NOX enzymes and the biology of reactive oxygen

Superoxide Dismutase

McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952

Production of large amounts of hydrogen peroxide by human tumor cells.

Szatrowski, T. P., & Nathan, C. (1991) · PubMed · Cited by 2,504

Cell transformation by the superoxide-generating oxidase Mox1

Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480

Superoxide and hydrogen peroxide in relation to mammalian cell proliferation

Burdon, R. H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00198-s · Cited by 1,174

Killing activity of neutrophils is mediated through activation of proteases by K+ flux

Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153

Reversible Inactivation of the Tumor Suppressor PTEN by H2O2

Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061

Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo

Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040

Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor

Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969

Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1

Abo, A., Pick, E., Hall, A., Totty, N. F., Teahan, C. G., & Segal, A. W. (1991) · Nature · doi:10.1038/353668a0 · Cited by 954

The Neutrophil NADPH Oxidase

BABIOR, B. M., Lambeth, J. D., & Nauseef, W. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2642 · Cited by 911

TNF-Induced Activation of the Nox1 NADPH Oxidase and Its Role in the Induction of Necrotic Cell Death

Kim, Y., Morgan, M. J., Choksi, S., & Liu, Z.-G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.021 · Cited by 523

Reactive Oxygen Species in the Immune System

Yang, Y., Bazhin, A. V., Werner, J., & Karakhanova, S. (2013) · International Reviews of Immunology · doi:10.3109/08830185.2012.755176 · Cited by 523

A Palette of Fluorescent Probes with Varying Emission Colors for Imaging Hydrogen Peroxide Signaling in Living Cells

Dickinson, B. C., Huynh, C., & Chang, C. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1014103 · Cited by 520

Targeting antioxidants for cancer therapy

Glasauer, A., & Chandel, N. S. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.07.017 · Cited by 516

A Magnetofluorescent Carbon Dot Assembly as an Acidic H 2 O 2 ‐Driven Oxygenerator to Regulate Tumor Hypoxia for Simultaneous Bimodal Imaging and Enhanced Photodynamic Therapy

Jia, Q., Ge, J., Liu, W., Zheng, X., Chen, S., Wen, Y., Zhang, H., & Wang, P. (2018) · Advanced Materials · doi:10.1002/adma.201706090 · Cited by 518

Redox regulation of immunometabolism

Muri, J., & Köpf, M. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-00478-8 · Cited by 519

Reactive Oxygen Species (ROS) Regulates Different Types of Cell Death by Acting as a Rheostat

Villalpando-Rodriguez, G. E., & Gibson, S. B. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9912436 · Cited by 515

Regulation of Nox and Duox enzymatic activity and expression

Lambeth, J. D., Kawahara, T., & Diebold, B. A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.028 · Cited by 510

Synergistic Activation of the Arabidopsis NADPH Oxidase AtrbohD by Ca2+ and Phosphorylation

Ogasawara, Y., Kaya, H., Hiraoka, G., Yumoto, F., Kimura, S., Kadota, Y., Hishinuma, H., Senzaki, E., Yamagoe, S., Nagata, K., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708106200 · Cited by 498

Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited

Lambeth, J. D., & Neish, A. S. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104651 · Cited by 495

The Biological Chemistry of Hydrogen Peroxide

Winterbourn, C. C. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405881-1.00001-x · Cited by 490

Amputation-induced reactive oxygen species are required for successful Xenopus tadpole tail regeneration

Love, N. R., Chen, Y., Ishibashi, S., Kritsiligkou, P., Lea, R., Koh, Y. W. H., Gallop, J. L., Dorey, K., & Amaya, E. (2013) · Nature Cell Biology · doi:10.1038/ncb2659 · Cited by 488

Reactive Oxygen Species in Macrophages: Sources and Targets

Canton, M., Sánchez‐Rodríguez, R., Spera, I., Venegas, F. C., Favia, M., Viola, A., & Castegna, A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.734229 · Cited by 490

Kupffer cells in non-alcoholic fatty liver disease: The emerging view

Baffy, G. (2009) · Journal of Hepatology · doi:10.1016/j.jhep.2009.03.008 · Cited by 487

NOX Enzymes in the Central Nervous System: From Signaling to Disease

Sorce, S., & Krause, K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2578 · Cited by 481

Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases

Quinn, M. T., & Gauss, K. A. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0404216 · Cited by 480

