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

Reduction in the incidence of type 2 diabetes with lifestyle intervention or metformin

(2002) · New England Journal of Medicine · doi:10.1056/nejmoa012512 · Cited by 19,011

Free Radicals in the Physiological Control of Cell Function

Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855

Mechanisms Underlying Acute Protection From Cardiac Ischemia-Reperfusion Injury

Murphy, E., & Steenbergen, C. (2008) · Physiological Reviews · doi:10.1152/physrev.00024.2007 · Cited by 1,504

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

AMP-Activated Protein Kinase in Metabolic Control and Insulin Signaling

Towler, M. C., & Hardie, D. G. (2007) · Circulation Research · doi:10.1161/01.res.0000256090.42690.05 · Cited by 1,262

Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress

Schulz, T. J., Zarse, K., Voigt, A., Urban, N., Birringer, M., & Ristow, M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.011 · Cited by 1,209

AMP-activated protein kinase signaling in metabolic regulation

Long, Y. C. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29044 · Cited by 1,125

Adiponectin protects against myocardial ischemia-reperfusion injury through AMPK- and COX-2–dependent mechanisms

Shibata, R., Sato, K., Pimentel, D. R., Takemura, Y., Kihara, S., Ohashi, K., Funahashi, T., Ouchi, N., & Walsh, K. (2005) · Nature Medicine · doi:10.1038/nm1295 · Cited by 982

Management of cellular energy by the AMP‐activated protein kinase system

Hardie, D. G., Scott, J. W., Pan, D. A., & Hudson, E. R. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00560-x · Cited by 868

Mitochondrial-targeted ubiquinone alleviates concanavalin A-induced hepatitis via immune modulation

Desta, Y. T., Wu, M., Bai, L., Wu, X., Xiong, M., & Weng, X. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106518 · Cited by 16

Suppression of the LKB1-AMPK-SLC7A11-GSH signaling pathway sensitizes NSCLC to albumin-bound paclitaxel via oxidative stress

Rong, D., Gao, L., Chen, Y., Gao, X.-Z., Tang, M., Tang, H., Gao, Y., Lu, G. X., Ling, Z., & Shen, H. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103567 · Cited by 13

Oxidative stress and oxidative damage-induced cell death

Madkour, L. H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-822481-6.00008-6 · Cited by 15

Calycosin Alleviates Injury in Airway Epithelial Cells Caused by PM 2.5 Exposure via Activation of AMPK Signalling

Wang, C., Luo, J., Bai, X., Hua, S., Jie, J., Liu, H., Gao, J., & Song, L. (2021) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2021/8885716 · Cited by 13

Negative regulation of pro-apoptotic AMPK/JNK pathway by itaconate in mice with fulminant liver injury

Fan, K., Chen, K., Zan, X., Zhi, Y., Zhang, X., Zhang, X., Qiu, J., Liu, G., Li, L., Tang, L. P., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06001-w · Cited by 13

Protein S-glutathionylation and the regulation of cellular functions

Mailloux, R. J., Gill, R., & Young, A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00013-4 · Cited by 15

The Interplay between Autophagy and Redox Signaling in Cardiovascular Diseases

Boťanská, B., Dovinová, I., & Barančı́k, M. (2022) · Cells · doi:10.3390/cells11071203 · Cited by 13

AMPK, a hub for the microenvironmental regulation of bone homeostasis and diseases

Liu, J., Liu, J.-X., Li, R., Zhang, Z., Zhang, X., Xing, S., Sui, B., Jin, F., Ma, B., & Zheng, C. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.31393 · Cited by 14

Selenocompounds and Sepsis: Redox Bypass Hypothesis for Early Diagnosis and Treatment: Part A—Early Acute Phase of Sepsis: An Extraordinary Redox Situation (Leukocyte/Endothelium Interaction Leading to Endothelial Damage)

Forceville, X., Antwerpen, P. V., & Preiser, J. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8063 · Cited by 13

Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling

Saks, V. A., Schlattner, U., Tokarska-Schlattner, M., Wallimann, T., Bagur, R., Zorman, S., Pelosse, M., Santos, P. D. D., Boucher, F. R., Käämbre, T., et al. (2013) · Springer series in biophysics · doi:10.1007/978-3-642-38505-6_11 · Cited by 13

