On the selectivity of superoxide dismutase mimetics and its importance in pharmacological studies
Open accessAbstract
The list of pathophysiological conditions associated with the overproduction of superoxide expands every day. Much of the knowledge compiled on the role of this radical in disease has been gathered using the native superoxide dismutase enzyme and, more recently, by the use of superoxide dismutase knockout models or transgenic models that overexpress the various isoforms of the enzyme. Although the native enzyme has shown promising anti‐inflammatory properties in both preclinical and clinical studies, there were drawbacks and issues associated with its use as a therapeutic agent and pharmacological tool. Based on the concept that removal of superoxide modulates the course of inflammation, synthetic, low‐molecular‐weight mimetics of the superoxide dismutase enzymes that could overcome some of the limitations associated with the use of the native enzyme have been designed. In this review, we will discuss the advances made using various superoxide dismutase mimetics that led to the proposal that superoxide (and/or the product of its interaction with nitric oxide, peroxynitrite) is an important mediator of inflammation, and to the conclusion that superoxide dismutase mimetics can be utilized as therapeutic agents in diseases of various etiologies. The importance of the selectivity of such compounds in pharmacological studies will be discussed. British Journal of Pharmacology (2003) 140 , 445–460. doi: 10.1038/sj.bjp.0705430
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To decrease the amount of damage caused by OH• radicals we need both to decrease their production and increase their removal to harmless substances.
“A corollary of such considerations is that to decrease the amount of damage caused by OH• (or any other) radicals we need both to decrease their production and increase their removal to harmless substances [2141]”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [2141]
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Proton-Coupled Electron Transfer
Weinberg, D. R., Gagliardi, C. J., Hull, J. F., Murphy, C. F., Kent, C. A., Westlake, B. C., Paul, A., Ess, D. H., McCafferty, D. G., & Meyer, T. J. (2012) · Chemical Reviews · doi:10.1021/cr200177j · Cited by 2,433 · see citing works
Proton-coupled electron transfer
Huynh, M. H. V., & Meyer, T. J. (2007) · Chemical Reviews · doi:10.1021/cr0500030 · Cited by 1,659 · see citing works
Stewart, F. A., Akleyev, A. V., Hauer-Jensen, M., Hendry, J. H., Kleiman, N. J., MacVittie, T. J., Aleman, B. M., Edgar, A. B., Mabuchi, K., Muirhead, C. R., et al. (2012) · Annals of the ICRP · doi:10.1016/j.icrp.2012.02.001 · Cited by 1,604 · see citing works
Nitric oxide, oxidants, and protein tyrosine nitration
Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,456 · see citing works
The role of oxidative stress during inflammatory processes
Lugrin, J., Rosenblatt‐Velin, N., Parapanov, R., & Liaudet, L. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0241 · Cited by 742 · see citing works
Reactive oxygen species and superoxide dismutases: Role in joint diseases
Afonso, V., Champy, R., Mitrovic, D. R., Collin, P., & Lomri, A. (2007) · Joint Bone Spine · doi:10.1016/j.jbspin.2007.02.002 · Cited by 640 · see citing works
S-glutathionylation uncouples eNOS and regulates its cellular and vascular function
Chen, C.-A., Wang, T.-Y., Varadharaj, S., Reyes, L. A., Hemann, C., Talukder, M. A. H., Chen, Y.-R., Druhan, L. J., & Zweier, J. L. (2010) · Nature · doi:10.1038/nature09599 · Cited by 594 · see citing works
Self-citationKell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Superoxide Dismutase Mimics: Chemistry, Pharmacology, and Therapeutic Potential
Batinic̈‐Haberle, I., Reboucas, J. S., & Spasojević, I. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2876 · Cited by 531 · see citing works
Classification of Metal-Based Drugs according to Their Mechanisms of Action
