{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T00:18:50Z","timestamp":1791937130571,"version":"4.3.4"},"reference-count":95,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,5,1]],"date-time":"2020-05-01T00:00:00Z","timestamp":1588291200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,5,1]],"date-time":"2020-05-01T00:00:00Z","timestamp":1588291200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,2,19]],"date-time":"2020-02-19T00:00:00Z","timestamp":1582070400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100008582","name":"McGill University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008582","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":[[2020,5]]},"DOI":"10.1016\/j.redox.2020.101472","type":"journal-article","created":{"date-parts":[[2020,3,7]],"date-time":"2020-03-07T11:42:13Z","timestamp":1583581333000},"page":"101472","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":103,"special_numbering":"C","title":["Protein S-glutathionylation reactions as a global inhibitor of cell metabolism for the desensitization of hydrogen peroxide signals"],"prefix":"10.1016","volume":"32","author":[{"given":"Ryan J.","family":"Mailloux","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"6","key":"10.1016\/j.redox.2020.101472_bib1","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1016\/j.cell.2014.11.034","article-title":"Metabolic inflexibility: when mitochondrial indecision leads to metabolic gridlock","volume":"159","author":"Muoio","year":"2014","journal-title":"Cell"},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib2","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/j.bpj.2012.11.3808","article-title":"Integrating mitochondrial energetics, redox and ROS metabolic networks: a two-compartment model","volume":"104","author":"Kembro","year":"2013","journal-title":"Biophys. J."},{"issue":"31","key":"10.1016\/j.redox.2020.101472_bib3","doi-asserted-by":"crossref","first-page":"4763","DOI":"10.2174\/1381612822666160629070914","article-title":"Application of mitochondria-targeted pharmaceuticals for the treatment of heart disease","volume":"22","author":"Mailloux","year":"2016","journal-title":"Curr. Pharmaceut. Des."},{"issue":"9","key":"10.1016\/j.redox.2020.101472_bib4","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1089\/ars.2015.6247","article-title":"The redox code","volume":"23","author":"Jones","year":"2015","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.redox.2020.101472_bib5","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.redox.2015.12.010","article-title":"Protein S-glutathionlyation links energy metabolism to redox signaling in mitochondria","volume":"8","author":"Mailloux","year":"2016","journal-title":"Redox Biol"},{"issue":"8","key":"10.1016\/j.redox.2020.101472_bib6","doi-asserted-by":"crossref","DOI":"10.3390\/nu11081952","article-title":"Role of glutathionylation in infection and inflammation","volume":"11","author":"Checconi","year":"2019","journal-title":"Nutrients"},{"issue":"15","key":"10.1016\/j.redox.2020.101472_bib7","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1089\/ars.2016.6697","article-title":"Protein thiol redox signaling in monocytes and macrophages","volume":"25","author":"Short","year":"2016","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.redox.2020.101472_bib8","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.cbi.2018.12.003","article-title":"Protein S-glutathionylation: the linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria","volume":"299","author":"Young","year":"2019","journal-title":"Chem. Biol. Interact."},{"issue":"5","key":"10.1016\/j.redox.2020.101472_bib9","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.2337\/db12-0981","article-title":"UCP2 regulates the glucagon response to fasting and starvation","volume":"62","author":"Allister","year":"2013","journal-title":"Diabetes"},{"issue":"11","key":"10.1016\/j.redox.2020.101472_bib10","doi-asserted-by":"crossref","first-page":"2710","DOI":"10.2337\/db11-0132","article-title":"Beta-cell uncoupling protein 2 regulates reactive oxygen species production, which influences both insulin and glucagon secretion","volume":"60","author":"Robson-Doucette","year":"2011","journal-title":"Diabetes"},{"key":"10.1016\/j.redox.2020.101472_bib11","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.abb.2017.01.008","article-title":"The role of sulfenic acids in cellular redox signaling: reconciling chemical kinetics and molecular detection strategies","volume":"616","author":"Heppner","year":"2017","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.redox.2020.101472_bib12","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/j.freeradbiomed.2018.03.038","article-title":"An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation","volume":"120","author":"Zhang","year":"2018","journal-title":"Free Radic. Biol. Med."