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

Agomelatine improves streptozotocin-induced diabetic nephropathy through melatonin receptors/SIRT1 signaling pathway

Mahmoud, N. M., Elshazly, S. M., Hassan, A. A., & Soliman, E. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109646 · Cited by 14

Treating Metabolic Dysregulation and Senescence by Caloric Restriction: Killing Two Birds with One Stone?

Russo, L., Babboni, S., Andreassi, M. G., Daher, J., Canale, P., Turco, S. D., & Basta, G. (2025) · Antioxidants · doi:10.3390/antiox14010099 · Cited by 16

Design, synthesis, in-vitro evaluation and molecular docking studies of novel indole derivatives as inhibitors of SIRT1 and SIRT2

Manjula, R., Gokhale, N., Unni, S., Deshmukh, P. H., Reddyrajula, R., Bharath, M. M. S., Dalimba, U., & Padmanabhan, B. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103281 · Cited by 14

A scaffold replacement approach towards new sirtuin 2 inhibitors

Seifert, T., Malo, M., Kokkola, T., Stéen, E. J. L., Meinander, K., Wallén, E. A. A., Jarho, E. M., & Luthman, K. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.115231 · Cited by 14

Oxidative nucleophilic substitution selectively produces cambinol derivatives with antiproliferative activity on bladder cancer cell lines

Botta, L., Filippi, S., Bizzarri, B. M., Meschini, R., Caputo, M., Proietti‐De‐Santis, L., Iside, C., Nebbioso, A., Gualandi, G., & Saladino, R. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.11.006 · Cited by 14

CircVAPA contributes to hyper-proliferation and inflammation of keratinocytes through miR-125b-5p/sirt6 axis in psoriasis

Chen, H., Xu, Z., Wang, Y., Xu, J., He, K., Wang, H., Bai, X., & Xiang, G. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109632 · Cited by 13

Targeting impaired nutrient sensing via the sirtuin pathway with novel compounds to prevent or treat dementia: A systematic review

Matysek, A., Sun, L., Kimmantudawage, S. P., Feng, L., & Maier, A. B. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102029 · Cited by 15

Sirtuins as Potential Targets for Neuroprotection: Mechanisms of Early Brain Injury Induced by Subarachnoid Hemorrhage

Lei, K., Wu, R., Wang, J., Lei, X., Zhou, E., Fan, R., & Gong, L. (2023) · Translational Stroke Research · doi:10.1007/s12975-023-01191-z · Cited by 14

Hippocampal SIRT1 signaling mediates the ameliorative effect of treadmill exercise on anxiety- and depression-like behavior in APP/PS1 mice

Wang, Y., Zhang, Z., Jiang, Y., Liao, J., Mu, L., & Hu, M. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1489214 · Cited by 16

Resveratrol and SIRT1 Activators for the Treatment of Aging and Age-Related Diseases

Stacchiotti, A., Favero, G., & Rezzani, R. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.78977 · Cited by 16

Identification of Inhibitors to Trypanosoma cruzi Sirtuins Based on Compounds Developed to Human Enzymes

Bastos, T. M., Soares, M. B. P., Franco, C. H., Alcântara, L. M., Antonini, L., Sabatino, M., Mautone, N., Freitas-Junior, L. H., Moraes, C. B., Ragno, R., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103659 · Cited by 13

Agomelatine ameliorates cadmium-induced toxicity through the modification of HMGB-1/TLR-4/NFκB pathway

Hafez, H. M., Waz, S., El‐Tahawy, N. F. G., & Mohamed, M. Z. (2022) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2022.116313 · Cited by 13

The use of Nicotinamide and Nicotinamide riboside as an adjunct therapy in the treatment of glaucoma

Silva, S. G. N. E., Occhiutto, M. L., & Costa, V. P. (2023) · European Journal of Ophthalmology · doi:10.1177/11206721231161101 · Cited by 14

SIRT6 Maintains Redox Homeostasis to Promote Porcine Oocyte Maturation

Li, Y., Miao, Y., Chen, J., & Xiong, B. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.625540 · Cited by 14

Icosapent ethyl alleviates acetic acid-induced ulcerative colitis via modulation of SIRT1 signaling pathway in rats

Abdelsameea, A. A., Alsemeh, A. E., Alabassery, N., Samy, W. M., Fawzy, A., & Abbas, N. A. T. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109621 · Cited by 12

Discovery of Novel SIRT1/2 Inhibitors with Effective Cytotoxicity against Human Leukemia Cells

