Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
Open accessAbstract
Caloric restriction (CR) extends the life span and health span of a variety of species and slows the progression of age-related hearing loss (AHL), a common age-related disorder associated with oxidative stress. Here, we report that CR reduces oxidative DNA damage in multiple tissues and prevents AHL in wild-type mice but fails to modify these phenotypes in mice lacking the mitochondrial deacetylase Sirt3, a member of the sirtuin family. In response to CR, Sirt3 directly deacetylates and activates mitochondrial isocitrate dehydrogenase 2 (Idh2), leading to increased NADPH levels and an increased ratio of reduced-to-oxidized glutathione in mitochondria. In cultured cells, overexpression of Sirt3 and/or Idh2 increases NADPH levels and protects from oxidative stress-induced cell death. Therefore, our findings identify Sirt3 as an essential player in enhancing the mitochondrial glutathione antioxidant defense system during CR and suggest that Sirt3-dependent mitochondrial adaptations may be a central mechanism of aging retardation in mammals.
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?
SIRT3 is essential for caloric restriction-mediated mitigation of oxidative damage by regulating the glutathione antioxidant system, thereby regulating senescence-associated pathologies propagated by oxidative stress.
“SIRT3 is also essential for the caloric restriction-mediated mitigation of oxidative damage by regulating the glutathione antioxidant system, thereby regulating senescence-associated pathologies propagated by oxidative stress [209].”
From Redox control of senescence and age-related disease. (2017) · cites this paper as [209]
SIRT3 deacetylates manganese superoxide dismutase and isocitrate dehydrogenase 2.
“The mitochondrial SIRT3 deacetylates two of these enzymes: manganese superoxide dismutase (MnSOD) (Tao et al. 2010) and isocitrate dehydrogenase 2 (IDH2)(Someya et al. 2010).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Someya et al. 2010
SIRT3 is necessary for the protective effect of calorie restriction on age-related hearing loss.
“Remarkably, SIRT3 is necessary for the protective effect of calorie restriction on age-related hearing loss supporting a key role for SIRT3-dependent mitochondrial adaptations against aging in mammals (Someya et al. 2010).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Someya et al. 2010
Many protective features of the calorie-restriction response, including resistance to oxidative stress and reduced hearing loss, require SIRT3.
“SIRT3 is required for many protective aspects of this adaptive shift ((Someya et al. 2010); (Qiu et al. 2010); (Amigo et al. 2017)), such as oxidative stress resistance and attenuated hearing loss.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Someya et al. 2010
Two enzymes involved in ROS detoxification, MnSOD and IDH2, are direct targets of SirT3.
“Recently, two enzymes that have a role in the detoxification of ROS were demonstrated to be direct targets of SirT3 (Qiu et al., 2010; Someya et al., 2010; Tao et al., 2010).”
From SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production (2011) · cites this paper as Someya et al., 2010
SIRT3 activity may decrease oxidative damage by increasing mitochondrial NADPH to allow for GR and TrxR reduction of GSH and oxidized Trx, respectively.
“Thus, SIRT3 activity may decrease oxidative damage by increasing mitochondrial NADPH to allow for GR and TrxR reduction of GSH and oxidized Trx, respectively (394).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [394]
Mitochondrial SIRT3 modulates mitochondrial function, possibly by targeting deacetylation of mitochondrial complex I or other mitochondrial proteins, including ICDH-2, a potential source for NADPH.
“The mitochondrial SIRT3 has been found to modulate mitochondrial function, possibly by targeting the deacetylation of mitochondrial complex I or other mitochondrial proteins, including ICDH-2, a potential source for NADPH (6, 389, 394).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [394]
SIRT3 has been suggested to mediate some longevity benefits of calorie restriction through targeting and deacetylation of mitochondrial proteins.