},{"issue":"42","key":"10.1016\/j.redox.2020.101472_bib13","doi-asserted-by":"crossref","first-page":"11144","DOI":"10.1021\/bi800966v","article-title":"Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles","volume":"47","author":"Gallogly","year":"2008","journal-title":"Biochemistry"},{"issue":"28","key":"10.1016\/j.redox.2020.101472_bib14","doi-asserted-by":"crossref","first-page":"8872","DOI":"10.1021\/ja070410o","article-title":"Redox regulation of protein tyrosine phosphatase 1B (PTP1B): a biomimetic study on the unexpected formation of a sulfenyl amide intermediate","volume":"129","author":"Sarma","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.redox.2020.101472_bib15","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.abb.2016.09.013","article-title":"Protein cysteine oxidation in redox signaling: caveats on sulfenic acid detection and quantification","volume":"617","author":"Forman","year":"2017","journal-title":"Arch. Biochem. Biophys."},{"issue":"46","key":"10.1016\/j.redox.2020.101472_bib16","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":"6","key":"10.1016\/j.redox.2020.101472_bib17","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1089\/ars.2011.4454","article-title":"Posttranslational modification of cysteine in redox signaling and oxidative stress: focus on s-glutathionylation","volume":"16","author":"Mieyal","year":"2012","journal-title":"Antioxidants Redox Signal."},{"issue":"4","key":"10.1016\/j.redox.2020.101472_bib18","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":"2","key":"10.1016\/j.redox.2020.101472_bib19","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.jmb.2018.12.006","article-title":"Molecular mechanisms of glutaredoxin enzymes: versatile hubs for thiol-disulfide exchange between protein thiols and glutathione","volume":"431","author":"Xiao","year":"2019","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.redox.2020.101472_bib20","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/j.redox.2016.12.035","article-title":"Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: oxidative eustress","volume":"11","author":"Sies","year":"2017","journal-title":"Redox Biol"},{"key":"10.1016\/j.redox.2020.101472_bib21","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1007\/978-981-13-8367-0_11","article-title":"Cysteine switches and the regulation of mitochondrial bioenergetics and ROS production","volume":"1158","author":"Mailloux","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"issue":"7","key":"10.1016\/j.redox.2020.101472_bib22","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1517\/17425255.2011.577738","article-title":"Reversible and irreversible protein glutathionylation: biological and clinical aspects","volume":"7","author":"Cooper","year":"2011","journal-title":"Expet Opin. Drug Metabol. Toxicol."},{"key":"10.1016\/j.redox.2020.101472_bib23","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.redox.2013.12.011","article-title":"Redox regulation of mitochondrial function with emphasis on cysteine oxidation reactions","volume":"2","author":"Mailloux","year":"2014","journal-title":"Redox Biol"},{"issue":"11","key":"10.1016\/j.redox.2020.101472_bib24","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1515\/hsz-2017-0160","article-title":"Progress in understanding the molecular oxygen paradox - function of mitochondrial reactive oxygen species in cell signaling","volume":"398","author":"Kuksal","year":"2017","journal-title":"Biol. Chem."},{"issue":"1","key":"10.1016\/j.redox.2020.101472_bib25","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/1759-7714.12148","article-title":"Review of aerobic glycolysis and its key enzymes - new targets for lung cancer therapy","volume":"6","author":"Li","year":"2015","journal-title":"Thorac Cancer"},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib26","first-page":"109","article-title":"Malate-aspartate shuttle mediates the intracellular ATP levels, antioxidation capacity and survival of differentiated PC12 cells","volume":"6","author":"Wang","year":"2014","journal-title":"Int J Physiol Pathophysiol Pharmacol"},{"issue":"4","key":"10.1016\/j.redox.2020.101472_bib27","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/j.cmet.2018.03.008","article-title":"The science and translation of lactate shuttle theory","volume":"27","author":"Brooks","year":"2018","journal-title":"Cell Metabol."