Mimicking caloric restriction for anti-aging effects: The pro-oxidant role of alpha-ketoglutarate

Bayliak, M. M., Gospodaryov, D. V., & Lushchak, V. I. (2022) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2022.02.012 · Cited by 11

Damage sensing mediated by serine proteases Hayan and Persephone for Toll pathway activation in apoptosis-deficient flies

Nakano, S., Kashio, S., Nishimura, K., Takeishi, A., Kosakamoto, H., Obata, F., Kuranaga, E., Chihara, T., Yamauchi, Y., Isobe, T., et al. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010761 · Cited by 10

A Reassessment of Sarcopenia from a Redox Perspective as a Basis for Preventive and Therapeutic Interventions

Arcaro, A., Lepore, A., Cetrangolo, G. P., Paventi, G., Ames, P. R. J., & Gentile, F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167787 · Cited by 14

MnTE-2-PyP Suppresses Prostate Cancer Cell Growth via H2O2 Production

Zhu, Y., Kosmacek, E. A., Chatterjee, A., & Oberley‐Deegan, R. E. (2020) · Antioxidants · doi:10.3390/antiox9060490 · Cited by 10

The Role Played by Autophagy in FcεRI-Dependent Activation of Mast Cells

Pavlyuchenkova, A. N., Smirnov, M. S., Chernyak, B. V., & Chelombitko, M. A. (2024) · Cells · doi:10.3390/cells13080690 · Cited by 10

Stressed Out Insects II. Physiology, Behavior, and Neuroendocrine Circuits Mediating Stress Responses

Johnson, E. C. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803592-4.00038-9 · Cited by 11

Targeting autophagy process in center nervous trauma

Wei, S., Leng, B., & Yan, G. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1128087 · Cited by 11

Overexpression of iASPP is required for autophagy in response to oxidative stress in choriocarcinoma

Chan, K.-K., Wong, E. S. Y., Wong, I. T.-L., Cheung, C. L.-Y., Wong, O. G., Ngan, H., & Cheung, A. (2019) · BMC Cancer · doi:10.1186/s12885-019-6206-z · Cited by 10

Transcriptome profiling of farmed rainbow trout (Oncorhynchus mykiss) liver from different sources of dietary zinc

Nazari, S., Pourkazemi, M., Paknejad, H., Kazemi, E., Ghaderi‐Zefrehei, M., & Eslamloo, K. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.737017 · Cited by 10

Redox regulation and dynamic control of brain-selective kinases BRSK1/2 in the AMPK family through cysteine-based mechanisms

Bendzunas, G. N., Byrne, D. P., Shrestha, S., Daly, L. A., Oswald, S. O., Katiyar, S., Venkat, A., Yeung, W., Eyers, C. E., Eyers, P. A., et al. (2025) · eLife · doi:10.7554/elife.92536.4 · Cited by 10

Hyperactive HRAS dysregulates energetic metabolism in fibroblasts from patients with Costello syndrome via enhanced production of reactive oxidizing species

Carpentieri, G., Leoni, C., Pietraforte, D., Cecchetti, S., Iorio, E., Belardo, A., Pietrucci, D., Nottia, M. D., Pajalunga, D., Megiorni, F., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab270 · Cited by 9

Inflammatory Role of ROS-Sensitive AMP-Activated Protein Kinase in the Hypersensitivity of Lung Vagal C Fibers Induced by Intermittent Hypoxia in Rats

Yang, C.-H., Shen, Y.-J., Lai, C. J., & Kou, Y. R. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00263 · Cited by 9

Dysfunctional BCAA degradation triggers neuronal damage through disrupted AMPK-mitochondrial axis due to enhanced PP2Ac interaction

Wu, S.-C., Chen, Y.-J., Su, S.-H., Fang, P.-H., Liu, R.-W., Tsai, H.-Y., Chang, Y.-J., Li, H.-H., Li, J., & Chen, C. (2025) · Communications Biology · doi:10.1038/s42003-025-07457-6 · Cited by 9

Renoprotective mechanisms of exercise training against acute and chronic renal diseases – A perspective based on experimental studies

