A redox-dependent mechanism for regulation of AMPK activation by thioredoxin1 during energy starvation

Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1

Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377 · see citing works

Oxidant signals and oxidative stress

Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393 · see citing works

Characterization of the AMP-activated Protein Kinase Kinase from Rat Liver and Identification of Threonine 172 as the Major Site at Which It Phosphorylates AMP-activated Protein Kinase

Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., & Hardie, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27879 · Cited by 1,264 · see citing works

Thioredoxin reductase

Mustacich, D. J., & Powis, G. (2000) · Biochemical Journal · doi:10.1042/bj3460001 · Cited by 828 · see citing works

AMP-activated protein kinase mediates ischemic glucose uptake and prevents postischemic cardiac dysfunction, apoptosis, and injury

Russell, R. R., Li, J., Coven, D. L., Pypaert, M., Zechner, C., Palmeri, M., Giordano, F. J., Mu, J., Birnbaum, M. J., & Young, L. H. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19297 · Cited by 738 · see citing works

Thioredoxin and Related Molecules–From Biology to Health and Disease

Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724 · see citing works

AMPK is a direct adenylate charge-regulated protein kinase

Oakhill, J. S., Steel, R., Chen, Z.-P., Scott, J. W., Ling, N., Tam, S., & Kemp, B. E. (2011) · Science · doi:10.1126/science.1200094 · Cited by 612 · see citing works

Aging-associated reductions in AMP-activated protein kinase activity and mitochondrial biogenesis

Reznick, R. M., Zong, H., Li, J., Morino, K., Moore, I. K., Yu, H. J., Liu, Z.-X., Dong, J., Mustard, K. J., Hawley, S. A., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.01.008 · Cited by 555 · see citing works

Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase

Zmijewski, J. W., Banerjee, S., Bae, H., Friggeri, A., Lazarowski, E. R., & Abraham, E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143685 · Cited by 441 · see citing works

Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli.

Kallis, G. B., & Holmgren, A. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70458-x · Cited by 366 · see citing works

A Redox-Dependent Pathway for Regulating Class II HDACs and Cardiac Hypertrophy

Ago, T., Liu, T., Zhai, P., Chen, W., Hong Li, A., Molkentin, J. D., Vatner, S. F., & Sadoshima, J. (2008) · Cell · doi:10.1016/j.cell.2008.04.041 · Cited by 362 · see citing works

Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system

Berndt, C., Lillig, C. H., & Holmgren, A. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01162.2006 · Cited by 350 · see citing works

Effect of Acute Exercise on AMPK Signaling in Skeletal Muscle of Subjects with Type 2 Diabetes

Sriwijitkamol, A., Coletta, D. K., Wajcberg, E., Balbontin, G. B., Reyna, S. M., Barrientes, J., Eagan, P. A., Jenkinson, C. P., Cersosimo, E., DeFronzo, R. A., et al. (2007) · Diabetes · doi:10.2337/db06-1119 · Cited by 304 · see citing works

Rheb is a Critical Regulator of Autophagy During Myocardial Ischemia: Pathophysiological Implications in Obesity and Metabolic Syndrome

Sciarretta, S., Zhai, P., Shao, D., Maejima, Y., Robbins, J., Volpe, M., Condorelli, G., & Sadoshima, J. (2012) · Circulation · doi:10.1161/circulationaha.111.078212 · Cited by 292 · see citing works

Thioredoxin reductase.

Mustacich, D. J., & Powis, G. (2000) · PubMed Central · Cited by 290 · see citing works

Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy

Yamamoto, M., Yang, G., Hong, C., Liu, J., Holle, E., Yu, X., Wagner, T. E., Vatner, S. F., & Sadoshima, J. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17700 · Cited by 274 · see citing works

Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy

Yamamoto, M., Yang, G., Hong, C., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200317700 · Cited by 239 · see citing works

In Vivo Characterization of a Thioredoxin h Target Protein Defines a New Peroxiredoxin Family

Verdoucq, L., Vignols, F., Jacquot, J., Chartier, Y., & Meyer, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19714 · Cited by 233 · see citing works

Resveratrol Prevents the Prohypertrophic Effects of Oxidative Stress on LKB1

Dolinsky, V. W., Chan, A. Y. M., Frayne, I. R., Light, P. E., Rosiers, C. D., & Dyck, J. R. B. (2009) · Circulation · doi:10.1161/circulationaha.108.787440 · Cited by 232 · see citing works

