Sirtuin 6—A Key Regulator of Hepatic Lipid Metabolism and Liver Health

Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6

Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637 · see citing works

SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111 · see citing works

SIRT6 Promotes DNA Repair Under Stress by Activating PARP1

Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., Seluanov, A., & Gorbunova, V. (2011) · Science · doi:10.1126/science.1202723 · Cited by 867 · see citing works

SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., et al. (2013) · Nature · doi:10.1038/nature12038 · Cited by 697 · see citing works

Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins

Feldman, J. L., Baeza, J., & Denu, J. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.511261 · Cited by 637 · see citing works

Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase

Liszt, G., Ford, E., Kurtev, M., & Guarente, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413296200 · Cited by 548 · see citing works

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(2010) · doi:10.1016/j.cmet.2010.06.009 · Cited by 512 · see citing works

SIRT6 represses LINE1 retrotransposons by ribosylating KAP1 but this repression fails with stress and age

Van Meter, M., Kashyap, M., Rezazadeh, S., Geneva, A. J., Morello, T. D., Seluanov, A., & Gorbunova, V. (2014) · Nature Communications · doi:10.1038/ncomms6011 · Cited by 455 · see citing works

Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6

Michishita, E., McCord, R. A., Boxer, L. D., Barber, M. F., Hong, T., Gozani, O., & Chua, K. F. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9367 · Cited by 384 · see citing works

The Deacetylase Sirt6 Activates the Acetyltransferase GCN5 and Suppresses Hepatic Gluconeogenesis

Dominy, J. E., Lee, Y., Jedrychowski, M. P., Chim, H., Jurczak, M. J., Camporez, J. P., Ruan, H., Feldman, J., Pierce, K. A., Mostoslavsky, R., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.030 · Cited by 296 · see citing works

Partitioning Circadian Transcription by SIRT6 Leads to Segregated Control of Cellular Metabolism

Masri, S., Rigor, P., Cervantes, M., Ceglia, N., Sebastian, C., Xiao, C., Roqueta-Rivera, M., Deng, C., Osborne, T. F., Mostoslavsky, R., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.050 · Cited by 292 · see citing works

Identification of a cellularly active SIRT6 allosteric activator

Huang, Z., Zhao, J., Deng, W., Chen, Y., Shang, J., Song, K., Zhang, L., Wang, C., Lu, S., Yang, X., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0150-0 · Cited by 277 · see citing works

The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability

Yang, B., Zwaans, B. M. M., Eckersdorff, M., & Lombard, D. B. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9329 · Cited by 254 · see citing works

Liver cancer initiation is controlled by AP-1 through SIRT6-dependent inhibition of survivin

Min, L., Ji, Y., Bakiri, L., Qiu, Z., Cen, J., Chen, X., Chen, L., Scheuch, H., Zheng, H., Qin, L., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2590 · Cited by 246 · see citing works

Tumor suppressor p53 cooperates with SIRT6 to regulate gluconeogenesis by promoting FoxO1 nuclear exclusion

Zhang, P., Tu, B., Wang, H., Cao, Z., Tang, M., Zhang, C., Gu, B., Li, Z., Wang, L., Yang, Y., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411026111 · Cited by 222 · see citing works

SIRT6 deacetylates H3K18ac at pericentric chromatin to prevent mitotic errors and cellular senescence

Tasselli, L., Xi, Y., Zheng, W., Tennen, R. I., Odrowaz, Z., Simeoni, F., Li, W., & Chua, K. F. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3202 · Cited by 213 · see citing works

FoxO3 Transcription Factor and Sirt6 Deacetylase Regulate Low Density Lipoprotein (LDL)-cholesterol Homeostasis via Control of the Proprotein Convertase Subtilisin/Kexin Type 9 (Pcsk9) Gene Expression

Tao, R., Xiong, X., DePinho, R. A., Deng, C., & Dong, X. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.481473 · Cited by 195 · see citing works

SIRT6 deficiency results in developmental retardation in cynomolgus monkeys

Zhang, W., Wan, H., Feng, G., Qu, J. T., Wang, J., Jing, Y., Ren, R., Liu, Z., Zhang, L., Chen, Z., et al. (2018) · Nature · doi:10.1038/s41586-018-0437-z · Cited by 191 · see citing works

Hepatic SREBP-2 and cholesterol biosynthesis are regulated by FoxO3 and Sirt6

Tao, R., Xiong, X., DePinho, R. A., Deng, C., & Dong, X. C. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m039339 · Cited by 179 · see citing works

Structural Basis of Sirtuin 6 Activation by Synthetic Small Molecules

You, W., Rotili, D., Li, T., Kambach, C., Meleshin, M., Schutkowski, M., Chua, K. F., Mai, A., & Steegborn, C. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201610082 · Cited by 170 · see citing works

SIRT6 modulates paclitaxel and epirubicin resistance and survival in breast cancer

Khongkow, M., Olmos, Y., Gong, C., Gomes, A., Monteiro, L. J., Yagüe, E., Cavaco, T. B., Khongkow, P., Man, E. P. S., Laohasinnarong, S., et al. (2013) · Carcinogenesis · doi:10.1093/carcin/bgt098 · Cited by 169 · see citing works

Sirtuin-6–Dependent Genetic And Epigenetic Alterations Are Associated With Poor Clinical Outcome in Hepatocellular Carcinoma Patients

Marquardt, J. U., Fischer, K., Baus, K., Kashyap, A., Ma, S., Krupp, M., Linke, M., Teufel, A., Zechner, U., Strand, D. J., et al. (2013) · Hepatology · doi:10.1002/hep.26413 · Cited by 161 · see citing works

Sirt6 Alleviated Liver Fibrosis by Deacetylating Conserved Lysine 54 on Smad2 in Hepatic Stellate Cells

