Dynamic redox control of NF-κB through glutaredoxin-regulated S-glutathionylation of inhibitory κB kinase β

NOX enzymes and the biology of reactive oxygen

Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125

A cytokine-responsive IκB kinase that activates the transcription factor NF-κB

DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125

IKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation

Mercurio, F., Zhu, H., Murray, B. W., Shevchenko, A., Bennett, B. L., Li, J. W., Young, D. B., Barbosa, M. S., Mann, M., Manning, A. M., et al. (1997) · Science · doi:10.1126/science.278.5339.860 · Cited by 2,042

Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase

Rossi, A., Kapahi, P., Natoli, G., Takahashi, T., Chen, Y., Karin, M., & Santoro, M. G. (2000) · Nature · doi:10.1038/47520 · Cited by 1,303

IKK-γ is an essential regulatory subunit of the IκB kinase complex

Rothwarf, D. M., Zandi, E., Natoli, G., & Karin, M. (1998) · Nature · doi:10.1038/26261 · Cited by 958

Positive and Negative Regulation of IκB Kinase Activity Through IKKβ Subunit Phosphorylation

Delhase, M., Hayakawa, M., Chen, Y., & Karin, M. (1999) · Science · doi:10.1126/science.284.5412.309 · Cited by 852

Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD

Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E. V., & Chumakov, P. M. (2004) · Science · doi:10.1126/science.1095569 · Cited by 731

Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System

Fernandes, A. P., & Holmgren, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/152308604771978354 · Cited by 670

S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide

Adachi, T. K., Weisbrod, R. M., Pimentel, D. R., Ying, J., Sharov, V. S., Schöneich, C., & Cohen, R. A. (2004) · Nature Medicine · doi:10.1038/nm1119 · Cited by 662

Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression

Yamamoto, Y., Verma, U. N., Prajapati, S., Kwak, Y.-T., & Gaynor, R. B. (2003) · Nature · doi:10.1038/nature01576 · Cited by 577

Protein S-glutathiolation: Redox-sensitive regulation of protein function

Hill, B. G., & Bhatnagar, A. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.07.009 · Cited by 123

Pharmacological antioxidant strategies as therapeutic interventions for COPD

Rahman, I. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.004 · Cited by 117

Reactive oxygen species (ROS) in cancer: from mechanism to therapeutic implications

Akter, S., Madhuvilakku, R., Kar, A. K., Nila, I. S., Liu, P., Inuzuka, H., Wei, W., & Hong, Y. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02583-x · Cited by 135

Mechanisms of Altered Redox Regulation in Neurodegenerative Diseases—Focus on S-Glutathionylation

Liedhegner, E. S., Gao, X., & Mieyal, J. J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4119 · Cited by 118

Carbon disulfide. Just toxic or also bioregulatory and/or therapeutic?

DeMartino, A. W., Zigler, D. F., Fukuto, J. M., & Ford, P. C. (2016) · Chemical Society Reviews · doi:10.1039/c6cs00585c · Cited by 117

Genetic dissection of the Nrf2-dependent redox signaling-regulated transcriptional programs of cell proliferation and cytoprotection

Reddy, N. M., Kleeberger, S. R., Yamamoto, M. P., Kensler, T. W., Scollick, C., Biswal, S. S., & Reddy, S. P. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00126.2007 · Cited by 113

Nuclear Factor Kappa B Signaling Complexes in Acute Inflammation

Rius‐Pérez, S., Pérez, S., Martí‐Andrés, P., Monsalve, M., & Sastre, J. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7975 · Cited by 116

Formation, Reactivity, and Detection of Protein Sulfenic Acids

Kettenhofen, N. J., & Wood, M. J. A. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100237w · Cited by 111

Oxidative stress underlying axonal degeneration in adrenoleukodystrophy: A paradigm for multifactorial neurodegenerative diseases?

Galea, E., Launay, N., Portero-Otin, M., Ruiz, M., Pamplona, R., Aubourg, P., Ferrer, I., & Pujol, A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.02.005 · Cited by 108

Regulation of apoptosis by Bcl-2 cysteine oxidation in human lung epithelial cells

Luanpitpong, S., Chanvorachote, P., Stehlik, C., Tse, W., Callery, P. S., Wang, L., & Rojanasakul, Y. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0747 · Cited by 102

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Ho, Y.-S., Xiong, Y., Ho, D. S., Gao, J., Chua, B. H. L., Pai, H. V., & Mieyal, J. J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.07.025 · Cited by 101

A reducing redox environment promotes C2C12 myogenesis: Implications for regeneration in aged muscle

