Mitochondrial Sirtuin 3: New emerging biological function and therapeutic target

Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation

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On the origin of cancer cells

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Parkinson's disease

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The emerging hallmarks of cancer metabolism

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MicroRNA therapeutics: towards a new era for the management of cancer and other diseases

Rupaimoole, R., & Slack, F. J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.246 · Cited by 4,741 · cited 1× · see citing works

Biological Functions of Autophagy Genes: A Disease Perspective

Levine, B., & Kroemer, G. (2019) · Cell · doi:10.1016/j.cell.2018.09.048 · Cited by 2,832 · see citing works

A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis

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Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction

Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works

An inhibitor of oxidative phosphorylation exploits cancer vulnerability

Molina, J. R., Sun, Y., Protopopova, M., Gera, S., Bandi, M., Bristow, C., McAfoos, T., Morlacchi, P., Ackroyd, J., Agip, A.-N. A., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0052-4 · Cited by 928 · see citing works

Pharmacological modulation of autophagy: therapeutic potential and persisting obstacles

Galluzzi, L., Bravo-San Pedro, J. M., Levine, B., Green, D. R., & Kroemer, G. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.22 · Cited by 842 · see citing works

Mitochondria as a therapeutic target for common pathologies

Murphy, M. P., & Hartley, R. C. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.174 · Cited by 832 · see citing works

Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity

Frye, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0897 · Cited by 809 · see citing works

Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor

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SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome

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

Venetoclax with azacitidine disrupts energy metabolism and targets leukemia stem cells in patients with acute myeloid leukemia

Pollyea, D. A., Stevens, B. M., Jones, C. L., Winters, A., Pei, S., Minhajuddin, M., D’Alessandro, A., Culp-Hill, R., Riemondy, K. A., Gillen, A. E., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0233-1 · Cited by 778 · see citing works

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 712 · see citing works

Building and decoding ubiquitin chains for mitophagy

Harper, J. W., Ordureau, A., & Heo, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.129 · Cited by 668 · see citing works

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 · see citing works

FOXO3A directs a protective autophagy program in haematopoietic stem cells

Warr, M. R., Binnewies, M., Flach, J., Reynaud, D., Garg, T., Malhotra, R., Debnath, J., & Passegué, E. (2013) · Nature · doi:10.1038/nature11895 · Cited by 625 · see citing works

Trimethylamine‐N‐Oxide Induces Vascular Inflammation by Activating the NLRP3 Inflammasome Through the SIRT3‐SOD2‐mtROS Signaling Pathway

Chen, M., Zhu, X., Ran, L., Lang, H., Yi, L., & Mi, M. (2017) · Journal of the American Heart Association · doi:10.1161/jaha.117.006347 · Cited by 600 · see citing works

The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide–dependent deacetylase

Schwer, B., North, B. J., Frye, R. A., Ott, M., & Verdin, E. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205057 · Cited by 599 · see citing works

SIRT3 Is a Stress-Responsive Deacetylase in Cardiomyocytes That Protects Cells from Stress-Mediated Cell Death by Deacetylation of Ku70

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

Fighting neurodegeneration with rapamycin: mechanistic insights

Bové, J., Martínez‐Vicente, M., & Vila, M. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn3068 · Cited by 525 · see citing works

Discovery, In Vivo Activity, and Mechanism of Action of a Small-Molecule p53 Activator

Laı́n, S., Hollick, J. J., Campbell, J., Staples, O. D., Higgins, M., Aoubala, M., McCarthy, A. R., Appleyard, V. C. L., Murray, K. E., Baker, L., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.03.004 · Cited by 523 · see citing works

Energy metabolism in heart failure

Ventura‐Clapier, R., Garnier, A., & Veksler, V. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.055095 · Cited by 499 · see citing works

Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex

Wei, W., Ayad, N. G., Wan, Y., Zhang, G.-J., Kirschner, M. W., & Kaelin, W. G. (2004) · Nature · doi:10.1038/nature02381 · Cited by 495 · see citing works

Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production

Jing, E., Emanuelli, B., Hirschey, M. D., Boucher, J., Lee, K. Y., Lombard, D., Verdin, E. M., & Kahn, C. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111308108 · Cited by 469 · see citing works

Honokiol blocks and reverses cardiac hypertrophy in mice by activating mitochondrial Sirt3

Pillai, V. B., Samant, S. A., Sundaresan, N. R., Raghuraman, H., Kim, G. H., Bonner, M. Y., Arbiser, J. L., Walker, D. I., Jones, D. P., Gius, D. R., et al. (2015) · Nature Communications · doi:10.1038/ncomms7656 · Cited by 453 · 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

SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production

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

Exogenous NAD Blocks Cardiac Hypertrophic Response via Activation of the SIRT3-LKB1-AMP-activated Kinase Pathway

Pillai, V. B., Sundaresan, N. R., Kim, G. H., Gupta, M., Rajamohan, S. B., Pillai, J. B., Samant, S. A., Ravindra, P. A., Isbatan, A., & Gupta, M. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077271 · Cited by 420 · see citing works

Conserved Metabolic Regulatory Functions of Sirtuins

Schwer, B., & Verdin, E. M. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.006 · Cited by 415 · see citing works

Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology

Zhan, M., Brooks, C. R., Liu, F., Sun, L., & Dong, Z. (2013) · Kidney International · doi:10.1038/ki.2012.441 · Cited by 396 · see citing works

Are sirtuins viable targets for improving healthspan and lifespan?

Baur, J. A., Ungvari, Z. I., Minor, R. K., Couteur, D. G. L., & de Cabo, R. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3738 · Cited by 389 · see citing works

SIRT1 and SIRT6 Signaling Pathways in Cardiovascular Disease Protection

D’Onofrio, N., Servillo, L., & Balestrieri, M. L. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7178 · Cited by 389 · see citing works

Sirtuin 3-dependent mitochondrial dynamic improvements protect against acute kidney injury.

