{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T17:55:20Z","timestamp":1792000520294,"version":"4.4.0"},"reference-count":151,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["The International Journal of Biochemistry & Cell Biology"],"published-print":{"date-parts":[[2021,2]]},"DOI":"10.1016\/j.biocel.2020.105904","type":"journal-article","created":{"date-parts":[[2020,12,24]],"date-time":"2020-12-24T21:00:05Z","timestamp":1608843605000},"page":"105904","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"special_numbering":"C","title":["Cellular S-denitrosylases: Potential role and interplay of Thioredoxin, TRP14, and Glutaredoxin systems in thiol-dependent protein denitrosylation"],"prefix":"10.1016","volume":"131","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9409-6194","authenticated-orcid":false,"given":"Ajanta","family":"Chatterji","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9665-8784","authenticated-orcid":false,"given":"Rajib","family":"Sengupta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"17","key":"10.1016\/j.biocel.2020.105904_bib0005","doi-asserted-by":"crossref","first-page":"3405","DOI":"10.1021\/bi200266v","article-title":"S-nitrosylation of ApoE in Alzheimer\u2019s disease","volume":"50","author":"Abrams","year":"2011","journal-title":"Biochemistry"},{"issue":"10","key":"10.1016\/j.biocel.2020.105904_bib0010","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/S0166-2236(02)02254-3","article-title":"cGMP and S-nitrosylation: two routes for modulation of neuronal excitability by NO","volume":"25","author":"Ahern","year":"2002","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.biocel.2020.105904_bib0015","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/bs.mie.2017.11.003","article-title":"Characterization of glutaredoxin Fe-S cluster-binding interactions using circular dichroism spectroscopy","volume":"599","author":"Albetel","year":"2018","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.biocel.2020.105904_bib0020","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/s00109-012-0878-z","article-title":"Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease","volume":"90","author":"Anand","year":"2012","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.biocel.2020.105904_bib0025","doi-asserted-by":"crossref","first-page":"9813","DOI":"10.1073\/pnas.91.21.9813","article-title":"Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin\/glutaredoxin 1 double mutant","volume":"91","author":"Aslund","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biocel.2020.105904_bib0030","doi-asserted-by":"crossref","first-page":"30780","DOI":"10.1074\/jbc.272.49.30780","article-title":"Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria","volume":"272","author":"Aslund","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biocel.2020.105904_bib0035","doi-asserted-by":"crossref","first-page":"8233","DOI":"10.1074\/jbc.M809338200","article-title":"Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for mammalian S phase ribonucleotide reductase","volume":"284","author":"Avval","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.biocel.2020.105904_bib0040","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1080\/10409238.2017.1304353","article-title":"The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy","volume":"52","author":"Barnett","year":"2017","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"issue":"2","key":"10.1016\/j.biocel.2020.105904_bib0045","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1073\/pnas.94.2.479","article-title":"The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I","volume":"94","author":"Bedford","year":"1997","journal-title":"Proc. Nat. Aca. Sci."},{"issue":"46","key":"10.1016\/j.biocel.2020.105904_bib0050","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":"5879","key":"10.1016\/j.biocel.2020.105904_bib0055","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1126\/science.1158265","article-title":"Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxin","volume":"320","author":"Benhar","year":"2008","journal-title":"Science"},{"issue":"32","key":"10.1016\/j.biocel.2020.105904_bib0060","doi-asserted-by":"crossref","first-page":"6963","DOI":"10.1021\/bi100619k","article-title":"Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach","volume":"49","author":"Benhar","year":"2010","journal-title":"Biochemistry"},{"issue":"2007","key":"10.1016\/j.biocel.2020.105904_bib0065","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1152\/ajpheart.01162.2006","article-title":"Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system","volume":"292","author":"Berndt","year":"2007","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"issue":"18","key":"10.1016\/j.biocel.2020.105904_bib0070","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1089\/ars.2017.7004","article-title":"Inflammation and nitrosative stress effects in ovarian and prostate pathology and carcinogenesis","volume":"26","author":"Burke","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biocel.2020.105904_bib0075","first-page":"3365","article-title":"Nitric oxide induces conformational and functional modifications of wild-type p53 tumor suppressor protein","volume":"57","author":"Calmels","year":"1997","journal-title":"Cancer Res."},{"issue":"4","key":"10.1016\/j.biocel.2020.105904_bib0080","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.bbadis.2016.02.005","article-title":"Altered S-nitrosothiol homeostasis provides a survival advantage to breast cancer cells in HER2 tumors and reduces their sensitivity to trastuzumab","volume":"1862","author":"Ca\u00f1as","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"issue":"2","key":"10.1016\/j.biocel.2020.105904_bib0085","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1093\/cvr\/cvy183","article-title":"A thioredoxin-mimetic peptide exerts potent anti-inflammatory, antioxidant, and atheroprotective effects in ApoE2.KI mice fed high fat diet","volume":"115","author":"Canesi","year":"2019","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.biocel.2020.105904_bib0090","first-page":"161","article-title":"Overexpression of thioredoxins 1 and 2 increases retinal ganglion cell survival after pharmacologically induced oxidative stress, optic nerve transection, and in experimental glaucoma","volume":"107","author":"Caprioli","year":"2009","journal-title":"Trans. Am. Ophthalmol. Soc."