The role of sirtuins in cellular homeostasis

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

Sirtuins as regulators of metabolism and healthspan

Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008

NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus

Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648

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

Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins

Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409

SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells

Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162

SIRT1 and other sirtuins in metabolism

Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,157

The sirtuin SIRT6 regulates lifespan in male mice

Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z., & Cohen, H. Y. (2012) · Nature · doi:10.1038/nature10815 · Cited by 1,059

The many faces of insulin-like peptide signalling in the brain

Fernandez, A. M., & Torres-Alemán, I. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3209 · Cited by 872

Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes

Pandey, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf660 · Cited by 783

Mitochondria in health, disease, and aging

Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 641

SIRT1 Activation by Natural Phytochemicals: An Overview

Iside, C., Scafuro, M., Nebbioso, A., & Altucci, L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01225 · Cited by 328

Sirtuins in gamete biology and reproductive physiology: emerging roles and therapeutic potential in female and male infertility

Tatone, C., Emidio, G. D., Barbonetti, A., Carta, G., Luciano, A. M., Falone, S., & Amicarelli, F. (2018) · Human Reproduction Update · doi:10.1093/humupd/dmy003 · Cited by 296

A Critical Review of the Evidence That Metformin Is a Putative Anti-Aging Drug That Enhances Healthspan and Extends Lifespan

Mohammed, I., Hollenberg, M. D., Ding, H., & Triggle, C. R. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.718942 · Cited by 278

Sirtuins and Their Roles in Brain Aging and Neurodegenerative Disorders

Jęśko, H. M., Wencel, P. L., Strosznajder, R. P., & Strosznajder, J. B. (2016) · Neurochemical Research · doi:10.1007/s11064-016-2110-y · Cited by 264

ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease

Lüscher, B., Bütepage, M., Eckei, L., Krieg, S., Verheugd, P., & Shilton, B. H. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00122 · Cited by 264

Epigenetics in NAFLD/NASH: Targets and therapy

Sodum, N., Kumar, G., Bojja, S. L., Kumar, N., & Rao, C. M. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105484 · Cited by 147

Mitochondrial dysfunction: A fatal blow in depression

Song, Y., Cao, H., Zuo, C., Gu, Z., Huang, Y., Miao, J., Fu, Y., Guo, Y., Jiang, Y., & Wang, F. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115652 · Cited by 141

The Critical Role of SIRT1 in Parkinson’s Disease: Mechanism and Therapeutic Considerations

Li, X., Feng, Y., Wang, X.-X., Truong, D., & Wu, Y. (2020) · Aging and Disease · doi:10.14336/ad.2020.0216 · Cited by 134

Systematic and comprehensive insights into HIF-1 stabilization under normoxic conditions: implications for cellular adaptation and therapeutic strategies in cancer

Zhang, J., Yao, M., Xia, S., Zeng, F., & Liu, Q. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00682-7 · Cited by 150

SIRT1 and SIRT6: The role in aging-related diseases

You, Y., & Liang, W. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166815 · Cited by 124

Natural Phytochemicals as SIRT Activators—Focus on Potential Biochemical Mechanisms

Wiciński, M., Erdmann, J., Nowacka, A., Kuźmiński, O., Michalak, K., Janowski, K., Ohla, J., Biernaciak, A., Szambelan, M., & Zabrzyński, J. (2023) · Nutrients · doi:10.3390/nu15163578 · Cited by 117

Sirtuins' control of autophagy and mitophagy in cancer

Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103

Review of the anti-inflammatory effect of SIRT1 and SIRT2 modulators on neurodegenerative diseases

Zhang, Y., Anoopkumar‐Dukie, S., Arora, D. S., & Davey, A. K. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172847 · Cited by 95

Sirtuins as Important Factors in Pathological States and the Role of Their Molecular Activity Modulators

Kratz, E. M., Sołkiewicz, K., Kubis-Kubiak, A., & Piwowar, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020630 · Cited by 97

Therapeutic role of sirtuins in neurodegenerative disease and their modulation by polyphenols

Ajami, M., Pazoki–Toroudi, H., Amani, H., Nabavi, S. F., Braidy, N., Vacca, R. A., Atanasov, A. G., MOCAN, A., & Nabavi, S. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.11.022 · Cited by 94

CD38: T Cell Immuno-Metabolic Modulator

Kar, A., Mehrotra, S., & Chatterjee, S. (2020) · Cells · doi:10.3390/cells9071716 · Cited by 94