“Interestingly, SIRT3 has been suggested to be the mediator of some of the longevity benefits of calorie restriction through its targeting and deacetylation of mitochondrial proteins55.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [55]
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
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413 · see citing works
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587 · see citing works
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388 · see citing works
Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185 · see citing works
Poirier, P., Giles, T. D., Bray, G. A., Hong, Y., Stern, J. S., Pi-Sunyer, F. X., & Eckel, R. H. (2006) · Circulation · doi:10.1161/circulationaha.106.171016 · Cited by 3,165 · see citing works
Oxidative Stress, Caloric Restriction, and Aging
Sohal, R. S., & Weindruch, R. H. (1996) · Science · doi:10.1126/science.273.5271.59 · Cited by 3,133 · see citing works
Caloric Restriction Delays Disease Onset and Mortality in Rhesus Monkeys
Colman, R. J., Anderson, R. M., Johnson, S. C., Kastman, E. K., Kosmatka, K. J., Beasley, T. M., Allison, D. B., Cruzen, C., Simmons, H. A., Kemnitz, J. W., et al. (2009) · Science · doi:10.1126/science.1173635 · Cited by 2,277 · see citing works
Rahman, I., Kode, A., & Biswas, S. K. (2006) · Nature Protocols · doi:10.1038/nprot.2006.378 · Cited by 2,262 · 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
Regulation of cellular metabolism by protein lysine acetylation
Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., et al. (2010) · Science · doi:10.1126/science.1179689 · Cited by 1,910 · see citing works
Self-citationLin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724 · see citing works
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687 · see citing works
Apoptosis in neurodegenerative disorders
Mattson, M. P. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35040009 · Cited by 1,605 · see citing works
Recent progress in the biology and physiology of sirtuins
Finkel, T., Deng, C., & Mostoslavsky, R. (2009) · Nature · doi:10.1038/nature08197 · Cited by 1,484 · see citing works
The retardation of aging and disease by dietary restriction
(1989) · Choice Reviews Online · doi:10.5860/choice.26-5101 · Cited by 1,477 · see citing works
A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291 · see citing works
Sundaresan, N. R., Gupta, M., Gene, K., Rajamohan, S. B., Isbatan, A., & Gupta, M. P. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39162 · Cited by 996 · see citing works
Mitochondrial Glutathione, a Key Survival Antioxidant
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 986 · see citing works
Lei, Q., Zhang, H., Zhao, B., Zha, Z., Bai, F., Pei, X., Zhao, S., Xiong, Y., & Guan, K. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01874-07 · Cited by 925 · see citing works
Glutathione: an overview of biosynthesis and modulation
Anderson, M. E. (1998) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(97)00146-4 · Cited by 917 · see citing works
Free radicals in biology and medicine
Lucy, J. A. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80903-0 · Cited by 908 · see citing works
Assessment of hearing in 80 inbred strains of mice by ABR threshold analyses
Zheng, Q. Y., Johnson, K. R., & Erway, L. C. (1999) · Hearing Research · doi:10.1016/s0378-5955(99)00003-9 · Cited by 832 · see citing works
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works
Self-citationDoes oxidative damage to DNA increase with age?
Hamilton, M. L., Van Remmen, H., Drake, J. A., Yang, H., Guo, Z. M., Kewitt, K., Walter, C. A., & Richardson, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171202698 · Cited by 768 · see citing works
Obesity and Cardiovascular Disease
Poirier, P., Giles, T. D., Bray, G. A., Hong, Y., Stern, J. S., Pi-Sunyer, X., & Eckel, R. H. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000216787.85457.f3 · Cited by 726 · see citing works
SIRT1 transgenic mice show phenotypes resembling calorie restriction
Bordone, L., Cohen, D., Robinson, A., Motta, M. C., Van Veen, E., Czopik, A., Steele, A. D., Crowe, H., Marmor, S., Luo, J., et al. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00335.x · Cited by 722 · see citing works
Caloric restriction and aging: an update
Masoro, E. J. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00084-x · Cited by 615 · see citing works
Barger, J. L., Kayo, T., Vann, J. M., Arias, E. B., Wang, J., Hacker, T. A., Wang, Y., Raederstorff, D., Morrow, J. D., Leeuwenburgh, C., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002264 · Cited by 580 · see citing works
Self-citationTissue-specific regulation of SIRT1 by calorie restriction
Chen, D., Bruno, J., Easlon, E., Lin, S.-J., Cheng, H.-L., Alt, F. W., & Guarente, L. (2008) · Genes & Development · doi:10.1101/gad.1650608 · Cited by 567 · see citing works
Sundaresan, N. R., Samant, S. A., Pillai, V. B., Rajamohan, S. B., & Gupta, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00426-08 · Cited by 542 · see citing works