Zhang, J., Li, Y., Liu, Q., Huang, Y., Li, R., Wu, T., Zhang, Z., Zhou, J., Huang, H., Tang, Q., et al. (2020) · Hepatology · doi:10.1002/hep.31418 · Cited by 158 · see citing works

Multiple Regulatory Layers of SREBP1/2 by SIRT6

Elhanati, S., Kanfi, Y., Varvak, A., Roichman, A., Carmel-Gross, I., Barth, S., Gibor, G., & Cohen, H. Y. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.006 · Cited by 155 · see citing works

SIRT6 deacetylates PKM2 to suppress its nuclear localization and oncogenic functions

Bhardwaj, A., & Das, S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1520045113 · Cited by 154 · see citing works

Progression of Chronic Liver Inflammation and Fibrosis Driven by Activation of c-JUN Signaling in Sirt6 Mutant Mice

Xiao, C., Wang, R.-H., Lahusen, T. J., Park, O., Bertola, A., Maruyama, T., Reynolds, D. A., Chen, Q., Xu, X., Young, H. A., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.415182 · Cited by 152 · see citing works

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

Natural polyphenols as sirtuin 6 modulators

Rahnasto‐Rilla, M., Tyni, J., Huovinen, M., Jarho, E. M., Kulikowicz, T., Ravichandran, S., Bohr, V. A., Ferrucci, L., Lahtela-Kakkonen, M. K., & Moaddel, R. (2018) · Scientific Reports · doi:10.1038/s41598-018-22388-5 · Cited by 149 · see citing works

USP48 Is Upregulated by Mettl14 to Attenuate Hepatocellular Carcinoma via Regulating SIRT6 Stabilization

Du, L., Yang, L., Kang, M., Feng, M., Ren, Y., Dai, H., Wang, Y., Wang, Y., & Tang, B. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-4163 · Cited by 145 · see citing works

Sirt6 attenuates chondrocyte senescence and osteoarthritis progression

Ji, M.-L., Jiang, H., Li, Z., Geng, R., Hu, J. Z., Lin, Y. C., & Lu, J. (2022) · Nature Communications · doi:10.1038/s41467-022-35424-w · Cited by 144 · see citing works

The epigenetic regulator SIRT6 protects the liver from alcohol-induced tissue injury by reducing oxidative stress in mice

Kim, H.-G., Huang, M., Yue, X., Zhang, Y., Zhang, X., Wang, G., Liu, S., Wan, J., Ahmadi, A. R., Sun, Z., et al. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.06.019 · Cited by 137 · see citing works

A novel SIRT6 activator ameliorates neuroinflammation and ischemic brain injury via EZH2/FOXC1 axis

He, T., Shang, J., Gao, C., Guan, X., Chen, Y., Zhu, L., Zhang, L., Zhang, C., Zhang, J., & Pang, T. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.11.002 · Cited by 137 · 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

Functional dissection of SIRT6: Identification of domains that regulate histone deacetylase activity and chromatin localization

Tennen, R. I., Berber, E., & Chua, K. F. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.01.006 · Cited by 132 · see citing works

Discovery of Novel and Selective SIRT6 Inhibitors

Parenti, M. D., Grozio, A., Bauer, I., Galeno, L., Damonte, P., Millo, E., Sociali, G., Franceschi, C., Ballestrero, A., Bruzzone, S., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500487d · Cited by 121 · see citing works

SIRT6 as a key event linking P53 and NRF2 counteracts APAP-induced hepatotoxicity through inhibiting oxidative stress and promoting hepatocyte proliferation

Zhou, Y., Fan, X., Jiao, T., Li, W., Chen, P., Jiang, Y., Sun, J., Chen, Y., Chen, P., Guan, L., et al. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.06.016 · Cited by 121 · see citing works

Ubiquitin‐Specific Peptidase 10 (USP10) Inhibits Hepatic Steatosis, Insulin Resistance, and Inflammation Through Sirt6

Luo, P., Qin, C., Zhu, L., Fang, C., Zhang, Y., Zhang, H., Pei, F., Tian, S., Zhu, X., Gong, J., et al. (2018) · Hepatology · doi:10.1002/hep.30062 · Cited by 120 · 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

SIRT6 Overexpression Potentiates Apoptosis Evasion in Hepatocellular Carcinoma via BCL2-Associated X Protein–Dependent Apoptotic Pathway

Ran, L.-K., Chen, Y., Zhang, Z., Tao, N., Ren, J., Zhou, L., Tang, H., Chen, X., Chen, K., Li, W., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1638 · Cited by 111 · see citing works

Cytoplasmic SIRT6-mediated ACSL5 deacetylation impedes nonalcoholic fatty liver disease by facilitating hepatic fatty acid oxidation

Hou, T., Tian, Y., Cao, Z., Zhang, J., Feng, T., Tao, W., Sun, H., Wen, H., Lu, X., Zhu, Q., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.018 · Cited by 106 · 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 100 · see citing works

Structural basis for the activation and inhibition of Sirtuin 6 by quercetin and its derivatives

You, W., Zheng, W., Weiss, S., Chua, K. F., & Steegborn, C. (2019) · Scientific Reports · doi:10.1038/s41598-019-55654-1 · 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 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

Deacetylation of Caveolin-1 by Sirt6 induces autophagy and retards high glucose-stimulated LDL transcytosis and atherosclerosis formation

Zhao, Y., Jia, X., Yang, X., Bai, X., Lu, Y., Zhu, L., Cheng, W., Shu, M., Zhu, Y., Du, X., et al. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155162 · 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

Sirtuin 6 deficiency transcriptionally up-regulates TGF-β signaling and induces fibrosis in mice

Maity, S., Muhamed, J., Sarikhani, M., Kumar, S. A., Ahamed, F., Spurthi, K. M., Ravi, V., Jain, A., Khan, D., Arathi, B. P., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007212 · Cited by 88 · see citing works

SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation

Zhang, X., Spiegelman, N. A., Nelson, O. D., Jing, H., & Lin, H. (2017) · eLife · doi:10.7554/elife.25158 · Cited by 86 · see citing works

Non-canonical mTORC2 Signaling Regulates Brown Adipocyte Lipid Catabolism through SIRT6-FoxO1

Jung, S. M., Hung, C., Hildebrand, S. R., Sánchez-Gurmaches, J., Martínez-Pastor, B., Gengatharan, J. M., Wallace, M., Mukhopadhyay, D., Calejman, C. M., Luciano, A. K., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.023 · Cited by 86 · 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

Insulin secretion impairment in Sirt6 knockout pancreatic β cells is mediated by suppression of the FoxO1-Pdx1-Glut2 pathway

Song, M.-Y., Wang, J., Ka, S., Bae, E. J., & Park, B. (2016) · Scientific Reports · doi:10.1038/srep30321 · Cited by 85 · see citing works

Structure and chemistry of the Sir2 family of NAD+-dependent histone/protein deactylases

Marmorstein, R. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320904 · Cited by 84 · 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

Sirtuin6 (SIRT6) Promotes the EMT of Hepatocellular Carcinoma by Stimulating Autophagic Degradation of E-Cadherin

Li, H., Jia, L., Wu, F., & Huang, C. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0321 · Cited by 82 · see citing works

Identification of and molecular basis for sirt6 loss-of-function point mutations in cancer

Kugel, S., Feldman, J. L., Klein, M. A., Silberman, D. M., Sebastián, C., Mermel, C., Dobersch, S., Clark, A. R., Getz, G., Denu, J. M., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.022 · Cited by 81 · see citing works

SIRT6 promotes transcription of a subset of NRF2 targets by mono-ADP-ribosylating BAF170

Rezazadeh, S., Yang, D. X., Tombline, G., Simon, M. A., Regan, S. P., Seluanov, A., & Gorbunova, V. A. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz528 · Cited by 80 · see citing works

Mechanotransduction in the pathogenesis of non-alcoholic fatty liver disease

Mitten, E. K., & Baffy, G. (2022) · Journal of Hepatology · doi:10.1016/j.jhep.2022.08.028 · Cited by 80 · see citing works

Quinazolinedione SIRT6 inhibitors sensitize cancer cells to chemotherapeutics

Sociali, G., Galeno, L., Parenti, M. D., Grozio, A., Bauer, I., Passalacqua, M., Boero, S., Donadini, A., Millo, E., Bellotti, M., et al. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.08.024 · Cited by 79 · see citing works

Sirtuin-mediated deacetylation of hnRNP A1 suppresses glycolysis and growth in hepatocellular carcinoma

Yang, H., Zhu, R., Zhao, X., Liu, L., Zhou, Z., Zhao, L., Liang, B., Ma, W., Zhao, J., Liu, J., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0764-z · Cited by 76 · see citing works

Sirtuin 6 in preosteoclasts suppresses age- and estrogen deficiency-related bone loss by stabilizing estrogen receptor α

Moon, Y. J., Zhang, Z., Bang, I. H., Kwon, O. K., Yoon, S., Kim, J. R., Lee, S., Bae, E. J., & Park, B. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0306-9 · Cited by 74 · see citing works

Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors

He, B., Hu, J., Zhang, X., & Lin, H. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob00860j · Cited by 73 · see citing works

Sirt6 suppresses hepatocellular carcinoma cell growth via inhibiting the extracellular signal-regulated kinase signaling pathway

Zhang, Z., & Qin, C. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1879 · Cited by 72 · see citing works

SIRT6 deacetylase activity regulates NAMPT activity and NAD(P)(H) pools in cancer cells

Sociali, G., Grozio, A., Caffa, I., Schuster, S., Becherini, P., Damonte, P., Sturla, L., Fresia, C., Passalacqua, M., Mazzola, F., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800321r · Cited by 68 · see citing works

A rare human centenarian variant of SIRT6 enhances genome stability and interaction with Lamin A

Simon, M. A., Yang, J., Gigas, J., Earley, E. J., Hillpot, E. C., Zhang, L. J., Zagorulya, M., Tombline, G., Gilbert, M. B., Yuen, S. L., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021110393 · Cited by 68 · see citing works

The deacetylase SIRT6 promotes the repair of UV-induced DNA damage by targeting DDB2

Geng, A., Tang, H., Huang, J., Qian, Z. Y., Qin, N., Yao, Y., Xu, Z., Chen, H., Lan, L., Xie, H., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa661 · Cited by 65 · see citing works

SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage

Rizzo, A., Iachettini, S., Salvati, E., Zizza, P., Maresca, C., D’Angelo, C., Benarroch, D., Capolupo, A., Gaudio, F. D., Cosconati, S., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1202 · Cited by 64 · see citing works

SIRT6 regulates the proliferation and apoptosis of hepatocellular carcinoma via the ERK1/2 signaling pathway

Zhang, C., Yu, Y., Huang, Q., & Tang, K. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10398 · Cited by 61 · see citing works

SIRT6 protects against hepatic ischemia/reperfusion injury by inhibiting apoptosis and autophagy related cell death

Zhang, S., Jiang, S., Wang, H., Di, W., Deng, C., Jin, Z., Yi, W., Xiao, X., Nie, Y., & Yang, Y. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.11.005 · Cited by 60 · see citing works

An inactivating mutation in the histone deacetylase SIRT6 causes human perinatal lethalityPreprint

Ferrer, C. M., Alders, M. M., Postma, A. V., Park, S., Klein, M. A., Çetinbaş, M., Pajkrt, E., Glas, A., van Koningsbruggen, S., Christoffels, V. M., et al. (2018) · Genes & Development · doi:10.1101/gad.307330.117 · Cited by 60 · see citing works