Malheiro, L. F. L., Fernandes, M. M., Oliveira, C. A., Barcelos, I. D. S., Fernandes, A. J. V., Silva, B. S., Ávila, J. S., Soares, T. D. J., & Amaral, L. S. D. B. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122628 · Cited by 8

Xanthene Derivatives Increase Glucose Utilization through Activation of LKB1-Dependent AMP-Activated Protein Kinase

Kwon, Y., Song, P., Yoon, J. H., Ghim, J., Kim, D., Kang, B., Lee, T. G., Kim, J.-A., Choi, J., Youn, I. K., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108771 · Cited by 9

Elimination of cancer stem cells and reactivation of latent HIV-1 via AMPK activation: Common mechanism of action linking inhibition of tumorigenesis and the potential eradication of HIV-1

Finley, J. (2017) · Medical Hypotheses · doi:10.1016/j.mehy.2017.05.032 · Cited by 9

The Roles and Mechanisms of ROS, Oxidative Stress, and Oxidative Damage

Madkour, L. H. (2020) · Nanomedicine and nanotoxicology · doi:10.1007/978-3-030-37297-2_4 · Cited by 8

The HO-1/CO System and Mitochondrial Quality Control in Skeletal Muscle

Gasier, H. G., Suliman, H. B., & Piantadosi, C. A. (2021) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000277 · Cited by 8

Neutrophil extracellular trap formation and gene programs distinguish TST/IGRA sensitization outcomes among Mycobacterium tuberculosis exposed persons living with HIV

Kroon, E. E., Correa-Macedo, W., Evans, R., Seeger, A., Engelbrecht, L., Kriel, J., Loos, B., Okugbeni, N., Orlova, M., Cassart, P., et al. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010888 · Cited by 8

Effect of hypobaric hypoxia on the fiber type transition of skeletal muscle: a synergistic therapy of exercise preconditioning with a nanocurcumin formulation

Kushwaha, A. D., Varshney, R. K., & Saraswat, D. (2023) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-023-00965-1 · Cited by 7

Redox-dependent AMPK inactivation disrupts metabolic adaptation to glucose starvation in xCT-overexpressing cancer cells

Lee, Y., Itahana, Y., Ong, C. C., & Itahana, K. (2022) · Journal of Cell Science · doi:10.1242/jcs.259090 · Cited by 10

Resistance to Obesity in SOD1 Deficient Mice with a High-Fat/High-Sucrose Diet

Sato, A., Shiraishi, Y., Kimura, T., Osaki, A., Kagami, K., Ido, Y., & Adachi, T. K. (2022) · Antioxidants · doi:10.3390/antiox11071403 · Cited by 7

Energy stress-induced PKCζ S-glutathionylation is essential for LKB1 cytoplasmic translocation and AMPK activation

Fei, J., Yu, S., Xu, M., Liu, Y., Wang, G., Li, X., Yu, X., Zhang, Y., Zhang, W., Wang, Y., et al. (2025) · Life Metabolism · doi:10.1093/lifemeta/loaf027 · Cited by 6

Sensing local energetics to acutely regulate mitophagy in skeletal muscle

Nichenko, A. S., Specht, K. S., Craige, S. M., & Drake, J. C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.987317 · Cited by 7

AMPK-mediated glutaminolysis maintains coelomocytes redox homeostasis in Vibrio splendidus-challenged Apostichopus japonicus

Zhou, F., Sun, L., Shao, Y., Zhang, X., & Li, C. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.02.012 · Cited by 6

Automating Complex, Multistep Processes on a Single Robotic Platform to Generate Reproducible Phosphoproteomic Data

Mullis, B. T., Hwang, S., Lee, L. A., Iliuk, A. B., Woolsey, R. J., Quilici, D. R., & Wang, Q. (2019) · SLAS DISCOVERY · doi:10.1177/2472555219878152 · Cited by 6

Defining the Protein Phosphatase 2A (PP2A) Subcomplexes That Regulate FoxO Transcription Factor Localization

Luperchio, A. M., & Salamango, D. J. (2025) · Cells · doi:10.3390/cells14050342 · Cited by 5

AMPK-mediated regulation of cardiac energy metabolism: Implications for thermotolerance in Argopecten irradians irradians