Boros, E., Dyson, P. J., & Gasser, G. (2019) · Chem · doi:10.1016/j.chempr.2019.10.013 · Cited by 451 · see citing works
Metal based drugs: from serendipity to design
Fricker, S. P. (2007) · Dalton Transactions · doi:10.1039/b705551j · Cited by 414 · see citing works
A Newly Identified Role for Superoxide in Inflammatory Pain
Wang, Z., Porreca, F., Cuzzocrea, S., Galen, K. P., Lightfoot, R. T., Masini, E., Muscoli, C., Mollace, V., Ndengele, M. M., Ischiropoulos, H., et al. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.103.064154 · Cited by 387 · see citing works
Self-citationModulation of Prostaglandin Biosynthesis by Nitric Oxide and Nitric Oxide Donors
Mollace, V., Muscoli, C., Masini, E., Cuzzocrea, S., & Salvemini, D. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.2.1 · Cited by 357 · see citing works
Self-citationHu, X., & Zhu, M. (2024) · Environmental Science & Technology · doi:10.1021/acs.est.3c10898 · Cited by 325 · see citing works
Singh, S. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00046 · Cited by 320 · see citing works
Egea, J., Fabregat, I., Frapart, Y., Ghezzi, P., Görlach, A., Kietzmann, T., Kubaichuk, K. I., Knaus, U. G., López, M. G., González, G. O., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.05.007 · Cited by 311 · see citing works
Roles of Reactive Oxygen and Nitrogen Species in Pain
Salvemini, D., Little, J., Doyle, T., & Neumann, W. (2011) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2011.01.026 · Cited by 300 · see citing works
Self-citationROLE of MITOCHONDRIA in TOXIC OXIDATIVE STRESS
Fariss, M. W. (2005) · Molecular Interventions · doi:10.1124/mi.5.2.7 · Cited by 288 · see citing works
Mitochondria-Targeted Cytoprotective Peptides for Ischemia–Reperfusion Injury
Szeto, H. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1892 · Cited by 269 · see citing works
Nanozymes in Point-of-Care Diagnosis: An Emerging Futuristic Approach for Biosensing
Das, B., Lou-Franco, J., Logan, N., Balasubramanian, P., Kim, M. I., & Cao, C. (2021) · Nano-Micro Letters · doi:10.1007/s40820-021-00717-0 · Cited by 266 · see citing works
Superoxide Dismutase Administration: A Review of Proposed Human Uses
Rosa, A. C., Corsi, D., Cavi, N., Bruni, N., & Dosio, F. (2021) · Molecules · doi:10.3390/molecules26071844 · Cited by 286 · see citing works
Effects of a potent antioxidant, platinum nanoparticle, on the lifespan of Caenorhabditis elegans
Kim, J., Takahashi, M. M., Shimizu, T., Shirasawa, T., Kajita, M., Kanayama, A., & Miyamoto, Y. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2008.02.011 · Cited by 235 · see citing works
Role of Superoxide as a Signaling Molecule
Buetler, T. M., Krauskopf, A., & Rüegg, U. T. (2004) · Physiology · doi:10.1152/nips.01514.2003 · Cited by 231 · see citing works
Shi, Y., Hu, X., Cheng, J., Zhang, X., Zhao, F., Shi, W., Ren, B., Yu, H., Yang, P., Li, Z., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09839-x · Cited by 223 · see citing works
Tumor Suppressor Function of the Plasma Glutathione Peroxidase Gpx3 in Colitis-Associated Carcinoma
Barrett, C. W., Wei, N., Chen, X., Smith, J. J., Washington, M. K., Hill, K. E., Coburn, L. A., Peek, R. M., Chaturvedi, R., Wilson, K. T., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-3150 · Cited by 196 · see citing works
Current state for the development of metallopharmaceutics and anti-diabetic metal complexes
Sakurai, H., Yoshikawa, Y., & Yasui, H. (2008) · Chemical Society Reviews · doi:10.1039/b710347f · Cited by 187 · see citing works
Manganese complexes displaying superoxide dismutase activity: A balance between different factors
Iranzo, O. (2011) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2011.02.001 · Cited by 176 · see citing works
Phosphorylation of Endothelial Nitric-oxide Synthase Regulates Superoxide Generation from the Enzyme
Chen, C., Druhan, L. J., Varadharaj, S., Chen, Y., & Zweier, J. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802269200 · Cited by 173 · see citing works
