The DOI matches its Crossref record; 202 of the 202 references it cites were found in a registry or an index.
Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds
Open accessAbstract
The sirtuins (SIRT1-7) are a family of nicotinamide adenine dinucleotide (NAD+)-dependent deacylases with remarkable abilities to prevent diseases and even reverse aspects of ageing. Mice engineered to express additional copies of SIRT1 or SIRT6, or treated with sirtuin-activating compounds (STACs) such as resveratrol and SRT2104 or with NAD+ precursors, have improved organ function, physical endurance, disease resistance and longevity. Trials in non-human primates and in humans have indicated that STACs may be safe and effective in treating inflammatory and metabolic disorders, among others. These advances have demonstrated that it is possible to rationally design molecules that can alleviate multiple diseases and possibly extend lifespan in humans.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Inhibitors of histone acetyltransferases also ameliorate the premature aging phenotype and extend lifespan of progeroid mice, while histone deacetylase activators promote longevity in part via upregulation of SIRT1 activity 61 .”
From Hallmarks of aging: An expanding universe (2023) · cites this paper as [61]
Experimental — accuracy not yet measuredIn the citing paper
“Thus, activation of SIRT1 by resveratrol and its synthetic structural derivatives288,289 and melatonin290 may prevent adduct formation and AGE-associated disease conditions.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [288]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Age related changes in NAD+ metabolism oxidative stress and Sirt1 activity in wistar rats
Braidy, N., Guillemin, G. J., Mansour, H., Chan-Ling, T., Poljak, A., & Grant, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019194 · Cited by 594
RetractedLópez-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290
Self-citationLagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057
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
Self-citationTranscriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
A C. elegans mutant that lives twice as long as wild type
Kenyon, C., Chang, J., Gensch, E., Rudner, A., & Tabtiang, R. (1993) · Nature · doi:10.1038/366461a0 · Cited by 3,387
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750
Cited by
Sorted by citations
Hallmarks of aging: An expanding universe
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2023) · Cell · doi:10.1016/j.cell.2022.11.001 · Cited by 6,549
From discoveries in ageing research to therapeutics for healthy ageing
Campisi, J., Kapahi, P., Lithgow, G. J., Melov, S., Newman, J. C., & Verdin, E. (2019) · Nature · doi:10.1038/s41586-019-1365-2 · Cited by 1,389
Functions and mechanisms of non-histone protein acetylation
Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232
The effects of polyphenols and other bioactives on human health
Fraga, C. G., Croft, K. D., Kennedy, D. O., & Tomás-Barberán, F. A. (2019) · Food & Function · doi:10.1039/c8fo01997e · Cited by 1,200
Why does COVID-19 disproportionately affect older people?
Mueller, A. L., McNamara, M. S., & Sinclair, D. A. (2020) · Aging · doi:10.18632/aging.103344 · Cited by 1,128
Self-citationModulation of cellular processes by histone and non-histone protein acetylation
Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 1,007
Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence
Rajman, L., Chwalek, K., & Sinclair, D. A. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.011 · Cited by 865
Self-citationNAD+ in Brain Aging and Neurodegenerative Disorders
Lautrup, S., Sinclair, D. A., Mattson, M. P., & Fang, E. F. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.001 · Cited by 790
Self-citationRegulation of SIRT1 and Its Roles in Inflammation
