Discovery of MK-8722: A systemic, direct pan-activator of amp-activated protein kinase

AMPK in Health and Disease

Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,633 · see citing works

Exercise, GLUT4, and skeletal muscle glucose uptake

Richter, E. A., & Hargreaves, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00038.2012 · Cited by 1,407 · see citing works

Single phosphorylation sites in Acc1 and Acc2 regulate lipid homeostasis and the insulin-sensitizing effects of metformin

Fullerton, M. D., Galic, S., Marcinko, K., Sikkema, S., Pulinilkunnil, T., Chen, Z.-P., O'Neill, H. M., Ford, R. J., Palanivel, R., O'Brien, M., et al. (2013) · Nature Medicine · doi:10.1038/nm.3372 · Cited by 893 · see citing works

Structural basis of AMPK regulation by small molecule activators

Xiao, B., Sanders, M. J., Carmena, D., Bright, N. J., Haire, L. F., Underwood, E., Patel, B. R., Heath, R. B., Walker, P. A., Hallén, S., et al. (2013) · Nature Communications · doi:10.1038/ncomms4017 · Cited by 547 · see citing works

AMP‐activated protein kinase in the regulation of hepatic energy metabolism: from physiology to therapeutic perspectives

Viollet, B., Guigas, B., Leclerc, J., Hébrard, S., Lantier, L., Mounier, R., Andréelli, F., & Foretz, M. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01970.x · Cited by 486 · see citing works

AMP-Activated Protein Kinase in the Heart

Arad, M., Seidman, C. E., & Seidman, J. G. (2007) · Circulation Research · doi:10.1161/01.res.0000258446.23525.37 · Cited by 356 · see citing works

Systemic pan-AMPK activator MK-8722 improves glucose homeostasis but induces cardiac hypertrophy

Myers, R. W., Guan, H.-P., Ehrhart, J., Petrov, A., Prahalada, S., Tozzo, E., Yang, X., Kurtz, M. M., Trujillo, M., Gonzalez Trotter, D., et al. (2017) · Science · doi:10.1126/science.aah5582 · Cited by 346 · see citing works

AMPK and Exercise: Glucose Uptake and Insulin Sensitivity

O'Neill, H. M. (2013) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2013.37.1.1 · Cited by 295 · see citing works

<scp>AMP</scp> ‐activated protein kinase: a key regulator of energy balance with many roles in human disease

Grahame Hardie, D. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12268 · Cited by 285 · see citing works

AMP-activated protein kinase: maintaining energy homeostasis at the cellular and whole-body levels

Hardie, D. G. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161148 · Cited by 281 · see citing works

5′AMP activated protein kinase expression in human skeletal muscle: effects of strength training and type 2 diabetes

Wojtaszewski, J. F. P., Birk, J. B., Frøsig, C., Holten, M., Pilegaard, H., & Dela, F. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.082669 · Cited by 170 · see citing works

Expression of the AMP‐activated protein kinase β1 and β2 subunits in skeletal muscle

Chen, Z., Heierhorst, J., Mann, R. J., Mitchelhill, K. I., Michell, B. J., Witters, L. A., Lynch, G. S., Kemp, B. E., & Stapleton, D. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01371-x · Cited by 134 · see citing works

A-769662 activates AMPK β 1 -containing complexes but induces glucose uptake through a PI3-kinase-dependent pathway in mouse skeletal muscle

Treebak, J. T., Birk, J. B., Hansen, B. F., Olsen, G. S., & Wojtaszewski, J. F. P. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00051.2009 · Cited by 108 · see citing works

Small Molecule Adenosine 5′-Monophosphate Activated Protein Kinase (AMPK) Modulators and Human Diseases

Rana, S., Blowers, E. C., & Natarajan, A. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401994c · Cited by 62 · see citing works

Effects of Aerobic Training, Resistance Training, or Both on Glycemic Control in Type 2 Diabetes: A Randomized Trial