Role of AMP‐activated protein kinase in the metabolic syndrome and in heart disease

Hardie, D. G. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.018 · Cited by 214 · see citing works

Activation of NADPH Oxidase 4 in the Endoplasmic Reticulum Promotes Cardiomyocyte Autophagy and Survival During Energy Stress Through the Protein Kinase RNA-Activated-Like Endoplasmic Reticulum Kinase/Eukaryotic Initiation Factor 2α/Activating Transcription Factor 4 Pathway

Sciarretta, S., Zhai, P., Shao, D., Zablocki, D., Nagarajan, N., Terada, L. S., Volpe, M., & Sadoshima, J. (2013) · Circulation Research · doi:10.1161/circresaha.113.301787 · Cited by 195 · see citing works

Cardioprotective effects of thioredoxin in myocardial ischemia and the reperfusion role of S-nitrosation

Tao, L., Gao, E., Bryan, N. S., Qu, Y., Liu, H., Hu, A., Christopher, T. A., Lopez, B. L., Yodoi, J., Koch, W. J., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402941101 · Cited by 189 · see citing works

1-Chloro-2,4-dinitrobenzene Is an Irreversible Inhibitor of Human Thioredoxin Reductase

Arnér, E. S. J., Björnstedt, M., & Holmgren, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.8.3479 · Cited by 187 · see citing works

α-Adrenergic Receptor–Stimulated Hypertrophy in Adult Rat Ventricular Myocytes Is Mediated via Thioredoxin-1–Sensitive Oxidative Modification of Thiols on Ras

Kuster, G. M., Pimentel, D. R., Adachi, T. K., Ido, Y., Brenner, D. A., Cohen, R. A., Liao, R., Siwik, D. A., & Colucci, W. S. (2005) · Circulation · doi:10.1161/01.cir.0000157148.59308.f5 · Cited by 119 · see citing works

Elucidation of Thioredoxin Target Protein Networks in Mouse

Fu, C., Wu, C., Liu, T., Ago, T., Zhai, P., Sadoshima, J., & Hong Li, A. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800580-mcp200 · Cited by 80 · see citing works

Thioredoxin affinity chromatography: a useful method for further understanding the thioredoxin network

Hisabori, T., Hara, S., Fujii, T., Yamazaki, D., Hosoya‐Matsuda, N., & Motohashi, K. (2005) · Journal of Experimental Botany · doi:10.1093/jxb/eri170 · Cited by 77 · see citing works

Structure and Dimerization of the Kinase Domain from Yeast Snf1, a Member of the Snf1/AMPK Protein Family

Nayak, V., Zhao, K., Wyce, A., Schwartz, M. F., Lo, W., Berger, S. L., & Marmorstein, R. (2006) · Structure · doi:10.1016/j.str.2005.12.008 · Cited by 72 · see citing works

Regulation of H(2)O(2)-induced necrosis by PKC and AMP-activated kinase signaling in primary cultured hepatocytes.

Saberi, B., Shinohara, M., Ybanez, M., Hanawa, N., Gaarde, W., Kaplowitz, N., & Han, D. (2008) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.90654.2007 · Cited by 62 · see citing works

Impact of obesity as a mortality predictor in high-risk patients with myocardial infarction or chronic heart failure: a pooled analysis of five registries

Abdulla, J., Køber, L., Abildstrom, S. Z., Christensen, E. F., James, W. P. T., & Torp-Pedersen, C. T. (2008) · European Heart Journal · doi:10.1093/eurheartj/ehn010 · Cited by 57 · see citing works

Oxidative Stress–Induced Degradation of Thioredoxin-1 and Apoptosis Is Inhibited by Thioredoxin-1–Actin Interaction in Endothelial Cells

Zschauer, T.-C., Kunze, K., Jakob, S., Haendeler, J., & Altschmied, J. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.218982 · Cited by 31 · see citing works

Molecular Views of Redox Regulation: Three-Dimensional Structures of Redox Regulatory Proteins and Protein Complexes

Qin, J., Yang, Y., Vėlyvis, A., & Gronenborn, A. M. (2000) · Antioxidants and Redox Signaling · doi:10.1089/ars.2000.2.4-827 · Cited by 15 · see citing works

AMPK: Mechanisms of Cellular Energy Sensing and Restoration of Metabolic Balance

Garcia, D., & Shaw, R. J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.032 · Cited by 1,997 · see citing works

Mechanisms of physiological and pathological cardiac hypertrophy

Nakamura, M., & Sadoshima, J. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0007-y · Cited by 1,662 · see citing works