Morigi, M., Perico, L., Rota, C., Longaretti, L., Conti, S., Rottoli, D., Novelli, R., Remuzzi, G., & Benigni, A. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77632 · Cited by 388 · see citing works

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 · see citing works

SIRT3-SOD2-mROS-dependent autophagy in cadmium-induced hepatotoxicity and salvage by melatonin

Pi, H., Xu, S., Reiter, R. J., Guo, P., Zhang, L., Li, Y., Li, M., Cao, Z., Tian, L., Xie, J., et al. (2015) · Autophagy · doi:10.1080/15548627.2015.1052208 · Cited by 363 · see citing works

Sirtuins in Renal Health and Disease

Morigi, M., Perico, L., & Benigni, A. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017111218 · Cited by 359 · see citing works

The FOXO3a Transcription Factor Regulates Cardiac Myocyte Size Downstream of AKT Signaling

Skurk, C., Izumiya, Y., Maatz, H., Razeghi, P., Shiojima, I., Sandri, M., Sato, K., Zeng, L., Schiekofer, S., Pimentel, D. R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500528200 · Cited by 353 · see citing works

Therapeutic effect of Sirtuin 3 on ameliorating nonalcoholic fatty liver disease: The role of the ERK-CREB pathway and Bnip3-mediated mitophagy

Li, R., Xin, T., Li, D., Wang, C., Zhu, H., & Zhou, H. (2018) · Redox Biology · doi:10.1016/j.redox.2018.07.011 · Cited by 353 · see citing works

Melatonin ameliorates myocardial ischemia reperfusion injury through SIRT 3‐dependent regulation of oxidative stress and apoptosis

Zhai, M., Li, B., Duan, W., Jing, L., Zhang, B., Zhang, M., Yu, L., Liu, Z., Yu, B., Ren, K., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12419 · Cited by 351 · see citing works

Sirtuins mediate mammalian metabolic responses to nutrient availability

Chalkiadaki, A., & Guarente, L. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.225 · Cited by 342 · see citing works

Mitochondrial Sirtuin Network Reveals Dynamic SIRT3-Dependent Deacetylation in Response to Membrane Depolarization

Yang, W., Nagasawa, K., Münch, C., Xu, Y., Satterstrom, F. K., Jeong, S., Hayes, S., Jedrychowski, M. P., Vyas, F. S., Zaganjor, E., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.016 · Cited by 341 · see citing works

Ex-527 inhibits Sirtuins by exploiting their unique NAD + -dependent deacetylation mechanism

Gertz, M., Fischer, F. F., Nguyen, G. T. T., Lakshminarasimhan, M., Schutkowski, M., Weyand, M., & Steegborn, C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303628110 · Cited by 320 · see citing works

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 309 · see citing works

Function of the SIRT 3 mitochondrial deacetylase in cellular physiology, cancer, and neurodegenerative disease

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 307 · see citing works

Tyr phosphorylation of PDP1 toggles recruitment between ACAT1 and SIRT3 to regulate the pyruvate dehydrogenase complex

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 · see citing works

SIRT2: Controversy and multiple roles in disease and physiology

Wang, Y., Yang, J., Hong, T., Chen, X., & Cui, L. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100961 · Cited by 288 · see citing works

Sirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation

Jing, E., O’Neill, B. T., Rardin, M. J., Kleinridders, A., Ilkeyeva, O. R., Ussar, S., Bain, J. R., Lee, K. Y., Verdin, E. M., Newgard, C. B., et al. (2013) · Diabetes · doi:10.2337/db12-1650 · Cited by 283 · see citing works

Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly

Rose, G., Dato, S., Altomare, K., Bellizzi, D., Garasto, S., Greco, V, Passarino, G., Feraco, E., Mari, V, Barbi, C., et al. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(03)00209-2 · Cited by 282 · see citing works

SIRT3 interacts with the daf-16 homolog FOXO3a in the Mitochondria, as well as increases FOXO3a Dependent Gene expression

Jacobs, K. M., Pennington, J. D., Bisht, K. S., Aykin‐Burns, N., Kim, H., Mishra, M. V., Sun, L., Nguyen, P., Ahn, B., Leclerc, J., et al. (2008) · International Journal of Biological Sciences · doi:10.7150/ijbs.4.291 · Cited by 282 · see citing works

The Role of p53 in Metabolic Regulation

Puzio-Kuter, A. M. (2011) · Genes & Cancer · doi:10.1177/1947601911409738 · Cited by 273 · see citing works

Mubritinib Targets the Electron Transport Chain Complex I and Reveals the Landscape of OXPHOS Dependency in Acute Myeloid Leukemia

Baccelli, I., Gareau, Y., Lehnertz, B., Gingras, S., Spinella, J.-F., Corneau, S., Mayotte, N., Girard, S., Fréchette, M., Blouin-Chagnon, V., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.06.003 · Cited by 257 · see citing works

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 · see citing works

Melatonin Ameliorates the Progression of Atherosclerosis via Mitophagy Activation and NLRP3 Inflammasome Inhibition

Ma, S., Chen, J., Feng, J. H., Zhang, R., Fan, M., Han, D. H., Li, X., Li, C., Ren, J. T., Wang, Y., et al. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9286458 · Cited by 242 · see citing works

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 232 · see citing works

Sirtuin-3 (SIRT3), a therapeutic target with oncogenic and tumor-suppressive function in cancer

Chen, Y., Fu, L., Wen, X., Wang, X. Y., Liu, J., Cheng, Y., & Huang, J. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.14 · Cited by 231 · see citing works

SIRT3‐dependent GOT2 acetylation status affects the malate–aspartate NADH shuttle activity and pancreatic tumor growth

Yang, H., Zhou, L., Shi, Q., Zhao, Y., Lin, H., Zhang, M., Zhao, S., Yang, Y. A., Ling, Z., Guan, K., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201591041 · Cited by 227 · see citing works

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 · 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

trans-(−)-ε-Viniferin Increases Mitochondrial Sirtuin 3 (SIRT3), Activates AMP-activated Protein Kinase (AMPK), and Protects Cells in Models of Huntington Disease

Fu, J., Jin, J., Cichewicz, R. H., Hageman, S. A., Ellis, T. K., Xiang, L., Peng, Q., Jiang, M., Arbez, N., Hotaling, K., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.382226 · Cited by 213 · 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

