{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T19:12:55Z","timestamp":1791141175202,"version":"4.1.0"},"reference-count":157,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2013,10,17]],"date-time":"2013-10-17T00:00:00Z","timestamp":1381968000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The perturbation of thiol-disulfide homeostasis is an important consequence of many diseases, with redox signals implicated in several physio-pathological processes. A prevalent form of cysteine modification is the reversible formation of protein mixed disulfides with glutathione (S-glutathionylation). The abundance of glutathione in cells and the ready conversion of sulfenic acids to S-glutathione mixed disulfides supports the reversible protein S-glutathionylation as a common feature of redox signal transduction, able to regulate the activities of several redox sensitive proteins. In particular, protein  S-glutathionylation is emerging as a critical signaling mechanism in cardiovascular diseases, because it regulates numerous physiological processes involved in cardiovascular homeostasis, including myocyte contraction, oxidative phosphorylation, protein synthesis, vasodilation, glycolytic metabolism and response to insulin. Thus, perturbations in protein glutathionylation status may contribute to the etiology of many cardiovascular diseases, such as myocardial infarction, cardiac hypertrophy and atherosclerosis. Various reports show the importance of oxidative cysteine modifications in modulating cardiovascular function. In this review, we illustrate tools and strategies to monitor protein  S-glutathionylation and describe the proteins so far identified as glutathionylated in myocardial contraction, hypertrophy and inflammation.<\/jats:p>","DOI":"10.3390\/ijms141020845","type":"journal-article","created":{"date-parts":[[2013,10,17]],"date-time":"2013-10-17T13:39:40Z","timestamp":1382017180000},"page":"20845-20876","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":87,"title":["Protein Glutathionylation in Cardiovascular Diseases"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0990-9419","authenticated-orcid":false,"given":"Anna","family":"Pastore","sequence":"first","affiliation":[{"name":"Laboratory of Biochemistry, Bambino Ges\u00f9 Children's Hospital, IRCCS, 00165 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1825-9347","authenticated-orcid":false,"given":"Fiorella","family":"Piemonte","sequence":"additional","affiliation":[{"name":"Unit of Neuromuscular and Neurodegenerative Diseases, Bambino Ges\u00f9 Children's Hospital, IRCCS, 00165 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2013,10,17]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"259","DOI":"10.4161\/oxim.2.5.9441","article-title":"Oxidative stress as a mediator of cardiovascular disease","volume":"2","author":"Elahi","year":"2009","journal-title":"Oxid. Med. Cell Longev"},{"key":"ref_2","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"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1089\/ars.2011.4336","article-title":"Regulation of cell physiology and pathology by protein S-glutathionylation: Lessons learned from the cardiovascular system","volume":"16","author":"Pimentel","year":"2012","journal-title":"Antioxid. Redox Signal"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1089\/ars.2012.4706","article-title":"Cardiovascular redox and ox stress proteomics","volume":"17","author":"Kumar","year":"2012","journal-title":"Antioxid. Redox Signal"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1920","DOI":"10.1089\/ars.2012.4926","article-title":"The role of redox signaling in epigenetics and cardiovascular disease","volume":"18","author":"Kim","year":"2013","journal-title":"Antioxid. Redox Signal"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1006\/jmcc.2002.2108","article-title":"Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion","volume":"34","author":"Eaton","year":"2002","journal-title":"J. Mol. Cell. Cardiol"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"C719","DOI":"10.1152\/ajpcell.00419.2005","article-title":"Decline of contractility during ischemia-reperfusion injury: Actin glutathionylation and its effect on allosteric interaction with tropomyosin","volume":"290","author":"Chen","year":"2006","journal-title":"Am. J. Physiol. Cell. Physiol"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"47763","DOI":"10.1074\/jbc.C100415200","article-title":"Reversible glutathionylation regulates actin polymerization in A431 cells","volume":"276","author":"Wang","year":"2001","journal-title":"J. Biol. Chem"},{"key":"ref_9","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"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.yjmcc.2007.08.022","article-title":"Role of glutaredoxin-1 in cardioprotection: An insight with Glrx1 transgenic and knockout animals","volume":"44","author":"Malik","year":"2008","journal-title":"J. Mol. Cell Cardiol"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.yjmcc.2007.08.021","article-title":"Overexpression of glutaredoxin-2 reduces myocardial cell death by preventing both apoptosis and necrosis","volume":"44","author":"Nagy","year":"2008","journal-title":"J. Mol. Cell Cardiol"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1021\/jf0728146","article-title":"Broccoli: A unique vegetable that protects mammalian hearts through the