},{"issue":"8","key":"10.1016\/j.biocel.2020.105904_bib0095","doi-asserted-by":"crossref","first-page":"2511","DOI":"10.1021\/jp7104665","article-title":"Mechanism of thioredoxin-catalyzed disulfide reduction. Activation of the buried thiol and role of the variable active-site residues","volume":"112","author":"Carvalho","year":"2008","journal-title":"J. Phys. Chem. B"},{"issue":"2","key":"10.1016\/j.biocel.2020.105904_bib0100","doi-asserted-by":"crossref","first-page":"C304","DOI":"10.1152\/ajpcell.00410.2019","article-title":"Dysregulation of the glutaredoxin\/S-glutathionylation redox axis in lung diseases","volume":"318","author":"Chia","year":"2020","journal-title":"Am. J. Physiol., Cell Physiol."},{"key":"10.1016\/j.biocel.2020.105904_bib0105","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/71090","article-title":"Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation","volume":"3","author":"Choi","year":"2000","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.biocel.2020.105904_bib0110","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.1126\/science.1093891","article-title":"S-nitrosylation of parkin regulates ubiquitination and compromises parkin\u2019s protective function","volume":"304","author":"Chung","year":"2004","journal-title":"Science"},{"issue":"7","key":"10.1016\/j.biocel.2020.105904_bib0115","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1016\/j.bcp.2013.01.003","article-title":"Thioredoxin-mimetic peptides (TXM) reverse auranofin induced apoptosis and restore insulin secretion in insulinoma cells","volume":"85","author":"Cohen-Kutner","year":"2013","journal-title":"Biochem. Pharmacol."},{"issue":"36","key":"10.1016\/j.biocel.2020.105904_bib0120","doi-asserted-by":"crossref","first-page":"33249","DOI":"10.1074\/jbc.M203036200","article-title":"Human mitochondrial thioredoxin. Involvement in mitochondrial membrane potential and cell death","volume":"277","author":"Damdimopoulos","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biocel.2020.105904_bib0125","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1002\/j.1460-2075.1984.tb01994.x","article-title":"Conformational and functional similarites between glutaredoxin and thioredoxins","volume":"3","author":"Eklund","year":"1984","journal-title":"EMBO J."},{"key":"10.1016\/j.biocel.2020.105904_bib0130","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.bbrc.2004.12.067","article-title":"Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release","volume":"327","author":"Enoksson","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"4","key":"10.1016\/j.biocel.2020.105904_bib0135","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."},{"issue":"26","key":"10.1016\/j.biocel.2020.105904_bib0140","doi-asserted-by":"crossref","first-page":"24544","DOI":"10.1074\/jbc.M500678200","article-title":"A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase","volume":"280","author":"Fernandes","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biocel.2020.105904_bib0145","doi-asserted-by":"crossref","first-page":"S46","DOI":"10.1016\/j.freeradbiomed.2018.04.153","article-title":"P-6 - Thioredoxin related protein of 14 kDa (TRP14, TXNDC17) represses Nrf2 and NF\u03baB activities and augments HIF activation","volume":"120","author":"Fern\u00e1ndez","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.biocel.2020.105904_bib0150","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1093\/eurheartj\/ehr304","article-title":"Nitric oxide synthases: regulation and function","volume":"33","author":"Forstermann","year":"2011","journal-title":"Eur. Heart J."},{"issue":"4","key":"10.1016\/j.biocel.2020.105904_bib0155","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/S1471-4914(03)00028-5","article-title":"S-nitrosylation in health and disease","volume":"9","author":"Foster","year":"2003","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.biocel.2020.105904_bib0160","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2019.101158","article-title":"Role of nitric oxide in pancreatic cancer cells exhibiting the invasive phenotype","volume":"22","author":"Fujita","year":"2019","journal-title":"Redox Biol."},{"key":"10.1016\/j.biocel.2020.105904_bib0165","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.coph.2007.06.003","article-title":"Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress","volume":"7","author":"Gallogly","year":"2007","journal-title":"Curr. Opin. Pharmacol."},{"issue":"10","key":"10.1016\/j.biocel.2020.105904_bib0170","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1002\/emmm.201201462","article-title":"Thioredoxin-80 is a product of alpha-secretase cleavage that inhibits amyloid-beta aggregation and is decreased in Alzheimer\u2019s disease brain","volume":"4","author":"Gil-Bea","year":"2012","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.biocel.2020.105904_bib0175","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1089\/ars.2006.8.735","article-title":"In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli","volume":"8","author":"Gon","year":"2006","journal-title":"Antioxid. Redox Signal."},{"issue":"3","key":"10.1016\/j.biocel.2020.105904_bib0180","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1097\/FJC.0b013e3181b72c9f","article-title":"S-Nitrosylation of cardiac ion channels","volume":"54","author":"Gonzalez","year":"2009","journal-title":"J. Cardiovasc. Pharmacol."