Sirtuin functions and modulation: from chemistry to the clinic

Resveratrol improves health and survival of mice on a high-calorie diet

Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290

In silico analysis enabling informed design for genome editing in medicinal cannabis; gene families and variant characterisation

Calamita, E., Schmid, M., Kunz, M., Ndebele-Murisa, M. R., Magadza, C. H. D., Nyambe, I., & Wehrli, B. (2019) · Figshare · doi:10.26181/6153922fe919c · Cited by 4,239

Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796

hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690

Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081

Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924

Sirtuin activators mimic caloric restriction and delay ageing in metazoans

Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707

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

Aging-Related Correlation between Serum Sirtuin 1 Activities and Basal Metabolic Rate in Women, but not in Men

Lee, H. J., & Yang, S. J. (2017) · Clinical Nutrition Research · doi:10.7762/cnr.2017.6.1.18 · Cited by 34

Influence of intermittent fasting on autophagy in the liver

Ma, Y., Jiang, X., Tang, W., & Song, P. (2023) · BioScience Trends · doi:10.5582/bst.2023.01207 · Cited by 36

Activation and inhibition of sirtuins: From bench to bedside

Fiorentino, F., Fabbrizi, E., Mai, A., & Rotili, D. (2024) · Medicinal Research Reviews · doi:10.1002/med.22076 · Cited by 35

D‑Pinitol alleviates cyclosporine A‑induced renal tubulointerstitial fibrosis via activating Sirt1 and Nrf2 antioxidant pathways

Koh, E., Kim, S., Kim, M., Hong, Y., Shin, S. J., Park, C., Chang, Y., Chung, S., & Kim, H. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3408 · Cited by 32

Sirtuin 1 Inhibiting Thiocyanates (S1th)—A New Class of Isotype Selective Inhibitors of NAD+ Dependent Lysine Deacetylases

Wössner, N., Alhalabi, Z., González, J., Swyter, S., Gan, J., Schmidtkunz, K., Zhang, L., Vaquero, A., Ovaa, H., Einsle, O., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00657 · Cited by 33

Lysine Acetyltransferase Inhibitors From Natural Sources

Fiorentino, F., Mai, A., & Rotili, D. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01243 · Cited by 32

Discovery and Characterization of R/S-N-3-Cyanophenyl-N′-(6-tert-butoxycarbonylamino-3,4-dihydro-2,2-dimethyl-2H-1-benzopyran-4-yl)urea, a New Histone Deacetylase Class III Inhibitor Exerting Antiproliferative Activity against Cancer Cell Lines

Schnekenburger, M., Goffin, E., Lee, J., Jang, J. Y., Mazumder, A., Ji, S., Rogister, B., Bouider, N., Lefranc, F., Miklos, W., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00533 · Cited by 31

Effects of Parkia biglobosa aqueous seed extract on some biochemical, haematological and histopathological parameters in streptozotocin induced diabetic rats

Ekperikpe, U. S., Owolabi, O. J., & Bolanle, I. O. (2018) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2018.09.016 · Cited by 31

Sirtuin 1 and oral cancer (Review)

Islam, S., Abiko, Y., Uehara, O., & Chiba, I. (2018) · Oncology Letters · doi:10.3892/ol.2018.9722 · Cited by 32

The prophylactic effects of BIFICO on the antibiotic-induced gut dysbiosis and gut microbiota

Wu, J., Gan, T., Zhang, Y., Xia, G., Deng, S., Lv, X., Zhang, B., & Lv, B. (2020) · Gut Pathogens · doi:10.1186/s13099-020-00379-0 · Cited by 31

Sirtuin function and metabolism: Role in pancreas, liver, and adipose tissue and their crosstalk impacting bone homeostasis

Avilkina, V., Chauveau, C., & Mhenni, O. G. (2021) · Bone · doi:10.1016/j.bone.2021.116232 · Cited by 33

