Sirtuin functions and modulation: from chemistry to the clinic
Open accessAbstract
Sirtuins are NAD(+)-dependent histone deacetylases regulating important metabolic pathways in prokaryotes and eukaryotes and are involved in many biological processes such as cell survival, senescence, proliferation, apoptosis, DNA repair, cell metabolism, and caloric restriction. The seven members of this family of enzymes are considered potential targets for the treatment of human pathologies including neurodegenerative diseases, cardiovascular diseases, and cancer. Furthermore, recent interest focusing on sirtuin modulators as epigenetic players in the regulation of fundamental biological pathways has prompted increased efforts to discover new small molecules able to modify sirtuin activity. Here, we review the role, mechanism of action, and biological function of the seven sirtuins, as well as their inhibitors and activators.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
NAD+ levels can be increased by supplying biosynthetic precursors, intermediates, or by inhibiting NAD+ consuming enzymes.
“NAD+ levels can be increased by supplying biosynthetic precursors, intermediates, or by inhibiting NAD+ consuming enzymes [reviewed in Carafa et al.260)].”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [260]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
SIRT1 Protects against α-Synuclein Aggregation by Activating Molecular Chaperones
Dönmez, G., Arun, A., Chung, C. Y., McLean, P. J., Lindquist, S. L., & Guarente, L. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3442-11.2012 · Cited by 207 · see citing works
RetractedResveratrol 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 · see citing works
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 4,222 · see citing works
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 · see citing works
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 2,653 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · 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
Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases
Park, S. J., Ahmad, F., Philp, A., Baar, K., Williams, T., Luo, H., Ke, H., Rehmann, H., Taussig, R., Brown, A. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.017 · Cited by 1,352 · see citing works
Mammalian SIRT1 Represses Forkhead Transcription Factors
Motta, M. C., Divecha, N., Lemieux, M. E., Kamel, C., Chen, D., Gu, W. J., Bultsma, Y., McBurney, M. W., & Guarente, L. (2004) · Cell · doi:10.1016/s0092-8674(04)00126-6 · Cited by 1,351 · see citing works
Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works
Sirtuin 2 Inhibitors Rescue α-Synuclein-Mediated Toxicity in Models of Parkinson's Disease
Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., Amore, A. M., Volk, C. B., Maxwell, M. M., Rochet, J., McLean, P. J., et al. (2007) · Science · doi:10.1126/science.1143780 · Cited by 1,066 · see citing works
Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration
Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060 · see citing works
SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., Garofalo, R. S., Griffith, D., Griffor, M., Loulakis, P., Pabst, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088682 · Cited by 915 · see citing works
Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899 · see citing works
Lysine glutarylation is a protein posttranslational modification regulated by SIRT5
Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.014 · Cited by 844 · see citing works
Valenzano, D. R., Tozzini, E. T., Genade, T., Cattaneo, A., Domenici, L., & Cellerino, A. (2006) · Current Biology · doi:10.1016/j.cub.2005.12.038 · Cited by 786 · see citing works
Substrate-specific activation of sirtuins by resveratrol
Kaeberlein, M., McDonagh, T., Heltweg, B., Hixon, J., Westman, E. A., Caldwell, S. D., Napper, A., Curtis, R., DiStefano, P. S., Fields, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500655200 · Cited by 745 · see citing works
Qin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., Chen, L., Zhao, W., Thiyagarajan, M., MacGrogan, D., Rodgers, J. T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602909200 · Cited by 626 · 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
Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators
Hubbard, B. P., Gomes, A. P., Dai, H., Li, J., Case, A. W., Considine, T., Riera, T. V., Lee, J. E., Yen, E. S., Lamming, D. W., et al. (2013) · Science · doi:10.1126/science.1231097 · Cited by 618 · see citing works
Small molecule SIRT1 activators for the treatment of aging and age-related diseases
Hubbard, B. P., & Sinclair, D. A. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.12.004 · Cited by 572 · see citing works
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
Discovery of Indoles as Potent and Selective Inhibitors of the Deacetylase SIRT1
Napper, A. D., Hixon, J., McDonagh, T., Keavey, K., Pons, J., Barker, J., Yau, W. T., Amouzegh, P., Flegg, A., Hamelin, E. M.-N., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050522v · Cited by 524 · see citing works
Discovery, In Vivo Activity, and Mechanism of Action of a Small-Molecule p53 Activator
Laı́n, S., Hollick, J. J., Campbell, J., Staples, O. D., Higgins, M., Aoubala, M., McCarthy, A. R., Appleyard, V. C. L., Murray, K. E., Baker, L., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.03.004 · Cited by 523 · see citing works
SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation
Jing, E., Gesta, S., & Kahn, C. R. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.07.003 · Cited by 490 · see citing works
Solomon, J. M., Pasupuleti, R., Xu, L., McDonagh, T., Curtis, R., DiStefano, P. S., & Huber, L. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.28-38.2006 · Cited by 481 · see citing works
Antitumor Activity of a Small-Molecule Inhibitor of Human Silent Information Regulator 2 Enzymes
Heltweg, B., Gatbonton, T., Schuler, A. D., Posakony, J., Li, H., Goehle, S., Kollipara, R., DePinho, R. A., Gu, Y., Simon, J. A., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3617 · Cited by 470 · see citing works
Honokiol blocks and reverses cardiac hypertrophy in mice by activating mitochondrial Sirt3
Pillai, V. B., Samant, S. A., Sundaresan, N. R., Raghuraman, H., Kim, G. H., Bonner, M. Y., Arbiser, J. L., Walker, D. I., Jones, D. P., Gius, D. R., et al. (2015) · Nature Communications · doi:10.1038/ncomms7656 · Cited by 448 · see citing works
Ota, H., Tokunaga, E., Chang, K., Hikasa, M., Iijima, K., Eto, M., Kozaki, K., Akishita, M., Ouchi, Y., & Kaneki, M. (2005) · Oncogene · doi:10.1038/sj.onc.1209049 · Cited by 431 · see citing works
Inhibition of SIRT1 Reactivates Silenced Cancer Genes without Loss of Promoter DNA Hypermethylation
Pruitt, K., Zinn, R. L., Ohm, J. E., McGarvey, K. M., Kang, S.-H. L., Watkins, D. N., Herman, J. G., & Baylin, S. B. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020040 · Cited by 387 · see citing works
Cui, L., Supinski, A., Savas, J. N., Yates, J. R., Bordone, L., Guarente, L., Cohen, D. E., Mazzulli, J. R., Krainc, D., & Jeong, H. (2011) · PubMed Central · doi:10.1038/nm.2559 · Cited by 367 · see citing works
Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity
Finley, L. W. S., Haas, W., Desquiret‐Dumas, V., Wallace, D. C., Procaccio, V., Gygi, S. P., & Haigis, M. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023295 · Cited by 364 · see citing works
Sirtuin activators and inhibitors
Villalba, J. M., & Alcain, F. J. (2012) · BioFactors · doi:10.1002/biof.1032 · Cited by 354 · see citing works
Identification of a small molecule inhibitor of Sir2p
Bedalov, A., Gatbonton, T., Irvine, W. P., Gottschling, D. E., & Simon, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261574398 · Cited by 344 · see citing works
SIRT1 Regulates HIV Transcription via Tat Deacetylation
Pagans, S., Pedal, A., North, B. J., Kaehlcke, K., Marshall, B. L., Dorr, A., Hetzer‐Egger, C., Henklein, P., Frye, R. A., McBurney, M. W., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030041 · Cited by 330 · 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
SIRT1, Is It a Tumor Promoter or Tumor Suppressor?
