iron balance to reduce ferroptosis

Portillo-Carrasquer, M., Sanz‐Alcázar, A., Sánchez-López, B., Delaspre, F., Pazos-Gil, M., Oliveira-Jorge, L., Castells‐Roca, L., Tamarit, J., Ros, J., & Cabiscol, E. (2026) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2026.119031 · Cited by 5

Molecular cloning and characterization of Sirt1 and its role in the follicle of juvenile Chinese soft‐shelled turtle (Pelodiscus sinensis)

Zhang, H., Gao, Y., Wang, G., Xin, Q., Tian, X., Wu, L., Shi, X., Ma, W., Liu, H., Jiang, H., et al. (2023) · Gene · doi:10.1016/j.gene.2023.147211 · Cited by 5

Dynamics of Mitochondrial Proteome and Acetylome in Glioblastoma Cells with Contrasting Metabolic Phenotypes

Fernández-Coto, D. L., Gil, J., Ayala, G., & Encarnación‐Guevara, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063450 · Cited by 5

Influence of the Microbial Metabolite Acetyl Phosphate on Mitochondrial Functions Under Conditions of Exogenous Acetylation and Alkalization

Nv, B., & Fedotcheva, N. I. (2024) · Metabolites · doi:10.3390/metabo14120703 · Cited by 5

Multivitamin Supplementation and Fertility Outcome: A Retrospective Single-Center Cohort Study and the Clinical and Medicolegal Value of Nutritional Counseling

Gullo, G., Zaami, S., Streva, A. V., Burgio, S., Billone, V., Kotlik, Y., Chitoran, E., Ganduscio, S., Baglìo, G., Perino, A., et al. (2025) · Life · doi:10.3390/life15010048 · Cited by 5

The curious case of mitochondrial sirtuin in rewiring breast cancer metabolism: Mr Hyde or Dr Jekyll?

Tharayil, J. S., Kandettu, A., & Chakrabarty, S. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167691 · Cited by 5

Mitochondrial Dysfunction and Sirtuins: Important Targets in Hearing Loss

Zhang, L., Du, Z., & Gong, S. (2021) · Neural Plasticity · doi:10.1155/2021/5520794 · Cited by 5

The mitochondria in schizophrenia with 22q11.2 deletion syndrome: From pathogenesis to therapeutic promise of targeted natural drugs

Xiong, Z., Wang, H., Qu, Y., Peng, S., He, Y., Yang, Q., Xu, X., Lv, D., Liu, Y., Xie, C., et al. (2023) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2023.110831 · Cited by 5

Long-term effects of prior diets, dietary transition and pregnancy on adipose gene expression in dairy heifers

Wærp, H. K. L., Waters, S. M., McCabe, M. S., Cormican, P., & Salte, R. (2019) · PLoS ONE · doi:10.1371/journal.pone.0218723 · Cited by 5

Sirtuins in metabolic and epigenetic regulation of stem cells

Fang, Y., & Li, X. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00004-8 · Cited by 5

Regulation of glucose metabolism in liver

Burgess, S. C. (2015) · Wiley eBooks · doi:10.1002/9781118387658.ch13 · Cited by 5

Bidirectional relationship between mitochondrial dysfunction and dysregulated lipid metabolism in Multiple Sclerosis: potential mechanisms and therapeutic implications

Xie, T., Fok, H. T., Quan, Z., Ku, C.-Y., Akefe, I. O., & Schweitzer, D. R. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107159 · Cited by 5

GPR43 regulates mitochondrial apoptosis through the cyclophilin D pathway in Alzheimer’s disease

Wang, X., Wu, S., Deng, Z., Yan, M., Wang, D., Yang, M., Zhong, F., Song, J., Chen, L., Chen, Y., et al. (2025) · Molecular Medicine · doi:10.1186/s10020-025-01269-4 · Cited by 4

Mitochondrial sirtuins: Emerging roles in metabolic regulations, energy homeostasis and diseases

Parihar, P., Solanki, I., Mansuri, M. L., & Parihar, M. S. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.12.004 · Cited by 114

Fine Tuning Our Cellular Factories: Sirtuins in Mitochondrial Biology

Zhong, L., & Mostoslavsky, R. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.05.004 · Cited by 90

Function and regulation of the mitochondrial Sirtuin isoform Sirt5 in Mammalia

Gertz, M., & Steegborn, C. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.09.011 · Cited by 75

SIRTUINS AS DRUG TARGETS AFFECTING MITOCHONDRIAL FUNCTIONS

Tok, K. C., Kartal, Y., & Kayaaltı, Z. (2016) · DergiPark (Istanbul University) · doi:10.13140/rg.2.1.4805.5924

Mitochondrial Metabolism, Sirtuins, and AgingPreprint

Sack, M. N., & Finkel, T. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013102 · Cited by 242