NAD+ dependent deacetylase Sirtuin 5 rescues the innate inflammatory response of endotoxin tolerant macrophages by promoting acetylation of p65

Qin, K., Han, C., Zhang, H., Li, T., Li, N., & Cao, X. (2017) · Journal of Autoimmunity · doi:10.1016/j.jaut.2017.04.006 · Cited by 89

Redox status of the plant cell determines epigenetic modifications under abiotic stress conditions and during developmental processes

Ramakrishnan, M., Papolu, P. K., Satish, L., Vinod, K. K., Wei, Q., Sharma, A., Emamverdian, A., Zou, L., & Zhou, M. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.04.007 · Cited by 85

Antioxidant Alternatives in the Treatment of Amyotrophic Lateral Sclerosis: A Comprehensive Review

Carrera‐Juliá, S., Moreno, M. L., Barrios, C., Ortí, J. E. D. L. R., & Drehmer, E. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00063 · Cited by 87

Cytochrome b5 reductases: Redox regulators of cell homeostasis

Hall, R., Yuan, S. S., Wood, K. C., Katona, M., & Straub, A. C. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102654 · Cited by 77

Resveratrol up-regulates ATP2A3 gene expression in breast cancer cell lines through epigenetic mechanisms

Izquierdo‐Torres, E., Hernández‐Oliveras, A., Meneses‐Morales, I., Rodrı́guez, G., Fuentes-García, G., & Zarain‐Herzberg, Á. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.05.020 · Cited by 77

A comprehensive review of Sirtuins: With a major focus on redox homeostasis and metabolism

Shahgaldi, S., & Kahmini, F. R. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119803 · Cited by 81

The role of ion disequilibrium in induction of root cell death and autophagy by environmental stresses

Demidchik, V. V., Tyutereva, E. V., & Voitsekhovskaja, O. V. (2017) · Functional Plant Biology · doi:10.1071/fp16380 · Cited by 396

Mitophagy in depression: Pathophysiology and treatment targets

Tripathi, A., Scaini, G., Barichello, T., Quevedo, J., & Pillai, A. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.08.016 · Cited by 71

The Role of SIRT3 in the Brain Under Physiological and Pathological Conditions

Sidorova‐Darmos, E., Sommer, R., & Eubanks, J. H. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00196 · Cited by 66

Sirtuin-1 and Its Relevance in Vascular Calcification

Lu, C., Liao, M.-T., Hou, Y., Fang, Y.-W., Zheng, C., Liu, W.-C., Chao, C., Lu, K., & Ng, Y.-Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051593 · Cited by 67

The anti-diabetic effects of betanin in streptozotocin-induced diabetic rats through modulating AMPK/SIRT1/NF-κB signaling pathway

Abedimanesh, N., Asghari, S., Mohammadnejad, K., Daneshvar, Z., Rahmani, S., Shokoohi, S., Farzaneh, A. H., Hosseini, S. H., Anarkooli, I. J., Noubarani, M., et al. (2021) · Nutrition & Metabolism · doi:10.1186/s12986-021-00621-9 · Cited by 69

Lysine Acetylation and Deacetylation in Brain Development and Neuropathies

Tapias, A., & Wang, Z. (2017) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2016.09.002 · Cited by 69

Sirt3 deficiency accelerates ovarian senescence without affecting spermatogenesis in aging mice

Zhu, J., Yang, Q., Li, H., Wang, Y., Jiang, Y., Wang, H., Cong, L., Xu, J., Shen, Z., Chen, W., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.10.324 · Cited by 64

The controversial role of senescence-associated secretory phenotype (SASP) in cancer therapy

Cao, L., Li, K., Li, Q., Tong, Q., Wang, Y., & Huang, L. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02475-8 · Cited by 79

Decoding the Rosetta stone of mitonuclear communication

English, J., Son, J. M., Cardamone, M. D., Lee, C., & Perissi, V. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105161 · Cited by 55

NAD+: A key metabolic regulator with great therapeutic potential

Sultani, G., Samsudeen, A., Osborne, B., & Turner, N. A. (2017) · Journal of Neuroendocrinology · doi:10.1111/jne.12508 · Cited by 54

More to NAD+ than meets the eye: A regulator of metabolic pools and gene expression in Arabidopsis

Gakière, B., Fernie, A. R., & Pétriacq, P. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.01.003 · Cited by 53

Salidroside reduces neuropathology in Alzheimer’s disease models by targeting NRF2/SIRT3 pathway

