{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:50:50Z","timestamp":1792785050616,"version":"4.5.0"},"reference-count":120,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,6,27]],"date-time":"2026-06-27T00:00:00Z","timestamp":1782518400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T00:00:00Z","timestamp":1790294400000},"content-version":"vor","delay-in-days":90,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"name":"Canadian Institutes of Health Research","award":["FDN-159916"],"award-info":[{"award-number":["FDN-159916"]}],"id":[{"id":"https:\/\/ror.org\/01gavpb45","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"DOI":"10.1038\/s41598-026-59950-5","type":"journal-article","created":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T05:58:22Z","timestamp":1782712702000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Clarifying the molecular mechanisms underlying the lethal in vitro cellular effects and mild organismal phenotype of SOD1 loss"],"prefix":"10.1038","volume":"16","author":[{"given":"Ying","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alycia","family":"No\u00eb","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Long","family":"Truong-Ong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Siegfried","family":"Hekimi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,6,27]]},"reference":[{"key":"59950_CR1","doi-asserted-by":"publisher","first-page":"585","DOI":"10.1016\/j.febslet.2011.10.048","volume":"586","author":"AF Miller","year":"2012","unstructured":"Miller, A. F. Superoxide dismutases: Ancient enzymes and new insights. FEBS Lett. 586, 585\u2013595. https:\/\/doi.org\/10.1016\/j.febslet.2011.10.048 (2012).","journal-title":"FEBS Lett."},{"key":"59950_CR2","doi-asserted-by":"publisher","first-page":"1915","DOI":"10.1083\/jcb.201708007","volume":"217","author":"Y Wang","year":"2018","unstructured":"Wang, Y., Branicky, R., Noe, A. & Hekimi, S. Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling. J. Cell Biol. 217, 1915\u20131928. https:\/\/doi.org\/10.1083\/jcb.201708007 (2018).","journal-title":"J. Cell Biol."},{"key":"59950_CR3","doi-asserted-by":"publisher","first-page":"38388","DOI":"10.1074\/jbc.M105395200","volume":"276","author":"A Okado-Matsumoto","year":"2001","unstructured":"Okado-Matsumoto, A. & Fridovich, I. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J. Biol. Chem. 276, 38388\u201338393. https:\/\/doi.org\/10.1074\/jbc.M105395200 (2001).","journal-title":"J. Biol. Chem."},{"key":"59950_CR4","doi-asserted-by":"publisher","first-page":"10405","DOI":"10.1073\/pnas.89.21.10405","volume":"89","author":"JD Crapo","year":"1992","unstructured":"Crapo, J. D., Oury, T., Rabouille, C., Slot, J. W. & Chang, L. Y. Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells. Proc. Natl. Acad. Sci. U.S.A. 89, 10405\u201310409 (1992).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"59950_CR5","doi-asserted-by":"publisher","first-page":"38084","DOI":"10.1074\/jbc.M105296200","volume":"276","author":"LA Sturtz","year":"2001","unstructured":"Sturtz, L. A., Diekert, K., Jensen, L. T., Lill, R. & Culotta, V. C. A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J. Biol. Chem. 276, 38084\u201338089. https:\/\/doi.org\/10.1074\/jbc.M105296200 (2001).","journal-title":"J. Biol. Chem."},{"key":"59950_CR6","doi-asserted-by":"publisher","first-page":"2169","DOI":"10.1083\/jcb.107.6.2169","volume":"107","author":"LY Chang","year":"1988","unstructured":"Chang, L. Y., Slot, J. W., Geuze, H. J. & Crapo, J. D. Molecular immunocytochemistry of the CuZn superoxide dismutase in rat hepatocytes. J. Cell Biol. 107, 2169\u20132179 (1988).","journal-title":"J. Cell Biol."},{"key":"59950_CR7","doi-asserted-by":"publisher","first-page":"mfag007","DOI":"10.1093\/mtomcs\/mfag007","volume":"18","author":"RL Peterson","year":"2026","unstructured":"Peterson, R. L. & Culotta, V. C. From hemocuprein to CSRP: The many faces of Cu\/Zn superoxide dismutase. Metallomics 18, mfag007. https:\/\/doi.org\/10.1093\/mtomcs\/mfag007 (2026).","journal-title":"Metallomics"},{"key":"59950_CR8","doi-asserted-by":"publisher","first-page":"236","DOI":"10.1016\/s0891-5849(03)00275-2","volume":"35","author":"CL Fattman","year":"2003","unstructured":"Fattman, C. L., Schaefer, L. M. & Oury, T. D. Extracellular superoxide dismutase in biology and medicine. Free Radic. Biol. Med. 35, 236\u2013256. https:\/\/doi.org\/10.1016\/s0891-5849(03)00275-2 (2003).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR9","doi-asserted-by":"publisher","first-page":"1583","DOI":"10.1089\/ars.2011.3999","volume":"15","author":"T Fukai","year":"2011","unstructured":"Fukai, T. & Ushio-Fukai, M. Superoxide dismutases: Role in redox signaling, vascular function, and diseases. Antioxid. Redox Signal. 15, 1583\u20131606. https:\/\/doi.org\/10.1089\/ars.2011.3999 (2011).","journal-title":"Antioxid. Redox Signal."},{"key":"59950_CR10","doi-asserted-by":"publisher","first-page":"954","DOI":"10.1073\/pnas.92.4.954","volume":"92","author":"CA Pardo","year":"1995","unstructured":"Pardo, C. A. et al. Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc. Natl. Acad. Sci. U.S.A. 92, 954\u2013958. https:\/\/doi.org\/10.1073\/pnas.92.4.954 (1995).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"59950_CR11","doi-asserted-by":"publisher","first-page":"1881","DOI":"10.1152\/physrev.00005.2022","volume":"102","author":"L Piacenza","year":"2022","unstructured":"Piacenza, L., Zeida, A., Trujillo, M. & Radi, R. The superoxide radical switch in the biology of nitric oxide and peroxynitrite. Physiol. Rev. 102, 1881\u20131906. https:\/\/doi.org\/10.1152\/physrev.00005.2022 (2022).","journal-title":"Physiol. Rev."},{"key":"59950_CR12","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1146\/annurev.micro.57.030502.090938","volume":"57","author":"JA Imlay","year":"2003","unstructured":"Imlay, J. A. Pathways of oxidative damage. Annu. Rev. Microbiol. 57, 395\u2013418. https:\/\/doi.org\/10.1146\/annurev.micro.57.030502.090938 (2003).","journal-title":"Annu. Rev. Microbiol."},{"key":"59950_CR13","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1007\/978-3-030-11488-6_1","volume":"1127","author":"MN Moller","year":"2019","unstructured":"Moller, M. N. et al. Diffusion and transport of reactive species across cell membranes. Adv. Exp. Med. Biol. 1127, 3\u201319. https:\/\/doi.org\/10.1007\/978-3-030-11488-6_1 (2019).","journal-title":"Adv. Exp. Med. Biol."