The DOI matches its Crossref record; 34 of the 35 references it cites were found in a registry or an index.
SIRT3 Is a Mitochondria-Localized Tumor Suppressor Required for Maintenance of Mitochondrial Integrity and Metabolism during Stress
Open accessAbstract
The sirtuin gene family (SIRT) is hypothesized to regulate the aging process and play a role in cellular repair. This work demonstrates that SIRT3(-/-) mouse embryonic fibroblasts (MEFs) exhibit abnormal mitochondrial physiology as well as increases in stress-induced superoxide levels and genomic instability. Expression of a single oncogene (Myc or Ras) in SIRT3(-/-) MEFs results in in vitro transformation and altered intracellular metabolism. Superoxide dismutase prevents transformation by a single oncogene in SIRT3(-/-) MEFs and reverses the tumor-permissive phenotype as well as stress-induced genomic instability. In addition, SIRT3(-/-) mice develop ER/PR-positive mammary tumors. Finally, human breast and other human cancer specimens exhibit reduced SIRT3 levels. These results identify SIRT3 as a genomically expressed, mitochondria-localized tumor suppressor.
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
“Our finding that loss of SIRT3 loss drives senescence appears to contradict a report in which cells from SIRT3 knockout mice were highly susceptible to oncogenic transformation; however, this susceptibility depended on the elevated ROS characteristic of sirt3−/− cells (Kim et al., 2010).”
From Mitochondrial Dysfunction Induces Senescence with a Distinct Secretory Phenotype (2016) · cites this paper as Kim et al., 2010
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“the genes encoding SIRT3 and SIRT6 are tumor suppressors”
From Influence of Metabolism on Epigenetics and Disease (2013) · cites this paper as Kim et al., 2010
Experimental — accuracy not yet measuredIn the citing paper
“SIRT3 has been reported as pro-apoptotic ((Allison and Milner 2007)) and SIRT3 loss is associated with a tumor-permissive environment via the inhibition of ROS production ((Kim et al. 2010);(Bell et al. 2011);(Finley et al. 2011)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Kim et al. 2010
In the citing paper
“Specifically, SirT3 deficiency alone is sufficient for the transformation of primary MEFs with Myc and/or RAS to from tumors in xenograft models.”
From SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production (2011) · cites this paper as Kim et al., 2010
In the citing paper
“Kim and colleagues also demonstrated that SirT3−/− Myc/Ras MEFs exhibit increased glycolysis, decreased oxidative phosphorylation and increased ROS.”
From SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production (2011) · cites this paper as Kim et al., 2010
In the citing paper
“Recently SirT3 was described to act as a mitochondrial localized tumor suppressor (Kim et al., 2010).”
From SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production (2011) · cites this paper as Kim et al., 2010
In the citing paper
“Previously, SirT3 has been demonstrated to act as a tumor suppressor by negatively regulating MnSOD/ROS-mediated genomic instability (Kim et al., 2010).”
From SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production (2011) · cites this paper as Kim et al., 2010
In the citing paper
“Another member of the sirtuin family, SIRT3, is critical to the maintenance of mitochondria and metabolism and controls ROS production during HSC aging29.”
From Stem cell aging: mechanisms, regulators and therapeutic opportunities (2014) · cites this paper as [29]
In the citing paper
“Likewise, mitochondrial function, largely regulated by sirtuins, not only affects stem cell functions directly but also causes secondary effects on ROS and nutrient-sensing activities, which further modulate stem cell phenotypes29,30,108,113,184.”