Myeloid sirtuin 6 deficiency accelerates experimental rheumatoid arthritis by enhancing macrophage activation and infiltration into synovium

Woo, S. J., Noh, H. S., Lee, N. Y., Cheon, Y., Yi, S. M., Jeon, H. M., Bae, E. J., Lee, S., & Park, B. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.11.005 · Cited by 60 · see citing works

Deacetylation of XBP1s by sirtuin 6 confers resistance to ER stress-induced hepatic steatosis

Bang, I. H., Kwon, O. K., Hao, L., Park, D., Chung, M.-J., Oh, B., Lee, S., Bae, E. J., & Park, B. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0309-0 · Cited by 56 · see citing works

NQO1 potentiates apoptosis evasion and upregulates XIAP via inhibiting proteasome-mediated degradation SIRT6 in hepatocellular carcinoma

Zhou, H., Zeng, H., Yuan, D., Ren, J., Cheng, S., Yu, H., Ren, F., Wang, Q., Qin, Y.-P., Huang, A., et al. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0491-7 · Cited by 56 · see citing works

Molecular Mechanism of Nuclear Tau Accumulation and its Role in Protein Synthesis

Portillo, M., Eremenko, E., Kaluski, S., García-Venzor, A., Onn, L., Stein, D., Slobodnik, Z., Zaretsky, A., Ueberham, U., Einav, M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109035 · Cited by 56 · see citing works

Small-molecule activating SIRT6 elicits therapeutic effects and synergistically promotes anti-tumor activity of vitamin D 3 in colorectal cancer

Shang, J., Zhu, Z., Chen, Y., Song, J., Huang, Y., Song, K., Zhong, J., Xu, X., Wei, J., Wang, C., et al. (2020) · Theranostics · doi:10.7150/thno.44043 · Cited by 55 · see citing works

Trichostatin A inhibits deacetylation of histone H3 and p53 by SIRT6

Wood, M., Rymarchyk, S., Zheng, S. G., & Cen, Y. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.12.009 · Cited by 54 · see citing works

Sirtuin 6 promotes transforming growth factor‐β1/H 2 O 2 / HOC l‐mediated enhancement of hepatocellular carcinoma cell tumorigenicity by suppressing cellular senescence

Feng, X., Luo, J., Liu, M., Yan, W., Zhou, Z., Xia, Y., Tu, W., Li, P., Feng, Z., & Tian, D. (2015) · Cancer Science · doi:10.1111/cas.12632 · Cited by 53 · see citing works

SIRT6 controls hepatic lipogenesis by suppressing LXR, ChREBP, and SREBP1

Zhu, C., Huang, M., Kim, H.-G., Chowdhury, K., Gao, J., Liu, S., Wan, J., Li, W., & Dong, X. C. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166249 · Cited by 50 · see citing works

Ginsenoside Rc Modulates SIRT6-NRF2 Interaction to Alleviate Alcoholic Liver Disease

Pan, Z., Guo, J., Tang, K., Chen, Y., Gong, X., Chen, Y., Zhong, Y., Xiao, X., Duan, S., Cui, T., et al. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c06146 · Cited by 49 · see citing works

SIRT6 Depletion Suppresses Tumor Growth by Promoting Cellular Senescence Induced by DNA Damage in HCC

Lee, N., Ryu, H. G., Kwon, J., Kim, D., Kim, S. R., Wang, H.-J., Kim, K., & Choi, K. Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165835 · Cited by 48 · see citing works

N‐Acylethanolamines Bind to SIRT6

Rahnasto‐Rilla, M., Kokkola, T., Jarho, E. M., Lahtela-Kakkonen, M. K., & Moaddel, R. (2015) · ChemBioChem · doi:10.1002/cbic.201500482 · Cited by 47 · see citing works

EP300 and SIRT1/6 Co-Regulate Lapatinib Sensitivity Via Modulating FOXO3-Acetylation and Activity in Breast Cancer

Mahmud, Z., Gomes, A., Lee, H. J., Aimjongjun, S., Jiramongkol, Y., Yao, S. J., Zona, S., Alasiri, G. A., Gong, G., Yagüe, E., et al. (2019) · Cancers · doi:10.3390/cancers11081067 · Cited by 47 · see citing works

Bone marrow mesenchymal stem cell exosomes suppress phosphate-induced aortic calcification via SIRT6–HMGB1 deacetylation

Wei, W., Guo, X., Gu, L., Jia, J., Yang, M. G., Yuan, W., & Rong, S. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02307-8 · Cited by 47 · see citing works

Capsaicin Attenuates Arterial Calcification Through Promoting SIRT6-Mediated Deacetylation and Degradation of Hif1α (Hypoxic-Inducible Factor-1 Alpha)

Luo, D., Li, W., Xie, C., Yin, L., Su, X., Chen, J., & Huang, H. (2022) · Hypertension · doi:10.1161/hypertensionaha.121.18778 · Cited by 46 · see citing works

SIRT6 inhibitors with salicylate-like structure show immunosuppressive and chemosensitizing effects

Damonte, P., Sociali, G., Parenti, M. D., Soncini, D., Bauer, I., Boero, S., Grozio, A., von Holtey, M., Piacente, F., Becherini, P., et al. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.09.023 · Cited by 45 · see citing works

Chromosomal organization and fluorescence in situ hybridization of the human Sirtuin 6 gene

Mahlknecht, U., Ho, A. D., & Voelter‐Mahlknecht, S. (2006) · International Journal of Oncology · doi:10.3892/ijo.28.2.447 · Cited by 44 · see citing works

SIRT6 mono-ADP ribosylates KDM2A to locally increase H3K36me2 at DNA damage sites to inhibit transcription and promote repair

Rezazadeh, S., Yang, D. X., Biashad, S. A., Firsanov, D., Takasugi, M., Gilbert, M. B., Tombline, G., Bhanu, N. V., Garcia, B. A., Seluanov, A., et al. (2020) · Aging · doi:10.18632/aging.103567 · Cited by 42 · see citing works