},{"issue":"5584","key":"10.1016\/j.biocel.2020.105904_bib0185","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1126\/science.1073634","article-title":"S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death","volume":"297","author":"Gu","year":"2002","journal-title":"Science"},{"issue":"4","key":"10.1016\/j.biocel.2020.105904_bib0190","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1006\/niox.1997.0134","article-title":"Effects of redox-related congeners of NO on apoptosis and Caspase-3 activity","volume":"1","author":"Haendeler","year":"1997","journal-title":"Nitric Oxide"},{"key":"10.1016\/j.biocel.2020.105904_bib0195","doi-asserted-by":"crossref","first-page":"21890","DOI":"10.1074\/jbc.M801047200","article-title":"Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues","volume":"283","author":"Hashemy","year":"2008","journal-title":"J. Biol. Chem."},{"issue":"19","key":"10.1016\/j.biocel.2020.105904_bib0200","doi-asserted-by":"crossref","first-page":"14428","DOI":"10.1074\/jbc.M700927200","article-title":"Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity","volume":"282","author":"Hashemy","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biocel.2020.105904_bib0205","first-page":"5268","article-title":"Thioredoxin reductase modulates NFkB signaling at the nuclear compartment","volume":"68","author":"Heilman","year":"2008","journal-title":"Cancer Res."},{"key":"10.1016\/j.biocel.2020.105904_bib0210","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1016\/j.freeradbiomed.2014.03.022","article-title":"\u03b1-Lipoic acid protects mitochondrial enzymes and attenuates lipopolysaccharide-induced hypothermia in mice","volume":"71","author":"Hiller","year":"2014","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.biocel.2020.105904_bib0215","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.bbagen.2015.09.001","article-title":"Alpha-lipoic acid supplementation protects enzymes from damage by nitrosative and oxidative stress","volume":"1860","author":"Hiller","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biocel.2020.105904_bib0220","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1111\/j.1432-1033.1968.tb00470.x","article-title":"Thioredoxin: amino acid sequence of the protein from Escherichia coli B","volume":"6","author":"Holmgren","year":"1968","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.biocel.2020.105904_bib0225","doi-asserted-by":"crossref","first-page":"2275","DOI":"10.1073\/pnas.73.7.2275","article-title":"Hydrogen donor system for Escherichia coli ribonucleosidediphosphate reductase dependent upon glutathione","volume":"73","author":"Holmgren","year":"1976","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biocel.2020.105904_bib0230","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1146\/annurev.bi.54.070185.001321","article-title":"Thioredoxin","volume":"54","author":"Holmgren","year":"1985","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.biocel.2020.105904_bib0235","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/0076-6879(95)52031-7","article-title":"Glutaredoxin","volume":"252","author":"Holmgren","year":"1995","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.biocel.2020.105904_bib0240","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.bbrc.2010.03.083","article-title":"Thioredoxin and thioredoxin reductase: current research with special reference to human disease","volume":"396","author":"Holmgren","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"24","key":"10.1016\/j.biocel.2020.105904_bib0245","doi-asserted-by":"crossref","first-page":"9265","DOI":"10.1073\/pnas.84.24.9265","article-title":"Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide","volume":"84","author":"Ignarro","year":"1987","journal-title":"Proc. Nat. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biocel.2020.105904_bib0250","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/S0968-0004(00)01685-6","article-title":"PICOT-HD: a highly conserved protein domain that is often associated with thioredoxin and glutaredoxin modules","volume":"25","author":"Isakov","year":"2000","journal-title":"Trends Biochem. Sci."},{"issue":"8","key":"10.1016\/j.biocel.2020.105904_bib0255","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1128\/EC.00133-08","article-title":"Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway","volume":"7","author":"Izquierdo","year":"2008","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.biocel.2020.105904_bib0260","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1016\/S0006-291X(05)80940-4","article-title":"Human thioredoxin reactivity-structure\/function relationship","volume":"173","author":"Jacquot","year":"1990","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"5","key":"10.1016\/j.biocel.2020.105904_bib0265","doi-asserted-by":"crossref","first-page":"3151","DOI":"10.1074\/jbc.M307959200","article-title":"Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways","volume":"279","author":"Jeong","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.biocel.2020.105904_bib0270","doi-asserted-by":"crossref","first-page":"3142","DOI":"10.1074\/jbc.M307932200","article-title":"Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin function","volume":"279","author":"Jeong","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.biocel.2020.105904_bib0275","doi-asserted-by":"crossref","first-page":"1294","DOI":"10.1016\/j.freeradbiomed.2009.07.021","article-title":"Thioredoxin-related protein 14, a new member of the thioredoxin family with disulfide reductase activity: implication in the redox regulation of TNF-alpha signaling","volume":"47","author":"Jeong","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.biocel.2020.105904_bib0280","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1111\/j.1469-7580.2007.00722.x","article-title":"Human TRP14 gene homologue from amphioxus Branchiostoma belcheri: identification, evolution, expression and functional characterization","volume":"210","author":"Jiang","year":"2007","journal-title":"J. Anat."