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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 1,138 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697 · see citing works

Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins

Feldman, J. L., Baeza, J., & Denu, J. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.511261 · Cited by 637 · see citing works

SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation

Barber, M. F., Michishita-Kioi, E., Xi, Y., Tasselli, L., Kioi, M., Moqtaderi, Z., Tennen, R. I., Paredes, S., Young, N. L., Chen, K., et al. (2012) · Nature · doi:10.1038/nature11043 · Cited by 621 · see citing works

Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS

Chen, Y., Zhang, J., Lin, Y., Lei, Q., Guan, K., Zhao, S., & Xiong, Y. (2011) · The EMBO Reports · doi:10.1038/embor.2011.65 · Cited by 572 · see citing works

Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase

Liszt, G., Ford, E., Kurtev, M., & Guarente, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413296200 · Cited by 548 · see citing works

Identification of a Class of Small Molecule Inhibitors of the Sirtuin Family of NAD-dependent Deacetylases by Phenotypic Screening

Grozinger, C. M., Chao, E. D., Blackwell, H. E., Moazed, D., & Schreiber, S. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106779200 · Cited by 533 · see citing works

Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity

Mathias, R. A., Greco, T. M., Oberstein, A., Budayeva, H. G., Chakrabarti, R., Rowland, E. A., Kang, Y., Shenk, T., & Cristea, I. M. (2014) · Cell · doi:10.1016/j.cell.2014.11.046 · Cited by 430 · see citing works

Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation

Hirschey, M. D., & Zhao, Y. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r114.046664 · Cited by 423 · see citing works

SIRT1 and SIRT2: emerging targets in neurodegeneration

Dönmez, G., & Outeiro, T. F. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302451 · Cited by 414 · see citing works

Structure of the histone deacetylase SIRT2.

Finnin, M. S., Donigian, J. R., & Pavletich, N. P. (2001) · Nature Structural Biology · doi:10.1038/89668 · Cited by 376 · see citing works

Chromatin and beyond: the multitasking roles for SIRT6

Kugel, S., & Mostoslavsky, R. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.002 · Cited by 367 · see citing works

SIRT1 and energy metabolism

Li, X. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms108 · Cited by 360 · see citing works

The Dual Role of Sirtuins in Cancer

Bosch‐Presegué, L., & Vaquero, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417862 · Cited by 329 · see citing works

Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach

Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D. (2014) · eLife · doi:10.7554/elife.02999 · Cited by 324 · see citing works

Histone Deacetylase Genes in Arabidopsis Development

Hollender, C. A., & Liu, Z. (2008) · Journal of Integrative Plant Biology · doi:10.1111/j.1744-7909.2008.00704.x · Cited by 301 · see citing works

A SIRT7-Dependent Acetylation Switch of GABPβ1 Controls Mitochondrial Function

Ryu, D., Jo, Y. S., Sasso, G. L., Stein, S., Zhang, H., Perino, A., Lee, J. U., Zeviani, M., Romand, R., Hottiger, M. O., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.001 · Cited by 258 · see citing works

Structural basis for sirtuin function: What we know and what we don't

Sanders, B. D., Jackson, B. A., & Marmorstein, R. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.09.009 · Cited by 248 · see citing works

Mitochondrial Metabolism, Sirtuins, and AgingPreprint

Sack, M. N., & Finkel, T. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013102 · Cited by 237 · see citing works

Sirtuin/Sir2 Phylogeny, Evolutionary Considerations and Structural Conservation

Greiss, S., & Gartner, A. (2009) · Molecules and Cells · doi:10.1007/s10059-009-0169-x · Cited by 207 · see citing works

Kinetic and Structural Basis for Acyl-Group Selectivity and NAD+ Dependence in Sirtuin-Catalyzed Deacylation

Feldman, J. L., Dittenhafer‐Reed, K. E., Kudo, N., Thelen, J. N., Ito, A., Yoshida, M., & Denu, J. M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00150 · Cited by 189 · see citing works