Peroxisome Proliferator-activated Receptor-γ Coactivator-1α Controls Transcription of the Sirt3 Gene, an Essential Component of the Thermogenic Brown Adipocyte Phenotype

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 · see citing works

SIRT3 Blocks Aging-Associated Tissue Fibrosis in Mice by Deacetylating and Activating Glycogen Synthase Kinase 3β

Sundaresan, N. R., Bindu, S., Pillai, V. B., Samant, S. A., Pan, Y., Huang, J.-Y., Gupta, M., Nagalingam, R. S., Wolfgeher, D. J., Verdin, E. M., et al. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00586-15 · Cited by 206 · see citing works

Interaction of Sirt3 with OGG1 contributes to repair of mitochondrial DNA and protects from apoptotic cell death under oxidative stress

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

SIRT3 deficiency impairs mitochondrial and contractile function in the heart

Koentges, C., Pfeil, K., Schnick, T., Wiese, S., Dahlbock, R., Cimolai, M. C., Meyer-Steenbuck, M., Cenkerova, K., Hoffmann, M. M., Jaeger, C., et al. (2015) · Basic Research in Cardiology · doi:10.1007/s00395-015-0493-6 · Cited by 201 · see citing works

Discovery of Thieno[3,2-d]pyrimidine-6-carboxamides as Potent Inhibitors of SIRT1, SIRT2, and SIRT3

Disch, J. S., Evindar, G., Chiu, C. H., Blum, C. A., Dai, H., Jin, L., Schuman, E., Lind, K. E., Belyanskaya, S. L., Deng, J., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400204k · Cited by 197 · see citing works

Honokiol, an activator of Sirtuin-3 (SIRT3) preserves mitochondria and protects the heart from doxorubicin-induced cardiomyopathy in mice

Pillai, V. B., Kanwal, A., Fang, Y. H., Sharp, W. W., Samant, S. A., Arbiser, J. L., & Gupta, M. P. (2017) · Oncotarget · doi:10.18632/oncotarget.16133 · Cited by 194 · see citing works

Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis

Wei, Z., Song, J., Wang, G., Cui, X., Zheng, J., Tang, Y., Chen, X., Li, J., Cui, L., Liu, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06812-y · Cited by 188 · see citing works

MicroRNA-195 Regulates Metabolism in Failing Myocardium Via Alterations in Sirtuin 3 Expression and Mitochondrial Protein Acetylation

Zhang, X., Ji, R., Liao, X., Castillero, E., Kennel, P. J., Brunjes, D. L., Franz, M., Möbius‐Winkler, S., Drosatos, K., George, I., et al. (2018) · Circulation · doi:10.1161/circulationaha.117.030486 · Cited by 186 · see citing works

Activation of SIRT3 by resveratrol ameliorates cardiac fibrosis and improves cardiac function via the TGF-β/Smad3 pathway

Chen, T., Li, J., Liu, J., Li, N., Wang, S., Liu, H., Zeng, M., Zhang, Y., & Bu, P. (2014) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00454.2014 · Cited by 178 · see citing works

SIRT1/3 Activation by Resveratrol Attenuates Acute Kidney Injury in a Septic Rat Model

Xu, S., Gao, Y., Zhang, Q., Wei, S., Chen, Z., Dai, X., Zeng, Z., & Zhao, K. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7296092 · Cited by 171 · see citing works

Melatonin improves age-induced fertility decline and attenuates ovarian mitochondrial oxidative stress in mice

Song, C., Peng, W., Yin, S., Zhao, J., Fu, B., Zhang, J., Mao, T., Wu, H., & Zhang, Y. (2016) · Scientific Reports · doi:10.1038/srep35165 · Cited by 170 · see citing works

Melatonin protects against maternal obesity‐associated oxidative stress and meiotic defects in oocytes via the SIRT 3‐ SOD 2‐dependent pathway

Han, L., Wang, H., Li, L., Li, X., Ge, J., Reiter, R. J., & Wang, Q. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12431 · Cited by 168 · see citing works

SIRT3-Dependent Mitochondrial Dynamics Remodeling Contributes to Oxidative Stress-Induced Melanocyte Degeneration in Vitiligo

Yi, X., Guo, W., Shi, Q., Yang, Y., Zhang, W., Chen, X., Kang, P., Chen, J., Cui, T., Ma, J., et al. (2019) · Theranostics · doi:10.7150/thno.30398 · Cited by 167 · see citing works

Therapeutic approaches to Huntington disease: from the bench to the clinic

Caron, N. S., Dorsey, E. R., & Hayden, M. R. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.133 · Cited by 161 · see citing works

SIRT3 protects hepatocytes from oxidative injury by enhancing ROS scavenging and mitochondrial integrity

Liu, J., Li, D., Zhang, T., Tong, Q., Ye, R. D., & Lin, L. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.564 · Cited by 158 · see citing works

Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3

Jin, L., Galonek, H. L., Israelian, K., Choy, W., Morrison, M. C., Xia, Y. X., Wang, X., Xu, Y., Yang, Y., Smith, J. J., et al. (2009) · Protein Science · doi:10.1002/pro.50 · Cited by 153 · see citing works

Amyotrophic Lateral Sclerosis

Tsai, M.-J., Hsu, C.-Y., & Sheu, C. (2017) · New England Journal of Medicine · doi:10.1056/nejmc1710379 · Cited by 152 · see citing works

SIRT3 is crucial for maintaining skeletal muscle insulin action and protects against severe insulin resistance in high-fat-fed mice

Lantier, L., Williams, A. S., Williams, I. M., Yang, K. K., Bracy, D. P., Goelzer, M., James, F. D., Gius, D., & Wasserman, D. H. (2015) · Diabetes · doi:10.2337/db14-1810 · Cited by 151 · see citing works

Small-molecule therapies for cardiac hypertrophy: moving beneath the cell surface

McKinsey, T. A., & Kass, D. A. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2193 · Cited by 151 · see citing works

Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions

Weinert, B. T., Moustafa, T., Iešmantavičius, V., Zechner, R., & Choudhary, C. (2015) · The EMBO Journal · doi:10.15252/embj.201591271 · Cited by 150 · see citing works

Oroxylin A induces dissociation of hexokinase II from the mitochondria and inhibits glycolysis by SIRT3-mediated deacetylation of cyclophilin D in breast carcinoma