},{"key":"10.1016\/j.biocel.2020.105904_bib0285","doi-asserted-by":"crossref","first-page":"7537","DOI":"10.1074\/jbc.M312719200","article-title":"Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase","volume":"279","author":"Johansson","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"13","key":"10.1016\/j.biocel.2020.105904_bib0290","doi-asserted-by":"crossref","first-page":"1562","DOI":"10.1134\/S0006297914130082","article-title":"Role of glutathione, glutathione transferase, and glutaredoxin in regulation of redox-dependent processes","volume":"79","author":"Kalinina","year":"2014","journal-title":"Biochemistry Mosc."},{"key":"10.1016\/j.biocel.2020.105904_bib0295","doi-asserted-by":"crossref","first-page":"31138","DOI":"10.1074\/jbc.272.49.31138","article-title":"Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms","volume":"272","author":"Kim","year":"1997","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.biocel.2020.105904_bib0300","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.molcel.2014.08.003","article-title":"Selective protein denitrosylation activity of Thioredoxin-h5 modulates plant Immunity","volume":"56","author":"Kneeshaw","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.biocel.2020.105904_bib0305","first-page":"1522","article-title":"S-nitrosylation of the p53 tumor suppressor protein in medulloblastoma","author":"Koldobskiy","year":"2013","journal-title":"NeuroOncology"},{"key":"10.1016\/j.biocel.2020.105904_bib0310","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1126\/science.1470903","article-title":"The molecule of the year","volume":"258","author":"Koshland","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.biocel.2020.105904_bib0315","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1186\/1750-1326-5-49","article-title":"NO signaling and S-nitrosylation regulate PTEN inhibition in neurodegeneration","volume":"5","author":"Kwak","year":"2010","journal-title":"Mol. Neurodegenerat."},{"issue":"17","key":"10.1016\/j.biocel.2020.105904_bib0320","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1093\/bioinformatics\/bts436","article-title":"dbSNO: a database of cysteine S-nitrosylation","volume":"28","author":"Lee","year":"2012","journal-title":"Bioinformatics"},{"issue":"1","key":"10.1016\/j.biocel.2020.105904_bib0325","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1074\/mcp.M113.032235","article-title":"Protein microarray characterization of the S-nitrosoproteome","volume":"13","author":"Lee","year":"2014","journal-title":"Mol. Cell Proteomics"},{"issue":"9","key":"10.1016\/j.biocel.2020.105904_bib0330","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1002\/glia.23178","article-title":"Iron-sulfur glutaredoxin 2 protects oligodendrocytes against damage induced by nitric oxide release from activated microglia","volume":"65","author":"Lepka","year":"2017","journal-title":"Glia"},{"key":"10.1016\/j.biocel.2020.105904_bib0335","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.molcel.2007.02.024","article-title":"Regulation of HIF-1 alpha stability through S-nitrosylation","volume":"26","author":"Li","year":"2007","journal-title":"Mol. Cell"},{"issue":"1","key":"10.1016\/j.biocel.2020.105904_bib0340","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1074\/jbc.M110.184176","article-title":"Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast","volume":"286","author":"Li","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.biocel.2020.105904_bib0345","doi-asserted-by":"crossref","first-page":"3896","DOI":"10.1038\/s41467-019-11892-5","article-title":"GSNOR provides plant tolerance to iron toxicity via preventing iron-dependent nitrosative and oxidative cytotoxicity","volume":"10","author":"Li","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.biocel.2020.105904_bib0350","doi-asserted-by":"crossref","first-page":"13227","DOI":"10.1073\/pnas.0401896101","article-title":"Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells towards doxorubicin and phenylarsine oxide","volume":"101","author":"Lillig","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"4","key":"10.1016\/j.biocel.2020.105904_bib0355","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1161\/CIRCRESAHA.109.207381","article-title":"S-nitrosylation in cardiovascular signaling","volume":"106","author":"Lima","year":"2010","journal-title":"Circ Res."},{"key":"10.1016\/j.biocel.2020.105904_bib0360","first-page":"1259","article-title":"Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-Mediated apoptosis in a redox activity-independent manner","volume":"90","author":"Liu","year":"2002","journal-title":"J. Am. Heart Assoc."},{"issue":"6827","key":"10.1016\/j.biocel.2020.105904_bib0365","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1038\/35068596","article-title":"A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans","volume":"410","author":"Liu","year":"2001","journal-title":"Nature."},{"key":"10.1016\/j.biocel.2020.105904_bib0370","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1089\/ars.2007.1821","article-title":"Expression pattern of human glutaredoxin 2 isoforms: identification and characterization of two testis\/cancer cell-specific isoforms","volume":"10","author":"Lonn","year":"2008","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biocel.2020.105904_bib0375","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1093\/cvr\/cvp085","article-title":"High glucose sensitizes adult cardiomyocytes to ischaemia\/reperfusion injury through nitrative thioredoxin inactivation","volume":"83","author":"Luan","year":"2009","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.biocel.2020.105904_bib0380","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0014-5793(98)01698-6","article-title":"Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A","volume":"443","author":"Lundstrom-Ljung","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biocel.2020.105904_bib0385","doi-asserted-by":"crossref","first-page":"6686","DOI":"10.1016\/S0021-9258(18)34484-3","article-title":"Glutaredoxin from calf thymus. Purification to homogeneity","volume":"257","author":"Luthman","year":"1982","journal-title":"J. Biol. Chem."