Cai, H., Wang, Y., Zhang, J., Wei, Z., Yan, T., Feng, C., Xu, Z., Zhou, A., & Wu, Y. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c00556 · Cited by 12

Histone acetylation regulated by histone deacetylases during spermatogenesis

Ou, X., Yang, J., Yang, L., Zeng, H., & Shao, L. (2024) · Andrology · doi:10.1111/andr.13723 · Cited by 12

Opening the Selectivity Pocket in the Human Lysine Deacetylase Sirtuin2 – New Opportunities, New Questions

Robaa, D., Monaldi, D., Wössner, N., Kudo, N., Rumpf, T., Schiedel, M., Yoshida, M., & Jung, M. (2018) · The Chemical Record · doi:10.1002/tcr.201800044 · Cited by 12

SIRT1-SIRT7 Expression in Patients with Lymphoproliferative Disorders Undergoing Hematopoietic Stem Cell Mobilization

Nowicki, M., Wierzbowska, A., Stec‐Martyna, E., Kulczycka-Wojdala, D., Nowicki, G., & Szmigielska‐Kapłon, A. (2022) · Cancers · doi:10.3390/cancers14051213 · Cited by 12

E3 ligase adaptor FBXO7 contributes to ubiquitination and proteasomal degradation of SIRT7 and promotes cell death in response to hydrogen peroxide

Lee, S. H., Lee, Y. J., Jung, S., & Chung, K. C. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.102909 · Cited by 12

Sirtuins, Healthspan, and Longevity in Mammals

Giblin, W., & Lombard, D. B. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-411596-5.00003-4 · Cited by 12

Leucine regulates lipid metabolism in adipose tissue through adipokine-mTOR-SIRT1 signaling pathway and bile acid–microbe axis in a finishing pig model

Yin, Y., Gong, S., Han, M., Wang, J., Shi, H., Jiang, X., Guo, L., Duan, Y., Guo, Q., Chen, Q., et al. (2023) · Animal nutrition · doi:10.1016/j.aninu.2023.10.005 · Cited by 11

Current epigenetic aspects the clinical kidney researcher should embrace

Witasp, A., Craenenbroeck, A. H. V., Shiels, P. G., Ekström, T. J., Stenvinkel, P., & Nordfors, L. (2017) · Clinical Science · doi:10.1042/cs20160596 · Cited by 13

Arabidopsis thaliana sirtuins control proliferation and glutamate dehydrogenase activity

Bruscalupi, G., Micco, P. D., Failla, C. M., Pascarella, G., Morea, V., Saliola, M., Paolis, A. D., Venditti, S., & Mauro, M. L. (2022) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2022.11.007 · Cited by 11

SPC-180002, a SIRT1/3 dual inhibitor, impairs mitochondrial function and redox homeostasis and represents an antitumor activity

Cho, Y., Hwang, J. W., Park, N.-J., Moon, J., Ali, K. H., Seo, Y. H., Kim, I. S., Kim, S., & Kim, Y. K. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.07.033 · Cited by 11

Opportunities and Difficulties in the Repurposing of HDAC Inhibitors as Antiparasitic Agents

Mohapatra, T. K., Nayak, R. R., Ganeshpurkar, A., Tiwari, P. K., & Kumar, D. (2024) · Drugs and Drug Candidates · doi:10.3390/ddc3010006 · Cited by 11

Dietary fatty acids as nutritional modulators of sirtuins: a systematic review

Caldas, A. P. S., Rocha, D. M. U. P., Bressan, J., & Hermsdorff, H. H. M. (2020) · Nutrition Reviews · doi:10.1093/nutrit/nuaa007 · Cited by 11

Are Hippocampal Hypoperfusion and ATP Depletion Prime Movers in the Genesis of Alzheimer’s Disease? A Review of Recent Pertinent Observations from Molecular Biology

Walker, V. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157328 · Cited by 11

Importance of Nutrient Availability and Metabolism for Skeletal Muscle Regeneration

Blum, J., Epstein, R., Watts, S. A., & Thalacker‐Mercer, A. E. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.696018 · Cited by 15

Role of SIRT1 in Potentially Toxic Trace Elements (Lead, Fluoride, Aluminum and Cadmium) Associated Neurodevelopmental Toxicity

Fathima, A., Bagang, N., Kumar, N., Dastidar, S. G., & Shenoy, S. (2024) · Biological Trace Element Research · doi:10.1007/s12011-024-04116-5 · Cited by 12