Sigal, R. J., Kenny, G. P., Boulé, N. G., Wells, G. A., Prud'homme, D., Fortier, M., Reid, R. D., Tulloch, H., Coyle, D., Phillips, P., et al. (2007) · Annals of Internal Medicine · doi:10.7326/0003-4819-147-6-200709180-00005 · Cited by 48 · see citing works

Recent progress in the identification of adenosine monophosphate-activated protein kinase (AMPK) activators

Cameron, K. O., & Kurumbail, R. G. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.09.065 · Cited by 43 · see citing works

Type 2 Diabetes Medication Review

Sterrett, J., Bragg, S. W., & Weart, C. W. (2016) · The American Journal of the Medical Sciences · doi:10.1016/j.amjms.2016.01.019 · Cited by 35 · see citing works

Hit-to-Lead Optimization and Discovery of 5-((5-([1,1′-Biphenyl]-4-yl)-6-chloro-1 H -benzo[ d ]imidazol-2-yl)oxy)-2-methylbenzoic Acid (MK-3903): A Novel Class of Benzimidazole-Based Activators of AMP-Activated Protein Kinase

Lan, P., Romero, F. A., Wódka, D., Kassick, A. J., Dang, Q., Gibson, T., Cashion, D. K., Zhou, G., Chen, Y., Zhang, X., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01344 · Cited by 28 · see citing works

AMPK, Mitochondrial Function, and Cardiovascular Disease

Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286 · 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

The Race to Bash NASH: Emerging Targets and Drug Development in a Complex Liver Disease

Romero, F. A., Jones, C. T., Xu, Y., Fenaux, M., & Halcomb, R. L. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01701 · Cited by 126 · see citing works

Mapping the Efficiency and Physicochemical Trajectories of Successful Optimizations

Young, R. J., & Leeson, P. D. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00180 · Cited by 112 · see citing works

Spatial regulation of AMPK signaling revealed by a sensitive kinase activity reporter

Schmitt, D. L., Curtis, S. D., Leung, A., Zhang, J., He, C. Y., He, C. Y., Mehta, S., Rangamani, P., Shaw, R. J., & Zhang, J. (2022) · Nature Communications · doi:10.1038/s41467-022-31190-x · Cited by 82 · see citing works

The Role of AMPK Signaling in Brown Adipose Tissue Activation

van der Vaart, J. I., Boon, M. R., & Houtkooper, R. H. (2021) · Cells · doi:10.3390/cells10051122 · Cited by 82 · see citing works

Metabolic control by AMPK in white adipose tissue

Göransson, O., Kopietz, F., & Rider, M. H. (2023) · Trends in Endocrinology &amp; Metabolism · doi:10.1016/j.tem.2023.08.011 · Cited by 74 · see citing works

Molecular Profiling Reveals a Common Metabolic Signature of Tissue Fibrosis

Zhang, J., Muise, E. S., Han, S., Kutchukian, P. S., Costet, P., Zhu, Y., Kan, Y., Zhou, H., Shah, V., Huang, Y., et al. (2020) · Cell Reports Medicine · doi:10.1016/j.xcrm.2020.100056 · Cited by 54 · see citing works

Pharmacological Manipulation of Translation as a Therapeutic Target for Chronic Pain

Yousuf, M. S., Shiers, S. I., Sahn, J. J., & Price, T. J. (2020) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000030 · Cited by 55 · see citing works

AMPK as a mediator of tissue preservation: time for a shift in dogma?