Yao, Y., Ren, Z., Yang, R., Mei, Y., Dai, Y., Cheng, Q., Xu, C., Xu, X., Wang, S., Kim, K. M., et al. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00918-z · Cited by 53

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

Grotegut, P., Perumal, N., Kuehn, S., Smit, A., Dick, H. B., Grus, F. H., & Joachim, S. C. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-02012-y · Cited by 54

Potential of Polyphenols to Restore SIRT1 and NAD+ Metabolism in Renal Disease

Tovar‐Palacio, C., Noriega, L. G., & Mercado, A. (2022) · Nutrients · doi:10.3390/nu14030653 · Cited by 52

The NAD + -Dependent Family of Sirtuins in Cerebral Ischemia and Preconditioning

Khoury, N., Koronowski, K. B., Young, J. I., & Pérez‐Pinzón, M. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7258 · Cited by 51

A New Vision of Mitochondrial Unfolded Protein Response to the Sirtuin Family

Weng, H., Ma, Y., Chen, L., Cai, G., Chen, Z., Zhang, S., & Ye, Q. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200123165002 · Cited by 51

Cardioprotective Effects of SIRT6 in a Mouse Model of Transverse Aortic Constriction-Induced Heart Failure

Li, Y., Meng, X., Wang, W., Liu, F., Hao, Z.-R., Yang, Y., Zhao, J., Yin, W., Xu, L., Zhao, R., et al. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00394 · Cited by 47

The Mitochondrial Antioxidant Sirtuin3 Cooperates with Lipid Metabolism to Safeguard Neurogenesis in Aging and Depression

Santos, S. S., Moreira, J. B., Costa, M., Rodrigues, R. S., Sebastião, A. M., Xapelli, S., & Solá, S. (2021) · Cells · doi:10.3390/cells11010090 · Cited by 44

Resveratrol Induces Expression of Metabolic and Antioxidant Machinery and Protects Tilapia under Cold Stress

Wang, M., Wang, Y.-C., Peng, H.-W., Hseu, J.-R., Wu, G.-C., Chang, C., & Tseng, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093338 · Cited by 41

Silencing Sirtuin 6 induces cell cycle arrest and apoptosis in non-small cell lung cancer cell lines

Krishnamoorthy, V., & Ravikumar, V. (2020) · Genomics · doi:10.1016/j.ygeno.2020.04.027 · Cited by 42

Sirtuin 2 enhances allergic asthmatic inflammation

Lee, Y. G., Reader, B. F., Herman, D. D., Streicher, A., Englert, J. A., Ziegler, M., Chung, S., Karpurapu, M., Park, G. Y., Christman, J. W., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.124710 · Cited by 42

Why Is Longevity Still a Scientific Mystery? Sirtuins—Past, Present and Future

Ziętara, P., Dziewięcka, M., & Augustyniak, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010728 · Cited by 40

SIRT1 activation with neuroheal is neuroprotective but SIRT2 inhibition with AK7 is detrimental for disconnected motoneurons

Romeo-Guitart, D., Leiva-Rodríguez, T., Espinosa‐Alcantud, M., Sima, N., Vaquero, A., Dominguez‐Martín, H., Ruano, D., & Casas, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0553-6 · Cited by 39

Sirtuins as molecular targets, mediators, and protective agents in metal-induced toxicity

Tinkov, A. A., Nguyen, T., Santamarı́a, A., Bowman, A. B., Djordjević, A. B., Paoliello, M. M. B., Skalny, A. V., & Aschner, M. (2021) · Archives of Toxicology · doi:10.1007/s00204-021-03048-6 · Cited by 38

Dual Deletion of the Sirtuins SIRT2 and SIRT3 Impacts on Metabolism and Inflammatory Responses of Macrophages and Protects From Endotoxemia

Heinonen, T., Ciarlo, E., Rigoni, E., Regina, J., Roy, D. L., & Roger, T. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02713 · Cited by 37

Evaluation of the Neuroprotective Effect of Sirt3 in Experimental Stroke

Verma, R., Ritzel, R. M., Crapser, J. D., Friedler, B. D., & McCullough, L. D. (2018) · Translational Stroke Research · doi:10.1007/s12975-017-0603-x · Cited by 36

Overview of the mammalian ADP-ribosyl-transferases clostridia toxin-like (ARTCs) family

Girolamo, M. D., & Fabrizio, G. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.07.004 · Cited by 36

Two novel SIRT1 activators, SCIC2 and SCIC2.1, enhance SIRT1-mediated effects in stress response and senescence