Chang, J., Zhang, J., Chu, L., Liu, A., Hou, X., Zhu, X., Huang, X., Xing, Q., Hu, J., & Bao, Z. (2024) · Gene · doi:10.1016/j.gene.2024.148922 · Cited by 7

A Spatiotemporally Controlled and Mitochondria-Targeted Prodrug of Hydrogen Sulfide Enables Mild Mitochondrial Uncoupling for the Prevention of Lipid Deposition

Zhang, X., Ye, M., Ge, Y., Xiao, C., Cui, K., You, Q., Jiang, Z., & Guo, X. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01599 · Cited by 5

Ouabain promotes claudin-1, -2, and -4 autophagic degradation through oxidative stress and AMPK activation in MDCK cells

Campos-Blázquez, J. P., Flores-Maldonado, C., Gallardo, J. M., Bonilla‐Delgado, J., Pedraza-Ramírez, A. A., López-Méndez, O., Cortés-Malagón, E. M., & Contreras, R. G. (2023) · Autophagy Reports · doi:10.1080/27694127.2023.2256146 · Cited by 5

Microglial Autophagic Dysregulation in Traumatic Brain Injury: Molecular Insights and Therapeutic Avenues

Bano, N., Khan, S., Ahamad, S., Dar, N. J., Alanazi, H. H., Nazir, A., & Bhat, S. A. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00617 · Cited by 6

The effect of adenosine monophosphate-activated protein kinase on lipolysis in adipose tissue: an historical and comprehensive review

Boone-Villa, D., Ventura-Sobrevilla, J. M., Méndez, A. A., & Jiménez-Villarreal, J. (2019) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2019.1661495 · Cited by 5

Electrochemical evaluation of proton beam radiation effect on the B16 cell culture

Onea, M., Bacalum, M., Rădulescu, A. L., Răileanu, M., Craciun, L. S., Esanu, T. R., & Enache, T. A. (2022) · Scientific Reports · doi:10.1038/s41598-022-06277-6 · Cited by 5

Analysis of Cysteine Redox Post-Translational Modifications in Cell Biology and Drug Pharmacology

Wani, R., & Murray, B. W. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6783-4_9 · Cited by 7

Correction: HMGB1 Accelerates Alveolar Epithelial Repair via an IL-1β- and αvβ6 Integrin-dependent Activation of TGF-β1

Pittet, J., Koh, H., Fang, X., Iles, K. E., Christiaans, S. C., Anjun, N., Wagener, B. M., Park, D. W., Zmijewski, J. W., Matthay, M. A., et al. (2013) · PLoS ONE · doi:10.1371/annotation/88f820f2-18dd-4d3b-8989-68f170b26b04 · Cited by 5

Endothelial Drp1 Couples VEGF-induced Redox Signaling with Glycolysis Through Cysteine Oxidation to Drive AngiogenesisPreprint

Nagarkoti, S., Kim, Y.-M., Das, A., Ash, D., Vitriol, E. A., Read, T., Varadarajan, S., Hossain, M. S., Yadav, S., McMenamin, M., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.15.599174 · Cited by 5

Modulation of Innate Immune Memory Dynamics by Subcellular Reactive Oxygen Species

Geng, S., Lin, R., Wu, Y., Wang, J., & Li, L. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0304 · Cited by 5

Oroxylin A reverses SHP-2 oxidative inactivation in GPVI signaling to suppress platelet activation and thrombus formation

Chen, Y., Lin, Y., Hong, J., Wang, J., Li, B.-X., Liu, Z., Ma, Y., Sun, X., Wang, S., Li, M., et al. (2025) · Thrombosis Journal · doi:10.1186/s12959-025-00709-9 · Cited by 4

An emerging role for cysteine-mediated redox signaling in aging

Jin, M. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103852 · Cited by 6

Influence of skeletal muscle heterogeneity on autophagic signaling and response

Rahman, F. A., & Quadrilatero, J. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2562429 · Cited by 4

AMP-Activated Protein Kinase: A Metabolic Stress Sensor in the Heart

Pelosse, M., Tokarska-Schlattner, M., & Schlattner, U. (2015) · Springer eBooks · doi:10.1007/978-3-319-15263-9_10 · Cited by 4

