The DOI matches its Crossref record; 118 of the 119 references it cites were found in a registry or an index.
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.
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“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]
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Citations
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 208
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
Calamita, E., Schmid, M., Kunz, M., Ndebele-Murisa, M. R., Magadza, C. H. D., Nyambe, I., & Wehrli, B. (2019) · Figshare · doi:10.26181/6153922fe919c · Cited by 4,239
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924
Sirtuin activators mimic caloric restriction and delay ageing in metazoans
Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · cited 1×
“Mice treated with resveratrol display improved mitochondrial functions and protection against high-fat diet-induced obesity [100], while in obese mice, treatment with resveratrol leads to increased healthspan and lifespan [101].”
BackgroundSirt5 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
Research works printed but not linked: 2
- Vu CB OC, Perni RB, Disch JS, Szczepankiewicz B, Gualtieri G, et al. Inventor solubilized thiazolopyridines. 2009.
- Vu CB DJ, Ng PY, Blum CA, Perni RB. Inventor benzimidazoles and related analogs as sirtuin modulators. 2010.
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 928
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
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
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 732
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 364
Metadata
- 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
- 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
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