Efficient Demyristoylase Activity of SIRT2 Revealed by Kinetic and Structural Studies

Teng, Y.-B., Jing, H., Aramsangtienchai, P., He, B., Khan, S., Hu, J., Lin, H., & Hao, Q. (2015) · Scientific Reports · doi:10.1038/srep08529 · Cited by 184 · see citing works

Sirtuins and Disease: The Road Ahead

Carafa, V., Nebbioso, A., & Altucci, L. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00004 · Cited by 179 · see citing works

Histone Deacetylases

Parbin, S., Kar, S., Shilpi, A., Sengupta, D., Deb, M., Rath, S. K., & Patra, S. K. (2013) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155413506582 · Cited by 172 · see citing works

Sirt6 Regulates Tnf-Alpha Secretion Through Hydrolysis of Long-Chain Fatty Acyl Lysine

Jiang, H. X., Khan, S., Wang, Y., Charron, G., He, B., Sebastián, C., Du, J., Kim, R., Ge, E. J., Mostoslavsky, R., et al. (2013) · Nature · doi:10.2210/pdb3zg6/pdb · Cited by 169 · see citing works

Histone deacetylases and their functions in plants

Ma, X., Lv, S., Zhang, C., & Yang, C. (2013) · Plant Cell Reports · doi:10.1007/s00299-013-1393-6 · Cited by 164 · see citing works

Structural Basis for Sirtuin Activity and Inhibition

Yuan, H., & Marmorstein, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.372300 · Cited by 160 · see citing works

Mitochondrial Sirtuins and Their Relationships with Metabolic Disease and Cancer

Kumar, S., & Lombard, D. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6213 · Cited by 158 · see citing works

Sirtuin-7 Inhibits the Activity of Hypoxia-inducible Factors

Hubbi, M. E., Hu, H., Gupta, K., Gilkes, D. M., & Semenza, G. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.476903 · Cited by 152 · see citing works

The chemical biology of sirtuins

Chen, B., Zang, W., Wang, J., Huang, Y., He, Y., Yan, L., Liu, J., & Zheng, W. (2015) · Chemical Society Reviews · doi:10.1039/c4cs00373j · Cited by 142 · see citing works

Regulation of Sirtuin Function by Posttranslational Modifications

Flick, F., & Lüscher, B. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00029 · Cited by 140 · see citing works

Arabidopsis Putative Deacetylase AtSRT2 Regulates Basal Defense by Suppressing PAD4, EDS5 and SID2 Expression

Wang, C., Gao, F., Wu, J., Dai, J., Wei, C., & Li, Y. (2010) · Plant and Cell Physiology · doi:10.1093/pcp/pcq087 · Cited by 139 · see citing works

SIRT2 as a Therapeutic Target for Age-Related Disorders

de Oliveira, R. M., Sarkander, J., Kazantsev, A. G., & Outeiro, T. F. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00082 · Cited by 138 · see citing works

The Sirtuin-2 Inhibitor AK7 Is Neuroprotective in Models of Parkinson’s Disease but Not Amyotrophic Lateral Sclerosis and Cerebral Ischemia

Chen, X., Wales, P., Quinti, L., Zuo, F., Moniot, S., Hérisson, F., Rauf, N. A., Wang, H., Silverman, R. B., Ayata, C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116919 · Cited by 138 · see citing works

Epigenetic effects of natural polyphenols: A focus on SIRT1‐mediated mechanisms

Owona, V. B. A., Ebrahimi, A., & Schluesener, H. J. (2013) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201300195 · Cited by 125 · see citing works

Sirtuin 7 Plays a Role in Ribosome Biogenesis and Protein Synthesis

Tsai, Y.-C., Greco, T. M., & Cristea, I. M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031377 · Cited by 124 · see citing works

Sirtuins: NAD+-dependent deacetylase mechanism and regulation

Sauve, A. A., & Youn, D. Y. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.10.003 · Cited by 119 · see citing works