Regulation and function of AMPK in physiology and diseases

Jeon, S. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.81 · Cited by 1,121 · see citing works

ROS-dependent signal transduction

Reczek, C. R., & Chandel, N. S. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.09.010 · Cited by 850 · see citing works

ROS and redox signaling in myocardial ischemia-reperfusion injury and cardioprotection

Cadenas, S. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.01.024 · Cited by 819 · see citing works

The Two Faces of Reactive Oxygen Species in Cancer

Reczek, C. R., & Chandel, N. S. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041916-065808 · Cited by 602 · see citing works

Redox regulation of the immune response

Morris, G., Gevezova, M., Sarafian, V. S., & Maes, M. H. J. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00902-0 · Cited by 600 · see citing works

Hydrogen peroxide – production, fate and role in redox signaling of tumor cells

Lennicke, C., Rahn, J., Lichtenfels, R., Wessjohann, L. A., & Seliger, B. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0118-6 · Cited by 572 · see citing works

AMPK maintains cellular metabolic homeostasis through regulation of mitochondrial reactive oxygen species

Rabinovitch, R. C., Samborska, B., Faubert, B., Ma, E. H., Gravel, S.-P., Andrzejewski, S., Raissi, T. C., Pause, A., St.-Pierre, J., & Jones, R. G. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.026 · Cited by 543 · see citing works

Reactive Oxygen Species and Mitochondrial Dynamics: The Yin and Yang of Mitochondrial Dysfunction and Cancer Progression

Ježek, J., Cooper, K. F., & Strich, R. (2018) · Antioxidants · doi:10.3390/antiox7010013 · Cited by 515 · see citing works

Fundamentals of redox regulation in biology

Sies, H., Mailloux, R. J., & Jakob, U. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00730-2 · Cited by 546 · see citing works

Redox homeostasis: The Golden Mean of healthy living

Ursini, F., Maiorino, M., & Forman, H. J. (2016) · Redox Biology · doi:10.1016/j.redox.2016.01.010 · Cited by 418 · see citing works

Redox regulation: mechanisms, biology and therapeutic targets in diseases

Li, B., Ming, H., Qin, S., Nice, E. C., Dong, J., Du, Z., & Huang, C. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02095-6 · Cited by 364 · see citing works

Mitochondria-derived ROS activate AMP-activated protein kinase (AMPK) indirectly

Hinchy, E. C., Gruszczyk, A. V., Willows, R., Navaratnam, N., Hall, A. R., Bates, G., Bright, T. P., Krieg, T., Carling, D., & Murphy, M. P. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002579 · Cited by 302 · see citing works

AMPK: energy sensor and survival mechanism in the ischemic heart

Qi, D., & Young, L. H. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.05.010 · Cited by 285 · see citing works

Cardiomyopathy in obesity, insulin resistance and diabetes

Nakamura, M., & Sadoshima, J. (2019) · The Journal of Physiology · doi:10.1113/jp276747 · Cited by 287 · 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 plant energy sensor: evolutionary conservation and divergence of SnRK1 structure, regulation, and function

Broeckx, T., Hulsmans, S., & Rolland, F. (2016) · Journal of Experimental Botany · doi:10.1093/jxb/erw416 · Cited by 268 · see citing works

Molecular regulation of autophagy machinery by mTOR‐dependent and ‐independent pathways

Al‐Bari, M. A. A., & Xu, P. (2020) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14305 · Cited by 265 · see citing works

AMPK signaling and its targeting in cancer progression and treatment

Hsu, C.-C., Peng, D., Cai, Z., & Lin, H. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.04.006 · Cited by 257 · see citing works

Ferroptosis and its emerging roles in cardiovascular diseases

Li, N., Jiang, W., Wang, W., Xiong, R., Wu, X., & Geng, Q. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105466 · Cited by 254 · see citing works

Mechanisms of regulation of SNF1/AMPK/SnRK1 protein kinases

Crozet, P., Margalha, L., Confraria, A., Rodrigues, A., Martinho, C., Adamo, M., Elias, A., & Gonzalez, E. B. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00190 · Cited by 234 · see citing works

AMPK–mTOR Signaling and Cellular Adaptations in Hypoxia

Chun, Y., & Kim, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189765 · Cited by 209 · see citing works

Oxidative stress and impaired oligodendrocyte precursor cell differentiation in neurological disorders