Oxidative stress and redox signalling in cardiac hypertrophy and heart failure

Seddon, M., Looi, Y. H., & Shah, A. M. (2006) · Heart · doi:10.1136/hrt.2005.068270 · Cited by 480

Beneficial and Detrimental Effects of Reactive Oxygen Species on Lifespan: A Comprehensive Review of Comparative and Experimental Studies

Shields, H. J., Traa, A., & Van Raamsdonk, J. M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.628157 · Cited by 478

Reactive Oxygen Species Play a Role in Regulating a Fungus–Perennial Ryegrass Mutualistic Interaction

Tanaka, A., Christensen, M. J., Takemoto, D., Park, P., & Scott, B. (2006) · The Plant Cell · doi:10.1105/tpc.105.039263 · Cited by 472

Nox1 Is Involved in Angiotensin II–Mediated Hypertension: A Study in Nox1-Deficient Mice

Matsuno, K., Yamada, H., Iwata, K., Jin, D., Katsuyama, M., Matsuki, M., Takai, S., Yamanishi, K., Miyazaki, M., Matsubara, H., et al. (2005) · Circulation · doi:10.1161/circulationaha.105.573709 · Cited by 470

Redox Reactions and Microbial Killing in the Neutrophil Phagosome

Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468

Oxidative Innate Immune Defenses by Nox/Duox Family NADPH Oxidases

Rada, B., & Leto, T. L. (2008) · KARGER eBooks · doi:10.1159/000136357 · Cited by 469

Regulation of Rice NADPH Oxidase by Binding of Rac GTPase to Its N-Terminal Extension

Wong, H. L., Pinontoan, R., Hayashi, K., Tabata, R., Yaeno, T., Hasegawa, K., Kojima, C., Yoshioka, H., Iba, K., Kawasaki, T., et al. (2007) · The Plant Cell · doi:10.1105/tpc.107.055624 · Cited by 467

ROS generation in plants: Boon or bane?

Garg, N., & Manchanda, G. (2009) · Plant Biosystems - An International Journal Dealing with all Aspects of Plant Biology · doi:10.1080/11263500802633626 · Cited by 466

Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy

Müller, F. L., Song, W., Liu, Y., Chaudhuri, A. R., Pieke-Dahl, S., Strong, R., Huang, T., Epstein, C. J., Roberts, L. J., CSETE, M. E., et al. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.036 · Cited by 466

Oxidative stress, consequences and ROS mediated cellular signaling in rheumatoid arthritis

Phull, A. R., Nasir, B., Haq, I. U., & Kim, S. J. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.12.024 · Cited by 465

NADPH Oxidases in the Kidney

Gill, P. S., & Wilcox, C. S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1597 · Cited by 464

The Nox Family of NAD(P)H Oxidases: Host Defense and Beyond

Geiszt, M., & Leto, T. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400024200 · Cited by 464

T cells express a phagocyte-type NADPH oxidase that is activated after T cell receptor stimulation

Jackson, S. H., Devadas, S., Kwon, J., Pinto, L. A., & Williams, M. S. (2004) · Nature Immunology · doi:10.1038/ni1096 · Cited by 457

NADPH oxidase-4 mediates protection against chronic load-induced stress in mouse hearts by enhancing angiogenesis

Zhang, M., Brewer, A. C., Schröder, K., Santos, C. X. C., Grieve, D., Wang, M., Anilkumar, N. P., Yu, B., Dong, X., Walker, S. J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009700107 · Cited by 452

Cerium oxide nanoparticles: properties, biosynthesis and biomedical application

Singh, K. R., Nayak, V., Sarkar, T., & Singh, R. P. (2020) · RSC Advances · doi:10.1039/d0ra04736h · Cited by 447

Oxidant Sensing by Reversible Disulfide Bond Formation

Cremers, C. M., & Jakob, U. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.462929 · Cited by 446

An antioxidant nanozyme that uncovers the cytoprotective potential of vanadia nanowires

Vernekar, A. A., Sinha, D., Srivastava, S., Paramasivam, P. U., D’Silva, P., & Mugesh, G. (2014) · Nature Communications · doi:10.1038/ncomms6301 · Cited by 445

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

Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603290103 · Cited by 442

Nrf2-induced antioxidant protection: A promising target to counteract ROS-mediated damage in neurodegenerative disease?

