{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T04:49:59Z","timestamp":1789015799294,"version":"build-2803163510"},"reference-count":47,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,4,1]],"date-time":"2018-04-01T00:00:00Z","timestamp":1522540800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,4,1]],"date-time":"2018-04-01T00:00:00Z","timestamp":1522540800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2017,10,24]],"date-time":"2017-10-24T00:00:00Z","timestamp":1508803200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["FDN 143278"],"award-info":[{"award-number":["FDN 143278"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000222","name":"Heart and Stroke Foundation of Canada","doi-asserted-by":"publisher","award":["NA7301"],"award-info":[{"award-number":["NA7301"]}],"id":[{"id":"10.13039\/501100000222","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008572","name":"University of Ottawa","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008572","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Redox Biology"],"published-print":{"date-parts":[[2018,4]]},"DOI":"10.1016\/j.redox.2017.10.019","type":"journal-article","created":{"date-parts":[[2017,10,26]],"date-time":"2017-10-26T20:47:10Z","timestamp":1509050830000},"page":"509-521","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":40,"special_numbering":"C","title":["Glutaredoxin-2 controls cardiac mitochondrial dynamics and energetics in mice, and protects against human cardiac pathologies"],"prefix":"10.1016","volume":"14","author":[{"given":"Georges N.","family":"Kanaan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bianca","family":"Ichim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lara","family":"Gharibeh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wael","family":"Maharsy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David A.","family":"Patten","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jian Ying","family":"Xuan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arkadiy","family":"Reunov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip","family":"Marshall","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Veinot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keir","family":"Menzies","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mona","family":"Nemer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mary-Ellen","family":"Harper","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.redox.2017.10.019_bib1","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1016\/S0891-5849(01)00480-4","article-title":"Redox environment of the cell as viewed through the redox state of the glutathione disulfide\/glutathione couple","volume":"30","author":"Schafer","year":"2001","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.redox.2017.10.019_bib2","doi-asserted-by":"crossref","first-page":"2601","DOI":"10.2174\/092986705774370646","article-title":"Mechanism of mitochondrial uncouplers, inhibitors, and toxins: focus on electron transfer, free radicals, and structure\u2013activity relationships","volume":"12","author":"Kovacic","year":"2005","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.redox.2017.10.019_bib3","doi-asserted-by":"crossref","first-page":"13147","DOI":"10.1073\/pnas.0502979102","article-title":"Nitric oxide regulates angiogenesis through a functional switch involving thrombospondin-1","volume":"102","author":"Ridnour","year":"2005","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"10.1016\/j.redox.2017.10.019_bib4","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1016\/j.bcp.2008.11.009","article-title":"Reactive oxygen species: destroyers or messengers?","volume":"77","author":"Bartosz","year":"2009","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.redox.2017.10.019_bib5","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/nri1312","article-title":"NOX enzymes and the biology of reactive oxygen","volume":"4","author":"Lambeth","year":"2004","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.redox.2017.10.019_bib6","series-title":"Toxicology of the Human Environment","first-page":"437","article-title":"Thermodynamic considerations of free radical reactions","author":"Butler","year":"2000"},{"key":"10.1016\/j.redox.2017.10.019_bib7","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1152\/physrev.00018.2001","article-title":"Free radicals in the physiological control of cell function","volume":"82","author":"Dr\u00f6ge","year":"2002","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.redox.2017.10.019_bib8","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1038\/embor.2012.128","article-title":"The intracellular redox state is a core determinant of mitochondrial fusion","volume":"13","author":"Shutt","year":"2012","journal-title":"EMBO Rep."