Spaas, J., van Veggel, L., Schepers, M., Tiane, A., van Horssen, J., Wilson, D. M., Moya, P. R., Piccart, E., Hellings, N., Eijnde, B. O., et al. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03802-0 · Cited by 217 · see citing works

Redox Regulation of Inflammation: Old Elements, a New Story

Lei, Y., Wang, K., Deng, L., Chen, Y., Nice, E. C., & Huang, C. (2014) · Medicinal Research Reviews · doi:10.1002/med.21330 · Cited by 208 · see citing works

Reactive oxygen species and redox compartmentalization

Kaludercic, N., Deshwal, S., & Lisa, F. D. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00285 · Cited by 213 · see citing works

Critical role of AMPK in redox regulation under glucose starvation

Ren, Y., & Shen, H. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101154 · Cited by 199 · see citing works

AMP-activated protein kinase: An energy sensor and survival mechanism in the reinstatement of metabolic homeostasis

Sharma, A., Anand, S. K., Singh, N., Dwivedi, U. N., & Kakkar, P. (2023) · Experimental Cell Research · doi:10.1016/j.yexcr.2023.113614 · Cited by 197 · see citing works

Targeting AMPK signaling pathway by natural products for treatment of diabetes mellitus and its complications

Joshi, T., Singh, A. K., Haratipour, P., Sah, A. N., Pandey, A. K., Naseri, R., Juyal, V., & Farzaei, M. H. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28528 · Cited by 179 · see citing works

Exercise-Stimulated ROS Sensitive Signaling Pathways in Skeletal Muscle

Bouvière, J., Fortunato, R. S., Dupuy, C., Werneck‐de‐Castro, J. P., de Carvalho, D. P., & Louzada, R. A. N. (2021) · Antioxidants · doi:10.3390/antiox10040537 · Cited by 175 · see citing works

Regulation of AMP-activated protein kinase by natural and synthetic activators

Hardie, D. G. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.06.002 · Cited by 176 · see citing works

AMPK/ULK1-mediated phosphorylation of Parkin ACT domain mediates an early step in mitophagy

Hung, C., Lombardo, P. S., Malik, N., Brun, S. N., Hellberg, K., Nostrand, J. L. V., Garcia, D., Baumgart, J. T., Diffenderfer, K. E., Asara, J. M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg4544 · Cited by 169 · see citing works

Thioredoxin and redox signaling: Roles of the thioredoxin system in control of cell fate

Matsuzawa, A. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.09.011 · Cited by 166 · see citing works

Targeting Metabolic–Redox Circuits for Cancer Therapy

Wang, K., Jiang, J., Lei, Y., Zhou, S., Wei, Y., & Huang, C. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.01.001 · Cited by 162 · see citing works

Redox homeostasis, oxidative stress and mitophagy

Garza-Lombó, C., Pappa, A., Panayiotidis, M. I., & Franco, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.01.002 · Cited by 161 · 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

AMPK and NRF2: Interactive players in the same team for cellular homeostasis?

Petsouki, E., Cabrera, S. N. S., & Heiß, E. H. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.07.014 · Cited by 157 · see citing works

Global redox proteome and phosphoproteome analysis reveals redox switch in Akt

Su, Z., Burchfield, J. G., Yang, P., Humphrey, S. J., Yang, G., Francis, D., Yasmin, S., Shin, S., Norris, D. M., Kearney, A. L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13114-4 · Cited by 145 · see citing works

Oxidative stress activates AMPK in cultured cells primarily by increasing cellular AMP and/or ADP

Auciello, F. R., Ross, F. A., Ikematsu, N., & Hardie, D. G. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.07.025 · Cited by 136 · see citing works

Exercise and mitochondrial dynamics: keeping in shape with ROS and AMPK

Trewin, A., Berry, B., & Wojtovich, A. (2018) · Antioxidants · doi:10.3390/antiox7010007 · Cited by 129 · see citing works

The thioredoxin-1 system is essential for fueling DNA synthesis during T-cell metabolic reprogramming and proliferation

Muri, J., Heer, S., Matsushita, M., Pohlmeier, L. M., Tortola, L., Fuhrer, T., Conrad, M., Zamboni, N., Kisielow, J., & Köpf, M. (2018) · Nature Communications · doi:10.1038/s41467-018-04274-w · Cited by 130 · see citing works

Redox basis of exercise physiology

Margaritelis, N. V., Paschalis, V., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101499 · Cited by 129 · see citing works

The Double-Faced Role of Nitric Oxide and Reactive Oxygen Species in Solid Tumors