Self-citationSuperoxide, peroxynitrite and oxidative/nitrative stress in inflammation
Salvemini, D., Doyle, T., & Cuzzocrea, S. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340965 · Cited by 170 · see citing works
Self-citationO’Connor, M. J., Kellett, A., McCann, M., Rosair, G. M., McNamara, M. E., Howe, O. L., Creaven, B. S., McClean, S., Kia, A. F.-A., O′Shea, D., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201041d · Cited by 170 · see citing works
Buonanno, M., de Toledo, S. M., Pain, D., & Azzam, E. I. (2011) · Radiation Research · doi:10.1667/rr2461.1 · Cited by 159 · see citing works
Rush, J., Denniss, S., & Graham, D. A. (2005) · Canadian Journal of Applied Physiology · doi:10.1139/h05-133 · Cited by 165 · see citing works
Li, L., Guo, J., Wang, Y., Xiong, X., Tao, H., Li, J., Jia, Y., Hu, H., & Zhang, J. (2018) · Advanced Science · doi:10.1002/advs.201800781 · Cited by 150 · see citing works
Devereux, M. M., O′Shea, D., O’Connor, M. J., Grehan, H., Connor, G., McCann, M., Rosair, G. M., Lyng, F. M., Kellett, A., Walsh, M., et al. (2007) · Polyhedron · doi:10.1016/j.poly.2007.05.006 · Cited by 145 · see citing works
Muscoli, C., Cuzzocrea, S., Ndengele, M. M., Mollace, V., Porreca, F., Fabrizi, F., Esposito, E., Masini, E., Matuschak, G. M., & Salvemini, D. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32420 · Cited by 145 · see citing works
Self-citationCysteine proteases as targets for metal-based drugs
Fricker, S. P. (2010) · Metallomics · doi:10.1039/b924677k · Cited by 144 · see citing works
Batinic̈‐Haberle, I., Cuzzocrea, S., Reboucas, J. S., Ferrer‐Sueta, G., Mazzon, E., Paola, R. D., Radí, R., Spasojević, I., Benov, L., & Salvemini, D. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.042 · Cited by 140 · see citing works
Self-citationSuperoxide dismutase and neurological disorders
Chidambaram, S. B., Anand, N., Varma, S. R., Ramamurthy, S., Vichitra, C., Sharma, A., Mahalakshmi, A. M., & Essa, M. M. (2024) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2023.11.007 · Cited by 154 · see citing works
Azimi, I., Petersen, R. M., Thompson, E. W., Roberts‐Thomson, S. J., & Monteith, G. R. (2017) · Scientific Reports · doi:10.1038/s41598-017-15474-7 · Cited by 137 · see citing works
Hu, D., Cao, P., Thiels, E., Chu, C. T., Wu, G., Oury, T. D., & Klann, E. (2006) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2006.10.003 · Cited by 127 · see citing works
Singh, N., Geethika, M., Eswarappa, S. M., & Mugesh, G. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201800770 · Cited by 124 · see citing works
Mini-Review: Mitochondrial dysfunction and chemotherapy-induced neuropathic pain
Doyle, T. M., & Salvemini, D. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.136087 · Cited by 124 · see citing works
Self-citationGreaney, J. L., Saunders, E. F. H., Santhanam, L., & Alexander, L. M. (2019) · Circulation Research · doi:10.1161/circresaha.118.313764 · Cited by 122 · see citing works
Kopf, P. G., Huwe, J. K., & Walker, M. K. (2008) · Cardiovascular Toxicology · doi:10.1007/s12012-008-9027-x · Cited by 120 · see citing works
Manganese‐Based Nanozymes: Preparation, Catalytic Mechanisms, and Biomedical Applications
Tang, M., Zhang, Z., Sun, T., Li, B., & Wu, Z. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202201733 · Cited by 117 · see citing works
Michalska, P., & Leon, R. M. (2020) · Antioxidants · doi:10.3390/antiox9080740 · Cited by 112 · see citing works
Vitamin B12 protects against superoxide-induced cell injury in human aortic endothelial cells
Bahnson, E. M., Brasch, N. E., & Yun, J. S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.034 · Cited by 107 · see citing works
Bahnson, E. M., Yun, J. S., Birch, C. S., Williams, J. H. H., McCaddon, A., & Brasch, N. E. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904670x · Cited by 106 · see citing works
Dees, A., Zahl, A., Puchta, R., Hommes, N. J. R. V. E., Heinemann, F. W., & Ivanović‐Burmazović, I. (2007) · Inorganic Chemistry · doi:10.1021/ic061852o · Cited by 100 · see citing works