Yang, Y., Liu, Y., Wang, Y., Chao, Y., Zhang, J., Jia, Y., Tie, J., & Hu, D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.831168 · Cited by 737
The metabolic roots of senescence: mechanisms and opportunities for intervention
Wiley, C. D., & Campisi, J. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00483-8 · Cited by 691
Epigenetic regulation of aging: implications for interventions of aging and diseases
Kang, W., Liu, H., Hu, Q., Wang, L., Liu, J., Zheng, Z., Zhang, W., Ren, J., Zhu, F., & Liu, G. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01211-8 · Cited by 732
Quantitative Analysis of NAD Synthesis-Breakdown Fluxes
Liu, L., Su, X., Quinn, W. J., Hui, S., Krukenberg, K., Frederick, D. W., Redpath, P., Zhan, L., Chellappa, K., White, E., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.018 · Cited by 564
Meta-hallmarks of aging and cancer
López-Otín, C., Pietrocola, F., Roiz-Valle, D., Galluzzi, L., & Kroemer, G. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2022.11.001 · Cited by 529
NAD+ metabolism, stemness, the immune response, and cancer
Navas, L. E., & Carnero, A. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00354-w · Cited by 551
Immunosenescence: a key player in cancer development
Lian, J., Yue, Y., Yu, W., & Zhang, Y. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00986-z · Cited by 510
NAD(+) in aging: molecular mechanisms and translational implications
Fang, E. F., Lautrup, S., Hou, Y., Demarest, T. G., Croteau, D. L., Mattson, M. P., & Bohr, V. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.08.001 · Cited by 501
Macrophage de novo NAD+ synthesis specifies immune function in aging and inflammation
Minhas, P. S., Liu, L., Moon, P. K., Joshi, A. U., Dove, C., Mhatre, S., Contrepois, K., Wang, Q., Lee, B. A., Coronado, M., et al. (2019) · Nature Immunology · doi:10.1038/s41590-018-0255-3 · Cited by 501
Sirtuins and NAD + in the Development and Treatment of Metabolic and Cardiovascular Diseases
Kane, A. E., & Sinclair, D. A. (2018) · Circulation Research · doi:10.1161/circresaha.118.312498 · Cited by 497
Self-citationHou, Y., Lautrup, S., Cordonnier, S., Wang, Y., Croteau, D. L., Zavala, E., Zhang, Y., Moritoh, K., O’Connell, J. F., Baptiste, B. A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718819115 · Cited by 472
Sirtuins, a promising target in slowing down the ageing process
Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470
Sirtuin activators and inhibitors: Promises, achievements, and challenges
Dai, H., Sinclair, D. A., Ellis, J. L., & Steegborn, C. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.03.004 · Cited by 463
Self-citationSirtuin signaling in cellular senescence and aging
Lee, S.-H., Lee, J.-H., Lee, H., & Min, K. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.1.290 · Cited by 449
Cai, Y., Song, W., Li, J., Jing, Y., Liang, C., Zhang, L., Zhang, X., Zhang, W., Liu, B., An, Y., et al. (2022) · Science China Life Sciences · doi:10.1007/s11427-022-2161-3 · Cited by 450
Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411
Zhu, X., Chen, Z., Shen, W., Huang, G., Sedivy, J. M., Wang, H., & Ju, Z. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00646-9 · Cited by 425
DNA damage and repair in age-related inflammation
Zhao, Y., Simon, M. A., Seluanov, A., & Gorbunova, V. A. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00751-y · Cited by 400
De novo NAD+ biosynthetic impairment in acute kidney injury in humans
Mehr, A. P., Tran, M. T., Ralto, K. M., Leaf, D. E., Washco, V., Messmer, J., Lerner, A., Kher, A., Kim, S. H., Khoury, C. C., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0138-z · Cited by 373
Mitophagy in neurodegeneration and aging
Fivenson, E. M., Lautrup, S., Sun, N., Scheibye-Knudsen, M., Stevnsner, T., Nilsen, H., Bohr, V. A., & Fang, E. F. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.02.007 · Cited by 364