},{"issue":"11","key":"10.1016\/j.redox.2020.101472_bib28","doi-asserted-by":"crossref","first-page":"3772","DOI":"10.1039\/c3cp43968b","article-title":"The catalytic mechanism of glyceraldehyde 3-phosphate dehydrogenase from Trypanosoma cruzi elucidated via the QM\/MM approach","volume":"15","author":"Reis","year":"2013","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.redox.2020.101472_bib29","series-title":"Innovative Medicine: Basic Research and Development, Tokyo","first-page":"3","article-title":"Diverting glycolysis to combat oxidative stress","author":"Mullarky","year":"2015"},{"key":"10.1016\/j.redox.2020.101472_bib30","doi-asserted-by":"crossref","first-page":"362","DOI":"10.3389\/fphys.2016.00362","article-title":"High concentrations of H2O2 make aerobic glycolysis energetically more favorable for cellular respiration","volume":"7","author":"Molavian","year":"2016","journal-title":"Front. Physiol."},{"issue":"40","key":"10.1016\/j.redox.2020.101472_bib31","doi-asserted-by":"crossref","first-page":"25010","DOI":"10.1016\/S0021-9258(17)31491-6","article-title":"S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes","volume":"269","author":"Ravichandran","year":"1994","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib32","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/nchembio.1720","article-title":"A proton relay enhances H2O2 sensitivity of GAPDH to facilitate metabolic adaptation","volume":"11","author":"Peralta","year":"2015","journal-title":"Nat. Chem. Biol."},{"issue":"12","key":"10.1016\/j.redox.2020.101472_bib33","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.1016\/j.bbagen.2017.09.008","article-title":"S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase induces formation of C150-C154 intrasubunit disulfide bond in the active site of the enzyme","volume":"1861","author":"Barinova","year":"2017","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.redox.2020.101472_bib34","article-title":"Influence of oxidative stress on catalytic and non-glycolytic functions of glyceraldehyde-3-phosphate dehydrogenase","author":"Muronetz","year":"2018","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.redox.2020.101472_bib35","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0076-6879(02)48636-3","article-title":"S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: role of thiol oxidation and catalysis by glutaredoxin","volume":"348","author":"Cotgreave","year":"2002","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.redox.2020.101472_bib36","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.redox.2018.05.011","article-title":"Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle","volume":"17","author":"Kramer","year":"2018","journal-title":"Redox Biol"},{"issue":"10","key":"10.1016\/j.redox.2020.101472_bib37","doi-asserted-by":"crossref","first-page":"2034","DOI":"10.1074\/mcp.RA118.000875","article-title":"Reactive metabolite-induced protein glutathionylation: a potentially novel mechanism underlying acetaminophen hepatotoxicity","volume":"17","author":"Chan","year":"2018","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.redox.2020.101472_bib38","doi-asserted-by":"crossref","first-page":"101049","DOI":"10.1016\/j.redox.2018.11.007","article-title":"Thioredoxin and glutaredoxin regulate metabolism through different multiplex thiol switches","volume":"21","author":"Lopez-Grueso","year":"2019","journal-title":"Redox Biol"},{"issue":"11","key":"10.1016\/j.redox.2020.101472_bib39","doi-asserted-by":"crossref","first-page":"2855","DOI":"10.1089\/ars.2011.4029","article-title":"Protein S-glutathionylation in malaria parasites","volume":"15","author":"Kehr","year":"2011","journal-title":"Antioxidants Redox Signal."},{"issue":"1","key":"10.1016\/j.redox.2020.101472_bib40","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/0014-5793(83)80494-3","article-title":"An essential role of cytosolic thioltransferase in protection of pyruvate kinase from rabbit liver against oxidative inactivation","volume":"152","author":"Axelsson","year":"1983","journal-title":"FEBS Lett."},{"key":"10.1016\/j.redox.2020.101472_bib41","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1146\/annurev.bi.54.070185.001513","article-title":"Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation","volume":"54","author":"Ziegler","year":"1985","journal-title":"Annu. Rev. Biochem."