Early Cardiac Ischemia–Reperfusion Injury: Interactions of Autophagy with Galectin-3 and Oxidative Stress

Al‐Salam, S., Hashmi, S., Jagadeesh, G. S., Sudhadevi, M., Awwad, A., & Nemmar, A. (2024) · Biomedicines · doi:10.3390/biomedicines12112474 · Cited by 4

Significance of 5’AMP-activated protein kinase in metabolomic regulation by skeletal muscle contraction

Miyamoto, L. (2015) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.4.93 · Cited by 5

Involvement of AMP-activated Protein Kinase α/Nuclear Factor (Erythroid-derived 2) Like 2-iniatived Signaling Pathway in Cytoprotective Effects of Wasabi 6-(Methylsulfinyl) Hexyl Isothiocyanate

Pan, X., Xie, K., Chen, K., He, Z., Sakao, K., & Hou, D.-X. (2022) · Journal of Cancer Prevention · doi:10.15430/jcp.2022.27.1.58 · Cited by 5

The Complex Crosstalk Between Autophagy and ROS Signalling Pathways

Airiau, K., & Djavaheri‐Mergny, M. (2016) · Springer eBooks · doi:10.1007/978-3-319-30079-5_3 · Cited by 4

Energy deprivation in youth and old age

Stern, M. (2025) · Journal of Cell Science · doi:10.1242/jcs.264018 · Cited by 3

Revisiting ROS: duality in organ aging progression

Yu, M., Liu, S., Zhang, C., & Yang, W. J. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-11342-0 · Cited by 3

Possible Metabolic Remodeling based on de novo Biosynthesis of L-serine in Se-Subtoxic or -Deficient Mammals

Wang, J., Zhang, X., Zhan, S., Han, F., Wang, Q., Liu, Y., & Huang, Z. (2024) · Journal of Nutrition · doi:10.1016/j.tjnut.2024.10.041 · Cited by 4

Mitochondrial calcium uniporter is required for thermogenic adaptation mediated by reactive oxygen species signaling

Kim, S., Cha, S., Park, K., & Namkung, J. (2025) · Journal of Lipid Research · doi:10.1016/j.jlr.2025.100834 · Cited by 3

Redox Reactions in the Physiopathology of the Liver

Méndez, I. G., Vázquez‐Cuevas, F. G., Hernández-Muñoz, R. E., Valente‐Godínez, H., Martínez, O. V., & Díaz‐Muñoz, M. (2017) · InTech eBooks · doi:10.5772/intechopen.68841 · Cited by 3

AMPK function in uterine vasculature and placenta at high altitude

Lorca, R. A. (2025) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2024.0174 · Cited by 3

A New Understanding of Metformin

Hardie, D. G. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00099-2 · Cited by 3

Synthetic lethality targeting LKB1 mutant and EGFR wild type human non-small cell lung cancer cells by glucose starvation and SGLT2 inhibitionPreprint

Ren, Y., Chen, J., Mo, X., Yang, Q., Chen, P., Lu, G. X., Tan, H. W. S., Yi, J., Yu, Q., Kim, Y., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/622126 · Cited by 3

Forchlorfenuron-Induced Mitochondrial Respiration Inhibition and Metabolic Shifts in Endometrial Cancer

Kim, K., Khazan, N., Rowswell-Turner, R. B., Singh, R. K., Moore, T., Strawderman, M. S., Miller, J. P., Snyder, C. W. A., Awada, A., & Moore, R. G. (2024) · Cancers · doi:10.3390/cancers16050976 · Cited by 2

Ribosome collisions and ZAKα activation: explores the therapeutic potential of metabolic diseases

Zhang, W., Zhang, K., Kan, C., Sheng, S., Hou, N., Han, F., Zhang, J., & Sun, X. (2025) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00334.2025 · Cited by 2

Fish Oil Present in High-Fat Diet, Unlike Other Fats, Attenuates Oxidative Stress and Activates Autophagy in Murine Adipose Tissue

Ciesielska, K., Wilczak, J., Prostek, A., Karpiński, P., Sapierzyński, R. A., Majewska, A., Dzięgelewska-Sokołowska, Ż., & Gajewska, M. (2025) · Nutrients · doi:10.3390/nu17233776 · Cited by 2