Sirtuins’ Deregulation in Bladder Cancer: SIRT7 Is Implicated in Tumor Progression through Epithelial to Mesenchymal Transition Promotion

Monteiro‐Reis, S., Lameirinhas, A., Miranda‐Gonçalves, V., Felizardo, D., Dias, P. C., Oliveira, J., Graça, I. C. R., Gonçalves, C. S., Costa, B. M., Henrique, R., et al. (2020) · Cancers · doi:10.3390/cancers12051066 · Cited by 31

Antiproliferative S-Trityl-l-Cysteine -Derived Compounds as SIRT2 Inhibitors: Repurposing and Solubility Enhancement

Radwan, M. O., Ciftci, H. I., Ali, T. F. S., Ellakwa, D. E., Koga, R., Tateishi, H., Nakata, A., Ito, A., Yoshida, M., Okamoto, Y., et al. (2019) · Molecules · doi:10.3390/molecules24183295 · Cited by 30

Decreased AMPK/SIRT1/PDK4 induced by androgen excess inhibits human endometrial stromal cell decidualization in PCOS

Hong, L., Xiao, S., Diao, L., Lian, R., Chen, C., Zeng, Y., & Liu, S. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05362-5 · Cited by 31

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

Dual role of sirtuin 1 in inflammatory bowel disease

Devi, K., Singh, N., & Jaggi, A. S. (2020) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2020.1790595 · Cited by 29

Pharmacological Advantage of SIRT2-Selective versus pan-SIRT1–3 Inhibitors

Hong, J. Y., Fernandez, I. R., Anmangandla, A., Lü, X., Bai, J. J., & Lin, H. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00331 · Cited by 30

Downregulation of LINC00886 facilitates epithelial–mesenchymal transition through SIRT7/ELF3/miR-144 pathway in esophageal squamous cell carcinoma

Dong, Z., Liu, Y., Lu, J., Guo, Y., Shen, S., Liang, J., & Guo, W. (2022) · Clinical & Experimental Metastasis · doi:10.1007/s10585-022-10171-w · Cited by 29

Screening Analysis of Sirtuins Family Expression on Anti-Inflammation of Resveratrol in Endothelial Cells

Yu, H., Pan, W., Huang, H., Chen, J., Sun, B., Yang, L., & Zhu, P. (2019) · Medical Science Monitor · doi:10.12659/msm.913240 · Cited by 29

Targeting histone modifiers in bladder cancer therapy — preclinical and clinical evidence

Zhang, S., Lin, T., Xiong, X., Chen, C., Tan, P., & Wei, Q. (2024) · Nature Reviews Urology · doi:10.1038/s41585-024-00857-z · Cited by 30

Sirtuins—The New Important Players in Women’s Gynecological Health

Kratz, E. M., Kokot, I., Dymicka-Piekarska, V., & Piwowar, A. (2021) · Antioxidants · doi:10.3390/antiox10010084 · Cited by 28

Interplay of autophagy and cancer stem cells in hepatocellular carcinoma

Wong, M. M.-T., Chan, H.-Y., Aziz, N. A., Ramasamy, T. S., Bong, J. J., Ch’ng, E. S., Armon, S., Peh, S., & Teow, S. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06334-9 · Cited by 28

Insights into the Conserved Regulatory Mechanisms of Human and Yeast Aging

Dahiya, R., Mohammad, T., Alajmi, M. F., Rehman, M. T., Hasan, G. M., Hussain, A., & Hassan, M. I. (2020) · Biomolecules · doi:10.3390/biom10060882 · Cited by 30

The New Role of Sirtuin1 in Human Osteoarthritis Chondrocytes by Regulating Autophagy

Liao, F., Huang, F., Ma, W.-G., Qin, K., Xu, P., Wu, Y.-F., Wang, H., Chang, J., & Yin, Z. (2019) · Cartilage · doi:10.1177/1947603519847736 · Cited by 27

Sodium butyrate activates HMGCS2 to promote ketone body production through SIRT5-mediated desuccinylation

