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Sirtuin 1 (SIRT1) Protein Degradation in Response to Persistent c-Jun N-terminal Kinase 1 (JNK1) Activation Contributes to Hepatic Steatosis in Obesity
Open accessAbstract
SIRT1 is involved in the pathogenesis of obesity, diabetes, and aging. However, it is not clear how SIRT1 activity is regulated by intracellular kinases in cells. In this study, we investigated SIRT1 phosphorylation and protein degradation in response to JNK1 activation in obese mice. Mouse SIRT1 is phosphorylated by JNK1 at Ser-46 (Ser-47 in human SIRT1), which is one of the four potential residues targeted by JNK1. The phosphorylation induces a brief activation of SIRT1 function and degradation of SIRT1 thereafter by the proteasome. Ubiquitination occurs in SIRT1 protein after the phosphorylation. Mutation of Ser-46 to alanine prevents the phosphorylation, ubiquitination, and degradation. In vivo, SIRT1 undergoes an extensive degradation in hepatocytes in obesity as a consequence of persistent activation of JNK1. The degradation leads to inhibition of SIRT1 function, which contributes to development of hepatic steatosis. The degradation disappears in obesity when JNK1 is inactivated in mice. JNK2 exhibits an opposite activity in the regulation of SIRT1 degradation. The JNK1-SIRT1 pathway provides a new molecular mechanism for the pathogenesis of hepatic steatosis in obesity.
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“Furthermore, persistent activation of JNK and/or p38K is positively associated with various liver diseases such as steatohepatitis and I/R injury [122], [123], [124], [125], suggesting the clinical importance of JNK and p38K in human disease states, as reviewed [126].”
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Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290
Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057
Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
Self-citationNutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
Özcan, U., Yilmaz, E., Özcan, L., Furuhashi, M., Vaillancourt, E., Smith, R. O., Görgün, C. Z., & Hotamisligil, G. S. (2006) · Science · doi:10.1126/science.1128294 · Cited by 2,413
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924
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Yang, Y., Liu, Y., Wang, Y., Chao, Y., Zhang, J., Jia, Y., Tie, J., & Hu, D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.831168 · Cited by 737
Self-citationJNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships
Zeke, A., Misheva, M., Reményi, A., & Bogoyevitch, M. A. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00043-14 · Cited by 552
Redox regulation of SIRT1 in inflammation and cellular senescence
Hwang, J.-W., Yao, H., Caito, S., Sundar, I. K., & Rahman, I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.015 · Cited by 503
Calorie restriction and sirtuins revisited
Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464
Crosstalk between Oxidative Stress and SIRT1: Impact on the Aging Process
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14023834 · Cited by 463
Xiong, H., Ni, Z., He, J., Jiang, S.-W., Li, X., He, J., Gong, W., Zheng, L., Chen, S., Li, B., et al. (2017) · Oncogene · doi:10.1038/onc.2016.521 · Cited by 362
Chalkiadaki, A., & Guarente, L. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.003 · Cited by 356
Castro, R. E., Ferreira, D. M. S., Afonso, M. B., Borralho, P. M., Machado, M. V., Cortez‐Pinto, H., & Rodrigues, C. M. P. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.08.008 · Cited by 351
Regulation of SIRT1 in aging: Roles in mitochondrial function and biogenesis
Yuan, Y., Cruzat, V. F., Newsholme, P., Cheng, J., Chen, Y., & Lu, Y. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.02.003 · Cited by 306