},{"key":"10.1016\/j.redox.2017.10.019_bib9","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1089\/ars.2006.8.813","article-title":"Redox pathways in the mitochondrion","volume":"8","author":"Koehler","year":"2006","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.redox.2017.10.019_bib10","first-page":"1385","article-title":"Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways","volume":"387","author":"Jacob","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"21","key":"10.1016\/j.redox.2017.10.019_bib11","doi-asserted-by":"crossref","first-page":"14812","DOI":"10.1074\/jbc.M114.550574","article-title":"Glutaredoxin-2 is required to control oxidative phosphorylation in cardiac muscle by mediating deglutathionylation reactions","volume":"289","author":"Mailloux","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2017.10.019_bib12","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1161\/01.CIR.102.4.470","article-title":"Left ventricular hypertrophy","volume":"102","author":"Lorell","year":"2000","journal-title":"Circulation"},{"key":"10.1016\/j.redox.2017.10.019_bib13","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1093\/cvr\/cvq240","article-title":"Mitochondria in heart failure","volume":"88","author":"Rosca","year":"2010","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.redox.2017.10.019_bib14","doi-asserted-by":"crossref","first-page":"26269","DOI":"10.1074\/jbc.M011605200","article-title":"Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms","volume":"276","author":"Lundberg","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2017.10.019_bib15","doi-asserted-by":"crossref","first-page":"8365","DOI":"10.1074\/jbc.M112.442905","article-title":"Glutaredoxin-2 is required to control proton leak through uncoupling protein-3","volume":"288","author":"Mailloux","year":"2013","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.redox.2017.10.019_bib16","doi-asserted-by":"crossref","first-page":"1941","DOI":"10.1089\/ars.2008.2089","article-title":"Molecular mechanisms and clinical implications of reversible protein S-glutathionylation","volume":"10","author":"Mieyal","year":"2008","journal-title":"Antioxid. Redox Signal."},{"issue":"37","key":"10.1016\/j.redox.2017.10.019_bib17","doi-asserted-by":"crossref","first-page":"26497","DOI":"10.1074\/jbc.R113.461368","article-title":"Causes and consequences of cysteine S-glutathionylation","volume":"288","author":"Grek","year":"2013","journal-title":"J. Biol. Chem."},{"issue":"46","key":"10.1016\/j.redox.2017.10.019_bib18","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":"12","key":"10.1016\/j.redox.2017.10.019_bib19","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1016\/j.tibs.2013.09.001","article-title":"Unearthing the secrets of mitochondria ROS and glutathione in bioenergetics","volume":"38","author":"Mailloux","year":"2013","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.redox.2017.10.019_bib20","doi-asserted-by":"crossref","first-page":"24801","DOI":"10.1074\/jbc.M803432200","article-title":"Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of Cys residues in decreasing oxidative damage","volume":"283","author":"Hurd","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2017.10.019_bib21","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1161\/CIRCRESAHA.111.246124","article-title":"Redox regulation of mitochondrial ATP synthase: implications for cardiac resynchronization therapy","volume":"109","author":"Wang","year":"2011","journal-title":"Circ. Res."},{"key":"10.1016\/j.redox.2017.10.019_bib22","first-page":"95","article-title":"GSSG-mediated complex I defect in isolated cardiac mitochondria","volume":"26","author":"Passarelli","year":"2010","journal-title":"Int. J. Mol. Med."},{"issue":"9\u201310","key":"10.1016\/j.redox.2017.10.019_bib23","doi-asserted-by":"crossref","first-page":"1737","DOI":"10.1089\/ars.2006.8.1737","article-title":"Mitochondrial oxidative stress, DNA damage, and heart failure","volume":"8","author":"Tsutsui","year":"2006","journal-title":"Antioxid. Redox Signal."