Mitochondria and Epigenetics – Crosstalk in Homeostasis and Stress
Matilainen, O., Quirós, P. M., & Auwerx, J. H. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.02.004 · Cited by 376
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
Sirtuins in Renal Health and Disease
Morigi, M., Perico, L., & Benigni, A. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017111218 · Cited by 359
Xie, C., Zhuang, X., Niu, Z., Ai, R., Lautrup, S., Zheng, S., Jiang, Y., Han, R., Gupta, T. S., Cao, S., et al. (2022) · Nature Biomedical Engineering · doi:10.1038/s41551-021-00819-5 · Cited by 350
SIRT2 Acts as a Cardioprotective Deacetylase in Pathological Cardiac Hypertrophy
Tang, X., Chen, X., Wang, N.-Y., Wang, X., Liang, S., Zheng, W., Lu, Y., Zhao, X., Hao, D., Zhang, Z., et al. (2017) · Circulation · doi:10.1161/circulationaha.117.028728 · Cited by 343
Song, T., Song, X., Zhu, C., Patrick, R., Skurla, M., Santangelo, I., Green, M., Harper, D., Ren, B., Forester, B. P., et al. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101503 · Cited by 346
Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337
Miao, Y., Cui, Z., Gao, Q., Rui, R., & Xiong, B. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107987 · Cited by 312
Targeting mitochondria for cardiovascular disorders: therapeutic potential and obstacles
Bonora, M., Wieckowski, M. R., Sinclair, D. A., Kroemer, G., Pinton, P., & Galluzzi, L. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0074-0 · Cited by 308
Self-citationNAD+ homeostasis in renal health and disease
Ralto, K. M., Rhee, E. P., & Parikh, S. M. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0216-6 · Cited by 293
Effects of hydrogen sulfide on mitochondrial function and cellular bioenergetics
Paul, B. D., Snyder, S. H., & Kashfi, K. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101772 · Cited by 289
Niacin in the Central Nervous System: An Update of Biological Aspects and Clinical Applications
Gasperi, V., Sibilano, M., Savini, I., & Catani, M. V. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040974 · Cited by 286
Drosophila as a model for ageing
Piper, M. D. W., & Partridge, L. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.016 · Cited by 273
Lysine acetyltransferases and lysine deacetylases as targets for cardiovascular disease
Li, P., Ge, J., & Li, H. (2020) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0235-9 · Cited by 269
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 274
Hano, C., & Tungmunnithum, D. (2020) · Medicines · doi:10.3390/medicines7050026 · Cited by 275
The role of nutrition in inflammaging
Giosia, P. D., Stamerra, C. A., Giorgini, P., Jamialahamdi, T., Butler, A. E., & Sahebkar, A. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101596 · Cited by 262
Mitochondrial sirtuins, metabolism, and aging
Ji, Z., Liu, G., & Qu, J. T. (2021) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2021.11.005 · Cited by 250
Stilbene-based natural compounds as promising drug candidates against COVID-19
Wahedi, H. M., Ahmad, S., & Abbasi, S. W. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1762743 · Cited by 249
Key proteins and pathways that regulate lifespan
Pan, H., & Finkel, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.771915 · Cited by 228
Aging - Oxidative stress, antioxidants and computational modeling
Warraich, U.-E.-A., Hussain, F., & Kayani, H. U. R. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e04107 · Cited by 222
Increase in blood–brain barrier leakage in healthy, older adults
Verheggen, I. C. M., de Jong, J. J. A., van Boxtel, M. P. J., Gronenschild, E. H. B. M., Palm, W. M., Postma, A. A., Jansen, J. F. A., Verhey, F. R. J., & Backes, W. H. (2020) · GeroScience · doi:10.1007/s11357-020-00211-2 · Cited by 214
Gut stem cell aging is driven by mTORC1 via a p38 MAPK-p53 pathway