Deng, C. (2009) · International Journal of Biological Sciences · doi:10.7150/ijbs.5.147 · Cited by 322 · see citing works
Ex-527 inhibits Sirtuins by exploiting their unique NAD + -dependent deacetylation mechanism
Gertz, M., Fischer, F. F., Nguyen, G. T. T., Lakshminarasimhan, M., Schutkowski, M., Weyand, M., & Steegborn, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303628110 · Cited by 320 · see citing works
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site
Rumpf, T., Schiedel, M., Karaman, B., Roessler, C., North, B. J., Lehotzky, A., Oláh, J., Ladwein, K. I., Schmidtkunz, K., Gajer, M., et al. (2015) · Nature Communications · doi:10.1038/ncomms7263 · Cited by 302 · see citing works
SRT1720 improves survival and healthspan of obese mice
Minor, R. K., Baur, J. A., Gomes, A. P., Ward, T. M., Csiszár, A., Mercken, E. M., Abdelmohsen, K., Shin, Y., Cantó, C., Scheibye‐Knudsen, M., et al. (2011) · Scientific Reports · doi:10.1038/srep00070 · Cited by 297 · see citing works
Serrano, L., Martínez‐Redondo, P., Marazuela-Duque, A., Vázquez, B. N., Dooley, S., Voigt, P., Beck, D. B., Kane‐Goldsmith, N., Tong, Q., Rabanal, R. M., et al. (2013) · Genes & Development · doi:10.1101/gad.211342.112 · Cited by 282 · see citing works
Inoue, T., Hiratsuka, M., Osaki, M., Yamada, H. Y., Kishimoto, I., Yamaguchi, S., Nakano, S., Katoh, M., Ito, H., & Oshimura, M. (2006) · Oncogene · doi:10.1038/sj.onc.1209857 · Cited by 258 · see citing works
Salermide, a Sirtuin inhibitor with a strong cancer-specific proapoptotic effect
Lara, E., Mai, A., Calvanese, V., Altucci, L., López‐Nieva, P., Martínez‐Chantar, M. L., Varela‐Rey, M., Rotili, D., Nebbioso, A., Ropero, S., et al. (2008) · Oncogene · doi:10.1038/onc.2008.436 · Cited by 258 · see citing works
SIRT1-Mediated eNAMPT Secretion from Adipose Tissue Regulates Hypothalamic NAD+ and Function in Mice
Yoon, M. J., Yoshida, M., Johnson, S., Takikawa, A., Usui, I., Tobe, K., Nakagawa, T., Yoshino, J., & Imai, S. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.002 · Cited by 242 · see citing works
Small-Molecule Allosteric Activators of Sirtuins
Sinclair, D. A., & Guarente, L. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134657 · Cited by 223 · see citing works
Crystallographic structure of a small molecule SIRT1 activator-enzyme complex
Dai, H., Case, A. W., Riera, T. V., Considine, T., Lee, J. E., Hamuro, Y., Zhao, H., Jiang, Y., Sweitzer, S. M., Pietrak, B., et al. (2015) · Nature Communications · doi:10.1038/ncomms8645 · Cited by 218 · see citing works
The Sirtuin 2 Inhibitor AK-7 Is Neuroprotective in Huntington’s Disease Mouse Models
Chopra, V., Quinti, L., Kim, J., Vollor, L., Narayanan, K. L., Edgerly, C. K., Cipicchio, P. M., Lauver, M. A., Choi, S. H., Silverman, R. B., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.11.001 · Cited by 214 · see citing works
Borra, M. T., Langer, M. R., Slama, J. T., & Denu, J. M. (2004) · Biochemistry · doi:10.1021/bi049592e · Cited by 214 · see citing works
SIRT1 Activation by Small Molecules
Dai, H., Kustigian, L. M., Carney, D. P., Case, A. W., Considine, T., Hubbard, B. P., Perni, R. B., Riera, T. V., Szczepankiewicz, B. G., Vlasuk, G. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.133892 · Cited by 211 · see citing works
The histone deacetylase SIRT2 stabilizes Myc oncoproteins
Liu, P. Y., Xu, N., Malyukova, A., Scarlett, C. J., Yt, S., Zhang, X. D., Ling, D., Su, S., Nelson, C. C., Chang, D. K.-F., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.147 · Cited by 208 · see citing works
Discovery of Thieno[3,2-d]pyrimidine-6-carboxamides as Potent Inhibitors of SIRT1, SIRT2, and SIRT3
Disch, J. S., Evindar, G., Chiu, C. H., Blum, C. A., Dai, H., Jin, L., Schuman, E., Lind, K. E., Belyanskaya, S. L., Deng, J., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400204k · Cited by 197 · see citing works
Activation of Stress Response Gene SIRT1 by BCR-ABL Promotes Leukemogenesis
Yuan, H., Wang, Z., Li, L., Zhang, H., Modi, H., Horne, D., Bhatia, R., & Chen, W. (2012) · Blood · doi:10.1182/blood-2011-06-361691 · Cited by 182 · 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
Süßmuth, S. D., Salman, H., Landwehrmeyer, G. B., Farmer, R. E., Frost, C. D., Tripepi, G., Andersen, C. A. F., Bacco, M. D., Lamanna, C., Diodato, E., et al. (2014) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.12512 · Cited by 177 · see citing works
A role for SIRT1 in cell growth and chemoresistance in prostate cancer PC3 and DU145 cells
Kojima, K., Ohhashi, R., Fujita, Y., Hamada, N., Akao, Y., Nozawa, Y., Deguchi, T., & Ito, M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.045 · Cited by 175 · see citing works
SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer
Lü, W., Zuo, Y., Feng, Y., & Zhang, M. (2014) · Tumor Biology · doi:10.1007/s13277-014-2372-4 · Cited by 172 · see citing works
Chen, X., Sun, K., Jiao, S., Cai, N., Zhao, X., Zou, H., Xie, Y., Wang, Z., Zhong, M., & Wei, L. (2014) · Scientific Reports · doi:10.1038/srep07481 · Cited by 166 · see citing works
Neugebauer, R. C., Uciechowska, U., Meier, R., Hruby, H., Valkov, V., Verdin, E. M., Sippl, W., & Jung, M. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm700972e · Cited by 166 · see citing works
Mai, A., Valente, S., Meade, S., Carafa, V., Tardugno, M., Nebbioso, A., Galmozzi, A., Mitro, N., Fabiani, E. D., Altucci, L., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9008289 · Cited by 159 · see citing works