Discovery of Potent Small-Molecule SIRT6 Activators: Structure–Activity Relationship and Anti-Pancreatic Ductal Adenocarcinoma Activity

Chen, X., Sun, W., Huang, S., Zhang, H., Lin, G., Li, H., Qiao, J., Li, L., & Yang, S. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01183 · Cited by 40 · see citing works

SIRT6 Suppresses NFATc4 Expression and Activation in Cardiomyocyte Hypertrophy

Li, Z., Zhang, X., Guo, Z., Yao, Z., Wang, P., Li, J., Li, Z., & Liu, P. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01519 · Cited by 37 · see citing works

Overexpression of sirtuin 6 suppresses allergic airway inflammation through deacetylation of GATA3

Jang, H., Gu, S., Lee, S., & Park, B. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.05.019 · Cited by 36 · see citing works

Haploinsufficiency of Trp53 dramatically extends the lifespan of Sirt6-deficient mice

Ghosh, S., Wong, S. K. K., Jiang, Z., Liu, B., Wang, Y., Hao, Q., Gorbunova, V. A., Liu, X., & Zhou, Z. (2018) · eLife · doi:10.7554/elife.32127 · Cited by 36 · see citing works

SIRT6 Is a Target of Regulation by UBE3A That Contributes to Liver Tumorigenesis in an ANXA2-Dependent Manner

Kohli, S., Bhardwaj, A., Kumari, R., & Das, S. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1692 · Cited by 35 · see citing works

Deacetylation of Ku70 by SIRT6 attenuates Bax-mediated apoptosis in hepatocellular carcinoma

Tao, N., Ren, J., Tang, H., Ran, L.-K., Zhou, H., Liu, B., Huang, A., & Chen, J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.02.111 · Cited by 35 · see citing works

Loss of Proximal Tubular Sirtuin 6 Aggravates Unilateral Ureteral Obstruction-Induced Tubulointerstitial Inflammation and Fibrosis by Regulation of β-Catenin Acetylation

Jin, J., Li, W., Wang, T., Park, B., Park, S. K., & Kang, K. P. (2022) · Cells · doi:10.3390/cells11091477 · Cited by 32 · see citing works

Quercetin inhibited the proliferation and invasion of hepatoblastoma cells through facilitating SIRT6-medicated FZD4 silence

Liu, T., Li, Z., & Tian, F. (2021) · Human & Experimental Toxicology · doi:10.1177/09603271211030558 · Cited by 31 · see citing works

ERRγ suppression by Sirt6 alleviates cholestatic liver injury and fibrosis

Hao, L., Bang, I. H., Wang, J., Mao, Y., Yang, J. D., Na, S., Seo, J. K., Choi, H., Bae, E. J., & Park, B. (2020) · JCI Insight · doi:10.1172/jci.insight.137566 · Cited by 29 · see citing works

Hepatocyte-specific Sirt6 deficiency impairs ketogenesis

Chen, L., Liu, Q., Tang, Q., Kuang, J., Li, H., Pu, S., Wu, T., Yang, X., Li, R., Zhang, J., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005309 · Cited by 28 · see citing works

Sirt6 deacetylase activity regulates circadian rhythms via Per2

Sun, S., Liu, Z., Feng, Y., Shi, L., Cao, X., Cai, Y., & Liu, B. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.01.143 · Cited by 27 · see citing works

SIRT6 Protects Against Myocardial Ischemia–Reperfusion Injury by Attenuating Aging-Related CHMP2B Accumulation

Li, X., Liu, L., Jiang, W., Liu, M., Wang, Y., Ma, H., Mu, N., & Wang, H. (2022) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-021-10184-y · Cited by 27 · see citing works

Hepatic SIRT6 Modulates Transcriptional Activities of FXR to Alleviate Acetaminophen-induced Hepatotoxicity

Liu, C., Pan, Z., Wu, Z.-L., Tang, K., Zhong, Y., Chen, Y., Xiao, X., Guo, J., Duan, S., Cui, T., et al. (2022) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2022.04.011 · Cited by 25 · see citing works

Sirtuin 6 attenuates angiotensin II-induced vascular adventitial aging in rat aortae by suppressing the NF-κB pathway

Liu, X., Jiang, D., Huang, W. L., Teng, P., Zhang, H., Wei, C., Cai, X., & Liang, Y. (2021) · Hypertension Research · doi:10.1038/s41440-021-00631-3 · Cited by 25 · see citing works

Histone deacetylase SIRT6 regulates chemosensitivity in liver cancer cells via modulation of FOXO3 activity

Hu, J., Deng, F., Hu, X., Zhang, W., Xiao-chen, Z., & Tian, X. (2018) · Oncology Reports · doi:10.3892/or.2018.6770 · Cited by 23 · see citing works

Statin suppresses sirtuin 6 through miR-495, increasing FoxO1-dependent hepatic gluconeogenesis

Shi, M. Y., Bang, I. H., Han, C. Y., Lee, D. H., Park, B., & Bae, E. J. (2020) · Theranostics · doi:10.7150/thno.49770 · Cited by 23 · see citing works

Acetylation of ELF5 suppresses breast cancer progression by promoting its degradation and targeting CCND1

Li, X., Li, S., Li, B., Li, Y., Aman, S., Xia, K., Yang, Y., Ahmad, B., & Wu, H. (2021) · npj Precision Oncology · doi:10.1038/s41698-021-00158-3 · Cited by 20 · see citing works

Nitro-fatty acids as activators of hSIRT6 deacetylase activity

Carreño, M., Bresque, M., Machado, M. R., Santos, L., Durán, R., Vitturi, D. A., Escande, C., & Denicola, A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014883 · Cited by 20 · see citing works