Musolino, V., Gliozzi, M., Scarano, F., Bosco, F., Scicchitano, M., Nucera, S., Carresi, C., Ruga, S., Zito, M. C., Maiuolo, J., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-59485-3 · Cited by 97 · see citing works
Self-citationA Review of Clinical Radioprotection and Chemoprotection for Oral Mucositis
Oronsky, B. T., Goyal, S., Kim, M. M., Cabrales, P., Lybeck, M., Caroen, S. Z., Oronsky, N. C., Burbano, E., Carter, C. A., & Oronsky, A. L. (2018) · Translational Oncology · doi:10.1016/j.tranon.2018.03.014 · Cited by 97 · see citing works
New insights into targeting mitochondria in ischemic injury
Jia, J., Jin, H., Nan, D., Yu, W., & Huang, Y. (2021) · APOPTOSIS · doi:10.1007/s10495-021-01661-5 · Cited by 94 · see citing works
Ndengele, M. M., Muscoli, C., Wang, Z. Q., Doyle, T. M., Matuschak, G. M., & Salvemini, D. (2005) · Shock · doi:10.1097/01.shk.0000144130.36771.d6 · Cited by 93 · see citing works
Self-citationNishio, N., Taniguchi, W., Sugimura, Y. K., Takiguchi, N., Yamanaka, M., Kiyoyuki, Y., Yamada, H., Miyazaki, N., Yoshida, M., & Nakatsuka, T. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.05.023 · Cited by 92 · see citing works
Liu, G.-F., Filipović, M. R., Heinemann, F. W., & Ivanović‐Burmazović, I. (2007) · Inorganic Chemistry · doi:10.1021/ic7012039 · Cited by 88 · see citing works
Murphy, C. K., Fey, E. G., Watkins, B. A., Wong, V., Rothstein, D., & Sonis, S. T. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-4669 · Cited by 85 · see citing works
Little, J. W., Doyle, T. M., & Salvemini, D. (2010) · Amino Acids · doi:10.1007/s00726-010-0633-0 · Cited by 83 · see citing works
Self-citationObligatory role for GPER in cardiovascular aging and disease
Meyer, M. R., Fredette, N. C., Daniel, C., Sharma, G., Amann, K., Arterburn, J. B., Barton, M., & Prossnitz, E. R. (2016) · Science Signaling · doi:10.1126/scisignal.aag0240 · Cited by 78 · see citing works
Superoxide Dismutase (SOD)-mimetic M40403 Is Protective in Cell and Fly Models of Paraquat Toxicity
Filograna, R., Godena, V. K., Sánchez-Martínez, Á., Ferrari, E., Casella, L., Beltramini, M., Bubacco, L., Whitworth, A. J., & Bisaglia, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.708057 · Cited by 76 · see citing works
Testosterone-Induced Effects on Lipids and Inflammation
Vodo, S., Bechi, N., Petroni, A., Muscoli, C., & Aloisi, A. M. (2013) · Mediators of Inflammation · doi:10.1155/2013/183041 · Cited by 75 · see citing works
Self-citationChen, C., Lin, C.-H., Druhan, L. J., Wang, T.-Y., Chen, Y.-R., & Zweier, J. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.240127 · Cited by 74 · see citing works
Self-citationTherapeutic Applications and Mechanisms of Superoxide Dismutase (SOD) in Different Pathogenesis
Anwar, S., Sarwar, T., Khan, A. A., & Rahmani, A. H. (2025) · Biomolecules · doi:10.3390/biom15081130 · Cited by 72 · see citing works
Cai, X., Chen, L., Li, L., Feng, M., Li, X., Zhang, K., Rong, Y., Hu, X., Zhang, M., Zhang, M., et al. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0128 · Cited by 72 · see citing works
The role of nitric oxide in prostaglandin biology; update
Kim, S. F. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.07.002 · Cited by 72 · see citing works
Massaad, C. A., Amin, S. K., Hu, L., Yuan, M., Klann, E., & Pautler, R. G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010561 · Cited by 71 · see citing works
Friedel, F. C., Lieb, D., & Ivanović‐Burmazović, I. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.12.008 · Cited by 70 · see citing works
Fernandes, A. S., Gaspar, J., Cabral, M. F., Caneiras, C. S. G., Guedes, R. C., Rueff, J., Castro, M., Costa, J., & Oliveira, N. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.01.013 · Cited by 67 · see citing works
Mitochondrial targeting as a novel therapy for stroke
Borlongan, C., Russo, E., Nguyen, H., Lippert, T., Tuazon, J. P., & Napoli, E. (2018) · Brain Circulation · doi:10.4103/bc.bc_14_18 · Cited by 67 · see citing works