Hansen, J. M., Klass, M., Harris, C., & CSETE, M. E. (2006) · Cell Biology International · doi:10.1016/j.cellbi.2006.11.027 · Cited by 100

The role of oxidative stress in the pathogenesis of infections with coronaviruses

Gain, C., Song, S., Angtuaco, T., Satta, S., & Kelesidis, T. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1111930 · Cited by 104

Glutathione Redox Control of Asthma: From Molecular Mechanisms to Therapeutic Opportunities

Fitzpatrick, A. M., Jones, D. P., & Brown, L. A. S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4198 · Cited by 101

Glutaredoxin-2 Is Required to Control Oxidative Phosphorylation in Cardiac Muscle by Mediating Deglutathionylation Reactions

Mailloux, R. J., Xuan, J. Y., McBride, S., Maharsy, W. M., Thorn, S., Holterman, C. E., Kennedy, C., Rippstein, P. U., deKemp, R. A., da Silva, J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.550574 · Cited by 101

Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling

Su, D. G. T., Gaffrey, M. J., Guo, J., Hatchell, K. E., Chu, R., Clauss, T. R., Aldrich, J. T., Wu, S., Purvine, S. O., Camp, D., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.004 · Cited by 98

Endoplasmic reticulum stress mediates house dust mite-induced airway epithelial apoptosis and fibrosis

Hoffman, S. M., Tully, J. E., Nolin, J. D., Lahue, K. G., Goldman, D. H., Daphtary, N., Aliyeva, M., Irvin, C. G., Dixon, A. E., Poynter, M. E., et al. (2013) · Respiratory Research · doi:10.1186/1465-9921-14-141 · Cited by 100

Loss of Transcription Factor Nuclear Factor-Erythroid 2 (NF-E2) p45-related Factor-2 (Nrf2) Leads to Dysregulation of Immune Functions, Redox Homeostasis, and Intracellular Signaling in Dendritic Cells

Yeang, H. X. A., Hamdam, J. M., Al-Huseini, L. M. A., Sethu, S., Djouhri, L., Walsh, J., Kitteringham, N. R., Park, B. K., Goldring, C. E., & Sathish, J. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322420 · Cited by 97

Redox regulation of macrophages

Tran, N., & Mills, E. L. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103123 · Cited by 101

Targeting tissue oxidative damage by means of cell signaling modulators: The antioxidant concept revisited

Leonarduzzi, G., Sottero, B., & Poli, G. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.08.003 · Cited by 100

Antiinflammatory Effects of Hydrogen Peroxide in Neutrophil Activation and Acute Lung Injury

Zmijewski, J. W., Lorne, E., Zhao, X., Tsuruta, Y., Sha, Y., Liu, G., & Abraham, E. H. (2009) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200806-851oc · Cited by 96

Antioxidant Supplementation in Oxidative Stress-Related Diseases: What Have We Learned from Studies on Alpha-Tocopherol?

Meulmeester, F. L., Luo, J. M., Martens, L. G., Mills, K. A., van Heemst, D., & Noordam, R. (2022) · Antioxidants · doi:10.3390/antiox11122322 · Cited by 103

AIM2 promotes the development of non-small cell lung cancer by modulating mitochondrial dynamics

Qi, M., Dai, D., Liu, J., Li, Z., Liang, P., Wang, Y., Lu, C., Zhan, Y., An, Z., Song, Y., et al. (2020) · Oncogene · doi:10.1038/s41388-020-1176-9 · Cited by 96

Protein Glutathionylation in Cardiovascular Diseases

Pastore, A., & Piemonte, F. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141020845 · Cited by 95

Redox signaling in the pancreas in health and disease

Sastre, J., Pérez, S., Sabater-Orti, L., & Rius‐Pérez, S. (2024) · Physiological Reviews · doi:10.1152/physrev.00044.2023 · Cited by 101

Oxidative stress as a therapeutic target during muscle wasting: considering the complex interactions

Arthur, P. G., Grounds, M. D., & Shavlakadze, T. (2008) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e328302f3fe · Cited by 95

New Insight into the Role of Reactive Oxygen Species (ROS) in Cellular Signal-Transduction Processes

Russell, E. G., & Cotter, T. G. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.07.004 · Cited by 95

Methods for Analysis of Protein Glutathionylation and their Application to Photosynthetic Organisms

Gao, X., Bedhomme, M., Veyel, D., Zaffagnini, M., & Lemaire, S. D. (2008) · Molecular Plant · doi:10.1093/mp/ssn072 · Cited by 97

