{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,15]],"date-time":"2026-08-15T14:16:25Z","timestamp":1786803385899,"version":"build-2736575974"},"reference-count":52,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2022,12,23]],"date-time":"2022-12-23T00:00:00Z","timestamp":1671753600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31670767"],"award-info":[{"award-number":["31670767"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["DUT20LK36"],"award-info":[{"award-number":["DUT20LK36"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["ZJKF2004"],"award-info":[{"award-number":["ZJKF2004"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"publisher","award":["31670767"],"award-info":[{"award-number":["31670767"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"publisher","award":["DUT20LK36"],"award-info":[{"award-number":["DUT20LK36"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"publisher","award":["ZJKF2004"],"award-info":[{"award-number":["ZJKF2004"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Liaoning Key Laboratory of Chemical Additive Synthesis and Separation","award":["31670767"],"award-info":[{"award-number":["31670767"]}]},{"name":"Liaoning Key Laboratory of Chemical Additive Synthesis and Separation","award":["DUT20LK36"],"award-info":[{"award-number":["DUT20LK36"]}]},{"name":"Liaoning Key Laboratory of Chemical Additive Synthesis and Separation","award":["ZJKF2004"],"award-info":[{"award-number":["ZJKF2004"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Macrophages secrete a variety of pro-inflammatory cytokines in response to pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs) but abnormal release of cytokines unfortunately promotes cytokine storms. Dimethyl fumarate (DMF), an FDA-approved drug for multiple sclerosis (MS) treatment, has been found as an effective therapeutic agent for resolution. In this study, the anti-inflammatory effect of DMF was found to correlate to selenoprotein thioredoxin reductase 1 (TXNRD1). DMF irreversibly modified the Sec498 residue and C-terminal catalytic cysteine residues of TXNRD1 in a time- and dose-dependent manner. In LPS-stimulated RAW 264.7 cells, cellular TXNRD activity was increased through up-regulation of the protein level and DMF inhibited TXNRD activity and the nitric oxide (NO) production of RAW 264.7 cells. Meanwhile, the inhibition of TXNRD1 by DMF would contribute to the redox regulation of inflammation and promote the nuclear factor erythroid 2-related factor 2 (NRF2) activation. Notably, inhibition of cellular TXNRD1 by auranofin or TRi-1 showed anti-inflammatory effect in RAW 264.7 cells. This finding demonstrated that targeting TXNRD1 is a potential mechanism of using immunometabolites for dousing inflammation in response to pathogens and highlights the potential of TXNRD1 inhibitors in immune regulation.<\/jats:p>","DOI":"10.3390\/molecules28010107","type":"journal-article","created":{"date-parts":[[2022,12,23]],"date-time":"2022-12-23T03:55:21Z","timestamp":1671767721000},"page":"107","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Anti-Inflammatory Effect of Dimethyl Fumarate Associates with the Inhibition of Thioredoxin Reductase 1 in RAW 264.7 Cells"],"prefix":"10.3390","volume":"28","author":[{"given":"Rui","family":"Yang","sequence":"first","affiliation":[{"name":"School of Life and Pharmaceutical Sciences (LPS), Panjin Institute of Industrial Technology (PIIT), Liaoning Key Laboratory of Chemical Additive Synthesis and Separation, Dalian University of Technology, Panjin 124221, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shibo","family":"Sun","sequence":"additional","affiliation":[{"name":"School of Life and Pharmaceutical Sciences (LPS), Panjin Institute of Industrial Technology (PIIT), Liaoning Key Laboratory of Chemical Additive Synthesis and Separation, Dalian University of Technology, Panjin 124221, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yining","family":"Guo","sequence":"additional","affiliation":[{"name":"School of Life and Pharmaceutical Sciences (LPS), Panjin Institute of Industrial Technology (PIIT), Liaoning Key Laboratory of Chemical Additive Synthesis and Separation, Dalian University of Technology, Panjin 124221, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yao","family":"Meng","sequence":"additional","affiliation":[{"name":"School of Life and Pharmaceutical Sciences (LPS), Panjin Institute of Industrial Technology (PIIT), Liaoning Key Laboratory of Chemical Additive Synthesis and Separation, Dalian University of Technology, Panjin 124221, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haowen","family":"Liu","sequence":"additional","affiliation":[{"name":"School of Life and Pharmaceutical Sciences (LPS), Panjin Institute of Industrial Technology (PIIT), Liaoning Key Laboratory of Chemical Additive Synthesis and Separation, Dalian University of Technology, Panjin 124221, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meiyun","family":"Shi","sequence":"additional","affiliation":[{"name":"School of Life and Pharmaceutical Sciences (LPS), Panjin Institute of Industrial Technology (PIIT), Liaoning Key Laboratory of Chemical