Jo, S.-H., Son, M.-K., Koh, H.-J., Lee, S.-M., Song, I.-H., Kim, Y.-O., Lee, Y.-S., Jeong, K.-S., Kim, W. B., Park, J.-W., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010120200 · Cited by 536 · see citing works
Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
Schlicker, C., Gertz, M., Papatheodorou, P., Kachholz, B., Becker, C. F. W., & Steegborn, C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.048 · Cited by 531 · see citing works
Noben‐Trauth, K., Zheng, Q. Y., & Johnson, K. R. (2003) · Nature Genetics · doi:10.1038/ng1226 · Cited by 482 · see citing works
How does calorie restriction work?Preprint
Koubova, J., & Guarente, L. (2003) · Genes & Development · doi:10.1101/gad.1052903 · Cited by 457 · see citing works
Lee, I.-M. M. (1993) · JAMA · doi:10.1001/jama.1993.03510230061036 · Cited by 430 · see citing works
Increase in Activity During Calorie Restriction Requires Sirt1
Chen, D., Steele, A. D., Lindquist, S., & Guarente, L. (2005) · Science · doi:10.1126/science.1118357 · Cited by 419 · see citing works
Paeratakul, S., Lovejoy, J., Ryan, D. H., & Bray, G. A. (2002) · International Journal of Obesity · doi:10.1038/sj.ijo.0802026 · Cited by 385 · see citing works
Age-related hearing loss in C57BL/6J mice is mediated by Bak-dependent mitochondrial apoptosis
Someya, S., Xu, J., Kondo, K., Ding, D., Salvi, R., Yamasoba, T., Rabinovitch, P. S., Weindruch, R. H., Leeuwenburgh, C., Tanokura, M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908786106 · Cited by 332 · see citing works
Self-citationXz, L., & Yan, D. (2007) · The Journal of Pathology · doi:10.1002/path.2102 · Cited by 327 · see citing works
Aging and disease: connections to sirtuins
Dönmez, G., & Guarente, L. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00548.x · Cited by 312 · see citing works
Calorie restriction alters mitochondrial protein acetylation
Schwer, B., Eckersdorff, M., Li, Y., Silva, J. C., Fermin, D., Kurtev, M. V., Giallourakis, C., Comb, M. J., Alt, F. W., & Lombard, D. B. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00503.x · Cited by 259 · cited 1× · see citing works
“A recent study has shown that CR increases Sirt3 levels in liver mitochondria (Schwer et al., 2009).”
BackgroundEffects of age and caloric restriction on glutathione redox state in mice
Rebrin, I., Kamzalov, S., & Sohal, R. S. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00388-5 · Cited by 243 · see citing works
Ohlemiller, K. K., McFadden, S. L., Ding, D., Flood, D. G., Reaume, A. G., Hoffman, E. K., Scott, R. W., Wright, J. S., Putcha, G. V., & Salvi, R. (1999) · Audiology and Neurotology · doi:10.1159/000013847 · Cited by 215 · see citing works
Oxidative imbalance in the aging inner ear
Jiang, H., Talaska, A. E., Schacht, J., & Sha, S. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.025 · Cited by 195 · see citing works
Pro-oxidant shift in glutathione redox state during aging
Rebrin, I., & Sohal, R. S. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2008.06.001 · Cited by 194 · see citing works
Age-related cochlear hair cell loss is enhanced in mice lacking copper/zinc superoxide dismutase
McFadden, S. L., Ding, D., Reaume, A. G., Flood, D. G., & Salvi, R. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00018-4 · Cited by 188 · see citing works
Zerez, C. R., Lee, S. J., & Tanaka, K. R. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90506-9 · Cited by 180 · see citing works
Aging and the auditory brainstem response in mice with severe or minimal presbycusis
Hunter, K. P., & Willott, J. F. (1987) · Hearing Research · doi:10.1016/0378-5955(87)90137-7 · Cited by 179 · see citing works
Controlling caloric consumption: protocols for rodents and rhesus monkeys☆
Pugh, T. D., Klopp, R. G., & Weindruch, R. H. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00043-3 · Cited by 174 · see citing works
A novel sensitive and specific assay for abasic sites, the most commonly produced DNA lesion
Kubo, K., Ide, H., Wallace, S. S., & Kow, Y. W. (1992) · Biochemistry · doi:10.1021/bi00129a020 · Cited by 173 · see citing works
Mitochondrial oxidative damage and apoptosis in age-related hearing loss
Someya, S., & Prolla, T. A. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.04.006 · Cited by 169 · see citing works
Self-citationRetention of oxidized glutathione by isolated rat liver mitochondria during hydroperoxide treatment
Ólafsdóttir, K. B., & Reed, D. J. (1988) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(88)90038-4 · Cited by 169 · see citing works
Zhu, H., Guo, Q., & Mattson, M. P. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01827-2 · Cited by 166 · see citing works
Age-related hearing loss and the ahl locus in mice
Keithley, E. M., Canto, C., Zheng, Q. Y., et al. (2003) · Hearing Research · doi:10.1016/s0378-5955(03)00365-4 · Cited by 154 · see citing works
Hofer, T., Seo, A. Y., Prudencio, M., & Leeuwenburgh, C. (2006) · Biological Chemistry · doi:10.1515/bc.2006.014 · Cited by 144 · see citing works
Self-citationA continuous microplate assay for sirtuins and nicotinamide-producing enzymes
Smith, B. C., Hallows, W. C., & Denu, J. M. (2009) · Analytical Biochemistry · doi:10.1016/j.ab.2009.07.019 · Cited by 141 · see citing works
