Resveratrol-Induced AMP-Activated Protein Kinase Activation Is Cell-Type Dependent: Lessons from Basic Research for Clinical Application

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 · see citing works

Therapeutic potential of resveratrol: the in vivo evidence

Baur, J. A., & Sinclair, D. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2060 · Cited by 3,958 · see citing works

Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796 · see citing works

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

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works

Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade

Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Mäkelä, T. P., Alessi, D. R., & Hardie, D. G. (2003) · Journal of Biology · doi:10.1186/1475-4924-2-28 · Cited by 1,666 · see citing works

Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase

Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.009 · Cited by 1,589 · see citing works

Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases

Park, S. J., Ahmad, F., Philp, A., Baar, K., Williams, T., Luo, H., Ke, H., Rehmann, H., Taussig, R., Brown, A. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.017 · Cited by 1,352 · see citing works

Circadian Control of the NAD ⁺ Salvage Pathway by CLOCK-SIRT1

Nakahata, Y., Sahar, S., Astarita, G., Kaluzova, M., & Sassone-Corsi, P. (2009) · Science · doi:10.1126/science.1170803 · Cited by 1,198 · see citing works

SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1

Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., Garofalo, R. S., Griffith, D., Griffor, M., Loulakis, P., Pabst, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088682 · Cited by 915 · see citing works

SIRT1 Modulation of the Acetylation Status, Cytosolic Localization, and Activity of LKB1

Lan, F., Cacicedo, J. M., Ruderman, N., & Ido, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805711200 · Cited by 825 · see citing works

AMP-Activated Protein Kinase – Development of the Energy Sensor Concept

Hardie, D. G., Hawley, S. A., & Scott, J. W. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.108944 · Cited by 813 · see citing works

Benfotiamine blocks three major pathways of hyperglycemic damage and prevents experimental diabetic retinopathy

Hammes, H.-P., Du, X., Edelstein, D., Taguchi, T., Matsumura, T., Ju, Q., Lin, J., Bierhaus, A., Nawroth, P., Hannak, D., et al. (2003) · Nature Medicine · doi:10.1038/nm834 · Cited by 785 · see citing works

Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans

Bieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750 · see citing works

Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade

Sanders, M. J., Grondin, P., Hegarty, B. D., Snowden, M. A., & Carling, D. (2007) · Biochemical Journal · doi:10.1042/bj20061520 · Cited by 660 · see citing works

Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators

Hubbard, B. P., Gomes, A. P., Dai, H., Li, J., Case, A. W., Considine, T., Riera, T. V., Lee, J. E., Yen, E. S., Lamming, D. W., et al. (2013) · Science · doi:10.1126/science.1231097 · Cited by 618 · see citing works

Mammalian TAK1 Activates Snf1 Protein Kinase in Yeast and Phosphorylates AMP-activated Protein Kinase in Vitro

Momcilovic, M., Hong, S. P., & Carlson, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604399200 · Cited by 474 · see citing works

Dissecting the Role of 5′-AMP for Allosteric Stimulation, Activation, and Deactivation of AMP-activated Protein Kinase

Suter, M., Riek, U., Tuerk, R. D., Schlattner, U., Wallimann, T., & Neumann, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606357200 · Cited by 473 · see citing works

Ubiquitin-mediated activation of TAK1 and IKK

Adhikari, A., Xu, M., & Chen, Z. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210413 · Cited by 455 · see citing works

Inhibition of mitochondrial proton F0F1‐ATPase/ATP synthase by polyphenolic phytochemicals

Zheng, J., & Ramirez, V. D. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703397 · Cited by 453 · see citing works

Resveratrol is not a direct activator of SIRT1 enzyme activity

Beher, D., Wu, J., Cumine, S., Kim, K. W., Lu, S., Atangan, L., & Wang, M. (2009) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2009.00901.x · Cited by 426 · see citing works

It takes two to tango: NAD(+) and sirtuins in aging/longevity control

Imai, S.-I., & Guarente, L. (2016) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2016.17 · Cited by 394 · see citing works

Mechanism of inhibition of bovine F 1 -ATPase by resveratrol and related polyphenols

Gledhill, J. R., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706290104 · Cited by 379 · see citing works

Hyperglycemia-Induced Apoptosis in Human Umbilical Vein Endothelial Cells

Ido, Y., Carling, D., & Ruderman, N. B. (2002) · Diabetes · doi:10.2337/diabetes.51.1.159 · Cited by 323 · see citing works

Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR

Sakamoto, K., Göransson, O., Hardie, D. G., & Alessi, D. R. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00074.2004 · Cited by 299 · see citing works

STO-609, a Specific Inhibitor of the Ca2+/Calmodulin-dependent Protein Kinase Kinase

Tokumitsu, H., Inuzuka, H., Ishikawa, Y., Ikeda, M., Saji, I., & Kobayashi, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201075200 · Cited by 293 · see citing works

Acute Regulation of Fatty Acid Oxidation and AMP-Activated Protein Kinase in Human Umbilical Vein Endothelial Cells

Dagher, Z., Ruderman, N. B., Tornheim, K., & Ido, Y. (2001) · Circulation Research · doi:10.1161/hh1201.092998 · Cited by 209 · see citing works

Benfotiamine in Diabetic Polyneuropathy (BENDIP): Results of a Randomised, Double Blind, Placebo-controlled Clinical Study

