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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
Cited by
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Items 401–500 of 788
Sirtuin 3 silencing improves oxaliplatin efficacy through acetylation of MnSOD in colon cancer
Torrens‐Mas, M., Hernández‐López, R., Oliver, J., Roca, P., & Sastre‐Serra, J. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26443 · Cited by 40
Herrera, K. N. G., Zaganjor, E., Ishikawa, Y., Spinelli, J. B., Yoon, H., Lin, J., Satterstrom, F. K., Ringel, A. E., Mulei, S., Souza, A., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.076 · Cited by 39
Sun, H., Yang, X., Zhao, Y., Tian, Q., Chen, M., Zhao, Y., & Jin, W. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.10.018 · Cited by 40
Sirt3‐dependent deacetylation of COX‐1 counteracts oxidative stress‐induced cell apoptosis
Tu, L., Cao, L., Zhang, Y., Guo, Y., Zhou, Y., Lu, W., Zhang, T., Zhang, T., Zhang, G., Kurihara, H., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900708r · Cited by 39
Chen, X., Overcash, R., Green, T., Hoffman, D. R., Asch, A. S., & Ruiz-Echevarría, M. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.193805 · Cited by 38
Kamarajan, P., Alhazzazi, T. Y., Danciu, T., D’Silva, N. J., Verdin, E. M., & Kapila, Y. L. (2012) · Cancer · doi:10.1002/cncr.27655 · Cited by 38
Curbing cancer's sweet tooth: Is there a role for MnSOD in regulation of the Warburg effect?
Holley, A. K., Dhar, S. K., & Clair, D. K. S. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.07.104 · Cited by 39
Germain, D. (2016) · Advances in cancer research · doi:10.1016/bs.acr.2016.01.004 · Cited by 38
Choi, J., Koh, E., Lee, Y. S., Lee, H., Kang, H.-G., Yoon, Y. E., Han, W. K., Choi, K. H., & Kim, K. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.117 · Cited by 39
Sirtuins in metabolism, stemness and differentiation
Correia, M., Perestrelo, T., Rodrigues, A. S., Ribeiro, M. F., Pereira, S. L., Sousa, M. I., & Ramalho‐Santos, J. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.09.008 · Cited by 40
Jeh, S. U., Park, J. J., Lee, J. S., Kim, D. C., Do, J., Lee, S. W., Choi, S. M., Hyun, J. S., Seo, D. H., Lee, C., et al. (2017) · Urologic Oncology Seminars and Original Investigations · doi:10.1016/j.urolonc.2017.08.016 · Cited by 39
Lipid peroxidation derived reactive aldehydes in alcoholic liver disease
Ali, H., Assiri, M. A., Shearn, C. T., & Fritz, K. S. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.10.003 · Cited by 38
Sirtuin 3 (SIRT3) Pathways in Age-Related Cardiovascular and Neurodegenerative Diseases
Silaghi, C. N., Farcas, M. F., & Craciun, A. M. (2021) · Biomedicines · doi:10.3390/biomedicines9111574 · Cited by 37
Mahjabeen, I., & Kayani, M. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146948 · Cited by 38
Wang, Z. P., Inuzuka, H., Zhong, J., Liu, P., Sarkar, F. H., Sun, Y., & Wei, W. (2012) · Oncotarget · doi:10.18632/oncotarget.740 · Cited by 37
The role of sirtuins in mitochondrial function and doxorubicin-induced cardiac dysfunction
Dolinsky, V. W. (2017) · Biological Chemistry · doi:10.1515/hsz-2016-0316 · Cited by 37
Perspectives of Reprogramming Breast Cancer Metabolism
Wang, Y.-P., & Lei, Q. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6020-5_10 · Cited by 39
Mapping genetic modifiers of radiation-induced cardiotoxicity to rat chromosome 3
Schlaak, R. A., Frei, A. C., Schottstaedt, A. M., Tsaih, S., Fish, B. L., Harmann, L. M., Liu, Q., Gasperetti, T., Medhora, M. M., North, P. E., et al. (2019) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00482.2018 · Cited by 37
ROS Mediate xCT-Dependent Cell Death in Human Breast Cancer Cells under Glucose Deprivation
Chen, M., Hsu, L.-L., Wang, S., Hsu, C., Lee, H., & Tseng, L. (2020) · Cells · doi:10.3390/cells9071598 · Cited by 37
Zuo, Z., He, L., Duan, X., Peng, Z., & Han, J. (2021) · Bioengineered · doi:10.1080/21655979.2021.2001925 · Cited by 37
Metabolic regulation of oxygen and redox homeostasis by p53: Lessons from evolutionary biology?