Self-citationSomeya, S., Yamasoba, T., Weindruch, R. H., Prolla, T. A., & Tanokura, M. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.024 · Cited by 135 · see citing works
Self-citationHereditary Inner-Ear Abnormalities in Animals: Relationships With Human Abnormalities
Steel, K. P., & Bock, G. R. (1983) · Archives of Otolaryngology - Head and Neck Surgery · doi:10.1001/archotol.1983.00800150026005 · Cited by 111 · see citing works
Rebrin, I., Forster, M. J., & Sohal, R. S. (2006) · Brain Research · doi:10.1016/j.brainres.2006.10.040 · Cited by 101 · see citing works
McNeill, D. R., & Wilson, D. M. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0329 · Cited by 97 · see citing works
[117] Isocitric dehydrogenase of yeast (TPN)
Kornberg, A. (1955) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(55)01122-1 · Cited by 89 · see citing works
Aag-initiated base excision repair drives alkylation-induced retinal degeneration in mice
Meira, L. B., Moroski-Erkul, C. A., Green, S. L., Calvo, J. A., Bronson, R. T., Shah, D., & Samson, L. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807030106 · Cited by 89 · see citing works
Johnson, K. R., Yu, H., Ding, D., et al. (2010) · Hearing Research · doi:10.1016/j.heares.2010.05.002 · Cited by 56 · see citing works
Matteo, M. A. D., Loweth, A. C., Thomas, S., Mabley, J. G., Morgan, N. G., Thorpe, J. R., & Green, I. C. (1997) · APOPTOSIS · doi:10.1023/a:1026412414666 · Cited by 54 · see citing works
Sweet, R. J., Price, J. M., & Henry, K. R. (1988) · International Journal of Audiology · doi:10.3109/00206098809081601 · Cited by 37 · see citing works
Mixed conductive and sensorineural hearing loss in LP/J mice
Steel, K. P., Moorjani, P., & Bock, G. R. (1987) · Hearing Research · doi:10.1016/0378-5955(87)90051-7 · Cited by 22 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
López-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 · see citing works
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648 · see citing works
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 · see citing works
NAD <sup>+</sup> in aging, metabolism, and neurodegeneration
Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319 · see citing works
Old, new and emerging functions of caspases
Shalini, S., Dorstyn, L., Dawar, S., & Kumar, S. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.216 · Cited by 1,267 · see citing works
Ketone bodies as signaling metabolites
Newman, J. C., & Verdin, E. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.002 · Cited by 966 · see citing works
Mitochondrial and metabolic dysfunction in ageing and age-related diseases
Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990 · see citing works
β-Hydroxybutyrate: A Signaling Metabolite
Newman, J. C., & Verdin, E. (2017) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064916 · Cited by 872 · see citing works
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 · see citing works
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · see citing works
SIRT3 Opposes Reprogramming of Cancer Cell Metabolism through HIF1α Destabilization
Finley, L. W. S., Carracedo, A., Lee, J., Souza, A., Egia, A., Zhang, J., Teruya-Feldstein, J., Moreira, P. I., Cardoso, S. M., Clish, C. B., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.02.014 · Cited by 782 · see citing works
Molecular mechanisms of dietary restriction promoting health and longevity
Green, C. L., Lamming, D. W., & Fontana, L. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00411-4 · Cited by 714 · see citing works
Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., Carson, J. J., Tonelli, M., Balloon, A. J., Higbee, A. J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.024 · Cited by 636 · see citing works
Self-citationRedox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Mammalian Mitochondria and Aging: An Update
Kauppila, T. E. S., Kauppila, J. H. K., & Larsson, N.-G. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.017 · Cited by 578 · see citing works
The updated biology of hypoxia-inducible factor
Greer, S. N., Metcalf, J. L., Wang, Y., & Ohh, M. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.125 · Cited by 545 · see citing works
Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)
Ristow, M., & Schmeisser, K. (2014) · Dose-Response · doi:10.2203/dose-response.13-035.ristow · Cited by 534 · see citing works
Guarente, L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1100831 · Cited by 510 · see citing works
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 · see citing works
Mitochondrial Sirtuin 3: New emerging biological function and therapeutic target
Zhang, J., Xiang, H., Liu, J., Chen, Y., He, R.-R., & Liu, B. (2020) · Theranostics · doi:10.7150/thno.45922 · Cited by 503 · see citing works
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 · see citing works
“Mammalian SIRT1, SIRT3 and SIRT6 are induced by calorie restriction and exercise, and their genetic ablation prevents many of the health benefits and longevity provided by these interventions (Boily et al., 2008; Chen et al., 2005; Cohen et al., 2004; Hebert et al., 2013; Qiu et al., 2010; Someya et al., 2010).”
