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SIRT6 protects vascular smooth muscle cells from osteogenic transdifferentiation via Runx2 in chronic kidney disease

Li, W., Feng, W., Su, X., Luo, D., Li, Z., Zhou, Y., Zhu, Y., Zhang, M., Chen, J., Liu, B., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci150051 · Cited by 152 · see citing works

Cold-Inducible SIRT6 Regulates Thermogenesis of Brown and Beige Fat

Yao, L., Cui, X., Chen, Q., Yang, X., Fang, F., Zhang, J., Liu, G., Jin, W., & Chang, Y. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.069 · Cited by 144 · see citing works

Effects of Resveratrol and other Polyphenols on Sirt1: Relevance to Brain Function During Aging

Sarubbo, F., Esteban, S., Miralles, A., & Moranta, D. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170703113212 · Cited by 144 · see citing works

Sirtuins and Insulin Resistance

Zhou, S., Tang, X., & Chen, H. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00748 · Cited by 143 · see citing works

“Cell Membrane Theory of Senescence” and the Role of Bioactive Lipids in Aging, and Aging Associated Diseases and Their Therapeutic Implications

Das, U. N. (2021) · Biomolecules · doi:10.3390/biom11020241 · Cited by 142 · see citing works

SIRT6 exhibits nucleosome-dependent deacetylase activity

Gil, R., Barth, S., Kanfi, Y., & Cohen, H. Y. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt642 · Cited by 133 · see citing works

A review of the sirtuin system, its clinical implications, and the potential role of dietary activators like resveratrol: part 1.

Kelly, G. S. (2010) · PubMed · Cited by 135 · see citing works

Direct evidence of sirtuin downregulation in the liver of non-alcoholic fatty liver disease patients.

Wu, T., Liu, Y., Fu, Y., Liu, X., & Zhou, X.-H. (2014) · PubMed · Cited by 135 · see citing works

Fat-Specific Sirt6 Ablation Sensitizes Mice to High-Fat Diet–Induced Obesity and Insulin Resistance by Inhibiting Lipolysis

Kuang, J., Zhang, Y., Liu, Q., Shen, J., Pu, S., Cheng, S., Chen, L., Li, H., Wu, T., Li, R., et al. (2017) · Diabetes · doi:10.2337/db16-1225 · Cited by 134 · see citing works

Nicotinamide improves glucose metabolism and affects the hepatic NAD-sirtuin pathway in a rodent model of obesity and type 2 diabetes

Yang, S. J., Choi, J. M., Kim, L., Park, S. E., Rhee, E., Lee, W., Oh, K. W., Park, S. W., & Park, C.-Y. (2013) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2013.09.004 · Cited by 131 · see citing works

JNK Phosphorylates SIRT6 to Stimulate DNA Double-Strand Break Repair in Response to Oxidative Stress by Recruiting PARP1 to DNA Breaks

Meter, M. V., Simon, M. A., Tombline, G., May, A., Morello, T. D., Hubbard, B. P., Bredbenner, K., Park, R., Sinclair, D. A., Bohr, V. A., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.006 · Cited by 130 · see citing works

Pathways for Ischemic Cytoprotection: Role of Sirtuins in Caloric Restriction, Resveratrol, and Ischemic Preconditioning

Morris, K. C., Lin, H. W., Thompson, J. W., & Pérez‐Pinzón, M. A. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2010.229 · Cited by 128 · see citing works

MicroRNAs in metabolism and metabolic diseasesPreprint

Rottiers, V., Najafi-Shoushtari, S. H., Kristo, F., Gurumurthy, S., Zhong, L., Li, Y.-X., Cohen, D. E., Gerszten, R. E., Bardeesy, N., Mostoslavsky, R., et al. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.011049 · Cited by 130 · see citing works

CDP-Diacylglycerol Synthases (CDS): Gateway to Phosphatidylinositol and Cardiolipin Synthesis

Blunsom, N. J., & Cockcroft, S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00063 · Cited by 123 · see citing works

Sirt7 promotes adipogenesis in the mouse by inhibiting autocatalytic activation of Sirt1

Fang, J. C., Ianni, A., Smolka, C., Vakhrusheva, O., Nolte, H., Krüger, M., Wietelmann, A., Simonet, N. G., Adrian-Segarra, J. M., Vaquero, A., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706945114 · Cited by 118 · see citing works