},{"issue":"12","key":"10.1016\/j.biocel.2020.105904_bib0390","doi-asserted-by":"crossref","first-page":"4747","DOI":"10.1167\/iovs.05-0128","article-title":"Activation of matrix metalloproteinase-9 via neuronal nitric oxide synthase contributes to NMDA-induced retinal ganglion cell death","volume":"46","author":"Manabe","year":"2005","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"issue":"6","key":"10.1016\/j.biocel.2020.105904_bib0395","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1186\/bcr3331","article-title":"S-nitrosylation of Ras in breast cancer","volume":"14","author":"Marshall","year":"2012","journal-title":"Breast Cancer Res."},{"key":"10.1016\/j.biocel.2020.105904_bib0400","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/S0969-2126(01)00154-X","article-title":"Thioredoxin- a fold for all reasons","volume":"3","author":"Martin","year":"1995","journal-title":"Structure"},{"key":"10.1016\/j.biocel.2020.105904_bib0405","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.plantsci.2018.05.001","article-title":"Thioredoxin-mediated redox signalling in plant immunity","volume":"279","author":"Mata-P\u00e9rez","year":"2019","journal-title":"Plant Sci."},{"issue":"4","key":"10.1016\/j.biocel.2020.105904_bib0410","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1016\/j.yjmcc.2010.09.020","article-title":"Application of recombinant thioredoxin1 for treatment of heart disease","volume":"51","author":"Matsushima","year":"2011","journal-title":"J. Mol. Cell. Cardiol."},{"issue":"15","key":"10.1016\/j.biocel.2020.105904_bib0415","doi-asserted-by":"crossref","first-page":"3821","DOI":"10.1093\/nar\/20.15.3821","article-title":"Thioredoxin regulates the DNA binding activity of NF-kappa \u03b2 by reduction of a disulphide bond involving cysteine 62","volume":"20","author":"Matthews","year":"1992","journal-title":"Nucleic Acids Res."},{"issue":"1 Supplement)","key":"10.1016\/j.biocel.2020.105904_bib0420","article-title":"Potential role of thioredoxin-interacting protein in non-IgE mast cell degranulation","volume":"204","author":"Mendoza","year":"2020","journal-title":"J. Immunol."},{"key":"10.1016\/j.biocel.2020.105904_bib0425","doi-asserted-by":"crossref","first-page":"1452","DOI":"10.1021\/bi7017865","article-title":"Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron\u2013sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins","volume":"47","author":"Mesecke","year":"2008","journal-title":"Biochemistry"},{"issue":"8","key":"10.1016\/j.biocel.2020.105904_bib0430","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1089\/ars.2011.4327","article-title":"Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance","volume":"17","author":"Meyer","year":"2012","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biocel.2020.105904_bib0435","doi-asserted-by":"crossref","DOI":"10.1177\/1178223419882688","article-title":"Nitric oxide and S-Nitrosylation in cancers: emphasis on breast cancer","volume":"14","author":"Mishra","year":"2020","journal-title":"Breast Cancer (Auckl)."},{"issue":"9","key":"10.1016\/j.biocel.2020.105904_bib0440","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1008379","article-title":"The monothiol glutaredoxin GrxD is essential for sensing iron starvation in Aspergillus fumigatus","volume":"15","author":"Misslinger","year":"2019","journal-title":"PLoS Genet."},{"issue":"28","key":"10.1016\/j.biocel.2020.105904_bib0445","doi-asserted-by":"crossref","first-page":"11609","DOI":"10.1073\/pnas.0704898104","article-title":"Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells","volume":"104","author":"Mitchell","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biocel.2020.105904_bib0450","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1006\/bbrc.1997.7304","article-title":"Inhibition of caspase-3 by S-nitrosation and oxidation caused by nitric oxide","volume":"238","author":"Mohr","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biocel.2020.105904_bib0455","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.niox.2019.04.009","article-title":"Nitric oxide and interactions with reactive oxygen species in the development of melanoma, breast, and colon cancer: a redox signaling perspective","volume":"89","author":"Monteiro","year":"2019","journal-title":"Nitric Oxide"},{"key":"10.1016\/j.biocel.2020.105904_bib0460","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1007\/978-1-4419-1399-9_41","article-title":"Thioredoxins 1 and 2 protect retinal ganglion cells from pharmacologically induced oxidative stress, optic nerve transection and ocular hypertension","volume":"664","author":"Munemasa","year":"2010","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.biocel.2020.105904_bib0465","doi-asserted-by":"crossref","first-page":"50226","DOI":"10.1074\/jbc.M310171200","article-title":"Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt","volume":"278","author":"Murata","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biocel.2020.105904_bib0470","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.molcel.2010.07.002","article-title":"Transnitrosylation of XIAP regulates caspase-dependent neuronal cell death","volume":"39","author":"Nakamura","year":"2010","journal-title":"Mol. Cell"},{"issue":"25","key":"10.1016\/j.biocel.2020.105904_bib0475","doi-asserted-by":"crossref","first-page":"10349","DOI":"10.1073\/pnas.1103503108","article-title":"On-off system for PI3-kinase-Akt signaling through S-nitrosylation of phosphatase with sequence homology to tensin (PTEN)","volume":"108","author":"Numajiri","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"19","key":"10.1016\/j.biocel.2020.105904_bib0480","doi-asserted-by":"crossref","first-page":"7439","DOI":"10.1073\/pnas.0401965101","article-title":"Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli","volume":"101","author":"Ortenberg","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"19","key":"10.1016\/j.biocel.2020.105904_bib0485","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. U. S. A."