Etchegaray, J., Chávez, L., Huang, Y., Ross, K. N., Choi, J., Martínez-Pastor, B., Walsh, R. M., Sommer, C., Lienhard, M., Gladden, A. D., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3147 · Cited by 155 · see citing works
Marshall, G. M., Liu, P. Y., Gherardi, S., Scarlett, C. J., Bedalov, A., Xu, N., Iraci, N., Valli, E., Ling, D., Thomas, W. D., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002135 · Cited by 153 · see citing works
Tumour-suppressive function of SIRT4 in human colorectal cancer
Miyo, M., Yamamoto, H., Konno, M., Colvin, H. S., Nishida, N., Koseki, J., Kawamoto, K., Ogawa, H., Hamabe, A., Uemura, M., et al. (2015) · British Journal of Cancer · doi:10.1038/bjc.2015.226 · Cited by 151 · see citing works
Fridén‐Saxin, M., Seifert, T., Landergren, M. R., Suuronen, T., Lahtela-Kakkonen, M. K., Jarho, E. M., & Luthman, K. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3005288 · Cited by 149 · see citing works
SIRT1 interacts with p73 and suppresses p73‐dependent transcriptional activity
Dai, J. M., Wang, Z. Y., Sun, D. C., Lin, R. X., & Wang, S. Q. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20831 · Cited by 147 · see citing works
Mechanism-Based Inhibition of Sir2 Deacetylases by Thioacetyl-Lysine Peptide
Smith, B. C., & Denu, J. M. (2007) · Biochemistry · doi:10.1021/bi7013294 · Cited by 144 · see citing works
Acetyl-lysine Analog Peptides as Mechanistic Probes of Protein Deacetylases
Smith, B. C., & Denu, J. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707878200 · Cited by 139 · see citing works
Sirtuin 3 regulates Foxo3a-mediated antioxidant pathway in microglia
Rangarajan, P., Karthikeyan, A., Lu, J., Ling, E., & Dheen, S. T. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.10.048 · Cited by 138 · see citing works
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
Taylor, D. M., Balabadra, U., Xiang, Z., Woodman, B., Meade, S., Amore, A. M., Maxwell, M. M., Reeves, S. A., Bates, G. P., Luthi‐Carter, R., et al. (2011) · ACS Chemical Biology · doi:10.1021/cb100376q · Cited by 132 · see citing works
Development of Pyrazolone and Isoxazol-5-one Cambinol Analogues as Sirtuin Inhibitors
Mahajan, S. S., Scian, M., Sripathy, S. P., Posakony, J., Lao, U., Loe, T. K., Leko, V., Thalhofer, A., Schuler, A. D., Bedalov, A., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4018064 · Cited by 126 · see citing works
SIRT2-mediated protein deacetylation: An emerging key regulator in brain physiology and pathology
Harting, K., & Knöll, B. (2009) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2009.11.006 · Cited by 126 · see citing works
Seifert, T., Malo, M., Kokkola, T., Engen, K., Fridén‐Saxin, M., Wallén, E. A. A., Lahtela-Kakkonen, M. K., Jarho, E. M., & Luthman, K. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500930h · Cited by 125 · see citing works
Medda, F., Russell, R. J. M., Higgins, M., McCarthy, A. R., Campbell, J., Slawin, A. M. Z., Lane, D. P., Laı́n, S., & Westwood, N. J. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm8014298 · Cited by 123 · see citing works
Discovery of Novel and Selective SIRT6 Inhibitors
Parenti, M. D., Grozio, A., Bauer, I., Galeno, L., Damonte, P., Millo, E., Sociali, G., Franceschi, C., Ballestrero, A., Bruzzone, S., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500487d · Cited by 121 · see citing works
Sirt1 activation by resveratrol is substrate sequence-selective
Lakshminarasimhan, M., Rauh, D., Schutkowski, M., & Steegborn, C. (2013) · Aging · doi:10.18632/aging.100542 · Cited by 119 · see citing works
Rascón, B., Hubbard, B. P., Sinclair, D. A., & Amdam, G. V. (2012) · Aging · doi:10.18632/aging.100474 · Cited by 116 · see citing works
Antitumor Effect of SIRT1 Inhibition in Human HCC Tumor Models In Vitro and In Vivo
Portmann, S., Fahrner, R., Lechleiter, A., Keogh, A., Overney, S., Laemmle, A., Mikami, K., Montani, M., Tschan, M. P., Candinas, D., et al. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0700 · Cited by 113 · see citing works
Sirt1 Promotes Axonogenesis by Deacetylation of Akt and Inactivation of GSK3
Li, X., Chen, C., Tu, Y., Sun, H., Zhao, M., Cheng, S., Qu, Y., & Zhang, S. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8437-3 · Cited by 112 · see citing works
Nε-Thioacetyl-lysine: A multi-facet functional probe for enzymatic protein lysine Nε-deacetylation
Fatkins, D. G., Monnot, A. D., & Zheng, W. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.04.075 · Cited by 112 · see citing works
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
Rotili, D., Tarantino, D., Nebbioso, A., Paolini, C., Huidobro, C., Lara, E., Mellini, P., Lenoci, A., Pezzi, R., Botta, G., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3011614 · Cited by 103 · see citing works
Autophagy induced by the class III histone deacetylase Sirt1 prevents prion peptide neurotoxicity
Jeong, J., Moon, M., Lee, Y.-J., Seol, J., & Park, S. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.04.002 · Cited by 102 · see citing works
Aminothiazoles as Potent and Selective Sirt2 Inhibitors: A Structure–Activity Relationship Study
Schiedel, M., Rumpf, T., Karaman, B., Lehotzky, A., Oláh, J., Gerhardt, S., Ovádi, J., Sippl, W., Einsle, O., & Jung, M. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01517 · Cited by 100 · see citing works
SIRT2: Tumour suppressor or tumour promoter in operable breast cancer?
