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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.
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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]
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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
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Rice, C. M., Sun, M., Kemp, K. C., Gray, E., Wilkins, A., & Scolding, N. J. (2012) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2012.08150.x · Cited by 25
McIntyre, A. J., Angel, C. Z., Smith, J. S., Templeman, A., Beattie, K., Beattie, S., Ormrod, A., Devlin, E., McGreevy, C., Bothwell, C., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac494 · Cited by 23
Chromatin Regulators with Tumor Suppressor Properties and their Alterations in Human Cancers
Shu, X., Li, L., & Tao, Q. (2012) · Epigenomics · doi:10.2217/epi.12.50 · Cited by 23
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Newman, D. L., & Gregory, S. L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184611 · Cited by 24
Acetylation control of metabolic enzymes in cancer: an updated version
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Zeng, X., Wang, N., Zhai, H., Wang, R., Wu, J., & Pu, W. (2017) · Tumor Biology · doi:10.1177/1010428317691178 · Cited by 22
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Liu, Y., Wei, H., & Li, J. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176155 · Cited by 22
The signaling pathways that mediate the anti-cancer effects of caloric restriction
Lu, Y., Tao, F., Zhou, M., & Tang, K. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.01.021 · Cited by 24
The oxidative stress in breast tumors of postmenopausal women is ERα/ERβ ratio dependent
Sastre‐Serra, J., Nadal‐Serrano, M., Pons, D. G., Valle, A., Garau, I., Garcia-Bonafe, M., Oliver, J., & Roca, P. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.005 · Cited by 23
Changes in sirtuin 2 and sirtuin 3 mRNA expressions in rheumatoid arthritis
Kara, M., Yolbaş, S., Şahin, C., & Koca, S. S. (2017) · European Journal of Rheumatology · doi:10.5152/eurjrheum.2017.16056 · Cited by 22
Gao, Y., Zhu, Y., Tran, E. L., Tokars, V. L., Dean, A. E., Quan, S., & Gius, D. R. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.51184 · Cited by 22
Self-citationLi, Y., Wang, Q., Li, J., Shi, B., Liu, Y., & Wang, P. (2021) · The Prostate · doi:10.1002/pros.24208 · Cited by 21
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Liu, Y., Zhang, D., & Chen, D. (2011) · Aging · doi:10.18632/aging.100256 · Cited by 21
Uzhachenko, R. V., Issaeva, N., Boyd, K. L., Ivanov, S. V., Carbone, D. P., & Ivanova, A. V. (2012) · The Journal of Pathology · doi:10.1002/path.4039 · Cited by 20
Schistosome Sirtuins as Drug Targets
Lancelot, J., Cabezas‐Cruz, A., Caby, S., Marek, M., Schultz, J., Romier, C., Sippl, W., Jung, M., & Pierce, R. J. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.24 · Cited by 22
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Gounden, S., Phulukdaree, A., Moodley, D., & Chuturgoon, A. A. (2015) · Metabolic Syndrome and Related Disorders · doi:10.1089/met.2014.0140 · Cited by 21
The expression levels of the sirtuins in patients with BCC
Temel, M., Koç, M. N., Ulutaş, S., & Göğebakan, B. (2015) · Tumor Biology · doi:10.1007/s13277-015-4522-8 · Cited by 21
Huang, S., Chen, X., Zheng, J., Huang, Y.-F., Song, L., Yin, Y., & Xiong, J. (2017) · Pathology - Research and Practice · doi:10.1016/j.prp.2017.07.023 · Cited by 21
Yao, H., Zhao, H., Du, Y., Zhang, Y., Li, Y., & Zhu, H. (2024) · Translational research · doi:10.1016/j.trsl.2024.03.005 · Cited by 20
The role of redox homeostasis in tumor progression: implications for cancer therapy
Liu, Y., Cai, X., Liu, J., Luo, Z. K., Zhang, J., Cao, Z., Ma, W., Tang, Y., Liu, T., Wei, H., et al. (2025) · Acta Biomaterialia · doi:10.1016/j.actbio.2025.07.067 · Cited by 23