},{"key":"10.1016\/j.biocel.2020.105904_bib0490","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1038\/327524a0","article-title":"Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor","volume":"327","author":"Palmer","year":"1987","journal-title":"Nature"},{"key":"10.1016\/j.biocel.2020.105904_bib0495","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1038\/333664a0","article-title":"Vascular endothelial cells synthesize nitric oxide from L-arginine","volume":"333","author":"Palmer","year":"1988","journal-title":"Nature"},{"issue":"29","key":"10.1016\/j.biocel.2020.105904_bib0500","doi-asserted-by":"crossref","first-page":"10810","DOI":"10.1073\/pnas.0404161101","article-title":"Nitrosative stress linked to sporadic Parkinson\u2019s disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity","volume":"101","author":"Palmer","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"8","key":"10.1016\/j.biocel.2020.105904_bib0505","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1007\/s11064-009-9938-3","article-title":"S-nitrosylation of PTEN Invovled in ischemic brain injury in rat hippocampal CA1 region","volume":"34","author":"Pei","year":"2009","journal-title":"Neurochem. Res."},{"issue":"4","key":"10.1016\/j.biocel.2020.105904_bib0510","doi-asserted-by":"crossref","first-page":"364","DOI":"10.4161\/pri.21250","article-title":"S-nitrosylation of Cdk5: potential implications in amyloid-\u03b2-related neurotoxicity in Alzheimer disease","volume":"6","author":"Qu","year":"2012","journal-title":"Prion"},{"key":"10.1016\/j.biocel.2020.105904_bib0515","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.1002\/1873-3468.13454","article-title":"Characterization of mammalian glutaredoxin isoforms as S-denitrosylases","volume":"593","author":"Ren","year":"2019","journal-title":"FEBS Lett."},{"issue":"5\u20136","key":"10.1016\/j.biocel.2020.105904_bib0520","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1615\/CritRevOncog.2017021074","article-title":"Tumor suppressor roles of the denitrosylase GSNOR","volume":"21","author":"Rizza","year":"2016","journal-title":"Crit. Rev. Oncog."},{"key":"10.1016\/j.biocel.2020.105904_bib0525","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1091\/mbc.01-10-0517","article-title":"Grx5 is a mitochondrial glutaredoxin required for the activity of iron\/sulfur enzymes","volume":"13","author":"Rodriguez-Manzaneque","year":"2002","journal-title":"Mol. Biol. Cell"},{"issue":"12","key":"10.1016\/j.biocel.2020.105904_bib0530","doi-asserted-by":"crossref","first-page":"8180","DOI":"10.1128\/MCB.19.12.8180","article-title":"Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae","volume":"19","author":"Rodr\u00edguez-Manzaneque","year":"1999","journal-title":"Mol. Cell. Biol."},{"issue":"3","key":"10.1016\/j.biocel.2020.105904_bib0535","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1002\/jnr.21897","article-title":"Intracellular glutathione mediates the denitrosylation of protein nitrosothiols in the rat spinal cord","volume":"87","author":"Romero","year":"2009","journal-title":"J. Neurosci. Res."},{"issue":"1","key":"10.1016\/j.biocel.2020.105904_bib0540","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.tibs.2009.08.005","article-title":"Glutaredoxins: roles in iron homeostasis","volume":"35","author":"Rouhier","year":"2010","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.biocel.2020.105904_bib0545","doi-asserted-by":"crossref","first-page":"4443","DOI":"10.1038\/sj.emboj.7600422","article-title":"NO activation of guanylyl cyclase","volume":"23","author":"Russwurm","year":"2004","journal-title":"EMBO J."},{"issue":"10","key":"10.1016\/j.biocel.2020.105904_bib0550","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1161\/CIRCULATIONAHA.109.872481","article-title":"Thioredoxin-1 gene therapy enhances angiogenic signaling and reduces ventricular remodeling in infarcted myocardium of diabetic rats","volume":"121","author":"Samuel","year":"2010","journal-title":"Circulation"},{"issue":"3","key":"10.1016\/j.biocel.2020.105904_bib0555","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1089\/ars.2012.4716","article-title":"Thioredoxin and thioredoxin reductase in relation to reversible S-nitrosylation","volume":"18","author":"Sengupta","year":"2013","journal-title":"Antioxid. Redox Signal."},{"issue":"28","key":"10.1016\/j.biocel.2020.105904_bib0560","doi-asserted-by":"crossref","first-page":"8472","DOI":"10.1021\/bi700449x","article-title":"Thioredoxin catalyzes the denitrosation of low-molecular mass and protein S-nitrosothiols","volume":"46","author":"Sengupta","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.biocel.2020.105904_bib0565","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1016\/j.febslet.2009.10.016","article-title":"Nitric oxide and dihydrolipoic acid modulate the activity of caspase 3 in HepG2 cells","volume":"583","author":"Sengupta","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biocel.2020.105904_bib0570","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1016\/j.bbrc.2009.12.036","article-title":"Nitric oxide and thioredoxin type 1 modulate the activity of caspase 8 in HepG2 cells","volume":"391","author":"Sengupta","year":"2010","journal-title":"Biochem. Biophy. Res. Com."},{"issue":"34","key":"10.1016\/j.biocel.2020.105904_bib0575","doi-asserted-by":"crossref","first-page":"12708","DOI":"10.1074\/jbc.RA119.008752","article-title":"Glutathione-glutaredoxin is an efficient electron donor system for mammalian p53R2-R1-dependent ribonucleotide reductase","volume":"294","author":"Sengupta","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biocel.2020.105904_bib0580","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1089\/ars.2010.3580","article-title":"Nitric oxide signaling and nitrosative stress in neurons: role for S-nitrosylation","volume":"14","author":"Shahani","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biocel.2020.105904_bib0585","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1089\/ars.2005.7.348","article-title":"Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation","volume":"7","author":"Shelton","year":"2005","journal-title":"Antioxid. Redox Signal."