de Vries, H. E., Witte, M. E., Hondius, D., Rozemüller, A. J. M., Drukarch, B., Hoozemans, J. J. M., & van Horssen, J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.001 · Cited by 436

Sulfenic acid chemistry, detection and cellular lifetime

Gupta, V., & Carroll, K. S. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.040 · Cited by 434

RONS and Oxidative Stress: An Overview of Basic Concepts

Aranda‐Rivera, A. K., Cruz‐Gregorio, A., Arancibia‐Hernández, Y. L., Cruz, E. Y. H., & Pedraza‐Chaverrí, J. (2022) · Oxygen · doi:10.3390/oxygen2040030 · Cited by 437

Iron and Cancer

Torti, S. V., Manz, D. H., Paul, B. T., Blanchette-Farra, N., & Torti, F. M. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-082117-051732 · Cited by 426

Oxidative stress pathways of air pollution mediated toxicity: Recent insights

Gangwar, R. S., Bevan, G. H., Palanivel, R., Das, L. M., & Rajagopalan, S. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101545 · Cited by 428

Function of reactive oxygen species during animal development: Passive or active?

Covarrubias, L., Hernández-García, D., Schnabel, D., Vidal, E. S., & Castro‐Obregón, S. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2008.04.041 · Cited by 418

Oxidative Stress, Chronic Disease, and Muscle Wasting

Moylan, J. S., & Reid, M. B. (2007) · Muscle & Nerve · doi:10.1002/mus.20743 · Cited by 416

Redox and NF-κB signaling in osteoarthritis

Lepetsos, P., Papavassiliou, K. A., & Papavassiliou, A. G. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.025 · Cited by 412

Mitochondria in innate immune signaling

Banoth, B., & Cassel, S. L. (2018) · Translational Research · doi:10.1016/j.trsl.2018.07.014 · Cited by 410

Symbiotic lactobacilli stimulate gut epithelial proliferation via Nox‐mediated generation of reactive oxygen species

Jones, R. M., Luo, L., Ardita, C., Richardson, A. N., Kwon, Y. M., Mercante, J. W., Alam, A. M., Gates, C. L., Wu, H., Swanson, P. A., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.224 · Cited by 409

Regulation of SUMOylation by Reversible Oxidation of SUMO Conjugating Enzymes

Bossis, G., & Melchior, F. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.12.019 · Cited by 406

PI3Kδ and PI3Kγ: partners in crime in inflammation in rheumatoid arthritis and beyond?

Rommel, C., Camps, M., & Ji, H. (2007) · Nature reviews. Immunology · doi:10.1038/nri2036 · Cited by 405

Oxidative Stress and Redox-Modulating Therapeutics in Inflammatory Bowel Disease

Bourgonje, A. R., Feelisch, M., Faber, K. N., Pasch, A., Dijkstra, G. D. H., & van Goor, H. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.06.006 · Cited by 405

Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance

Bubici, C., Papa, S., Dean, K., & Franzoso, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209936 · Cited by 399

The Role of Oxidative Stress in Cardiac Disease: From Physiological Response to Injury Factor

D’Oria, R., Schipani, R., Leonardini, A., Natalicchio, A., Perrini, S., Cignarelli, A., Laviola, L., & Giorgino, F. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5732956 · Cited by 399

Microglial Activation in Stroke: Therapeutic Targets

Yenari, M. A., Kauppinen, T. M., & Swanson, R. A. (2010) · Neurotherapeutics · doi:10.1016/j.nurt.2010.07.005 · Cited by 398

Role of oxygen gradients in shaping redox relationships between the human intestine and its microbiota

Espey, M. G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.554 · Cited by 396

Myeloid‐derived suppressor cell heterogeneity in human cancers

Solito, S., Marigo, I., Pinton, L., Damuzzo, V., Mandruzzato, S., & Bronte, V. (2014) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12469 · Cited by 395

Mitochondrial ROS Generation and Its Regulation: Mechanisms Involved in H 2 O 2 Signaling

Rigoulet, M., Yoboue, E. D., & Devin, A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3363 · Cited by 394

Novel Action of Paclitaxel against Cancer Cells: Bystander Effect Mediated by Reactive Oxygen Species

Alexandre, J., Hu, Y., Lu, W., Pelicano, H., & Huang, P. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3914 · Cited by 391

MAPK Signaling Regulates Nitric Oxide and NADPH Oxidase-Dependent Oxidative Bursts inNicotiana benthamiana