Hong, S., Moreno‐Navarrete, J. M., Wei, X., Kikukawa, Y., Tzameli, I., Prasad, D., Lee, Y., Asara, J. M., Fernández‐Real, J. M., Maratos–Flier, E., et al. (2015) · Nature Medicine · doi:10.1038/nm.3882 · Cited by 260
Sorting out functions of sirtuins in cancer
Roth, M., & Chen, W. (2013) · Oncogene · doi:10.1038/onc.2013.120 · Cited by 242
New Insights for Oxidative Stress and Diabetes Mellitus
Maiese, K. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/875961 · Cited by 230
Sung, K., Jeong, W. S., Wild, S. H., & Byrne, C. D. (2012) · Diabetes Care · doi:10.2337/dc11-1853 · Cited by 217
Sirtuins' modulation of autophagy
Ng, F., & Tang, B. L. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24399 · Cited by 198
Resolution of Fatty Liver and Risk of Incident Diabetes
Sung, K., Wild, S. H., & Byrne, C. D. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-1519 · Cited by 172
Understanding the Function of Mammalian Sirtuins and Protein Lysine Acylation
Wang, M., & Lin, H. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-082520-125411 · Cited by 174
The ways and means that fine tune Sirt1 activity
Revollo, J. R., & Li, X. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.12.004 · Cited by 166
Cellular Stresses and Stress Responses in the Pathogenesis of Insulin Resistance
Onyango, A. N. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/4321714 · Cited by 168
Shen, B., Zhao, C., Wang, Y., Peng, Y., Cheng, J., Li, Z., Wu, L., Jin, M., & Feng, H. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14293 · Cited by 157
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Ganesan, R., Hos, N. J., Gutiérrez, S., Fischer, J., Stepek, J. M., Daglidu, E., Krönke, M., & Robinson, N. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006227 · Cited by 143
Mechanisms of intrahepatic triglyceride accumulation
Ress, C. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i4.1664 · Cited by 135
García‐Rodríguez, J. L., Barbier‐Torres, L., Fernández-Álvarez, S., Juan, V. G., Monte, M. J., Halilbasic, E., Herranz, D., Álvarez, L., Aspichueta, P., Marı́n, J. J. G., et al. (2013) · Hepatology · doi:10.1002/hep.26971 · Cited by 128
Song, B.-J., Akbar, M., Abdelmegeed, M. A., Byun, K., Lee, B., Yoon, S. K., & Hardwick, J. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.10.004 · Cited by 123
“A recent study also showed that sustained JNK activation led to phosphorylation at Ser-46 of sirtuin 1, NADþ-dependent deacetylase in cytosol (described later), followed by ubiquitin-dependent degradation, contributing to fat accumulation in obese mice [124].”
BackgroundmIGF‐1/JNK1/SirT1 signaling confers protection against oxidative stress in the heart
Vinciguerra, M., Santini, M. P., Martínez, C., Pazienza, V., Claycomb, W. C., Giuliani, A., & Rosenthal, N. A. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00766.x · Cited by 122
O-GlcNAcylation of SIRT1 enhances its deacetylase activity and promotes cytoprotection under stress
Han, C., Gu, Y., Shan, H., Mi, W., Sun, J., Shi, M., Zhang, X., Lu, X., Han, F., Gong, Q., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01654-6 · Cited by 125
Nin, V., Escande, C., Chini, C. C. S., Giri, S., Camacho-Pereira, J., Matalonga, J., Lou, Z., & Chini, E. N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365874 · Cited by 123
Non-alcoholic fatty liver disease: An update with special focus on the role of gut microbiota
Doulberis, M., Kotronis, G., Gialamprinou, D., Kountouras, J., & Katsinelos, P. (2017) · Metabolism · doi:10.1016/j.metabol.2017.03.013 · Cited by 117
Huang, C.-Y., Kuo, W.-W., Yeh, Y.-L., Ho, T.-J., Lin, J.-Y., Dy, L., Chu, C.-H., Tsai, F.-J., Tsai, C.-H., & Huang, C.-Y. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.46 · Cited by 107
Amphetamines promote mitochondrial dysfunction and DNA damage in pulmonary hypertension