Langer, H. T., Rohm, M., Goncalves, M. D., & Sylow, L. (2024) · Nature Reviews Endocrinology · doi:10.1038/s41574-024-00992-y · Cited by 51 · see citing works

Design, semisynthesis, α-glucosidase inhibitory, cytotoxic, and antibacterial activities of p-terphenyl derivatives

Zhang, X., Mou, X., Mao, N., Hao, J., Liu, M., Zheng, J., Wang, C., Gu, Y., & Shao, C. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.057 · Cited by 51 · see citing works

Structures of AMP-activated protein kinase bound to novel pharmacological activators in phosphorylated, non-phosphorylated, and nucleotide-free states

Yan, Y., Zhou, X. E., Novick, S. J., Shaw, S. J., Li, Y., Brunzelle, J. S., Hitoshi, Y., Griffin, P. R., Xu, H. E., & Melcher, K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004883 · Cited by 44 · see citing works

Alleviation of paclitaxel-induced mechanical hypersensitivity and hyperalgesic priming with AMPK activators in male and female mice

Inyang, K. E., McDougal, T. A., Ramirez, E. D., Williams, M., Laumet, G. O., Kavelaars, A., Heijnen, C. J., Burton, M. D., Dussor, G. O., & Price, T. J. (2019) · Neurobiology of Pain · doi:10.1016/j.ynpai.2019.100037 · Cited by 43 · see citing works

AMPK and Diseases: State of the Art Regulation by AMPK-Targeting Molecules

Tarasiuk, O., Miceli, M., Domizio, A. D., & Nicolini, G. (2022) · Biology · doi:10.3390/biology11071041 · Cited by 39 · see citing works

PAN-AMPK Activation Improves Renal Function in a Rat Model of Progressive Diabetic Nephropathy

Zhou, X., Muise, E. S., Haimbach, R. E., Sebhat, I. K., Zhu, Y., Liu, F., Souza, S. C., Kan, Y., Pinto, S., Kelley, D. E., et al. (2019) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.119.258244 · Cited by 28 · see citing works

Indirect AMP-Activated Protein Kinase Activators Prevent Incision-Induced Hyperalgesia and Block Hyperalgesic Priming, Whereas Positive Allosteric Modulators Block Only Priming in Mice

Inyang, K. E., Burton, M. D., Szabo-Pardi, T. A., Winchester, E. W., McDougal, T. A., Ramirez, E. D., Pradhan, G., Dussor, G. O., & Price, T. J. (2019) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.119.258400 · Cited by 28 · see citing works

AMPK regulates phagophore-to-autophagosome maturation

Barnaba, C., Broadbent, D. G., Kaminsky, E. G., Perez, G. I., & Schmidt, J. C. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202309145 · 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

Small Molecule Modulators of AMP-Activated Protein Kinase (AMPK) Activity and Their Potential in Cancer Therapy

Strang, J. E., Astridge, D. D., Nguyen, V., & Reigan, P. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02354 · Cited by 25 · see citing works

Pseudonatural Products for Chemical Biology and Drug Discovery

Greiner, L. C., Pahl, A., Heinzke, A. L., Zdrazil, B., Leach, A. R., Young, R. J., Leeson, P. D., & Waldmann, H. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00643 · Cited by 23 · see citing works

Structural elucidation of 3-nitrophenylhydrazine derivatives of tricarboxylic acid cycle acids and optimization of their fragmentation to boost sensitivity in liquid chromatography-mass spectrometry

Hodek, O., Henderson, J., Argemi‐Muntadas, L., Khan, A., & Möritz, T. (2023) · Journal of Chromatography B · doi:10.1016/j.jchromb.2023.123719 · Cited by 22 · see citing works

Optimization of Metabolic and Renal Clearance in a Series of Indole Acid Direct Activators of 5′-Adenosine Monophosphate-Activated Protein Kinase (AMPK)

Edmonds, D. J., Kung, D. W., Kalgutkar, A. S. S., Filipski, K. J., Ebner, D. C., Cabral, S., Smith, A. C. T., Aspnes, G. E., Bhattacharya, S. K., Borzilleri, K. A., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01641 · Cited by 21 · see citing works

Macrophage AMPK β1 activation by PF-06409577 reduces the inflammatory response, cholesterol synthesis, and atherosclerosis in mice

Day, E. A., Townsend, L. K., Rehal, S., Batchuluun, B., Wang, D., Morrow, M. R., Lu, R., Lundenberg, L., Lu, J. H., Desjardins, E. M., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108269 · Cited by 20 · see citing works