redox cycling of the thioredoxin superfamily","volume":"56","author":"Mukherjee","year":"2008","journal-title":"J. Agric. Food Chem"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"19603","DOI":"10.1074\/jbc.M209359200","article-title":"Reversible glutathionylation of Complex I increases mitochondrial superoxide formation","volume":"278","author":"Taylor","year":"2003","journal-title":"J. Biol. Chem"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1038\/nrm1983","article-title":"Regulation of cardiac hypertrophy by intracellular signalling pathways","volume":"7","author":"Heineke","year":"2006","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/j.yjmcc.2006.05.009","article-title":"Strain-stimulated hypertrophy in cardiac myocytes is mediated by reactive oxygen species-dependent Ras S-glutathiolation","volume":"41","author":"Pimentel","year":"2006","journal-title":"J. Mol. Cell Cardiol"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1791","DOI":"10.1089\/ars.2006.8.1791","article-title":"Redox-sensitive kinases of the nuclear factor-kB signaling pathway","volume":"8","author":"Pantano","year":"2006","journal-title":"Antioxid. Redox Signal"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/j.freeradbiomed.2006.05.029","article-title":"Molecular mechanism of glutathione-mediated protection from oxidized low-density lipoprotein-induced cell injury in human macrophages: Role of glutathione reductase and glutaredoxin","volume":"41","author":"Wang","year":"2006","journal-title":"Free Radic. Biol. Med"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1483","DOI":"10.1161\/hq0901.095550","article-title":"Expression of glutaredoxin in human coronary arteries: Its potential role in antioxidant protection against atherosclerosis","volume":"21","author":"Okuda","year":"2001","journal-title":"Arterioscler. Thromb. Vasc. Biol"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1055\/s-2004-861509","article-title":"Pathobiology of atherosclerosis\u2014A brief review","volume":"30","author":"Kher","year":"2004","journal-title":"Semin. Thromb. Hemost"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1253\/circj.71.100","article-title":"Serum levels of S-glutathionylated proteins as a risk marker for arteriosclerosis obliterans","volume":"71","author":"Nonaka","year":"2007","journal-title":"Circ. J"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1038\/nm1119","article-title":"S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide","volume":"10","author":"Adachi","year":"2004","journal-title":"Nat. Med"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"29857","DOI":"10.1074\/jbc.M313320200","article-title":"S-glutathiolation of Ras mediates redox-sensitive signaling by Angiotensin ii in vascular smooth muscle cells","volume":"279","author":"Adachi","year":"2004","journal-title":"J. Biol. Chem"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1161\/01.HYP.0000032100.23772.98","article-title":"Role of p47(phox) in vascular oxidative stress and hypertension caused by angiotensin II","volume":"40","author":"Landmesser","year":"2002","journal-title":"Hypertension"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1161\/hh0901.089987","article-title":"Role of NADPH oxidase in the vascular hypertrophic and oxidative stress response to angiotensin II in mice","volume":"88","author":"Wang","year":"2001","journal-title":"Circ. Res"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1096\/fj.05-4875fje","article-title":"S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells","volume":"20","author":"Clavreul","year":"2006","journal-title":"FASEB J"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1161\/ATVBAHA.107.144659","article-title":"Glutaredoxin mediates Akt and eNOS activation by flow in a glutathione reductase dependent manner","volume":"27","author":"Wang","year":"2007","journal-title":"Arterioscler. Thromb. Vasc.Biol"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1080\/08941930701366471","article-title":"Akt in ischemia and reperfusion","volume":"20","author":"Mullonkal","year":"2007","journal-title":"J. Invest. Surg"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1132","DOI":"10.1136\/ard.2006.063867","article-title":"What effects might anti-TNFalpha treatment be expected to have on cardiovascular morbidity and mortality in rheumatoid arthritis? A review of the role of TNFalpha in cardiovascular pathophysiology","volume":"66","author":"Dixon","year":"2007","journal-title":"Ann. Rheum. Dis"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1161\/01.RES.0000256089.30318.20","article-title":"Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: Key role for glutaredoxin in the death pathway","volume":"100","author":"Pan","year":"2007","journal-title":"Circ. Res"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/0076-6879(95)51145-8","article-title":"Analysis of cells and tissues for S-thiolation of specific proteins","volume":"251","author":"Thomas","year":"1995","journal-title":"Methods Enzymol"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1089\/ars.2007.1716","article-title":"Molecular mechanisms and potential clinical significance of S-glutathionylation","volume":"10","author":"Milzani","year":"2008","journal-title":"Antioxid. Redox Signal"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Lu, J., and Holmgren, A (2013). The thioredoxin antioxidant