Zhuang, J., Ma, W., Lago, C. U., & Hwang, P. M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.07.026 · Cited by 37
Superoxide Mediates Acute Liver Injury in Irradiated Mice Lacking Sirtuin 3
Coleman, M. C., Olivier, A. K., Jacobus, J. A., Mapuskar, K. A., Mao, G., Martin, S. M., Riley, D. P., Gius, D. R., & Spitz, D. R. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5091 · Cited by 36
Self-citationIdentification of novel SIRT3 inhibitor scaffolds by virtual screening
Salo, H. S., Laitinen, T., Poso, A., Jarho, E. M., & Lahtela-Kakkonen, M. K. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.03.033 · Cited by 36
Yang, W., Liu, J., Hou, L., Chen, Q., & Liu, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118796 · Cited by 36
Sirtuins, aging, and cardiovascular risks
Favero, G., Franceschetti, L., Rodella, L. F., & Rezzani, R. (2015) · AGE · doi:10.1007/s11357-015-9804-y · Cited by 36
Zeng, H., Li, L., & Chen, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107011 · Cited by 36
Yang, Y., Wang, W., Xiong, Z., Kong, J., Qiu, Y., Shen, F., & Huang, Z. (2016) · Toxicology in Vitro · doi:10.1016/j.tiv.2016.03.020 · Cited by 35
Yu, X., Hu, Y., Huang, W., Ye, N., Yan, Q., Ni, W.-J., & Jiang, X. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107925 · Cited by 36
Shiozaki, M., Hayakawa, N., Shibata, M., Koike, M., Uchiyama, Y., & Gotow, T. (2011) · Histochemistry and Cell Biology · doi:10.1007/s00418-011-0847-6 · Cited by 35
Mitochondrial Sirtuins as Therapeutic Targets for Age-Related Disorders
Shih, J., & Dönmez, G. (2013) · Genes & Cancer · doi:10.1177/1947601912474931 · Cited by 35
The hypoxic response and aging
Kaeberlein, M. R., & Kapahi, P. (2009) · Cell Cycle · doi:10.4161/cc.8.15.9126 · Cited by 36
Redox Dysregulation in the Tumor Microenvironment Contributes to Cancer Metastasis
Liu, W., Wang, B., Zhou, M., Liu, D., Chen, F., Zhao, X., & Lu, Y. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0272 · Cited by 37
Mitochondrial pyruvate transport regulates presynaptic metabolism and neurotransmission
Tiwari, A., Myeong, J., Hashemiaghdam, A., Zhang, H., Niu, X., Laramie, M. A., Stunault, M. I., Sponagel, J., Patti, G. J., Shriver, L. P., et al. (2024) · Science Advances · doi:10.1126/sciadv.adp7423 · Cited by 33
Molecular Sentinels: Unveiling the Role of Sirtuins in Prostate Cancer Progression
Chouhan, S., Muhammad, N., Usmani, D., Khan, T. H., & Kumar, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms26010183 · Cited by 34
Activation and inhibition of sirtuins: From bench to bedside
Fiorentino, F., Fabbrizi, E., Mai, A., & Rotili, D. (2024) · Medicinal Research Reviews · doi:10.1002/med.22076 · Cited by 35
Systematic analysis of the achaete-scute complex-like gene signature in clinical cancer patients
Wang, C., Shahi, P., Huang, J., Phan, N. N., Sun, Z., Lin, Y.-C., Lai, M., & Werb, Z. (2016) · Molecular and Clinical Oncology · doi:10.3892/mco.2016.1094 · Cited by 33
Genetic Variants and Oxidative Stress in Alzheimer’s Disease
Kowalska, M., Wize, K., Prendecki, M., Lianeri, M., Kozubski, W. P., & Dorszewska, J. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200224121447 · Cited by 34
Poirault‐Chassac, S., Nivet‐Antoine, V., Houvert, A., Kauskot, A., Lauret, E., Lai–Kuen, R., Dusanter‐Fourt, I., & Baruch, D. (2021) · Blood Advances · doi:10.1182/bloodadvances.2020002847 · Cited by 36