Stracke, H. H. G., Gaus, W., Achenbach, U., Federlin, K., & Bretzel, R. G. (2008) · Experimental and Clinical Endocrinology & Diabetes · doi:10.1055/s-2008-1065351 · Cited by 192 · see citing works

Inhibitors of Sir2: Evaluation of Splitomicin Analogues

Posakony, J., Hirao, M., Stevens, S. D., Simon, J. A., & Bedalov, A. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm030473r · Cited by 160 · see citing works

Resveratrol Prevents Oxidative Stress-Induced Senescence and Proliferative Dysfunction by Activating the AMPK-FOXO3 Cascade in Cultured Primary Human Keratinocytes

Ido, Y., Duranton, A., Lan, F., Weikel, K., Breton, L., & Ruderman, N. B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0115341 · Cited by 141 · see citing works

Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis

Schweiger, M., Hennig, K., Lerner, F., Niere, M., Hirsch‐Kauffmann, M., Specht, T., Weise, C., Oei, S. L., & Ziegler, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02180-9 · Cited by 137 · see citing works

Weak Coupling of ATP Hydrolysis to the Chemical Equilibrium of Human Nicotinamide Phosphoribosyltransferase

Burgos, E. S., & Schramm, V. L. (2008) · Biochemistry · doi:10.1021/bi801198m · Cited by 123 · see citing works

Unlocking the Secrets of Longevity Genes

Sinclair, D. A., & Guarente, L. (2006) · Scientific American · doi:10.1038/scientificamerican0306-48 · Cited by 120 · see citing works

The ubiquitin-associated domain of AMPK-related kinases regulates conformation and LKB1-mediated phosphorylation and activation

Jaleel, M., Villa, F., Deák, M., Toth, R. L., Prescott, A. R., van Aalten, D. M. F., & Alessi, D. R. (2006) · Biochemical Journal · doi:10.1042/bj20051844 · Cited by 119 · see citing works

Sirt1 activation by resveratrol is substrate sequence-selective

Lakshminarasimhan, M., Rauh, D., Schutkowski, M., & Steegborn, C. (2013) · Aging · doi:10.18632/aging.100542 · Cited by 117 · see citing works

Metformin and phenformin activate AMP-activated protein kinase in the heart by increasing cytosolic AMP concentration

Zhang, L., He, H., & Balschi, J. A. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00002.2007 · Cited by 114 · see citing works

Neither LKB1 Nor AMPK Are the Direct Targets of Metformin

Hardie, D. G. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.07.032 · Cited by 111 · see citing works

Skp2-Dependent Ubiquitination and Activation of LKB1 Is Essential for Cancer Cell Survival under Energy Stress

Lee, S.-W., Li, C., Jin, G., Cai, Z., Han, F., Chan, C., Yang, W., Li, B., Rezaeian, A. H., Li, H., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.015 · Cited by 109 · see citing works

Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability

Boudeau, J., Deák, M., Lawlor, M. A., MORRICE, N. A., & Alessi, D. R. (2003) · Biochemical Journal · doi:10.1042/bj20021813 · Cited by 87 · see citing works

Transketolase protein TKTL1 overexpression: A potential biomarker and therapeutic target in breast cancer

Földi, M., Stickeler, E., Bau, L. A., Kretz, O., Watermann, D. O., Gitsch, G., Kayser, G., Hausen, A. Z., & Coy, J. (2007) · Oncology Reports · doi:10.3892/or.17.4.841 · Cited by 75 · see citing works

Effect of Estradiol, Diethylstilbestrol, and Resveratrol on F0F1-ATPase Activity from Mitochondrial Preparations of Rat Heart, Liver, and Brain

Kipp, J. L., & Ramirez, V. D. (2001) · Endocrine · doi:10.1385/endo:15:2:165 · Cited by 69 · see citing works

Green Tea Polyphenols as Proteasome Inhibitors: Implication in Chemoprevention

Yang, H., Landis‐Piwowar, K. R., Chan, T. H., & Dou, Q. P. (2011) · Current Cancer Drug Targets · doi:10.2174/156800911794519743 · Cited by 68 · see citing works

The Heat Shock Protein 90 Inhibitor, (−)-Epigallocatechin Gallate, Has Anticancer Activity in a Novel Human Prostate Cancer Progression Model

Moses, M. A., Henry, E. C., Ricke, W. A., & Gasiewicz, T. A. (2015) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-14-0224 · Cited by 64 · see citing works

Stability of the Peutz–Jeghers syndrome kinase LKB1 requires its binding to the molecular chaperones Hsp90/Cdc37

Nony, P., Gaude, H., Rossel, M., Fournier, L., Rouault, J.-P., & Billaud, M. (2003) · Oncogene · doi:10.1038/sj.onc.1207179 · Cited by 61 · see citing works

Bioluminometric Assay of ADP and ATP at High ATP/ADP Ratios: Assay of ADP After Enzymatic Removal of ATP

Schultz, V., Sussman, I., Bokvist, K. B., & Tornheim, K. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1591 · Cited by 54 · see citing works

Resveratrol is neuroprotective because it is not a direct activator of Sirt1—A hypothesis

Tang, B. L. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.12.007 · Cited by 47 · see citing works

Functional analysis of LKB1/STK11 mutants and two aberrant isoforms found in Peutz-Jeghers Syndrome patients

Boudeau, J., Kieloch, A., Alessi, D. R., Stella, A., Guanti, G., & Resta, N. (2003) · Human Mutation · doi:10.1002/humu.9112 · Cited by 45 · see citing works