Wei, L., Zhou, Y., Dai, Q., Qiao, C., Zhao, L., Hui, H., Lu, N., & Guo, Q.-L. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.131 · Cited by 143 · see citing works

SIRT7-mediated ATM deacetylation is essential for its deactivation and DNA damage repair

Tang, M., Li, Z., Zhang, C., Lu, X., Tu, B., Cao, Z., Li, Y., Chen, Y., Jiang, L., Wang, H., et al. (2019) · Science Advances · doi:10.1126/sciadv.aav1118 · Cited by 142 · see citing works

Non-oncogene Addiction to SIRT3 Plays a Critical Role in Lymphomagenesis

Li, M., Chiang, Y., Lyssiotis, C. A., Teater, M. R., Hong, J. Y., Shen, H., Wang, L., Hu, J., Jing, H., Chen, Z., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.05.002 · Cited by 141 · see citing works

SIRT3: Oncogene and Tumor Suppressor in Cancer

Torrens‐Mas, M., Oliver, J., Roca, P., & Sastre‐Serra, J. (2017) · Cancers · doi:10.3390/cancers9070090 · Cited by 138 · see citing works

Sirtuin 3 Deficiency Accelerates Hypertensive Cardiac Remodeling by Impairing Angiogenesis

Wei, T., Huang, G., Gao, J., Huang, C., Sun, M., Wu, J., Bu, J., & Shen, W. (2017) · Journal of the American Heart Association · doi:10.1161/jaha.117.006114 · Cited by 137 · see citing works

Metabolic regulation by SIRT3: implications for tumorigenesis

Finley, L. W. S., & Haigis, M. C. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.004 · Cited by 130 · see citing works

Sirtuin 3 acts as a negative regulator of autophagy dictating hepatocyte susceptibility to lipotoxicity

Li, S., Dou, X., Ning, H., Song, Q., Wei, W., Zhang, X., Shen, C., Li, J., Sun, C., & Song, Z. (2017) · Hepatology · doi:10.1002/hep.29229 · Cited by 130 · see citing works

High‐fat diet induces cardiac remodelling and dysfunction: assessment of the role played by SIRT 3 loss

Zeng, H., Vaka, V. R., He, X., Booz, G. W., & Chen, J. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12556 · Cited by 129 · see citing works

NMNAT2:HSP90 Complex Mediates Proteostasis in Proteinopathies

Ali, Y., Allen, H. M., Yu, L., Li‐Kroeger, D., Bakhshizadehmahmoudi, D., Hatcher, A., Aubin, C., Xu, J., Bjorklund, N. L., Taglialatela, G., et al. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002472 · Cited by 128 · see citing works

4-hydroxynonenal inhibits SIRT3 via thiol-specific modification

Fritz, K. S., Galligan, J. J., Smathers, R. L., Roede, J. R., Shearn, C. T., Reigan, P., & Petersen, D. R. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100355a · Cited by 127 · see citing works

Development of Pyrazolone and Isoxazol-5-one Cambinol Analogues as Sirtuin Inhibitors

Mahajan, S. S., Scian, M., Sripathy, S. P., Posakony, J., Lao, U., Loe, T. K., Leko, V., Thalhofer, A., Schuler, A. D., Bedalov, A., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4018064 · Cited by 126 · see citing works

Mouse SIRT3 Attenuates Hypertrophy-Related Lipid Accumulation in the Heart through the Deacetylation of LCAD

Chen, T., Liu, J., Li, N., Wang, S., Liu, H., Li, J., Zhang, Y., & Bu, P. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118909 · Cited by 126 · see citing works

NNMT activation can contribute to the development of fatty liver disease by modulating the NAD + metabolism

Komatsu, M., Kanda, T., Urai, H., Kurokochi, A., Kitahama, R., Shigaki, S., Ono, T., Yukioka, H., Hasegawa, K., Tokuyama, H., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-26882-8 · Cited by 126 · see citing works

SIRT3 Protects Rotenone-induced Injury in SH-SY5Y Cells by Promoting Autophagy through the LKB1-AMPK-mTOR Pathway

Zhang, M., Deng, Y., Zhang, J., Liu, J., Li, Y., Su, H., & Qu, Q. (2018) · Aging and Disease · doi:10.14336/ad.2017.0517 · Cited by 125 · see citing works

Sirt3 protects dopaminergic neurons from mitochondrial oxidative stress

Shi, H., Deng, H., Gius, D. R., Schumacker, P. T., Surmeier, D. J., & Ma, Y. C. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx100 · Cited by 122 · see citing works

Endothelial specific SIRT3 deletion impairs glycolysis and angiogenesis and causes diastolic dysfunction

He, X., Zeng, H., Chen, S. T., Roman, R. J., Aschner, J. L., Didion, S. P., & Chen, J.-X. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.09.007 · Cited by 120 · see citing works

LPS causes pericyte loss and microvascular dysfunction via disruption of Sirt3/angiopoietins/Tie-2 and HIF-2α/Notch3 pathways

Zeng, H., He, X., Tuo, Q., Liao, D., Zhang, G., & Chen, J. (2016) · Scientific Reports · doi:10.1038/srep20931 · Cited by 119 · see citing works

Activation of Sirtuin 3 by Silybin Attenuates Mitochondrial Dysfunction in Cisplatin-induced Acute Kidney Injury

Li, Y., Ye, Z.-C., Lai, W., Rao, J., Huang, W., Zhang, X., Yao, Z., & Lou, T. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00178 · Cited by 111 · see citing works

DNA-Encoded Dynamic Chemical Library and Its Applications in Ligand Discovery

Zhou, Y., Li, C., Peng, J., Xie, L., Meng, L. H., Li, Q., Zhang, J., Li, X., Li, X., Huang, X., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09277 · Cited by 110 · see citing works

Sirt3 Deficiency Shortens Life Span and Impairs Cardiac Mitochondrial Function Rescued by Opa1 Gene Transfer

Benigni, A., Cassis, P., Conti, S., Perico, L., Corna, D., Cerullo, D., Zentilin, L., Zoja, C., Perna, A., Lionetti, V., et al. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7703 · Cited by 106 · see citing works