system. Free Radic. Biol. Med, in press.","DOI":"10.1016\/j.freeradbiomed.2013.07.036"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"6800","DOI":"10.1158\/0008-5472.CAN-06-0484","article-title":"A novel role for human sulfiredoxin in the reversal of glutathionylation","volume":"66","author":"Findlay","year":"2006","journal-title":"Cancer Res"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"25769","DOI":"10.1074\/jbc.M113.487785","article-title":"A role for glutathione transferase omega 1 (GSTO1\u20131) in the glutathionylation cycle","volume":"288","author":"Menon","year":"2013","journal-title":"J. Biol. Chem"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.cbpa.2010.10.016","article-title":"Redox platforms in cancer drug discovery and development","volume":"15","author":"Tew","year":"2011","journal-title":"Curr. Opin. Chem. Biol"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"10153","DOI":"10.1073\/pnas.1221210110","article-title":"Top-down proteomics reveals a unique protein S-thiolation switch in Salmonella Typhimurium in response to infection-like conditions","volume":"25","author":"Ansong","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1074\/jbc.M805586200","article-title":"Novel role for glutathione S-transferase pi. Regulator of protein S-Glutathionylation following oxidative and nitrosative stress","volume":"284","author":"Townsend","year":"2009","journal-title":"J. Biol. Chem"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Pastore, A., Martinelli, D., Piemonte, F., Tozzi, G., Boenzi, S., Di Giovamberardino, G., Petrillo, S., Bertini, E., and Dionisi-Vici, C (2013). Glutathione metabolism in cobalamin deficiency type C (cblC). J. Inherit. Metab. Dis, in press.","DOI":"10.1007\/s10545-013-9605-3"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/j.ymgme.2013.05.009","article-title":"Glutathione imbalance in patients with X-linked adrenoleukodystrophy","volume":"109","author":"Petrillo","year":"2013","journal-title":"Mol. Genet. Metab"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.ymgme.2013.03.011","article-title":"Glutathione: A redox signature in monitoring EPI-743 therapy in children with mitochondrial encephalomyopathies","volume":"109","author":"Pastore","year":"2013","journal-title":"Mol. Genet. Metab"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.ab.2012.10.009","article-title":"A fluorometric method to quantify protein glutathionylation using glutathione derivatization with 2,3-naphthalenedicarboxaldehyde","volume":"433","author":"Menon","year":"2013","journal-title":"Anal. Biochem"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1006\/bbrc.1998.8695","article-title":"Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: Catalysis by glutaredoxin","volume":"247","author":"Lind","year":"1998","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"10319","DOI":"10.1021\/bi000781g","article-title":"Oxidant-induced S-glutathiolation inactivates protein kinase C-alpha (PKC-alpha): A potential mechanism of PKC isozyme regulation","volume":"39","author":"Ward","year":"2000","journal-title":"Biochemistry"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"3780","DOI":"10.1073\/pnas.0400181101","article-title":"Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST","volume":"101","author":"Manevich","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"26473","DOI":"10.1074\/jbc.M600451200","article-title":"A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation","volume":"281","author":"Hidalgo","year":"2006","journal-title":"J. Biol. Chem"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"260","DOI":"10.4049\/jimmunol.147.1.260","article-title":"Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages","volume":"147","author":"Rokutan","year":"1991","journal-title":"J. Immunol"},{"key":"ref_47","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"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1973","DOI":"10.4049\/jimmunol.156.5.1973","article-title":"Protein S-thiolation and dethiolation during the respiratory burst in human monocytes: A reversible post-translational modification with potential for buffer ring the effects of oxidant stress","volume":"156","author":"Seres","year":"1996","journal-title":"J. Immunol"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"3505","DOI":"10.1073\/pnas.052592699","article-title":"Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes","volume":"99","author":"Fratelli","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1074\/mcp.M500212-MCP200","article-title":"The utility of N,N-biotinyl glutathione disulfide in the study of protein S-glutathiolation","volume":"5","author":"Brennan","year":"2006","journal-title":"Mol. Cell. Proteomics"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"13086","DOI":"10.1073\/pnas.0603290103","article-title":"Dynamic redox control of NF-kappaB through glutaredoxin regulated S-glutathionylation of inhibitory kappaB kinase beta","volume":"103","author":"Reynaert","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/S0891-5849(02)01182-6","article-title":"Reversible S-glutathionylation of Cys374 regulates actin filament formation by inducing structural changes in the actin molecule","volume":"34","author":"Giustarini","year":"2003","journal-title":"Free Radic. Biol. Med"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"5103","DOI":"10.1073\/pnas.0931345100","article-title":"Stable