Modulation of redox homeostasis: A strategy to overcome cancer drug resistance

Yang, L., Zhang, X., Wang, Z., Li, B., & Zhu, H. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1156538 · Cited by 96

Glutathione adducts induced by ischemia and deletion of glutaredoxin-1 stabilize HIF-1α and improve limb revascularization

Watanabe, Y., Murdoch, C. E., Sano, S., Ido, Y., Bachschmid, M. M., Cohen, R. A., & Matsui, R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1524198113 · Cited by 91

Fishing the PTM proteome with chemical approaches using functional solid phases

Zhang, Y., Zhang, C., Jiang, H., Yang, P., & Lu, H. (2015) · Chemical Society Reviews · doi:10.1039/c4cs00529e · Cited by 90

Enterovirus 71 2C Protein Inhibits TNF-α–Mediated Activation of NF-κB by Suppressing IκB Kinase β Phosphorylation

Zheng, Z., Li, H., Zhang, Z., Meng, J., Mao, D., Bai, B., Lu, B., Mao, P., Hu, Q., & Wang, H. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100285 · Cited by 85

Redox-Based Regulation of Apoptosis: S-Glutathionylation As a Regulatory Mechanism to Control Cell Death

Anathy, V., Roberson, E. C., Guala, A. S., Godburn, K. E., Budd, R. C., & Janssen-Heininger, Y. M. W. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4281 · Cited by 85

NADPH Oxidase Limits Lipopolysaccharide-Induced Lung Inflammation and Injury in Mice through Reduction-Oxidation Regulation of NF-κB Activity

Han, W., Li, H., Cai, J., Gleaves, L. A., Polosukhin, V. V., Segal, B. H., Yull, F. E., & Blackwell, T. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201809 · Cited by 84

Quantitative Profiling of Protein S-Glutathionylation Reveals Redox-Dependent Regulation of Macrophage Function during Nanoparticle-Induced Oxidative Stress

Duan, J., Kodali, V., Gaffrey, M. J., Guo, J., Chu, R., Camp, D., Smith, R. D., Thrall, B. D., & Qian, W. (2015) · ACS Nano · doi:10.1021/acsnano.5b05524 · Cited by 82

Glutathione depletion activates mitogen-activated protein kinase (MAPK) pathways that display organ-specific responses and brain protection in mice

Limón-Pacheco, J. H., Hernández, N. A. H., Fanjul‐Moles, M. L., & Gonsebatt, M. E. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.028 · Cited by 83

Oxidative Stress and Intervertebral Disc Degeneration: Pathophysiology, Signaling Pathway, and Therapy

Li, Y., Chen, L., Gao, Y. Z., Zou, X., & Wei, F. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1984742 · Cited by 82

Pathways Impacted by Genomic Alterations in Pulmonary Carcinoid Tumors

Asiedu, M. K., Thomas, C. F., Dong, J., Schulte, S. C., Khadka, P., Sun, Z., Kosari, F., Jen, J., Molina, J. R., Vasmatzis, G., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-0252 · Cited by 82

Fifty years in the thioredoxin field and a bountiful harvest

Buchanan, B. B., Holmgren, A., Jacquot, J., & Scheibe, R. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.07.006 · Cited by 80

Glutathione S-transferase pi modulates NF-κB activation and pro-inflammatory responses in lung epithelial cells

Jones, J. T., Qian, X., van der Velden, J. L. J., Chia, S. B., McMillan, D. H., Flemer, S., Hoffman, S. M., Lahue, K. G., Schneider, R. W., Nolin, J. D., et al. (2016) · Redox Biology · doi:10.1016/j.redox.2016.03.005 · Cited by 79

Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding

Beedle, A. E. M., Lynham, S., & Garcia-Manyes, S. (2016) · Nature Communications · doi:10.1038/ncomms12490 · Cited by 80

Attenuation of doxorubicin-induced cardiac injury by mitochondrial glutaredoxin 2

Diotte, N. M., Xiong, Y., Gao, J., Chua, B. H. L., & Ho, Y.-S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.014 · Cited by 78

Hydrogen peroxide inhibits caspase-dependent apoptosis by inactivating procaspase-9 in an iron-dependent manner

Barbouti, A., Amorgianiotis, C., Kolettas, E., Kanavaros, P., & Galaris, D. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.020 · Cited by 78

Structure, function and disease relevance of Omega-class glutathione transferases

Philip G. Board, & Menon, D. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1691-1 · Cited by 78

S‐glutathionylation of IRF3 regulates IRF3–CBP interaction and activation of the IFNβ pathway

Prinarakis, E., Chantzoura, E., Thanos, D., & Spyrou, G. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.28 · Cited by 77