From Stem cell aging: mechanisms, regulators and therapeutic opportunities (2014) · cites this paper as [29]
In the citing paper
“Recent work demonstrates that mitochondrial ROS directly contribute to cellular transformation induced by either Ras or Myc overexpression.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [72]
In the citing paper
“Moreover, Sirt3−/− murine fibroblasts display increased levels of mitochondrial ROS accumulation (compared to wild-type cells) when either Myc or Ras oncogenes are expressed.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [72]
In the citing paper
“The NAD-dependent deacetylase sirtuin 3 (SIRT3) acts as a tumor suppressor through its regulation of FOXO activity and ROS maintenance 72.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [72]
In the citing paper
“This ROS accumulation is associated with decreased flux through mitochondrial complexes I and III (possibly allowing for increased escape of electrons to O2), and reduced cellular levels of SOD2 72.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [72]
In the citing paper
“Expression of SOD2 inhibited this oncogene-mediated transformation of Sirt3−/− cells, suggesting that mitochondrial ROS play an important role in the Sirt3−/− phenotype.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [72]
In the citing paper
“These finding are consistent with observations in Sod2−/− fibroblasts, which like their Sirt3−/− counterparts, are capable of transformation with single oncogenes 72.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [72]
In the citing paper
“Sirt3−/− cells become transformed after expression of either Myc or Ras, whereas wild-type cells require expression of both oncogenes.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [72]
In the citing paper
“SIRT3 deacetylates FOXO3a, promoting its nuclear localization and transcriptional activation 40, 72.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [72]
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
Warburg, O. (1956) · Science · doi:10.1126/science.123.3191.309 · Cited by 13,425
Mutation and cancer: statistical study of retinoblastoma
Knudson, A. G. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.4.820 · Cited by 7,612
Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,218 · cited 2×
“It has been previously shown that overexpression of Myc in primary cells results in massive programmed cell death, whereas overexpression of Ras induces premature senescence (Sebastian et al., 2005; Serrano et al., 1997).”
BackgroundCancer cell metabolism: warburg and beyond
Hsu, P. P., & Sabatini, D. M. (2008) · Cell · doi:10.1016/j.cell.2008.08.021 · Cited by 2,452 · cited 2×
“Mitochondrial abnormalities associated with altered oxidative metabolism are observed in tumor cells in vitro and in vivo and appear to contribute to a chronic condition of oxidative stress (Hsu and Sabatini, 2008).”
BackgroundRhodes, D. R., Sundaram, S. K., Mahavisno, V., Varambally, R., Yu, J., Briggs, B., Barrette, T. R., Anstett, M. J., Kincead-Beal, C., Kulkarni, P., et al. (2007) · Neoplasia · doi:10.1593/neo.07112 · Cited by 2,057
Sotiriou, C. P., Wirapati, P., Loi, S., Harris, A. L., Fox, S., Smeds, J., Nordgren, H., Farmer, P. J., Praz, V., Haibe‐Kains, B., et al. (2006) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djj052 · Cited by 2,050
Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,603
Recent progress in the biology and physiology of sirtuins
Finkel, T., Deng, C., & Mostoslavsky, R. (2009) · Nature · doi:10.1038/nature08197 · Cited by 1,506
Self-citationSir2 mediates longevity in the fly through a pathway related to calorie restriction
Rogina, B., & Helfand, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404184101 · Cited by 1,361
Genetic pathways that regulate ageing in model organisms
Guarente, L., & Kenyon, C. J. (2000) · Nature · doi:10.1038/35041700 · Cited by 1,337
Cited by
Sorted by citations
The role of ROS in tumour development and progression
Cheung, E. C., & Vousden, K. H. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-021-00435-0 · Cited by 1,663
Oxidative stress and cancer: An overview
Iglesias, V. S., Moliné, T., Somoza, R., Paciucci, R., Kondoh, H., & LLeonart, M. E. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.10.004 · Cited by 1,488
Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310
Mitochondrial Dysfunction Induces Senescence with a Distinct Secretory Phenotype
Wiley, C. D., Velarde, M. C., Lecot, P., Liu, S., Sarnoski, E. A., Freund, A., Shirakawa, K., Lim, H. W., Davis, S. S., Ramanathan, A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.11.011 · Cited by 1,275
“Our finding that loss of SIRT3 loss drives senescence appears to contradict a report in which cells from SIRT3 knockout mice were highly susceptible to oncogenic transformation; however, this susceptibility depended on the elevated ROS characteristic of sirt3 / cells (Kim et al., 2010).”
BackgroundSIRT1 and other sirtuins in metabolism
Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,157
NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
Xie, N., Zhang, L., Gao, W. Q., Huang, C., Huber, P., Zhou, X., Li, C. L., Shen, G., & Zou, B. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00311-7 · Cited by 1,147
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011
Influence of Metabolism on Epigenetics and Disease
Kaelin, W. G., & McKnight, S. L. (2013) · Cell · doi:10.1016/j.cell.2013.03.004 · Cited by 920
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
Self-citationReactive oxygen species and cancer paradox: To promote or to suppress?
