SIRT1 Promotes Proliferation and Prevents Senescence Through Targeting LKB1 in Primary Porcine Aortic Endothelial Cells

AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

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AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy

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Sirtuins in mammals: insights into their biological function

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LKB1 is the upstream kinase in the AMP-activated protein kinase cascade

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AMP-activated protein kinase induces a p53-dependent metabolic checkpoint

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A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy

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SIRT1 Promotes Endothelium-Dependent Vascular Relaxation by Activating Endothelial Nitric Oxide Synthase

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LKB1 inhibits telomerase activity resulting in cellular senescence through histone lactylation in lung adenocarcinoma

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Vascular Ageing and Exercise: Focus on Cellular Reparative Processes

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miRNA biomarkers in renal disease

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Epigenetic Regulation of Vascular Aging and Age-Related Vascular Diseases

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H 2 O 2 Accumulation Mediates Differentiation Capacity Alteration, But Not Proliferative Decline, in Senescent Human Fetal Mesenchymal Stem Cells

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The Multifaceted Role of Endothelial Sirt1 in Vascular Aging: An Update

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Effect of mild heat stress on the proliferative and differentiative ability of human mesenchymal stromal cells

Choudhery, M. S., Badowski, M., Muise, A., & Harris, D. T. (2014) · Cytotherapy · doi:10.1016/j.jcyt.2014.11.003 · Cited by 52

Regulation of Sirt1 on energy metabolism and immune response in rheumatoid arthritis

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SIRT1 in metabolic syndrome: Where to target matters

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Endothelial SIRT1 prevents adverse arterial remodeling by facilitating HERC2-mediated degradation of acetylated LKB1

Bai, B., Man, A. W. C., Yang, K., Guo, Y., Xu, C., Tse, H., Han, W., Bloksgaard, M., Mey, J. G. R. D., Vanhoutte, P. M., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9687 · Cited by 51

Sirtuins in kidney health and disease

Perico, L., Remuzzi, G., & Benigni, A. (2024) · Nature Reviews Nephrology · doi:10.1038/s41581-024-00806-4 · Cited by 52

Nutrient sensing, growth and senescence

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Disturbance of Fatty Acid Metabolism Promoted Vascular Endothelial Cell Senescence via Acetyl‐CoA‐Induced Protein Acetylation Modification

Lin, T., Yang, W., Luo, W., Zhang, L., Mai, Y., Li, Z., Liu, S., Jiang, L.-J., Liu, P., & Li, Z. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1198607 · Cited by 50

hnRNP A1 antagonizes cellular senescence and senescence‐associated secretory phenotype via regulation of SIRT1 mRNA stability

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Metformin prevents aggressive ovarian cancer growth driven by high-energy diet: similarity with calorie restriction

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SIRT1 inhibition in pancreatic cancer models: Contrasting effects in vitro and in vivo

Oon, C. E., Strell, C., Yeong, K. Y., Östman, A., & Prakash, J. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.03.064 · Cited by 45

Endothelial SIRT1 prevents age-induced impairment of vasodilator responses by enhancing the expression and activity of soluble guanylyl cyclase in smooth muscle cells

Guo, Y., Xu, C., Man, A. W. C., Bai, B., Luo, C., Huang, Y., Xu, A., Vanhoutte, P. M., & Wang, Y. (2018) · Cardiovascular Research · doi:10.1093/cvr/cvy212 · Cited by 45

SIRT1 Inactivation Evokes Antitumor Activities in NSCLC through the Tumor Suppressor p27

Zhu, L., Chiao, C., Enzer, K. G., Stankiewicz, A. J., Faller, D. V., & Dai, Y. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0239 · Cited by 42

Aspirin attenuates vinorelbine-induced endothelial inflammation via modulating SIRT1/AMPK axis

Tsai, K., Huang, P., Kao, C.-L., Leu, H., Cheng, Y., Liao, Y., Yang, Y.-P., Chien, Y., Wang, C., Hsiao, C.-Y., et al. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.005 · Cited by 41

Effects of rhein lysinate on D-galactose-induced aging mice

Zhen, Y., Lin, Y., Li, K., ZHANG, G.-L., ZHAO, Y.-F., Wang, M., Jing-bo, W., Wei, J., & Hu, G. (2015) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2015.2858 · Cited by 41

SIRT1 in Endothelial Cells as a Novel Target for the Prevention of Early Vascular Aging