},{"key":"59950_CR14","doi-asserted-by":"publisher","first-page":"1579","DOI":"10.1007\/s11357-020-00200-5","volume":"42","author":"YC Jang","year":"2020","unstructured":"Jang, Y. C. et al. Superoxide-mediated oxidative stress accelerates skeletal muscle atrophy by synchronous activation of proteolytic systems. Geroscience 42, 1579\u20131591. https:\/\/doi.org\/10.1007\/s11357-020-00200-5 (2020).","journal-title":"Geroscience"},{"key":"59950_CR15","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2023328119","author":"C Montllor-Albalate","year":"2022","unstructured":"Montllor-Albalate, C. et al. Sod1 integrates oxygen availability to redox regulate NADPH production and the thiol redoxome. Proc. Natl. Acad. Sci. U.S.A. https:\/\/doi.org\/10.1073\/pnas.2023328119 (2022).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"59950_CR16","doi-asserted-by":"publisher","first-page":"7147","DOI":"10.1073\/pnas.0709451105","volume":"105","author":"JC Juarez","year":"2008","unstructured":"Juarez, J. C. et al. Superoxide dismutase 1 (SOD1) is essential for H2O2-mediated oxidation and inactivation of phosphatases in growth factor signaling. Proc. Natl. Acad. Sci. U.S.A. 105, 7147\u20137152. https:\/\/doi.org\/10.1073\/pnas.0709451105 (2008).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"59950_CR17","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1016\/j.cell.2012.11.046","volume":"152","author":"AR Reddi","year":"2013","unstructured":"Reddi, A. R. & Culotta, V. C. SOD1 integrates signals from oxygen and glucose to repress respiration. Cell 152, 224\u2013235. https:\/\/doi.org\/10.1016\/j.cell.2012.11.046 (2013).","journal-title":"Cell"},{"key":"59950_CR18","doi-asserted-by":"publisher","first-page":"3446","DOI":"10.1038\/ncomms4446","volume":"5","author":"CK Tsang","year":"2014","unstructured":"Tsang, C. K., Liu, Y., Thomas, J., Zhang, Y. & Zheng, X. F. Superoxide dismutase 1 acts as a nuclear transcription factor to regulate oxidative stress resistance. Nat. Commun. 5, 3446. https:\/\/doi.org\/10.1038\/ncomms4446 (2014).","journal-title":"Nat. Commun."},{"key":"59950_CR19","doi-asserted-by":"publisher","DOI":"10.1016\/j.abb.2020.108701","volume":"697","author":"ECA Eleutherio","year":"2021","unstructured":"Eleutherio, E. C. A., Silva Magalhaes, R. S., de Araujo Brasil, A., Monteiro Neto, J. R. & de Holanda Paranhos, L. SOD1, more than just an antioxidant. Arch. Biochem. Biophys. 697, 108701. https:\/\/doi.org\/10.1016\/j.abb.2020.108701 (2021).","journal-title":"Arch. Biochem. Biophys."},{"key":"59950_CR20","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1152\/physrev.00010.2014","volume":"96","author":"XG Lei","year":"2016","unstructured":"Lei, X. G. et al. Paradoxical roles of antioxidant enzymes: Basic mechanisms and health implications. Physiol Rev 96, 307\u2013364. https:\/\/doi.org\/10.1152\/physrev.00010.2014 (2016).","journal-title":"Physiol Rev"},{"key":"59950_CR21","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2205044120","volume":"120","author":"CH Switzer","year":"2023","unstructured":"Switzer, C. H., Kasamatsu, S., Ihara, H. & Eaton, P. SOD1 is an essential H(2)S detoxifying enzyme. Proc. Natl. Acad. Sci. U.S.A. 120, e2205044120. https:\/\/doi.org\/10.1073\/pnas.2205044120 (2023).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"59950_CR22","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2018.11.022","volume":"21","author":"C Montllor-Albalate","year":"2019","unstructured":"Montllor-Albalate, C. et al. Extra-mitochondrial Cu\/Zn superoxide dismutase (Sod1) is dispensable for protection against oxidative stress but mediates peroxide signaling in Saccharomyces cerevisiae. Redox Biol. 21, 101064. https:\/\/doi.org\/10.1016\/j.redox.2018.11.022 (2019).","journal-title":"Redox Biol."},{"key":"59950_CR23","doi-asserted-by":"publisher","first-page":"7765","DOI":"10.1074\/jbc.273.13.7765","volume":"273","author":"YS Ho","year":"1998","unstructured":"Ho, Y. S. et al. Reduced fertility in female mice lacking copper-zinc superoxide dismutase. J. Biol. Chem. 273, 7765\u20137769. https:\/\/doi.org\/10.1074\/jbc.273.13.7765 (1998).","journal-title":"J. Biol. Chem."},{"key":"59950_CR24","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1038\/sj.onc.1208207","volume":"24","author":"S Elchuri","year":"2005","unstructured":"Elchuri, S. et al. CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life. Oncogene 24, 367\u2013380. https:\/\/doi.org\/10.1038\/sj.onc.1208207 (2005).","journal-title":"Oncogene"},{"key":"59950_CR25","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1038\/ng0596-43","volume":"13","author":"AG Reaume","year":"1996","unstructured":"Reaume, A. G. et al. Motor neurons in Cu\/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet. 13, 43\u201347. https:\/\/doi.org\/10.1038\/ng0596-43 (1996).","journal-title":"Nat. Genet."},{"key":"59950_CR26","doi-asserted-by":"publisher","first-page":"1993","DOI":"10.1016\/j.freeradbiomed.2006.01.036","volume":"40","author":"FL Muller","year":"2006","unstructured":"Muller, F. L. et al. Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy. Free Radic. Biol. Med. 40, 1993\u20132004. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2006.01.036 (2006).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR27","doi-asserted-by":"publisher","first-page":"254","DOI":"10.1016\/j.freeradbiomed.2015.03.021","volume":"84","author":"MV Ivannikov","year":"2015","unstructured":"Ivannikov, M. V. & Van Remmen, H. Sod1 gene ablation in adult mice leads to physiological changes at the neuromuscular junction similar to changes that occur in old wild-type mice. Free Radic. Biol. Med. 84, 254\u2013262. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2015.03.021 (2015).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR28","doi-asserted-by":"publisher","first-page":"1376","DOI":"10.1096\/fj.09-146308","volume":"24","author":"YC Jang","year":"2010","unstructured":"Jang, Y. C. et al. Increased superoxide in vivo accelerates age-associated muscle atrophy through mitochondrial dysfunction and neuromuscular junction degeneration. FASEB J. 24, 1376\u20131390. https:\/\/doi.org\/10.1096\/fj.09-146308 (2010).","journal-title":"FASEB J."},{"key":"59950_CR29","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1042\/BJ20061386","volume":"402","author":"Y Iuchi","year":"2007","unstructured":"Iuchi, Y. et al. Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production. Biochem. J. 402, 219\u2013227. https:\/\/doi.org\/10.1042\/BJ20061386 (2007).","journal-title":"Biochem. J."