Xu, Y., Ye, X., Zhou, Y., Cao, X., Peng, S., Peng, Y., Zhang, X., Sun, Y., Jiang, H., Huang, W., et al. (2023) · Frontiers of Medicine · doi:10.1007/s11684-022-0943-0 · Cited by 29

Role of sirtuins in metabolic disease-related renal injury

Chen, H., Zhang, Y., Lv, J.-L., Liu, Y., Guo, J., Zhao, L., Nan, Y.-X., Wu, Q., & Zhao, Y. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114417 · Cited by 27

Signaling Pathways Involved in Manganese-Induced Neurotoxicity

Cheng, H., Ferrer, B., Deza-Ponzio, R., Aschner, M., & Chen, P. (2023) · Cells · doi:10.3390/cells12242842 · Cited by 25

Identification of Diketopiperazine-Containing 2-Anilinobenzamides as Potent Sirtuin 2 (SIRT2)-Selective Inhibitors Targeting the “Selectivity Pocket”, Substrate-Binding Site, and NAD+-Binding Site

Mellini, P., Itoh, Y., Elboray, E. E., Tsumoto, H., Li, Y., SUZUKI, M. T., Takahashi, Y., Tojo, T., Kurohara, T., Miyake, Y., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00255 · Cited by 26

Epigenetic Regulation of Excitatory Amino Acid Transporter 2 in Neurological Disorders

Alam, M. A., & Datta, P. K. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01510 · Cited by 26

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

Sirtuins, a key regulator of ageing and age-related neurodegenerative diseases

Bhatt, V., & Tiwari, A. K. (2023) · International Journal of Neuroscience · doi:10.1080/00207454.2022.2057849 · Cited by 28

Sirtuins: Promising Therapeutic Targets to Treat Ischemic Stroke

Liu, Y., Wang, L., Yang, G., Chi, X., Liang, X., & Zhang, Y. (2023) · Biomolecules · doi:10.3390/biom13081210 · Cited by 26

The sirtuin 1/2 inhibitor tenovin-1 induces a nonlinear apoptosis-inducing factor-dependent cell death in a p53 null Ewing’s sarcoma cell line

Marx, C., Marx-Blümel, L., Lindig, N., Thierbach, R., Hoelzer, D., Becker, S., Wittig, S., Lehmann, R., Slevogt, H., Heinzel, T., et al. (2017) · Investigational New Drugs · doi:10.1007/s10637-017-0541-1 · Cited by 25

Activators of Sirtuin-1 and their Involvement in Cardioprotection

Granchi, C., & Minutolo, F. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180214115438 · Cited by 25

Assessment of Pharmacological Interactions between SIRT2 Inhibitor AGK2 and Paclitaxel in Different Molecular Subtypes of Breast Cancer Cells

Wawruszak, A., Łuszczki, J. J., Czerwonka, A., Okoń, E., & Stepulak, A. (2022) · Cells · doi:10.3390/cells11071211 · Cited by 25

The pathogenesis of amyotrophic lateral sclerosis: Mitochondrial dysfunction, protein misfolding and epigenetics

Chen, W., Guo, L., Li, M., Wei, C., Li, S., & Xu, R. (2022) · Brain Research · doi:10.1016/j.brainres.2022.147904 · Cited by 26

Novel 1,4-Dihydropyridines as Specific Binders and Activators of SIRT3 Impair Cell Viability and Clonogenicity and Downregulate Hypoxia-Induced Targets in Cancer Cells

Zwergel, C., Aventaggiato, M., Garbo, S., Bello, E. D., Fassari, B., Noce, B., Castiello, C., Lambona, C., Barreca, F., Rotili, D., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00337 · Cited by 25

Discovery of new human Sirtuin 5 inhibitors by mimicking glutaryl-lysine substrates

Yang, F., Su, H., Deng, J. W., Mou, L., Wang, H., Li, R., Dai, Q.-Q., Yan, Y., Qian, S., Wang, Z., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113803 · Cited by 24