},{"issue":"25","key":"10.1016\/j.biocel.2020.105904_bib0590","doi-asserted-by":"crossref","first-page":"14428","DOI":"10.1073\/pnas.93.25.14428","article-title":"The chemistry of the S-nitrosoglutathione\/glutathione system","volume":"93","author":"Singh","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"10","key":"10.1016\/j.biocel.2020.105904_bib0595","doi-asserted-by":"crossref","first-page":"8733","DOI":"10.1074\/jbc.M408080200","article-title":"Characterization of the S-denitrosation activity of protein disulfide isomerase","volume":"280","author":"Sliskovic","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.biocel.2020.105904_bib0600","doi-asserted-by":"crossref","first-page":"1568","DOI":"10.1074\/jbc.RA118.004947","article-title":"Molecular recognition of S-nitrosothiol substrate by its cognate protein denitrosylase","volume":"294","author":"Stomberski","year":"2019","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.biocel.2020.105904_bib0605","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1021\/bi9519718","article-title":"Spectral and kinetic studies on the activation of soluble guanylate cyclase by nitric oxide","volume":"35","author":"Stone","year":"1996","journal-title":"Biochemistry"},{"issue":"45","key":"10.1016\/j.biocel.2020.105904_bib0610","doi-asserted-by":"crossref","first-page":"15815","DOI":"10.1021\/ja0529135","article-title":"Thioredoxin and Lipoic Acid Catalyze the Denitrosation of Low Molecular Weight and Protein S-Nitrosothiols","volume":"127","author":"Stoyanovsky","year":"2005","journal-title":"J. Am. Chem. Soc."},{"issue":"3","key":"10.1016\/j.biocel.2020.105904_bib0615","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1042\/BJ20112131","article-title":"The biological roles of glutaredoxins","volume":"446","author":"Str\u00f6her","year":"2012","journal-title":"Biochem. J."},{"issue":"28","key":"10.1016\/j.biocel.2020.105904_bib0620","doi-asserted-by":"crossref","first-page":"26491","DOI":"10.1074\/jbc.M503638200","article-title":"Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation","volume":"280","author":"Su","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biocel.2020.105904_bib0625","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.nbd.2005.10.004","article-title":"Identification of nitrated proteins in Alzheimer\u2019s disease brain using a redox proteomics approach","volume":"22","author":"Sultana","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.biocel.2020.105904_bib0630","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.ijcard.2015.08.117","article-title":"Thioredoxin-1 (Trx1) engineered mesenchymal stem cell therapy increased pro-angiogenic factors, reduced fibrosis and improved heart function in the infarcted rat myocardium","volume":"201","author":"Suresh","year":"2015","journal-title":"Int. J. Cardiol."},{"issue":"2","key":"10.1016\/j.biocel.2020.105904_bib0635","first-page":"117","article-title":"S-nitrosation mediates multiple pathways that lead to tumor progression in estrogen receptor-negative breast Cancer","volume":"3","author":"Switzer","year":"2012","journal-title":"For. Immunopathol. Dis. Therap."},{"key":"10.1016\/j.biocel.2020.105904_bib0640","first-page":"1343","article-title":"TRP14 promotes resistance to cisplatin by inducing autophagy in ovarian cancer","volume":"42","author":"Tan","year":"2019","journal-title":"Oncol. Rep."},{"issue":"2","key":"10.1016\/j.biocel.2020.105904_bib0645","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/0378-1119(91)90081-L","article-title":"Isolation and characterization of human thioredoxin-encoding genes","volume":"102","author":"Tonissen","year":"1991","journal-title":"Gene"},{"key":"10.1016\/j.biocel.2020.105904_bib0650","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1002\/eji.200939724","article-title":"Thioredoxin suppresses airway inflammation independently of systemic Th1\/Th2 immune modulation","volume":"40","author":"Torii","year":"2010","journal-title":"Eur. J. Immunol."},{"issue":"47","key":"10.1016\/j.biocel.2020.105904_bib0655","doi-asserted-by":"crossref","first-page":"39732","DOI":"10.1074\/jbc.M112.409235","article-title":"Thioredoxin, the processivity factor, sequesters an exposed cysteine in the thumb domain of bacteriophage T7 DNA polymerase","volume":"287","author":"Tran","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biocel.2020.105904_bib0660","doi-asserted-by":"crossref","first-page":"4900","DOI":"10.1073\/pnas.0810595106","article-title":"S-nitrosylation of XIAP compromises neuronal survival in Parkinson\u2019s disease","volume":"106","author":"Tsang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"6","key":"10.1016\/j.biocel.2020.105904_bib0665","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/S0022-2828(03)00117-2","article-title":"Thioredoxin redox signaling in the ischemic heart: an insight with transgenic mice overexpressing Trx1","volume":"35","author":"Turoczi","year":"2003","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.biocel.2020.105904_bib0670","doi-asserted-by":"crossref","first-page":"S115","DOI":"10.1097\/00005344-198800125-00020","article-title":"Biochemical mechanisms underlying vascular smooth muscle relaxation: the guanylate cyclase-cyclic GMP system","volume":"12","author":"Waldman","year":"1988","journal-title":"J. Cardiovasc. Pharmacol."},{"issue":"19","key":"10.1016\/j.biocel.2020.105904_bib0675","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.3000328","article-title":"S-nitrosylation from GSNOR deficiency impairs DNA repair and promotes hepatocarcinogenesis","volume":"2","author":"Wei","year":"2010","journal-title":"Sci. Transl. Med."},{"issue":"5","key":"10.1016\/j.biocel.2020.105904_bib0680","doi-asserted-by":"crossref","first-page":"1670","DOI":"10.1016\/j.fsi.2013.08.010","article-title":"Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa from orange-spotted grouper, Epinephelus coioides","volume":"35","author":"Wei","year":"2013","journal-title":"Fish Shellfish Immunol."