Anthracycline-induced cardiomyopathy: cellular and molecular mechanisms
Dadson, K., Arguelles, O. C., Thavendiranathan, P., & Billia, F. (2020) · Clinical Science · doi:10.1042/cs20190653 · Cited by 20
Yang, Q., Wang, Y., Wang, H., Li, H., Zhu, J., Cong, L., Xu, J., Chen, W., Jiang, Y., & Sun, Y. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.628 · Cited by 20
CPT2 K79 acetylation regulates platelet life span
Fan, X., Wang, Y., Cai, X., Shen, Y., Xu, T., Xu, Y., Cheng, J., Wang, X., Zhang, L., Dai, J., et al. (2022) · Blood Advances · doi:10.1182/bloodadvances.2021006687 · Cited by 20
Sirtfoods: New Concept Foods, Functions, and Mechanisms
Akan, O. D., Qin, D., Guo, T., Lin, Q., & Luo, F. (2022) · Foods · doi:10.3390/foods11192955 · Cited by 22
Zhang, W., Zhang, Y., Xu, T., Wang, Z., Wang, J., Xiong, W., Lu, W., Zheng, H., & Yuan, J. (2015) · Toxicology Research · doi:10.1039/c5tx00229j · Cited by 20
Akhmedov, A. T., Montecucco, F., Costantino, S., Vdovenko, D., Clerigué, A. S., Gaul, D. S., Burger, F., Roth, A., Carbone, F., Liberale, L., et al. (2019) · Thrombosis and Haemostasis · doi:10.1055/s-0039-3400299 · Cited by 20
Tan, X., Zhou, Y., Agarwal, A., Lim, M., Xu, Y., Zhu, Y., O'Brien, J., Tran, E. L., Zheng, J., Gius, D. R., et al. (2020) · PubMed Central · Cited by 18
Self-citationCantrell, A. C., Besanson, J., Williams, Q. A., Hoang, N., Edwards, K. S., Bishop, G. R., Chen, Y., Zeng, H., & Chen, J. (2024) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2024.05.003 · Cited by 19
Proteome profile and lentiviral transduction of cultured honey bee ( Apis mellifera L.) cells
Chan, M. M. Y., Choi, S., Chan, Q. W. T., Li, P., Guarna, M. M., & Foster, L. J. (2010) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2010.01022.x · Cited by 19
Chen, I., Chiang, W., Chen, P., & Chiang, H. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24667 · Cited by 19
Staszkiewicz, J., Power, R. A., Harkins, L. L., Barnes, C. W., Strickler, K. L., Rim, J. S., Bondioli, K. R., & Eilersten, K. J. (2013) · Cellular Reprogramming · doi:10.1089/cell.2013.0026 · Cited by 18
Metabolic Alterations at the Crossroad of Aging and Oncogenesis
Raffaghello, L., & Longo, V. D. (2017) · International review of cytology · doi:10.1016/bs.ircmb.2017.01.003 · Cited by 19
Patel, S., Shah, L., Dang, N., Tan, X., Almudevar, A., & White, P. M. (2020) · PLoS ONE · doi:10.1371/journal.pone.0235491 · Cited by 18
Rossi, G., Placidi, M., Castellini, C., Rea, F., D’Andrea, S., Alonso, G. L., Gravina, G. L., Tatone, C., Emidio, G. D., & D’Alessandro, A. M. (2021) · Molecules · doi:10.3390/molecules26061676 · Cited by 18
Hayashi, H., Cherpokova, D., Martinod, K., Witsch, T., Wong, S. L., Gallant, M., Cifuni, S. M., Guarente, L., & Wagner, D. D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0188341 · Cited by 17
Lü, H., Sun, L., Chen, W., Zhou, Y., Liu, K., Chen, J., Zhang, Z., Zhang, C., & Tian, H. (2019) · Annals of Vascular Surgery · doi:10.1016/j.avsg.2019.05.044 · Cited by 17
Kim, H., Richardson, K. K., Krager, K. J., Ling, W., Simmons, P., Allen, A. R., & Aykin‐Burns, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111711 · Cited by 17
Self-citationRezaeian, A.-H., Phan, L. M., Zhou, X., Wei, W., & Inuzuka, H. (2023) · Neoplasia · doi:10.1016/j.neo.2023.100890 · Cited by 16
Dong, K. K., Pelle, E., Yarosh, D. B., & Pernodet, N. (2012) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01439.x · Cited by 17
The multifaceted mitochondrion: An attractive candidate for therapeutic strategies
Strappazzon, F., & Cecconi, F. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.03.007 · Cited by 17
Bondagji, N., Morad, F. A., Al‐Nefaei, A. A. A., Khan, I. A., Elango, R., Abdullah, L. S., Almansouri, N., Sabir, J. S. M., Banaganapalli, B., Edris, S., et al. (2016) · Journal of obstetrics and gynaecology research · doi:10.1111/jog.13217 · Cited by 17
Human SIRT2 and SIRT3 deacetylases function in DNA homologous recombinational repair