Sirt3 modulate renal ischemia‐reperfusion injury through enhancing mitochondrial fusion and activating the ERK‐OPA1 signaling pathway

Wang, Q., Xu, J., Li, X., Liu, Z., Han, Y., Xu, X., Li, X., Tang, Y., Liu, Y., Tao, Y., et al. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28918 · Cited by 106 · see citing works

The PIK3CA E542K and E545K mutations promote glycolysis and proliferation via induction of the β-catenin/SIRT3 signaling pathway in cervical cancer

Jiang, W., He, T., Liu, S., Zheng, Y., Xiang, L., Pei, X., Wang, Z., & Yang, H. (2018) · Journal of Hematology & Oncology · doi:10.1186/s13045-018-0674-5 · Cited by 105 · see citing works

SIRT3 activator honokiol ameliorates surgery/anesthesia‐induced cognitive decline in mice through anti‐oxidative stress and anti‐inflammatory in hippocampus

Ye, J., Chen, L., Lu, Y., Lei, S., Peng, M., & Xia, Z. (2018) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13053 · Cited by 104 · see citing works

SnapShot: Mammalian Sirtuins

Anderson, K. A., Green, M. F., Huynh, F. K., Wagner, G. R., & Hirschey, M. D. (2014) · Cell · doi:10.1016/j.cell.2014.10.045 · Cited by 100 · see citing works

Old Enzymes, New Tricks: Sirtuins Are NAD+-Dependent De-acylases

Hirschey, M. D. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.10.006 · Cited by 99 · see citing works

SIRT3 deficiency exacerbates p53/Parkin‑mediated mitophagy inhibition and promotes mitochondrial dysfunction: Implication for aged hearts

Li, Y., Ma, Y., Song, L., Yu, L., Zhang, L., Zhang, Y., Xing, Y., Yin, Y., & Ma, H. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3555 · Cited by 98 · see citing works

SIRT3 restricts hepatitis B virus transcription and replication through epigenetic regulation of covalently closed circular DNA involving suppressor of variegation 3‐9 homolog 1 and SET domain containing 1A histone methyltransferases

Ren, J., Hu, J., Cheng, S., Yu, H., Wong, V. K. W., Law, B. Y. K., Yang, Y., Huang, Y., Liu, Y., Chen, W., et al. (2018) · Hepatology · doi:10.1002/hep.29912 · Cited by 98 · see citing works

MicroRNA miR-31 targets SIRT3 to disrupt mitochondrial activity and increase oxidative stress in oral carcinoma

Kao, Y.-Y., Chou, C., Yeh, L.-Y., Chen, Y., Chang, K., Liu, C., Chiang, C. F., & Lin, S. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.04.028 · Cited by 98 · see citing works

NMN Deamidase Delays Wallerian Degeneration and Rescues Axonal Defects Caused by NMNAT2 Deficiency In Vivo

Stefano, M. D., Loreto, A., Orsomando, G., Mori, V., Zamporlini, F., Hulse, R. P., Webster, J., Donaldson, L. F., Gering, M., Raffaelli, N., et al. (2017) · Current Biology · doi:10.1016/j.cub.2017.01.070 · Cited by 97 · see citing works

Loss of SIRT3 Provides Growth Advantage for B Cell Malignancies

Yu, W., Denu, R. A., Krautkramer, K. A., Grindle, K. M., Yang, D. T., Asimakopoulos, F. A., Hematti, P., & Denu, J. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.702076 · Cited by 96 · see citing works

A small molecule activator of SIRT3 promotes deacetylation and activation of manganese superoxide dismutase

Lu, J., Zhang, H., Chen, X., Zou, Y., Li, J., Wang, L., Wu, M., Zang, J., Yu, Y., Zhuang, W., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.07.012 · Cited by 96 · see citing works

Polydatin protects cardiomyocytes against myocardial infarction injury by activating Sirt3

Zhang, M., Zhao, Z., Shen, M., Zhang, Y., Duan, J.-H., Guo, Y., Zhang, D., Hu, J., Lin, J. M., Man, W., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.09.003 · Cited by 95 · see citing works

Sirtuin Inhibition: Strategies, Inhibitors, and Therapeutic Potential

Jiang, Y., Liu, J., Chen, D., Yan, L., & Zheng, W. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.01.009 · Cited by 93 · see citing works

Metformin and insulin impact on clinical outcome in patients with advanced hepatocellular carcinoma receiving sorafenib: Validation study and biological rationale

Gardini, A. C., Faloppi, L., Matteis, S. D., Foschi, F. G., Silvestris, N., Tovoli, F., Palmieri, V. O., Marisi, G., Brunetti, O., Gentilucci, U. V., et al. (2017) · European Journal of Cancer · doi:10.1016/j.ejca.2017.09.003 · Cited by 89 · see citing works

LncRNA TUG1 sponges miR-145 to promote cancer progression and regulate glutamine metabolism via Sirt3/GDH axis

Zeng, B., Ye, H., Chen, J., Cheng, D., Cai, C., Chen, G., Chen, X., Xin, H., Tang, C., & Zeng, J. (2017) · Oncotarget · doi:10.18632/oncotarget.21922 · Cited by 89 · see citing works

Small-Molecule Activator of UNC-51-Like Kinase 1 (ULK1) That Induces Cytoprotective Autophagy for Parkinson’s Disease Treatment

Ouyang, L., Zhang, L., Zhang, S., Yao, D., Zhao, Y., Wang, G., Fu, L., Lei, P., & Liu, B. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01575 · Cited by 89 · see citing works

Sirtuin 3 Activation by Honokiol Decreases Unilateral Ureteral Obstruction-Induced Renal Inflammation and Fibrosis via Regulation of Mitochondrial Dynamics and the Renal NF-κB-TGF-β1/Smad Signaling Pathway

Quan, Y., Park, W. S., Jin, J., Kim, W. B., Park, S. K., & Kang, K. P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020402 · Cited by 89 · see citing works

Sirtuin 3 (SIRT3) maintains bone homeostasis by regulating AMPK-PGC-1β axis in mice