Cytosolic NAD+ content strictly depends on ATP concentration in isolated liver cells

Devin, A., Guérin, B., & Rigoulet, M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00612-1 · Cited by 24 · see citing works

Diabetic complications within the context of aging: Nicotinamide adenine dinucleotide redox, insulin C‐peptide, sirtuin 1–liver kinase B1–adenosine monophosphate‐activated protein kinase positive feedback and forkhead box O3

Ido, Y. (2016) · Journal of Diabetes Investigation · doi:10.1111/jdi.12485 · Cited by 21 · see citing works

Healthy Effects of Plant Polyphenols: Molecular Mechanisms

Leri, M., Scuto, M. C., Ontario, M. L., Calabrese, V., Calabrese, E. J., Bucciantini, M., & Stefani, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041250 · Cited by 440 · see citing works

Mediterranean diet nutrients to turn the tide against insulin resistance and related diseases

Mirabelli, M., Chiefari, E., Arcidiacono, B., Corigliano, D. M., Brunetti, F. S., Maggisano, V., Russo, D., Foti, D. P., & Brunetti, A. (2020) · Nutrients · doi:10.3390/nu12041066 · Cited by 272 · see citing works

A multi-scale approach to study biochemical and biophysical aspects of resveratrol on diesel exhaust particle-human primary lung cell interaction

Zhang, W., Li, Q., Tang, M., Zhang, H., Sun, X., Zou, S., Jensen, J. L., Liou, T. G., & Zhou, A. (2019) · Scientific Reports · doi:10.1038/s41598-019-54552-w · Cited by 245 · see citing works

The mechanism(s) of action of antioxidants: From scavenging reactive oxygen/nitrogen species to redox signaling and the generation of bioactive secondary metabolites

Hunyadi, A. (2019) · Medicinal Research Reviews · doi:10.1002/med.21592 · Cited by 229 · see citing works

Metabolic Control of Dendritic Cell Functions: Digesting Information

Wculek, S. K., Khouili, S. C., Priego, E., Heras‐Murillo, I., & Sancho, D. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00775 · Cited by 212 · see citing works

The Role of AMPK Activation for Cardioprotection in Doxorubicin-Induced Cardiotoxicity

Timm, K. N., & Tyler, D. J. (2020) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-020-06941-x · Cited by 189 · see citing works

Targeting AMPK Signaling as a Neuroprotective Strategy in Parkinson’s Disease

Curry, D. W., Stutz, B., Andrews, Z. B., & Elsworth, J. D. (2018) · Journal of Parkinson s Disease · doi:10.3233/jpd-171296 · Cited by 159 · see citing works

Unraveling the AMPK-SIRT1-FOXO Pathway: The In-Depth Analysis and Breakthrough Prospects of Oxidative Stress-Induced Diseases

Guan, G., Chen, Y., & Dong, Y. (2025) · Antioxidants · doi:10.3390/antiox14010070 · Cited by 165 · see citing works

Resveratrol targets PD-L1 glycosylation and dimerization to enhance antitumor T-cell immunity

Verdura, S., Cuyàs, E., Cortada, È., Brunet, J., López‐Bonet, E., Martı́n-Castillo, B., Bosch‐Barrera, J., Encinar, J. A., & Menéndez, J. A. (2020) · Aging · doi:10.18632/aging.102646 · Cited by 148 · 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

Interactions among mTORC, AMPK and SIRT: a computational model for cell energy balance and metabolism

Sadria, M., & Layton, A. T. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00706-1 · Cited by 141 · see citing works

In Vitro Models for Non-Alcoholic Fatty Liver Disease: Emerging Platforms and Their Applications

Ramos, M. J., Bandiera, L., Menolascina, F., & Fallowfield, J. A. (2022) · iScience · doi:10.1016/j.isci.2021.103549 · Cited by 127 · see citing works

AMPK: a therapeutic target of heart failure—not only metabolism regulation

Li, X., Liu, J., Lü, Q., Ren, D., Sun, X., Rousselle, T. V., Tan, Y., & Li, J. (2018) · Bioscience Reports · doi:10.1042/bsr20181767 · Cited by 118 · see citing works

Resveratrol improves osteogenic differentiation of senescent bone mesenchymal stem cells through inhibiting endogenous reactive oxygen species productionviaAMPK activation

Zhou, T., Yan, Y., Zhao, C., Xu, Y., Wang, Q., & Xu, N. (2019) · Redox Report · doi:10.1080/13510002.2019.1658376 · Cited by 102 · see citing works

Impaired nicotinamide adenine dinucleotide (NAD ⁺ ) metabolism in diabetes and diabetic tissues: Implications for nicotinamide‐related compound treatment

Fan, L., Cacicedo, J. M., & Ido, Y. (2020) · Journal of Diabetes Investigation · doi:10.1111/jdi.13303 · Cited by 86 · see citing works

Research Progress on Alzheimer's Disease and Resveratrol

Yan, Y., Yang, H., Xie, Y., Ding, Y., Kong, D., & Yu, H. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03007-0 · Cited by 91 · see citing works

AMPK and cardiac remodelling

Feng, Y., Zhang, Y., & Xiao, H. (2017) · Science China Life Sciences · doi:10.1007/s11427-017-9197-5 · Cited by 89 · see citing works

Cardiolipin-targeted peptides rejuvenate mitochondrial function, remodel mitochondria, and promote tissue regeneration during aging