BackgroundCalorie restriction and sirtuins revisited
Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464 · see citing works
SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress
Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01483-13 · Cited by 446 · see citing works
Bell, E. L., Emerling, B. M., Ricoult, S. J. H., & Guarente, L. (2011) · Oncogene · doi:10.1038/onc.2011.37 · Cited by 440 · see citing works
SIRT3 Reverses Aging-Associated Degeneration
Brown, K., Xie, S., Qiu, X., Mohrin, M., Shin, J., Liu, Y., Zhang, D., Scadden, D. T., & Chen, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.005 · Cited by 436 · see citing works
Energy intake and exercise as determinants of brain health and vulnerability to injury and disease
Mattson, M. P. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.08.012 · Cited by 434 · see citing works
He, M., Chiang, H.-H., Luo, H., Zheng, Z., Qiao, Q., Wang, L., Tan, M., Ohkubo, R., Mu, W.-C., Zhao, S., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.009 · Cited by 425 · see citing works
Joseph, A., Adhihetty, P. J., Buford, T. W., Wohlgemuth, S. E., Lees, H. A., Nguyen, L. M. ‐., Aranda, J. M., Sandesara, B. D., Pahor, M., Manini, T. M., et al. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00844.x · Cited by 395 · see citing works
Self-citationPicciotto, N. E., Gano, L. B., Johnson, L. C., Martens, C. R., Sindler, A. L., Mills, K. F., Imai, S., & Seals, D. R. (2016) · Aging Cell · doi:10.1111/acel.12461 · Cited by 396 · see citing works
Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
Hallows, W. C., Yu, W., Smith, B. C., Devires, M. K., Ellinger, J. J., Someya, S., Shortreed, M. R., Prolla, T., Markley, J. L., Smith, L. M., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.002 · Cited by 389 · see citing works
Self-citationNuclear DNA damage signalling to mitochondria in ageing
Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387 · see citing works
Sirtuin functions and modulation: from chemistry to the clinic
Carafa, V., Rotili, D., Forgione, M., Cuomo, F., Serretiello, E., Hailu, G. S., Jarho, E., Lahtela-Kakkonen, M., Mai, A., & Altucci, L. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0224-3 · Cited by 387 · see citing works
Cheng, A., Yang, Y., Zhou, Y., Maharana, C., Lu, D., Peng, W., Liu, Y., Wan, R., Marosi, K., Misiak, M., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.10.013 · Cited by 371 · see citing works
Redox control of senescence and age-related disease.