The Influence of Light on Reactive Oxygen Species and NF-кB in Disease Progression

Rajendran, N. K., George, B. P. A., Chandran, R., Tynga, I. M., Houreld, N. N., & Abrahamse, H. (2019) · Antioxidants · doi:10.3390/antiox8120640 · Cited by 79

Control of SUMO and Ubiquitin by ROS: Signaling and disease implications

Stankovic‐Valentin, N., & Melchior, F. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.07.002 · Cited by 79

Regulation of Cell Physiology and Pathology by Protein S-Glutathionylation: Lessons Learned from the Cardiovascular System

Pimentel, D. R., Haeussler, D. J., Matsui, R., Burgoyne, J. R., Cohen, R. A., & Bachschmid, M. M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4336 · Cited by 78

Decreased Expression of the Host Long-Noncoding RNA-GM Facilitates Viral Escape by Inhibiting the Kinase activity TBK1 via S-glutathionylation

Wang, Y., Wang, P., Zhang, Y., Xu, J., Li, Z., Li, Z., Zhou, Z., Liu, L., & Cao, X. (2020) · Immunity · doi:10.1016/j.immuni.2020.11.010 · Cited by 75

Toxicological Evaluation of Thiol-Reactive Compounds Identified Using a La Assay To Detect Reactive Molecules by Nuclear Magnetic Resonance

Huth, J. R., Song, D., Mendoza, R. R., Black-Schaefer, C. L., Mack, J. C., Dorwin, S. A., Ladror, U. S., Severin, J. M., Walter, K. A., Bartley, D. M., et al. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700319t · Cited by 76

Glutathione transferase Omega 1 is required for the lipopolysaccharide-stimulated induction of NADPH oxidase 1 and the production of reactive oxygen species in macrophages

Menon, D., Coll, R. C., O'Neill, L. A. J., & Philip G. Board (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.05.020 · Cited by 77

Peroxides and Peroxide-Degrading Enzymes in the Thyroid

Schweizer, U., Chiu, J., & Köhrle, J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2054 · Cited by 74

Glutaredoxin Regulates Apoptosis in Cardiomyocytes via NFκB Targets Bcl-2 and Bcl-xL: Implications for Cardiac Aging

Gallogly, M. M., Shelton, M. D., Qanungo, S., Pai, H. V., Starke, D. W., Hoppel, C. L., Lesnefsky, E. J., & Mieyal, J. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2791 · Cited by 73

Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae

Greetham, D., Vickerstaff, J., Shenton, D., Perrone, G. G., Dawes, I. W., & Grant, C. M. (2010) · BMC Biochemistry · doi:10.1186/1471-2091-11-3 · Cited by 72

Redox signaling in innate immunity and inflammation: focus on macrophages and neutrophils

Braunstein, I., Motohashi, H., Dallenga, T. K., Schaible, U. E., & Benhar, M. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.006 · Cited by 75

Oxidants Positively or Negatively Regulate Nuclear Factor κB in a Context-dependent Manner

Loukili, N., Rosenblatt‐Velin, N., Rolli, J., Levrand, S., Feihl, F., Waeber, B., Pacher, P., & Liaudet, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.103259 · Cited by 71

KEAP1-Dependent Synthetic Lethality Induced by AKT and TXNRD1 Inhibitors in Lung Cancer

Dai, B., Yoo, S., Bartholomeusz, G. A., Graham, R. A., Majidi, M., Yan, S., Meng, J., Ji, L., Coombes, K. R., Minna, J. D., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0712 · Cited by 71

Mitochondria in neurodegenerative disorders: regulation of the redox state and death signaling leading to neuronal death and survival

Naoi, M., Maruyama, W., Yi, H., Inaba, K., Akao, Y., & Shamoto‐Nagai, M. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0309-7 · Cited by 70

Chemical-proteomic strategies to investigate cysteine posttranslational modifications

Couvertier, S. M., Zhou, Y., & Weerapana, E. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.09.024 · Cited by 72

Doxorubicin‐induced platelet cytotoxicity: a new contributory factor for doxorubicin‐mediated thrombocytopenia

KIM, E. J., Lim, K., Kim, K., Bae, O., NOH, J. Y., Chung, S.-M., Shin, S., Yun, Y., & Chung, J. H. (2009) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2009.03477.x · Cited by 68

Interplay between BMPs and Reactive Oxygen Species in Cell Signaling and Pathology

Sánchez‐de‐Diego, C., Valer, J. A., Pimenta-Lopes, C., Rosa, J. L., & Ventura, F. (2019) · Biomolecules · doi:10.3390/biom9100534 · Cited by 70