Guo, Y., Xu, A., & Wang, Y. (2015) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000344 · Cited by 43

Betalain- and betacyanin-rich supplements’ impacts on the PBMC SIRT1 and LOX1 genes expression and Sirtuin-1 protein levels in coronary artery disease patients: A pilot crossover clinical trial

Rahimi, P., Mesbah‐Namin, S. A., Ostadrahimi, A., Separham, A., & Jafarabadi, M. A. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.06.003 · Cited by 44

Senescent endothelial cells: a potential target for diabetic retinopathy

Liao, Y.-L., Fang, Y., Sun, J., & Dou, G. (2024) · Angiogenesis · doi:10.1007/s10456-024-09943-7 · Cited by 40

Global Gene Expression Profiling Reveals Functional Importance of Sirt2 in Endothelial Cells under Oxidative Stress

Liu, J., Wu, X. B., Wang, X., Zhang, Y., Bu, P., Zhang, Q., & Jiang, F. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14035633 · Cited by 40

Sirt1-inducible deacetylation of p21 promotes cardiomyocyte proliferation

Li, B., Li, M., Li, X., Li, H., Lai, Y., Huang, S., He, X. F., Si, X., Zheng, H., Liao, W., et al. (2019) · Aging · doi:10.18632/aging.102587 · Cited by 40

Targeting ALDH2 for Therapeutic Interventions in Chronic Pain-Related Myocardial Ischemic Susceptibility

Li, C., Sun, W., Gu, C., Yang, Z., Quan, N., Yang, J., Shi, Z., Yu, L., & Ma, H. (2018) · Theranostics · doi:10.7150/thno.22414 · Cited by 39

Cellular Senescence in Obesity and Associated Complications: a New Therapeutic Target

Narasimhan, A., Flores, R. R., Camell, C. D., Bernlohr, D., Robbins, P. D., & Niedernhofer, L. J. (2022) · Current Diabetes Reports · doi:10.1007/s11892-022-01493-w · Cited by 40

Endothelium-Derived Relaxing Factors and Endothelial Function: A Systematic Review

Nappi, F., Fiore, A., Masiglat, J., Cavuoti, T., Romandini, M., Nappi, P., Singh, S. S. A., & Couëtil, J.-P. (2022) · Biomedicines · doi:10.3390/biomedicines10112884 · Cited by 38

Caloric restriction can improve learning and memory in C57/BL mice probably via regulation of the AMPK signaling pathway

Ma, L., Wang, R., Dong, W., & Zhao, Z. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.11.013 · Cited by 38

Metformin and tenovin‐6 synergistically induces apoptosis through LKB1‐independent SIRT1 down‐regulation in non‐small cell lung cancer cells

Lee, B. B., Kim, Y., Kim, D., Cho, E. Y., Han, J., Kim, H. K., Shim, Y. M., & Kim, D. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14194 · Cited by 38

Endothelial SIRT1 as a Target for the Prevention of Arterial Aging: Promises and Challenges

Begum, M. K., Konja, D., Singh, S., Chłopicki, S., & Wang, Y. (2021) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001154 · Cited by 40

Effects of Rhein Lysinate on H2O2-induced cellular senescence of human umbilical vascular endothelial cells

Lin, Y., Zhen, Y., Wei, J., Liu, B., Zong-yuan, Y., & Hu, G. (2011) · Acta Pharmacologica Sinica · doi:10.1038/aps.2011.101 · Cited by 38

Calorie Restriction Prevents Metabolic Aging Caused by Abnormal SIRT1 Function in Adipose Tissues

Xu, C., Cai, Y., Fan, P., Bai, B., Chen, J., Deng, H., Che, C., Xu, A., Vanhoutte, P. M., & Wang, Y. (2014) · Diabetes · doi:10.2337/db14-1180 · Cited by 36

The Preconditioning of Berberine Suppresses Hydrogen Peroxide‐Induced Premature Senescence via Regulation of Sirtuin 1

Zhu, X., Yue, H., Guo, X., Yang, J., Liu, J., Liu, J., Wang, R., & Zhu, W. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2391820 · Cited by 36

Resveratrol and Resveratrol-Aspirin Hybrid Compounds as Potent Intestinal Anti-Inflammatory and Anti-Tumor Drugs

Salla, M., Pandya, V., Bhullar, K. S., Kerek, E. M., Wong, Y. F., Losch, R., Ou, J., Aldawsari, F. S., Velázquez‐Martínez, C. A., Thiesen, A., et al. (2020) · Molecules · doi:10.3390/molecules25173849 · Cited by 35