Zhang, B., Qin, L., Zhou, C.-J., Liu, Y.-L., Qian, H., & He, S. (2013) · Asian Pacific Journal of Tropical Medicine · doi:10.1016/s1995-7645(13)60112-1 · Cited by 33
Metabolic modulation of cancer: a new frontier with great translational potential
Kinnaird, A. S., & Michelakis, E. D. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1250-2 · Cited by 32
Palma, S. D., Leone, R., Grumati, P., Vasso, M., Polishchuk, R., Capitanio, D., Braghetta, P., Bernardi, P., Bonaldo, P., & Gelfi, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056716 · Cited by 35
Russo, M. A., Sansone, L., Polletta, L., Runci, A., Rashid, M., Santis, E. D., Vernucci, E., Carnevale, I., & Tafani, M. (2014) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/1871530314666140709093305 · Cited by 32
Lee, M., Jeon, J. Y., Neugent, M. L., Kim, J., & Yun, M. (2017) · Clinical & Experimental Metastasis · doi:10.1007/s10585-017-9847-9 · Cited by 32
Jo, H., Park, Y., Kim, T., Kim, J., Lee, J. S., Kim, S. Y., Chung, J.-I., Ko, H. Y., Pyun, J., Kim, K. S., et al. (2020) · BMC Cancer · doi:10.1186/s12885-020-06822-4 · Cited by 32
Bergmann, L., Lang, A., Bross, C., Altinoluk-Hambüchen, S., Fey, I., Overbeck, N., Stefanski, A., Wiek, C., Kefalas, A., Verhülsdonk, P., et al. (2020) · Cells · doi:10.3390/cells9091950 · Cited by 32
Dallio, M., Romeo, M., Gravina, A. G., Masarone, M., Larussa, T., Abenavoli, L., Persico, M., Loguercio, C., & Federico, A. (2021) · Nutrients · doi:10.3390/nu13051679 · Cited by 32
A “Weird” Mitochondrial Fatty Acid Oxidation as a Metabolic “Secret” of Cancer
Zhelev, Z., Aoki, I., Lazarova, D., Vlaykova, T. I., Higashi, T., & Bakalova, R. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2339584 · Cited by 34
Aykin‐Burns, N., Slane, B. G., Liu, A. T. Y., Owens, K. M., O'Malley, M. S., Smith, B. J., Domann, F. E., & Spitz, D. R. (2010) · Radiation Research · doi:10.1667/rr2220.1 · Cited by 34
Self-citationGlutamine, Glucose and other Fuels for Cancer
Ruiz-Pérez, M. V., Sánchez‐Jiménez, F., Alonso, F. J., Segura, J., Márquez, J., & Medina, M. Á. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113199990482 · Cited by 31
SIRT3 mediates decrease of oxidative damage and prevention of ageing in porcine fetal fibroblasts
Xie, X., Wang, L., Zhao, B., Chen, Y., & Li, J. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.01.010 · Cited by 33
Kong, J., Wang, L., Ren, L., Yan, Y., Cheng, Y., Huang, Z., & Shen, F. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.01.011 · Cited by 31
Hou, L., Wang, R., Wei, H., Li, S., Liu, L., Lü, X., Yu, H., & Liu, Z. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116561 · Cited by 31
Lin, C., Cao, X., Qu, Z., Zhang, S., Naqvi, N. I., & Deng, Y. (2021) · mSphere · doi:10.1128/msphere.00118-21 · Cited by 31
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Onyiba, C. I., Scarlett, C. J., & Weidenhofer, J. (2022) · Cancers · doi:10.3390/cancers14205118 · Cited by 31
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Roth, M., Wang, Z., & Chen, W. (2013) · Critical Reviews™ in Oncogenesis · doi:10.1615/critrevoncog.2013010187 · Cited by 31
Tsusaka, T., Guo, T., Yagura, T., Inoue, T., Yokode, M., Inagaki, N., & Kondoh, H. (2014) · Genes to Cells · doi:10.1111/gtc.12176 · Cited by 31
Rezaei, M., Keshtzar, E., Khodayar, M. J., & Javadipour, M. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.10.025 · Cited by 31