Yasuda, T., Takizawa, K., Ui, A., Hama, M., Kagawa, W., Sugasawa, K., & Tajima, K. (2021) · Genes to Cells · doi:10.1111/gtc.12842 · Cited by 18
Fang, Y., Wang, J., Xu, L., Cao, Y., Xu, F., Yan, L., Nie, M., Zhang, S., Zhang, S., Zhao, R., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9592 · Cited by 19
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Yu, F., Xu, Q., Wu, D., Lau, A. T. Y., & Xu, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0159801 · Cited by 16
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Wu, Z., Wang, Z., Wu, L., Yu, L., Xie, X., Yu, F., Kong, W., Bi, S., Liu, S., Yin, G., et al. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s494841 · Cited by 16
Role of Sirtuins in Linking Metabolic Syndrome with Depression
Song, J., & Kim, J. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00086 · Cited by 16
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Matteis, S. D., Granato, A. M., Napolitano, R., Molinari, C., Valgiusti, M., Santini, D., Foschi, F. G., Ercolani, G., Gentilucci, U. V., Faloppi, L., et al. (2017) · Digestive Diseases and Sciences · doi:10.1007/s10620-017-4615-x · Cited by 16
Dysregulated Epigenetic Modifications in the Pathogenesis of NAFLD-HCC
Zhao, F. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-8684-7_7 · Cited by 17
Campit, S., Meliki, A., Youngson, N. A., & Chandrasekaran, S. (2020) · BioEssays · doi:10.1002/bies.202000083 · Cited by 17
Luthra, S., Chandran, U. R., Diergaarde, B. B., Becich, M. J., Lee, A. V., & Neumann, C. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.011 · Cited by 16
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LoBianco, F. V., Krager, K. J., Carter, G. S., Alam, S., Yuan, Y., Lavoie, É. G., Dranoff, J. A., & Aykin‐Burns, N. (2020) · Antioxidants · doi:10.3390/antiox9050409 · Cited by 16
Self-citationBelužić, R., Šimunić, E., Podgorski, I. I., Pinterić, M., Hadžija, M. P., Balog, T., & Sobočanec, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073868 · Cited by 17
Ahmed, M. W., Mahjabeen, I., Gul, S., Khursheed, A., Mehmood, A., & Kayani, M. A. (2019) · Future Oncology · doi:10.2217/fon-2019-0365 · Cited by 15
Smolková, K., Špačková, J., Gotvaldová, K., Dvořák, A., Křenková, A., Hubálek, M., Holendová, B., Vı́tek, L., & Ježek, P. (2020) · Scientific Reports · doi:10.1038/s41598-020-65351-z · Cited by 15
Yokoyama, N. N., Denmon, A. P., Uchio, E., Jordan, M. L., Mercola, D., & Zi, X. (2015) · Current Pharmacology Reports · doi:10.1007/s40495-015-0039-5 · Cited by 15
Characteristics of expression and regulation of sirtuins in chicken (Gallus gallus)
Ren, J., Xu, N., Ma, Z., Li, Y., Li, C., Wang, Y., Tian, Y., Liu, X., & Kang, X. (2016) · Genome · doi:10.1139/gen-2016-0125 · Cited by 15
Li, C., Ge, C., Wang, Q., Teng, P., Jia, H., Yao, S., & Huang, Z. (2025) · Cellular Oncology · doi:10.1007/s13402-025-01058-5 · Cited by 19
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Tao, S., Tao, K., & Cai, X. (2024) · Scientific Reports · doi:10.1038/s41598-024-55455-1 · Cited by 14
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Zhang, D., Liu, Y., & Chen, D. (2011) · Aging · doi:10.18632/aging.100283 · Cited by 14
Chen, I., Huang, H.-H., Chen, P., & Chiang, H. (2016) · Toxicological Sciences · doi:10.1093/toxsci/kfw073 · Cited by 14
Sadek, N. B., Gamal, S. M., Aboulhoda, B. E., Rashed, L. A., Shawky, H. M., & El‐Din, M. G. (2019) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248419876632 · Cited by 14
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Xu, Y., Jian, X., Shi, L., Shock, L. S., Chen, L., Chow, L. T., & Wang, H. (2026) · Cells · doi:10.3390/cells15020095 · Cited by 13
Parsons, R. B., Kocinaj, A., Ruiz-Pulido, G., Prendergast, S. A., Parsons, A. E., Facey, P. D., & Hirth, F. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac077 · Cited by 13
Abdelmaksoud, N. M., Abulsoud, A. I., Abdelghany, T. M., Elshaer, S. S., Rizk, S. M., Senousy, M. A., & Maurice, N. W. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.114150 · Cited by 14