Szeto, H. H., & Liu, S. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.10.013 · Cited by 87 · see citing works

Role of Flavonoids in Neurodegenerative Diseases: Limitations and Future Perspectives

Maan, G., Sikdar, B., Kumar, A., Shukla, R., & Mishra, A. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200416085330 · Cited by 85 · see citing works

SIRT1 Regulation in Ageing and Obesity

Pardo, P. S., & Boriek, A. M. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111249 · Cited by 90 · see citing works

Reactive Oxygen Species Induced Pathways in Heart Failure Pathogenesis and Potential Therapeutic Strategies

Mongirdienė, A., Skrodenis, L., Varoneckaitė, L., Mierkytė, G., & Gerulis, J. (2022) · Biomedicines · doi:10.3390/biomedicines10030602 · Cited by 83 · see citing works

Resveratrol, Metabolic Dysregulation, and Alzheimer’s Disease: Considerations for Neurogenerative Disease

Yang, A. J. T., Bagit, A., & MacPherson, R. E. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094628 · Cited by 74 · see citing works

Role of Sirtuins in Modulating Neurodegeneration of the Enteric Nervous System and Central Nervous System

Chandramowlishwaran, P., Vijay, A., Abraham, D., Li, G., Mwangi, S. M., & Srinivasan, S. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.614331 · Cited by 74 · see citing works

Genistein protects against ox-LDL-induced senescence through enhancing SIRT1/LKB1/AMPK-mediated autophagy flux in HUVECs

Zhang, H., Yang, X., Pang, X.-F., Zhao, Z., Yu, H., & Zhou, H. M. (2018) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-018-3476-8 · Cited by 64 · see citing works

Doxorubicin cardiomyopathy is ameliorated by acacetin via Sirt1‐mediated activation of AMPK/Nrf2 signal molecules

Wu, W., Cui, Y., Hong, Y., Li, Y., Wu, Y., Li, G., Li, G., & Wang, Y. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15859 · Cited by 62 · see citing works

Recent Advances in Health Benefits of Stilbenoids

Koh, Y., Ho, C., & Pan, M. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c03699 · Cited by 61 · see citing works

A Molecular Insight into the Role of Antioxidants in Nonalcoholic Fatty Liver Diseases

Ezhilarasan, D., & Thangavelu, L. P. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/9233650 · Cited by 63 · see citing works

Resveratrol Action on Lipid Metabolism in Cancer

Kisková, T., & Kassayová, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112704 · Cited by 53 · see citing works

Relieving Cellular Energy Stress in Aging, Neurodegenerative, and Metabolic Diseases, SIRT1 as a Therapeutic and Promising Node

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 50 · see citing works

AMPK in microvascular complications of diabetes and the beneficial effects of AMPK activators from plants

Basavarajappa, S. C., & Nandini, C. (2018) · Phytomedicine · doi:10.1016/j.phymed.2018.12.031 · Cited by 46 · see citing works

Role of Resveratrol in Prevention and Control of Cardiovascular Disorders and Cardiovascular Complications Related to COVID-19 Disease: Mode of Action and Approaches Explored to Increase Its Bioavailability

Gligorijević, N., Stanić-Vučinić, D., Radomirović, M., Stojadinović, M., Olgica, N., Khulal, U., & Veličković, T. Ć. (2021) · Molecules · doi:10.3390/molecules26102834 · Cited by 47 · see citing works

AMPK: An odyssey of a metabolic regulator, a tumor suppressor, and now a contextual oncogene

Penugurti, V., Mishra, Y. G., & Manavathi, B. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188785 · Cited by 38 · see citing works

Therapeutic Potential of Resveratrol in Diabetic Nephropathy According to Molecular Signaling

Salami, M., Salami, R., Mafi, A., Aarabi, M. H., Vakili, O., & Asemi, Z. (2021) · Current Molecular Pharmacology · doi:10.2174/1874467215666211217122523 · Cited by 37 · see citing works

The antioxidant resveratrol acts as a non-selective adenosine receptor agonist

Sánchez-Melgar, A., Albasanz, J. L., Guixà-González, R., Saleh, N., Selent, J., & Martı́n, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.03.019 · Cited by 34 · see citing works

Eugenol improves high-fat diet/streptomycin-induced type 2 diabetes mellitus (T2DM) mice muscle dysfunction by alleviating inflammation and increasing muscle glucose uptake

Jiang, Y., Feng, C., Shi, Y., Kou, X., & Le, G. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1039753 · Cited by 33 · see citing works

The effects of combined resveratrol and high intensity interval training on the hippocampus in aged male rats: An investigation into some signaling pathways related to mitochondria.