The Role of Sirt6 in Obesity and Diabetes

Kuang, J., Chen, L., Tang, Q., Zhang, J., Li, Y., & He, J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00135 · Cited by 122 · see citing works

Mitochondria, the NLRP3 Inflammasome, and Sirtuins in Type 2 Diabetes: New Therapeutic TargetsReviewing Editors: Markus Bachschmid, Dylan Burger, Vittorio Calabrese, Amadou Camara, Lukas Kubala, Giuseppe Poli, and Chandan K. Sen

Rovira‐Llopis, S., Apostolova, N., Bañuls, C., Muntané, J., Rocha, M., & Víctor, V. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7313 · Cited by 120 · see citing works

SIRT1 and SIRT6: The role in aging-related diseases

You, Y., & Liang, W. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166815 · Cited by 120 · see citing works

SIRT6 rescues the age related decline in base excision repair in a PARP1-dependent manner

Xu, Z., Zhang, L., Zhang, W., Du, M., Zhang, H., Jiang, Y., Xu, X., Meter, M. V., Seluanov, A., Gorbunova, V. A., et al. (2015) · Cell Cycle · doi:10.4161/15384101.2014.980641 · Cited by 118 · see citing works

Lithocholic acid binds TULP3 to activate sirtuins and AMPK to slow down ageing

Qu, Q., Chen, Y., Wang, Y., Wang, W., Long, S., Yang, H.-Y., Wu, J., Li, M., Tian, X., Wei, X., et al. (2024) · Nature · doi:10.1038/s41586-024-08348-2 · Cited by 115 · see citing works

Myeloid Sirtuin 6 Deficiency Causes Insulin Resistance in High-Fat Diet–Fed Mice by Eliciting Macrophage Polarization Toward an M1 Phenotype

Lee, Y., Ka, S.-O., Cha, H.-N., Chae, Y.-N., Kim, M.-K., Park, S.-Y., Bae, E. J., & Park, B.-H. (2017) · Diabetes · doi:10.2337/db16-1446 · Cited by 114 · see citing works

Sirtuin 7 in cell proliferation, stress and disease: Rise of the Seventh Sirtuin!

Kiran, S., Anwar, T., Kiran, M., & Ramakrishna, G. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.11.026 · Cited by 112 · see citing works

Multiple pathways of SIRT6 at the crossroads in the control of longevity, cancer, and cardiovascular diseases

Vitiello, M., Zullo, A., Servillo, L., Mancini, F. P., Borriello, A., Giovane, A., Ragione, F. D., D’Onofrio, N., & Balestrieri, M. L. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.10.008 · Cited by 101 · see citing works

Adipose tissue and liver expression of SIRT1, 3, and 6 increase after extensive weight loss in morbid obesity

Moschen, A. R., Wieser, V. E., Gerner, R. R., Bichler, A., Enrich, B., Moser, P. L., Ebenbichler, C. F., Kaser, S., & Tilg, H. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.07.027 · Cited by 103 · see citing works

Adipose tissue NAD+-homeostasis, sirtuins and poly(ADP-ribose) polymerases -important players in mitochondrial metabolism and metabolic health

Jokinen, R., Pirnes-Karhu, S., Pietiläinen, K. H., & Pirinen, E. (2017) · Redox Biology · doi:10.1016/j.redox.2017.02.011 · Cited by 103 · see citing works

SIRT6 in mouse spermatogenesis is modulated by diet-induced obesity

McPherson, N. O., Fullston, T., Mitchell, M., Setchell, B. P., & Lane, M. (2011) · Reproduction Fertility and Development · doi:10.1071/rd10326 · Cited by 101 · see citing works

Sirtuin 6 protects cardiomyocytes from hypertrophy in vitro via inhibition of NF‐κB‐dependent transcriptional activity

Yu, S., Cai, Y., Ye, J., Pi, R., Chen, S., Liu, P., Shen, X., & Ji, Y. H. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.01903.x · Cited by 100 · see citing works

Hepatocyte‐specific sirtuin 6 deletion predisposes to nonalcoholic steatohepatitis by up‐regulation of Bach1, an Nrf2 repressor

Ka, S., Bang, I. H., Bae, E. J., & Park, B. (2017) · The FASEB Journal · doi:10.1096/fj.201700098rr · Cited by 98 · see citing works

SIRT6 Promotes Hepatic Beta-Oxidation via Activation of PPARα

Naiman, S., Huynh, F. K., Gil, R., Glick, Y., Shahar, Y., Touitou, N., Nahum, L., Avivi, M. Y., Roichman, A., Kanfi, Y., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.11.067 · Cited by 98 · see citing works