Perspectives of Targeting mTORC1–S6K1 in Cardiovascular Aging

Ming, X., Montani, J., & Yang, Z. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00005 · Cited by 36

Loss of Sirt3 Limits Bone Marrow Cell-Mediated Angiogenesis and Cardiac Repair in Post-Myocardial Infarction

Zeng, H., Li, L., & Chen, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107011 · Cited by 36

Sirtuins family as a target in endothelial cell dysfunction: implications for vascular ageing

Zhang, H., Dai, Y., Zhang, C., Alfred, M. O., Ghosh, A., Khanra, I., Chakraborty, M., Yu, X., & Liang, J. L. (2020) · Biogerontology · doi:10.1007/s10522-020-09873-z · Cited by 35

Alzheimer’s Amyloid-β Accelerates Human Neuronal Cell Senescence Which Could Be Rescued by Sirtuin-1 and Aspirin

Li, Y., Lü, J., Hou, Y., Huang, S., & Pei, G. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.906270 · Cited by 36

Epigenetics, sirtuins and osteoarthritis

Gabay, O., & Sanchez, C. (2012) · Joint Bone Spine · doi:10.1016/j.jbspin.2012.04.005 · Cited by 34

Overexpression of a dominant-negative mutant of SIRT1 in mouse heart causes cardiomyocyte apoptosis and early-onset heart failure

Mu, W., Zhang, Q., Tang, X., Fu, W., Zheng, W., Lu, Y., Li, H., Wei, Y., Li, L., She, Z., et al. (2014) · Science China Life Sciences · doi:10.1007/s11427-014-4687-1 · Cited by 34

Association of SIRT1 expression with shear stress induced endothelial progenitor cell differentiation

Cheng, B., Yan, Z., Yao, Q., Shen, B., Wang, J., Gao, L., Li, Y., Yuan, H., Qi, Y., & Jiang, Z. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24239 · Cited by 34

mPGES-2 blockade antagonizes β-cell senescence to ameliorate diabetes by acting on NR4A1

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Mechanisms and Subclinical Consequences of Aortic Stiffness

Pierce, G. L. (2017) · Hypertension · doi:10.1161/hypertensionaha.117.08933 · Cited by 33

A TagSNP in SIRT1 Gene Confers Susceptibility to Myocardial Infarction in a Chinese Han Population

Cheng, J., Cho, M., Cen, J.-M., Cai, M., Xu, S., Ma, Z.-W., Liu, X., Yang, X.-L., Chen, C., Suh, Y., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0115339 · Cited by 32

Multi-Omics Integration Analysis Identifies Lipid Disorder of a Non-Alcoholic Fatty Liver Disease (NAFLD) Mouse Model Improved by Zexie–Baizhu Decoction

Cao, Y., Shi, J., Song, L., Xu, J., Lu, H., Sun, J., Hou, J., Chen, J., Wu, W., & Gong, L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.858795 · Cited by 33

Reduced activity of SKC a and Na‐K ATP ase underlies the accelerated impairment of EDH ‐type relaxations in mesenteric arteries of aging spontaneously hypertensive rats

Kong, B. W. C., Man, R. Y. K., Gao, Y., Vanhoutte, P. M., & Leung, S. W. S. (2015) · Pharmacology Research & Perspectives · doi:10.1002/prp2.150 · Cited by 33

Novel role of PKR in palmitate-induced Sirt1 inactivation and endothelial cell senescence

Li, Y., Peng, Z., Wang, C., Li, L., Leng, Y., Chen, R., Yuan, H., Zhou, S., Zhang, Z., & Chen, A. F. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00038.2018 · Cited by 32

Age‐related AMP‐activated protein kinase alterations: From cellular energetics to longevity

Васильевна, М. Г., & Клебанов, А. А. (2019) · Cell Biochemistry and Function · doi:10.1002/cbf.3384 · Cited by 32

Endothelial Senescence: From Macro- to Micro-Vasculature and Its Implications on Cardiovascular Health

Wang, P., Konja, D., Singh, S., Zhang, B., & Wang, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25041978 · Cited by 37

A nutrigeroscience approach: Dietary macronutrients and cellular senescence

Calubag, M. F., Robbins, P. D., & Lamming, D. W. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.07.025 · Cited by 33

New Insight in HDACs: Potential Therapeutic Targets for the Treatment of Atherosclerosis