},{"issue":"9","key":"10.1016\/j.redox.2017.10.019_bib24","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1007\/s00204-015-1477-x","article-title":"Pathophysiology of cardiac hypertrophy and heart failure: signaling pathways and novel therapeutic targets","volume":"89","author":"Tham","year":"2015","journal-title":"Arch. Toxicol."},{"issue":"1","key":"10.1016\/j.redox.2017.10.019_bib25","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1210\/en.2007-0877","article-title":"Oxidative stress triggers cardiac fibrosis in the heart of diabetic rats","volume":"149","author":"Aragno","year":"2008","journal-title":"Endocrinology"},{"issue":"3","key":"10.1016\/j.redox.2017.10.019_bib26","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/j.yjmcc.2007.06.010","article-title":"Neutral sphingomyelinase inhibition participates to the benefits of N-acetylcysteine treatment in post-myocardial infarction failing heart rats","volume":"43","author":"Adamy","year":"2007","journal-title":"J. Mol. Cell. Cardiol."},{"issue":"10","key":"10.1016\/j.redox.2017.10.019_bib27","doi-asserted-by":"crossref","first-page":"H1720","DOI":"10.1152\/ajpheart.00339.2015","article-title":"N-acetylcysteine reverses diastolic dysfunction and hypertrophy in familial hypertrophic cardiomyopathy","volume":"309","author":"Wilder","year":"2015","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"10.1016\/j.redox.2017.10.019_bib28","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/1465-9921-15-65","article-title":"N-acetylcysteine improves established monocrotaline-induced pulmonary hypertension in rats","volume":"15","author":"Chaumais","year":"2014","journal-title":"Respir. Res."},{"issue":"7","key":"10.1016\/j.redox.2017.10.019_bib29","doi-asserted-by":"crossref","DOI":"10.14814\/phy2.12757","article-title":"N-acetylcysteine attenuates the development of cardiac fibrosis and remodeling in a mouse model of heart failure","volume":"4","author":"Giam","year":"2016","journal-title":"Physiol. Rep."},{"issue":"2","key":"10.1016\/j.redox.2017.10.019_bib30","doi-asserted-by":"crossref","first-page":"156","DOI":"10.2174\/1389200217666151210124713","article-title":"Therapeutic potential of N-acetylcysteine for wound healing, acute bronchiolitis, and congenital heart defects","volume":"17","author":"AlMatar","year":"2016","journal-title":"Curr. Drug Metab."},{"key":"10.1016\/j.redox.2017.10.019_bib31","first-page":"2","article-title":"Pharmacological treatment of idiopathic pulmonary fibrosis - preclinical and clinical studies of pirfenidone, nintedanib, and N-acetylcysteine","author":"Myll\u00e4rniemi","year":"2015","journal-title":"Eur. Clin. Respir. J."},{"key":"10.1016\/j.redox.2017.10.019_bib32","doi-asserted-by":"crossref","first-page":"R393","DOI":"10.1152\/ajpregu.00584.2012","article-title":"Mitochondrial morphology transitions and functions: implications for retrograde signaling?","volume":"304","author":"Picard","year":"2013","journal-title":"Am. J. Physiol.- Regul., Integr. Comp. Physiol."},{"key":"10.1016\/j.redox.2017.10.019_bib33","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.cmet.2015.06.006","article-title":"Redox Homeostasis and Mitochondrial Dynamics","volume":"22","author":"Willems","year":"2015","journal-title":"Cell Metab."},{"issue":"8","key":"10.1016\/j.redox.2017.10.019_bib34","doi-asserted-by":"crossref","first-page":"4117","DOI":"10.1016\/j.bbagen.2013.04.016","article-title":"The chemistry and biological activities of N-acetylcysteine","volume":"1830","author":"Samuni","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"10.1016\/j.redox.2017.10.019_bib35","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1161\/01.CIR.78.1.202","article-title":"Glutathione redox pathway and reperfusion injury.\u00a0Effect of N-acetylcysteine on infarct size and ventricular function","volume":"78","author":"Forman","year":"1988","journal-title":"Circulation"},{"issue":"6","key":"10.1016\/j.redox.2017.10.019_bib36","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1007\/BF02284964","article-title":"Failure of N-acetylcysteine to reduce low-density lipoprotein oxidizability in healthy subjects","volume":"43","author":"Kleinveld","year":"1992","journal-title":"Eur. J. Clin. Pharmacol."},{"issue":"3","key":"10.1016\/j.redox.2017.10.019_bib37","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1164\/ajrccm.152.3.7663783","article-title":"Intravenous N-acetylcysteine and lung glutathione of patients with pulmonary fibrosis and normals","volume":"152","author":"Meyer","year":"1995","journal-title":"Am. J. Respir. Crit. Care Med."