Mijatović, S., Savic-Radojevic, A. R., Pljesa-Ercegovac, M. S., Simic, T. P., Nicoletti, F., & Maksimović‐Ivanić, D. (2020) · Antioxidants · doi:10.3390/antiox9050374 · Cited by 125 · see citing works

New Insights into the Role of Mitochondrial Dynamics and Autophagy during Oxidative Stress and Aging in the Heart

Ikeda, Y., Sciarretta, S., Nagarajan, N., Rubattu, S., Volpe, M., Frati, G., & Sadoshima, J. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/210934 · Cited by 124 · see citing works

The H+-ATP synthase: A gate to ROS-mediated cell death or cell survival

Martínez‐Reyes, I., & Cuezva, J. M. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.03.010 · Cited by 123 · see citing works

AMPK in cardiac fibrosis and repair: Actions beyond metabolic regulation

Daskalopoulos, E. P., Dufeys, C., Bertrand, L., Beauloye, C., & Horman, S. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.01.001 · Cited by 119 · see citing works

Ketone Bodies in the Brain Beyond Fuel Metabolism: From Excitability to Gene Expression and Cell Signaling

García-Rodríguez, D., & Giménez-Cassina, A. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.732120 · Cited by 123 · see citing works

Differential Cysteine Labeling and Global Label-Free Proteomics Reveals an Altered Metabolic State in Skeletal Muscle Aging

McDonagh, B., Sakellariou, G. K., Smith, N. T., Brownridge, P., & Jackson, M. J. (2014) · Journal of Proteome Research · doi:10.1021/pr5006394 · Cited by 110 · see citing works

Selenium deficiency-induced redox imbalance leads to metabolic reprogramming and inflammation in the liver

Tang, C., Li, S., Zhang, K., Li, J., Han, Y., Zhan, T., Zhao, Q., Guo, X., & Zhang, J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101519 · Cited by 112 · see citing works

Evolution of TOR–SnRK dynamics in green plants and its integration with phytohormone signaling networks

Muhammed Jamsheer, K., Jindal, S., & Laxmi, A. (2019) · Journal of Experimental Botany · doi:10.1093/jxb/erz107 · Cited by 107 · see citing works

Noise-induced loss of sensory hair cells is mediated by ROS/AMPKα pathway

Wu, F., Xiong, H., & Sha, S. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101406 · Cited by 103 · see citing works

Nutrient-sensing mTORC1 and AMPK pathways in chronic kidney diseases

Huynh, C. Q., Ryu, J., Lee, J., Inoki, A., & Inoki, K. (2022) · Nature Reviews Nephrology · doi:10.1038/s41581-022-00648-y · Cited by 104 · see citing works

Diet rich in high glucoraphanin broccoli reduces plasma LDL cholesterol: Evidence from randomised controlled trials

Armah, C. N., Derdemezis, C. S., Τράκα, Μ., Dainty, J. R., Doleman, J. F., Saha, S., Leung, W., Potter, J. F., Lovegrove, J. A., & Mithen, R. F. (2015) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400863 · Cited by 103 · see citing works

Aurora A regulation by reversible cysteine oxidation reveals evolutionarily conserved redox control of Ser/Thr protein kinase activity

Byrne, D. P., Shrestha, S., Galler, M., Cao, M., Daly, L. A., Campbell, A. E., Eyers, C. E., Veal, E. A., Kannan, N., & Eyers, P. A. (2020) · Science Signaling · doi:10.1126/scisignal.aax2713 · Cited by 101 · see citing works

The A to Z of modulated cell patterning by mammalian thioredoxin reductases

Dagnell, M., Schmidt, E. E., & Arnér, E. S. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.12.029 · Cited by 100 · see citing works

Till Death Do Us Part: The Marriage of Autophagy and Apoptosis

Cooper, K. F. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/4701275 · Cited by 98 · see citing works

The protein kinase activity of fructokinase A specifies the antioxidant responses of tumor cells by phosphorylating p62

Xu, D., Li, X., Shao, F., Lv, G., Lv, H., Lee, J.-H., Qian, X., Zheng, W., Xia, Y., Du, L., et al. (2019) · Science Advances · doi:10.1126/sciadv.aav4570 · Cited by 99 · see citing works

Perturbed Redox Signaling Exacerbates a Mitochondrial Myopathy

Doğan, Ş. A., Cerutti, R., Benincá, C., Brea‐Calvo, G., Jacobs, H. T., Zeviani, M., Szibor, M., & Viscomi, C. F. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.012 · Cited by 98 · see citing works