Monteiro‐Reis, S., Lameirinhas, A., Miranda‐Gonçalves, V., Felizardo, D., Dias, P. C., Oliveira, J., Graça, I. C. R., Gonçalves, C. S., Costa, B. M., Henrique, R., et al. (2020) · Cancers · doi:10.3390/cancers12051066 · Cited by 31
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Waypa, G. B., Osborne, S. W., Marks, J. D., Berkelhamer, S. K., Kondapalli, J., & Schumacker, P. T. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0191oc · Cited by 32
Panza, S., Santoro, M., Amicis, F. D., Morelli, C., Passarelli, V., D’Aquila, P., Giordano, F., Cione, E., Passarino, G., Bellizzi, D., et al. (2017) · Tumor Biology · doi:10.1177/1010428317701642 · Cited by 31
Kenny, T. C., & Germain, D. (2017) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-017-9722-z · Cited by 31
Moore, M. P., Cunningham, R. P., Kelty, T. J., Boccardi, L., Nguyen, N., Booth, F. W., & Rector, R. S. (2019) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2019-0042 · Cited by 29
Wang, S., Chang, Y.-L., Tzeng, Y. T., Wu, C.-L., Wang, Y.-Z., Tseng, L., Chen, S., & Lee, H. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.09.043 · Cited by 28
Ma, J., Zhao, G., Du, J., Jiang, L., Lin, G., & Zhang, J. (2021) · Cancer Management and Research · doi:10.2147/cmar.s329419 · Cited by 29
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Dong, X. C. (2012) · Diabetes Management · doi:10.2217/dmt.12.16 · Cited by 29
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Effect of ganoderic acid D on colon cancer Warburg effect: Role of SIRT3/cyclophilin D
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Marmolejo-Garza, A., Medeiros-Furquim, T., Rao, R. G., Eggen, B. J. L., Boddeke, E., & Dolga, A. M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119326 · Cited by 29
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Weigl, S., Paradiso, A., & Tommasi, S. (2013) · Current Genomics · doi:10.2174/1389202911314030005 · Cited by 28
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Kincaid, J. W. R., & Berger, N. A. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220929287 · Cited by 29
Schumacker, P. T. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.032 · Cited by 28
Xu, G., Quan, S., Schell, J. R., Gao, Y., Varmazyad, M., Sreenivas, P., Cruz, D., Jiang, H., Pan, M., Han, X., et al. (2024) · Science Advances · doi:10.1126/sciadv.adj5942 · Cited by 30
Self-citationDebsharma, S., Pramanik, S., Bindu, S., Mazumder, S., Das, T., Saha, D., De, R., Nag, S., Banerjee, C., Siddiqui, A. A., et al. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16070 · Cited by 26
Zhu, X., Ma, E., Ge, Y., Meng, Y., Guo, X., Peng, J., Zhu, W., Ren, D., & Wo, D. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116476 · Cited by 26
Shulyakova, N., Sidorova‐Darmos, E., Fong, J., Zhang, G., Mills, L. R., & Eubanks, J. H. (2014) · Brain Research · doi:10.1016/j.brainres.2014.08.066 · Cited by 26
Mitochondrial Acetylation and Genetic Models of Parkinson's Disease
Auburger, G. W. J., Gispert, S., & Jendrach, M. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00006-4 · Cited by 27
Mitochondrial sirtuin 3 and various cell death modalities
Yapryntseva, M. A., Maximchik, P. V., Zhivotovsky, B., & Gogvadze, V. G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.947357 · Cited by 28
Exploiting aneuploidy-imposed stresses and coping mechanisms to battle cancer
Zhou, L., Jilderda, L. J., & Foijer, F. (2020) · Open Biology · doi:10.1098/rsob.200148 · Cited by 30
SIRT3 protects endothelial cells from high glucose-induced cytotoxicity.