},{"issue":"11","key":"10.1016\/j.redox.2017.10.019_bib38","doi-asserted-by":"crossref","first-page":"2920","DOI":"10.1007\/s00125-012-2685-z","article-title":"N-Acetylcysteine inhibits platelet-monocyte conjugation in patients with type 2 diabetes with depleted intraplatelet glutathione: a randomised controlled trial","volume":"55","author":"Treweeke","year":"2012","journal-title":"Diabetologia"},{"issue":"2","key":"10.1016\/j.redox.2017.10.019_bib39","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.pharmthera.2013.09.006","article-title":"Existing and potential therapeutic uses for N-acetylcysteine: the need for conversion to intracellular glutathione for antioxidant benefits","volume":"141","author":"Rushworth","year":"2014","journal-title":"Pharmacol. Ther."},{"issue":"16\u201317","key":"10.1016\/j.redox.2017.10.019_bib40","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1016\/j.clinbiochem.2015.04.017","article-title":"A review on the possible molecular mechanism of action of N-acetylcysteine against insulin resistance and type-2 diabetes development","volume":"48","author":"Lasram","year":"2015","journal-title":"Clin. Biochem."},{"issue":"2","key":"10.1016\/j.redox.2017.10.019_bib41","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.bbamcr.2008.10.014","article-title":"Attenuation of doxorubicin-induced cardiac injury by mitochondrial glutaredoxin 2","volume":"1793","author":"Diotte","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"issue":"52","key":"10.1016\/j.redox.2017.10.019_bib42","doi-asserted-by":"crossref","first-page":"36125","DOI":"10.1074\/jbc.M114.620047","article-title":"Glutaredoxin 2 (Grx2) gene deletion induces early onset of age-dependent cataracts in mice","volume":"289","author":"Wu","year":"2014","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.redox.2017.10.019_bib43","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1083\/jcb.201511036","article-title":"Metabolic regulation of mitochondrial dynamics","volume":"212","author":"Mishra","year":"2016","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.redox.2017.10.019_bib44","first-page":"129","article-title":"Neutrophil activation, antioxidant supplements and exercise-induced oxidative stress","volume":"10","author":"Peake","year":"2004","journal-title":"Exerc. Immunol. Rev."},{"issue":"6","key":"10.1016\/j.redox.2017.10.019_bib45","doi-asserted-by":"crossref","first-page":"855","DOI":"10.33549\/physiolres.931590","article-title":"The comparison of antioxidant and hematological properties of N-acetylcysteine and alpha-lipoic acid in physically active males","volume":"58","author":"Zembron-Lacny","year":"2009","journal-title":"Physiol. Res."},{"issue":"7","key":"10.1016\/j.redox.2017.10.019_bib46","doi-asserted-by":"crossref","first-page":"1428","DOI":"10.3390\/jcm4071428","article-title":"Mitochondrial glutathione in diabetic nephropathy","volume":"4","author":"Lash","year":"2015","journal-title":"J. Clin. Med."},{"issue":"5","key":"10.1016\/j.redox.2017.10.019_bib47","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/j.febslet.2015.01.027","article-title":"The mitochondrial dicarboxylate and 2-oxoglutarate carriers do not transport glutathione","volume":"589","author":"Booty","year":"2015","journal-title":"FEBS Lett."}],"container-title":["Redox Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231717308066?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231717308066?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T06:05:17Z","timestamp":1761977117000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2213231717308066"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,4]]},"references-count":47,"alternative-id":["S2213231717308066"],"URL":"https:\/\/doi.org\/10.1016\/j.redox.2017.10.019","relation":{},"ISSN":["2213-2317"],"issn-type":[{"value":"2213-2317","type":"print"}],"subject":[],"published":{"date-parts":[[2018,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Glutaredoxin-2 controls cardiac mitochondrial dynamics and energetics in mice, and protects against human cardiac pathologies","name":"articletitle","label":"Article Title"},{"value":"Redox Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.redox.2017.10.019","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}