The Study of Overexpression of Peroxiredoxin-2 Reduces MPP+-Induced Toxicity in the Cell Model of Parkinson’s Disease

Liu, M., Zuo, S., Guo, X., Peng, J., Xing, Y., Guo, Y., Li, C., & Xing, H. (2023) · Neurochemical Research · doi:10.1007/s11064-023-03880-5 · Cited by 24

The Role of Increased Expression of Sirtuin 6 in the Prevention of Premature Aging Pathomechanisms

Dzidek, A., Czerwińska‐Ledwig, O., Żychowska, M., Pilch, W., & Piotrowska, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119655 · Cited by 24

Biochemical Functions and Clinical Characterizations of the Sirtuins in Diabetes-Induced Retinal Pathologies

Taurone, S., Ponte, C. D., Rotili, D., Santis, E. D., Mai, A., Fiorentino, F., Scarpa, S., Artico, M., & Micera, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23074048 · Cited by 23

Exploring the Multi-Faceted Role of Sirtuins in Glioblastoma Pathogenesis and Targeting Options

Kunadis, E., & Piperi, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112889 · Cited by 23

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

Combating cellular senescence by sirtuins: Implications for atherosclerosis

Ma, S., Fan, L., & Cao, F. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.06.011 · Cited by 23

Differential Response of Lung Cancer Cells, with Various Driver Mutations, to Plant Polyphenol Resveratrol and Vitamin D Active Metabolite PRI-2191

Maj, E., Maj, B., Bobak, K., Gos, M., Chodyński, M., Kutner, A., & Wietrzyk, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052354 · Cited by 23

The NAD-dependent deacetylase SIRT2 regulates T cell differentiation involved in tumor immune response

Jiang, C., Liu, J., Guo, M., Gao, X., Wu, X., Bai, N., Guo, W., Li, N., Yi, F., Cheng, R., et al. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.49735 · Cited by 22

Hypothalamic Actions of SIRT1 and SIRT6 on Energy Balance

Quiñones, M., Martínez-Grobas, E., Fernø, J., Pérez-Lois, R., Seoane, L. M., & Al–Massadi, O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031430 · Cited by 23

Metformin prevents the onset and progression of intervertebral disc degeneration: New insights and potential mechanisms (Review)

Yang, W., Yang, Y., Wang, Y., Gao, Z., Zhang, J., Gao, W., Chen, Y., Lü, Y., Wang, H., Zhou, L., et al. (2024) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2024.5395 · Cited by 22

Akt-Dependent Glycolysis-Driven Lipogenesis Supports Proliferation and Survival of Human Pulmonary Arterial Smooth Muscle Cells in Pulmonary Hypertension

Jiang, L., Goncharov, D. A., Shen, Y., Lin, D., Chang, B., Pena, A. Z., DeLisser, H. M., Goncharova, E. A., & Kudryashova, T. V. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.886868 · Cited by 21

Modulation of tumor‐associated macrophages in colitis‐associated colorectal cancer

Dong, Y., Yang, Q., Niu, R., Zhang, Z., Huang, Y., Bi, Y., & Liu, G. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30906 · Cited by 22

Yinchen Linggui Zhugan decoction ameliorates high fat diet-induced nonalcoholic fatty liver disease by modulation of SIRT1/Nrf2 signaling pathway and gut microbiota

Jiang, H., Mao, T., Sun, Z., Shi, L., Han, X., Zhang, Y., Zhang, X., Wang, J., Hu, J., Zhang, L., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1001778 · Cited by 23

Resveratrol: Its Path from Isolation to Therapeutic Action in Eye Diseases

Pop, R., Dăescu, A. M., Rugină, D. O., & Pintea, A. (2022) · Antioxidants · doi:10.3390/antiox11122447 · Cited by 23

Insights into the Therapeutic and Pharmacological Properties of Resveratrol as a Nutraceutical Antioxidant Polyphenol in Health Promotion and Disease Prevention