Sirtuin 6 supra‐physiological overexpression in hypothalamic pro‐opiomelanocortin neurons promotes obesity via the hypothalamus‐adipose axis

Tang, Q., Liu, Q., Yang, X., Wu, T., Huang, C., Zhang, J., Zhang, Z., Zhang, G., Zhao, Y., Zhou, J., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202002607 · Cited by 20 · see citing works

Sirtuin 6 ameliorates alcohol-induced liver injury by reducing endoplasmic reticulum stress in mice

Yue, X., Xu, L., Zhang, X., Yang, C., Wang, Q., & Xiong, X. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.01.061 · Cited by 19 · see citing works

Sirtuin 6 protects against hepatic fibrogenesis by suppressing the YAP and TAZ function

Chowdhury, K., Huang, M., Kim, H.-G., & Dong, X. C. (2022) · The FASEB Journal · doi:10.1096/fj.202200522r · Cited by 19 · see citing works

Design, synthesis, and pharmacological evaluations of pyrrolo[1,2-a]quinoxaline-based derivatives as potent and selective sirt6 activators

Xu, J., Shi, S., Liu, G., Xie, X., Li, J., Bolinger, A. A., Chen, H., Zhang, W., Shi, P., Liu, H., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114998 · Cited by 19 · see citing works

Protective effects of SIRT6 against lipopolysaccharide (LPS) are mediated by deacetylation of Ku70

Zhang, L., Bai, L., Ren, Q., Sun, G., & Si, Y.-J. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.07.009 · Cited by 18 · see citing works

Discovery of 5-(4-methylpiperazin-1-yl)-2-nitroaniline derivatives as a new class of SIRT6 inhibitors

Sun, W., Chen, X., Huang, S., Li, W., Tian, C., Yang, S., & Li, L. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127215 · Cited by 17 · see citing works

SIRT6 Promotes Osteogenic Differentiation of Adipose-Derived Mesenchymal Stem Cells Through Antagonizing DNMT1

Jia, B., Chen, J., Wang, Q. L., Sun, X., Han, J., Guastaldi, F. P. S., Xiang, S., Ye, Q., & He, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.648627 · Cited by 17 · see citing works

Human centenarian–associated SIRT6 mutants modulate hepatocyte metabolism and collagen deposition in multilineage hepatic 3D spheroids

Fröhlich, J., Raffaele, M., Skálová, H., Leire, E., Pata, I., Pata, P., Gorbunova, V. A., & Vinciguerra, M. (2022) · GeroScience · doi:10.1007/s11357-022-00713-1 · Cited by 16 · see citing works

SIRT6 mediates MRTF-A deacetylation in vascular endothelial cells to antagonize oxLDL-induced ICAM-1 transcription

Huang, S., Shao, T., Liu, H. S., Wang, Q., Li, T., & Zhao, Q. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-00903-y · Cited by 15 · see citing works

SIRT6 regulates endothelium-dependent relaxation by modulating nitric oxide synthase 3 (NOS3)

Wang, J., Liu, Z., Lü, J., Zou, J., Ye, W., Li, H., Gao, S., & Liu, P. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115439 · Cited by 14 · see citing works

Long intergenic noncoding RNA smad7 (Linc‐smad7) promotes the epithelial‐mesenchymal transition of HCC by targeting the miR‑125b/SIRT6 axis

Han, L., Jia, L., & Zan, Y. (2020) · Cancer Medicine · doi:10.1002/cam4.3515 · Cited by 14 · see citing works

Hepatic SIRT6 deficit promotes liver tumorigenesis in the mice models

Wang, M., Lan, L., Yang, F., Jiang, S., Xu, H., Zhang, C., Zhou, G., Xia, H., & Xia, J. (2020) · Genes & Diseases · doi:10.1016/j.gendis.2020.08.007 · Cited by 13 · see citing works

ATL I, Acts as a SIRT6 Activator to Alleviate Hepatic Steatosis in Mice via Suppression of NLRP3 Inflammasome Formation

Kong, D., Mai, Z., Chen, Y., Luo, L., Liu, H., Le, Z., Huang, R., Wang, S., Chen, R., Zhou, H., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15121526 · Cited by 11 · see citing works

Impaired reciprocal regulation between SIRT6 and TGF‐β signaling in fatty liver

Xiang, X., Ohshiro, K., Zaidi, S., Yang, X., Bhowmick, K., Vegesna, A. K., Bernstein, D., Crawford, J. M., Mishra, B., Latham, P. S., et al. (2022) · The FASEB Journal · doi:10.1096/fj.202101518r · Cited by 10 · see citing works

Metformin alleviates HFD-induced oxidative stress in hepatocyte via activating SIRT6/PGC-1α/ENDOG signaling

Gao, S., Yang, Q., Liu, Z., Kong, W., Chen, J., Xie, L., Peng, Y., Bao, M., Bian, X., Zhang, Y., et al. (2022) · Clinical Science · doi:10.1042/cs20220242 · Cited by 9 · see citing works

The mechanism of radiotherapy for lung adenocarcinoma in promoting protein SIRT6-mediated deacetylation of RBBP8 to enhance the sensitivity of targeted therapy

Wang, J., Sheng, Z., Dong, Z., Wu, Q., & Cai, Y. (2022) · International Journal of Immunopathology and Pharmacology · doi:10.1177/03946320221130727 · Cited by 7 · see citing works

Reciprocal interaction between SIRT6 and APC/C regulates genomic stability

Wang, H., Feng, K., Wang, Q., & Deng, H. (2021) · Scientific Reports · doi:10.1038/s41598-021-93684-w · Cited by 6 · see citing works

Macrophage plasticity: signaling pathways, tissue repair, and regeneration

Yan, L., Wang, J., Cai, X., Liou, Y., Shen, H., Hao, J., Huang, C., Luo, G., & He, W. (2024) · MedComm · doi:10.1002/mco2.658 · Cited by 396 · see citing works