Silent Information Regulator 1/Peroxisome Proliferator‐Activated Receptor‐γ Coactivator‐1α Axis: A Promising Target for Parkinson's and Alzheimer's Disease Therapies

Goyal, A., Kumari, A., Verma, A., Chaudhary, V., Agrawal, V., & Yadav, H. N. (2024) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.70078 · Cited by 10

Advancements in understanding the role and mechanism of sirtuin family (SIRT1-7) in breast cancer management

Sharma, D. K., Panchaksaram, M., & Muniyan, R. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116743 · Cited by 10

Antagonistic Interaction between Histone Deacetylase Inhibitor: Cambinol and Cisplatin—An Isobolographic Analysis in Breast Cancer In Vitro Models

Hałasa, M., Łuszczki, J. J., Dmoszyńska‐Graniczka, M., Baran, M. T., Okoń, E., Stepulak, A., & Wawruszak, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168573 · Cited by 10

The emerging importance of NAD+ metabolome for nutrition and food sciences: A bibliometric analysis

Alegre, G. F. S., & Pastore, G. M. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.103126 · Cited by 10

Interaction of Klotho and sirtuins

Rostamzadeh, F., Moosavi-Saeed, Y., & Yeganeh‐Hajahmadi, M. (2023) · Experimental Gerontology · doi:10.1016/j.exger.2023.112306 · Cited by 10

Nuclear Nicotinamide Adenine Dinucleotide Deficiency by Nmnat1 Deletion Impaired Hepatic Insulin Signaling, Mitochondrial Function, and Hepatokine Expression in Mice Fed a High-Fat Diet

Dong, H., Guo, W., Yue, R., Sun, X., & Zhou, Z. (2024) · Laboratory Investigation · doi:10.1016/j.labinv.2024.100329 · Cited by 10

Bioinformatics Analysis of the SIRT Family Members and Assessment of Their Potential Clinical Value

Liu, M., Yu, J., Hu, J., Wang, S., Ding, J., Xing, H., He, S., & Zeng, Y. (2021) · OncoTargets and Therapy · doi:10.2147/ott.s298616 · Cited by 10

Age-Associated Changes of Sirtuin 2 Expression in CNS and the Periphery

Garmendia-Berges, M., Sola-Sevilla, N., Mera-Delgado, M., & Puerta, E. (2023) · Biology · doi:10.3390/biology12121476 · Cited by 9

Sirtuin 3 ameliorates inflammatory bowel disease via inhibiting intestinal inflammation and oxidative stress

Qin, Z., Chu, Q., Ding, A.-L., Li, C., & Zhang, M.-Y. (2024) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.23-42 · Cited by 9

Role of sirtuins in sepsis and sepsis-induced organ dysfunction: A review

Yang, X., Wen, R., Yang, N., & Zhang, T. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134853 · Cited by 9

Exercise in Diabetic Cardiomyopathy: Its Protective Effects and Molecular Mechanism

Chen, H.-M., & Guo, L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26041465 · Cited by 12

Metformin alleviates HFD-induced oxidative stress in hepatocyte via activating SIRT6/PGC-1α/ENDOG signaling

Gao, S., Yang, Q., Liu, Z., Kong, W., Chen, J., Xie, L., Peng, Y., Bao, M., Bian, X., Zhang, Y., et al. (2022) · Clinical Science · doi:10.1042/cs20220242 · Cited by 9

Exogenous Nicotinamide Adenine Dinucleotide Attenuates Postresuscitation Myocardial and Neurologic Dysfunction in a Rat Model of Cardiac Arrest

Su, C., Xiao, Y., Zhang, G., Liang, L., Li, H., Cheng, C., Jin, T., Bradley, J., Peberdy, M. A., Ornato, J. P., et al. (2021) · Critical Care Medicine · doi:10.1097/ccm.0000000000005268 · Cited by 9

Hit evaluation results in 5-benzyl-1,3,4-thiadiazole-2-carboxamide based SIRT2-selective inhibitor with improved affinity and selectivity

Gozelle, M., Kaya, S. G., Aksel, A. B., Özkan, E., Bakar‐Ates, F., Özkan, Y., & Eren, G. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.105746 · Cited by 9

Mammalian Sirtuins and Their Relevance in Vascular Calcification

Pan, X., Pi, C., Ruan, X., Zheng, H., Zhang, D., & Liu, X. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.907835 · Cited by 9

The new function of FaSRT2-1 protein in energy metabolism: Promoting strawberry fruit quality and ripening

Yang, M., Song, C., He, X., Wang, L., He, C., Yu, H., Xiao, W., Lin, Y., Zhang, Y., Wang, Y., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136199 · Cited by 8