Doyle, T. M., Bryant, L., Muscoli, C., Cuzzocrea, S., Esposito, E., Chen, Z., & Salvemini, D. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.07.013 · Cited by 64 · see citing works
Self-citationRadiation-induced reductions in neurogenesis are ameliorated in mice deficient in CuZnSOD or MnSOD
Fishman, K., Baure, J., Zou, Y., Huang, T., Andres‐Mach, M., Rola, R., Suarez, T., Acharya, M. M., Limoli, C. L., Lamborn, K. R., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.016 · Cited by 63 · see citing works
Manganese Salen Complexes with Acid–Base Catalytic Auxiliary: Functional Mimetics of Catalase
Noritake, Y., Umezawa, N., Kato, N., & Higuchi, T. (2013) · Inorganic Chemistry · doi:10.1021/ic302101c · Cited by 60 · see citing works
Raber, J., Villasana, L., Rosenberg, J. S., Zou, Y., Huang, T., & Fike, J. R. (2009) · Hippocampus · doi:10.1002/hipo.20724 · Cited by 59 · see citing works
Moreno, D. M., Daier, V., Palopoli, C. M., Tuchagues, J., & Signorella, S. (2010) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2009.12.016 · Cited by 58 · see citing works
Redox Systems Biology of Nutrition and Oxidative Stress
Dennis, K. K., Go, Y., & Jones, D. P. (2018) · Journal of Nutrition · doi:10.1093/jn/nxy306 · Cited by 60 · see citing works
Mayorov, D. N., Head, G. A., & Matteo, R. M. D. (2004) · Hypertension · doi:10.1161/01.hyp.0000131290.12255.04 · Cited by 57 · see citing works
Doyle, T. M., Bryant, L., Batinic-Haberle, I., Little, J. W., Cuzzocrea, S., Masini, E., Spasojević, I., & Salvemini, D. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.07.019 · Cited by 56 · see citing works
Self-citationSimple Biological Systems for Assessing the Activity of Superoxide Dismutase Mimics
Tovmasyan, A. G., Reboucas, J. S., & Benov, L. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5576 · Cited by 56 · see citing works
Jaulmes, A., Sansilvestri, P., Rolland-Valognes, G., Bernhardt, F., Gaertner, R., Lockhart, B. P., Cordi, A. A., Wierzbicki, M., Rupin, A., & Verbeuren, T. J. (2009) · Thrombosis Research · doi:10.1016/j.thromres.2009.05.018 · Cited by 55 · see citing works
Lu, J., Gong, N., Wang, Y., & Wang, Y. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01680.x · Cited by 54 · see citing works
Filipović, M. R., Koh, A. C. W., Arbault, S., Niketić, V., Debus, A., Schleicher, U., Bogdan, C., Guille‐Collignon, M., Lemaître, F., Amatore, C. A., et al. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200905936 · Cited by 54 · see citing works
Merenda, A., Gugliotta, M., Holloway, R., Levasseur, J. E., Alessandri, B., Sun, D., & Bullock, M. R. (2008) · Journal of Neurotrauma · doi:10.1089/neu.2007.0359 · Cited by 53 · see citing works
Sinha, A., Singh, A., Satchidanandam, V., & Natarajan, K. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.1.468 · Cited by 52 · see citing works
Kartha, S., Yan, L., Weisshaar, C. L., Ita, M. E., Shuvaev, V. V., Muzykantov, V. R., Tsourkas, A., Winkelstein, B. A., & Cheng, Z. (2017) · Advanced Healthcare Materials · doi:10.1002/adhm.201700500 · Cited by 52 · see citing works
Failli, P., Bani, D., Bencini, A., Cantore, M., Mannelli, L. D. C., Ghelardini, C., Giorgi, C., Innocenti, M., Rugi, F., Spepi, A., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901298x · Cited by 51 · see citing works
Sanches, L. J., Marinello, P. C., Panis, C., Fagundes, T. R., Morgado‐Díaz, J. A., de‐Freitas‐Junior, J. C. M., Cecchini, R., Cecchini, A. L., & Luiz, R. C. (2017) · Tumor Biology · doi:10.1177/1010428317695914 · Cited by 50 · see citing works
Endothelial Dysfunction and Extra-Articular Neurological Manifestations in Rheumatoid Arthritis
Maiuolo, J., Muscoli, C., Gliozzi, M., Musolino, V., Carresi, C., Scicchitano, M., Bosco, F., Macrì, R., Scarano, F., Ruga, S., et al. (2021) · Biomolecules · doi:10.3390/biom11010081 · Cited by 50 · see citing works
Self-citationShih, C., Chang, J.-H., Yang, S., Chou, T.-W., & Cheng, H.-H. (2007) · British Journal Of Nutrition · doi:10.1017/s0007114507781497 · Cited by 50 · see citing works