Targeting proprotein convertase subtilisin/kexin type 9 (PCSK9): From bench to bedside

Bao, X., Liang, Y., Chang, H., Cai, T., Feng, B., Gordon, K., Zhu, Y., Shi, H., He, Y., & Xie, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01690-3 · Cited by 187 · see citing works

Macrophage in liver Fibrosis: Identities and mechanisms

Wang, Z., Du, K., Jin, N., Tang, B., & Zhang, W. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110357 · Cited by 114 · see citing works

Targeting PPARs for therapy of atherosclerosis: A review

Miao, M., Wang, X., Liu, T., Li, Y., Yu, W., Yang, T.-M., & Guo, S. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125008 · Cited by 40 · see citing works

Discussion on structure classification and regulation function of histone deacetylase and their inhibitor

Han, H., Feng, X., He, T., Wu, Y., He, T., Yue, Z., & Zhou, W. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14366 · Cited by 39 · see citing works

Long-chain acyl-CoA synthetases: biological functions, diseases and therapeutic targets

Deng, X., Luo, Y., Gao, Y., & Wu, T. (2025) · Molecular Biomedicine · doi:10.1186/s43556-025-00366-4 · Cited by 39 · see citing works

TGF-β inhibitors: the future for prevention and treatment of liver fibrosis?

Wang, W., Gao, Y., Chen, Y., Cheng, M., Sang, Y., Wei, L., Dai, R., Wang, Y., & Zhang, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1583616 · Cited by 35 · see citing works

Sirtuins in macrophage immune metabolism: A novel target for cardiovascular disorders

Xu, C.-Q., Li, J., Liang, Z., Zhong, Y.-L., Zhang, Z., Hu, X., Cao, Y., & Chen, J. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128270 · Cited by 32 · see citing works

A promising therapy for fatty liver disease: PCSK9 inhibitors

Han, L., Wu, L., Yin, Q., Li, L., Zheng, X., Du, S., Huang, X., Bai, L., Wang, Y., & Bian, Y. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.155505 · Cited by 31 · see citing works

SIRT6 in health and diseases: From molecular mechanisms to therapeutic prospects

Chen, R., Li, Y., Wu, J., Wang, Y., Song, W., Shao, D., Gao, W., & Yu, H. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107984 · Cited by 24 · see citing works

Loss of PPARα function promotes epigenetic dysregulation of lipid homeostasis driving ferroptosis and pyroptosis lipotoxicity in metabolic dysfunction associated Steatotic liver disease (MASLD)

Theys, C., Vanderhaeghen, T., Dijck, E. V., Peleman, C., Scheepers, A., Ibrahim, J., Mateiu, L. M., Timmermans, S., Berghe, T. V., Francque, S., et al. (2024) · Frontiers in Molecular Medicine · doi:10.3389/fmmed.2023.1283170 · Cited by 23 · see citing works

Recent Advances in the Discovery of SIRT1/2 Inhibitors via Computational Methods: A Perspective

Scarano, N., Brullo, C., Musumeci, F., Millo, E., Bruzzone, S., Schenone, S., & Cichero, E. (2024) · Pharmaceuticals · doi:10.3390/ph17050601 · Cited by 18 · see citing works

Effects of Portulaca oleracea (purslane) on liver function tests, metabolic profile, oxidative stress and inflammatory biomarkers in patients with non-alcoholic fatty liver disease: a randomized, double-blind clinical trial

Milkarizi, N., Barghchi, H., Belyani, S., Bahari, H., Rajabzade, F., Ostad, A. N., Goshayeshi, L., Nematy, M., & Askari, V. R. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1371137 · Cited by 18 · see citing works

The role of mammalian Sirtuin 6 in cardiovascular diseases and diabetes mellitus

Wu, K., Wang, Y., Liu, R., Wang, H., & Tao, R. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1207133 · Cited by 16 · see citing works

Inulin alleviates atherosclerosis through improving lipid metabolism, inflammation, and gut microbiota in ApoE-knockout mice: the short-chain is more efficacious

Zhang, K., Zeng, Y., Li, J., Huang, Y., Zhang, N., Gong, Y., Xiao, K., Chen, J., Chen, T., Qiu, H., et al. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1445528 · Cited by 16 · see citing works

MiR-34a-5p suppresses cutaneous squamous cell carcinoma progression by targeting SIRT6

Chen, S., Yuan, M., Chen, H., Wu, T., Wu, T., Zhang, D., Xu, M., & Shi, J. (2024) · Archives of Dermatological Research · doi:10.1007/s00403-024-03106-w · Cited by 15 · see citing works

Carboxylic acid metabolism in cancer: Mechanisms, microenvironment interactions, and therapeutic opportunities

Bian, X., Zhuo, Y., Zhou, L., Zhu, Y. Z., Li, N., & Wu, J. (2025) · Metabolism · doi:10.1016/j.metabol.2025.156334 · Cited by 13 · see citing works

Lipid metabolism: a molecular switch to control inflammation

Cheng, S., Xie, L., Wu, J., & Yang, F. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116294 · Cited by 13 · see citing works

Impaired SUMOylation of FoxA1 promotes nonalcoholic fatty liver disease through down-regulation of Sirt6

Zou, D., Liao, J., Xiao, M., Liu, L., Dai, D., & Xu, M. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07054-1 · Cited by 11 · see citing works

ErTao decoction alleviates liver fibrosis by suppressing STING-mediated macrophages and NLRP3 inflammasome activation

Jia, H., Li, J., Chen, X., Liu, Z., Wu, C., Liu, C., Zhang, J., Luo, M., Huang, M., Huang, S., et al. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.156489 · Cited by 11 · see citing works

SIRT6 in Regulation of Mitochondrial Damage and Associated Cardiac Dysfunctions: A Possible Therapeutic Target for CVDs