AMPK as a regulatory node in cell death

Rong, D., You, S., & Shen, H. (2026) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2026.02.006 · Cited by 3

The Positive Roles for Reactive Oxygen Species in Human Reproduction; Implications for the Therapeutic Application of Antioxidants

Pyneandee, E. M., Bakos, H. W., Iuliis, G. N. D., & Aitken, R. J. (2026) · Antioxidants · doi:10.3390/antiox15060674 · Cited by 2

Adenosine Monophosphate-Activated Protein Kinase, Oxidative Stress, and Diabetic Endothelial Dysfunction

Zou, M., & Wu, S. (2021) · Cardiology Discovery · doi:10.1097/cd9.0000000000000009 · Cited by 2

Redox regulation of protein kinase signaling

van der Vliet, A., Dustin, C. M., & Heppner, D. E. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00016-x · Cited by 2

[A Review of the Redox Regulation of Tumor Metabolism].

Wang, K., Ming, H., Zuo, J., Tian, H., & Huang, C. (2021) · PubMed Central · doi:10.12182/20210160204 · Cited by 2

A redox-dependent mechanism for AMPK dysregulation interrupts metabolic adaptation of cancer under glucose deprivationPreprint

Lee, Y., Itahana, Y., Ong, C. C., & Itahana, K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.10.434352 · Cited by 2

Altered neutrophil extracellular traps in response to Mycobacterium tuberculosis in persons living with HIV with no previous TB and negative TST and IGRAPreprint

Kroon, E. E., Correa-Macedo, W., Evans, R. G., Seeger, A., Engelbrecht, L., Kriel, J., Loos, B., Okugbeni, N., Orlova, M., Cassart, P., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.19.537498 · Cited by 2

Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanismsPreprint

Bendzunas, G. N., Byrne, D. P., Shrestha, S., Daly, L. A., Oswald, S. O., Katiyar, S., Venkat, A., Yeung, W., Eyers, C. E., Eyers, P. A., et al. (2024) · eLife · doi:10.7554/elife.92536.2 · Cited by 1

An improved superoxide-generating nanodevice for oxidative stress studies in cultured cells

TAMURA, M. N., Kunihiro, S., Hamashima, Y., Yoshioka, Y., Toné, S., & Kameda, K. (2015) · Biotechnology Reports · doi:10.1016/j.btre.2015.02.003 · Cited by 1

Evaluation of the Cytotoxic Effect of Thymol Loaded Albumin-Coated Fe3O4 Magnetic Nanoparticles on MDA-MB-231 Cell Line and the Expression of Autophagic MAP1LC3A Gene

Haghighi, A., Shahanipour, K., Monajemi, R., Yazdanpanahi, N., & Fouladgar, M. (2023) · Pharmaceutical Chemistry Journal · doi:10.1007/s11094-023-02910-4 · Cited by 1

Redox signaling‑mediated muscle atrophy in ACL injury: Role of physical exercise (Review)

Wang, Y., Gu, C., Zhao, H., Li, Z., & Thirupathi, A. (2025) · Molecular Medicine Reports · doi:10.3892/mmr.2025.13484 · Cited by 1

Targeting peroxiredoxin 2 prevents hepatocarcinogenesis in metabolic liver disease models

Crouchet, É., Schaeffer, E., Oudot, M. A., Moehlin, J., Gadenne, C., Jühling, F., Saghire, H. E., Fujiwara, N., Zhu, S., Rasha, F. A., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci169395 · Cited by 1

Proteasome-mediated ubiquitination in neural regeneration

Li, H., Hu, Y., Cheng, M., Wang, J., Zhao, M., Cao, B., Zhao, Y., & Jiang, J. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118563 · Cited by 1

Mitochondrial NADH dehydrogenase subunit Ⅳ supports CncC-mediated detoxification genes to confer dimefluthrin resistance in Aedes albopictus

Zhou, X., Ma, L., Xu, Q., Dong, Y., & Jiang, D. A. (2026) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2026.104940 · Cited by 1

Redox‐Guided Metabolic Control in Cancer: Integration of the Reactive Oxygen Species–AMP‐Activated Protein Kinase–Sirtuin Axis in Tumour Adaptation and Therapy

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