},{"key":"59950_CR30","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1530\/REP-13-0229","volume":"146","author":"M Garratt","year":"2013","unstructured":"Garratt, M., Bathgate, R., de Graaf, S. P. & Brooks, R. C. Copper-zinc superoxide dismutase deficiency impairs sperm motility and in vivo fertility. Reproduction 146, 297\u2013304. https:\/\/doi.org\/10.1530\/REP-13-0229 (2013).","journal-title":"Reproduction"},{"key":"59950_CR31","doi-asserted-by":"publisher","first-page":"391","DOI":"10.1089\/ars.2010.3302","volume":"14","author":"X Wang","year":"2011","unstructured":"Wang, X. et al. Knockouts of SOD1 and GPX1 exert different impacts on murine islet function and pancreatic integrity. Antioxid. Redox Signal. 14, 391\u2013401. https:\/\/doi.org\/10.1089\/ars.2010.3302 (2011).","journal-title":"Antioxid. Redox Signal."},{"key":"59950_CR32","doi-asserted-by":"publisher","DOI":"10.1155\/2014\/140165","volume":"2014","author":"K Watanabe","year":"2014","unstructured":"Watanabe, K. et al. Superoxide dismutase 1 loss disturbs intracellular redox signaling, resulting in global age-related pathological changes. Biomed. Res. Int. 2014, 140165. https:\/\/doi.org\/10.1155\/2014\/140165 (2014).","journal-title":"Biomed. Res. Int."},{"key":"59950_CR33","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.freeradbiomed.2018.06.032","volume":"132","author":"SS Deepa","year":"2019","unstructured":"Deepa, S. S. et al. Accelerated sarcopenia in Cu\/Zn superoxide dismutase knockout mice. Free Radic. Biol. Med. 132, 19\u201323. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2018.06.032 (2019).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR34","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1089\/ars.2017.7249","volume":"28","author":"GK Sakellariou","year":"2018","unstructured":"Sakellariou, G. K. et al. Comparison of whole body SOD1 knockout with muscle-specific SOD1 knockout mice reveals a role for nerve redox signaling in regulation of degenerative pathways in skeletal muscle. Antioxid. Redox Signal. 28, 275\u2013295. https:\/\/doi.org\/10.1089\/ars.2017.7249 (2018).","journal-title":"Antioxid. Redox Signal."},{"key":"59950_CR35","doi-asserted-by":"publisher","first-page":"6904","DOI":"10.1074\/jbc.M510764200","volume":"281","author":"ML Sentman","year":"2006","unstructured":"Sentman, M. L. et al. Phenotypes of mice lacking extracellular superoxide dismutase and copper- and zinc-containing superoxide dismutase. J. Biol. Chem. 281, 6904\u20136909. https:\/\/doi.org\/10.1074\/jbc.M510764200 (2006).","journal-title":"J. Biol. Chem."},{"key":"59950_CR36","doi-asserted-by":"publisher","first-page":"559","DOI":"10.1016\/j.freeradbiomed.2009.05.022","volume":"47","author":"D Yoshihara","year":"2009","unstructured":"Yoshihara, D. et al. Protective role of glutathione S-transferase A4 induced in copper\/zinc-superoxide dismutase knockout mice. Free Radic. Biol. Med. 47, 559\u2013567. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2009.05.022 (2009).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR37","doi-asserted-by":"publisher","DOI":"10.1111\/acel.13225","volume":"19","author":"S Bhaskaran","year":"2020","unstructured":"Bhaskaran, S. et al. Neuron-specific deletion of CuZnSOD leads to an advanced sarcopenic phenotype in older mice. Aging Cell 19, e13225. https:\/\/doi.org\/10.1111\/acel.13225 (2020).","journal-title":"Aging Cell"},{"key":"59950_CR38","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0026963","volume":"6","author":"MP Siegel","year":"2011","unstructured":"Siegel, M. P. et al. Reduced coupling of oxidative phosphorylation in vivo precedes electron transport chain defects due to mild oxidative stress in mice. PLoS ONE 6, e26963. https:\/\/doi.org\/10.1371\/journal.pone.0026963 (2011).","journal-title":"PLoS ONE"},{"key":"59950_CR39","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1016\/j.abb.2013.06.008","volume":"537","author":"S Tsunoda","year":"2013","unstructured":"Tsunoda, S., Kibe, N., Kurahashi, T. & Fujii, J. Differential responses of SOD1-deficient mouse embryonic fibroblasts to oxygen concentrations. Arch. Biochem. Biophys. 537, 5\u201311. https:\/\/doi.org\/10.1016\/j.abb.2013.06.008 (2013).","journal-title":"Arch. Biochem. Biophys."},{"key":"59950_CR40","doi-asserted-by":"publisher","first-page":"10998","DOI":"10.3390\/ijms140610998","volume":"14","author":"K Watanabe","year":"2013","unstructured":"Watanabe, K. et al. Sod1 loss induces intrinsic superoxide accumulation leading to p53-mediated growth arrest and apoptosis. Int. J. Mol. Sci. 14, 10998\u201311010. https:\/\/doi.org\/10.3390\/ijms140610998 (2013).","journal-title":"Int. J. Mol. Sci."},{"key":"59950_CR41","doi-asserted-by":"publisher","first-page":"424","DOI":"10.1006\/abbi.1997.0237","volume":"344","author":"TT Huang","year":"1997","unstructured":"Huang, T. T. et al. Superoxide-mediated cytotoxicity in superoxide dismutase-deficient fetal fibroblasts. Arch. Biochem. Biophys. 344, 424\u2013432. https:\/\/doi.org\/10.1006\/abbi.1997.0237 (1997).","journal-title":"Arch. Biochem. Biophys."},{"key":"59950_CR42","doi-asserted-by":"publisher","DOI":"10.4061\/2010\/795946","author":"E Inoue","year":"2010","unstructured":"Inoue, E. et al. SOD1 is essential for the viability of DT40 cells and nuclear SOD1 functions as a guardian of genomic DNA. J. Nucleic Acids https:\/\/doi.org\/10.4061\/2010\/795946 (2010).","journal-title":"J. Nucleic Acids"},{"key":"59950_CR43","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/s0891-5849(98)00198-1","volume":"26","author":"D Ross","year":"1999","unstructured":"Ross, D., Mendiratta, S., Qu, Z. C., Cobb, C. E. & May, J. M. Ascorbate 6-palmitate protects human erythrocytes from oxidative damage. Free Radic. Biol. Med. 26, 81\u201389. https:\/\/doi.org\/10.1016\/s0891-5849(98)00198-1 (1999).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR44","doi-asserted-by":"publisher","first-page":"433","DOI":"10.1089\/neu.1998.15.433","volume":"15","author":"RH Fabian","year":"1998","unstructured":"Fabian, R. H., Dewitt, D. S. & Kent, T. A. The 21-aminosteroid U-74389G reduces cerebral superoxide anion concentration following fluid percussion injury of the brain. J. Neurotrauma 15, 433\u2013440. https:\/\/doi.org\/10.1089\/neu.1998.15.433 (1998).","journal-title":"J. Neurotrauma"},{"key":"59950_CR45","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1046\/j.1365-2133.1999.02762.x","volume":"140","author":"E Camera","year":"1999","unstructured":"Camera, E., Cannistraci, C., Briganti, S., Colombo, D. & Picardo, M. Scavenging effects of terbinafine on free radicals in vitro. Br. J. Dermatol. 