Mohammadi, S., Moghadam, M. D., Nasiriasl, M., Akhzari, M., & Barazesh, M. (2024) · Current Clinical Pharmacology · doi:10.2174/0127724328268507231218051058 · Cited by 22

SIRT6 activates PPARα to improve doxorubicin-induced myocardial cell aging and damage

Wang, S., Zhang, X., Hou, Y., Zhang, Y., Chen, J., Gao, S., Duan, H., Gu, S., Yu, S., & Cai, Y. (2024) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2024.110920 · Cited by 22

Chemogenomic analysis reveals key role for lysine acetylation in regulating Arc stability

Lalonde, J., Reis, S. A., Sivakumaran, S., Holland, C. S., Wesseling, H., Sauld, J. F. K., Alural, B., Zhao, W., Steen, J. A. J., & Haggarty, S. J. (2017) · Nature Communications · doi:10.1038/s41467-017-01750-7 · Cited by 23

Survival and Clinicopathological Significance of SIRT1 Expression in Cancers: A Meta-Analysis

Sun, M., Du, M., Zhang, W., Xiong, S., Gong, X., Lei, P., Zha, J., Zhu, H., Li, H., Huang, D., et al. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00121 · Cited by 21

Deacetylation of CHK2 by SIRT1 protects cells from oxidative stress-dependent DNA damage response

Kwon, J., Lee, S., Kim, Y.-N., & Lee, I. H. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0232-4 · Cited by 22

Recent advances in epigenetic proteolysis targeting chimeras (Epi-PROTACs)

Tomaselli, D., Mautone, N., Mai, A., & Rotili, D. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112750 · Cited by 21

Regulation of Cellular Immune Responses in Sepsis by Histone Modifications

Carson, W. F., & Kunkel, S. L. (2016) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2016.08.004 · Cited by 20

Multifaced role of protein deacetylase sirtuins in neurodegenerative disease

Gupta, R. V., Ambasta, R. K., & Kumar, P. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.10.047 · Cited by 20

NSAID targets SIRT3 to trigger mitochondrial dysfunction and gastric cancer cell death

Debsharma, S., Pramanik, S., Bindu, S., Mazumder, S., Das, T., Pal, U., Saha, D., De, R., Nag, S., Banerjee, C., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109384 · Cited by 20

Sirtuin 6 mitigated LPS‐induced human umbilical vein endothelial cells inflammatory responses through modulating nuclear factor erythroid 2‐related factor 2

Qin, Y., Cao, L., & Hu, L. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28407 · Cited by 20

Arsenic Trioxide, Itraconazole, All-Trans Retinoic Acid and Nicotinamide: A Proof of Concept for Combined Treatments with Hedgehog Inhibitors in Advanced Basal Cell Carcinoma

Cosio, T., Prete, M. D., & Campione, E. (2020) · Biomedicines · doi:10.3390/biomedicines8060156 · Cited by 20

Rapha Myr®, a Blend of Sulforaphane and Myrosinase, Exerts Antitumor and Anoikis-Sensitizing Effects on Human Astrocytoma Cells Modulating Sirtuins and DNA Methylation

Tomasello, B., Mauro, M. D. D., Malfa, G. A., Acquaviva, R., Sinatra, F., Spampinato, G., Laudani, S., Villaggio, G., Bielak-Żmijewska, A., Grabowska, W., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155328 · Cited by 19

Cooperative effects of SIRT1 and SIRT2 on APP acetylation

Li, N., Bai, N., Zhao, X., Cheng, R., Wu, X., Jiang, B., Li, X., Xue, M., Xu, H., Guo, Q., et al. (2023) · Aging Cell · doi:10.1111/acel.13967 · Cited by 19