A Multi-Target Pharmacological Correction of a Lipoyltransferase LIPT1 Gene Mutation in Patient-Derived Cellular Models

Gómez-Fernández, D., Romero-González, A., Suarez-Rivero, J. M., Cilleros-Holgado, P., Álvarez-Córdoba, M., Piñero-Pérez, R., Romero-Domínguez, J. M., Reche-López, D., López-Cabrera, A., Ibáñez‐Micó, S., et al. (2024) · Antioxidants · doi:10.3390/antiox13081023 · Cited by 9

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

SIRT7 is a Prognostic Biomarker in Kidney Renal Clear Cell Carcinoma That is Correlated with Immune Cell Infiltration

Li, M., Qian, Y., Mu, L., Wang, Y., Jin, X., & Zhang, W. (2022) · International Journal of General Medicine · doi:10.2147/ijgm.s353610 · Cited by 8

Dietary energy restriction in neurological diseases: what’s new?

Zhang, B., Huang, R., Xu, S., He, Y., Li, J., Wan, L., Xiao, B., & Luo, Z. (2022) · European Journal of Nutrition · doi:10.1007/s00394-022-03036-1 · Cited by 8

The Role of SIRT1 in Leukemia

Wu, Z., Lyu, T., Wu, L., Yang, H., & Li, W. (2024) · Current Treatment Options in Oncology · doi:10.1007/s11864-024-01265-6 · Cited by 7

NAA60 (HAT4): the newly discovered bi-functional Golgi member of the acetyltransferase family

Donnarumma, F., Tucci, V., Ambrosino, C., Altucci, L., & Carafa, V. (2022) · Clinical Epigenetics · doi:10.1186/s13148-022-01402-8 · Cited by 7

Genetic modification of miR-34a enhances efficacy of transplanted human dental pulp stem cells after ischemic stroke

Wang, J., He, P., Tian, Q., Luo, Y., He, Y., Liu, C., Gong, P., Guo, Y., Ye, Q., & Li, M. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.367831 · Cited by 7

AtSRT1 regulates flowering by regulating flowering integrators and energy signals in Arabidopsis

Wang, P., Su, L., Cao, L., Hu, H., Wan, H., Wu, C., Zheng, Y., Bao, C., & Liu, X. (2024) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2024.108841 · Cited by 7

Fructose Intake: Metabolism and Role in Diseases

He, L., Babar, G., Redel, J. M., Young, S. L., Chagas, C. E., Moore, W. V., & Yan, Y. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.95754 · Cited by 7

The potential of 4-aryl-6-morpholino-3(2H)-pyridazinone-2-arylpiperazinylacetamide as a new scaffold for SIRT2 inhibition: in silico approach guided by pharmacophore mapping and molecular docking

Sukuroglu, M. K., Gozelle, M., Özkan, Y., & Eren, G. (2021) · Medicinal Chemistry Research · doi:10.1007/s00044-021-02782-x · Cited by 7

Trichostatin A and Sirtinol Regulate the Expression and Nucleocytoplasmic Shuttling of Histone Deacetylases in All-Trans Retinoic Acid-Induced Differentiation of Neuroblastoma Cells

Jang, B.-G., Choi, B., Kim, S., Lee, J., & Kim, M.-J. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1050-1 · Cited by 7

Deacetylation-activated construction of single quantum dot-based nanosensor for sirtuin 1 assay

Hu, J., Pan, L., Li, Y., Zou, X., Liu, B., Jiang, B., & Zhang, C. (2020) · Talanta · doi:10.1016/j.talanta.2020.121918 · Cited by 7

Mitochondrial Deoxyguanosine Kinase Regulates NAD+ Biogenesis Independent of Mitochondria Complex I Activity

Sang, L., He, Y., Kang, J., Ye, H., Bai, W., Luo, X., & Sun, J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.570656 · Cited by 7

Reactivity‐Tunable Fluorescent Platform for Selective and Biocompatible Modification of Cysteine or Lysine

Ren, X., Li, H., Peng, H., Yang, Y., Su, H., Huang, C., Wang, X., Zhang, J., Liu, Z., Wei, W., et al. (2024) · Advanced Science · doi:10.1002/advs.202402838 · Cited by 5

NAD+ enhancers as therapeutic agents in the cardiorenal axis

Marin-Blazquez, M., Rovira, J., Ramírez-Bajo, M. J., Perez, R. Z., & Rabadán-Ros, R. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01903-4 · Cited by 7