Galadari, S., Rahman, A. U., Pallichankandy, S., & Thayyullathil, F. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.004 · Cited by 918
Stem cell aging: mechanisms, regulators and therapeutic opportunities
Oh, J., Lee, Y. D., & Wagers, A. J. (2014) · Nature Medicine · doi:10.1038/nm.3651 · Cited by 796
Transcriptional integration of mitochondrial biogenesis
Scarpulla, R. C., Vega, R. B., & Kelly, D. P. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.06.006 · Cited by 798
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
“, 2008), and increased reactive oxygen species (Kim et al., 2010; Qiu et al., 2010; Someya et al., 2010; Tao et al., 2010).”
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
Sirtuin 1 and Sirtuin 3: Physiological Modulators of Metabolism
Nogueiras, R., Habegger, K. M., Chaudhary, N., Finan, B., Banks, A. S., Dietrich, M. O., Horváth, T. L., Sinclair, D. A., Pfluger, P. T., & Tschöp, M. H. (2012) · Physiological Reviews · doi:10.1152/physrev.00022.2011 · Cited by 724
Oxidative Stress in Cancer Cell Metabolism
Arfin, S., Jha, N. K., Jha, S. K., Kesari, K. K., Ruokolainen, J., Roychoudhury, S., Rathi, B., & Kumar, D. (2021) · Antioxidants · doi:10.3390/antiox10050642 · Cited by 721
Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling
Verdin, E., Hirschey, M. D., Finley, L. W. S., & Haigis, M. C. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.003 · Cited by 661
The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism
Sebastián, C., Zwaans, B. M. M., Silberman, D. M., Gymrek, M., Goren, A., Zhong, L., Ram, O., Truelove, J., Guimaraes, A. R., Toiber, D., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.047 · Cited by 660
Metabolic control of cell death
Green, D. R., Galluzzi, L., & Kroemer, G. (2014) · Science · doi:10.1126/science.1250256 · Cited by 678
The NAD metabolome — a key determinant of cancer cell biology
Chiarugi, A., Dölle, C., Felici, R., & Ziegler, M. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3340 · Cited by 660
Mitochondria-Ros Crosstalk in the Control of Cell Death and Aging
Marchi, S., Giorgi, C., Suski, J. M., Agnoletto, C., Bononi, A., Bonora, M., Marchi, E. D., Missiroli, S., Patergnani, S., Poletti, F., et al. (2011) · Journal of Signal Transduction · doi:10.1155/2012/329635 · Cited by 658
The mTORC1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4
Csibi, A., Fendt, S.-M., Li, C., Poulogiannis, G., Choo, A. Y., Chapski, D. J., Jeong, S. M., Dempsey, J. M., Parkhitko, A., Morrison, T., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.023 · Cited by 586
The Two Faces of Reactive Oxygen Species in Cancer
Reczek, C. R., & Chandel, N. S. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041916-065808 · Cited by 602
“In the absence of SIRT3, SOD2 activity is decreased, resulting in ROS accumulation, HIF-1α protein stabilization, and tumorigenesis (Bell et al. 2011, Finley et al. 2011, Kim et al. 2010, Tao et al. 2010).”
BackgroundTumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
Chen, Y., Zhang, J., Lin, Y., Lei, Q., Guan, K., Zhao, S., & Xiong, Y. (2011) · The EMBO Reports · doi:10.1038/embor.2011.65 · Cited by 572
Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C., Palmeira, C. M., Rosenzweig, A., & Sinclair, D. A. (2010) · Aging · doi:10.18632/aging.100252 · Cited by 554
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
SIRT2 Maintains Genome Integrity and Suppresses Tumorigenesis through Regulating APC/C Activity
Kim, H., Vassilopoulos, A., Wang, R.-H., Lahusen, T. J., Xiao, Z., Xu, X., Li, C., Veenstra, T. D., Li, B., Yu, H., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.004 · Cited by 536
Self-citationMitohormesis: 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
(2010) · doi:10.1016/j.cmet.2010.06.009 · Cited by 512
Self-citationGuarente, L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1100831 · Cited by 510
The multifaceted functions of sirtuins in cancer
Chalkiadaki, A., & Guarente, L. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3985 · Cited by 513
Zhang, S., Weinberg, S., DeBerge, M., Gainullina, A., Schipma, M., Kinchen, J. M., Ben-Sahra, I., Gius, D. R., Yvan-Charvet, L., Chandel, N. S., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2018.12.004 · Cited by 485
Self-citationSIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage
Tseng, A. H.-H., Shieh, S.-S., & Wang, D. L. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.002 · Cited by 458
Tumor glycolysis, an essential sweet tooth of tumor cells
Paul, S., Ghosh, S., & Kumar, S. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.09.007 · Cited by 449
Jeong, S. M., Xiao, C., Finley, L. W. S., Lahusen, T., Souza, A. L., Pierce, K., Li, Y.-H., Wang, X., Laurent, G., German, N. J., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.024 · Cited by 445
Self-citationHistone deacetylases and cancer
Barneda‐Zahonero, B., & Parra, M. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.07.003 · Cited by 449
Yu, W., Dittenhafer‐Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355206 · Cited by 452
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
Bell, E. L., Emerling, B. M., Ricoult, S. J. H., & Guarente, L. (2011) · Oncogene · doi:10.1038/onc.2011.37 · Cited by 440
Role of Cardiolipin in Mitochondrial Signaling Pathways
Dudek, J. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00090 · Cited by 444
Metabolic control of epigenetics in cancer
Kinnaird, A. S., Zhao, S., Wellen, K. E., & Michelakis, E. D. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.82 · Cited by 429
Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K., & Zhao, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.028 · Cited by 424
Fatty liver is associated with reduced SIRT3 activity and mitochondrial protein hyperacetylation
Kendrick, A. A., Choudhury, M., Rahman, S. M., McCurdy, C. E., Friederich, M., Van Hove, J. L. K., Watson, P. A., Birdsey, N., Bao, J., Gius, D., et al. (2011) · Biochemical Journal · doi:10.1042/bj20100791 · Cited by 382
Self-citationSeven sirtuins for seven deadly diseases ofaging
Morris, B. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.525 · Cited by 386
Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
Ali, I., Conrad, R. J., Verdin, E. M., & Ott, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00181 · Cited by 375
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
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
Manganese Superoxide Dismutase: Guardian of the Powerhouse
Holley, A. K., Bakthavatchalu, V., Velez-Roman, J. M., & St. Clair, D. K. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12107114 · Cited by 358
Sirtuins mediate mammalian metabolic responses to nutrient availability
Chalkiadaki, A., & Guarente, L. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.225 · Cited by 344
Effects of Oxidative Stress on Mesenchymal Stem Cell Biology
Denu, R. A., & Hematti, P. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2989076 · Cited by 338
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
The Dual Role of Sirtuins in Cancer
Bosch‐Presegué, L., & Vaquero, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417862 · Cited by 337
Chen, J., & Russo, J. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.06.004 · Cited by 340
Wang, R.-H., Kim, H., Xiao, C., Xu, X., Gavrilova, O., & Deng, C. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46243 · Cited by 315
Self-citationForever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration
Kincaid, B., & Bossy‐Wetzel, E. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00048 · Cited by 317
Fan, J., Shan, C., Kang, H.-B., Elf, S., Xie, J., Tucker, M., Gu, T.-L., Aguiar, M., Lonning, S., Chen, H., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.026 · Cited by 305
Mitochondrial Sirtuins and Molecular Mechanisms of Aging
van de Ven, R. A. H., Santos, D., & Haigis, M. C. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.02.005 · Cited by 312
Dysregulated metabolism contributes to oncogenesis
Hirschey, M. D., DeBerardinis, R. J., Diehl, A. M., Drew, J. E., Frezza, C., Green, M. F., Jones, L. W., Ko, Y. H., Le, A., Lea, M. A., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.10.002 · Cited by 316
Ansari, A., Rahman, M. S., Saha, S. K., Saikot, F. K., Deep, A., & Kim, K. (2016) · Aging Cell · doi:10.1111/acel.12538 · Cited by 315
Role of mitochondrial dysfunction in cancer progression
Hsu, C., Tseng, L., & Lee, H. (2016) · Experimental Biology and Medicine · doi:10.1177/1535370216641787 · Cited by 320
Mitochondrial ROS control of cancer
Idelchik, M. D. P. S., Begley, U., Begley, T. J., & Melendez, J. A. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.04.005 · Cited by 313
Tatone, C., Emidio, G. D., Barbonetti, A., Carta, G., Luciano, A. M., Falone, S., & Amicarelli, F. (2018) · Human Reproduction Update · doi:10.1093/humupd/dmy003 · Cited by 296
Sirtuins: guardians of mammalian healthspan
Giblin, W., Skinner, M. E., & Lombard, D. B. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.04.007 · Cited by 286
Energy metabolism in adult neural stem cell fate
Rafalski, V. A., & Brunet, A. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.10.007 · Cited by 294
SirT3 Regulates the Mitochondrial Unfolded Protein Response
Papa, L., & Germain, D. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01337-13 · Cited by 292
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
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
SIRT3‐dependent delactylation of cyclin E2 prevents hepatocellular carcinoma growth
Jin, J., Bai, L., Wang, D., Ding, W., Cao, Z., Yan, P., Li, Y., Xi, L., Wang, Y., Zheng, X., et al. (2023) · EMBO Reports · doi:10.15252/embr.202256052 · Cited by 259
SIRT3, a pivotal actor in mitochondrial functions: metabolism, cell death and aging
Giralt, A., & Villarroya, F. (2012) · Biochemical Journal · doi:10.1042/bj20120030 · Cited by 258
SENP1-Sirt3 Signaling Controls Mitochondrial Protein Acetylation and Metabolism
Wang, T., Cao, Y., Zheng, Q., Tu, J., Zhou, W., He, J., Zhong, J., Chen, Y., Wang, J., Cai, R., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.008 · Cited by 250
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
Sorting out functions of sirtuins in cancer
Roth, M., & Chen, W. (2013) · Oncogene · doi:10.1038/onc.2013.120 · Cited by 242
FOXO3a from the Nucleus to the Mitochondria: A Round Trip in Cellular Stress Response
Fasano, C., Disciglio, V., Bertora, S., Signorile, M. L., & Simone, C. (2019) · Cells · doi:10.3390/cells8091110 · Cited by 251
Trials with ‘epigenetic’ drugs: An update
Nebbioso, A., Carafa, V., Benedetti, R., & Altucci, L. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.09.004 · Cited by 242
Mitochondria in Vascular Health and Disease
Dromparis, P., & Michelakis, E. D. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183804 · Cited by 248
Mitochondrial Metabolism, Sirtuins, and AgingPreprint
Sack, M. N., & Finkel, T. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013102 · Cited by 242
The sirtuin family’s role in aging and age-associated pathologies
Hall, J. A., Dominy, J. E., Lee, Y., & Puigserver, P. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64094 · Cited by 240
The SirT3 Divining Rod Points to Oxidative Stress
Bell, E. L., & Guarente, L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.008 · Cited by 235
From sirtuin biology to human diseases: an update
Sebastián, C., Satterstrom, F. K., Haigis, M. C., & Mostoslavsky, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.402768 · Cited by 201
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
Acetylation-Dependent Regulation of Skp2 Function
Inuzuka, H., Gao, D., Finley, L. W. S., Yang, W., Wan, L., Fukushima, H., Chin, Y. R., Zhai, B., Shaik, S., Lau, A. W., et al. (2012) · Cell · doi:10.1016/j.cell.2012.05.038 · Cited by 218
The engine driving the ship: metabolic steering of cell proliferation and death
Buchakjian, M. R., & Kornbluth, S. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2972 · Cited by 228