He, D. N., Wu, H., Xiang, J., Ruan, X., Peng, P., Ruan, Y., Chen, Y., Wang, Y., Yu, Q., Zhang, H., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13911-x · Cited by 198
Song, Y., Li, S., Geng, W., Luo, R., Liu, W., Tu, J., Wang, K., Kang, L., Yin, H., Wu, X., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.006 · Cited by 194
A conserved NAD + binding pocket that regulates protein-protein interactions during aging
Li, J., Bonkowski, M. S., Moniot, S., Zhang, D., Hubbard, B. P., Ling, A. J. Y., Rajman, L. A., Qin, B., Lou, Z., Gorbunova, V. A., et al. (2017) · Science · doi:10.1126/science.aad8242 · Cited by 188
Self-citationMetabolic landscape in cardiac aging: insights into molecular biology and therapeutic implications
Xie, S., Xu, S., Deng, W., & Tang, Q. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01378-8 · Cited by 197
Dellinger, R. W., Santos, S. R., Morris, M., Evans, M., Alminana, D., Guarente, L., & Marcotulli, E. (2017) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-017-0016-9 · Cited by 181
Santos, A. L., Sinha, S., & Lindner, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1941285 · Cited by 168
Shenoy, S. (2020) · Inflammation Research · doi:10.1007/s00011-020-01389-z · Cited by 179
The multifaceted benefits of walking for healthy aging: from Blue Zones to molecular mechanisms
Ungvari, Z. I., Fazekas‐Pongor, V., Csiszár, A., & Kunutsor, S. K. (2023) · GeroScience · doi:10.1007/s11357-023-00873-8 · Cited by 208
Johnson, A. A., Shokhirev, M. N., Wyss-Coray, T., & Lehallier, B. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101070 · Cited by 166
The metabolomics of human aging: Advances, challenges, and opportunities
Panyard, D. J., Yu, B., & Snyder, M. P. (2022) · Science Advances · doi:10.1126/sciadv.add6155 · Cited by 159
Turning back time with emerging rejuvenation strategies
Mahmoudi, S., Xu, L., & Brunet, A. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0206-0 · Cited by 171
Remie, C. M., Roumans, K. H., Moonen, M. P., Connell, N. J., Havekes, B., Mevenkamp, J., Lindeboom, L., de Wit, V. H., van de Weijer, T., Aarts, S. A., et al. (2020) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqaa072 · Cited by 160
Tolahunase, M., Sagar, R., & Dada, R. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7928981 · Cited by 172
NLRP3 inflammasome activation in inflammaging
Latz, E., & Duewell, P. (2018) · Seminars in Immunology · doi:10.1016/j.smim.2018.09.001 · Cited by 174
Mediterranean diet and inflammaging within the hormesis paradigm
Martucci, M., Ostan, R., Biondi, F., Bellavista, E., Fabbri, C., Bertarelli, C., Salvioli, S., Capri, M., Franceschi, C., & Santoro, A. (2017) · Nutrition Reviews · doi:10.1093/nutrit/nux013 · Cited by 167
New insight into dyslipidemia‐induced cellular senescence in atherosclerosis
Xiang, Q., Tian, F., Xu, J. R., Du, X., Zhang, S., & Liu, L. (2022) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12866 · Cited by 169
Zhang, G., Deng, Y.-J., Xie, Q.-Q., Ren, E., Ma, Z., He, X., Gao, Y., & Kang, X. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.04.016 · Cited by 158
SIRT6 in Aging, Metabolism, Inflammation and Cardiovascular Diseases
Guo, Z., Li, P., Ge, J., & Li, H. (2022) · Aging and Disease · doi:10.14336/ad.2022.0413 · Cited by 166
Huang, K., Gao, X., & Wei, W. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.09.042 · Cited by 155
SIRT1 activation attenuates cardiac fibrosis by endothelial-to-mesenchymal transition
Liu, Z., Zhang, Y., Wang, X., Fan, X., Zhang, Y., Li, X., Gong, Y., & Han, L. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109227 · Cited by 158
Mitochondria initiate and regulate sarcopenia
Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153
“SIRT1 is important for deacetylation of mitochondrial-interacting targets like PGC-1α, FOXO3, p53, and NF-kB (reviewed in (13,110) and has been implicated in improving function and life span in aging (95).”