Chen, P.-I., Cao, A., Miyagawa, K., Tojais, N. F., Hennigs, J. K., Li, C. G., Sweeney, N. M., Inglis, A. S., Wang, L., Li, D., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.90427 · Cited by 106
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Maiese, K. (2014) · Current Neurovascular Research · doi:10.2174/1567202611666140912115107 · Cited by 105
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Pani, G. (2015) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.03.004 · Cited by 103
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
Kanwal, A., Pillai, V. B., Samant, S. A., Gupta, M., & Gupta, M. P. (2019) · The FASEB Journal · doi:10.1096/fj.201900767r · Cited by 104
Liu, L., Liu, C., Zhang, Q., Shen, J., Zhang, H., Shan, J., Duan, G., Guo, D., Chen, X., Cheng, J., et al. (2016) · Hepatology · doi:10.1002/hep.28690 · Cited by 102
Free radicals and sprint exercise in humans
Morales‐Álamo, D., & Calbet, J. A. L. (2013) · Free Radical Research · doi:10.3109/10715762.2013.825043 · Cited by 91
Targher, G., Marchesini, G., & Byrne, C. D. (2016) · Diabetes & Metabolism · doi:10.1016/j.diabet.2016.04.002 · Cited by 90
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Lau, A. W., Liu, P., Inuzuka, H., & Gao, D. (2014) · PubMed Central · Cited by 86
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Dong, S., Jia, C., Zhang, S., Fan, G., Li, Y., Shan, P., Sun, L., Xiao, W., Li, L., Zheng, Y., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.08.012 · Cited by 85
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Pardo, P. S., & Boriek, A. M. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111249 · Cited by 92
Bahl, S., & Seto, E. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03599-4 · Cited by 82
Emerging Roles of SIRT1 in Cancer Drug Resistance
Wang, Z., & Chen, W. (2013) · Genes & Cancer · doi:10.1177/1947601912473826 · Cited by 87
Sarne, Y., Toledano, R., Rachmany, L., Sasson, E., & Doron, R. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.09.025 · Cited by 83
Morales‐Álamo, D., Ponce‐González, J. G., Guadalupe‐Grau, A., Rodríguez‐García, L., Santana, A., Cussó, M. R., Guerrero, M., Guerra, B., Dorado, C., & Calbet, J. A. L. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00415.2012 · Cited by 83
3,5-Diiodo-l-thyronine ameliorates diabetic nephropathy in streptozotocin-induced diabetic rats
Shang, G., Gao, P., Zhao, Z., Chen, Q., Jiang, T., Zhang, N., & Li, H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.01.023 · Cited by 79
Nelson, L. E., Valentine, R. J., Cacicedo, J. M., Gauthier, M., Ido, Y., & Ruderman, N. B. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00296.2011 · Cited by 81
Zeng, Y., Guo, M., Wu, Q., Tan, X., Jiang, C., Teng, F., Chen, J., Zhang, F., Ma, X., Li, X., et al. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.08.018 · Cited by 89
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Song, Z., Liu, Y., Hao, B., Yu, S., Zhang, H., Liu, D., Zhou, B., Wu, L., Wang, M., Xiong, Z., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0112699 · Cited by 76
Role of Sirtuins in Regulating Pathophysiology of the Heart
Bindu, S., Pillai, V. B., & Gupta, M. P. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.04.015 · Cited by 76
Ham, M., Choe, S. S., Shin, K. C., Choi, G., Kim, J., Noh, J., Kim, Y., Ryu, J.-W., Yoon, K., Lee, C., et al. (2016) · Diabetes · doi:10.2337/db16-0060 · Cited by 73
AMPK signaling in skeletal muscle during exercise: Role of reactive oxygen and nitrogen species
Morales-Alamo, D., & Calbet, J. A. L. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.01.012 · Cited by 72
Xie, X., Cao, Y., Dai, L., & Zhou, D. (2023) · Molecular Medicine · doi:10.1186/s10020-022-00595-1 · Cited by 71