Additive Synthesis and Separation, Dalian University of Technology, Panjin 124221, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7617-8081","authenticated-orcid":false,"given":"Shui","family":"Guan","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Fine Chemicals, Dalian R&D Center for Stem Cell and Tissue Engineering, School of Chemical Engineering, Dalian University of Technology, Dalian 116023, China"},{"name":"Research & Educational Center for the Control Engineering of Translational Precision Medicine, School of Biomedical Engineering, Dalian University of Technology, Dalian 116024, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1289-5943","authenticated-orcid":false,"given":"Jianqiang","family":"Xu","sequence":"additional","affiliation":[{"name":"School of Life and Pharmaceutical Sciences (LPS), Panjin Institute of Industrial Technology (PIIT), Liaoning Key Laboratory of Chemical Additive Synthesis and Separation, Dalian University of Technology, Panjin 124221, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,12,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.freeradbiomed.2017.12.029","article-title":"The A to Z of modulated cell patterning by mammalian thioredoxin reductases","volume":"115","author":"Dagnell","year":"2018","journal-title":"Free Radic Biol. Med."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Zhang, J., Li, X., Zhao, Z., Cai, W., and Fang, J. (2022). Thioredoxin signaling pathways in cancer. Antioxid Redox Signal.","DOI":"10.1089\/ars.2022.0074"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1111\/bph.14479","article-title":"Thioredoxin-related protein of 14 kDa as a modulator of redox signalling pathways","volume":"176","author":"Espinosa","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1146\/annurev-pharmtox-052220-102509","article-title":"Thioredoxin Reductase Inhibition for Cancer Therapy","volume":"62","author":"Gencheva","year":"2021","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"6964","DOI":"10.1073\/pnas.1317320111","article-title":"Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase","volume":"111","author":"Pader","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1089\/ars.2015.6378","article-title":"TrxR1 as a potent regulator of the Nrf2-Keap1 response system","volume":"23","author":"Cebula","year":"2015","journal-title":"Antioxid Redox Signal."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.redox.2017.03.013","article-title":"Time- and cell-resolved dynamics of redox-sensitive Nrf2, HIF and NF-kappaB activities in 3D spheroids enriched for cancer stem cells","volume":"12","author":"Kipp","year":"2017","journal-title":"Redox Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1146\/annurev.immunol.021908.132532","article-title":"Alternative activation of macrophages: An immunologic functional perspective","volume":"27","author":"Martinez","year":"2009","journal-title":"Annu. Rev. Immunol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"dev156018","DOI":"10.1242\/dev.156018","article-title":"Toll and Toll-like receptor signalling in development","volume":"145","author":"Anthoney","year":"2018","journal-title":"Development"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1038\/s41577-020-00478-8","article-title":"Redox regulation of immunometabolism","volume":"21","author":"Muri","year":"2021","journal-title":"Nat. Rev. Immunol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1038\/s41589-019-0323-5","article-title":"S-glycosylation-based cysteine profiling reveals regulation of glycolysis by itaconate","volume":"15","author":"Qin","year":"2019","journal-title":"Nat. Chem. Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/s41577-019-0128-5","article-title":"Itaconate: The poster child of metabolic reprogramming in macrophage function","volume":"19","author":"Artyomov","year":"2019","journal-title":"Nat. Rev. Immunol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"53627","DOI":"10.7554\/eLife.53627","article-title":"Thioredoxin-1 distinctly promotes NF-kappaB target DNA binding and NLRP3 inflammasome activation independently of Txnip","volume":"9","author":"Muri","year":"2020","journal-title":"Elife"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1851","DOI":"10.1038\/s41467-018-04274-w","article-title":"The thioredoxin-1 system is essential for fueling DNA synthesis during T-cell metabolic reprogramming and proliferation","volume":"9","author":"Muri","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.freeradbiomed.2019.03.018","article-title":"Differential induction of nuclear factor-like 2 signature genes with toll-like receptor stimulation","volume":"135","author":"Ingram","year":"2019","journal-title":"Free Radic Biol. Med."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"100410","DOI":"10.1016\/j.jbc.2021.100410","article-title":"Selenium-dependent metabolic reprogramming during inflammation and resolution","volume":"296","author":"Korwar","year":"2021","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1177\/2040622316653307","article-title":"Dimethyl fumarate in multiple sclerosis: Latest developments, evidence and place in therapy","volume":"7","author":"Linker","year":"2016","journal-title":"Ther Adv. Chronic Dis."