Sirtuin 6 protects the heart from hypoxic damage

Maksin-Matveev, A., Kanfi, Y., Hochhauser, E., Isak, A., Cohen, H. Y., & Shainberg, A. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.07.013 · Cited by 95 · see citing works

The complex role of SIRT6 in carcinogenesis

Lerrer, B., Gertler, A. A., & Cohen, H. Y. (2015) · Carcinogenesis · doi:10.1093/carcin/bgv167 · Cited by 91 · see citing works

Emerging Therapeutic Potential of SIRT6 Modulators

Fiorentino, F., Mai, A., & Rotili, D. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00601 · Cited by 93 · see citing works

SIRT6 regulates metabolic homeostasis in skeletal muscle through activation of AMPK

Cui, X., Yao, L., Yang, X., Gao, Y., Fang, F., Zhang, J., Wang, Q., & Chang, Y. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00122.2017 · Cited by 90 · see citing works

Sirtuin 6: a review of biological effects and potential therapeutic properties

Beauharnois, J. M., Bolívar, B. E., & Welch, J. T. (2013) · Molecular BioSystems · doi:10.1039/c3mb00001j · Cited by 90 · see citing works

SIRT6 Regulates Osteogenic Differentiation of Rat Bone Marrow Mesenchymal Stem Cells Partially via Suppressing the Nuclear Factor-κB Signaling Pathway

Sun, H., Wu, Y., Fu, D., Liu, Y., & Huang, C. (2014) · Stem Cells · doi:10.1002/stem.1671 · Cited by 89 · see citing works

Sirtuins and the circadian clock: Bridging chromatin and metabolism

Masri, S., & Sassone‐Corsi, P. (2014) · Science Signaling · doi:10.1126/scisignal.2005685 · Cited by 88 · see citing works

SIRT6 Protects Against Liver Fibrosis by Deacetylation and Suppression of SMAD3 in Hepatic Stellate Cells

Zhong, X., Huang, M., Kim, H.-G., Zhang, Y., Chowdhury, K., Cai, W., Saxena, R., Schwabe, R. F., Liangpunsakul, S., & Dong, X. C. (2020) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2020.04.005 · Cited by 90 · see citing works

SIRT6, a protein with many faces

Gertler, A. A., & Cohen, H. Y. (2013) · Biogerontology · doi:10.1007/s10522-013-9478-8 · Cited by 84 · see citing works

SIRT6

Zhong, L., & Mostoslavsky, R. (2010) · Transcription · doi:10.4161/trns.1.1.12143 · Cited by 86 · see citing works

Reciprocal Regulation between SIRT6 and miR-122 Controls Liver Metabolism and Predicts Hepatocarcinoma Prognosis

Elhanati, S., Ben‐Hamo, R., Kanfi, Y., Varvak, A., Glazz, R., Lerrer, B., Efroni, S., & Cohen, H. Y. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.12.023 · Cited by 84 · see citing works

Genomic Instabilities, Cellular Senescence, and Aging: In Vitro, In Vivo and Aging-Like Human Syndromes

Lidzbarsky, G. A., Gutman, D., Shekhidem, H. A., Sharvit, L. E., & Atzmon, G. (2018) · Frontiers in Medicine · doi:10.3389/fmed.2018.00104 · Cited by 80 · see citing works

Biological and catalytic functions of sirtuin 6 as targets for small-molecule modulators

Klein, M. A., & Denu, J. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011438 · Cited by 86 · see citing works

Interplay between sirtuins, MYC and hypoxia-inducible factor in cancer-associated metabolic reprogramming

Zwaans, B. M. M., & Lombard, D. B. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.016287 · Cited by 81 · see citing works

Repairing split ends: SIRT6, mono-ADP ribosylation and DNA repair

Van Meter, M., Mao, Z., Gorbunova, V., & Seluanov, A. (2011) · Aging · doi:10.18632/aging.100389 · Cited by 80 · see citing works

Weight Loss Is Associated With Increased NAD+/SIRT1 Expression But Reduced PARP Activity in White Adipose Tissue

Rappou, E., Jukarainen, S., Rinnankoski‐Tuikka, R., Kaye, S. M., Heinonen, S., Hakkarainen, A., Lundbom, J., Lundbom, N. M. I., Saunavaara, V., Rissanen, A., et al. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-3054 · Cited by 78 · see citing works