Ferreira, D. M. S., Afonso, M. B., Rodrigues, P. M., Simão, A. L., Pereira, D. M., Borralho, P. M., Rodrigues, C. M. P., & Castro, R. E. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00420-13 · Cited by 70
Panes-Fernández, J., Godoy, P. A., Silva-Grecchi, T., Celis, M. T., Ramírez-Molina, O., Gavilán, J., Muñoz-Montesino, C., Castro, P. A., Moraga‐Cid, G., Yévenes, G. E., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00709 · Cited by 71
Huang, K., Chen, C., Hao, J., Huang, J., Liu, P., & Huang, H. (2014) · Endocrinology · doi:10.1210/en.2014-1381 · Cited by 69
Kang, H., & Kim, B. (2023) · Foods · doi:10.3390/foods12050925 · Cited by 74
Zou, Z., Liu, B., Zeng, L., Yang, X., Huang, R., Wu, C., Zhu, H., Gao, Y., Yuan, D., & Yu, J. (2019) · Mediators of Inflammation · doi:10.1155/2019/7854389 · Cited by 66
Genealogy of an ancient protein family: the Sirtuins, a family of disordered members
Costantini, S., Sharma, A., Raucci, R., Costantini, M., Autiero, I., & Colonna, G. (2013) · BMC Evolutionary Biology · doi:10.1186/1471-2148-13-60 · Cited by 66
Peng, L., Yuan, Z., Li, Y., Ling, H., Izumi, V., Fang, B., Fukasawa, K., Koomen, J. M., Chen, J., & Seto, E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.612796 · Cited by 69
A Redox-resistant Sirtuin-1 Mutant Protects against Hepatic Metabolic and Oxidant Stress
Shao, D., Fry, J., Han, J., Hou, X., Pimentel, D. R., Matsui, R., Cohen, R. A., & Bachschmid, M. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520403 · Cited by 66
SIRT1 and stem cells: In the forefront with cardiovascular disease, neurodegeneration and cancer
Maiese, K. (2015) · World Journal of Stem Cells · doi:10.4252/wjsc.v7.i2.235 · Cited by 67
Zhao, X., Liu, Y., Zhu, G., Liang, Y.-Y., Liu, B., Wu, Y., Han, M., Sun, W., Han, Y. K., Chen, G., et al. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.07.363 · Cited by 63
CERKL regulates autophagy via the NAD-dependent deacetylase SIRT1
Hu, X., Lu, Z., Yu, S., Reilly, J., Liu, F., Jia, D., Qin, Y., Han, S., Liu, X., Qu, Z., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1520548 · Cited by 63
Armour, S. M., Bennett, E. J., Braun, C. R., Zhang, X., McMahon, S. B., Gygi, S. P., Harper, J. W., & Sinclair, D. A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00971-12 · Cited by 64
SIRT1 in the Development and Treatment of Hepatocellular Carcinoma
Farcas, M. F., Andrei-Alexandru, G., Gulei, D., Ionescu, C., Irimie, A., Cătană, C.-S., & Berindan‐Neagoe, I. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00148 · Cited by 61
Li, Z., Bridges, B., Olson, J. C., & Weinman, S. A. (2016) · Oncogene · doi:10.1038/onc.2016.359 · Cited by 58
Kim, T. H., Yang, Y. M., Han, C. Y., Koo, J. H., Oh, H., Kim, S. S., You, B. H., Choi, Y. H., Park, T., Lee, C. H., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci97831 · Cited by 62
Wang, S., Zhong Chong, Z., Chen Shang, Y., & Maiese, K. (2013) · Current Neurovascular Research · doi:10.2174/156720213804805945 · Cited by 58
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Lee, W., Lee, W.-T., Cheng, C., Chen, K., Chou, C., Chung, C., Sun, M.-S., Cheng, H., Ho, M.-N., & Lin, C. (2015) · Oncotarget · doi:10.18632/oncotarget.4768 · Cited by 58
Regeneration in the nervous system with erythropoietin
Maiese, K. (2015) · Frontiers in bioscience · doi:10.2741/4408 · Cited by 54
Tong, X., Zhang, D., Arthurs, B., Li, P., Durudogan, L., Gupta, N., & Yin, L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130047 · Cited by 53
Fusco, S., Maulucci, G., & Pani, G. (2012) · Cell Cycle · doi:10.4161/cc.22074 · Cited by 54
Yang, H., Yan, B., Liao, D., Huang, S., & Qiu, Y. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.106 · Cited by 54
RelB acts as a molecular switch driving chronic inflammation in glioblastoma multiforme
Waters, M. R., Gupta, A. S., Mockenhaupt, K., Brown, L. N., Biswas, D. D., & Kordula, T. (2019) · Oncogenesis · doi:10.1038/s41389-019-0146-y · Cited by 52