Acute, next‐generation AMPK activation initiates a disease‐resistant gene expression program in dystrophic skeletal muscle

Ng, S. Y., Mikhail, A. I., Mattina, S. R., Manta, A., Diffey, I. J., & Ljubicic, V. (2023) · The FASEB Journal · doi:10.1096/fj.202201846rr · Cited by 18 · see citing works

Metformin slows liver cyst formation and fibrosis in experimental model of polycystic liver disease

Sato, Y., Qiu, J., Hirose, T., Miura, T., Sato, Y., Kohzuki, M., & Ito, O. (2021) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00120.2020 · Cited by 17 · see citing works

Oxadiazolopyridine Derivatives as Efficacious Mitochondrial Uncouplers in the Prevention of Diet-Induced Obesity

Murray, J. H., Burgio, A. L., Beretta, M., Hargett, S. R., Harris, T. E., Olzomer, E. M., Grams, R. J., Garcia, C. J., Li, C., Salamoun, J. M., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01573 · Cited by 14 · see citing works

AMPK protects endothelial cells against HSV-1 replication via inhibition of mTORC1 and ACC1

Doshi, H., Spengler, K., Godbole, A., Gee, Y. S., Baell, J. B., Oakhill, J. S., Henke, A., & Heller, R. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.00417-23 · Cited by 16 · see citing works

Phosphorylation-Inducing Molecules for Regulating Dynamic Cellular Processes

Pergu, R., Sreekanth, V., Kokkonda, P., Lai, S., Tiwari, P. K., Singh, S., Kawai, J., Singha, S., Tian, W., Thimaradka, V., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c04275 · Cited by 15 · see citing works

Gossypetin Prevents the Progression of Nonalcoholic Steatohepatitis by Regulating Oxidative Stress and AMP-Activated Protein Kinase

Oh, E.-J., Lee, J., Cho, S., Kim, S. W., Jo, K. W., Shin, W., Gwak, S. H., Ha, J., Jeon, S. Y., Park, J.-H., et al. (2023) · Molecular Pharmacology · doi:10.1124/molpharm.123.000675 · Cited by 12 · see citing works

Design, synthesis and anti-HBV activity evaluation of new substituted imidazo[4,5-b]pyridines

Gerasi, M., Frakolaki, E., Papadakis, G., Chalari, A., Lougiakis, N., Marakos, P., Pouli, N., & Vassilaki, N. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.103580 · Cited by 12 · see citing works

Identification of novel indole derivatives as highly potent AMPK activators with anti-diabetic profiles

Tamura, Y., Morita, I., Hinata, Y., Kojima, E., Ozasa, H., Ikemoto, H., Asano, M., Wada, T., Hayasaki‐Kajiwara, Y., Iwasaki, T., et al. (2022) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2022.128769 · Cited by 11 · see citing works

Optimization of Pharmacokinetic and In Vitro Safety Profile of a Series of Pyridine Diamide Indirect AMPK Activators

Shaw, S. J., Goff, D. A., Boralsky, L. A., Singh, R., Sweeny, D. J., Park, G., Sun, T., Jenkins, Y., Markovtsov, V. V., Issakani, S. D., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01983 · Cited by 10 · see citing works

Identification of novel benzimidazole derivatives as highly potent AMPK activators with anti-diabetic profiles

Tamura, Y., Morita, I., Hinata, Y., Kojima, E., Sasaki, Y., Wada, T., Asano, M., Fujioka, M., Hayasaki‐Kajiwara, Y., Iwasaki, T., et al. (2022) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2022.129059 · Cited by 9 · see citing works

The role of AMP-activated protein kinase activators on energy balance and cellular metabolism in type 2 diabetes mellitus

Aydın, S., Tekinalp, S. G., Tuzcu, B., Çam, F., Sevik, M. O., Tatar, E., Kalaskar, D. M., & Çam, M. E. (2024) · Obesity Medicine · doi:10.1016/j.obmed.2024.100577 · Cited by 7 · see citing works