Reactive oxygen species are required for driving efficient and sustained aerobic glycolysis during CD4+ T cell activation

Previte, D. M., O’Connor, E. C., Novak, E. A., Martins, C. P., Mollen, K. P., & Piganelli, J. D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0175549 · Cited by 96 · see citing works

Autophagy and cardiac aging

Miyamoto, S. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0286-9 · Cited by 96 · see citing works

Reciprocal Control of the Circadian Clock and Cellular Redox State - a Critical Appraisal

Putker, M., & O'Neill, J. S. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2323 · Cited by 92 · see citing works

Punicalagin, an active component in pomegranate, ameliorates cardiac mitochondrial impairment in obese rats via AMPK activation

Cao, K., Xu, J., Pu, W., Dong, Z., Sun, L., Zang, W., Gao, F., Zhang, Y., Feng, Z., & Liu, J. (2015) · Scientific Reports · doi:10.1038/srep14014 · Cited by 90 · see citing works

Cancer-induced cardiac cachexia: Pathogenesis and impact of physical activity

Belloum, Y., Rannou‐Bekono, F., & Favier, F. B. (2017) · Oncology Reports · doi:10.3892/or.2017.5542 · Cited by 90 · see citing works

The pleiotropic AMPK–CncC signaling pathway regulates the trade-off between detoxification and reproduction

Jiang, H., Meng, X., Zhang, N., Ge, H., Wei, J., Qian, K., Yang, Z., Park, Y., Palli, S. R., & Wang, J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214038120 · Cited by 89 · see citing works

Circadian redox oscillations and metabolism

Milev, N. B., & Reddy, A. B. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.05.012 · Cited by 84 · see citing works

PRKAA/AMPK restricts HBV replication through promotion of autophagic degradation

Xie, N., Yuan, K., Zhou, L., Wang, K., Chen, H., Lei, Y., Lan, J., Pu, Q., Gao, W. Q., Zhang, L., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1191857 · Cited by 86 · see citing works

Targeting Oxidative Stress with Polyphenols to Fight Liver Diseases

Machado, I. F., Miranda, R. G., Dorta, D. J., Rolo, A. P., & Palmeira, C. M. (2023) · Antioxidants · doi:10.3390/antiox12061212 · Cited by 85 · see citing works

Glutamine suppresses senescence and promotes autophagy through glycolysis inhibition-mediated AMPKα lactylation in intervertebral disc degeneration

Zhang, Y., Huang, Z., Han, W., Wu, J., Li, S., Qin, T., Zhang, C., Shi, M., Han, S., Gao, B., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06000-3 · Cited by 80 · see citing works

Redox Signaling, Neuroinflammation, and Neurodegeneration

Aguilera, G., Colín-González, A. L., Rangel‐López, E., Chavarría, A., & Santamarı́a, A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7099 · Cited by 79 · see citing works

AMPK–a key factor in crosstalk between tumor cell energy metabolism and immune microenvironment?

Wang, N., Wang, B., Maswikiti, E. P., Yu, Y., Song, K., Ma, C., Han, X., Ma, H., Deng, X., Yu, R., et al. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02011-5 · Cited by 78 · see citing works

Aldehyde dehydrogenase‐2 (ALDH2) opposes hepatocellular carcinoma progression by regulating AMP‐activated protein kinase signaling in mice

Hou, G., Chen, L., Liu, G., Li, L., Yang, Y., Yan, H., Zhang, H., Tang, J. P., Yang, Y., Lin, X., et al. (2016) · Hepatology · doi:10.1002/hep.29006 · Cited by 77 · see citing works

Linking ROS Levels to Autophagy: The Key Role of AMPK

Agostini, F., Bisaglia, M., & Plotegher, N. (2023) · Antioxidants · doi:10.3390/antiox12071406 · Cited by 76 · see citing works

Nuclear Factor (Erythroid-Derived 2)-Like 2 and Thioredoxin-1 in Atherosclerosis and Ischemia/Reperfusion Injury in the Heart

Jakobs, P., Serbulea, V., Leitinger, N., Eckers, A., & Haendeler, J. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6795 · Cited by 74 · see citing works

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 · see citing works

Modulation of signaling mechanisms in the heart by thioredoxin 1

Nagarajan, N., Oka, S., & Sadoshima, J. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.020 · Cited by 69 · see citing works