140, 640\u2013644. https:\/\/doi.org\/10.1046\/j.1365-2133.1999.02762.x (1999).","journal-title":"Br. J. Dermatol."},{"key":"59950_CR46","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/s0300-483x(02)00512-7","volume":"183","author":"A Higuchi","year":"2003","unstructured":"Higuchi, A., Yonemitsu, K., Koreeda, A. & Tsunenari, S. Inhibitory activity of epigallocatechin gallate (EGCg) in paraquat-induced microsomal lipid peroxidation\u2014A mechanism of protective effects of EGCg against paraquat toxicity. Toxicology 183, 143\u2013149. https:\/\/doi.org\/10.1016\/s0300-483x(02)00512-7 (2003).","journal-title":"Toxicology"},{"key":"59950_CR47","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/s0014-4835(02)00256-7","volume":"76","author":"JR Reddan","year":"2003","unstructured":"Reddan, J. R. et al. Propyl gallate is a superoxide dismutase mimic and protects cultured lens epithelial cells from H2O2 insult. Exp. Eye Res. 76, 49\u201359. https:\/\/doi.org\/10.1016\/s0014-4835(02)00256-7 (2003).","journal-title":"Exp. Eye Res."},{"key":"59950_CR48","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/0891-5849(91)90181-2","volume":"11","author":"G Sichel","year":"1991","unstructured":"Sichel, G., Corsaro, C., Scalia, M., Di Bilio, A. J. & Bonomo, R. P. In vitro scavenger activity of some flavonoids and melanins against O2\u2212\u00b7. Free Radic. Biol. Med. 11, 1\u20138. https:\/\/doi.org\/10.1016\/0891-5849(91)90181-2 (1991).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR49","doi-asserted-by":"publisher","first-page":"210","DOI":"10.1016\/s0005-2760(96)00122-1","volume":"1304","author":"Q Guo","year":"1996","unstructured":"Guo, Q., Zhao, B., Li, M., Shen, S. & Xin, W. Studies on protective mechanisms of four components of green tea polyphenols against lipid peroxidation in synaptosomes. Biochim. Biophys. Acta 1304, 210\u2013222. https:\/\/doi.org\/10.1016\/s0005-2760(96)00122-1 (1996).","journal-title":"Biochim. Biophys. Acta"},{"key":"59950_CR50","doi-asserted-by":"publisher","first-page":"374","DOI":"10.1038\/sj.bjp.0702796","volume":"128","author":"A Galal","year":"1999","unstructured":"Galal, A. & Souich, P. 21-aminosteroids prevent the down-regulation of hepatic cytochrome P450 induced by hypoxia and inflammation in conscious rabbits. Br. J. Pharmacol. 128, 374\u2013379. https:\/\/doi.org\/10.1038\/sj.bjp.0702796 (1999).","journal-title":"Br. J. Pharmacol."},{"key":"59950_CR51","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1046\/j.1439-0507.2002.00756.x","volume":"45","author":"CS Sander","year":"2002","unstructured":"Sander, C. S., Hipler, U. C., Wollina, U. & Elsner, P. Inhibitory effect of terbinafine on reactive oxygen species (ROS) generation by Candida albicans. Mycoses 45, 152\u2013155. https:\/\/doi.org\/10.1046\/j.1439-0507.2002.00756.x (2002).","journal-title":"Mycoses"},{"key":"59950_CR52","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1016\/j.foodchem.2015.11.118","volume":"199","author":"S Chan","year":"2016","unstructured":"Chan, S. et al. Metal chelation, radical scavenging and inhibition of Abeta(4)(2) fibrillation by food constituents in relation to Alzheimer\u2019s disease. Food Chem. 199, 185\u2013194. https:\/\/doi.org\/10.1016\/j.foodchem.2015.11.118 (2016).","journal-title":"Food Chem."},{"key":"59950_CR53","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2020.101680","volume":"36","author":"Y Wang","year":"2020","unstructured":"Wang, Y. & Hekimi, S. Micellization of coenzyme Q by the fungicide caspofungin allows for safe intravenous administration to reach extreme supraphysiological concentrations. Redox Biol. 36, 101680. https:\/\/doi.org\/10.1016\/j.redox.2020.101680 (2020).","journal-title":"Redox Biol."},{"key":"59950_CR54","first-page":"10","volume":"8","author":"RA Sansone","year":"2011","unstructured":"Sansone, R. A. & Sansone, L. A. Getting a knack for NAC: N-acetyl-cysteine. Innov. Clin. Neurosci. 8, 10\u201314 (2011).","journal-title":"Innov. Clin. Neurosci."},{"issue":"Pt 1","key":"59950_CR55","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1042\/bj3150021","volume":"315","author":"EA Slee","year":"1996","unstructured":"Slee, E. A. et al. Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32. Biochem. J. 315(Pt 1), 21\u201324. https:\/\/doi.org\/10.1042\/bj3150021 (1996).","journal-title":"Biochem. J."},{"key":"59950_CR56","doi-asserted-by":"publisher","first-page":"32608","DOI":"10.1074\/jbc.273.49.32608","volume":"273","author":"M Garcia-Calvo","year":"1998","unstructured":"Garcia-Calvo, M. et al. Inhibition of human caspases by peptide-based and macromolecular inhibitors. J. Biol. Chem. 273, 32608\u201332613. https:\/\/doi.org\/10.1074\/jbc.273.49.32608 (1998).","journal-title":"J. Biol. Chem."},{"key":"59950_CR57","doi-asserted-by":"publisher","first-page":"195","DOI":"10.3109\/10715769309145868","volume":"18","author":"RE Huie","year":"1993","unstructured":"Huie, R. E. & Padmaja, S. The reaction of no with superoxide. Free Radic. Res. Commun. 18, 195\u2013199. https:\/\/doi.org\/10.3109\/10715769309145868 (1993).","journal-title":"Free Radic. Res. Commun."},{"key":"59950_CR58","doi-asserted-by":"publisher","first-page":"3854","DOI":"10.1021\/cr4005296","volume":"114","author":"Y Sheng","year":"2014","unstructured":"Sheng, Y. et al. Superoxide dismutases and superoxide reductases. Chem. Rev. 114, 3854\u20133918. https:\/\/doi.org\/10.1021\/cr4005296 (2014).","journal-title":"Chem. Rev."},{"key":"59950_CR59","doi-asserted-by":"publisher","first-page":"618","DOI":"10.1016\/j.redox.2017.09.009","volume":"14","author":"S Bartesaghi","year":"2018","unstructured":"Bartesaghi, S. & Radi, R. Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration. Redox Biol. 14, 618\u2013625. https:\/\/doi.org\/10.1016\/j.redox.2017.09.009 (2018).","journal-title":"Redox Biol."},{"key":"59950_CR60","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1111\/j.1474-9726.2011.00709.x","volume":"10","author":"GK Sakellariou","year":"2011","unstructured":"Sakellariou, G. K. et al. Role of superoxide-nitric oxide interactions in the accelerated age-related loss of muscle mass in mice lacking Cu,Zn superoxide dismutase. Aging Cell 10, 749\u2013760. https:\/\/doi.org\/10.1111\/j.1474-9726.2011.00709.x (2011).","journal-title":"Aging Cell"},{"key":"59950_CR61","doi-asserted-by":"publisher","first-page":"2002","DOI":"10.1056\/NEJM199312303292706","volume":"329","author":"S Moncada","year":"1993","unstructured":"Moncada, S. & Higgs, A. The l-arginine-nitric oxide pathway. N. Engl. J. Med. 329, 2002\u20132012. https:\/\/doi.org\/10.1056\/NEJM199312303292706 (1993).","journal-title":"N. Engl. J. Med."