Huh, J.-E., Shin, J. H., Jang, E., Park, S. J., Park, D. R., Ko, R., Seo, D.-H., Kim, H. S., Lee, S. H., Choi, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep22511 · Cited by 86 · see citing works

Inhibition of epithelial cell migration and Src/FAK signaling by SIRT3

Lee, J. J., van de Ven, R. A. H., Zaganjor, E., Ng, M. R., Barakat, A., Demmers, J. J. P. G., Finley, L. W. S., Herrera, K. N. G., Hung, Y. P., Harris, I. S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800440115 · Cited by 86 · see citing works

Suppression of Endothelial-to-Mesenchymal Transition by SIRT (Sirtuin) 3 Alleviated the Development of Hypertensive Renal Injury

Lin, J., Zheng, Y., Zhang, Z.-B., Shen, W., Li, X., Wei, T., Ruan, C., Chen, X.-H., Zhu, D., & Gao, P. (2018) · Hypertension · doi:10.1161/hypertensionaha.118.10482 · Cited by 85 · see citing works

SIRT3 Activation by Dihydromyricetin Suppresses Chondrocytes Degeneration via Maintaining Mitochondrial Homeostasis

Wang, J., Wang, K., Huang, C., Lin, D., Zhou, Y., Wu, Y., Tian, N., Fan, P., Pan, X., Xu, D., et al. (2018) · International Journal of Biological Sciences · doi:10.7150/ijbs.27746 · Cited by 83 · see citing works

Mechanism of Inhibition of the Human Sirtuin Enzyme SIRT3 by Nicotinamide: Computational and Experimental Studies

Guan, X., Lin, P. C., Knoll, E., & Chakrabarti, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107729 · Cited by 82 · see citing works

Inhibition of Mitochondrial Oxidative Damage Improves Reendothelialization Capacity of Endothelial Progenitor Cells via SIRT3 (Sirtuin 3)-Enhanced SOD2 (Superoxide Dismutase 2) Deacetylation in Hypertension

He, J., Liu, X., Chen, S., Wu, F., Sun, J., Zhang, J., Yang, X., Zhang, C., Zhou, Z., Zhang, X., et al. (2019) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.312613 · Cited by 82 · see citing works

SIRT3 Enhances Mesenchymal Stem Cell Longevity and Differentiation

Denu, R. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5841716 · Cited by 79 · see citing works

Profilin-1 suppresses tumorigenicity in pancreatic cancer through regulation of the SIRT3-HIF1α axis

Yao, W., Ji, S., Qin, Y., Yang, J., Xu, J., Zhang, B., Xu, W., Liu, J., Shi, S., Liu, L., et al. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-187 · Cited by 78 · see citing works

Melatonin-mediated upregulation of Sirt3 attenuates sodium fluoride-induced hepatotoxicity by activating the MT1-PI3K/AKT-PGC-1α signaling pathway

Song, C., Zhao, J., Fu, B., Li, D., Mao, T., Peng, W., Wu, H., & Zhang, Y. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.09.005 · Cited by 77 · see citing works

Adjudin protects rodent cochlear hair cells against gentamicin ototoxicity via the SIRT3-ROS pathway

Quan, Y., Li, X., Shao, J., Yin, S., Cheng, C. Y., Xia, W., & Gao, W. (2015) · Scientific Reports · doi:10.1038/srep08181 · Cited by 75 · see citing works

Crystal Structures of Sirt3 Complexes with 4′-Bromo-Resveratrol Reveal Binding Sites and Inhibition Mechanism

Nguyen, G. T. T., Gertz, M., & Steegborn, C. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.09.019 · Cited by 75 · see citing works

Sirt3 is a tumor suppressor in lung adenocarcinoma cells

Xiao, K., Jiang, J., Wang, W., Cao, S., ZHU, L., Zeng, H., Ouyang, R., Zhou, R., & Chen, P. (2013) · Oncology Reports · doi:10.3892/or.2013.2604 · Cited by 72 · see citing works

Daily melatonin protects the endothelial lineage and functional integrity against the aging process, oxidative stress, and toxic environment and restores blood flow in critical limb ischemia area in mice

Lee, F., Sun, C., Sung, P., Chen, K., Chua, S. O., Sheu, J., Chung, S., Chai, H., Chen, Y., Huang, T., et al. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12489 · Cited by 72 · see citing works

SIRT5 impairs aggregation and activation of the signaling adaptor MAVS through catalyzing lysine desuccinylation

Liu, X., Zhu, C., Zha, H., Tang, J., Rong, F., Chen, X., Fan, S., Xu, C., Du, J., Zhu, J., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103285 · Cited by 72 · see citing works

Mitochondrial cytopathies and cardiovascular disease

Dominic, E. A., Ramezani, A., Anker, S. D., et al. (2014) · Heart · doi:10.1136/heartjnl-2013-304657 · Cited by 71 · see citing works

Loss of Fatty Acid Binding Protein 4/aP2 Reduces Macrophage Inflammation Through Activation of SIRT3

Xu, H., Hertzel, A. V., Steen, K. A., & Bernlohr, D. (2016) · Molecular Endocrinology · doi:10.1210/me.2015-1301 · Cited by 70 · see citing works

Oroxylin A promotes PTEN-mediated negative regulation of MDM2 transcription via SIRT3-mediated deacetylation to stabilize p53 and inhibit glycolysis in wt-p53 cancer cells

Zhao, K., Zhou, Y., Qiao, C., Ni, T., Li, Z., Wang, X., Guo, Q., Lu, N., & Wei, L. (2015) · Journal of Hematology & Oncology · doi:10.1186/s13045-015-0137-1 · Cited by 68 · see citing works

Identification of a sirtuin 3 inhibitor that displays selectivity over sirtuin 1 and 2

Galli, U., Mesenzani, O., Coppo, C., Sorba, G., Canonico, P. L., Tron, G. C., & Genazzani, A. A. (2012) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.07.001 · Cited by 68 · see citing works

Sirtuin 3 inhibits hepatocellular carcinoma growth through the glycogen synthase kinase-3β/BCL2-associated X protein-dependent apoptotic pathway