Sirtuin Family in Acute Kidney Injury: Insights into Cellular Mechanisms and Potential Targets for Treatment

Yang, S., Wu, C., Li, S., Zhao, S., & Fan, C. (2025) · Biomolecules · doi:10.3390/biom15101445 · Cited by 6

The role of histone deacetylases in inflammatory respiratory diseases: an update

Pan, S., Wang, X., Jiao, J., & Zhang, L. (2024) · Expert Review of Clinical Immunology · doi:10.1080/1744666x.2024.2363803 · Cited by 6

Is SIRT3 and Mitochondria a Reliable Target for Parkinson’s Disease and Aging? A Narrative Review

Kandy, A. T., Chand, J., Baba, M. Z., & Subramanian, G. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04486-w · Cited by 6

Traditional Therapeutics and Potential Epidrugs for CVD: Why Not Both?

Gladwell, L. R., Ahiarah, C., Rasheed, S., Rahman, S. M., & Choudhury, M. (2023) · Life · doi:10.3390/life14010023 · Cited by 7

Sirtuin 6 protects human retinal pigment epithelium cells from LPS-induced inflammation and apoptosis partly by regulating autophagy

Liu, J., & Liu, D. (2020) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2020.1788377 · Cited by 6

Molecular imaging of NAD+‐dependent deacetylase SIRT1 in the brain

Xu, Y., Chen, Z., Wey, H., Liang, Y., Tanzi, R. E., Zhang, C. M., & Wang, C. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12344 · Cited by 6

Medicinal chemistry of histone deacetylase inhibitors

Ružić, D., Djoković, N., Nikolic, K. M., & Vujić, Z. B. (2021) · Arhiv za farmaciju · doi:10.5937/arhfarm71-30618 · Cited by 6

Insight from sirtuins interactome: topological prominence and multifaceted roles of SIRT1 in modulating immunity, aging and cancer

Zulkifli, N. D., & Zulkifle, N. (2023) · Genomics & Informatics · doi:10.5808/gi.23003 · Cited by 5

Hydrogen Sulfide Promotes Postnatal Cardiomyocyte Proliferation by Upregulating SIRT1 Signaling Pathway

Gan, L., Peng, C., Wu, J., Li, Q., Pan, J., Ding, Y., Gao, X.-F., & Chen, L. (2024) · International Heart Journal · doi:10.1536/ihj.23-370 · 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

Lead-Structure-Based Rigidization Approach to Optimize SirReal-Type Sirt2 Inhibitors

Frei, M., Wein, T., & Bracher, F. (2025) · Molecules · doi:10.3390/molecules30081728 · Cited by 5

SIRT2-mediated ACSS2 K271 deacetylation suppresses lipogenesis under nutrient stressPreprint

Karim, R., Teng, W., Behram, C. D., & Lin, H. (2024) · eLife · doi:10.7554/elife.97019.3 · Cited by 6

SIRT1 Activation Promotes Long-Term Functional Recovery After Subarachnoid Hemorrhage in Rats

Chu, D., Li, X., Qu, X., Diwan, D., Warner, D. S., Zipfel, G. J., & Sheng, H. (2022) · Neurocritical Care · doi:10.1007/s12028-022-01614-z · Cited by 7

Bisphenol A instigates diminished sirtuin-1 mediated vascular complications in type 2 diabetes mellitus

Nehru, M., Subramanian, P., Ganesan, V. K., Janardhanan, R., & Venkataraman, P. (2023) · Journal of Nephropharmacology · doi:10.34172/npj.2023.10531 · Cited by 5

Cellular senescence: A potential mode of circular RNAs regulating prostate cancer

Li, Y., Fan, A., Zhang, Y., Guo, Z., Meng, W., Pan, W., Ma, Z., & Chen, W. (2023) · MedComm – Oncology · doi:10.1002/mog2.61 · Cited by 6

Novel xanthone derivatives as potent sirtuin 2 inhibitors

Mazur, G., Pańczyk, K., Krysińska, K., Niemiec, K., & Waszkielewicz, A. M. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129620 · Cited by 5

New sirtuin modulators: their uncovering, pharmacophore, and implications in drug discovery

Chen, P.-T., & Yeong, K. Y. (2024) · Medicinal Chemistry Research · doi:10.1007/s00044-024-03249-5 · Cited by 8

SIRT7 Inhibits Melanin Synthesis of PIG1 and PIG3V by Suppressing the Succinylation of EZR

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The sirtuin family in health and disease

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