Amirazodi, M., Mehrabi, A., Rajizadeh, M. A., Bejeshk, M. A., Esmaeilpour, K., Daryanoosh, F., & Gaeini, A. A. (2022) · PubMed Central · doi:10.22038/ijbms.2022.57780.12853 · Cited by 31 · see citing works

A mitochondrial nexus in major depressive disorder: Integration with the psycho-immune-neuroendocrine network

Ciubuc-Batcu, M. T., Stapelberg, N. J. C., Headrick, J. P., & Renshaw, G. M. C. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166920 · Cited by 29 · see citing works

Resvega Alleviates Hydroquinone-Induced Oxidative Stress in ARPE-19 Cells

Bhattarai, N., Korhonen, E., Toppila, M., Koskela, A. K. J., Kaarniranta, K., Mysore, Y., & Kauppinen, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062066 · Cited by 27 · see citing works

Trans-Resveratrol Oral Bioavailability in Humans Using LipiSperse™ Dispersion Technology

Briskey, D. R., & Rao, A. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12121190 · Cited by 28 · see citing works

Resveratrol attenuates hydrogen peroxide‑induced apoptosis, reactive oxygen species generation, and PSGL‑1 and VWF activation in human umbilical vein endothelial cells, potentially via MAPK signalling pathways

Lou, Z., Li, X., Zhao, X., Du, K., Li, X., & Wang, B. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.8124 · Cited by 27 · see citing works

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 26 · see citing works

AMPK in Intestinal Health and Disease: A Multifaceted Therapeutic Target for Metabolic and Inflammatory Disorders

Yibcharoenporn, C., Muanprasat, C., Moonwiriyakit, A., Satitsri, S., & Pathomthongtaweechai, N. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s507489 · Cited by 25 · see citing works

Natural Products and Altered Metabolism in Cancer: Therapeutic Targets and Mechanisms of Action

Talib, W. H., Baban, M. M., Bulbul, M. F., Al-Zaidaneen, E., Allan, A., Al-Rousan, E. W., Ahmad, R. H. Y., Alshaeri, H. K., Alasmari, M. M., & Law, D. S. N. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179593 · Cited by 25 · see citing works

Resveratrol and Vitamin D: Eclectic Molecules Promoting Mitochondrial Health in Sarcopenia

Russo, C., Valle, M. S., D’Angeli, F., Surdo, S., & Malaguarnera, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147503 · Cited by 24 · see citing works

Oregonin inhibits inflammation and protects against barrier disruption in intestinal epithelial cells

Chi, J.-H., Seo, G. S., & Lee, S. H. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.04.006 · Cited by 23 · see citing works

Mitigation of Radiation-induced Gastrointestinal System Injury using Resveratrol or Alpha-lipoic Acid: A Pilot Histopathological Study

Farhood, B., Hassanzadeh, G., Amini, P., Shabeeb, D., Musa, A. E., Khodamoradi, E., Mohseni, M., Aliasgharzadeh, A., Moradi, H., & Najafi, M. (2019) · Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry · doi:10.2174/1871523018666191111124028 · Cited by 22 · see citing works

Activation of cardiac Nmnat/NAD+/SIR2 pathways mediates endurance exercise resistance to lipotoxic cardiomyopathy in aging Drosophila

Wen, D., Zheng, L., Lǚ, K., & Hou, W.-Q. (2021) · Journal of Experimental Biology · doi:10.1242/jeb.242425 · Cited by 22 · see citing works

Inhibition of Non-Small Cell Lung Cancer Proliferation and Survival by Rosemary Extract Is Associated with Activation of ERK and AMPK

O’Neill, E. J., Moore, J., Song, J. S., & Tsiani, E. (2021) · Life · doi:10.3390/life12010052 · Cited by 22 · see citing works

Resveratrol reserved hypoxia-ischemia induced childhood hippocampal dysfunction and neurogenesis via improving mitochondrial dynamics

Li, H., Xiao, L., Liu, Z., Wu, S., Guo, J., Shi, R., Sun, Y., Wang, Y., & Yin, H. (2019) · Neuroscience Research · doi:10.1016/j.neures.2019.11.012 · Cited by 22 · see citing works

Metformin alleviates the cognitive impairment caused by aluminum by improving energy metabolism disorders in mice

Song, Y., Liu, Z., Zhu, X., Hao, C., Hao, W., Wu, S., Yang, J., Lu, X., & Jin, C. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115140 · Cited by 21 · see citing works

Innovative treatments for obesity and NAFLD: A bibliometric study on antioxidants, herbs, phytochemicals, and natural compounds

Pezzino, S., Sofia, M., Mazzone, C., Litrico, G., Greco, L. P., Gallo, L., Greca, G. L., & Latteri, S. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e35498 · Cited by 23 · see citing works

Has resveratrol a potential for mucopolysaccharidosis treatment?

Rintz, E., Pierzynowska, K., Podlacha, M., & Węgrzyn, G. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173534 · Cited by 21 · see citing works

Roles of AMPK and Its Downstream Signals in Pain Regulation

Wang, S., & Dai, Y. (2021) · Life · doi:10.3390/life11080836 · Cited by 21 · see citing works

Resveratrol Inhibits Porcine Intestinal Glucose and Alanine Transport: Potential Roles of Na+/K+-ATPase Activity, Protein Kinase A, AMP-Activated Protein Kinase and the Association of Selected Nutrient Transport Proteins with Detergent Resistant Membranes

Klinger, S., & Breves, G. (2018) · Nutrients · doi:10.3390/nu10030302 · Cited by 21 · see citing works

Association of placental nutrient sensing pathways with birth weight

Lazo-de-la-Vega-Monroy, M.-L., Mata-Tapia, K.-A., García-Santillán, J.-A., Corona-Figueroa, M.-A., Gónzalez-Domínguez, M.-I., Gomez-Zapata, H.-M., Malacara, J. M., Daza-Benítez, L., & Barbosa‐Sabanero, G. (2020) · Reproduction · doi:10.1530/rep-20-0186 · Cited by 20 · see citing works

A Novel Multidrug Combination Mitigates Rat Liver Steatosis Through Activating AMPK Pathway During Normothermic Machine Perfusion