Asai, S., Ohta, K., & Yoshioka, H. (2008) · The Plant Cell · doi:10.1105/tpc.107.055855 · Cited by 390

Molecular mechanism of α-tocopherol action

Azzi, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.013 · Cited by 387

A Mesoporous Nanoenzyme Derived from Metal–Organic Frameworks with Endogenous Oxygen Generation to Alleviate Tumor Hypoxia for Significantly Enhanced Photodynamic Therapy

Wang, D., Wu, H., Lim, W. Q., Phua, S. Z. F., Xu, P., Chen, Q., Guo, Z. G., & Zhao, Y. (2019) · Advanced Materials · doi:10.1002/adma.201901893 · Cited by 386

ROS: Crucial Intermediators in the Pathogenesis of Intervertebral Disc Degeneration

Feng, C., Yang, M., Lan, M., Liu, C., Zhang, Y., Huang, B., Liu, H., & Zhou, Y. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5601593 · Cited by 384

Controlled Elimination of Intracellular H 2 O2: Regulation of Peroxiredoxin, Catalase, and Glutathione Peroxidase via Post-translational Modification

Rhee, S. G., Yang, K.-S., Kang, S. W., Woo, H. A., & Chang, T.-S. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.619 · Cited by 376

Leukocyte Recruitment and Vascular Injury in Diabetic Nephropathy

Galkina, E., & Ley, K. F. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2005080859 · Cited by 376

Compartmentalization of Redox Signaling Through NADPH Oxidase–Derived ROS

Ushio‐Fukai, M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2333 · Cited by 375

SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model

Harraz, M. M., Marden, J. J., Zhou, W., Zhang, Y., Williams, A. J., Sharov, V. S., Nelson, K., Luo, M., Paulson, H. L., Schöneich, C., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34060 · Cited by 375

Redox Regulation by Keap1 and Nrf2 Controls Intestinal Stem Cell Proliferation in Drosophila

Hochmuth, C. E., Biteau, B., Bohmann, D., & Jasper, H. (2011) · Cell stem cell · doi:10.1016/j.stem.2010.12.006 · Cited by 374

Similarities and Distinctions of Cancer and Immune Metabolism in Inflammation and Tumors

Andrejeva, G., & Rathmell, J. C. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.06.004 · Cited by 374

Single‐Atom Catalysts in Catalytic Biomedicine

Xiang, H., Feng, W., & Chen, Y. (2020) · Advanced Materials · doi:10.1002/adma.201905994 · Cited by 375

Nox4: A Hydrogen Peroxide-Generating Oxygen Sensor

Nisimoto, Y., Diebold, B. A., Cosentino‐Gomes, D., & Lambeth, J. D. (2014) · Biochemistry · doi:10.1021/bi500331y · Cited by 370

Reactive oxygen species mediate crosstalk between NF-κB and JNK

Nakano, H., Nakajima, A., Sakon-Komazawa, S., Piao, J.-H., Xue, X., & Okumura, K. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401830 · Cited by 370

Redox Signaling by Reactive Electrophiles and Oxidants

Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 372

Effect of Particulate Matter Air Pollution on Cardiovascular Oxidative Stress Pathways

Rao, X., Zhong, J., Brook, R. D., & Rajagopalan, S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7394 · Cited by 368

NADPH Oxidases of the Brain: Distribution, Regulation, and Function

Infanger, D. W., Sharma, R. V., & Davisson, R. L. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1583 · Cited by 365

The cysteine proteome

Go, Y., Chandler, J. D., & Jones, D. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.022 · Cited by 363

Oxidative stress in autoimmune rheumatic diseases

Smallwood, M. J., Nissim, A., Knight, A. R., Whiteman, M., Haigh, R. C., & Winyard, P. G. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.086 · Cited by 358

Angiotensin II-Induced Production of Mitochondrial Reactive Oxygen Species: Potential Mechanisms and Relevance for Cardiovascular Disease

Dikalov, S. I., & Nazarewicz, R. R. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4604 · Cited by 356

Oxidative stress in early diabetic nephropathy: fueling the fire

Singh, D. K., Winocour, P. H., & Farrington, K. (2010) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2010.212 · Cited by 353

Isoprostane Generation and Function

Milne, G. L., Yin, H., Hardy, K. D., Davies, S. S., & Roberts, L. J. (2011) · Chemical Reviews · doi:10.1021/cr200160h · Cited by 349