},{"issue":"1","key":"10.1016\/j.biocel.2020.105904_bib0685","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0210827","article-title":"IL-33 induction and signaling are controlled by glutaredoxin-1 in mouse macrophages","volume":"14","author":"Weinberg","year":"2019","journal-title":"PLoS One"},{"key":"10.1016\/j.biocel.2020.105904_bib0690","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/nature06231","article-title":"Probing the chemistry of thioredoxin catalysis with force","volume":"450","author":"Wiita","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.biocel.2020.105904_bib0695","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.freeradbiomed.2017.02.013","article-title":"How widespread is stable protein S-nitrosylation as an end-effector of protein regulation?","volume":"109","author":"Wolhuter","year":"2017","journal-title":"Free Radic. Biol. Med."},{"issue":"3","key":"10.1016\/j.biocel.2020.105904_bib0700","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/j.molcel.2017.12.019","article-title":"Evidence against stable protein S-Nitrosylation as a widespread mechanism of post-translational regulation","volume":"69","author":"Wolhuter","year":"2018","journal-title":"Mol. Cell"},{"issue":"46","key":"10.1016\/j.biocel.2020.105904_bib0705","doi-asserted-by":"crossref","first-page":"48120","DOI":"10.1074\/jbc.M407079200","article-title":"Structural basis of cellular redox regulation by human TRP14","volume":"279","author":"Woo","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.biocel.2020.105904_bib0710","doi-asserted-by":"crossref","first-page":"2498","DOI":"10.1016\/j.jprot.2011.06.001","article-title":"Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach","volume":"74","author":"Wu","year":"2011","journal-title":"J. Proteomics"},{"key":"10.1016\/j.biocel.2020.105904_bib0715","first-page":"1","article-title":"Role of thioredoxin-interacting protein in diabetic myocardial ischemia-reperfusion injury","volume":"34","author":"Ye","year":"2020","journal-title":"FASEB J."},{"issue":"21","key":"10.1016\/j.biocel.2020.105904_bib0720","doi-asserted-by":"crossref","first-page":"2581","DOI":"10.1161\/01.CIR.0000129771.32215.44","article-title":"Thioredoxin-interacting protein controls cardiac hypertrophy through regulation of thioredoxin activity","volume":"109","author":"Yoshioka","year":"2004","journal-title":"Circulation"},{"issue":"8","key":"10.1016\/j.biocel.2020.105904_bib0725","doi-asserted-by":"crossref","first-page":"2616","DOI":"10.1074\/jbc.RA118.006096","article-title":"Glutaredoxin 1 up-regulates deglutathionylation of \u03b14 integrin and thereby restricts neutrophil mobilization from bone marrow","volume":"294","author":"You","year":"2019","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.biocel.2020.105904_bib0730","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1007\/s10695-015-0158-2","article-title":"Insights into Trx1, TRP14, and Prx1 homologs of Paralichthys olivaceus: molecular profiles and transcriptional responses to immune stimulations","volume":"42","author":"Yuan","year":"2016","journal-title":"Fish Physiol. Biochem."},{"issue":"43","key":"10.1016\/j.biocel.2020.105904_bib0735","doi-asserted-by":"crossref","first-page":"14366","DOI":"10.1523\/JNEUROSCI.3899-10.2010","article-title":"S-Nitrosylation of cyclin-dependent kinase 5 (cdk5) regulates its kinase activity and dendrite growth during neuronal development","volume":"30","author":"Zhang","year":"2010","journal-title":"J. Neurosci."},{"key":"10.1016\/j.biocel.2020.105904_bib0740","doi-asserted-by":"crossref","first-page":"5854","DOI":"10.1073\/pnas.100114897","article-title":"Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol\/selenenylsulfide formed from the conserved cysteine\u2013selenocysteine sequence","volume":"97","author":"Zhong","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biocel.2020.105904_bib0745","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1038\/sj.jcbfm.9600036","article-title":"Nitric oxide inhibits caspase activation and apoptotic morphology but does not rescue neuronal death","volume":"25","author":"Zhou","year":"2005","journal-title":"J. Cereb. Blood Flow Metab."},{"issue":"7737","key":"10.1016\/j.biocel.2020.105904_bib0750","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/s41586-018-0749-z","article-title":"Metabolic reprogramming by the S-nitroso-CoA reductase system protects against kidney injury","volume":"565","author":"Zhou","year":"2019","journal-title":"Nature"},{"issue":"11","key":"10.1016\/j.biocel.2020.105904_bib0755","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1089\/ars.2019.7807","article-title":"Anti-allergic and anti-inflammatory effects and molecular mechanisms of thioredoxin on respiratory system diseases","volume":"32","author":"Zhou","year":"2020","journal-title":"Antioxid. Redox Signal."}],"container-title":["The International Journal of Biochemistry & Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1357272520302211?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1357272520302211?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T07:19:07Z","timestamp":1761203947000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1357272520302211"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2]]},"references-count":151,"alternative-id":["S1357272520302211"],"URL":"https:\/\/doi.org\/10.1016\/j.biocel.2020.105904","relation":{},"ISSN":["1357-2725"],"issn-type":[{"value":"1357-2725","type":"print"}],"subject":[],"published":{"date-parts":[[2021,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cellular S-denitrosylases: Potential role and interplay of Thioredoxin, TRP14, and Glutaredoxin systems in thiol-dependent protein denitrosylation","name":"articletitle","label":"Article Title"},{"value":"The International Journal of Biochemistry & Cell Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biocel.2020.105904","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"105904"}}