McGlynn, L. M., Zino, S., Macdonald, A. I., Curle, J., Reilly, J. E., Mohammed, Z. M. A., McMillan, D. C., Mallon, E., Payne, A. P., Edwards, J., et al. (2013) · European Journal of Cancer · doi:10.1016/j.ejca.2013.10.005 · Cited by 98 · see citing works
Schistosoma mansoni Sirtuins: Characterization and Potential as Chemotherapeutic Targets
Lancelot, J., Caby, S., Dubois, F., Vanderstraete, M., Trolet, J., Oliveira, G., Bracher, F., Jung, M., & Pierce, R. J. (2013) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0002428 · Cited by 96 · see citing works
Spallotta, F., Cencioni, C., Straino, S., Nanni, S., Rosati, J. D., Artuso, S., Manni, I., Colussi, C., Piaggio, G., Martelli, F., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.441816 · Cited by 91 · see citing works
Discovery of oxazolo[4,5-b]pyridines and related heterocyclic analogs as novel SIRT1 activators
Bemis, J. E., Vu, C. B., Xie, R. L., Nunes, J. J., Ng, P. Y., Disch, J. S., Milne, J. C., Carney, D. P., Lynch, A. V., Jin, L., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.11.106 · Cited by 91 · see citing works
Kozako, T., Aikawa, A., Shoji, T., Fujimoto, T., Yoshimitsu, M., Shirasawa, S., Tanaka, H., Honda, S., Shimeno, H., Arima, N., et al. (2012) · International Journal of Cancer · doi:10.1002/ijc.27481 · Cited by 89 · see citing works
Discovery of Potent and Selective Sirtuin 2 (SIRT2) Inhibitors Using a Fragment-Based Approach
Cui, H., Kamal, Z., Ai, T., Xü, Y., More, S. S., Wilson, D. J., & Chen, L. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500777s · Cited by 86 · see citing works
Langsfeld, E. S., Bodily, J. M., & Laimins, L. A. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005181 · Cited by 84 · see citing works
Valente, S., Mellini, P., Spallotta, F., Carafa, V., Nebbioso, A., Polletta, L., Carnevale, I., Saladini, S., Trisciuoglio, D., Gabellini, C., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01117 · Cited by 80 · see citing works
SIRT2 activity is required for the survival of C6 glioma cells
He, X. Q., Nie, H., Hong, Y., Sheng, C., Xia, W., & Ying, W. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.11.141 · Cited by 76 · see citing works
Derr, R. S., van Hoesel, A. Q., Benard, A., Goossens-Beumer, I. J., Sajet, A., Dekker-Ensink, N. G., de Kruijf, E. M., Bastiaannet, E., Smit, V. T. H. B. M., van de Velde, C. J., et al. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-604 · Cited by 72 · see citing works
The effect of combined treatment with cisplatin and histone deacetylase inhibitors on HeLa cells
Jin, K. L., Park, J., Noh, E. J., Hoe, K., Lee, J. H., Kim, J.-H., & Nam, J. (2010) · Journal of Gynecologic Oncology · doi:10.3802/jgo.2010.21.4.262 · Cited by 71 · see citing works
Discovery of SIRT3 Inhibitors Using SAMDI Mass Spectrometry
Patel, K., Sherrill, J., Mrksich, M., & Scholle, M. D. (2015) · SLAS DISCOVERY · doi:10.1177/1087057115588512 · Cited by 62 · see citing works
Inhibition of Human Sirtuins by in Situ Generation of an Acetylated Lysine−ADP−Ribose Conjugate
Asaba, T., Suzuki, T., Ueda, R., Tsumoto, H., Nakagawa, H., & Miyata, N. (2009) · Journal of the American Chemical Society · doi:10.1021/ja807083y · Cited by 61 · see citing works
Repositioning antipsychotic chlorpromazine for treating colorectal cancer by inhibiting sirtuin 1
Lee, W., Lee, W.-T., Cheng, C., Chen, K., Chou, C., Chung, C., Sun, M.-S., Cheng, H., Ho, M.-N., & Lin, C. (2015) · Oncotarget · doi:10.18632/oncotarget.4768 · Cited by 58 · see citing works
Zhang, T., Rong, N., Chen, J., Zou, C., Jing, H., Zhu, X., & Zhang, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079162 · Cited by 57 · see citing works
Nϵ-Thioacetyl-Lysine-Containing Tri-, Tetra-, and Pentapeptides as SIRT1 and SIRT2 Inhibitors
Kiviranta, P. H., Suuronen, T., Wallén, E. A. A., Leppänen, J., Tervonen, J., Kyrylenko, S., Salminen, A., Poso, A., & Jarho, E. M. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm801401k · Cited by 56 · see citing works
Pasco, M. Y., Rotili, D., Altucci, L., Farina, F., Rouleau, G. A., Mai, A., & Néri, C. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9013345 · Cited by 52 · see citing works
Regulation of SIRT2 levels for human non-small cell lung cancer therapy
Li, Z., Xie, Q. R., Chen, Z., Lü, S., & Xia, W. (2013) · Lung Cancer · doi:10.1016/j.lungcan.2013.05.013 · Cited by 52 · see citing works
Identification of Tri‐ and Tetracyclic Pyrimidinediones as Sirtuin Inhibitors
Rotili, D., Tarantino, D., Carafa, V., Lara, E., Meade, S., Botta, G., Nebbioso, A., Schemies, J., Jung, M., Kazantsev, A. G., et al. (2010) · ChemMedChem · doi:10.1002/cmdc.201000030 · Cited by 49 · see citing works
Fatkins, D. G., & Zheng, W. (2008) · International Journal of Molecular Sciences · doi:10.3390/ijms9010001 · Cited by 46 · see citing works
Identification of a cell-active non-peptide sirtuin inhibitor containing N-thioacetyl lysine
Suzuki, T., Asaba, T., Imai, E., Tsumoto, H., Nakagawa, H., & Miyata, N. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.08.028 · Cited by 45 · see citing works
Structure-Based Design of Pseudopeptidic Inhibitors for SIRT1 and SIRT2
Huhtiniemi, T., Salo, H. S., Suuronen, T., Poso, A., Salminen, A., Leppänen, J., Jarho, E. M., & Lahtela-Kakkonen, M. K. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200590k · Cited by 44 · see citing works
Hirai, S., Endo, S., Saito, R., Hirose, M., Ueno, T., Suzuki, H., Yamato, K., Abei, M., & Hyodo, I. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102831 · Cited by 43 · see citing works
Park, J.-M., Kim, T. H., JO, S., Kim, M.-Y., & Ahn, Y. (2015) · Scientific Reports · doi:10.1038/srep17395 · Cited by 41 · see citing works
SIRT1 expression is associated with poor prognosis of lung adenocarcinoma
Li, C. V., Wang, L., Zheng, L., Zhan, X., Xu, B., Jiang, J., & Wu, C. (2015) · OncoTargets and Therapy · doi:10.2147/ott.s82378 · Cited by 40 · see citing works