AMP-activated protein kinase sparks the fire of cardioprotection against myocardial ischemia and cardiac ageing

Gu, C., Li, T. X., Jiang, S., Yang, Z. P., Lv, J., Yi, W., Yang, Y., & Fang, M. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.08.002 · Cited by 66 · see citing works

Melatonin protects rabbit spermatozoa from cryo-damage via decreasing oxidative stress

Zhu, Z., Li, R., Lv, Y., & Zeng, W. (2019) · Cryobiology · doi:10.1016/j.cryobiol.2019.04.009 · Cited by 66 · see citing works

Down-regulation of oxidative phosphorylation in the liver by expression of the ATPase inhibitory factor 1 induces a tumor-promoter metabolic state

Santacatterina, F., Sánchez-Cenizo, L., Formentini, L., Mobasher, M. A., Casas, E., Rueda, C. B., Martínez‐Reyes, I., de Arenas, C. N., García‐Bermúdez, J., Zapata, J. M., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6357 · Cited by 64 · see citing works

Mitochondrial dynamics in exercise physiology

Tanaka, T., Nishimura, A., Nishiyama, K., Goto, T., Numaga‐Tomita, T., & Nishida, M. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02258-3 · Cited by 66 · see citing works

Safety and anti-hyperglycemic efficacy of various tea types in mice

Han, M., Zhao, G., Wang, Y., Wang, D., Sun, F., Ning, J., Wan, X., & Zhang, J. (2016) · Scientific Reports · doi:10.1038/srep31703 · Cited by 62 · see citing works

Nampt Potentiates Antioxidant Defense in Diabetic Cardiomyopathy

Oka, S., Byun, J., Huang, C.-Y., Imai, N., Ralda, G., Zhai, P., Xu, X., Kashyap, S., Warren, J. S., Maschek, J. A., et al. (2021) · Circulation Research · doi:10.1161/circresaha.120.317943 · Cited by 59 · see citing works

Reactive oxygen species control protein degradation at the mitochondrial import gate

McMinimy, R. A., Manford, A. G., Gee, C. L., Chandrasekhar, S., Mousa, G. A., Chuang, J., Phu, L., Shih, K. Y., Rose, C. M., Kuriyan, J., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.11.004 · Cited by 59 · see citing works

Reciprocal regulation of carbon monoxide metabolism and the circadian clock

Klemz, R., Reischl, S., Wallach, T. E., Witte, N., Jürchott, K., Klemz, S., Lang, V., Lorenzen, S., Knauer, M., Heidenreich, S., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3331 · Cited by 59 · see citing works

Glucose Metabolism and AMPK Signaling Regulate Dopaminergic Cell Death Induced by Gene (α-Synuclein)-Environment (Paraquat) Interactions

Anandhan, A., Lei, S., Levytskyy, R. M., Pappa, A., Panayiotidis, M. I., Cerny, R. L., Khalimonchuk, O., Powers, R., & Franco, R. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9906-2 · Cited by 58 · see citing works

Mitochondrial involvement in sarcopenia

Affourtit, C., & Carré, J. E. (2024) · Acta Physiologica · doi:10.1111/apha.14107 · Cited by 58 · see citing works

Development of a microfluidic wearable electrochemical sensor for the non-invasive monitoring of oxidative stress biomarkers in human sweat

Ying, Z., Qiao, L., Liu, B., Gao, L., & Zhang, P. (2024) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2024.116502 · Cited by 55 · see citing works

Activation of cardiac AMPK-FGF21 feed-forward loop in acute myocardial infarction: Role of adrenergic overdrive and lipolysis byproducts

Sunaga, H., Koitabashi, N., Iso, T., Matsui, H., Obokata, M., Kawakami, R., Murakami, M., Yokoyama, T., & Kurabayashi, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-48356-1 · Cited by 55 · see citing works

Cross-talk between redox signalling and protein aggregation

van Dam, L., & Dansen, T. B. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190054 · Cited by 53 · see citing works

Redox Signaling and Sarcopenia: Searching for the Primary Suspect

Foreman, N. A., Hesse, A. S., & Ji, L. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169045 · Cited by 52 · see citing works

Thioredoxin-1 maintains mechanistic target of rapamycin (mTOR) function during oxidative stress in cardiomyocytes

Oka, S., Hirata, T., Suzuki, W., Naito, D., Chen, Y., Chin, A., Yaginuma, H., Saito, T., Nagarajan, N., Zhai, P., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.807735 · Cited by 51 · see citing works