Luan, Y., Liu, H., Luan, Y., Yang, Y., Yang, J., & Ren, K. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.863677 · Cited by 32

LKB1: An emerging therapeutic target for cardiovascular diseases

Molaei, A., Molaei, E., Sadeghnia, H. R., Hayes, A. W., & Karimi, G. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120844 · Cited by 30

Red wine extract protects against oxidative-stress-induced endothelial senescence

Botden, I. P. G., Oeseburg, H., Durik, M., Leijten, F. P. J., der Zee, L. C. V. V., Musterd‐Bhaggoe, U. M., Garrelds, I. M., Seynhaeve, A. L. B., Langendonk, J. G., Sijbrands, E. J. G., et al. (2012) · Clinical Science · doi:10.1042/cs20110679 · Cited by 34

Docosahexaenoic acid attenuates adipose tissue angiogenesis and insulin resistance in high fat diet‐fed middle‐aged mice via a sirt1‐dependent mechanism

Luo, X., Jia, R., Yao, Q., Xu, Y., Luo, Z., Luo, X., & Wang, N. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500714 · Cited by 30

The Endothelium Abridges Insulin Resistance to Premature Aging

Avogaro, A., de Kreutzenberg, S. V., Federici, M., & Fadini, G. P. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000262 · Cited by 30

Material basis, effect, and mechanism of ethanol extract of Pinellia ternata tubers on oxidative stress-induced cell senescence

Tang, D., Yan, R., Sun, Y., Kai, G., Chen, K., & Li, J. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153275 · Cited by 30

Regulation of SIRT1/AMPK axis is critically involved in gallotannin-induced senescence and impaired autophagy leading to cell death in hepatocellular carcinoma cells

Kwon, H. Y., Kim, J., Kim, B., Srivastava, S., & Kim, S. (2017) · Archives of Toxicology · doi:10.1007/s00204-017-2021-y · Cited by 30

Sirtuin biology and relevance to diabetes treatment

Dong, X. C. (2012) · Diabetes Management · doi:10.2217/dmt.12.16 · Cited by 29

Identification of a small molecule activator of SIRT1 gene expression

Cho, S., Cho, M., Seo, D. B., Lee, S. J., & Suh, Y. (2013) · Aging · doi:10.18632/aging.100539 · Cited by 28

Endothelial Cell Senescence Increases Traction Forces due to Age-Associated Changes in the Glycocalyx and SIRT1

Cheung, T. M., Yan, J. B., Fu, J. J., Huang, J., Yuan, F., & Truskey, G. A. (2014) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-014-0371-6 · Cited by 28

Implication of the deacetylase sirtuin-1 on synovial angiogenesis and persistence of experimental arthritis

Leblond, A., Pezet, S., Cauvet, A., Casas, C., Silva, J. P. D., Hervé, R., Clavel, G., Dumas, S. J., Cohen‐Kaminsky, S., Bessis, N., et al. (2020) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2020-217377 · Cited by 28

Sirtuin 1 Mediates the Actions of Peroxisome Proliferator-Activated Receptor δ on the Oxidized Low-Density Lipoprotein–Triggered Migration and Proliferation of Vascular Smooth Muscle Cells

Hwang, J. S., Ham, S. A., Yoo, T., Lee, W. J., Paek, K. S., Lee, C.-H., & Seo, H. G. (2016) · Molecular Pharmacology · doi:10.1124/mol.116.104679 · Cited by 27

Association between serum Klotho concentration and all-cause and cardiovascular mortality among American individuals with hypertension

Yan, Y.-Q., & Chen, J. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1013747 · Cited by 27

Cellular lifespan and senescence: a complex balance between multiple cellular pathways

Dolivo, D., Hernandez, S. J., & Dominko, T. (2016) · BioEssays · doi:10.1002/bies.201670906 · Cited by 29

Cytosolic DNA initiates a vicious circle of aging-related endothelial inflammation and mitochondrial dysfunction via STING: the inhibitory effect of Cilostazol

Zheng, Z., Wang, J., Lin, J.-G., Ye, W., Zou, J., Liang, L.-Y., Yang, P.-L., Qiu, W., Li, Y.-Y., Yang, S.-J., et al. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01281-0 · Cited by 28

Dual-edged role of SIRT1 in energy metabolism and cardiovascular disease

Zhou, R., Barnes, K., Gibson, S., & Fillmore, N. (2024) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00001.2024 · Cited by 29