},{"key":"59950_CR62","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1007\/BF02615072","volume":"13","author":"J Feng","year":"1977","unstructured":"Feng, J., Melcher, A. H., Brunette, D. M. & Moe, H. K. Determination of l-ascorbic acid levels in culture medium: Concentrations in commercial media and maintenance of levels under conditions of organ culture. In Vitro 13, 91\u201399. https:\/\/doi.org\/10.1007\/BF02615072 (1977).","journal-title":"In Vitro"},{"key":"59950_CR63","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1290\/1071-2690(2001)037<0026:MOAAAC>2.0.CO;2","volume":"37","author":"T Chepda","year":"2001","unstructured":"Chepda, T., Cadau, M., Girin, P., Frey, J. & Chamson, A. Monitoring of ascorbate at a constant rate in cell culture: Effect on cell growth. In Vitro Cell. Dev. Biol. Anim. 37, 26\u201330. https:\/\/doi.org\/10.1290\/1071-2690(2001)037%3c0026:MOAAAC%3e2.0.CO;2 (2001).","journal-title":"In Vitro Cell. Dev. Biol. Anim."},{"key":"59950_CR64","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1002\/jcp.1041380103","volume":"138","author":"R Hata","year":"1989","unstructured":"Hata, R. & Senoo, H. l-ascorbic acid 2-phosphate stimulates collagen accumulation, cell proliferation, and formation of a three-dimensional tissuelike substance by skin fibroblasts. J. Cell. Physiol. 138, 8\u201316. https:\/\/doi.org\/10.1002\/jcp.1041380103 (1989).","journal-title":"J. Cell. Physiol."},{"key":"59950_CR65","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1289\/ehp.845537","volume":"55","author":"JS Bus","year":"1984","unstructured":"Bus, J. S. & Gibson, J. E. Paraquat: Model for oxidant-initiated toxicity. Environ. Health Perspect. 55, 37\u201346. https:\/\/doi.org\/10.1289\/ehp.845537 (1984).","journal-title":"Environ. Health Perspect."},{"key":"59950_CR66","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1016\/s0300-483x(02)00382-7","volume":"180","author":"ZE Suntres","year":"2002","unstructured":"Suntres, Z. E. Role of antioxidants in paraquat toxicity. Toxicology 180, 65\u201377. https:\/\/doi.org\/10.1016\/s0300-483x(02)00382-7 (2002).","journal-title":"Toxicology"},{"key":"59950_CR67","doi-asserted-by":"publisher","first-page":"1101","DOI":"10.1007\/s11357-020-00189-x","volume":"42","author":"K Sataranatarajan","year":"2020","unstructured":"Sataranatarajan, K. et al. Molecular changes in transcription and metabolic pathways underlying muscle atrophy in the CuZnSOD null mouse model of sarcopenia. Geroscience 42, 1101\u20131118. https:\/\/doi.org\/10.1007\/s11357-020-00189-x (2020).","journal-title":"Geroscience"},{"key":"59950_CR68","doi-asserted-by":"publisher","first-page":"4768","DOI":"10.1093\/hmg\/ddt330","volume":"22","author":"Y Wang","year":"2013","unstructured":"Wang, Y. & Hekimi, S. Mitochondrial respiration without ubiquinone biosynthesis. Hum. Mol. Genet. 22, 4768\u20134783. https:\/\/doi.org\/10.1093\/hmg\/ddt330 (2013).","journal-title":"Hum. Mol. Genet."},{"key":"59950_CR69","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1042\/bj1470493","volume":"147","author":"DD Tyler","year":"1975","unstructured":"Tyler, D. D. Polarographic assay and intracellular distribution of superoxide dismutase in rat liver. Biochem. J. 147, 493\u2013504. https:\/\/doi.org\/10.1042\/bj1470493 (1975).","journal-title":"Biochem. J."},{"key":"59950_CR70","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1042\/bj2220649","volume":"222","author":"SL Marklund","year":"1984","unstructured":"Marklund, S. L. Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species. Biochem. J. 222, 649\u2013655. https:\/\/doi.org\/10.1042\/bj2220649 (1984).","journal-title":"Biochem. J."},{"key":"59950_CR71","doi-asserted-by":"publisher","first-page":"6393","DOI":"10.1038\/ncomms7393","volume":"6","author":"Y Wang","year":"2015","unstructured":"Wang, Y., Oxer, D. & Hekimi, S. Mitochondrial function and lifespan of mice with controlled ubiquinone biosynthesis. Nat. Commun. 6, 6393. https:\/\/doi.org\/10.1038\/ncomms7393 (2015).","journal-title":"Nat. Commun."},{"key":"59950_CR72","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1006\/dbio.2002.0597","volume":"244","author":"S Hayashi","year":"2002","unstructured":"Hayashi, S. & McMahon, A. P. Efficient recombination in diverse tissues by a tamoxifen-inducible form of Cre: A tool for temporally regulated gene activation\/inactivation in the mouse. Dev. Biol. 244, 305\u2013318. https:\/\/doi.org\/10.1006\/dbio.2002.0597 (2002).","journal-title":"Dev. Biol."},{"key":"59950_CR73","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1210\/endocr\/bqad104","volume":"164","author":"J Svensson","year":"2023","unstructured":"Svensson, J. et al. Bone-derived IGF-I regulates radial bone growth in adult male mice. Endocrinology 164, 104. https:\/\/doi.org\/10.1210\/endocr\/bqad104 (2023).","journal-title":"Endocrinology"},{"key":"59950_CR74","doi-asserted-by":"publisher","first-page":"R1400","DOI":"10.1152\/ajpregu.00093.2011","volume":"301","author":"LM Larkin","year":"2011","unstructured":"Larkin, L. M. et al. Skeletal muscle weakness due to deficiency of CuZn-superoxide dismutase is associated with loss of functional innervation. Am. J. Physiol. Regul. Integr. Comp. Physiol. 301, R1400-1407. https:\/\/doi.org\/10.1152\/ajpregu.00093.2011 (2011).","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"59950_CR75","doi-asserted-by":"publisher","first-page":"9345970","DOI":"10.1155\/2016\/9345970","volume":"2016","author":"H Nagahisa","year":"2016","unstructured":"Nagahisa, H., Okabe, K., Iuchi, Y., Fujii, J. & Miyata, H. Characteristics of skeletal muscle fibers of SOD1 knockout mice. Oxid. Med. Cell. Longev. 2016, 9345970. https:\/\/doi.org\/10.1155\/2016\/9345970 (2016).","journal-title":"Oxid. Med. Cell. Longev."},{"key":"59950_CR76","doi-asserted-by":"publisher","first-page":"1212","DOI":"10.1080\/09168451.2014.915728","volume":"78","author":"S Shibuya","year":"2014","unstructured":"Shibuya, S. et al. Collagen peptide and vitamin C additively attenuate age-related skin atrophy in Sod1-deficient mice. Biosci. Biotechnol. Biochem. 