Activation of Peroxisome Proliferator-Activated Receptor Gamma by Rosiglitazone Increases Sirt6 Expression and Ameliorates Hepatic Steatosis in Rats

Yang, S. J., Choi, J. M., Chae, S. W., Kim, W. J., Park, S. E., Rhee, E., Lee, W., Oh, K. W., Park, S. W., Kim, S. W., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017057 · Cited by 76 · see citing works

Dietary polyphenols and neurogenesis: Molecular interactions and implication for brain ageing and cognition

Sarubbo, F., Moranta, D., & Pani, G. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.05.011 · Cited by 77 · see citing works

A comprehensive review of Sirtuins: With a major focus on redox homeostasis and metabolism

Shahgaldi, S., & Kahmini, F. R. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119803 · Cited by 79 · see citing works

Pharmacological Sirt6 inhibition improves glucose tolerance in a type 2 diabetes mouse model

Sociali, G., Magnone, M., Ravera, S., Damonte, P., Vigliarolo, T., von Holtey, M., Vellone, V. G., Millo, E., Caffa, I., Cea, M., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201601294r · Cited by 76 · see citing works

Ergothioneine and its congeners: anti-ageing mechanisms and pharmacophore biosynthesis

Chen, L., Zhang, L., Ye, X., Deng, Z., & Zhao, C. (2023) · Protein & Cell · doi:10.1093/procel/pwad048 · Cited by 77 · see citing works

Role of histone acetyltransferases and histone deacetylases in adipocyte differentiation and adipogenesis

Zhou, Y., Peng, J., & Jiang, S. (2014) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2014.03.001 · Cited by 75 · see citing works

Sirtuins in Cancer: a Balancing Act between Genome Stability and Metabolism

Jeong, S. M., & Haigis, M. C. (2015) · Molecules and Cells · doi:10.14348/molcells.2015.0167 · Cited by 74 · see citing works

Energy metabolism disorders and potential therapeutic drugs in heart failure

He, Y., Huang, W., Zhang, C., Chen, L., Xu, R., Li, N., Wang, F., Han, L., Yang, M., & Zhang, D. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.007 · Cited by 73 · see citing works

Sirtuin 6 regulates glucose-stimulated insulin secretion in mouse pancreatic beta cells

Xiong, X., Wang, G., Tao, R., Wu, P., Kono, T., Li, K., Ding, W., Tong, X., Tersey, S. A., Harris, R. A., et al. (2015) · Diabetologia · doi:10.1007/s00125-015-3778-2 · Cited by 72 · see citing works

Sirtuin-6 inhibits cardiac fibroblasts differentiation into myofibroblasts via inactivation of nuclear factor κB signaling

Tian, K., Liu, Z., Wang, J., Xu, S., You, T., & Liu, P. (2014) · Translational research · doi:10.1016/j.trsl.2014.08.008 · Cited by 74 · see citing works

Protein deacetylation by sirtuins: delineating a post-translational regulatory program responsive to nutrient and redox stressors

Bao, J., & Sack, M. N. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0402-y · Cited by 67 · see citing works

Distinctive Roles of Sirtuins on Diabetes, Protective or Detrimental?

Song, J., Yang, B., Jia, X., Li, M., Tan, W. F., Ma, S., Shi, X., & Feng, L. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00724 · Cited by 66 · see citing works

The Role of Sirt6 in Obesity and Diabetes

Kuang, J., Chen, L., Tang, Q., Zhang, J., Li, Y., & He, J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00135 · Cited by 122 · see citing works

Oxidative Stress Induced by Excess of Adiposity Is Related to a Downregulation of Hepatic SIRT6 Expression in Obese Individuals

Carreira, M. C., Izquierdo, A. G., Amil, M., Casanueva, F. F., & Crujeiras, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6256052 · Cited by 30 · see citing works

Sirt6 Deacetylase: A Potential Key Regulator in the Prevention of Obesity, Diabetes and Neurodegenerative Disease

Raj, S., Dsouza, L. A., Singh, S. P., & Kanwal, A. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.598326 · Cited by 30 · see citing works

IMPROVING HEALTHSPAN BY MANIPULATING SIRT6 LEVELS: HOW DOES IT WORK?

Cohen, H. Y. (2017) · Innovation in Aging · doi:10.1093/geroni/igx004.036

Sirt1 protects against high-fat diet-induced metabolic damage

Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschöp, M. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802917105 · Cited by 932 · see citing works