BackgroundAging and Caloric Restriction Research: A Biological Perspective with Translational Potential
Balasubramanian, P., Howell, P. R., & Anderson, R. M. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.06.015 · Cited by 148
Mechanisms and disease implications of sirtuin-mediated autophagic regulation
Lee, I. H. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0302-7 · Cited by 151
Immunosenescence: signaling pathways, diseases and therapeutic targets
Fu, Y., Wang, B., Alu, A., Hong, W., Hong, L., He, X., Shi, H., Cheng, P., & Yang, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02371-z · Cited by 168
AMP-Activated Protein Kinase Regulation of the NLRP3 Inflammasome during Aging
Cordero, M. D., Williams, M. R., & Ryffel, B. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.10.009 · Cited by 149
Dollerup, O. L., Chubanava, S., Agerholm, M., Søndergård, S. D., Altıntaş, A., Møller, A. B., Høyer, K. F., Ringgaard, S., Stødkilde‐Jørgensen, H., Lavery, G. G., et al. (2020) · The Journal of Physiology · doi:10.1113/jp278752 · Cited by 145
Possible Adverse Effects of High-Dose Nicotinamide: Mechanisms and Safety Assessment
Hwang, E., & Song, S. (2020) · Biomolecules · doi:10.3390/biom10050687 · Cited by 144
The landscape of transcription errors in eukaryotic cells
Goût, J.-F., Li, W., Fritsch, C., Li, A., Haroon, S., Singh, L. N., Ding, H., Fazelinia, H., Smith, Z., Seeholzer, S. H., et al. (2017) · Science Advances · doi:10.1126/sciadv.1701484 · Cited by 143
Sirtuins and Insulin Resistance
Zhou, S., Tang, X., & Chen, H. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00748 · Cited by 155
Ni, D., Wei, J., He, X., Rehman, A. U., Li, X., Qiu, Y., Pu, J., Lu, S., & Zhang, J. (2020) · Chemical Science · doi:10.1039/d0sc05131d · Cited by 138
The flavonoid 4,4′-dimethoxychalcone promotes autophagy-dependent longevity across species
Carmona‐Gutiérrez, D., Zimmermann, A., Kainz, K., Pietrocola, F., Chen, G., Maglioni, S., Schiavi, A., Nah, J., Mertel, S., Beuschel, C. B., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08555-w · Cited by 138
Shi, S., Lei, S., Tang, C., Wang, K., & Xia, Z. (2019) · Bioscience Reports · doi:10.1042/bsr20181614 · Cited by 135
Semisynthetic biosensors for mapping cellular concentrations of nicotinamide adenine dinucleotides
Sallin, O., Reymond, L., Gondrand, C., Raith, F., Koch, B., & Johnsson, K. (2018) · eLife · doi:10.7554/elife.32638 · Cited by 137
Kiss, T., Balasubramanian, P., Valcarcel‐Ares, M. N., Tarantini, S., Yabluchanskiy, A., Csípő, T., Lipécz, Á., Reglődi, D., Zhang, X. A., Bari, F., et al. (2019) · GeroScience · doi:10.1007/s11357-019-00074-2 · Cited by 134
Targeting Mitochondrial Impairment in Parkinson's Disease: Challenges and Opportunities
Prasuhn, J., Davis, R. L., & Kumar, K. R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.615461 · Cited by 135
Sirtuins and FoxOs in osteoporosis and osteoarthritis
Almeida, M., & Porter, R. M. (2019) · Bone · doi:10.1016/j.bone.2019.01.018 · Cited by 131
Zhuang, L., Xia, W., Chen, D., Ye, Y., Hu, T., Li, S., & Hou, M. (2020) · Journal of Nanobiotechnology · doi:10.1186/s12951-020-00716-0 · Cited by 125
Metformin Is a Direct SIRT1-Activating Compound: Computational Modeling and Experimental Validation
Cuyàs, E., Verdura, S., Llorach-Parés, L., Fernández-Arroyo, S., Joven, J., Martin-Castillo, B., Bosch-Barrera, J., Brunet, J., Nonell-Canals, A., Sanchez-Martinez, M., et al. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00657 · Cited by 122
Mitochondrial Regulation of Stem Cells in Bone Homeostasis