},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib42","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/0304-4165(88)90161-4","article-title":"S-thiolation of creatine kinase and glycogen phosphorylase b initiated by partially reduced oxygen species","volume":"964","author":"Park","year":"1988","journal-title":"Biochim. Biophys. Acta"},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib43","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/0003-9861(91)90295-T","article-title":"Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions","volume":"284","author":"Chai","year":"1991","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.redox.2020.101472_bib44","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.3389\/fpls.2016.01942","article-title":"Cytosolic triosephosphate isomerase from Arabidopsis thaliana is reversibly modified by glutathione on cysteines 127 and 218","volume":"7","author":"Dumont","year":"2016","journal-title":"Front. Plant Sci."},{"issue":"4","key":"10.1016\/j.redox.2020.101472_bib45","doi-asserted-by":"crossref","first-page":"830","DOI":"10.1016\/j.jmb.2013.11.021","article-title":"PFKFB3 regulates oxidative stress homeostasis via its S-glutathionylation in cancer","volume":"426","author":"Seo","year":"2014","journal-title":"J. Mol. Biol."},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib46","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/0005-2744(80)90087-X","article-title":"General specificity of cytoplasmic thioltransferase (thiol:disulfide oxidoreductase) from rat liver for thiol and disulfide substrates","volume":"613","author":"Axelsson","year":"1980","journal-title":"Biochim. Biophys. Acta"},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib47","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/0003-9861(90)90732-E","article-title":"Phosphorylase and creatine kinase modification by thiol-disulfide exchange and by xanthine oxidase-initiated S-thiolation","volume":"276","author":"Miller","year":"1990","journal-title":"Arch. Biochem. Biophys."},{"issue":"17","key":"10.1016\/j.redox.2020.101472_bib48","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1089\/ars.2018.7715","article-title":"Deletion of the glutaredoxin-2 gene protects mice from diet-induced weight gain, which correlates with increased mitochondrial respiration and proton leaks in skeletal muscle","volume":"31","author":"Young","year":"2019","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.redox.2020.101472_bib49","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.freeradbiomed.2016.10.007","article-title":"Glutaredoxins concomitant with optimal ROS activate AMPK through S-glutathionylation to improve glucose metabolism in type 2 diabetes","volume":"101","author":"Dong","year":"2016","journal-title":"Free Radic. Biol. Med."},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib50","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1042\/BJ20110162","article-title":"Assessing mitochondrial dysfunction in cells","volume":"435","author":"Brand","year":"2011","journal-title":"Biochem. J."},{"issue":"7\u20138","key":"10.1016\/j.redox.2020.101472_bib51","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1016\/j.bbabio.2008.03.014","article-title":"Forty years of Mitchell's proton circuit: from little grey books to little grey cells","volume":"1777","author":"Nicholls","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.redox.2020.101472_bib52","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/j.freeradbiomed.2016.06.014","article-title":"2-Oxoglutarate dehydrogenase is a more significant source of O2(.-)\/H2O2 than pyruvate dehydrogenase in cardiac and liver tissue","volume":"97","author":"Mailloux","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.redox.2020.101472_bib53","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1146\/annurev-biochem-061516-045037","article-title":"Oxidative stress","volume":"86","author":"Sies","year":"2017","journal-title":"Annu. Rev. Biochem."},{"issue":"3","key":"10.1016\/j.redox.2020.101472_bib54","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1093\/geronj\/11.3.298","article-title":"Aging: a theory based on free radical and radiation chemistry","volume":"11","author":"Harman","year":"1956","journal-title":"J. Gerontol."},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib55","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1038\/jcbfm.1983.28","article-title":"Respiratory activity of isolated rat brain mitochondria following in vitro exposure to oxygen radicals","volume":"3","author":"Hillered","year":"1983","journal-title":"J. Cerebr. Blood Flow Metabol."