Serum Sirtuin 1, 3 and 6 Levels in Acute Myocardial Infarction Patients

Kızıltunç, E., Kösem, A., Özkan, C., Uğurlu, B., Kundi, H., Çetın, M., & Örnek, E. (2019) · Arquivos Brasileiros de Cardiologia · doi:10.5935/abc.20190114 · Cited by 20

Unraveling the Unbinding Pathways of Products Formed in Catalytic Reactions Involved in SIRT1–3: A Random Acceleration Molecular Dynamics Simulation Study

Muvva, C., Murugan, N. A., Choutipalli, V. S. K., & Subramanian, V. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00513 · Cited by 19

The Serum Concentration of Anti-Aging Proteins, Sirtuin1 and αKlotho in Patients with End-Stage Kidney Disease on Maintenance Hemodialysis

Zbroch, E., Bielach-Bazyluk, A., Małyszko, J., Koc‐Żórawska, E., Rydzewska–Rosołowska, A., Kakareko, K., & Hryszko, T. (2020) · Clinical Interventions in Aging · doi:10.2147/cia.s236980 · Cited by 19

The role of autophagy in fibrosis: Mechanisms, progression and therapeutic potential (Review)

Chen, Y., Wang, Z., Ma, Q., & Sun, C. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5502 · Cited by 23

Sirtuin 6 is a key contributor to gender differences in acute kidney injury

Miao, J., Huang, J., Liang, Y., Zhang, Y., Li, J., Meng, P., Shen, W., Li, X., Wu, Q., Wang, X., et al. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01432-y · Cited by 18

The role of Klotho and sirtuins in sleep-related cardiovascular diseases: a review study

Rostamzadeh, F., Joukar, S., & Yeganeh‐Hajahmadi, M. (2024) · npj Aging · doi:10.1038/s41514-024-00165-1 · Cited by 18

Metabolomic analysis of longissimus from underperforming piglets relative to piglets with normal preweaning growth

Ramsay, T. G., Stoll, M. J., Shannon, A. E., & Blomberg, L. A. (2018) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-018-0251-3 · Cited by 18

Structure activity study of S-trityl-cysteamine dimethylaminopyridine derivatives as SIRT2 inhibitors: Improvement of SIRT2 binding and inhibition

Radwan, M. O., Ciftci, H. I., Ali, T. F. S., Koga, R., Tateishi, H., Nakata, A., Ito, A., Yoshida, M., Fujita, M., & Otsuka, M. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127458 · Cited by 18

Sirtuins play critical and diverse roles in acute kidney injury

Peasley, K., Chiba, T., Goetzman, E. S., & Sims‐Lucas, S. (2021) · Pediatric Nephrology · doi:10.1007/s00467-020-04866-z · Cited by 18

MiR-140-3p inhibits the cell viability and promotes apoptosis of synovial fibroblasts in rheumatoid arthritis through targeting sirtuin 3

Zu, B., Liu, L., Wang, J., Li, M., & Yang, J. (2021) · Journal of Orthopaedic Surgery and Research · doi:10.1186/s13018-021-02236-5 · Cited by 18

Global research trends and hot spots on autophagy and kidney diseases: a bibliometric analysis from 2000 to 2022

Ai, S., Li, Y., Zheng, H., Wang, Z., Liu, W., Tao, J., Li, Y., & Wang, Y. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1275792 · Cited by 17

The Pan-Sirtuin Inhibitor MC2494 Regulates Mitochondrial Function in a Leukemia Cell Line

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SIRT6 mediates MRTF-A deacetylation in vascular endothelial cells to antagonize oxLDL-induced ICAM-1 transcription

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Expanding the Accessible Chemical Space of SIRT2 Inhibitors through Exploration of Binding Pocket Dynamics

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Modulation of autophagy by melatonin via sirtuins in stroke: From mechanisms to therapies

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Assisted reproductive technique in women of advanced fertility age

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

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Sirtuin modulators: small molecules and natural compounds

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Sirtuin-targeting drugs: Mechanisms of action and potential therapeutic applications.

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Sirtuins and Disease: The Road Ahead

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