Zheng, C., Sui, B., Qiu, X., Hu, C., & Jin, Y. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.04.008 · Cited by 121
The road ahead for health and lifespan interventions
Gonzalez-Freire, M., Diaz-Ruiz, A., Hauser, D., Martinez-Romero, J., Ferrucci, L., Bernier, M., & de Cabo, R. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101037 · Cited by 118
From molecular promise to preclinical results: HDAC inhibitors in the race for healthy aging drugs
McIntyre, R. L., Daniels, E. G., Molenaars, M., Houtkooper, R. H., & Janssens, G. E. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201809854 · Cited by 115
Zou, Y., Wang, A., Huang, L. Z., Zhu, X., Hu, Q., Zhang, Y., Chen, X., Li, F., Wang, Q., Wang, H., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.02.017 · Cited by 117
Park, H.-K., Hong, J.-H., Oh, Y. T., Kim, S. S., Yin, J., Lee, A., Chae, Y. C., Kim, J. H., Park, S., Park, C.-K., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-2558 · Cited by 119
Role of epigenetic regulation in myocardial ischemia/reperfusion injury
Wang, K., Li, Y., Qiang, T., Chen, J., & Wang, X. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105743 · Cited by 118
Evidence for Biological Age Acceleration and Telomere Shortening in COVID-19 Survivors
Mongelli, A., Barbi, V., Zamperla, M. G., Atlante, S., Forleo, L., Nesta, M., Massetti, M., Pontecorvi, A., Nanni, S., Farsetti, A., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116151 · Cited by 113
Sirtuins, resveratrol and the intertwining cellular pathways connecting them
Ungurianu, A., Zanfirescu, A., & Margina, D. M. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101936 · Cited by 114
Caloric Restriction Mimetics in Nutrition and Clinical Trials
Hofer, S. J., Davinelli, S., Bergmann, M., Scapagnini, G., & Madeo, F. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.717343 · Cited by 109
The chemistry of the vitamin B3 metabolome
Makarov, M. V., Trammell, S. A. J., & Migaud, M. E. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180420 · Cited by 115
D'Arcy, M. (2024) · APOPTOSIS · doi:10.1007/s10495-024-01977-y · Cited by 118
Dolopikou, C. F., Kourtzidis, I. A., Margaritelis, N. V., Vrabas, I. S., Koidou, E., Kyparos, A., Theodorou, A. A., Paschalis, V., & Nikolaidis, M. G. (2019) · European Journal of Nutrition · doi:10.1007/s00394-019-01919-4 · Cited by 106
Metadata
- Authors
- Bonkowski, M. S., & Sinclair, D. A.
- Affiliations
- Harvard University (US)
- Corresponding author
- Sinclair, David A.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2016-08-24
- Volume
- 17
- Issue
- 11
- Pages
- 679-690
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC5107309
- OpenAlex
- W2515158101
- Cited by
- 834
- References
- 202
- Citations by year
- 2026: 59 · 2025: 87 · 2024: 105 · 2023: 80 · 2022: 93 · 2021: 108 · 2020: 106 · 2019: 66 · 2018: 71 · 2017: 57 · 2016: 2
- FWCI
- 6.61
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Glenn Foundation for Medical Research
- National Institute on Aging (R37AG028730)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK100263)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- sirtuins, NAD+ precursors, aging, lifespan extension, SIRT1, SIRT6, resveratrol, SRT2104, NAD+-dependent deacylases, metabolic disorders, inflammatory diseases, drug design
- MeSH terms
- Resveratrol, Aging, Allosteric Regulation, Animals, Clinical Trials as Topic, Humans, NAD, Stilbenes, Enzyme Activators, Sirtuins
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