Chandrasekaran, A., Idelchik, M. D. P. S., & Melendez, J. A. (2017) · Redox Biology · doi:10.1016/j.redox.2016.11.005 · Cited by 360 · see citing works
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 · see citing works
Protein acetylation in metabolism – metabolites and cofactors
Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works
Carrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331 · see citing works
The metabolic regulation of aging
Finkel, T. (2015) · Nature Medicine · doi:10.1038/nm.3998 · Cited by 325 · see citing works
SIRT3 regulation of mitochondrial oxidative stress
Bause, A. S., & Haigis, M. C. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2012.08.007 · Cited by 311 · see citing works
Barja, G. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5148 · Cited by 290 · see citing works
Brown, K. D., Maqsood, S., Huang, J.-Y., Pan, Y., Harkcom, W., Li, W., Sauve, A., Verdin, E., & Jaffrey, S. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.003 · Cited by 277 · see citing works
Skeletal muscle insulin resistance: role of mitochondria and other ROS sources
Di Meo, S., Iossa, S., & Venditti, P. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0598 · Cited by 282 · see citing works
Circadian Clocks and Metabolism
Marcheva, B., Ramsey, K. M., Peek, C. B., Affinati, A., Maury, E., & Bass, J. (2013) · Handbook of Experimental Pharmacology · doi:10.1007/978-3-642-25950-0_6 · Cited by 282 · see citing works
The sirtuins, oxidative stress and aging: an emerging link
Merksamer, P. I., Liu, Y., He, W., Hirschey, M. D., Chen, D., & Verdin, E. (2013) · Aging · doi:10.18632/aging.100544 · Cited by 275 · see citing works
NAD metabolism: Implications in aging and longevity
Yaku, K., Okabe, K., & Nakagawa, T. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.05.006 · Cited by 269 · see citing works
Mitochondrial sirtuins: regulators of protein acylation and metabolism
He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262 · see citing works
Sirtuin catalysis and regulation
Feldman, J. L., Dittenhafer-Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.378877 · Cited by 248 · see citing works
Self-citationAging Hallmarks: The Benefits of Physical Exercise
Rebelo-Marques, A., De Sousa Lages, A., Andrade, R., Ribeiro, C. F., Mota-Pinto, A., Carrilho, F., & Espregueira-Mendes, J. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00258 · Cited by 246 · see citing works
Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes
Cantó, C., Sauve, A. A., & Bai, P. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.004 · Cited by 246 · see citing works
Yang, Q., Liang, X., Sun, X., Zhang, L., Fu, X., Rogers, C. J., Berim, A., Zhang, S., Wang, S., Wang, B., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.010 · Cited by 237 · see citing works
The Pharmacology of CD38/NADase: An Emerging Target in Cancer and Diseases of Aging
Chini, E. N., Chini, C. C. S., Espindola Netto, J. M., de Oliveira, G. C., & van Schooten, W. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.02.001 · Cited by 227 · see citing works
SIRT3 regulates progression and development of diseases of aging
McDonnell, E., Peterson, B. S., Bomze, H. M., & Hirschey, M. D. (2015) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2015.06.001 · Cited by 217 · see citing works
Scott, I., Webster, B. R., Li, J. H., & Sack, M. N. (2012) · Biochemical Journal · doi:10.1042/bj20120118 · Cited by 214 · see citing works
SIRT3 deregulation is linked to mitochondrial dysfunction in Alzheimer's disease
Lee, J., Kim, Y., Liu, T., Hwang, Y. J., Hyeon, S. J., Im, H., Lee, K., Alvarez, V. E., McKee, A. C., Um, S., et al. (2018) · Aging Cell · doi:10.1111/acel.12679 · Cited by 213 · see citing works
NAD and the aging process: role in life, death and everything in between
Chini, C. C. S., Tarragó, M. G., & Chini, E. N. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.11.003 · Cited by 208 · see citing works
Protective effects and mechanisms of sirtuins in the nervous system
Zhang, F., Wang, S., Gan, L., Vosler, P. S., Gao, Y., Zigmond, M. J., & Chen, J. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.09.001 · Cited by 211 · see citing works
Cheng, Y., Ren, X., Gowda, A. S., Shan, Y., Zhang, L., Yuan, Y.-S., Patel, R., Wu, H., Huber-Keener, K., Yang, J. W., et al. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.254 · Cited by 205 · see citing works
Molecular Mechanisms and Genetics of Oxidative Stress in Alzheimer’s Disease
Cioffi, F., Adam, R. H. I., & Broersen, K. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190863 · Cited by 204 · see citing works
“A study involving 74 human subjects demonstrated that GSH levels of autopsied brains did not significantly decrease with aging [128].”