Coordination of multiple dual oxidase–regulatory pathways in responses to commensal and infectious microbes in drosophila gut

Ha, E.-M., Lee, K.-A., Seo, Y. Y., Kim, S.-H., Lim, J.-H., Oh, B., Kim, J., & Lee, W. (2009) · Nature Immunology · doi:10.1038/ni.1765 · Cited by 349

Reactive Oxygen Species Regulate Hematopoietic Stem Cell Self-Renewal, Migration and Development, As Well As Their Bone Marrow Microenvironment

Ludin, A., Gur‐Cohen, S., Golan, K., Kaufmann, K. B., Itkin, T., Medaglia, C., Lu, X., Ledergor, G., Kollet, Ó., & Lapidot, T. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5941 · Cited by 349

Reactive Nitrogen Species: Molecular Mechanisms and Potential Significance in Health and Disease

Martínez, M. C., & Andriantsitohaina, R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1993 · Cited by 345

NOX4/NADPH oxidase expression is increased in pulmonary fibroblasts from patients with idiopathic pulmonary fibrosis and mediates TGF 1-induced fibroblast differentiation into myofibroblasts

Amara, N., Goven, D., Prost, F., Muloway, R., Crestani, B., & Boczkowski, J. (2010) · Thorax · doi:10.1136/thx.2009.113456 · Cited by 345

Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes

Kawahara, T., Quinn, M. T., & Lambeth, J. D. (2007) · BMC Evolutionary Biology · doi:10.1186/1471-2148-7-109 · Cited by 346

Facet Energy versus Enzyme-like Activities: The Unexpected Protection of Palladium Nanocrystals against Oxidative Damage

Ge, C., Ge, F., Shen, X., Chong, Y., Wamer, W. G., Gao, X., Chai, Z., Chen, C., & Yin, J. (2016) · ACS Nano · doi:10.1021/acsnano.6b06297 · Cited by 345

NADPH oxidase-dependent redox signalling in cardiac hypertrophy, remodelling and failure

Murdoch, C. E., Zhang, M., Cave, A. C., & Shah, A. M. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.03.016 · Cited by 344

Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity

Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342

Features of Microglia and Neuroinflammation Relevant to Environmental Exposure and Neurotoxicity

Kraft, A. D., & Harry, G. J. (2011) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph8072980 · Cited by 340

Mitochondria as a Therapeutic Target in Heart Failure

Bayeva, M., Gheorghiade, M., & Ardehali, H. (2012) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2012.08.1021 · Cited by 340

DNA damage-induced reactive oxygen species (ROS) stress response in Saccharomyces cerevisiae

Rowe, L. A., Degtyareva, N. P., & Doetsch, P. W. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.07.018 · Cited by 339

Chemotherapy-Induced Weakness and Fatigue in Skeletal Muscle: The Role of Oxidative Stress

Gilliam, L. A. A., & Clair, D. K. S. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3965 · Cited by 338

Oxidative stress and cardiovascular disease: Novel tools give (free) radical insight

Fearon, I. M., & Faux, S. P. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.05.013 · Cited by 334

Tuning of Redox Regulatory Mechanisms, Reactive Oxygen Species and Redox Homeostasis under Salinity Stress

Hossain, M. S., & Dietz, K. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00548 · Cited by 333

Unconventional Roles of the NADPH Oxidase: Signaling, Ion Homeostasis, and Cell Death

Steinberg, B. E., & Grinstein, S. (2007) · Science s STKE · doi:10.1126/stke.3792007pe11 · Cited by 331

Oxygen toxicity: chemistry and biology of reactive oxygen species

Buonocore, G., Perrone, S., & Tataranno, M. L. (2010) · Seminars in Fetal and Neonatal Medicine · doi:10.1016/j.siny.2010.04.003 · Cited by 329

Redox Paradox

Goldstein, B. J., Mahadev, K., & Wu, X. (2005) · Diabetes · doi:10.2337/diabetes.54.2.311 · Cited by 329

Metastasis: cancer cell’s escape from oxidative stress

Pani, G., Galeotti, T., & Chiarugi, P. (2010) · Cancer and Metastasis Reviews · doi:10.1007/s10555-010-9225-4 · Cited by 328

2-Cys peroxiredoxin function in intracellular signal transduction: therapeutic implications

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