Song, C.-L., Tang, H., Ran, L.-K., Ko, B. C. B., Zhang, Z.-Z., Chen, X. '., Ren, J.-H., Tao, N.-N., Wy, L., Huang, A.-L., et al. (2015) · Oncogene · doi:10.1038/onc.2015.121 · Cited by 68 · see citing works

Enoyl-CoA hydratase-1 regulates mTOR signaling and apoptosis by sensing nutrients

Zhang, Y.-K., Qu, Y.-Y., Lin, Y., Wu, X.-H., Chen, H.-Z., Wang, X., Zhou, K.-Q., Wei, Y., Guo, F., Yao, C.-F., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00489-5 · Cited by 68 · see citing works

SIRT3 deacetylase activity confers chemoresistance in AML via regulation of mitochondrial oxidative phosphorylation

Ma, J., Liu, B., Yu, D., Zuo, Y., Cai, R., Yang, J., & Cheng, J. (2019) · British Journal of Haematology · doi:10.1111/bjh.16044 · Cited by 68 · see citing works

SIRT6, a novel direct transcriptional target of FoxO3a, mediates colon cancer therapy

Zhang, Y., Nie, L., Xu, K., Fu, Y., Zhong, J., Gu, K., & Zhang, L. (2019) · Theranostics · doi:10.7150/thno.29724 · Cited by 67 · see citing works

Sirt3 Deficiency Increased the Vulnerability of Pancreatic Beta Cells to Oxidative Stress-Induced Dysfunction

Zhou, Y., Chung, A. C. K., Fan, R., Lee, H. M., Xu, G., Tomlinson, B., Chan, J. C. N., & Kong, A. P. S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6859 · Cited by 66 · see citing works

miR-494-3p modulates the progression of in vitro and in vivo Parkinson’s disease models by targeting SIRT3

Geng, L., Zhang, T., Liu, W., & Chen, Y. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.03.037 · Cited by 65 · see citing works

SIRT3 regulates cancer cell proliferation through deacetylation of PYCR1 in proline metabolism

Chen, S., Yang, X. P., Yu, M., Wang, Z., Liu, B., Liu, M., Liu, L., Ren, M., Qi, H., Zou, J., et al. (2019) · Neoplasia · doi:10.1016/j.neo.2019.04.008 · Cited by 65 · see citing works

Pyrroloquinoline quinone increases the expression and activity of Sirt1 and -3 genes in HepG2 cells

Zhang, J., Meruvu, S., Bedi, Y. S., Chau, J., Arguelles, A. O., Rucker, R. B., & Choudhury, M. (2015) · Nutrition Research · doi:10.1016/j.nutres.2015.06.014 · Cited by 62 · see citing works

IDH2 inhibition enhances proteasome inhibitor responsiveness in hematological malignancies

Bergaggio, E., Riganti, C., Garaffo, G., Vitale, N., Mereu, E., Bandini, C., Pellegrino, E., Pullano, V., Omedè, P., Todoerti, K., et al. (2018) · Blood · doi:10.1182/blood-2018-05-850826 · Cited by 62 · see citing works

A Novel Sirtuin-3 Inhibitor, LC-0296, Inhibits Cell Survival and Proliferation, and Promotes Apoptosis of Head and Neck Cancer Cells.

Alhazzazi, T. Y., Kamarajan, P., Xu, Y., Ai, T., Chen, L., Verdin, E. M., & Kapila, Y. L. (2016) · PubMed · Cited by 61 · see citing works

Context-dependent activation of SIRT3 is necessary for anchorage-independent survival and metastasis of ovarian cancer cells

Kim, Y. S., Vallur, P. G., Jones, V. M., Worley, B. L., Shimko, S., Shin, D., Crawford, L. C., Chen, C., Aird, K. M., Abraham, T., et al. (2019) · Oncogene · doi:10.1038/s41388-019-1097-7 · Cited by 61 · see citing works

Inhibition of ROS and upregulation of inflammatory cytokines by FoxO3a promotes survival against Salmonella typhimurium

Joseph, J., Ametepe, E. S., Haribabu, N., Agbayani, G., Krishnan, L., Blais, A., & Sad, S. (2016) · Nature Communications · doi:10.1038/ncomms12748 · Cited by 60 · see citing works

NMNAT3 is involved in the protective effect of SIRT3 in Ang II-induced cardiac hypertrophy

Yue, Z., Ma, Y., You, J., Li, Z., Ding, Y.-Q., He, P., Lu, X., Jiang, J., Chen, S., & Liu, P. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.07.006 · Cited by 59 · see citing works

Does Metformin Protect Diabetic Patients from Oxidative Stress and Leukocyte-Endothelium Interactions?

Díaz‐Morales, N., Rovira‐Llopis, S., Bañuls, C., López‐Domènech, S., Escribano‐López, I., Veses, S., Jover, A., Rocha, M., Hernández‐Mijares, A., & Víctor, V. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7122 · Cited by 58 · see citing works

Mechanisms of autophagy and relevant small-molecule compounds for targeted cancer therapy

Zhang, J. C., Wang, G., Zhou, Y., Chen, Y., Ouyang, L., & Liu, B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2759-2 · Cited by 58 · see citing works

Dexmedetomidine attenuation of renal ischaemia-reperfusion injury requires sirtuin 3 activation

Si, Y., Bao, H., Han, L., Chen, L., Zeng, L., Li, J., Xing, Y., & Geng, Y. (2018) · British Journal of Anaesthesia · doi:10.1016/j.bja.2018.07.007 · Cited by 57 · see citing works

Impaired SIRT3 activity mediates cardiac dysfunction in endotoxemia by calpain-dependent disruption of ATP synthesis

Koentges, C., Cimolai, M. C., Pfeil, K., Wolf, D., Marchini, T., Tarkhnishvili, A., Hoffmann, M. M., Odening, K. E., Diehl, P., Mühlen, C. V. Z., et al. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.06.008 · Cited by 56 · see citing works

MicroRNA-421 induces hepatic mitochondrial dysfunction in non-alcoholic fatty liver disease mice by inhibiting sirtuin 3

Cheng, Y., Mai, J., Hou, T., et al. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.04.065 · Cited by 54 · see citing works

Loss of Sirt3 accelerates arterial thrombosis by increasing formation of neutrophil extracellular traps and plasma tissue factor activity