Sirtuin-3 (SIRT3), a novel potential therapeutic target for oral cancer
Alhazzazi, T. Y., Kamarajan, P., Joo, N., Huang, J., Verdin, E., D'Silva, N. J., & Kapila, Y. L. (2011) · Cancer · doi:10.1002/cncr.25676 · Cited by 208
Zhang, L., & Han, J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.02.101 · Cited by 213
Paulin, R., Dromparis, P., Sutendra, G., Gurtu, V., Zervopoulos, S., Bowers, L., Haromy, A., Webster, L., Provencher, S., Bonnet, S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.011 · Cited by 214
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
Giralt, A., Hondares, E., Villena, J. A., Ribas, F., Díaz-Delfín, J., Giralt, M., Iglesias, R., & Villarroya, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202390 · Cited by 210
(2010) · doi:10.1074/jbc.m110.168039 · Cited by 207
Self-citationNewman, J. C., He, W., & Verdin, E. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.404863 · Cited by 210
Zhou, X., Chen, M., Zeng, X., Yang, J., Deng, H., Yi, L., & Mt, M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.530 · Cited by 208
An overview of Sirtuins as potential therapeutic target: Structure, function and modulators
Wang, Y., He, J., Liao, M., Hu, M., Li, W., Ouyang, H., Wang, X., Ye, T., Zhang, Y., & Ouyang, L. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.10.028 · Cited by 210
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
Yu, L., Gong, B., Duan, W., Fan, C., Zhang, J., Li, Z., Xue, X., Xu, Y., Meng, D., Li, B., et al. (2017) · Scientific Reports · doi:10.1038/srep41337 · Cited by 210
Sirtuins, Aging, and MetabolismPreprint
Guarente, L. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010629 · Cited by 213
Tao, R., Vassilopoulos, A., Parisiadou, L., Yan, Y., & Gius, D. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5482 · Cited by 194
Self-citationRole of Oxidative Stress and the Microenvironment in Breast Cancer Development and Progression
Jezierska‐Drutel, A., Rosenzweig, S. A., & Neumann, C. A. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-407190-2.00003-4 · Cited by 203
Miller, V. J., Villamena, F. A., & Volek, J. S. (2018) · Journal of Nutrition and Metabolism · doi:10.1155/2018/5157645 · Cited by 205
Angiotensin II and the vascular phenotype in hypertension
Savoia, C., Burger, D. E., Nishigaki, N., Montezano, A. C. I., & Touyz, R. M. (2011) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411001815 · Cited by 203
Manganese superoxide dismutase regulation and cancer
Dhar, S. K., & St. Clair, D. K. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.03.009 · Cited by 196
Haigis, M. C., Deng, C., Finley, L. W. S., Kim, H., & Gius, D. R. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3633 · Cited by 196
Self-citation
Metadata
- Authors
- Kim, H.-S., Patel, K., Muldoon-Jacobs, K., Bisht, K. S., Aykin-Burns, N., Pennington, J. D., van der Meer, R., Nguyen, P., Savage, J., Owens, K. M., Vassilopoulos, A., Ozden, O., Park, S.-H., Singh, K. K., Abdulkadir, S. A., Spitz, D. R., Deng, C.-X., & Gius, D.
- Affiliations
- National Institutes of Health (US)
- Roswell Park Comprehensive Cancer Center (US)
- Vanderbilt University Medical Center (US)
- University of Iowa (US)
- Corresponding author
- Deng, Chu-Xia
- Gius, David
- ORCID
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 17
- Issue
- 1
- Pages
- 41-52
- ISSN
- 1535-6108 (ISSN-L)
- PMC
- PMC3711519
- OpenAlex
- W2145755327
- Cited by
- 785
- References
- 35
- Citations by year
- 2026: 11 · 2025: 30 · 2024: 35 · 2023: 20 · 2022: 44 · 2021: 49 · 2020: 44 · 2019: 47 · 2018: 48 · 2017: 56 · 2016: 71 · 2015: 53 · 2014: 61 · 2013: 74 · 2012: 67
- FWCI
- 27.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service (116430, R01 121904)
- National Institute on Aging (F30AG030839)
- National Cancer Institute (CA094858, CA123484, R01CA116430, R01CA094858, R01CA133114, R01CA100045, R01CA123484, R01CA121904, T32CA078586, P30CA086862)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- SIRT3, sirtuins, tumor suppressor, mitochondria, mitochondrial integrity, mitochondrial metabolism, superoxide, genomic instability, oncogenic transformation, c-Myc, Ras, superoxide dismutase, mammary tumors, breast cancer, cellular stress
- MeSH terms
- Aging, Animals, Breast Neoplasms, Cell Transformation, Neoplastic, Female, Fibroblasts, Humans, Immunohistochemistry, Mitochondria, Stress, Physiological, Superoxides, Genes, Tumor Suppressor, Mice, Knockout, Oxidative Stress, 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