Xu, M., Zhou, F., Ahmed, O., Upadhya, G. A., Jia, J., Lee, C., Xing, J., Li, Y., Shim, S. H., Zhang, Z., et al. (2021) · Transplantation · doi:10.1097/tp.0000000000003675 · Cited by 19 · see citing works

Resveratrol Induces Myotube Development by Altering Circadian Metabolism via the SIRT1-AMPK-PP2A Axis

Avital-Cohen, N., Chapnik, N., & Froy, O. (2024) · Cells · doi:10.3390/cells13121069 · Cited by 16 · see citing works

AMP-independent activator of AMPK for treatment of mitochondrial disorders

Moore, T., Yanes, R. E., Calton, M. A., Vollrath, D., Enns, G. M., & Cowan, T. M. (2020) · PLoS ONE · doi:10.1371/journal.pone.0240517 · Cited by 16 · see citing works

Nanostructured Lipid Carriers Deliver Resveratrol, Restoring Attenuated Dilation in Small Coronary Arteries, via the AMPK Pathway

Astley, C., Houacine, C., Zaabalawi, A., Wilkinson, F. L., Lightfoot, A. P., Alexander, M. Y., Whitehead, D. E., Singh, K. K., & Azzawi, M. (2021) · Biomedicines · doi:10.3390/biomedicines9121852 · Cited by 16 · see citing works

The role of resveratrol in neurogenesis: a systematic review

Azargoonjahromi, A., Abutalebian, F., & Hoseinpour, F. (2024) · Nutrition Reviews · doi:10.1093/nutrit/nuae025 · Cited by 17 · see citing works

Selective AMPK activator leads to unfolded protein response downregulation and induces breast cancer cell death and autophagy

Mello, A. L. D. N., Sagrillo, F. S., de Souza, A. G., Costa, A. R. P., Campos, V. R., Cunha, A. C., Filho, R. I., Boechat, F. D. C. S., Sola‐Penna, M., de Souza, M. C. B. V., et al. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119470 · Cited by 16 · see citing works

Tetrahydroxy stilbene glucoside alters neurogenesis and neuroinflammation to ameliorate radiation-associated cognitive disability via AMPK/Tet2

Miao, B.-B., Gao, D., Hao, J.-P., Li, Y.-L., Li, L., Wang, J., Xiao, X., Yang, C., & Zhang, L. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108928 · Cited by 16 · see citing works

Endurance exercise resistance to lipotoxic cardiomyopathy is associated with cardiac NAD+/dSIR2/PGC-1αpathway activation in oldDrosophila

Wen, D., Zheng, L., Li, J., Cheng, D., Liu, Y., Lǚ, K., & Hou, W.-Q. (2019) · Biology Open · doi:10.1242/bio.044719 · Cited by 15 · see citing works

Resveratrol Prevents GLUT3 Up-Regulation Induced by Middle Cerebral Artery Occlusion

Aguilar, G. F. G., Alquisiras-Burgos, I., Franco‐Pérez, J., Pineda-Ramírez, N., Ortíz-Plata, A., Torres, I., Pedraza‐Chaverrí, J., & Aguilera, P. (2020) · Brain Sciences · doi:10.3390/brainsci10090651 · Cited by 15 · see citing works

Perisciatic Nerve Dexmedetomidine Alleviates Spinal Oxidative Stress and Improves Peripheral Mitochondrial Dynamic Equilibrium in a Neuropathic Pain Mouse Model in an AMPK-Dependent Manner

Mu, Y., Yang, M., Chen, Y., Li, Y., Zhu, D., Cui, J. G., & Yu, L. (2022) · Disease Markers · doi:10.1155/2022/6889676 · Cited by 14 · see citing works

A comprehensive review of the effects of resveratrol on glucose metabolism: unveiling the molecular pathways and therapeutic potential in diabetes management

Moon, D. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08746-1 · Cited by 13 · see citing works

Resveratrol and SIRT1 Activators for the Treatment of Aging and Age-Related Diseases

Stacchiotti, A., Favero, G., & Rezzani, R. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.78977 · Cited by 13 · see citing works

The capacity of differentiation of stromal vascular fraction cells into beige adipocytes is markedly reduced in subjects with overweight/obesity and insulin resistance: effect of genistein

Rodríguez-López, L. A., Torre-Villalvazo, I., Alemán, G., Flores‐López, A., Guevara‐Cruz, M., Sánchez‐Tapia, M., Torre-Anaya, E. A., Martínez-López, V., Vásquez‐Reyes, S., Torres‐Villalobos, G., et al. (2021) · International Journal of Obesity · doi:10.1038/s41366-021-00921-3 · Cited by 12 · see citing works

Resveratrol Induces the Fasting State and Alters Circadian Metabolism in Hepatocytes

Chatam, O., Chapnik, N., & Froy, O. (2022) · Plant Foods for Human Nutrition · doi:10.1007/s11130-022-00954-7 · Cited by 12 · see citing works

Resveratrol-based biorefinery models for favoring its inclusion along the market value-added chains: A critical review

Arias, A., Costa, C. E., Moreira, M. T., Feijóo, G., & Domingues, L. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.168199 · Cited by 12 · see citing works

Resveratrol Suppresses Matrix Metalloproteinase-2 Activation Induced by Lipopolysaccharide in Mouse Osteoblasts via Interactions with AMP-Activated Protein Kinase and Suppressor of Cytokine Signaling 1