The conserved role of sirtuins in chromatin regulation

Vaquero, A. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082675av · Cited by 116 · see citing works

The Arabidopsis Class II Sirtuin Is a Lysine Deacetylase and Interacts with Mitochondrial Energy Metabolism

König, A., Hartl, M., Pham, P. A., Laxa, M., Boersema, P. J., Orwat, A., Kalitventseva, I., Plöchinger, M., Braun, H., Leister, D., et al. (2014) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.232496 · Cited by 116 · see citing works

Potential Modulation of Sirtuins by Oxidative Stress

Santos, L., Escande, C., & Denicola, A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9831825 · Cited by 115 · see citing works

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 112 · see citing works

A small molecule Inauhzin inhibits SIRT1 activity and suppresses tumour growth through activation of p53

Zhang, Q., Zeng, S. X., Zhang, Y., Zhang, Y.-W., Ding, D., Ye, Q.-Z., Meroueh, S. O., & Lu, H. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100211 · Cited by 110 · see citing works

Analysis of histone acetyltransferase and deacetylase families of Vitis vinifera

Aquea, F., Timmermann, T., & Arce‐Johnson, P. (2010) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2009.12.009 · Cited by 93 · see citing works

Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum)

Zhao, L., Lu, J., Zhang, J., Wu, P.-Y., Yang, S., & Wu, K. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00760 · Cited by 86 · see citing works

Genetic and chemical analyses of the action mechanisms of sirtinol in Arabidopsis

Dai, X., Hayashi, K., Nozaki, H., Cheng, Y., & Zhao, Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500185102 · Cited by 84 · see citing works

SIRT3 and SIRT4 are mitochondrial tumor suppressor proteins that connect mitochondrial metabolism and carcinogenesis

Zhu, Y., Yan, Y., Principe, D. R., Zou, X., Vassilopoulos, A., & Gius, D. R. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-15 · Cited by 76 · see citing works

Sirtinol Treatment Reduces Inflammation in Human Dermal Microvascular Endothelial Cells

Orecchia, A., Scarponi, C., Felice, F. D., Cesarini, E., Avitabile, S., Mai, A., Mauro, M. L., Sirri, V., Zambruno, G., Albanesi, C., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024307 · Cited by 73 · see citing works

Histone Acylation beyond Acetylation: Terra Incognita in Chromatin Biology.

Rousseaux, S., & Khochbin, S. (2015) · PubMed Central · doi:10.22074/cellj.2015.506 · Cited by 73 · see citing works

Integrative Chemical Biology Approaches for Identification and Characterization of “Erasers” for Fatty‐Acid‐Acylated Lysine Residues within Proteins

Liu, Z., Yang, T., Li, X., Peng, T., Hang, H. C., & Li, X. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201408763 · Cited by 63 · see citing works

Synthesis and biological characterisation of sirtuin inhibitors based on the tenovins

McCarthy, A. R., Pirrie, L., Hollick, J. J., Ronseaux, S., Campbell, J., Higgins, M., Staples, O. D., Tran, F., Slawin, A. M. Z., Laı́n, S., et al. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.01.001 · Cited by 62 · see citing works

The Rice NAD+-Dependent Histone Deacetylase OsSRT1 Targets Preferentially to Stress- and Metabolism-Related Genes and Transposable Elements

Zhong, X., Zhang, H., Zhao, Y. J., Sun, Q., Hu, Y., Peng, H., & Zhou, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066807 · Cited by 58 · see citing works

SIRT5 deacetylates and activates urate oxidase in liver mitochondria of mice

Nakamura, Y., Ogura, M., Ogura, K., Tanaka, D., & Inagaki, N. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.10.009 · Cited by 55 · see citing works

Sirtuin 1 activator SRT 2104 protects Huntington's disease mice

Jiang, M., Zheng, J., Peng, Q., Hou, Z., Zhang, J., Mori, S., Ellis, J. L., Vlasuk, G. P., Fries, H. E., Suri, V., et al. (2014) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.135 · Cited by 54 · see citing works