Gaul, D. S., Weber, J., van Tits, L. J., Sluka, S. H. M., Pasterk, L., Reiner, M. F., Calatayud, N., Lohmann, C., Klingenberg, R., Pahla, J., et al. (2018) · Cardiovascular Research · doi:10.1093/cvr/cvy036 · Cited by 54 · see citing works

SIRT3 promotes the invasion and metastasis of cervical cancer cells by regulating fatty acid synthase

Xu, L., Hao, L., Ma, J. Q., Liu, J. K., & Hasim, A. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-019-03644-2 · Cited by 54 · see citing works

Salidroside attenuates endothelial cellular senescence via decreasing the expression of inflammatory cytokines and increasing the expression of SIRT3

Xing, S., Li, J., Chen, L., Yang, Y., He, P., Li, J., & Yang, J. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.12.005 · Cited by 53 · see citing works

A small-molecule activator induces ULK1-modulating autophagy-associated cell death in triple negative breast cancer

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Human sirtuin 3 (SIRT3) deacetylates histone H3 lysine 56 to promote nonhomologous end joining repair

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Skp2 suppresses apoptosis in Rb1-deficient tumours by limiting E2F1 activity

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SIRT3 Deficiency Induces Endothelial Insulin Resistance and Blunts Endothelial-Dependent Vasorelaxation in Mice and Human with Obesity

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Sirtuin 3: A Janus face in cancer (Review)

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Non-mitotic effect of albendazole triggers apoptosis of human leukemia cells via SIRT3/ROS/p38 MAPK/TTP axis-mediated TNF-α upregulation

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NAD + -dependent deacetylase SIRT3 in adipocytes is dispensable for maintaining normal adipose tissue mitochondrial function and whole body metabolism

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Sesamin Protects Against Cardiac Remodeling Via Sirt3/ROS Pathway

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MicroRNA-210 Modulates the Cellular Energy Metabolism Shift During H2O2-Induced Oxidative Stress by Repressing ISCU in H9c2 Cardiomyocytes

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Sirtuin 3 enhanced drug sensitivity of human hepatoma cells through glutathione S-transferase pi 1/JNK signaling pathway

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SIRT3 deacetylates and promotes degradation of P53 in PTEN-defective non-small cell lung cancer

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SIRT3 Inactivation Promotes Acute Kidney Injury Through Elevated Acetylation of SOD2 and p53

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SIRT3 attenuates AngII-induced cardiac fibrosis by inhibiting myofibroblasts transdifferentiation via STAT3-NFATc2 pathway.

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Sirtuin 3 deficiency aggravates contrast-induced acute kidney injury

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LncRNA DYNLRB2-2 inhibits THP-1 macrophage foam cell formation by enhancing autophagy

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4′‐Bromo‐resveratrol, a dual Sirtuin‐1 and Sirtuin‐3 inhibitor, inhibits melanoma cell growth through mitochondrial metabolic reprogramming

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Hepatic SIRT3 Upregulation in Response to Chronic Alcohol Consumption Contributes to Alcoholic Liver Disease in Mice

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A novel metadherinΔ7 splice variant enhances triple negative breast cancer aggressiveness by modulating mitochondrial function via NFĸB-SIRT3 axis

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Alzheimer's Disease

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MiR-708-5p inhibits the progression of pancreatic ductal adenocarcinoma by targeting Sirt3

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Global gene expression profiles in skeletal muscle of monozygotic female twins discordant for hormone replacement therapy

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The expression of SIRT3 in primary hepatocellular carcinoma and the mechanism of its tumor suppressing effects.

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SIRT3 inhibited the formation of calcium oxalate‐induced kidney stones through regulating NRF2/HO‐1 signaling pathway

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Modulation of SIRT3 expression through CDK4/6 enhances the anti-cancer effect of sorafenib in hepatocellular carcinoma cells

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2-Methoxyestradiol Affects Mitochondrial Biogenesis Pathway and Succinate Dehydrogenase Complex Flavoprotein Subunit A in Osteosarcoma Cancer Cells

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ABT737 enhances ovarian cancer cells sensitivity to cisplatin through regulation of mitochondrial fission via Sirt3 activation

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Docking and binding free energy calculations of sirtuin inhibitors

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Protective effects of polydatin against sulfur mustard-induced hepatic injury

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Color-Mediated Contrast Sensitivity in Disabled Readers

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Mitochondrial NOS1 suppresses apoptosis in colon cancer cells through increasing SIRT3 activity

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Celastrol protects human retinal pigment epithelial cells against hydrogen peroxide mediated oxidative stress, autophagy, and apoptosis through sirtuin 3 signal pathway

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Human SIRT3 tripeptidic inhibitors containing Nε-thioacetyl-lysine

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Correction for Papa and Germain, “SirT3 Regulates a Novel Arm of the Mitochondrial Unfolded Protein Response”

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Zinc finger E-box-binding homeobox 1 mediates aerobic glycolysis via suppression of sirtuin 3 in pancreatic cancer

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Context-Dependent Roles for SIRT2 and SIRT3 in Tumor Development Upon Calorie Restriction or High Fat Diet

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Cyclic peptide-based potent and selective SIRT1/2 dual inhibitors harboring Nε-thioacetyl-lysine

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SIRT3 Directs Carbon Traffic in Muscle to Promote Glucose Control

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Understanding the role of histone deacetylase and their inhibitors in neurodegenerative disorders: current targets and future perspective

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Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery

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HIV TAT-mediated microglial senescence: Role of SIRT3-dependent mitochondrial oxidative stress

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Alzheimer Disease: Recent Updates on Apolipoprotein E and Gut Microbiome Mediation of Oxidative Stress, and Prospective Interventional Agents

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Mangiferin alleviates diabetic pulmonary fibrosis in mice via inhibiting endothelial-mesenchymal transition through AMPK/FoxO3/SIRT3 axis

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P6-003 Sirtuin-1はヒト単球のinterleukin-10制御に関与する

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Effect of caloric restriction on the expression of the Sirtuin Proteins

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Expression of sirtuins in ovarian follicles of postnatal mice

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Regulation of SIRT1 and Its Roles in Inflammation

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Neuroprotective mechanisms of SIRT1

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