Divya, K. P., Kanwar, N., Anuranjana, P. V., Kumar, G., Beegum, F., George, K. T., Kumar, N., Nandakumar, K., & Kanwal, A. (2024) · Cardiovascular Toxicology · doi:10.1007/s12012-024-09858-1 · Cited by 11 · see citing works

MDL-800 protects against inflammatory and metabolic dysfunction: role of SIRT6 in the cross-regulation of NFκB, AMPK, and PPAR signaling in rats

Hamad, R. S., Hasan, W. A., Saber, S., Elmorsy, E. A., Farrag, A. A. M., Anwer, H. M., AbuoHashish, N. A., Hellal, D., Elmetwally, A. A.-M., Elmowafy, R., et al. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115452 · Cited by 10 · see citing works

The role of ubiquitination and deubiquitination in the pathogenesis of non-alcoholic fatty liver disease

Zhang, L., Liu, S., Zhao, Q., Liu, X., Zhang, Q., Liu, M., & Zhao, W. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1535362 · Cited by 9 · see citing works

GB1a Activates SIRT6 to Regulate Lipid Metabolism in Mouse Primary Hepatocytes

Sun, Y., Zheng, C., Li, T., He, X., Yang, F., Guo, W., Song, J., Gao, Y., Deng, C., & Huang, X. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119540 · Cited by 9 · see citing works

Friend or foe? The role of SIRT6 on macrophage polarized to M2 subtype in acute kidney injury to chronic kidney disease

Xiaoqin, G., Liu, X., Han, Z., Liao, H., & Li, R. (2025) · Renal Failure · doi:10.1080/0886022x.2025.2482121 · Cited by 8 · see citing works

Swertianin Suppresses M1 Macrophage Polarization and Inflammation in Metabolic Dysfunction-Associated Fatty Liver Disease via PPARG Activation

Xia, J., Xiong, W., Yang, C., Tan, Y. C., Peng, X., & Wang, W. (2025) · Genes · doi:10.3390/genes16060693 · Cited by 7 · see citing works

SIRT6 Is a Key Regulator of Pancreatic β-Cell Survival and Function During Aging

Park, J., Lokuge, S. D., Huang, M., Wang, S., Liu, S., Liang, J., Katturajan, R., Marakovits, C. N., Yang, Z., Wan, J., et al. (2025) · Diabetes · doi:10.2337/db25-0116 · Cited by 7 · see citing works

Advancing the Metabolic Dysfunction-Associated Steatotic Liver Disease Proteome: A Post-Translational Outlook

Chowdhury, K., Das, D., & Huang, M. (2025) · Genes · doi:10.3390/genes16030334 · Cited by 7 · see citing works

The SIRT6 Activator MDL-800 Inhibits PPARα and Fatty acid Oxidation-Related Gene Expression in Hepatocytes

Kim, Y. S., Lim, H., Cho, Y. E., & Hwang, S. (2025) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2024.251 · Cited by 6 · see citing works

PKM2 Drives Lactate-mediated Fibrosis in Liver Transplantation

Liu, J.-Y., Liao, W., Chen, Z.-Y., Liu, T., Wang, R., Gong, J.-P., Xu, X.-S., & Wu, H. (2025) · Transplantation · doi:10.1097/tp.0000000000005461 · Cited by 6 · see citing works

NAD+ enhancers as therapeutic agents in the cardiorenal axis

Marin-Blazquez, M., Rovira, J., Ramírez-Bajo, M. J., Perez, R. Z., & Rabadán-Ros, R. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01903-4 · Cited by 6 · see citing works

Sirtuin 6-driven ASC deacetylation confers hepatoprotection: A promising approach to inflammasome inhibition in experimental NASH

Hamad, R. S., Hasan, W. A., Elmorsy, E. A., Farrag, A. A. M., Abdelaziz, M. A., Alalawy, A. I., Alsirhani, A. M., Dawsari, M. M. A., El-kott, A. F., AlShehri, M. A., et al. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.178202 · Cited by 5 · see citing works

Senkyunolide A mitigates lipid deposition in hyperlipidemic hepatocytes through SIRT6-mediated suppression of oxidative stress and fetuin-A

Ko, J. H., Jung, T. W., Pyo, M. K., Lim, D. S., Gwon, H. J., El‐Aty, A. M. A., Yağan, R., Shin, J. W., Lee, M. Y., Song, J.-H., et al. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152046 · Cited by 4 · see citing works

Uvaol ameliorates lipid deposition in hyperlipidemic hepatocytes by suppressing protein-tyrosine phosphatase 1B/ER stress signaling

Gwon, H. J., Chung, Y., Lim, D. S., Cho, W., Choi, S. W., El‐Aty, A. M. A., Song, J.-H., Shin, Y. K., Jeong, J. H., & Jung, T. W. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150387 · Cited by 4 · see citing works

Modulation of SIRT6 related signaling pathways of p-AKT/mTOR and NRF2/HO-1 by memantine contributes to curbing the progression of tamoxifen/HFD-induced MASH in rats

Ezz-Eldin, Y. M., Ewees, M. G., Khalaf, M. M., & Azouz, A. A. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.177069 · Cited by 3 · see citing works

Effects of POPs-induced SIRT6 alteration on intestinal mucosal barrier function: A comprehensive review

Chen, G., Huang, T., Dai, Y., Huo, X., & Xu, X. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.117705 · Cited by 3 · see citing works

NAD + in fatty liver disease: mechanistic insights and associated targets

Guo, Y.-X., Wang, Y., Wu, S., Wang, Y., & Liu, X. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-025-10106-7 · Cited by 3 · see citing works

Reprogramming tumour‐associated macrophages in breast cancer via si‐FOXM1‐loaded lipid nanoparticles enhances immune checkpoint inhibitor efficacy

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miR‐338‐3p Targets SIRT6 to Inhibit Liver Cancer Malignancy and Paclitaxel Resistance

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