Scisciola, L., Sarno, F., Carafa, V., Cosconati, S., Maro, S. D., Ciuffreda, L. P., Angelis, A. D., Stiuso, P., Feoli, A., Sbardella, G., et al. (2020) · Epigenetics · doi:10.1080/15592294.2019.1704349 · Cited by 37

Regulation of Pyridine Nucleotide Metabolism During Tomato Fruit Development Through Transcript and Protein Profiling

Decros, G., Beauvoit, B., Colombié, S., Cabasson, C., Bernillon, S., Arrivault, S., Guenther, M., Belouah, I., Prigent, S., Baldet, P., et al. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01201 · Cited by 35

Oxidative Stress-Induced Sirtuin1 Downregulation Correlates to HIF-1α, GLUT-1, and VEGF-A Upregulation in Th1 Autoimmune Hashimoto’s Thyroiditis

Hepp, M., Wérion, A., Greef, A. D., de Goyet, C. D. V., de Bournonville, M., Behets, C., Lengelé, B., Daumerie, C., Mourad, M., Ludgate, M., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083806 · Cited by 36

SIRT1 regulates DNA damage signaling through the PP4 phosphatase complex

Rasti, G., Becker, M., Vázquez, B. N., Espinosa‐Alcantud, M., Fernández-Duran, I., Gámez-García, A., Ianni, A., González, J., Bosch‐Presegué, L., Marazuela-Duque, A., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad504 · Cited by 36

Recovery of Olfactory Function After Excitotoxic Lesion of the Olfactory Bulbs Is Associated with Increases in Bulbar SIRT1 and SIRT4 Expressions

Marı́n, C., Langdon, C., Alobid, I., Fuentes, M., Bonastre, M., & Mullol, J. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1472-y · Cited by 31

NAD+ Metabolism as an Emerging Therapeutic Target for Cardiovascular Diseases Associated With Sudden Cardiac Death

Xu, W., Li, L., & Zhang, L. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00901 · Cited by 35

Modulation of H4K16Ac levels reduces pro-fibrotic gene expression and mitigates lung fibrosis in aged mice

Zhang, X., Liu, H., Zhou, J. Q., Krick, S., Barnes, J. W., Thannickal, V. J., & Sanders, Y. Y. (2021) · Theranostics · doi:10.7150/thno.62760 · Cited by 32

Sirtuins as therapeutic targets for improving delayed wound healing in diabetes

Beegum, F., Anuranjana, P. V., George, K. T., Divya, K. P., Begum, F., Nandakumar, K., & Shenoy, R. R. (2022) · Journal of drug targeting · doi:10.1080/1061186x.2022.2085729 · Cited by 31

Sirt6 Deacetylase: A Potential Key Regulator in the Prevention of Obesity, Diabetes and Neurodegenerative Disease

Raj, S., Dsouza, L. A., Singh, S. P., & Kanwal, A. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.598326 · Cited by 31

Moderate SIRT1 overexpression protects against brown adipose tissue inflammation

Escalona-Garrido, C., Vázquez, P., Mera, P., Zagmutt, S., García-Casarrubios, E., Montero‐Pedrazuela, A., Rey-Stolle, F., Guadaño‐Ferraz, A., Rupérez, F. J., Serra, D., et al. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101097 · Cited by 31

Redox Homeostasis in Cardiovascular Disease: The Role of Mitochondrial Sirtuins

Zullo, A., Guida, R., Sciarrillo, R., & Mancini, F. P. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.858330 · Cited by 30

Melatonin and Vitamin D Orchestrate Adipose Derived Stem Cell Fate by Modulating Epigenetic Regulatory Genes

Santaniello, S., Cruciani, S., Basoli, V., Balzano, F., Bellu, E., Garroni, G., Ginesu, G. C., Cossu, M. L., Facchin, F., Delitala, A., et al. (2018) · International Journal of Medical Sciences · doi:10.7150/ijms.27669 · Cited by 30

The NAD + precursor nicotinic acid improves genomic integrity in human peripheral blood mononuclear cells after X-irradiation

Weidele, K., Beneke, S., & Bürkle, A. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.02.001 · Cited by 30

Mitochondrial Sirtuins in Skin and Skin Cancers

Su, S., Ndiaye, M. A., Singh, C. K., & Ahmad, N. (2020) · Photochemistry and Photobiology · doi:10.1111/php.13254 · Cited by 29

Review: The plant sirtuins

Zheng, W. (2020) · Plant Science · doi:10.1016/j.plantsci.2020.110434 · Cited by 28