The sirtuins: Markers of metabolic health

Covington, J. D., & Bajpeyi, S. (2015) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500340 · Cited by 50 · see citing works

Catalysis and Mechanistic Insights into Sirtuin Activation

Dittenhafer‐Reed, K. E., Feldman, J. L., & Denu, J. M. (2010) · ChemBioChem · doi:10.1002/cbic.201000434 · Cited by 34 · see citing works

Sirtuin Modulators

Mahajan, S. S., Leko, V., Simon, J. A., & Bedalov, A. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_11 · Cited by 31 · see citing works

Spontaneous Electrical Activity of Cultured Interstitial Cells of Cajal from Mouse Urinary Bladder

Kim, S., Jeong, H., Jang, S., Wu, M.-J., Park, J. K., Jiao, H.-Y., Jun, J. Y., & Park, J.-S. (2013) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2013.17.6.531 · Cited by 28 · see citing works

SIRT7 an emerging sirtuin: deciphering newer roles.

Kim, W., & Kim, J. (2013) · PubMed · Cited by 27 · see citing works

Identification of benzofuran-3-yl(phenyl)methanones as novel SIRT1 inhibitors: Binding mode, inhibitory mechanism and biological action

Wu, J., Li, Y., Chen, K., Jiang, H., Xu, M., & Liu, D. (2012) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.12.026 · Cited by 21 · see citing works

Characterization and differential expression analysis of complete coding sequences of Vitis vinifera L. sirtuin genes

Cucurachi, M., Busconi, M., Morreale, G., Zanetti, A., Bavaresco, L., & Fogher, C. (2012) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2012.02.017 · Cited by 20 · see citing works

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 622 · see citing works

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 318 · see citing works

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 294 · see citing works

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 · see citing works

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 262 · see citing works

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 258 · see citing works

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 145 · see citing works

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 138 · see citing works

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 · see citing works

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 139 · see citing works

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 120 · see citing works

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 · see citing works

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 · see citing works

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 93 · see citing works

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 93 · see citing works

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 91 · see citing works

CD38: T Cell Immuno-Metabolic Modulator

Kar, A., Mehrotra, S., & Chatterjee, S. (2020) · Cells · doi:10.3390/cells9071716 · Cited by 91 · see citing works

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 87 · see citing works

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 · see citing works

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 83 · see citing works

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 78 · see citing works

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 · see citing works

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 79 · see citing works

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 76 · see citing works

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 69 · see citing works

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 · see citing works

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 66 · see citing works

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 66 · see citing works

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 66 · see citing works

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 · see citing works

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 70 · see citing works

Decoding the Rosetta stone of mitonuclear communication

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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 · see citing works

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 · see citing works

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

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

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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 51 · see citing works

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 49 · see citing works

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 50 · see citing works

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 · see citing works

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 43 · see citing works

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 42 · see citing works

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 41 · see citing works

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 40 · see citing works

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 · see citing works

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 37 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 36 · see citing works

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 · see citing works

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. E., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083806 · Cited by 34 · see citing works

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 33 · see citing works

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 32 · see citing works

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 33 · see citing works

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 · see citing works

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 · see citing works

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 30 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 29 · see citing works

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 · see citing works

Review: The plant sirtuins

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

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 27 · see citing works

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 27 · see citing works

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 · see citing works

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 26 · see citing works

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 · see citing works

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 25 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 22 · see citing works

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 · see citing works

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 22 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Sirtfoods: New Concept Foods, Functions, and Mechanisms

Akan, O. D., Qin, D., Guo, T., Lin, Q., & Luo, F. (2022) · Foods · doi:10.3390/foods11192955 · Cited by 20 · see citing works

Biochemical Mechanisms of Sirtuin-Directed Protein Acylation in Hepatic Pathologies of Mitochondrial Dysfunction

McGinnis, C. D., Jennings, E. Q., Harris, P. S., Galligan, J. J., & Fritz, K. S. (2022) · Cells · doi:10.3390/cells11132045 · Cited by 18 · see citing works