An update on current type 2 diabetes mellitus (T2DM) druggable targets and drugs targeting them

Uniyal, P., Panwar, S., Bhatt, A., Marianesan, A. B., Kumar, R., Singh, T. G., Tyagi, Y., Bushi, G., Gaidhane, A. M., & Kumar, B. (2025) · Molecular Diversity · doi:10.1007/s11030-025-11149-y · Cited by 7 · see citing works

AMPKβ isoform expression patterns in various adipocyte models and in relation to body mass index

Kopietz, F., Degerman, E., & Göransson, O. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.928964 · Cited by 7 · see citing works

Imaging Subcellular AMPK Activity Using an Excitation‐Ratiometric AMPK Activity Reporter

Schmitt, D. L. (2023) · Current Protocols · doi:10.1002/cpz1.771 · Cited by 6 · see citing works

The drug discovery and therapeutic nano-strategies targeting cellular senescence

Wang, Y., Liu, M., Chen, X., Wang, S., Li, J., Sun, Y., Zheng, X., Zhang, J.-X., & Li, H. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102480 · Cited by 5 · see citing works

Kinase inhibitors: 20 years of success and many new challenges and recent trends in their patents

Aboul‐Soud, M. A. M., Al‐Sheikh, Y. A., Ghneim, H. K., Supuran, C. T., & Carta, F. (2024) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2024.2355247 · Cited by 4 · see citing works

A Terphenyllin Derivative CHNQD-00824 from the Marine Compound Library Induced DNA Damage as a Potential Anticancer Agent

Cao, X.-Z., Zhang, B.-Q., Wang, C.-F., Yin, J.-N., Haider, W., Said, G., Wei, M., & Lu, L. (2023) · Marine Drugs · doi:10.3390/md21100512 · Cited by 4 · see citing works

Novel AMP-activated protein kinase activators and their potential for mitigating renal injury and fibrosis

Harley, G., & Mount, P. F. (2025) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2025.103741 · Cited by 3 · see citing works

Structure activity relationships leading to the identification of the indirect activator of AMPK, R419

Shaw, S. J., Goff, D. A., Carroll, D. C., Singh, R., Sweeny, D. J., Park, G., Jenkins, Y., Markovtsov, V. V., Sun, T., Issakani, S. D., et al. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116951 · Cited by 3 · 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

Modulating phosphorylation by proximity-inducing strategy: an update

Xia, Y., Zhai, D., You, Q., Wang, L., & Zhang, Q. (2026) · RSC Medicinal Chemistry · doi:10.1039/d6md00484a · Cited by 2 · see citing works

Insights into enterovirus a-71 antiviral development: from natural sources to synthetic nanoparticles

Feferbaum-Leite, S., Santos, I. A., Grosche, V. R., da Silva, G. C. D., & Jardim, A. C. G. (2023) · Archives of Microbiology · doi:10.1007/s00203-023-03660-3 · Cited by 2 · see citing works

The thienopyridine A-769662 and benzimidazole 991 inhibit human TASK-3 potassium channels in an AMPK-independent manner

Said, E. A., Lewis, R. W., Dallas, M. L., Peers, C., Ross, F. A., Unciti‐Broceta, A., Hardie, D. G., & Evans, A. M. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116562 · Cited by 2 · see citing works

AMPK activation prevents hepatocellular carcinoma development through inhibition of HNF4α activityPreprint

Sun, Z., Linares, B., Urdiales, C., Al-sarmi, F., Putluri, N., & Nostrand, J. L. V. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.16.652569 · Cited by 2 · see citing works

AMPK Signaling Regulates Epithelioid Hemangioendothelioma Cell Growth

Kanai, R., McMullan, S., Baniya, P., Dai, R. S., Norton, E., Lasher, K., Purello, C. T., Seavey, C. N., Rubin, B. P., & Lamar, J. M. (2025) · Cancers · doi:10.3390/cancers17172889 · Cited by 1 · see citing works