78, 1212\u20131220. https:\/\/doi.org\/10.1080\/09168451.2014.915728 (2014).","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"59950_CR77","doi-asserted-by":"publisher","first-page":"116","DOI":"10.1016\/j.freeradbiomed.2018.03.033","volume":"122","author":"N Smirnoff","year":"2018","unstructured":"Smirnoff, N. Ascorbic acid metabolism and functions: A comparison of plants and mammals. Free Radic. Biol. Med. 122, 116\u2013129. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2018.03.033 (2018).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR78","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1016\/0006-291x(75)90710-x","volume":"63","author":"M Nishikimi","year":"1975","unstructured":"Nishikimi, M. Oxidation of ascorbic acid with superoxide anion generated by the xanthine\u2013xanthine oxidase system. Biochem. Biophys. Res. Commun. 63, 463\u2013468. https:\/\/doi.org\/10.1016\/0006-291x(75)90710-x (1975).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"59950_CR79","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1016\/0304-4165(92)90054-x","volume":"1115","author":"N Gotoh","year":"1992","unstructured":"Gotoh, N. & Niki, E. Rates of interactions of superoxide with vitamin E, vitamin C and related compounds as measured by chemiluminescence. Biochim. Biophys. Acta 1115, 201\u2013207. https:\/\/doi.org\/10.1016\/0304-4165(92)90054-x (1992).","journal-title":"Biochim. Biophys. Acta"},{"key":"59950_CR80","doi-asserted-by":"publisher","first-page":"916","DOI":"10.1161\/01.res.83.9.916","volume":"83","author":"TS Jackson","year":"1998","unstructured":"Jackson, T. S., Xu, A., Vita, J. A. & Keaney, J. F. Jr. Ascorbate prevents the interaction of superoxide and nitric oxide only at very high physiological concentrations. Circ. Res. 83, 916\u2013922. https:\/\/doi.org\/10.1161\/01.res.83.9.916 (1998).","journal-title":"Circ. Res."},{"key":"59950_CR81","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0032957","volume":"7","author":"SM Kuo","year":"2012","unstructured":"Kuo, S. M., Burl, L. R. & Hu, Z. Cellular phenotype-dependent and -independent effects of vitamin C on the renewal and gene expression of mouse embryonic fibroblasts. PLoS ONE 7, e32957. https:\/\/doi.org\/10.1371\/journal.pone.0032957 (2012).","journal-title":"PLoS ONE"},{"key":"59950_CR82","doi-asserted-by":"publisher","first-page":"793","DOI":"10.1016\/s0891-5849(97)00062-2","volume":"23","author":"G Banhegyi","year":"1997","unstructured":"Banhegyi, G., Braun, L., Csala, M., Puskas, F. & Mandl, J. Ascorbate metabolism and its regulation in animals. Free Radic. Biol. Med. 23, 793\u2013803. https:\/\/doi.org\/10.1016\/s0891-5849(97)00062-2 (1997).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR83","doi-asserted-by":"publisher","first-page":"544","DOI":"10.1038\/sj.emboj.7600954","volume":"25","author":"SL Clarke","year":"2006","unstructured":"Clarke, S. L. et al. Iron-responsive degradation of iron-regulatory protein 1 does not require the Fe-S cluster. EMBO J. 25, 544\u2013553. https:\/\/doi.org\/10.1038\/sj.emboj.7600954 (2006).","journal-title":"EMBO J."},{"key":"59950_CR84","doi-asserted-by":"publisher","first-page":"4207","DOI":"10.1074\/jbc.M411055200","volume":"280","author":"RR Starzynski","year":"2005","unstructured":"Starzynski, R. R. et al. Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism. J. Biol. Chem. 280, 4207\u20134212. https:\/\/doi.org\/10.1074\/jbc.M411055200 (2005).","journal-title":"J. Biol. Chem."},{"key":"59950_CR85","doi-asserted-by":"publisher","first-page":"5118","DOI":"10.1038\/s41598-018-23175-y","volume":"8","author":"H Li","year":"2018","unstructured":"Li, H. et al. Iron regulatory protein deficiency compromises mitochondrial function in murine embryonic fibroblasts. Sci. Rep. 8, 5118. https:\/\/doi.org\/10.1038\/s41598-018-23175-y (2018).","journal-title":"Sci. Rep."},{"key":"59950_CR86","doi-asserted-by":"publisher","first-page":"7452","DOI":"10.1074\/jbc.M510603200","volume":"281","author":"ZQ Chen","year":"2006","unstructured":"Chen, Z. Q. et al. The essential vertebrate ABCE1 protein interacts with eukaryotic initiation factors. J. Biol. Chem. 281, 7452\u20137457. https:\/\/doi.org\/10.1074\/jbc.M510603200 (2006).","journal-title":"J. Biol. Chem."},{"key":"59950_CR87","doi-asserted-by":"publisher","first-page":"3582","DOI":"10.1091\/mbc.E12-05-0413","volume":"23","author":"A Alhebshi","year":"2012","unstructured":"Alhebshi, A., Sideri, T. C., Holland, S. L. & Avery, S. V. The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species. Mol. Biol. Cell 23, 3582\u20133590. https:\/\/doi.org\/10.1091\/mbc.E12-05-0413 (2012).","journal-title":"Mol. Biol. Cell"},{"key":"59950_CR88","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1007\/s13238-015-0134-8","volume":"6","author":"L Liu","year":"2015","unstructured":"Liu, L. & Huang, M. Essential role of the iron-sulfur cluster binding domain of the primase regulatory subunit Pri2 in DNA replication initiation. Protein Cell 6, 194\u2013210. https:\/\/doi.org\/10.1007\/s13238-015-0134-8 (2015).","journal-title":"Protein Cell"},{"key":"59950_CR89","doi-asserted-by":"publisher","first-page":"6384","DOI":"10.1073\/pnas.91.14.6384","volume":"91","author":"CM Troy","year":"1994","unstructured":"Troy, C. M. & Shelanski, M. L. Down-regulation of copper\/zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells. Proc. Natl. Acad. Sci. U.S.A. 91, 6384\u20136387. https:\/\/doi.org\/10.1073\/pnas.91.14.6384 (1994).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"59950_CR90","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1523\/JNEUROSCI.16-01-00253.1996","volume":"16","author":"CM Troy","year":"1996","unstructured":"Troy, C. M., Derossi, D., Prochiantz, A., Greene, L. A. & Shelanski, M. L. Downregulation of Cu\/Zn superoxide dismutase leads to cell death via the nitric oxide-peroxynitrite pathway. J. Neurosci. 16, 253\u2013261. https:\/\/doi.org\/10.1523\/JNEUROSCI.16-01-00253.1996 (1996).","journal-title":"J. Neurosci."},{"key":"59950_CR91","doi-asserted-by":"publisher","first-page":"785","DOI":"10.1016\/0891-5849(95)00081-8","volume":"19","author":"G Czapski","year":"1995","unstructured":"Czapski, G. & Goldstein, S. The role of the reactions of \u00b7NO with superoxide and oxygen in biological systems: A kinetic approach. Free Radic. Biol. Med. 19, 785\u2013794. https:\/\/doi.org\/10.1016\/0891-5849(95)00081-8 (1995).