Glutathionylation regulates IκB

Kil, I. S., Kim, S. Y., & Park, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.007 · Cited by 67

Ablation of Glutaredoxin-1 Attenuates Lipopolysaccharide-Induced Lung Inflammation and Alveolar Macrophage Activation

Aesif, S. W., Anathy, V., Kuipers, I., Guala, A. S., Reiss, J. N., Ho, Y., & Janssen-Heininger, Y. M. W. (2010) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2009-0136oc · Cited by 67

The Glutaredoxin/Glutathione System Modulates NF-κB Activity by Glutathionylation of p65 in Cinnamaldehyde-Treated Endothelial Cells

Liao, B., Hsieh, C., Lin, Y.-C., & Wung, B. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq098 · Cited by 67

Systems approaches to investigate the role of NF-κB signaling in aging

Haga, M., & Okada, M. (2022) · Biochemical Journal · doi:10.1042/bcj20210547 · Cited by 67

Participation of mitochondrial respiratory complex III in neutrophil activation and lung injury

Zmijewski, J. W., Lorne, E., Banerjee, S., & Abraham, E. H. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90522.2008 · Cited by 66

LPS-mediated endothelial activation in pulmonary endothelial cells: role of Nox2-dependent IKK-β phosphorylation

Menden, H. L., Tate, E. R., Hogg, N., & Sampath, V. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00261.2012 · Cited by 65

Functional Aspects of Redox Control During Neuroinflammation

Rosales‐Corral, S., Reiter, R. J., Tan, D., Ortiz, G. G., & López-Armas, G. D. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2629 · Cited by 66

The role of keratinocytes in inflammation

Juráňová, J., Franková, J., & Ulrichová, J. (2017) · Journal of Applied Biomedicine · doi:10.1016/j.jab.2017.05.003 · Cited by 67

S-glutathionylation, friend or foe in cardiovascular health and disease

Rashdan, N. A., Shrestha, B., & Pattillo, C. B. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101693 · Cited by 64

Glutaredoxin-1 Up-regulation Induces Soluble Vascular Endothelial Growth Factor Receptor 1, Attenuating Post-ischemia Limb Revascularization

Murdoch, C. E., Shuler, M. M., Haeussler, D. J., Kikuchi, R., Bearelly, P., Han, J., Watanabe, Y., Fuster, J. J., Walsh, K. X., Ho, Y.-S., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.517219 · Cited by 64

CaMKII Is Essential for the Proasthmatic Effects of Oxidation

Sanders, P. N., Koval, O. M., Jaffer, O. A., Prasad, A. M., Businga, T. R., Scott, J. A., Hayden, P. J., Luczak, E. D., Dickey, D. D., Allamargot, C., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006135 · Cited by 62

Oxidative stress and immunotoxic effects of bisphenol A on the larvae of rare minnow Gobiocypris rarus

Tao, S., Zhang, Y., Yuan, C., Gao, J., Wu, F., & Wang, Z. (2015) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2015.11.014 · Cited by 62

Glutathionyl systems and metabolic dysfunction in obesity

Picklo, M. J., Long, E. K., & Vomhof‐DeKrey, E. E. (2015) · Nutrition Reviews · doi:10.1093/nutrit/nuv042 · Cited by 64

The role of sulfenic acids in cellular redox signaling: Reconciling chemical kinetics and molecular detection strategies

Heppner, D. E., Janssen-Heininger, Y. M. W., & van der Vliet, A. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.01.008 · Cited by 62

Oxidative Stress Mechanisms in the Pathogenesis of Environmental Lung Diseases

Thimmulappa, R. K., Chattopadhyay, I., & Rajasekaran, S. (2019) · Springer eBooks · doi:10.1007/978-981-32-9366-3_5 · Cited by 63

Cocaine-Induced Adaptations in Cellular Redox Balance Contributes to Enduring Behavioral Plasticity

Uys, J. D. K., Knackstedt, L. A., Hurt, P., Tew, K. D., Manevich, Y., Hutchens, S., Townsend, D. M., & Kalivas, P. W. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2011.143 · Cited by 62

Glutathione S-transferases and their implications in the lung diseases asthma and chronic obstructive pulmonary disease: Early life susceptibility?

van de Wetering, C., Elko, E. A., Berg, M., Schiffers, C., Stylianidis, V., van den Berge, M., Nawijn, M. C., Wouters, E. F. �., Janssen-Heininger, Y. M. W., & Reynaert, N. L. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101995 · Cited by 64

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