Design and Synthesis of New Benzimidazole–Biphenyl Scaffolds as Anti‐Inflammatory, Antioxidant Agents and Computational Screening

Gadeela, P. K., Jyothi, K., Konidena, L. N. S., Mallikanti, V., & Velidandi, A. (2025) · Chemistry & Biodiversity · doi:10.1002/cbdv.202502180 · Cited by 1 · see citing works

Exploring natural AMPK activators from bioactive compounds in fenugreek and oyster mushroom for management of type 2 diabetes

Mazumdar, S., Faruque, M. O., Islam, T., Amin, M. R., Rakib, M. A., & Alauddin, M. (2025) · Scientific Reports · doi:10.1038/s41598-025-28349-z · Cited by 1 · see citing works

RAB5A regulates cell proliferation and lipid metabolism by modulating mitochondrial ROS via AMPK signaling pathway in ovarian granulosa cells

Liu, S.-H., Yang, P., Zhu, B.-H., Li, H.-Y., Wang, S., Wang, Y., & Liu, X.-M. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104183 · Cited by 1 · see citing works

Activation of AMPK as a therapeutic strategy for FBXL4-related mitochondrial DNA depletion syndrome

Bishnu, A., Zapata‐Muñoz, J., Taylor, R. W., Sakamoto, K., & Ganley, I. G. (2026) · EMBO Molecular Medicine · doi:10.1038/s44321-026-00471-z · Cited by 1 · see citing works

Probing Hepatic Glucose Metabolism via 13C NMR Spectroscopy in Perfused Livers—Applications to Drug Development

Miller, C. O., & Cao, J. (2021) · Metabolites · doi:10.3390/metabo11110712 · Cited by 1 · see citing works

The AMPK Activator A-769662 Inhibits Human TASK-3 Potassium Channels in an AMPK-Independent MannerPreprint

Said, E. A., Lewis, R. W., Dallas, M. L., Peers, C., Ross, F. A., Hardie, D. G., & Evans, A. M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.24.493214

AMPK Activation by MK-8722 Measured with [18F]FDG-PET Imaging in Rodents and Non-Human Primates

Rubins, D. J., Meng, X., Wang, S., Haley, H., Posavec, D. J., Purcell, M. L., Riffel, K. A., Myers, R. W., Sebhat, I. K., Trotter, D. E. G., et al. (2025) · Molecular Imaging and Biology · doi:10.1007/s11307-025-02078-1

Constitutive AMPK activation prevents hepatocellular carcinoma development through inhibition of HNF4α activity

Sun, Z., Linarés, B., Urdiales, C., Al-sarmi, F., Sang, B., Putluri, N., & Nostrand, J. L. V. (2026) · Science Advances · doi:10.1126/sciadv.aea8017

In Silico Prediction of EZHIP Post-Translational Modification Sites and Small-Molecule High-Throughput Screening for Quantitative EZHIP Modulation

Moon, J., Hwang, J., & Chung, C. (2026) · Brain Tumor Research and Treatment · doi:10.14791/btrt.2025.0047

Small Molecule Insulin Sensitisers: New Leads and Targets for Next-Generation Insulin Sensitising Strategies

Lee, C. Y. (2026) · Medicinal Chemistry Research · doi:10.1007/s00044-026-03577-8

AMPK-mediated modulation of JAK2/STAT3 signaling in asthma: a promising target for controlling airway inflammation and remodeling

Althagafi, H. J., Al-Kuraishy, H. M., Badawy, H. K., Mustafa, A. M., & Batiha, G. E. (2026) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-026-05537-w

AMPK Therapy—A Little Goes A Long Way

CEBALLOS, H. M., Eryun, Z., & Huang, W. (2026) · Cells · doi:10.3390/cells15161503

AMPK Activator MK ‐8722 Improves Spatial Memory Deficit and Alters Metabolome in APP / PS1 AD Mouse Model