Benzodeazaoxaflavins as Sirtuin Inhibitors with Antiproliferative Properties in Cancer Stem Cells
Rotili, D., Tarantino, D., Carafa, V., Paolini, C., Schemies, J., Jung, M., Botta, G., Maro, S. D., Novellino, E., Steinkühler, C., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301115r · Cited by 40 · see citing works
Mellini, P., Kokkola, T., Suuronen, T., Salo, H. S., Tolvanen, L., Mai, A., Lahtela-Kakkonen, M. K., & Jarho, E. M. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400438k · Cited by 38 · see citing works
Peptides and Pseudopeptides as SIRT6 Deacetylation Inhibitors
Kokkonen, P., Rahnasto‐Rilla, M., Kiviranta, P. H., Huhtiniemi, T., Laitinen, T., Poso, A., Jarho, E. M., & Lahtela-Kakkonen, M. K. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300139n · Cited by 37 · see citing works
Rotili, D., Carafa, V., Tarantino, D., Botta, G., Nebbioso, A., Altucci, L., & Mai, A. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.01.025 · Cited by 36 · see citing works
Sirtuin deacetylases: A new target for melanoma management
Wilking, M. J., Singh, C. K., Nihal, M., Ndiaye, M. A., & Ahmad, N. (2014) · Cell Cycle · doi:10.4161/15384101.2014.949085 · Cited by 33 · see citing works
N-Modified lysine containing inhibitors for SIRT1 and SIRT2
Huhtiniemi, T., Suuronen, T., Lahtela-Kakkonen, M. K., Bruijn, T., Jääskeläinen, S., Poso, A., Salminen, A., Leppänen, J., & Jarho, E. M. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.06.035 · Cited by 30 · see citing works
N ε -Methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for N ε -acetyl-lysine
Jamonnak, N., Fatkins, D. G., Wei, L., & Zheng, W. (2007) · Organic & Biomolecular Chemistry · doi:10.1039/b617185k · Cited by 20 · see citing works
Flagged first, then by citations
1 of the 119 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The sirtuin family in health and disease
Wu, Q., Zhang, T., Chen, H., Yu, X., Lv, J.-L., Liu, Y., Liu, Y., Zheng, G., Zhao, J.-Q., Wei, Y., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01257-8 · Cited by 891 · see citing works
Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds
Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834 · see citing works
Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease
Smith, R. L., Soeters, M. R., Wüst, R. C. I., & Houtkooper, R. H. (2018) · Endocrine Reviews · doi:10.1210/er.2017-00211 · Cited by 787 · see citing works
Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development
Salo‐Ahen, O. M. H., Alanko, I., Bhadane, R. N., Bonvin, A. M. J. J., Honorato, R. V., Hossain, S., Juffer, A. H., Kabedev, A., Lahtela-Kakkonen, M. K., Larsen, A. S., et al. (2020) · Processes · doi:10.3390/pr9010071 · Cited by 693 · see citing works
The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy
Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 358 · see citing works
The Beneficial Roles of SIRT1 in Neuroinflammation-Related Diseases
Jiao, F., & Gong, Z. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6782872 · Cited by 293 · see citing works
SIRT6: Novel Mechanisms and Links to Aging and Disease
Tasselli, L., Zheng, W., & Chua, K. F. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.10.002 · Cited by 267 · 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
Chaudhary, M. R., Chaudhary, S., Sharma, Y., Singh, T. A., Mishra, A. K., Sharma, S. G., & Mehdi, M. M. (2023) · Biogerontology · doi:10.1007/s10522-023-10050-1 · Cited by 210 · see citing works
SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases
Manjula, R., Anuja, K., & Alcain, F. J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.585821 · Cited by 193 · see citing works
Dual Tumor Suppressor and Tumor Promoter Action of Sirtuins in Determining Malignant Phenotype
Carafa, V., Altucci, L., & Nebbioso, A. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00038 · Cited by 183 · see citing works
Shi, Y., Zhu, X.-T., Su-na, Z., Ma, Y., Han, Y., Yue, J., & Zhang, Y. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1172481 · Cited by 179 · see citing works
The role of SIRT1 in diabetic cardiomyopathy
Karbasforooshan, H., & Karimi, G. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.03.056 · Cited by 155 · see citing works
Possible Adverse Effects of High-Dose Nicotinamide: Mechanisms and Safety Assessment
Hwang, E., & Song, S. (2020) · Biomolecules · doi:10.3390/biom10050687 · Cited by 144 · see citing works
Sirtuin 6 protects the brain from cerebral ischemia/reperfusion injury through NRF2 activation
Zhang, W., Wei, R., Zhang, L., Tan, Y., & Qian, C. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.09.035 · Cited by 137 · see citing works
How to reprogram microglia toward beneficial functions
Fumagalli, M., Lombardi, M., Gressèns, P., & Verderio, C. (2018) · Glia · doi:10.1002/glia.23484 · Cited by 134 · see citing works
Lee, J., & Hyun, D. (2023) · Antioxidants · doi:10.3390/antiox12040918 · Cited by 137 · see citing works
Sirtuins and nonalcoholic fatty liver disease
Nassir, F., & Ibdah, J. A. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i46.10084 · Cited by 127 · see citing works
Li, K., Zhai, M., Jiang, L., Song, F., Zhang, B., Li, J., Li, H., Li, B., Xia, L., Xu, L. L., et al. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6746907 · Cited by 123 · see citing works
Yu, L., Dong, X., Xue, X., Zhang, J., Li, Z., Wu, H., Yang, Z., Yang, Y., & Wang, H. (2019) · Food & Function · doi:10.1039/c9fo00001a · Cited by 121 · see citing works
Moniot, S., Forgione, M., Lucidi, A., Hailu, G. S., Nebbioso, A., Carafa, V., Baratta, F., Altucci, L., Giacchè, N., Passeri, D., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01609 · Cited by 110 · see citing works
Lv, Q., Wang, K., Qiao, S., Yang, L., Xin, Y., Dai, Y., & Wei, Z. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0297-3 · Cited by 110 · see citing works