Wei, S., Schell, J. R., Qian, W., Silguero, M., Baseviciene, A., Chen, W. H., Trevino, R., Chocrón, E. S., Ogle, M. M., Varmazyad, M., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116026 · Cited by 15
Self-citationGülmez, C., & Atakişi, O. (2019) · Nutrition and Cancer · doi:10.1080/01635581.2019.1635628 · Cited by 12
Haumann, S., Boix, J., Knuever, J., Bieling, A. M., Vila‐Sanjurjo, A., Elson, J. L., Blakely, E. L., Taylor, R. W., Riet, N., Abken, H., et al. (2020) · Carcinogenesis · doi:10.1093/carcin/bgaa032 · Cited by 12
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Haigis, M. C., & Sinclair, D. A. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-378638-8.00011-7 · Cited by 13
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Chabi, B., Fouret, G., Lecomte, J., Cortade, F., Pessemesse, L., Baati, N., Coudray, C., Lin, L., Tong, Q., Wrutniak‐Cabello, C., et al. (2018) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-018-9752-1 · Cited by 13
Alam, S., Carter, G. S., Krager, K. J., Li, X., Lehmler, H., & Aykin‐Burns, N. (2018) · Antioxidants · doi:10.3390/antiox7090121 · Cited by 13
Self-citationPinterić, M., Podgorski, I. I., Sobočanec, S., Hadžija, M. P., Paradžik, M., Dekanić, A., Marinović, M., Halasz, M., Belužić, R., Davidović, G., et al. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1462495 · Cited by 13
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Ghinis-Hozumi, Y., Antaramián, A., Villarroya, F., Piña, E., & Mora, O. (2012) · animal · doi:10.1017/s1751731112001115 · Cited by 12
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Stankova, K., Ivanova, K., Nikolov, V., Aneva, N., Georgieva, R. T., & Boteva, R. (2013) · International Journal of Radiation Biology · doi:10.3109/09553002.2013.782451 · Cited by 12
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Giblin, W., & Lombard, D. B. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-411596-5.00003-4 · Cited by 12
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Satterstrom, F. K., & Haigis, M. C. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801329-8.00007-6 · Cited by 12
Fyn kinase regulates translation in mammalian mitochondria
Koc, E. C., Miller‐Lee, J. L., & Koç, H. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.12.004 · Cited by 12
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Jenkins, E. C., Chattopadhyay, M., & Germain, D. (2021) · Aging and Cancer · doi:10.1002/aac2.12035 · Cited by 11
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Wang, T., Han, T., Xiao, X., Guo, D., Sun, X., Liu, Y., Zhao, L., Xu, H., Li, R., Jiang, L., et al. (2025) · Science China Life Sciences · doi:10.1007/s11427-024-2823-2 · Cited by 12
The mitochondrial LONP1 protease: molecular targets and role in pathophysiology
Tang, P. C., Qun, Z., Li, Y., Wang, J., & She, M. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10500-8 · Cited by 12
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Garg, G., Singh, A. K., Singh, S., & Rizvi, S. I. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1915980 · Cited by 11
Szychowski, K. A., Skóra, B., & Wójtowicz, A. K. (2022) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2022.105131 · Cited by 11
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Haq, M. F. U., Hussain, M. Z., Mahjabeen, I., Akram, Z., Saeed, N., Shafique, R., Abbasi, S. F., & Kayani, M. A. (2023) · PLoS ONE · doi:10.1371/journal.pone.0281840 · Cited by 11
Identification of polymorphisms in cancer patients that differentially affect survival with age
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Apocrine papillary cystadenoma of a minor salivary gland on the lower lip: case presentation.
Halbritter, S. A., Altermatt, H. J., Caversaccio, M. D., & Bornstein, M. M. (2009) · PubMed · Cited by 11
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
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