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Sci."},{"issue":"1","key":"10.1016\/j.bbrc.2026.154290_bib61","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1146\/annurev.pa.30.040190.003131","article-title":"Glutathione: toxicological implications","volume":"30","author":"Reed","year":"1990","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"issue":"11","key":"10.1016\/j.bbrc.2026.154290_bib62","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1016\/j.bbagen.2008.01.011","article-title":"Redox compartmentalization in eukaryotic cells","volume":"1780","author":"Go","year":"2008","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"issue":"5","key":"10.1016\/j.bbrc.2026.154290_bib63","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1016\/S0891-5849(00)00161-1","article-title":"Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene","volume":"28","author":"Esposito","year":"2000","journal-title":"Free Radic. Biol. 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Chem."},{"issue":"46","key":"10.1016\/j.bbrc.2026.154290_bib72","doi-asserted-by":"crossref","first-page":"47939","DOI":"10.1074\/jbc.M408011200","article-title":"Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant DEFENSE","volume":"279","author":"Beer","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.bbrc.2026.154290_bib73","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/abbi.1995.1261","article-title":"Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation","volume":"319","author":"Thomas","year":"1995","journal-title":"Arch. Biochem. 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Chem."},{"issue":"12","key":"10.1016\/j.bbrc.2026.154290_bib82","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1089\/ars.2016.6795","article-title":"Nuclear factor (erythroid-derived 2)-like 2 and thioredoxin-1 in atherosclerosis and ischemia\/reperfusion injury in the heart","volume":"26","author":"Jakobs","year":"2017","journal-title":"Antioxid. Redox Signaling"},{"issue":"3","key":"10.1016\/j.bbrc.2026.154290_bib83","doi-asserted-by":"crossref","first-page":"1108","DOI":"10.2353\/ajpath.2007.060960","article-title":"Endothelial-specific expression of mitochondrial thioredoxin improves endothelial cell function and reduces atherosclerotic lesions","volume":"170","author":"Zhang","year":"2007","journal-title":"Am. J. Pathol."},{"issue":"2\u20133","key":"10.1016\/j.bbrc.2026.154290_bib84","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1046\/j.1432-0436.2000.660209.x","article-title":"Atmospheric oxygen accelerates the induction of a post-mitotic phenotype in human dermal fibroblasts: the key protective role of glutathione","volume":"66","author":"Alaluf","year":"2000","journal-title":"Differentiation"},{"issue":"1","key":"10.1016\/j.bbrc.2026.154290_bib85","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/0925-4439(95)00007-Q","article-title":"Mitochondrial changes associated with glutathione deficiency","volume":"1271","author":"Meister","year":"1995","journal-title":"Biochim. Biophys. Acta, Mol. 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Nutr."},{"issue":"1","key":"10.1016\/j.bbrc.2026.154290_bib88","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0047-6374(85)90047-8","article-title":"Age-related changes in the redox status of rat muscle cels and their role in enzyme-aging","volume":"29","author":"Noy","year":"1985","journal-title":"Mech. Ageing Dev."},{"issue":"2\u20133","key":"10.1016\/j.bbrc.2026.154290_bib89","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/0165-2478(95)00213-O","article-title":"Induction of ADF\/TRX by oxidative stress in keratinocytes and lymphoid cells","volume":"44","author":"Sachi","year":"1995","journal-title":"Immunol. Lett."},{"issue":"30","key":"10.1016\/j.bbrc.2026.154290_bib90","doi-asserted-by":"crossref","first-page":"15506","DOI":"10.1016\/S0021-9258(19)37617-3","article-title":"Cloning and expression of a cDNA for human thioredoxin","volume":"263","author":"Wollman","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2026.154290_bib91","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1385\/MN:29:3:229","article-title":"Thioredoxin as a neurotrophic cofactor and an important regulator of neuroprotection","volume":"29","author":"Masutani","year":"2004","journal-title":"Mol. Neurobiol."},{"issue":"5","key":"10.1016\/j.bbrc.2026.154290_bib92","doi-asserted-by":"crossref","first-page":"2936","DOI":"10.1074\/jbc.272.5.2936","article-title":"Cloning and expression of a novel mammalian thioredoxin","volume":"272","author":"Spyrou","year":"1997","journal-title":"J. Biol. Chem."},{"issue":"7","key":"10.1016\/j.bbrc.2026.154290_bib93","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1093\/emboj\/18.7.1905","article-title":"Molecular mechanisms of transcription activation by HLF and HIF1\u03b1 in response to hypoxia: their stabilization and redox signal-induced interaction with CBP\/p300","volume":"18","author":"Ema","year":"1999","journal-title":"EMBO J."},{"issue":"1","key":"10.1016\/j.bbrc.2026.154290_bib94","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/0014-4886(90)90050-3","article-title":"Sciatic nerve regeneration across gaps within silicone chambers: long-term effects of NGF and consideration of axonal branching","volume":"110","author":"Hollowell","year":"1990","journal-title":"Exp. 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