Alpha-Secretase ADAM10 Regulation: Insights into Alzheimer’s Disease Treatment
Peron, R., Vatanabe, I. P., Manzine, P. R., Camins, A., & Cominetti, M. R. (2018) · Pharmaceuticals · doi:10.3390/ph11010012 · Cited by 111 · see citing works
DNA-Encoded Dynamic Chemical Library and Its Applications in Ligand Discovery
Zhou, Y., Li, C., Peng, J., Xie, L., Meng, L. H., Li, Q., Zhang, J., Li, X., Li, X., Huang, X., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09277 · Cited by 110 · see citing works
Epigenetic regulation in fibrosis progress
Xue, T., Qiu, X., Liu, H., Gan, C., Tan, Z., Xie, Y., Wang, D., & Ye, T. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105910 · Cited by 109 · see citing works
Lysine Deacetylase Inhibitors in Parasites: Past, Present, and Future Perspectives
Hailu, G. S., Robaa, D., Forgione, M., Sippl, W., Rotili, D., & Mai, A. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01595 · Cited by 106 · 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 118 · see citing works
Microglia-Mediated Neurodegeneration in Perinatal Brain Injuries
Fleiss, B., Steenwinckel, J. V., Bokobza, C., Shearer, I. K., Ross-Munro, E., & Gressèns, P. (2021) · Biomolecules · doi:10.3390/biom11010099 · Cited by 103 · see citing works
SIRT1/SREBPs-mediated regulation of lipid metabolism
Shen, S., Shen, M., Kuang, L., Yang, K., Wu, S., Liu, X., Wang, Y., & Wang, Y. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.107037 · Cited by 98 · see citing works
Targeting sirtuins for cancer therapy: epigenetics modifications and beyond
Shen, H., Qi, X., Hu, Y., Wang, Y., Zhang, J., Liu, Z., & Qin, Z. (2024) · Theranostics · doi:10.7150/thno.100667 · Cited by 95 · see citing works
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
Halsall, J. A., & Turner, B. M. (2016) · BioEssays · doi:10.1002/bies.201600070 · Cited by 85 · see citing works
Recent advances in the therapeutic applications of selenium nanoparticles
Ansari, J. A., Malik, J. A., Ahmed, S., Manzoor, M., Ahemad, N., & Anwar, S. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09598-z · Cited by 85 · see citing works
Sirtuin 1 and Alzheimer's disease: An up-to-date review
Rizzi, L., & Roriz‐Cruz, M. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.07.001 · Cited by 83 · see citing works
Bahl, S., & Seto, E. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03599-4 · Cited by 82 · see citing works
SIRT5 promotes cell proliferation and invasion in hepatocellular carcinoma by targeting E2F1
Chang, L., Liang, X., Liu, Y., Liu, R., Wu, Z., & Jian, Z. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7875 · Cited by 81 · see citing works
Subcellular compartmentalization of NAD+ and its role in cancer: A sereNADe of metabolic melodies
Zhu, Y., Liu, J., Park, J., Rai, P., & Zhai, R. G. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.04.002 · Cited by 82 · see citing works
Katwal, G., Baral, D., Fan, X., He, W., Zhang, X., Li, L., Xiong, Y., Ye, Q., & Wang, Y. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2976957 · Cited by 78 · see citing works
Trending topics of SIRT1 in tumorigenicity
Garcia‐Peterson, L. M., & Li, X. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129952 · Cited by 78 · see citing works
Sirtuin Acetylation and Deacetylation: a Complex Paradigm in Neurodegenerative Disease
Khan, H., Tiwari, P., Kaur, A., & Singh, T. G. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02387-w · Cited by 75 · see citing works
Bartoli‐Leonard, F., Wilkinson, F. L., Schiro, A., Serracino‐Inglott, F., Alexander, M. Y., & Weston, R. (2019) · Scientific Reports · doi:10.1038/s41598-018-37027-2 · Cited by 76 · see citing works
Zhang, Q., Chen, Y., Ni, D., Huang, Z., Wei, J., Li, F., Su, J., Wei, Y., Ning, S., Yang, X., et al. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.06.015 · Cited by 72 · see citing works
Zou, H., Chen, Y., Qu, H., Sun, J. G., Wang, T., Ma, Y., Yuan, Y., Bian, J., & Liu, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214411 · Cited by 76 · see citing works
Energy metabolism disorders and potential therapeutic drugs in heart failure
He, Y., Huang, W., Zhang, C., Chen, L., Xu, R., Li, N., Wang, F., Han, L., Yang, M., & Zhang, D. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.007 · Cited by 74 · see citing works
Yin, Y., Jiang, C. S., Zhang, M., Jin, J., Ge, S., & Wang, X. (2019) · Aging · doi:10.18632/aging.101954 · Cited by 73 · see citing works
Diverse therapeutic efficacies and more diverse mechanisms of nicotinamide
Song, S. B., Park, J., Chung, G. J., Lee, I. H., & Hwang, E. S. (2019) · Metabolomics · doi:10.1007/s11306-019-1604-4 · Cited by 73 · see citing works
Metabolic requirements of the nephron
Cargill, K. R., & Sims‐Lucas, S. (2018) · Pediatric Nephrology · doi:10.1007/s00467-018-4157-2 · Cited by 71 · see citing works
SIRT1 and Autophagy: Implications in Endocrine Disorders
Kim, J. Y., Mondaca‐Ruff, D., Singh, S., & Wang, Y. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.930919 · Cited by 71 · see citing works
Extranuclear Sirtuins and Metabolic Stress
Elkhwanky, M., & Hakkola, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7270 · Cited by 67 · see citing works
Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5
Fiorentino, F., Castiello, C., Mai, A., & Rotili, D. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00687 · Cited by 69 · see citing works
Histone Deacetylases and Their Inhibitors in Cancer Epigenetics
Hassell, K. N. (2019) · Diseases · doi:10.3390/diseases7040057 · Cited by 64 · see citing works
Groundbreaking Anticancer Activity of Highly Diversified Oxadiazole Scaffolds
Benassi, A., Doria, F., & Pirota, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228692 · Cited by 66 · see citing works
Accelerated Vascular Aging in Chronic Kidney Disease: The Potential for Novel Therapies