Microbiota governs host chenodeoxycholic acid glucuronidation to ameliorate bile acid disorder induced diarrhea

Lin, Z., Feng, Y., Wang, J., Men, Z., & Ma, X. (2025) · Microbiome · doi:10.1186/s40168-024-02011-8 · Cited by 27

l ‐Citrulline ameliorates pathophysiology in a rat model of superimposed preeclampsia

Man, A. W. C., Zhou, Y., Lam, U. D. P., Reifenberg, G., Werner, A., Habermeier, A., Closs, E. I., Daiber, A., Münzel, T. F., Xia, N., et al. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15783 · Cited by 25

Endogenous Transmembrane TNF-Alpha Protects Against Premature Senescence in Endothelial Colony Forming Cells

Green, L. A., Njoku, V., Mund, J. A., Case, J., Yöder, M. C., Murphy, M. P., & Clauss, M. A. (2016) · Circulation Research · doi:10.1161/circresaha.116.308332 · Cited by 26

Oxidative–Inflammatory Crosstalk and Multi-Target Natural Agents: Decoding Diabetic Vascular Complications

Liu, J., Li, K., Yi, Z., Saqirile, Wang, C., & Yang, R. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47080614 · Cited by 30

Fasting as Medicine: Mitochondrial and Endothelial Rejuvenation in Vascular Aging

Milan, M., Troyano‐Rodriguez, E., Ihuoma, J., Negri, S., Rudraboina, R., Kosmider, A., Awasthi, S., Balasubramanian, P., Conley, S. M., Yabluchanskiy, A., et al. (2026) · Aging Cell · doi:10.1111/acel.70372 · Cited by 25

The endothelial glycocalyx in critical illness: A pediatric perspective

Richter, R. P., Payne, G. A., Ambalavanan, N., Gaggar, A., & Richter, J. R. (2022) · Matrix Biology Plus · doi:10.1016/j.mbplus.2022.100106 · Cited by 25

Lipopolysaccharides Promote S-Nitrosylation and Proteasomal Degradation of Liver Kinase B1 (LKB1) in Macrophages in Vivo

Liu, Z., Dai, X., Zhu, H., Zhang, M., & Zou, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.649210 · Cited by 24

Resveratrol-downregulated phosphorylated liver kinase B1 is involved in senescence of acute myeloid leukemia stem cells

Peng, D., Song, H. K., & Liu, L. (2015) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-015-1457-7 · Cited by 25

miRNAs driving diagnosis, prognosis and progression in Merkel cell carcinoma

AL‐Noshokaty, T. M., Elballal, M. S., Helal, G. K., Abulsoud, A. I., Elshaer, S. S., El-Husseiny, A. A., Fathi, D., Abdelmaksoud, N. M., Mageed, S. S. A., Midan, H. M., et al. (2023) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.154763 · Cited by 23

Calcium dobesilate mediates renal interstitial fibrosis and delay renal peritubular capillary loss through Sirt1/p53 signaling pathway

Wang, Y., Zuo, B., Wang, N., Li, S., Liu, C., & Sun, D. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110798 · Cited by 23

Enhanced activation of NAD(P)H

Kim, Y., Hwang, J. H., Kim, K.-S., Noh, J., Gang, G., Oh, W. K., Jeong, K., Kwak, T. H., Choi, H., Lee, I., et al. (2013) · Journal of Hypertension · doi:10.1097/hjh.0000000000000018 · Cited by 23

Combating cellular senescence by sirtuins: Implications for atherosclerosis

Ma, S., Fan, L., & Cao, F. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.06.011 · Cited by 23

AMPK-SIRT1-PGC1α Signal Pathway Influences the Cognitive Function of Aged Rats in Sevoflurane-Induced Anesthesia

Yang, X., Li, Q.-J., Zhang, W., Zheng, S., Qu, Z., Xi, Y., & Wang, G. (2020) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01612-w · Cited by 24

Inhibition of nucleolar stress response by Sirt1: A potential mechanism of acetylation‐independent regulation of p53 accumulation

Bi, X., Ye, Q., Li, D., Peng, Q., Wang, Z., Wu, X. B., Zhang, Y., Zhang, Q., & Jiang, F. (2019) · Aging Cell · doi:10.1111/acel.12900 · Cited by 23

Klotho and SIRT1 changes from pre-diabetes to diabetes and pre-hypertension to hypertension

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Hypertension and cellular senescence

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