Waller‐Evans, H., Hue, C., Fearnside, J., Rothwell, A. R., Lockstone, H. E., Caldérari, S., Wilder, S. P., Cazier, J., Scott, J., & Gauguier, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082825 · Cited by 51
Chattopadhyay, T., Maniyadath, B., Bagul, H. P., Chakraborty, A., Shukla, N., Budnar, S., Rajendran, A., Shukla, A., Kamat, S. S., & Kolthur‐Seetharam, U. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1909943117 · Cited by 51
Yang, F., Wang, X., Yang, D., Lu, Y., Wei, G., Yu, W., Liu, X., Zheng, Q., Ying, J., & Hua, F. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.738686 · Cited by 53
Proteasome‐mediated proteostasis: Novel medicinal and pharmacological strategies for diseases
Mishra, R., Upadhyay, A., Prajapati, V. K., & Mishra, A. (2018) · Medicinal Research Reviews · doi:10.1002/med.21502 · Cited by 51
Zhao, X., Wu, Y., Li, J., Li, D., Yang, J., Zhu, P., Liu, Y., Zhuang, Y., Yu, S., Cao, W., et al. (2019) · Toxicology · doi:10.1016/j.tox.2019.05.003 · Cited by 50
Song, B., Akbar, M. D., Jo, I., Hardwick, J. P., & Abdelmegeed, M. A. (2015) · Advances in pharmacology · doi:10.1016/bs.apha.2015.04.002 · Cited by 50
Liu, L., Yasen, M., Tang, D., Ye, J., Aisa, H. A., & Xin, X. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.01.143 · Cited by 48
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Ip, B. C., & Wang, X. (2013) · Nutrients · doi:10.3390/nu6010124 · Cited by 47
Reverting p53 activation after recovery of cellular stress to resume with cell cycle progression
Lazo, P. A. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.02.005 · Cited by 48
Inhibition of ATG3 ameliorates liver steatosis by increasing mitochondrial function
Lima, N. D. S., Fondevila, M. F., Nóvoa, E., Buqué, X., Mercado-Gómez, M., Gallet, S., Gonzalez-Rellan, M. J., Fernandez, U., Loyens, A., García-Vence, M., et al. (2021) · Journal of Hepatology · doi:10.1016/j.jhep.2021.09.008 · Cited by 46
Senthil, K. K. J., Gokila, V. M., Mau, J., Lin, C.-C., Chu, F., Wei, C., Liao, V. H., & Wang, S. (2016) · Oncotarget · doi:10.18632/oncotarget.11229 · Cited by 46
Choi, S., Kwon, S., Seok, S., Xiao, Z., Lee, K. W., KANG, Y. Y., Li, X., Shinoda, K., Kajimura, S., KEMPER, B. W., et al. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00006-17 · Cited by 46
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Metadata
- Authors
- Gao, Z., Zhang, J., Kheterpal, I., Kennedy, N., Davis, R. J., & Ye, J.
- Affiliations
- Pennington Biomedical Research Center (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Ye, Jianping
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-06
- Volume
- 286
- Issue
- 25
- Pages
- 22227-22234
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3121368
- OpenAlex
- W2001428385
- Cited by
- 187
- References
- 46
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 7 · 2023: 5 · 2022: 6 · 2021: 15 · 2020: 12 · 2019: 15 · 2018: 16 · 2017: 16 · 2016: 17 · 2015: 20 · 2014: 13 · 2013: 21 · 2012: 13
- FWCI
- 7.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Funders
- National Institutes of Health (DK085495)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-085495, R56DK068036, R01DK085495, R01DK068036, DK068036, P30DK072476)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Hepatology › Liver Disease Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- SIRT1, JNK1, JNK2, protein degradation, ubiquitination, proteasome, hepatic steatosis, obesity, hepatocytes
- MeSH terms
- Animals, Cell Line, Dietary Fats, Enzyme Activation, Fatty Liver, Histone Deacetylases, Humans, Male, Mice, Inbred C57BL, Obesity, Phosphorylation, Mitogen-Activated Protein Kinase 8, Mice, Rats, Ubiquitination, Gene Knockout Techniques, Sirtuin 1
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