Hobson, S., Arefin, S., Witasp, A., Hernandez, L. N., Kublickiene, K. R., Shiels, P. G., & Stenvinkel, P. (2023) · Circulation Research · doi:10.1161/circresaha.122.321751 · Cited by 62 · see citing works
The Role of Histone Protein Acetylation in Regulating Endothelial Function
Fang, Z. H., Wang, X., Sun, X., Hu, W., & Miao, Q. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.672447 · Cited by 65 · see citing works
Sirtuins as endogenous regulators of lung fibrosis: A current perspective
Mazumder, S., Barman, M., Bandyopadhyay, U., & Bindu, S. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118201 · Cited by 61 · see citing works
Therapeutic effects of histone deacetylase inhibitors on heart disease
Chun, P. (2020) · Archives of Pharmacal Research · doi:10.1007/s12272-020-01297-0 · Cited by 61 · see citing works
Lambona, C., Zwergel, C., Valente, S., & Mai, A. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01979 · Cited by 61 · see citing works
Sirtuin modulators: where are we now? A review of patents from 2015 to 2019
Mautone, N., Zwergel, C., Mai, A., & Rotili, D. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2020.1749264 · Cited by 57 · see citing works
Histone H4 lysine 16 acetylation controls central carbon metabolism and diet-induced obesity in mice
Rodrigues, C. P., Chatterjee, A., Wiese, M., Stehlé, T., Szymanski, W. G., Shvedunova, M., & Akhtar, A. (2021) · Nature Communications · doi:10.1038/s41467-021-26277-w · Cited by 57 · see citing works
Sirtuin Modulators: Past, Present, and Future Perspectives
Fiorentino, F., Mautone, N., Menna, M., D’Acunzo, F., Mai, A., & Rotili, D. (2022) · Future Medicinal Chemistry · doi:10.4155/fmc-2022-0031 · Cited by 56 · see citing works
Salivary Biomarkers for Alzheimer’s Disease: A Systematic Review with Meta-Analysis
Nijakowski, K., Owecki, W., Jankowski, J., & Surdacka, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021168 · Cited by 56 · see citing works
Role of SIRT1 and Progesterone Resistance in Normal and Abnormal Endometrium
Kim, T. H., Young, S. L., Sasaki, T., Deaton, J. L., Schammel, D. P., Palomino, W. A., Jeong, J., & Lessey, B. A. (2021) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgab753 · Cited by 55 · see citing works
Yu, L., Dong, X., Xue, X., Zhang, J., Li, Z., Wu, H., Yang, Z., Yang, Y., & Wang, H. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.05.003 · Cited by 55 · see citing works
Growth factor, energy and nutrient sensing signalling pathways in metabolic ageing
Bettedi, L., & Foukas, L. C. (2017) · Biogerontology · doi:10.1007/s10522-017-9724-6 · Cited by 54 · see citing works
Sirtuin-4 (SIRT4), a therapeutic target with oncogenic and tumor-suppressive activity in cancer
Huang, G., & Zhu, G. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s157724 · Cited by 52 · see citing works
RIP1–HAT1–SIRT Complex Identification and Targeting in Treatment and Prevention of Cancer
Carafa, V., Nebbioso, A., Cuomo, F., Rotili, D., Cobellis, G., Bontempo, P., Baldi, A., Spugnini, E. P., Citro, G., Chambery, A., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3081 · Cited by 50 · see citing works
Nebbioso, M., Lambìase, A., Armentano, M., Tucciarone, G., Sacchetti, M., Greco, A., & Alisi, L. (2021) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2021.04.003 · Cited by 50 · see citing works
Ceballos, M. P., Decándido, G., Quiroga, A. D., Comanzo, C. G., Livore, V. I., Lorenzetti, F., Lambertucci, F., Chazarreta-Cifre, L., Banchio, C., Álvarez, M. D. L., et al. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.03.011 · Cited by 49 · see citing works
The Role of Sirtuin 1 (SIRT1) in Neurodegeneration
Razick, D., Akhtar, M., Wen, J., Alam, M., Dean, N., Karabala, M., Ansari, U., Ansari, Z., Tabaie, E. A., & Siddiqui, S. (2023) · Cureus · doi:10.7759/cureus.40463 · Cited by 48 · see citing works
Therapeutic effects of histone deacetylase inhibitors on kidney disease
Chun, P. (2017) · Archives of Pharmacal Research · doi:10.1007/s12272-017-0998-7 · Cited by 48 · see citing works
Human sirtuins: Structures and flexibility
Sacconnay, L., Carrupt, P., & Nurisso, A. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.10.008 · Cited by 47 · see citing works
Wei, W., Guo, X., Gu, L., Jia, J., Yang, M. G., Yuan, W., & Rong, S. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02307-8 · Cited by 47 · see citing works
Imidazo[1,2-b]pyridazine as privileged scaffold in medicinal chemistry: An extensive review
Garrido, A., Vera, G., Delaye, P., & Enguehard‐Gueiffier, C. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113867 · Cited by 47 · see citing works
Mayor, E. (2023) · Frontiers in Aging · doi:10.3389/fragi.2023.1161814 · Cited by 46 · see citing works
Islam, S., Uehara, O., Matsuoka, H., Kuramitsu, Y., Adhikari, B. R., Hiraki, D., Toraya, S., Jayawardena, A., Saito, I., Muthumala, M., et al. (2020) · Clinical Epigenetics · doi:10.1186/s13148-019-0806-y · Cited by 45 · see citing works
Terminal Schwann Cell Aging: Implications for Age-Associated Neuromuscular Dysfunction
Fuertes-Álvarez, S., & Izeta, A. (2021) · Aging and Disease · doi:10.14336/ad.2020.0708 · Cited by 43 · see citing works
Fruits: A Source of Polyphenols and Health Benefits
Calderón‐Oliver, M., & Ponce‐Alquicira, E. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-811518-3.00007-7 · Cited by 42 · see citing works
Cardioprotective effect of a moderate and prolonged exercise training involves sirtuin pathway
Donniacuo, M., Urbanek, K., Nebbioso, A., Sodano, L., Gallo, L., Altucci, L., & Rinaldi, B. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.001 · Cited by 42 · see citing works
Palomer, E., Martín‐Flores, N., Jolly, S., Vargas, P. P., Benvegnù, S., Podpolny, M., Teo, S., Vaher, K., Saito, T., Saido, T. C., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01492-z · Cited by 42 · see citing works
Urbán, V. S., Ceglédi, A., & Mikala, G. (2022) · GeroScience · doi:10.1007/s11357-022-00698-x · Cited by 43 · see citing works