Chen, Y., Hou, M., Li, Y., Traverse, J. H., Ping, Z., Salvemini, D., Fukai, T., & Bache, R. J. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00851.2003 · Cited by 48 · see citing works
Self-citationCheung, C., McCartney, S. J., & Anseth, K. S. (2008) · Advanced Functional Materials · doi:10.1002/adfm.200800566 · Cited by 48 · see citing works
A superoxide dismutase mimic nanocomposite for amperometric sensing of superoxide anions
Dashtestani, F., Ghourchian, H., Eskandari, K., & Rafiee‐Pour, H. (2014) · Microchimica Acta · doi:10.1007/s00604-014-1424-1 · Cited by 46 · see citing works
Maroz, A., Kelso, G. F., Smith, R. A. J., Ware, D. C., & Anderson, R. F. (2008) · The Journal of Physical Chemistry A · doi:10.1021/jp800690u · Cited by 46 · see citing works
Clares, M. P., Serena, C., Blasco, S., Nebot, A., del Castillo, L., Soriano, C., Doménech‐Carbó, A., Sánchez-Sánchez, A. V., Soler-Calero, L., Mullor, J. L., et al. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.11.001 · Cited by 45 · see citing works
Lupidi, G., Marchetti, F., Masciocchi, N., Reger, D. L., Tabassum, S., Astolfi, P., Damiani, E., & Pettinari, C. (2010) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2010.03.013 · Cited by 44 · see citing works
Cuzzocrea, S., Genovese, T., Mazzon, E., Paola, R. D., Mui, C., Britti, D., & Salvemini, D. (2004) · Shock · doi:10.1097/01.shk.0000132490.79498.11 · Cited by 44 · see citing works
Self-citationApolipoprotein E Genotype-Dependent Paradoxical Short-Term Effects of 56Fe Irradiation on the Brain
Haley, G. E., Villasana, L., Dayger, C. A., Davis, M. J., & Raber, J. (2012) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2011.12.049 · Cited by 43 · see citing works
Reactive oxygen species: Advanced detection methods and coordination with nanozymes
Krishnendu, M. R., & Singh, S. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.161296 · Cited by 42 · see citing works
Role of Reactive Oxygen Species in Injury-Induced Insulin Resistance
Zhai, L., Ballinger, S. W., & Messina, J. L. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0224 · Cited by 42 · see citing works
Muscoli, C., Sacco, I., Alecce, W., Palma, E., Nisticò, R., Costa, N., Clementi, F., Rotiroti, D., Romeo, F., Salvemini, D., et al. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.068205 · Cited by 42 · see citing works
Self-citationRetractedOtašević, V., Korać, A., Vučetić, M., Macanovic, B., Garalejić, E., Ivanović‐Burmazović, I., Filipović, M. R., Buzadžić, B., Stančić, A., Janković, A., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4684 · Cited by 42 · see citing works
Peroxynitrite: a strategic linchpin of opioid analgesic tolerance
Salvemini, D., & Neumann, W. L. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.12.005 · Cited by 41 · see citing works
Self-citation
- Authors
- Muscoli, C., Cuzzocrea, S., Riley, D. P., Zweier, J. L., Thiemermann, C., Wang, Z., & Salvemini, D.
- Affiliations
- Magna Graecia University (IT)
- University of Messina (IT)
- The Ohio State University (US)
- William Harvey Research Institute (GB)
- Corresponding author
- Salvemini, Daniela
- Venue
- British Journal of Pharmacology
- Publisher
- Wiley
- Published
- 2003-10
- Volume
- 140
- Issue
- 3
- Pages
- 445-460
- ISSN
- 0007-1188 (ISSN-L)
- 1476-5381
- PMC
- PMC1574047
- OpenAlex
- W2095342832
- Cited by
- 271
- References
- 217
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 10 · 2023: 7 · 2022: 6 · 2021: 12 · 2020: 6 · 2019: 11 · 2018: 13 · 2017: 11 · 2016: 11 · 2015: 7 · 2014: 12 · 2013: 14 · 2012: 19
- FWCI
- 0.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- British Journal of Pharmacology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- superoxide dismutase mimetic, superoxide, peroxynitrite, nitric oxide, inflammation, anti-inflammatory therapy, enzyme selectivity, superoxide dismutase isoforms, reactive oxygen species
- MeSH terms
- Animals, Humans, Superoxide Dismutase, Drug Delivery Systems, Biomimetic Materials
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