},{"key":"10.1016\/j.redox.2020.101472_bib56","first-page":"235","article-title":"Susceptibility of mitochondrial membranes to calcium and reactive oxygen species: implications for ischemic and toxic tissue damage","volume":"282","author":"Malis","year":"1988","journal-title":"Prog. Clin. Biol. Res."},{"issue":"3","key":"10.1016\/j.redox.2020.101472_bib57","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S0304-3940(99)00593-5","article-title":"Effect of thiol modification on brain mitochondrial complex I activity","volume":"272","author":"Balijepalli","year":"1999","journal-title":"Neurosci. Lett."},{"issue":"11","key":"10.1016\/j.redox.2020.101472_bib58","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1016\/j.chembiol.2015.09.012","article-title":"Development of a clickable probe for profiling of protein glutathionylation in the central cellular metabolism of E. coli and Drosophila","volume":"22","author":"Feng","year":"2015","journal-title":"Chem. Biol."},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib59","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.cmet.2012.07.013","article-title":"The mitochondrial pyruvate carrier: has it been unearthed at last?","volume":"16","author":"Halestrap","year":"2012","journal-title":"Cell Metabol."},{"issue":"16","key":"10.1016\/j.redox.2020.101472_bib60","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.1089\/ars.2017.7311","article-title":"Redox-driven signaling: 2-oxo acid dehydrogenase complexes as sensors and transmitters of metabolic imbalance","volume":"30","author":"Bunik","year":"2019","journal-title":"Antioxidants Redox Signal."},{"issue":"5","key":"10.1016\/j.redox.2020.101472_bib61","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1515\/hsz-2017-0284","article-title":"Generation of superoxide and hydrogen peroxide by side reactions of mitochondrial 2-oxoacid dehydrogenase complexes in isolation and in cells","volume":"399","author":"Bunik","year":"2018","journal-title":"Biol. Chem."},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib62","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1006\/abbi.1996.0560","article-title":"Reactive oxygen species-mediated inactivation of pyruvate dehydrogenase","volume":"336","author":"Tabatabaie","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"issue":"45","key":"10.1016\/j.redox.2020.101472_bib63","doi-asserted-by":"crossref","first-page":"15835","DOI":"10.1021\/bi981512h","article-title":"Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal","volume":"37","author":"Humphries","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.redox.2020.101472_bib64","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1016\/j.freeradbiomed.2013.09.008","article-title":"Mitochondrial glutathione depletion reveals a novel role for the pyruvate dehydrogenase complex as a key H2O2-emitting source under conditions of nutrient overload","volume":"65","author":"Fisher-Wellman","year":"2013","journal-title":"Free Radic. Biol. Med."},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib65","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1042\/BJ20141447","article-title":"Pyruvate dehydrogenase complex and nicotinamide nucleotide transhydrogenase constitute an energy-consuming redox circuit","volume":"467","author":"Fisher-Wellman","year":"2015","journal-title":"Biochem. J."},{"key":"10.1016\/j.redox.2020.101472_bib66","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.freeradbiomed.2017.02.046","article-title":"Protein S-glutathionylation alters superoxide\/hydrogen peroxide emission from pyruvate dehydrogenase complex","volume":"106","author":"O'Brien","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.redox.2020.101472_bib67","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.redox.2017.12.006","article-title":"Characterization of the impact of glutaredoxin-2 (GRX2) deficiency on superoxide\/hydrogen peroxide release from cardiac and liver mitochondria","volume":"15","author":"Chalker","year":"2018","journal-title":"Redox Biol"},{"issue":"3","key":"10.1016\/j.redox.2020.101472_bib68","doi-asserted-by":"crossref","first-page":"581","DOI":"10.2337\/diabetes.52.3.581","article-title":"Glucose toxicity in beta-cells: type 2 diabetes, good radicals gone bad, and the glutathione connection","volume":"52","author":"Robertson","year":"2003","journal-title":"Diabetes"},{"issue":"2","key":"10.1016\/j.redox.2020.101472_bib69","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0192801","article-title":"Protein