Nicol, N. I., Li, T., Su, Q., Suhocki, A., Dunlap, E., 周雪艳, Jester, H. M., Swift, N. A., Underwood, E. B., Lee, J., et al. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70563

The AMPK signaling pathway in cell metabolism and human diseases

Zhang, Z., Gu, Y., He, H., Qiao, S., Shao, Y., 龙先铭, Huang, J., Zhang, L., & Zhou, F. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02790-6

BindingDB Entry 50000276: Optimization of Metabolic and Renal Clearance in a Series of Indole Acid Direct Activators of 5'-Adenosine Monophosphate-Activated Protein Kinase (AMPK).

BindingDB (2019) · UC San Diego · doi:10.7270/q2028tzt

BindingDB Entry 50002377: Design, semisynthesis, α-glucosidase inhibitory, cytotoxic, and antibacterial activities of p-terphenyl derivatives.

BindingDB (2020) · UC San Diego · doi:10.7270/q29p3494

BindingDB Entry 50002351: Mapping the Efficiency and Physicochemical Trajectories of Successful Optimizations.

BindingDB (2020) · UC San Diego · doi:10.7270/q2dj5j62

BindingDB Entry 50018159: Identification of novel benzimidazole derivatives as highly potent AMPK activators with anti-diabetic profiles.

BindingDB (2024) · UC San Diego · doi:10.7270/q2cr5zkq

BindingDB Entry 50015971: Structure activity relationships leading to the identification of the indirect activator of AMPK, R419.

BindingDB (2023) · UC San Diego · doi:10.7270/q2hx1hm7

BindingDB Entry 50017260: Identification of novel indole derivatives as highly potent AMPK activators with anti-diabetic profiles.

BindingDB (2023) · UC San Diego · doi:10.7270/q2dj5kpr

BindingDB Entry 50020577: Optimization of Pharmacokinetic and In Vitro Safety Profile of a Series of Pyridine Diamide Indirect AMPK Activators.

BindingDB (2024) · UC San Diego · doi:10.7270/q2v12997

BindingDB Entry 50007641: The Race to Bash NASH: Emerging Targets and Drug Development in a Complex Liver Disease.

BindingDB (2021) · UC San Diego · doi:10.7270/q2dj5jxg

BindingDB Entry 50023428: Small Molecule Modulators of AMP-Activated Protein Kinase (AMPK) Activity and Their Potential in Cancer Therapy.

BindingDB (2026) · UC San Diego · doi:10.7270/q2ns10tk

Systemic pan-AMPK activator MK-8722 improves glucose homeostasis but induces cardiac hypertrophy

Myers, R. W., Guan, H.-P., Ehrhart, J., Petrov, A., Prahalada, S., Tozzo, E., Yang, X., Kurtz, M. M., Trujillo, M., Gonzalez Trotter, D., et al. (2017) · Science · doi:10.1126/science.aah5582 · Cited by 346 · see citing works

Targeting the AMP-Activated Protein Kinase for the Treatment of Type 2 Diabetes

Musi, N., & Goodyear, L. J. (2002) · Current Drug Targets - Immune Endocrine & Metabolic Disorders · doi:10.2174/1568005310202020119 · Cited by 68 · see citing works

Identification of Novel Indole Derivatives as Highly Potent AMPK Activators With Anti-Diabetic ProfilesPreprint

Tamura, Y., Morita, I., Hinata, Y., Kojima, E., Ozasa, H., Ikemoto, H., Asano, M., Wada, T., Hayasaki‐Kajiwara, Y., Iwasaki, T., et al. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4074255

AMP-Activated Protein Kinase and Type 2 Diabetes

Musi, N. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706776055724 · Cited by 74 · see citing works

Adenosine Monophosphate-Activated Protein Kinase (AMPK) as a New Target for Antidiabetic Drugs: A Review on Metabolic, Pharmacological and Chemical Considerations

Arie Gruzman, G. B. (2023) · The Review of Diabetic Studies