Anticancer Activities of a Benzimidazole Compound Through Sirtuin Inhibition in Colorectal Cancer
Tan, Y. J., Lee, Y. T., Yeong, K. Y., Petersen, S. H., Kono, K., Tan, S. C., & Oon, C. E. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0052 · Cited by 39 · see citing works
Melatonin as Potential Targets for Delaying Ovarian Aging
Yang, Y., Cheung, H., Zhang, C., Wu, J., & Chan, W. (2018) · Current Drug Targets · doi:10.2174/1389450119666180828144843 · Cited by 39 · see citing works
Effects of (−)-epicatechin on mitochondria
Daussin, F., Heyman, E., & Burelle, Y. (2020) · Nutrition Reviews · doi:10.1093/nutrit/nuaa094 · Cited by 38 · see citing works
Sirtuin Modulators in Cellular and Animal Models of Human Diseases
Hong, J. Y., & Lin, H. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.735044 · Cited by 39 · see citing works
Sirtuins in metabolism, stemness and differentiation
Correia, M., Perestrelo, T., Rodrigues, A. S., Ribeiro, M. F., Pereira, S. L., Sousa, M. I., & Ramalho‐Santos, J. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.09.008 · Cited by 40 · see citing works
Histone deacetylases as targets in autoimmune and autoinflammatory diseases
Hamminger, P., Rîca, R., & Ellmeier, W. (2020) · Advances in immunology · doi:10.1016/bs.ai.2020.06.001 · Cited by 38 · 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
Designing HDAC-PROTACs: Lessons Learned So Far
Fischer, F., Avelar, L. A. A., Murray, L., & Kurz, T. (2021) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0206 · Cited by 38 · see citing works
NAD+ centric mechanisms and molecular determinants of skeletal muscle disease and aging
Wagner, S., Manickam, R., Brotto, M. A. P., & Tipparaju, S. M. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04408-1 · Cited by 39 · see citing works
Shen, H., Ma, W., Hu, Y., Liu, Y., Song, Y., Fu, L., & Qin, Z. (2024) · Theranostics · doi:10.7150/thno.97320 · Cited by 38 · see citing works
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
Moore, A. M., Zhou, L., Cui, J., Li, L., Wu, N., Yu, A. C., Poddar, S., Liang, K., Abt, E. R., Kim, S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012469118 · Cited by 36 · see citing works
p53 regulated senescence mechanism and role of its modulators in age-related disorders
Pawge, G., & Khatik, G. L. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114651 · Cited by 36 · see citing works
Alterations of Chromatin Regulators in the Pathogenesis of Urinary Bladder Urothelial Carcinoma
Hoffmann, M. J., & Schulz, W. A. (2021) · Cancers · doi:10.3390/cancers13236040 · Cited by 37 · see citing works
Exploring the therapeutic potential of quercetin: A focus on its sirtuin‐mediated benefits
Ungurianu, A., Zanfirescu, A., & Margina, D. M. (2024) · Phytotherapy Research · doi:10.1002/ptr.8168 · Cited by 36 · see citing works
SIRT2 Contributes to the Resistance of Melanoma Cells to the Multikinase Inhibitor Dasatinib
Karwaciak, I., Sałkowska, A., Karaś, K., Sobalska‐Kwapis, M., Walczak‐Drzewiecka, A., Pułaski, Ł., Strapagiel, D., Dastych, J., & Ratajewski, M. (2019) · Cancers · doi:10.3390/cancers11050673 · Cited by 35 · see citing works
Sinha, S., Sharma, S., Vora, J., & Shrivastava, N. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104880 · Cited by 35 · see citing works
Natural Bioactive Products as Epigenetic Modulators for Treating Neurodegenerative Disorders
Martínez-Iglesias, O. A., Naidoo, V., Carrera, I., Corzo, L., & Cacabelos, R. (2023) · Pharmaceuticals · doi:10.3390/ph16020216 · Cited by 36 · see citing works
Molecular Sentinels: Unveiling the Role of Sirtuins in Prostate Cancer Progression
Chouhan, S., Muhammad, N., Usmani, D., Khan, T. H., & Kumar, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms26010183 · Cited by 34 · see citing works
HDAC6—An Emerging Target Against Chronic Myeloid Leukemia?
Losson, H., Schnekenburger, M., Dicato, M. A., & Diederich, M. F. (2020) · Cancers · doi:10.3390/cancers12020318 · Cited by 32 · see citing works
- Authors
- Carafa, V., Rotili, D., Forgione, M., Cuomo, F., Serretiello, E., Hailu, G. S., Jarho, E., Lahtela-Kakkonen, M., Mai, A., & Altucci, L.
- Affiliations
- University of Campania "Luigi Vanvitelli" (IT)
- Sapienza University of Rome (IT)
- Italian Institute of Technology (IT)
- University of Eastern Finland (FI)
- Istituto Pasteur (IT)
- Corresponding author
- Mai, Antonello
- Altucci, Lucia
- ORCID
- Venue
- Clinical Epigenetics
- Published
- 2016-05-25
- Volume
- 8
- Issue
- 1
- Pages
- 61-61
- ISSN
- 1868-7075 (ISSN-L)
- 1868-7083
- PMC
- PMC4879741
- OpenAlex
- W2405840972
- Cited by
- 387
- References
- 119
- Citations by year
- 2026: 23 · 2025: 27 · 2024: 54 · 2023: 53 · 2022: 44 · 2021: 55 · 2020: 45 · 2019: 32 · 2018: 25 · 2017: 19 · 2016: 9 · 2015: 1
- FWCI
- 2.91
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Clinical Epigenetics (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UEF eRepo (University of Eastern Finland) (submittedVersion, cc-by)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion, cc-by)
- Archivio Istituzionale della Ricerca - Università degli Studi della Campania "Luigi Vanvitelli" (submittedVersion)
- Iris (Roma Tre University) (submittedVersion)
- Funders
- EU-Blueprint (282510)
- EU-A-PARADDISE (602080)
- EU-Cost action EPICHEMBIO (CM1406)
- PRIN-2012
- AIRC (17217)
- AIRC-Fondazione Cariplo TRIDEO (17515)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- sirtuins, NAD+-dependent histone deacetylase, sirtuin inhibitors, sirtuin activators, small molecule modulators, epigenetic regulation, caloric restriction, aging, neurodegenerative diseases, cardiovascular disease, cancer, cellular metabolism, apoptosis, DNA repair
- MeSH terms
- Cell Survival, DNA Repair, Enzyme Inhibitors, Gene Expression Regulation, Humans, Cellular Senescence, Sirtuins, Epigenesis, Genetic, Cell Proliferation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review