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1182\/blood-2016-01-694117","article-title":"Dimethyl fumarate restores apoptosis sensitivity and inhibits tumor growth and metastasis in CTCL by targeting NF-kappaB","volume":"128","author":"Nicolay","year":"2016","journal-title":"Blood"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1126\/science.aan4665","article-title":"Dimethyl fumarate targets GAPDH and aerobic glycolysis to modulate immunity","volume":"360","author":"Kornberg","year":"2018","journal-title":"Science"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1182\/blood.2020009404","article-title":"Dimethyl fumarate induces ferroptosis and impairs NF-kappaB\/STAT3 signaling in DLBCL","volume":"138","author":"Schmitt","year":"2021","journal-title":"Blood"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"43168","DOI":"10.1038\/srep43168","article-title":"Targeting Thioredoxin-1 by dimethyl fumarate induces ripoptosome-mediated cell death","volume":"7","author":"Schroeder","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"101647","DOI":"10.1016\/j.redox.2020.101647","article-title":"Electrophilic Nrf2 activators and itaconate inhibit inflammation at low dose and promote IL-1beta production and inflammatory apoptosis at high dose","volume":"36","author":"Muri","year":"2020","journal-title":"Redox Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"102351","DOI":"10.1016\/j.redox.2022.102351","article-title":"Mecheliolide elicits ROS-mediated ERS driven immunogenic cell death in hepatocellular carcinoma","volume":"54","author":"Xu","year":"2022","journal-title":"Redox Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"5518","DOI":"10.1039\/D1CS00933H","article-title":"Recent development of gold(I) and gold(III) complexes as therapeutic agents for cancer diseases","volume":"51","author":"Lu","year":"2022","journal-title":"Chem. Soc. Rev."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.freeradbiomed.2022.05.007","article-title":"Targeting thioredoxin reductase by micheliolide contributes to radiosensitizing and inducing apoptosis of HeLa cells","volume":"186","author":"Zhang","year":"2022","journal-title":"Free Radic Biol. Med."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1146\/annurev-cancerbio-030518-055844","article-title":"The Hallmarks of Ferroptosis","volume":"3","author":"Dixon","year":"2019","journal-title":"Annu. Rev. Cancer Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"143691","DOI":"10.1172\/JCI143691","article-title":"HIF-2alpha activation potentiates oxidative cell death in colorectal cancers by increasing cellular iron","volume":"131","author":"Singhal","year":"2021","journal-title":"J. Clin. Invest."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1146\/annurev-pharmtox-052220-104025","article-title":"Targeting NRF2 and Its Downstream Processes: Opportunities and Challenges","volume":"62","author":"Torrente","year":"2022","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"3593","DOI":"10.1002\/asia.201801136","article-title":"Small Molecules to Target the Selenoprotein Thioredoxin Reductase","volume":"13","author":"Zhang","year":"2018","journal-title":"Chem. Asian J."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1002\/med.21507","article-title":"Small molecule inhibitors of mammalian thioredoxin reductase as potential anticancer agents: An update","volume":"39","author":"Zhang","year":"2019","journal-title":"Med. Res. Rev."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.freeradbiomed.2016.02.013","article-title":"Details in the catalytic mechanism of mammalian thioredoxin reductase 1 revealed using point mutations and juglone-coupled enzyme activities","volume":"94","author":"Xu","year":"2016","journal-title":"Free Radic Biol. Med."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"112546","DOI":"10.1016\/j.biopha.2021.112546","article-title":"Plumbagin reduction by thioredoxin reductase 1 possesses synergy effects with GLUT1 inhibitor on KEAP1-mutant NSCLC cells","volume":"146","author":"Sun","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1016\/j.freeradbiomed.2006.12.021","article-title":"Inhibition of thioredoxin reductase by auranofin induces apoptosis in cisplatin-resistant human ovarian cancer cells","volume":"42","author":"Marzano","year":"2007","journal-title":"Free Radic Biol. Med."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Anestal, K., Prast-Nielsen, S., Cenas, N., and Arn\u00e9r, E.S.J. (2008). Cell death by SecTRAPs: Thioredoxin reductase as a prooxidant killer of cells. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0001846"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"21708","DOI":"10.1074\/jbc.M110.117259","article-title":"The selenium-independent inherent pro-oxidant NADPH oxidase activity of mammalian thioredoxin reductase and its selenium-dependent direct peroxidase activities","volume":"285","author":"Cheng","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.freeradbiomed.2021.06.023","article-title":"Menadione inhibits thioredoxin reductase 1 via arylation at the Sec(498) residue and enhances both NADPH oxidation and superoxide production in Sec(498) to Cys(498) substitution","volume":"172","author":"Sun","year":"2021","journal-title":"Free Radic Biol. Med."