Liu, G., Cao, M., Xu, Y., & Li, Y. (2015) · Europe PMC (PubMed Central) · Cited by 25
Regulation of Cancer and Cancer-Related Genes via NAD +
Sharif, T., Martell, E., Dai, C., Ghassemi-Rad, M. S., Kennedy, B. E., Lee, P. W. K., & Gujar, S. A. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7478 · Cited by 25
Nie, Z.-J., Zhang, Y., Chang, Y., Li, Q., & Zhang, Y.-L. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.07.092 · Cited by 25
Morita, M., & Kanasaki, K. (2020) · Diabetes & Metabolism · doi:10.1016/j.diabet.2020.06.005 · Cited by 24
Chasing the FOXO3: Insights into Its New Mitochondrial Lair in Colorectal Cancer Landscape
Grossi, V., Fasano, C., Celestini, V., Signorile, M. L., Sanese, P., & Simone, C. (2019) · Cancers · doi:10.3390/cancers11030414 · Cited by 25
Mitochondrial quality control: the real dawn of intervertebral disc degeneration?
Qiu, B., Xie, X., & Xi, Y. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05943-9 · Cited by 28
Roles of SIRT3 in aging and aging-related diseases
You, Y., & Wang, Z. (2025) · International Journal of Biological Sciences · doi:10.7150/ijbs.115518 · Cited by 26
SIRT3 is a novel prognostic biomarker for esophageal squamous cell carcinoma
Yan, S., Han, X., Han, P., Chen, H.-M., Huang, L., & Li, Y. (2014) · Medical Oncology · doi:10.1007/s12032-014-0103-8 · Cited by 24
Sirtuin-3 modulates Bak- and Bax-dependent apoptosis
Verma, M., Shulga, N., & Pastorino, J. G. (2012) · Journal of Cell Science · doi:10.1242/jcs.115188 · Cited by 24
RetractedNdlovu, S. S., Nagiah, S., Abdul, N. S., Ghazi, T., & Chuturgoon, A. A. (2021) · Toxicon · doi:10.1016/j.toxicon.2021.01.017 · Cited by 24
Eldridge, M. J. G., & Hamon, M. A. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010173 · Cited by 25
Dhillon, R. S., Qin, Y., van Ginkel, P. R., Fu, V. X., Vann, J. M., Lawton, A. J., Green, C. L., Manchado-Gobatto, F. D. B., Gobatto, C. A., Lamming, D. W., et al. (2022) · Aging Cell · doi:10.1111/acel.13721 · Cited by 25
Sirt3 restricts tumor initiation via promoting LONP1 deacetylation and K63 ubiquitination
Wu, L., Yan, X., Sun, R., Ma, Y., Yao, W., Gao, B., Zhang, Q., You, J., Wang, H., Han, Q., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-03925-x · Cited by 28
Intersections between mitochondrial sirtuin signaling and tumor cell metabolism
Herrera, K. N. G., Lee, J. J., & Haigis, M. C. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1031879 · Cited by 25
The sirtuins in the pathogenesis of cancer
Voelter‐Mahlknecht, S., & Mahlknecht, U. (2010) · Clinical Epigenetics · doi:10.1007/s13148-010-0008-0 · Cited by 24
Bioactive food components, cancer cell growth limitation and reversal of glycolytic metabolism
Keijer, J., Bekkenkamp‐Grovenstein, M., Venema, D. P., & Dommels, Y. E. M. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.08.007 · Cited by 25
Son, M. J., Ryu, J., Kim, J. Y., Kwon, Y., Chung, K., Mun, S. J., & Cho, Y. S. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.74 · Cited by 24
Neuroprotective role of retinal SIRT3 against acute photo-stress
Ban, N., Ozawa, Y., Osada, H., Lin, J. B., Toda, E., 渡辺, 光., Yuki, K., Kubota, S., Apte, R. S., & Tsubota, K. (2017) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-017-0017-8 · Cited by 24
Sirt3 is dispensable for oocyte quality and female fertility in lean and obese mice
Iljas, J. D., & Homer, H. A. (2020) · The FASEB Journal · doi:10.1096/fj.202000153r · Cited by 24
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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