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR92","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1096\/fasebj.12.10.773","volume":"12","author":"U Forstermann","year":"1998","unstructured":"Forstermann, U., Boissel, J. P. & Kleinert, H. Expressional control of the \u201cconstitutive\u201d isoforms of nitric oxide synthase (NOS I and NOS III). FASEB J. 12, 773\u2013790 (1998).","journal-title":"FASEB J."},{"key":"59950_CR93","doi-asserted-by":"publisher","first-page":"6740","DOI":"10.1523\/JNEUROSCI.19-16-06740.1999","volume":"19","author":"YM Kim","year":"1999","unstructured":"Kim, Y. M. et al. Nitric oxide protects PC12 cells from serum deprivation-induced apoptosis by cGMP-dependent inhibition of caspase signaling. J. Neurosci. 19, 6740\u20136747. https:\/\/doi.org\/10.1523\/JNEUROSCI.19-16-06740.1999 (1999).","journal-title":"J. Neurosci."},{"key":"59950_CR94","doi-asserted-by":"publisher","first-page":"2387","DOI":"10.1096\/fj.06-6366fje","volume":"20","author":"M Kapoor","year":"2006","unstructured":"Kapoor, M., Kojima, F., Qian, M., Yang, L. & Crofford, L. J. Shunting of prostanoid biosynthesis in microsomal prostaglandin E synthase-1 null embryo fibroblasts: Regulatory effects on inducible nitric oxide synthase expression and nitrite synthesis. FASEB J. 20, 2387\u20132389. https:\/\/doi.org\/10.1096\/fj.06-6366fje (2006).","journal-title":"FASEB J."},{"key":"59950_CR95","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1006\/abbi.2001.2738","volume":"399","author":"Y Kira","year":"2002","unstructured":"Kira, Y., Sato, E. F. & Inoue, M. Association of Cu,Zn-type superoxide dismutase with mitochondria and peroxisomes. Arch. Biochem. Biophys. 399, 96\u2013102. https:\/\/doi.org\/10.1006\/abbi.2001.2738 (2002).","journal-title":"Arch. Biochem. Biophys."},{"key":"59950_CR96","doi-asserted-by":"publisher","first-page":"1711","DOI":"10.1111\/j.1600-0854.2009.00966.x","volume":"10","author":"M Islinger","year":"2009","unstructured":"Islinger, M., Li, K. W., Seitz, J., Volkl, A. & Luers, G. H. Hitchhiking of Cu\/Zn superoxide dismutase to peroxisomes\u2013evidence for a natural piggyback import mechanism in mammals. Traffic 10, 1711\u20131721. https:\/\/doi.org\/10.1111\/j.1600-0854.2009.00966.x (2009).","journal-title":"Traffic"},{"key":"59950_CR97","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1093\/brain\/awq314","volume":"134","author":"LR Fischer","year":"2011","unstructured":"Fischer, L. R. et al. SOD1 targeted to the mitochondrial intermembrane space prevents motor neuropathy in the Sod1 knockout mouse. Brain 134, 196\u2013209. https:\/\/doi.org\/10.1093\/brain\/awq314 (2011).","journal-title":"Brain"},{"key":"59950_CR98","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.molcel.2013.08.038","volume":"52","author":"K Homma","year":"2013","unstructured":"Homma, K. et al. SOD1 as a molecular switch for initiating the homeostatic ER stress response under zinc deficiency. Mol. Cell 52, 75\u201386. https:\/\/doi.org\/10.1016\/j.molcel.2013.08.038 (2013).","journal-title":"Mol. Cell"},{"key":"59950_CR99","doi-asserted-by":"publisher","first-page":"44798","DOI":"10.1074\/jbc.M104708200","volume":"276","author":"JP Wei","year":"2001","unstructured":"Wei, J. P., Srinivasan, C., Han, H., Valentine, J. S. & Gralla, E. B. Evidence for a novel role of copper-zinc superoxide dismutase in zinc metabolism. J. Biol. Chem. 276, 44798\u201344803. https:\/\/doi.org\/10.1074\/jbc.M104708200 (2001).","journal-title":"J. Biol. Chem."},{"key":"59950_CR100","doi-asserted-by":"publisher","first-page":"29991","DOI":"10.1074\/jbc.270.50.29991","volume":"270","author":"VC Culotta","year":"1995","unstructured":"Culotta, V. C., Joh, H. D., Lin, S. J., Slekar, K. H. & Strain, J. A physiological role for Saccharomyces cerevisiae copper\/zinc superoxide dismutase in copper buffering. J. Biol. Chem. 270, 29991\u201329997. https:\/\/doi.org\/10.1074\/jbc.270.50.29991 (1995).","journal-title":"J. Biol. Chem."},{"key":"59950_CR101","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1523\/JNEUROSCI.1233-11.2012","volume":"32","author":"J Magrane","year":"2012","unstructured":"Magrane, J., Sahawneh, M. A., Przedborski, S., Estevez, A. G. & Manfredi, G. Mitochondrial dynamics and bioenergetic dysfunction is associated with synaptic alterations in mutant SOD1 motor neurons. J. Neurosci. 32, 229\u2013242. https:\/\/doi.org\/10.1523\/JNEUROSCI.1233-11.2012 (2012).","journal-title":"J. Neurosci."},{"key":"59950_CR102","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.00354-17","volume":"37","author":"CJ Banks","year":"2017","unstructured":"Banks, C. J. et al. Acylation of superoxide dismutase 1 (SOD1) at K122 governs SOD1-mediated inhibition of mitochondrial respiration. Mol. Cell. Biol. 37, e00354. https:\/\/doi.org\/10.1128\/MCB.00354-17 (2017).","journal-title":"Mol. Cell. Biol."},{"key":"59950_CR103","doi-asserted-by":"publisher","first-page":"3123","DOI":"10.3390\/cells11193123","volume":"11","author":"R Alva","year":"2022","unstructured":"Alva, R., Gardner, G. L., Liang, P. & Stuart, J. A. Supraphysiological oxygen levels in mammalian cell culture: Current state and future perspectives. Cells 11, 3123. https:\/\/doi.org\/10.3390\/cells11193123 (2022).","journal-title":"Cells"},{"key":"59950_CR104","doi-asserted-by":"publisher","first-page":"4180","DOI":"10.1523\/JNEUROSCI.17-11-04180.1997","volume":"17","author":"T Kondo","year":"1997","unstructured":"Kondo, T. et al. Reduction of CuZn-superoxide dismutase activity exacerbates neuronal cell injury and edema formation after transient focal cerebral ischemia. J. Neurosci. 17, 4180\u20134189. https:\/\/doi.org\/10.1523\/JNEUROSCI.17-11-04180.1997 (1997).","journal-title":"J. Neurosci."},{"key":"59950_CR105","doi-asserted-by":"publisher","first-page":"1962","DOI":"10.1161\/01.str.30.9.1962","volume":"30","author":"M Kawase","year":"1999","unstructured":"Kawase, M. et al. Exacerbation of delayed cell injury after transient global ischemia in mutant mice with CuZn superoxide dismutase deficiency. Stroke 30, 1962\u20131968. https:\/\/doi.org\/10.1161\/01.str.30.9.1962 (1999).","journal-title":"Stroke"},{"key":"59950_CR106","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1152\/physiolgenomics.00239.2007","volume":"34","author":"ES Han","year":"2008","unstructured":"Han, E. S. et al. The in vivo gene expression signature of oxidative stress. Physiol. Genom. 34, 112\u2013126. https:\/\/doi.org\/10.1152\/physiolgenomics.00239.2007 (2008).","journal-title":"Physiol. Genom."