Yu, Y.-Q., Li, X., Mi, J., Qu, L., Yang, D., Guo, J., & Qiu, L. (2018) · Molecules · doi:10.3390/molecules23092327 · Cited by 12 · see citing works

Effects of grape phenolics, myricetin and piceatannol, on bovine granulosa and theca cell proliferation and steroid production in vitro

SPICER, L. J., & Schütz, L. F. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113288 · Cited by 10 · see citing works

Inhibition of lactate dehydrogenase A by diclofenac sodium induces apoptosis in H e L a cells through activation of AMPK

Malla, A., Gupta, S., & Sur, R. (2024) · FEBS Journal · doi:10.1111/febs.17158 · Cited by 9 · see citing works

AMPK‐Dependent Epigenetic Regulation of Metabolism Mediates the Anti‐Cancer Action of Pterostilbene in Hepatocellular Carcinoma

Boycott, C., Beetch, M., Lubecka, K., Ramsey, B. S., Torregrosa‐Allen, S. E., Elzey, B. D., Cox, A. D., Lanman, N. A., de Conti, A., Li, M., et al. (2025) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.70217 · Cited by 8 · see citing works

Activation of the AMPK Signaling and Brain Function: A Friend or Foe?

Nicol, N. I., & Ma, T. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70283 · Cited by 8 · see citing works

Natural products are an important source for proteasome regulating agents

An, P., Zhang, L., Peng, W., Chen, Y., Liu, Q., Luan, X., & Zhang, H. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153799 · Cited by 8 · see citing works

Transient Ca2+ entry by plasmalogen-mediated activation of receptor potential cation channel promotes AMPK activity

Honsho, M., Mawatari, S., & Fujino, T. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1008626 · Cited by 6 · see citing works

Relating aging and autophagy – a new perspective towards the welfare of human health

Chowdhury, S. G., Ray, R., & Karmakar, P. (2023) · EXCLI journal · doi:10.17179/excli2023-6300 · Cited by 6 · see citing works

Tuning the Fire: Context-Dependent Mitochondrial ROS Signaling, Mitohormesis, and Redox-Modulating Interventions

Charidemou, E., Andreou, E. P., & Papaneophytou, C. P. (2026) · Biomolecules · doi:10.3390/biom16060867 · Cited by 7 · see citing works

Lygodium microphyllum Inhibits de Novo Lipogenesis Activity in the Hepatocytes of High-Fat High-Fructose-Induced Rats by Increasing the Levels of SIRT1 and AMPK

Anggreini, P., Kuncoro, H., Sumiwi, S. A., & Levita, J. (2024) · Journal of Experimental Pharmacology · doi:10.2147/jep.s473763 · Cited by 5 · see citing works

Effect of Resveratrol in Melinjo Seed (Gnetum gnemon L.) Extract on Type 2 Diabetes Mellitus Patients and its Possible Mechanism: A Review

Ariyanto, E. F., Danil, A. S., Rohmawaty, E., Sujatmiko, B., & Berbudi, A. (2022) · Current Diabetes Reviews · doi:10.2174/1573399818666220228160908 · Cited by 5 · see citing works

Differentiated modulation of signaling molecules AMPK and SIRT1 in experimentally drug-induced hepatocyte injury

WOJNAROVÁ, L., Canová, N. K., Arora, M., & Farghali, H. (2022) · Biomedical Papers · doi:10.5507/bp.2022.018 · Cited by 5 · see citing works

Exploring Skin Longevity Pathways: Rosa hybrid Extract-Mediated AMP-Activated Protein Kinase Activation, Antioxidant, and Autophagic Mechanisms in Human Keratinocytes

Gouin, O., Cavagnino, A., Azadiguian, G., Jäger, S., Comte, G., Bendahmane, M., Breton, L., Baraibar, M. A., & Black, A. F. (2025) · Cosmetics · doi:10.3390/cosmetics12020057 · Cited by 4 · see citing works

From molecular damage to regulatory constraint: epigenetic and metabolic limits of cellular plasticity in aging

Godlewski, A., & Dziaman, T. (2026) · Frontiers in Aging · doi:10.3389/fragi.2026.1872180 · Cited by 4 · see citing works

Low-dose trans-resveratrol induce poly(ADP)-ribosylation-dependent increase of the PPAR-γ protein expression level in the in vitro model of non-alcoholic fatty liver disease

Kachlishvili, T., Ksovreli, M., Gabruashvili, D., Museridze, M., Bezhuashvili, M., Zaalishvili, G., & Kulikova, N. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05863-z · Cited by 3 · see citing works

Is resveratrol a prospective therapeutic strategy in the co-association of glucose metabolism disorders and neurodegenerative diseases?