Satiety Associated with Calorie Restriction and Time-Restricted Feeding: Central Neuroendocrine Integration

Tacad, D. K., Tovar, A. P., Richardson, C. E., Horn, W. F., Keim, N. L., Krishnan, G. P., & Krishnan, S. (2022) · Advances in Nutrition · doi:10.1093/advances/nmac011 · Cited by 26

Xiyangshen Sanqi Danshen granules attenuated D-gal-induced C57BL/6J mouse aging through the AMPK/SIRT1 signaling pathway

Yin, Z., Tian, L., Kou, W., Cao, G., Wang, L., Xia, Y.-F., Lin, Y., Tang, S., Zhang, J., & Yang, H. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.156213 · Cited by 28

Impact of Dietary Modifications on Plasma Sirtuins 1, 3 and 5 in Older Overweight Individuals Undergoing 12-Weeks of Circuit Training

Wasserfurth, P., Nebl, J., Rühling, M. R., Shammas, H., Bednarczyk, J., Koehler, K., Boßlau, T. K., Krüger, K., Hahn, A., & Das, A. M. (2021) · Nutrients · doi:10.3390/nu13113824 · Cited by 27

Fibrosis: Sirtuins at the checkpoints of myofibroblast differentiation and profibrotic activity

Zullo, A., Mancini, F. P., Schleip, R., Wearing, S. C., & Klingler, W. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12943 · Cited by 25

Genetic Analysis of Sirtuin Deacetylases in Hyphal Growth of Candida albicans

Zhao, G., & Rusché, L. N. (2021) · mSphere · doi:10.1128/msphere.00053-21 · Cited by 25

Obesity and Male Reproduction: Do Sirtuins Play a Role?

Barbagallo, F., Vignera, S. L., Cannarella, R., Mongioì, L. M., Garofalo, V., Leanza, C., Marino, M., Calogero, A. E., & Condorelli, R. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020973 · Cited by 27

Paeonol prevents lipid metabolism dysfunction in palmitic acid-induced HepG2 injury through promoting SIRT1-FoxO1-ATG14-dependent autophagy

Dong, Z., Xie, X., Sun, Y., Wu, H., & Dai, M. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173145 · Cited by 24

Shikimic acid protects skin cells from UV-induced senescence through activation of the NAD+-dependent deacetylase SIRT1

Martínez-Gutiérrez, A., Fernández-Duran, I., Marazuela-Duque, A., Simonet, N. G., Yousef, I., Martínez‐Rovira, I., Martínez-Hoyos, J., & Vaquero, A. (2021) · Aging · doi:10.18632/aging.203010 · Cited by 23

Flavonoids as Sirtuin Modulators

Şenol, F. S., Eren, G., & Orhan, İ. E. (2022) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026622666220422094744 · Cited by 24

Sirtuins: Subtle Regulators Involved in Convoluted Mechanisms of Pregnancy

Kahmini, F. R., Ghaleh, H. D., & Shahgaldi, S. (2022) · Cellular Physiology and Biochemistry · doi:10.33594/000000588 · Cited by 23

Emerging roles of Sirtuin 2 in cardiovascular diseases

Taneja, A., Ravi, V., Hong, J. Y., Lin, H., & Sundaresan, N. R. (2021) · The FASEB Journal · doi:10.1096/fj.202100490r · Cited by 23

Phosphoribosyltransferases and Their Roles in Plant Development and Abiotic Stress Response

Liu, Y., Wu, P., Li, B., Wang, W., & Zhu, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411828 · Cited by 22

Functions of mammalian SIRT4 in cellular metabolism and research progress in human cancer (Review)

Wang, C., Liu, Y., Zhu, Y., & Kong, C. (2020) · Oncology Letters · doi:10.3892/ol.2020.11872 · Cited by 24

Early loss of endogenous NAD + following rotenone treatment leads to mitochondrial dysfunction and Sarm1 induction that is ameliorated by PARP inhibition

Sarkar, A., Dutta, S., Sur, M., Chakraborty, S., Dey, P., & Mukherjee, P. (2022) · FEBS Journal · doi:10.1111/febs.16652 · Cited by 23

Distinct and diverse chromatin proteomes of ageing mouse organs reveal protein signatures that correlate with physiological functions

Oliviero, G., Kovalchuk, S. I., Rogowska-Wrzesińska, A., Schwämmle, V., & Jensen, O. N. (2022) · eLife · doi:10.7554/elife.73524 · Cited by 25

Multifaced role of protein deacetylase sirtuins in neurodegenerative disease

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