Thioredoxin-1 improves the immunometabolic phenotype of antitumor T cells

Chakraborty, P., Chatterjee, S., Kesarwani, P., Thyagarajan, K., Iamsawat, S., Dalheim, A. V., Nguyen, H. D., Selvam, S. P., Nasarre, P., Scurti, G. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006753 · Cited by 51 · see citing works

Redox control of non-shivering thermogenesis

Lettieri‐Barbato, D. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.04.002 · Cited by 50 · see citing works

Promising Nutritional Fruits Against Cardiovascular Diseases: An Overview of Experimental Evidence and Understanding Their Mechanisms of Action

Zuraini, N. Z. A., Sekar, M., Wu, Y. S., Gan, S. H., Bonam, S. R., Rani, N. N. I. M., Begum, M. Y., Lum, P. T., Subramaniyan, V., Fuloria, N. K., et al. (2021) · Vascular Health and Risk Management · doi:10.2147/vhrm.s328096 · Cited by 50 · see citing works

Redox state‐dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals

Wurzinger, B., Mair, A., Fischer-Schrader, K., Nukarinen, E., Roustan, V., Weckwerth, W., & Teige, M. (2017) · FEBS Letters · doi:10.1002/1873-3468.12852 · Cited by 50 · see citing works

Post-Translational Modifications of the Energy Guardian AMP-Activated Protein Kinase

Ovens, A. J., Scott, J. W., Langendorf, C. G., Kemp, B. E., Oakhill, J. S., & Smiles, W. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031229 · Cited by 46 · see citing works

Redox signaling and skeletal muscle adaptation during aerobic exercise

Zhou, Y., Zhang, X., Baker, J. S., Davison, G. W., & Yan, X. (2024) · iScience · doi:10.1016/j.isci.2024.109643 · Cited by 52 · see citing works

Dynamic regulation of epigenetic demethylation by oxygen availability and cellular redox

Lamadema, N., Burr, S., & Brewer, A. C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.12.009 · Cited by 48 · see citing works

Sensing and responding to energetic stress: Evolution of the AMPK network

Craig, P. M., Moyes, C. D., & LeMoine, C. M. R. (2018) · Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2017.11.001 · Cited by 46 · see citing works

AMPK at the interface of nutrient sensing, metabolic flux and energy homeostasis

Smith, T. K. T., Townsend, L. K., Smiles, W. J., Oakhill, J. S., Fullerton, M. D., & Steinberg, G. R. (2026) · Nature Metabolism · doi:10.1038/s42255-025-01442-3 · Cited by 51 · see citing works

Boosting autophagy in the diabetic heart: a translational perspective.

Sciarretta, S., Boppana, V. S., Umapathi, M., Frati, G., & Sadoshima, J. (2015) · PubMed Central · doi:10.3978/j.issn.2223-3652.2015.07.02 · Cited by 45 · see citing works

Abstract 17681: A Redox Dependent Mechanism for Regulation of AMPK Activation by Thioredoxin1 during Energy Starvation

Shao, D., Oka, S., Liu, T., Zhai, P., Ago, T., Sciarretta, S., Hong Li, A., & Sadoshima, J. (2013) · Circulation · doi:10.1161/circ.128.suppl_22.a541

Activation of the AMPK-FOXO3 Pathway Reduces Fatty Acid–Induced Increase in Intracellular Reactive Oxygen Species by Upregulating Thioredoxin

Li, X., Song, J., Zhang, L., LeMaire, S. A., Hou, X., Zhang, C., Coselli, J. S., Chen, L., Wang, X. L., Zhang, Y., et al. (2009) · Diabetes · doi:10.2337/db08-1512 · Cited by 237 · see citing works

Activation of the AMPK-FOXO3 Pathway Reduces Fatty Acid–Induced Increase in Intracellular Reactive Oxygen Species by

Thioredoxin, U., Li, X.-N., Song, J., Zhang, L., Lemaire, S. A., Hou, X., Zhang, C., Coselli, J. S., Chen, L., Wang, X. L., et al. (2016)

AMPK: A cellular metabolic and redox sensor. A minireview

Shirwany, N. A. (2014) · Frontiers in bioscience · doi:10.2741/4218 · Cited by 142 · see citing works

AMPK in cardiovascular health and disease

Shirwany, N. A., & Zou, M. (2010) · Acta Pharmacologica Sinica · doi:10.1038/aps.2010.139 · Cited by 121 · see citing works