Ribeiro, R., dos Santos, A. C. S., Calazans, M., de Oliveira, A. C. P., & Vieira, L. B. (2021) · Nutritional Neuroscience · doi:10.1080/1028415x.2021.1972514 · Cited by 3 · see citing works

Cardiomyocyte-specific deletion of PTP1B protects against HFD-induced cardiomyopathy through direct regulation of cardiac metabolic signalingPreprint

Sun, Y., Chanrasekhar, V., Kessinger, C. W., Tang, P., Gao, Y., Kamli-Salino, S., Nelson, K., Delibegović, M., Abel, E. D., & Kontaridis, M. I. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.19.541546 · Cited by 3 · see citing works

SRT2183 and SRT1720, but not Resveratrol, Inhibit Osteoclast Formation and Resorption in the Presence or Absence of Sirt1Preprint

Thiyagarajan, R., González, M. R., Zaw, C., Seldeen, K. L., Hernandez, M., Pang, M., & Troen, B. R. (2020) · Research Square · doi:10.21203/rs.3.rs-125262/v1 · Cited by 3 · see citing works

Qualia NAD+® Increases NAD+ Levels In Human Participants: A Double-Blind, Placebo-Controlled StudyPreprint

Blomquist, S. A., Kelly, G., Adães, S., D’Adamo, C. R., Ardagh, A., Ramer, S., & Scuba, W. (2025) · medRxiv · doi:10.1101/2025.03.19.25324259 · Cited by 3 · see citing works

Mediterranean Pattern Diet in Multiple Sclerosis: A Review Focusing on Immunometabolites

Papiri, G., Paci, C., D’Andreamatteo, G., Membrino, V., Crescenzo, T. D., Cacchiò, G., Cagnetti, C., & Vignini, A. (2025) · Current Neuropharmacology · doi:10.2174/011570159x382929250719084728 · Cited by 2 · see citing works

AMPK : Accumulating Evidence in Support of its role in Dual Regulation of Vascular Function and Metabolism During Human Pregnancy

MOORE, L. G., Wesolowski, S. R., Lorca, R. A., & Julian, C. G. (2025) · Acta Physiologica · doi:10.1111/apha.70093 · Cited by 2 · see citing works

Zein/β-cyclodextrin nanocarriers for dual delivery of resveratrol and piperine: a synergistic approach for enhanced nutraceutical stability and function

Khanal, A., Cheunkar, S., & Oaew, S. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149531 · Cited by 2 · see citing works

Resveratrol as a Regulator of Inflammation, Oxidative Stress, and Glucose Stability in Diabetes

Hasbullah, A. M., Binesh, A., & Venkatachalam, K. (2025) · Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry · doi:10.2174/0118715230414089250926071435 · Cited by 2 · see citing works

Polyphenols and Neuroprotection: The Role of Adenosine Receptors

Sánchez-Melgar, A., Albasanz, J. L., & Martı́n, M. (2019) · Journal of Caffeine and Adenosine Research · doi:10.1089/caff.2019.0007 · Cited by 1 · see citing works

Modulatory effect of ethylacetate fraction from Theobroma cacao pod husk on blood pressure in L-NAME-induced hypertensive rats using in vivo and in silico approaches

Nwaso-Sunday, E. O., Adeoye, R. I., Olasehinde, O. R., Afolabi, O. B., & Arise, R. O. (2024) · Journal of Applied Pharmaceutical Science · doi:10.7324/japs.2024.154314 · Cited by 1 · see citing works

Is choline kinase alpha a drug target for obesity?

Lacal, J. C., Ibrahim, S. A., & Zimmerman, T. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1492753 · Cited by 1 · see citing works

The Combination of Resveratrol and Conjugated Linoleic Acid Dienes Enhances the Individual Effects of These Molecules on De Novo Fatty Acid Biosynthesis in 3T3-L1 Adipocytes

Oczkowicz, J., Piasna-Słupecka, E., Drozdowska, M., Koronowicz, A. A., & Kopeć, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252413429 · Cited by 1 · see citing works

Resveratrol engages SIRT1/AMPK networks to restore BDNF signaling, autophagy, and mitochondrial function in age-related cognitive decline: A geroscience perspective

Al-Dhahi, A. S., Al‐kuraishy, H. M., Fawzy, M. N., & Batiha, G. E. (2026) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2026.111925 · Cited by 1 · see citing works

Resveratrol prevents gallstones in mice fed on a high fat diet via regulating PPAR-γ and SR-BI

Zhao, M., Xie, B., Li, Y., Dong, H., Jiang, S., Zhu, T., Wu, X., Xu, C., Zhang, J., Sun, S., et al. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1543865 · Cited by 1 · see citing works

Deletion of PTP1B in cardiomyocytes alters cardiac metabolic signaling to protect against cardiomyopathy induced by a high-fat diet

Sun, Y., Mishra, A. K., Chanrasekhar, V., Door, M. M., Kessinger, C. W., Xu, B., Tang, P., Gao, Y., Kamli-Salino, S., Nelson, K., et al. (2025) · Science Signaling · doi:10.1126/scisignal.adp6006 · Cited by 1 · see citing works

Identifying novel targets of resveratrol

Legg, K. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3717 · Cited by 8 · see citing works

AMP-activated protein kinase-deficient mice are resistant to the metabolic effects of resveratrol

Um, J.-H., Park, S.-J., Kang, H., Yang, S., Foretz, M., McBurney, M. W., Kim, M. K., Viollet, B., & Chung, J. H. (2010) · Diabetes · doi:10.2337/db09-0482 · Cited by 647 · see citing works

SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function

Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.003 · Cited by 1,602 · see citing works

SIRT1 takes a backseat to AMPK in the regulation of insulin sensitivity by resveratrol

Fullerton, M. D., & Steinberg, G. R. (2010) · Diabetes · doi:10.2337/db09-1732 · Cited by 77 · see citing works

ORIGINAL ARTICLE AMP-Activated Protein Kinase–Deficient Mice Are Resistant to the Metabolic Effects of Resveratrol

Um, J.-H., Park, S.-J., Kang, H., Yang, S., Foretz, M., Mcburney, M. W., Kim, M. K., Viollet, B., & Chung, J. H. (2013)