Pharmacological Approaches to Decelerate Aging: A Promising Path

Hassani, B., Goshtasbi, G., Nooraddini, S., & Firouzabadi, N. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4201533 · Cited by 19 · see citing works

Potent Activation of NAD+‑Dependent Deacetylase Sirt7 by Nucleosome Binding

Kuznetsov, V. I., Liu, W. H., Klein, M. A., & Denu, J. M. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00348 · Cited by 18 · see citing works

Detection of Insertions/Deletions Within SIRT1, SIRT2 and SIRT3 Genes and Their Associations with Body Measurement Traits in Cattle

Jin, Y., Yang, Q., Gao, J., Tang, Q., Duan, B., Yu, T. Y., Qi, X., Liu, J., Wang, R., Dang, R., et al. (2018) · Biochemical Genetics · doi:10.1007/s10528-018-9868-3 · Cited by 18 · see citing works

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 · see citing works

Insights on attenuating autophagy cellular and molecular pathways versus methotrexate-induced toxicity via liposomal turmeric therapy

Kadry, M. O., Ammar, N. M., Hassan, H. A., & Megeed, R. M. A. (2022) · Journal of Genetic Engineering and Biotechnology · doi:10.1186/s43141-022-00430-4 · Cited by 17 · see citing works

Estradiol as the Trigger of Sirtuin-1-Dependent Cell Signaling with a Potential Utility in Anti-Aging Therapies

Karolczak, K., & Watała, C. W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813753 · Cited by 17 · see citing works

Mitochondrial targets in hyperammonemia: Addressing urea cycle function to improve drug therapies

Moedas, M. F., Simões, R. J., & Silva, M. F. B. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116034 · Cited by 17 · see citing works

Emerging interactions between mitochondria and NAD+ metabolism in cardiometabolic diseases

Nasuhidehnavi, A., Zarzycka, W., Gorecki, I., Chiao, Y. A., & Lee, C. F. (2024) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2024.07.010 · Cited by 18 · see citing works

Crosstalk between SIRT1/Nrf2 signaling and NLRP3 inflammasome/pyroptosis as a mechanistic approach for the neuroprotective effect of linagliptin in Parkinson’s disease

Ghaith, W. Z., Wadie, W., & El-Yamany, M. F. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113716 · Cited by 17 · see citing works

Sirtuins: not only animal proteins

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Senolytic and senomorphic secondary metabolites as therapeutic agents in Drosophila melanogaster models of Parkinson’s disease

Miller, S. J., Darji, R. Y., Walaieh, S., Lewis, J. A., & Logan, R. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1271941 · Cited by 16 · see citing works

Sirtuins as Interesting Players in the Course of HIV Infection and Comorbidities

Jurkowska, K., Szymańska, B., Knysz, B., Kuźniarski, A., & Piwowar, A. (2021) · Cells · doi:10.3390/cells10102739 · Cited by 16 · see citing works

The Role of Sirtuin 6 in the Deacetylation of Histone Proteins as a Factor in the Progression of Neoplastic Disease

Baran, M. T., Miziak, P. A., Stepulak, A., & Cybulski, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010497 · Cited by 16 · see citing works

Recent Advances on Mutant p53: Unveiling Novel Oncogenic Roles, Degradation Pathways, and Therapeutic Interventions

Cordani, M., Garufi, A., Benedetti, R., Tafani, M., Aventaggiato, M., D’Orazi, G., & Cirone, M. (2024) · Biomolecules · doi:10.3390/biom14060649 · Cited by 16 · see citing works

The Role of Sirtuins in the Control of Metabolic Homeostasis

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Characterization of Nuclear Sirtuins: Molecular Mechanisms and Physiological Relevance

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Function of SIRT1 in physiology

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Sirtuin Functions in Health and Disease

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Pharmacological manipulations of CNS sirtuins: Potential effects on metabolic homeostasis

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