S-glutathionylation lowers superoxide\/hydrogen peroxide release from skeletal muscle mitochondria through modification of complex I and inhibition of pyruvate uptake","volume":"13","author":"Gill","year":"2018","journal-title":"PloS One"},{"issue":"1\u20133","key":"10.1016\/j.redox.2020.101472_bib70","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1159\/000468779","article-title":"Hepatocyte heterogeneity in the metabolism of amino acids and ammonia","volume":"46","author":"Haussinger","year":"1992","journal-title":"Enzyme"},{"issue":"34","key":"10.1016\/j.redox.2020.101472_bib71","doi-asserted-by":"crossref","first-page":"30409","DOI":"10.1074\/jbc.R200006200","article-title":"The key role of anaplerosis and cataplerosis for citric acid cycle function","volume":"277","author":"Owen","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2020.101472_bib72","doi-asserted-by":"crossref","first-page":"68","DOI":"10.3389\/fcell.2014.00068","article-title":"S-glutathionylation reactions in mitochondrial function and disease","volume":"2","author":"Mailloux","year":"2014","journal-title":"Front Cell Dev Biol"},{"issue":"21","key":"10.1016\/j.redox.2020.101472_bib73","doi-asserted-by":"crossref","first-page":"3342","DOI":"10.1091\/mbc.e14-07-1178","article-title":"The novel component Kgd4 recruits the E3 subunit to the mitochondrial alpha-ketoglutarate dehydrogenase","volume":"25","author":"Heublein","year":"2014","journal-title":"Mol. Biol. Cell"},{"issue":"24","key":"10.1016\/j.redox.2020.101472_bib74","doi-asserted-by":"crossref","first-page":"8972","DOI":"10.1523\/JNEUROSCI.20-24-08972.2000","article-title":"Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress","volume":"20","author":"Tretter","year":"2000","journal-title":"J. Neurosci."},{"issue":"14","key":"10.1016\/j.redox.2020.101472_bib75","doi-asserted-by":"crossref","first-page":"4235","DOI":"10.1021\/bi027370f","article-title":"Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status","volume":"42","author":"Nulton-Persson","year":"2003","journal-title":"Biochemistry"},{"issue":"1464","key":"10.1016\/j.redox.2020.101472_bib76","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1098\/rstb.2005.1764","article-title":"Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress","volume":"360","author":"Tretter","year":"2005","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"issue":"1","key":"10.1016\/j.redox.2020.101472_bib77","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1021\/bi7017464","article-title":"Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid","volume":"47","author":"Applegate","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.redox.2020.101472_bib78","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.freeradbiomed.2013.03.020","article-title":"Glutathionylation of alpha-ketoglutarate dehydrogenase: the chemical nature and relative susceptibility of the cofactor lipoic acid to modification","volume":"61","author":"McLain","year":"2013","journal-title":"Free Radic. Biol. Med."},{"issue":"8","key":"10.1016\/j.redox.2020.101472_bib79","doi-asserted-by":"crossref","first-page":"1960","DOI":"10.1016\/j.bbagen.2017.05.010","article-title":"Examination of the superoxide\/hydrogen peroxide forming and quenching potential of mouse liver mitochondria","volume":"1861","author":"Slade","year":"2017","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"issue":"12","key":"10.1016\/j.redox.2020.101472_bib80","doi-asserted-by":"crossref","first-page":"1265","DOI":"10.1038\/cr.2016.138","article-title":"The mitokine quest(ion)","volume":"26","author":"Deng","year":"2016","journal-title":"Cell Res."},{"issue":"495","key":"10.1016\/j.redox.2020.101472_bib81","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.aaj1978","article-title":"Mitochondrial redox signaling enables repair of injured skeletal muscle cells","volume":"10","author":"Horn","year":"2017","journal-title":"Sci. Signal."},{"key":"10.1016\/j.redox.2020.101472_bib82","doi-asserted-by":"crossref","first-page":"347","DOI":"10.3389\/fphys.2015.00347","article-title":"The measurement of reversible redox dependent post-translational modifications and their regulation of mitochondrial and skeletal muscle function","volume":"6","author":"Kramer","year":"2015","journal-title":"Front. Physiol."