BackgroundInfluentialTao, R., Vassilopoulos, A., Parisiadou, L., Yan, Y., & Gius, D. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5482 · Cited by 194 · see citing works
NAD <sup>+</sup> metabolism: A therapeutic target for age-related metabolic disease
Mouchiroud, L., Houtkooper, R. H., & Auwerx, J. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.789479 · Cited by 193 · see citing works
“…in oxidative phosphorylation (Ahn et al., 2008), fatty acid oxidation (Hirschey et al., 2010), ketogenesis (Shimazu et al., 2010), oxidative stress (Someya et al., 2010), glutamate metabolism (Haigis et al., 2006), urea cycle (Nakagawa et al., 2009), as well as several other mitochondrial…”
BackgroundSirt3 promotes antimycobacterial defenses by coordinating mitochondrial and autophagic functions
Kim, T. S., Jin, Y. B., Kim, Y. S., Kim, S., Kim, J. K., Lee, H.-M., Suh, H.-W., Choe, J. H., Kim, Y. J., Koo, B.-S., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1582743 · Cited by 172 · see citing works
SIRT3 regulates mitochondrial protein acetylation and intermediary metabolism
Hirschey, M. D., Shimazu, T., Huang, J. Y., Schwer, B., & Verdin, E. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010850 · Cited by 180 · see citing works
The effects of dietary restriction on oxidative stress in rodents
Walsh, M. E., Shi, Y., & Van Remmen, H. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.037 · Cited by 181 · see citing works
Cytoplasmic and Mitochondrial NADPH-Coupled Redox Systems in the Regulation of Aging
Bradshaw, P. C. (2019) · Nutrients · doi:10.3390/nu11030504 · Cited by 178 · see citing works
Extended wakefulness: compromised metabolics in and degeneration of locus ceruleus neurons
Zhang, J., Zhu, Y., Zhan, G., Fenik, P., Panossian, L., Wang, M. M., Reid, S., Lai, D., Davis, J. G., Baur, J. A., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.5025-12.2014 · Cited by 171 · see citing works
Santos, A. L., Sinha, S., & Lindner, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1941285 · Cited by 168 · see citing works
Karnewar, S., Neeli, P. K., Panuganti, D., Kotagiri, S., Mallappa, S., Jain, N., Jerald, M. K., & Kotamraju, S. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.01.018 · Cited by 161 · see citing works
Signaling networks determining life span
Riera, C. E., Merkwirth, C., De Magalhaes Filho, C. D., & Dillin, A. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014451 · Cited by 161 · see citing works
Turn up the power - pharmacological activation of mitochondrial biogenesis in mouse models
Komen, J. C., & Thorburn, D. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12413 · Cited by 149 · see citing works
Fernandez-Marcos, P. J., Jeninga, E. H., Canto, C., Harach, T., de Boer, V. C. J., Andreux, P., Moullan, N., Pirinen, E., Yamamoto, H., Houten, S. M., et al. (2012) · Scientific Reports · doi:10.1038/srep00425 · Cited by 137 · see citing works
Tian, G., Sawashita, J., Kubo, H., Nishio, S.-Y., Hashimoto, S., Suzuki, N., Yoshimura, H., Tsuruoka, M., Wang, Y., Liu, Y., et al. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5406 · Cited by 123 · see citing works
Gräff, J., Kahn, M., Samiei, A., Gao, J., Ota, K. T., Rei, D., & Tsai, L.-H. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.5657-12.2013 · Cited by 124 · see citing works
Fritz, K. S., Galligan, J. J., Hirschey, M. D., Verdin, E., & Petersen, D. R. (2012) · Journal of Proteome Research · doi:10.1021/pr2008384 · Cited by 121 · see citing works
NAD+ flux is maintained in aged mice despite lower tissue concentrations
McReynolds, M. R., Chellappa, K., Chiles, E., Jankowski, C., Shen, Y., Chen, L., Descamps, H. C., Mukherjee, S., Bhat, Y. R., Lingala, S. R., et al. (2021) · Cell Systems · doi:10.1016/j.cels.2021.09.001 · Cited by 112 · see citing works
<i>Drosophila</i> Sirt2/mammalian SIRT3 deacetylates ATP synthase β and regulates complex V activity
Rahman, M., Nirala, N. K., Singh, A., Zhu, L. J., Taguchi, K., Bamba, T., Fukusaki, E., Shaw, L. M., Lambright, D. G., Acharya, J. K., et al. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201404118 · Cited by 116 · see citing works
Tseng, A. H.-H., Wu, L.-H., Shieh, S.-S., & Wang, D. L. (2014) · Biochemical Journal · doi:10.1042/bj20140213 · Cited by 114 · see citing works
Geisler, J. G. (2019) · Cells · doi:10.3390/cells8030280 · Cited by 104 · see citing works
Harlan, B. A., Pehar, M., Sharma, D. R., Beeson, G., Beeson, C. C., & Vargas, M. R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.698779 · Cited by 94 · see citing works
Huo, J., Xu, Z., Hosoe, K., Kubo, H., Miyahara, H., Dai, J., Mori, M., Sawashita, J., & Higuchi, K. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/3181759 · Cited by 87 · see citing works
Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism
Pougovkina, O., te Brinke, H., Wanders, R. J. A., Houten, S. M., & de Boer, V. C. J. (2014) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-014-9684-9 · Cited by 80 · see citing works
Decreased sirtuin deacetylase activity in LRRK2 G2019S iPSC-derived dopaminergic neurons
Schwab, A. J., Sison, S. L., Meade, M. R., Broniowska, K. A., Corbett, J. A., & Ebert, A. D. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.10.010 · Cited by 80 · see citing works
Regulation of skeletal muscle oxidative capacity and muscle mass by SIRT3
Lin, L., Chen, K., Khalek, W. A., Ward, J. L., Yang, H., Chabi, B., Wrutniak-Cabello, C., & Tong, Q. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085636 · Cited by 67 · see citing works
Sirt3 deficiency accelerates ovarian senescence without affecting spermatogenesis in aging mice
Zhu, J., Yang, Q., Li, H., Wang, Y., Jiang, Y., Wang, H., Cong, L., Xu, J., Shen, Z., Chen, W., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.10.324 · Cited by 64 · see citing works
Self-citationWan, X., Wang, C., Huang, Z., Zhou, D., Xiang, S., Qi, Q., Chen, X., Arbely, E., Liu, C.-Y., Du, P., et al. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-02825-y · Cited by 60 · see citing works
Self-citationInflammatory signaling in NASH driven by hepatocyte mitochondrial dysfunctions
Myint, M., Oppedisano, F., De Giorgi, V., Kim, B.-M., Marincola, F. M., Alter, H. J., & Nesci, S. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04627-0 · Cited by 61 · see citing works
Lloret, A., & Beal, M. F. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02809-1 · Cited by 52 · see citing works
Is sleep disruption a risk factor for Alzheimer's disease?
Macedo, A. C., Balouch, S., & Tabet, N. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-161287 · Cited by 49 · see citing works
Evidence supporting a mechanistic role of sirtuins in mood and metabolic disorders
Alageel, A., Tomasi, J., Tersigni, C., Brietzke, E., Zuckerman, H., Subramaniapillai, M., Lee, Y., Iacobucci, M., Rosenblat, J. D., Mansur, R. B., et al. (2018) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2018.05.017 · Cited by 45 · see citing works
Facts and controversies in our understanding of how caloric restriction impacts the mitochondrion
Gouspillou, G., & Hepple, R. T. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.03.004 · Cited by 42 · see citing works
Metabolic reprogramming: a bridge between aging and tumorigenesis
Drapela, S., Ilter, D., & Gomes, A. P. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13261 · Cited by 41 · see citing works
Role of SIRT3 in Angiotensin II-induced human umbilical vein endothelial cells dysfunction
Liu, H., Chen, T., Li, N., Wang, S., & Bu, P. (2015) · BMC Cardiovascular Disorders · doi:10.1186/s12872-015-0075-4 · Cited by 36 · see citing works
Botchway, B. O., Okoye, F. C., Chen, Y., Arthur, W. E., & Fang, M. (2022) · Aging and disease · doi:10.14336/ad.2021.0616 · Cited by 32 · see citing works
Could sirtuin activities modify ALS onset and progression?
Tang, B. L. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0452-2 · Cited by 24 · see citing works
The Role of Sirtuins in Sarcopenia and Frailty
Anwar, M., Pradhan, R., Dey, S., & Kumar, R. (2023) · Aging and disease · doi:10.14336/ad.2022.0622 · Cited by 19 · see citing works
- Authors
- Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A.
- Affiliations
- University of Wisconsin–Madison (US)
- University of Florida (US)
- The University of Tokyo (JP)
- Corresponding author
- Denu, John M.
- Prolla, Tomas A.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-11
- Volume
- 143
- Issue
- 5
- Pages
- 802-812
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3018849
- OpenAlex
- W2101580126
- Cited by
- 1,150
- References
- 68
- Citations by year
- 2026: 40 · 2025: 58 · 2024: 39 · 2023: 41 · 2022: 82 · 2021: 94 · 2020: 83 · 2019: 72 · 2018: 84 · 2017: 83 · 2016: 86 · 2015: 85 · 2014: 83 · 2013: 99 · 2012: 62
- FWCI
- 27.82
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 989 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (R01AG021905, AG021905, P30AG028740)
- National Institute of General Medical Sciences (GM-065386, R01GM065386)
- 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 › Mitochondrial Function and Pathology
- Keywords
- SIRT3, caloric restriction, age-related hearing loss, oxidative stress, oxidative DNA damage, IDH2, NADPH, glutathione, sirtuins, aging
- MeSH terms
- Aging, Animals, Antioxidants, DNA Damage, Female, Glutathione, Isocitrate Dehydrogenase, Male, Mice, Inbred C57BL, Mitochondria, Oxidative Stress, Caloric Restriction, Hearing Loss, Mice, Sirtuin 3
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