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.freeradbiomed.2021.12.314","article-title":"Thioredoxin reductase 1 inhibitor shikonin promotes cell necroptosis via SecTRAPs generation and oxygen-coupled redox cycling","volume":"180","author":"Zhang","year":"2022","journal-title":"Free Radic Biol. Med."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1016\/j.freeradbiomed.2009.09.016","article-title":"High levels of thioredoxin reductase 1 modulate drug-specific cytotoxic efficacy","volume":"47","author":"Eriksson","year":"2009","journal-title":"Free Radic Biol. Med."},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Yang, Y., Sun, S., Xu, W., Zhang, Y., Yang, R., Ma, K., Zhang, J., and Xu, J. (2022). Piperlongumine Inhibits Thioredoxin Reductase 1 by Targeting Selenocysteine Residues and Sensitizes Cancer Cells to Erastin. Antioxidants, 11.","DOI":"10.3390\/antiox11040710"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.freeradbiomed.2013.07.036","article-title":"The thioredoxin antioxidant system","volume":"66","author":"Lu","year":"2014","journal-title":"Free Radic Biol. Med."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"38210","DOI":"10.1074\/jbc.M112.392225","article-title":"Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose","volume":"287","author":"Du","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/j.bbagen.2009.01.014","article-title":"Focus on mammalian thioredoxin reductases--important selenoproteins with versatile functions","volume":"1790","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"e1616","DOI":"10.1038\/cddis.2014.574","article-title":"The conserved Trp114 residue of thioredoxin reductase 1 has a redox sensor-like function triggering oligomerization and crosslinking upon oxidative stress related to cell death","volume":"6","author":"Xu","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.freeradbiomed.2021.10.020","article-title":"Thioredoxin reductase-1 levels are associated with NRF2 pathway activation and tumor recurrence in non-small cell lung cancer","volume":"177","author":"Delgobo","year":"2021","journal-title":"Free Radic Biol. Med."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"106347","DOI":"10.1016\/j.compbiomed.2022.106347","article-title":"Omics-based identification of an NRF2-related auranofin resistance signature in cancer: Insights into drug repurposing","volume":"152","author":"Falchetti","year":"2022","journal-title":"Comput. Biol. Med."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.ccell.2018.03.022","article-title":"NRF2 and the Hallmarks of Cancer","volume":"34","author":"Chapman","year":"2018","journal-title":"Cancer Cell"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3691","DOI":"10.1016\/j.molcel.2021.08.018","article-title":"Redox metabolism: ROS as specific molecular regulators of cell signaling and function","volume":"81","author":"Lennicke","year":"2021","journal-title":"Mol. Cell"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"9800","DOI":"10.1093\/nar\/gkt764","article-title":"Wobble decoding by the Escherichia coli selenocysteine insertion machinery","volume":"41","author":"Xu","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.procbio.2020.11.019","article-title":"Efficient purification of selenoprotein thioredoxin reductase 1 by using chelating reagents to protect the affinity resins and rescue the enzyme activities","volume":"101","author":"Sun","year":"2021","journal-title":"Process. Biochem."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Sun, S., Zhang, Y., Xu, W., Zhang, Y., Yang, R., Guo, J., Guan, S., Ma, Q., Ma, K., and Xu, J. (2021). Chlorophyllin Inhibits Mammalian Thioredoxin Reductase 1 and Triggers Cancer Cell Death. Antioxidants, 10.","DOI":"10.3390\/antiox10111733"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Wang, H., Sun, S., Ren, Y., Yang, R., Guo, J., Zong, Y., Zhang, Q., Zhao, J., Zhang, W., and Xu, W. (2022). Selenite Ameliorates Cadmium-induced Cytotoxicity Through Downregulation of ROS Levels and Upregulation of Selenoprotein Thioredoxin Reductase 1 in SH-SY5Y Cells. Biol. Trace Elem. Res.","DOI":"10.1007\/s12011-022-03117-6"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/j.bcp.2011.12.028","article-title":"Pyrroloquinoline quinone modulates the kinetic parameters of the mammalian selenoprotein thioredoxin reductase 1 and is an inhibitor of glutathione reductase","volume":"83","author":"Xu","year":"2012","journal-title":"Biochem. Pharmacol."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/28\/1\/107\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T01:49:00Z","timestamp":1760147340000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/28\/1\/107"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12,23]]},"references-count":52,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2023,1]]}},"alternative-id":["molecules28010107"],"URL":"https:\/\/doi.org\/10.3390\/molecules28010107","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,12,23]]}}}