},{"key":"10.1016\/j.redox.2020.101472_bib83","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.redox.2016.02.002","article-title":"Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase","volume":"8","author":"Mailloux","year":"2016","journal-title":"Redox Biol"},{"issue":"8","key":"10.1016\/j.redox.2020.101472_bib84","article-title":"Sex-dependent differences in the bioenergetics of liver and muscle mitochondria from mice containing a deletion for glutaredoxin-2","volume":"8","author":"Mallay","year":"2019","journal-title":"Antioxidants (Basel)"},{"issue":"19","key":"10.1016\/j.redox.2020.101472_bib85","doi-asserted-by":"crossref","first-page":"5465","DOI":"10.1021\/bi800303h","article-title":"Regulatory control of human cytosolic branched-chain aminotransferase by oxidation and S-glutathionylation and its interactions with redox sensitive neuronal proteins","volume":"47","author":"Conway","year":"2008","journal-title":"Biochemistry"},{"issue":"1","key":"10.1016\/j.redox.2020.101472_bib86","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20081386","article-title":"How mitochondria produce reactive oxygen species","volume":"417","author":"Murphy","year":"2009","journal-title":"Biochem. J."},{"issue":"36","key":"10.1016\/j.redox.2020.101472_bib87","doi-asserted-by":"crossref","first-page":"11986","DOI":"10.1021\/bi0509393","article-title":"Sites and mechanisms of aconitase inactivation by peroxynitrite: modulation by citrate and glutathione","volume":"44","author":"Han","year":"2005","journal-title":"Biochemistry"},{"issue":"11","key":"10.1016\/j.redox.2020.101472_bib88","doi-asserted-by":"crossref","first-page":"10846","DOI":"10.1074\/jbc.M411306200","article-title":"Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation","volume":"280","author":"Kil","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"21","key":"10.1016\/j.redox.2020.101472_bib89","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."},{"issue":"52","key":"10.1016\/j.redox.2020.101472_bib90","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":"7","key":"10.1016\/j.redox.2020.101472_bib91","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1016\/j.bbabio.2015.12.013","article-title":"Ischemic A\/D transition of mitochondrial complex I and its role in ROS generation","volume":"1857","author":"Drose","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"issue":"45","key":"10.1016\/j.redox.2020.101472_bib92","doi-asserted-by":"crossref","first-page":"32640","DOI":"10.1074\/jbc.M702294200","article-title":"Mitochondrial complex II in the post-ischemic heart: oxidative injury and the role of protein S-glutathionylation","volume":"282","author":"Chen","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"7527","key":"10.1016\/j.redox.2020.101472_bib93","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1038\/nature13909","article-title":"Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS","volume":"515","author":"Chouchani","year":"2014","journal-title":"Nature"},{"issue":"256","key":"10.1016\/j.redox.2020.101472_bib94","doi-asserted-by":"crossref","first-page":"rs1","DOI":"10.1126\/scisignal.2003252","article-title":"Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation","volume":"6","author":"Doulias","year":"2013","journal-title":"Sci. Signal."},{"issue":"11","key":"10.1016\/j.redox.2020.101472_bib95","doi-asserted-by":"crossref","first-page":"5299","DOI":"10.1016\/j.bbagen.2013.08.003","article-title":"Glutathione controls the redox state of the mitochondrial carnitine\/acylcarnitine carrier Cys residues by glutathionylation","volume":"1830","author":"Giangregorio","year":"2013","journal-title":"Biochim. Biophys. Acta"}],"container-title":["Redox Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231719315034?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231719315034?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T06:12:24Z","timestamp":1761977544000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2213231719315034"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,5]]},"references-count":95,"alternative-id":["S2213231719315034"],"URL":"https:\/\/doi.org\/10.1016\/j.redox.2020.101472","relation":{},"ISSN":["2213-2317"],"issn-type":[{"value":"2213-2317","type":"print"}],"subject":[],"published":{"date-parts":[[2020,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Protein S-glutathionylation reactions as a global inhibitor of cell metabolism for the desensitization of hydrogen peroxide signals","name":"articletitle","label":"Article Title"},{"value":"Redox Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.redox.2020.101472","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"101472"}}