},{"key":"59950_CR107","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1007\/s11010-010-0449-y","volume":"341","author":"Y Iuchi","year":"2010","unstructured":"Iuchi, Y. et al. Spontaneous skin damage and delayed wound healing in SOD1-deficient mice. Mol. Cell. Biochem. 341, 181\u2013194. https:\/\/doi.org\/10.1007\/s11010-010-0449-y (2010).","journal-title":"Mol. Cell. Biochem."},{"key":"59950_CR108","doi-asserted-by":"publisher","first-page":"140","DOI":"10.1016\/j.redox.2015.04.005","volume":"5","author":"K Sataranatarajan","year":"2015","unstructured":"Sataranatarajan, K. et al. Neuron specific reduction in CuZnSOD is not sufficient to initiate a full sarcopenia phenotype. Redox Biol. 5, 140\u2013148. https:\/\/doi.org\/10.1016\/j.redox.2015.04.005 (2015).","journal-title":"Redox Biol."},{"key":"59950_CR109","doi-asserted-by":"publisher","first-page":"2259","DOI":"10.1038\/s41467-021-22480-x","volume":"12","author":"X Wang","year":"2021","unstructured":"Wang, X. et al. SOD1 regulates ribosome biogenesis in KRAS mutant non-small cell lung cancer. Nat. Commun. 12, 2259. https:\/\/doi.org\/10.1038\/s41467-021-22480-x (2021).","journal-title":"Nat. Commun."},{"key":"59950_CR110","doi-asserted-by":"publisher","first-page":"6187","DOI":"10.3390\/molecules27196187","volume":"27","author":"J Fujii","year":"2022","unstructured":"Fujii, J., Osaki, T. & Bo, T. Ascorbate Is a primary antioxidant in mammals. Molecules 27, 6187. https:\/\/doi.org\/10.3390\/molecules27196187 (2022).","journal-title":"Molecules"},{"key":"59950_CR111","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1016\/j.freeradbiomed.2020.10.023","volume":"162","author":"T Homma","year":"2021","unstructured":"Homma, T. et al. Defective biosynthesis of ascorbic acid in Sod1-deficient mice results in lethal damage to lung tissue. Free Radic. Biol. Med. 162, 255\u2013265. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2020.10.023 (2021).","journal-title":"Free Radic. Biol. Med."},{"key":"59950_CR112","doi-asserted-by":"publisher","first-page":"fcad017","DOI":"10.1093\/braincomms\/fcad017","volume":"5","author":"JH Park","year":"2023","unstructured":"Park, J. H. et al. The motor system is exceptionally vulnerable to absence of the ubiquitously expressed superoxide dismutase-1. Brain Commun. 5, fcad017. https:\/\/doi.org\/10.1093\/braincomms\/fcad017 (2023).","journal-title":"Brain Commun."},{"key":"59950_CR113","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1056\/NEJMc1905039","volume":"381","author":"PM Andersen","year":"2019","unstructured":"Andersen, P. M. et al. Phenotype in an infant with SOD1 homozygous truncating mutation. N. Engl. J. Med. 381, 486\u2013488. https:\/\/doi.org\/10.1056\/NEJMc1905039 (2019).","journal-title":"N. Engl. J. Med."},{"key":"59950_CR114","doi-asserted-by":"publisher","first-page":"2230","DOI":"10.1093\/brain\/awz182","volume":"142","author":"JH Park","year":"2019","unstructured":"Park, J. H. et al. SOD1 deficiency: A novel syndrome distinct from amyotrophic lateral sclerosis. Brain 142, 2230\u20132237. https:\/\/doi.org\/10.1093\/brain\/awz182 (2019).","journal-title":"Brain"},{"key":"59950_CR115","doi-asserted-by":"publisher","first-page":"872","DOI":"10.1093\/brain\/awab416","volume":"145","author":"S Ezer","year":"2022","unstructured":"Ezer, S. et al. Infantile SOD1 deficiency syndrome caused by a homozygous SOD1 variant with absence of enzyme activity. Brain 145, 872\u2013878. https:\/\/doi.org\/10.1093\/brain\/awab416 (2022).","journal-title":"Brain"},{"key":"59950_CR116","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1186\/s13023-021-01993-0","volume":"16","author":"PVS de Souza","year":"2021","unstructured":"de Souza, P. V. S. et al. Progressive spastic tetraplegia and axial hypotonia (STAHP) due to SOD1 deficiency: Is it really a new entity?. Orphanet J. Rare Dis. 16, 360. https:\/\/doi.org\/10.1186\/s13023-021-01993-0 (2021).","journal-title":"Orphanet J. Rare Dis."},{"key":"59950_CR117","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1080\/21678421.2023.2189925","volume":"24","author":"A Cakar","year":"2023","unstructured":"Cakar, A. et al. A novel homozygous loss-of-function variant in SOD1 causing progressive spastic tetraplegia and axial hypotonia. Amyotroph Lateral Scler Frontotemporal Degener 24, 535\u2013538. https:\/\/doi.org\/10.1080\/21678421.2023.2189925 (2023).","journal-title":"Amyotroph Lateral Scler Frontotemporal Degener"},{"key":"59950_CR118","doi-asserted-by":"publisher","first-page":"580","DOI":"10.1007\/s11033-024-09513-6","volume":"51","author":"M Dogan","year":"2024","unstructured":"Dogan, M. et al. Discovery of a novel homozygous SOD1 truncating variant bolsters infantile SOD1 deficiency syndrome. Mol. Biol. Rep. 51, 580. https:\/\/doi.org\/10.1007\/s11033-024-09513-6 (2024).","journal-title":"Mol. Biol. Rep."},{"key":"59950_CR119","doi-asserted-by":"publisher","DOI":"10.1002\/ajmg.a.63949","volume":"197","author":"RCT Boutin","year":"2025","unstructured":"Boutin, R. C. T. et al. Immune dysregulation in a child with SOD1-related neurological disease. Am. J. Med. Genet. A 197, e63949. https:\/\/doi.org\/10.1002\/ajmg.a.63949 (2025).","journal-title":"Am. J. Med. Genet. A"},{"key":"59950_CR120","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1038\/s41420-021-00591-0","volume":"7","author":"Y Wang","year":"2021","unstructured":"Wang, Y. & Hekimi, S. Minimal mitochondrial respiration is required to prevent cell death by inhibition of mTOR signaling in CoQ-deficient cells. Cell Death Discov. 7, 201. https:\/\/doi.org\/10.1038\/s41420-021-00591-0 (2021).","journal-title":"Cell Death Discov."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-59950-5","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-59950-5.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-59950-5.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T22:33:42Z","timestamp":1790289222000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-59950-5"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,27]]},"references-count":120,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["59950"],"URL":"https:\/\/doi.org\/10.1038\/s41598-026-59950-5","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,27]]},"assertion":[{"value":"25 March 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"24 June 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 June 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Declarations"}}],"article-number":"29766"}}