and controllable RNA interference: Investigating the physiological function of glutathionylated actin","volume":"100","author":"Wang","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"42588","DOI":"10.1074\/jbc.M301872200","article-title":"Actin glutathionylation increases in fibroblasts of patients with Friedreich\u2019s ataxia: A potential role in the pathogenesis of the disease","volume":"43","author":"Pastore","year":"2003","journal-title":"J. Biol. Chem"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"22983","DOI":"10.1074\/jbc.M603040200","article-title":"Redox regulation of beta-actin during integrin-mediated cell adhesion","volume":"281","author":"Fiaschi","year":"2006","journal-title":"J. Biol. Chem"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1002\/jnr.20729","article-title":"Protein glutathionylation in human central nervous system: Potential role in redox regulation of neuronal defense against free radicals","volume":"83","author":"Sparaco","year":"2006","journal-title":"J. Neurosci. Res"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1002\/cm.20425","article-title":"Susceptibility of isolated myofibrils to in vitro glutathionylation: potential relevance to muscle functions","volume":"67","author":"Passarelli","year":"2010","journal-title":"Cytoskeleton"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1007\/s10974-008-9145-x","article-title":"Myosin as a potential redox-sensor: An in vitro study","volume":"29","author":"Passarelli","year":"2008","journal-title":"J. Muscle Res. Cell. Motil"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.bbrc.2004.08.065","article-title":"Redox modulation of tau and microtubule-associated protein-2 by the glutathione\/glutaredoxin reductase system","volume":"323","author":"Landino","year":"2004","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"ref_60","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":"ref_61","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/j.exer.2004.02.001","article-title":"Protein S-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone","volume":"78","author":"Hoppe","year":"2004","journal-title":"Exp. Eye Res"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1096\/fj.06-5843fje","article-title":"Protein glutathiolation by nitric oxide: An intracellular mechanism regulating redox protein modification","volume":"20","author":"West","year":"2006","journal-title":"FASEB J"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1089\/ars.2005.7.870","article-title":"Effects of S-glutathionylation and S-nitrosylation on calmodulin binding to triads and FKBP12 binding to type 1 calcium release channels","volume":"7","author":"Aracena","year":"2005","journal-title":"Antioxid. Redox Signal"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"40354","DOI":"10.1074\/jbc.M600876200","article-title":"Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in RyR1","volume":"281","author":"Goonasekera","year":"2006","journal-title":"J. Biol. Chem"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1042\/bj20031367","article-title":"The identification of a reaction site of glutathione mixed-disulphide formation on cS-crystallin in human lens","volume":"379","author":"Craghill","year":"2004","journal-title":"Biochem. J"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1002\/jnr.21275","article-title":"An increase in S-glutathionylated proteins in the Alzheimer\u2019s disease inferior parietal lobule, a proteomics approach","volume":"85","author":"Newman","year":"2007","journal-title":"J. Neurosci. Res"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1124\/mol.105.018523","article-title":"A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with Sglutathionylation of proteins","volume":"69","author":"Townsend","year":"2006","journal-title":"Mol. Pharmacol"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"9208","DOI":"10.1021\/jp030556j","article-title":"Conformational analysis of glutathione in aqueous solution with molecular dynamics","volume":"107","author":"Lampela","year":"2003","journal-title":"J. Phys. Chem. A"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/nmeth.2369","article-title":"Proteoform: A single term describing protein complexity","volume":"10","author":"Smith","year":"2013","journal-title":"Nat. Methods"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.abb.2005.10.013","article-title":"S-thiolation mimicry: Quantitative and kinetic analysis of redox status of protein cysteines by glutathione-affinity chromatography","volume":"444","author":"Niture","year":"2005","journal-title":"Arch. Biochem. Biophys"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"7765","DOI":"10.1021\/bi700425y","article-title":"Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress","volume":"46","author":"Velu","year":"2007","journal-title":"Biochemistry"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/S0378-4347(99)00139-5","article-title":"Determination of glutathionyl hemoglobin in hemodialysis patients using electrospray ionization liquid chromatography-mass spectrometry","volume":"731","author":"Naito","year":"1999","journal-title":"J. Chromatogr. B"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0003-2697(02)00500-6","article-title":"Determination of glutathionyl-hemoglobin in human erythrocytes by cation-exchange high-performance liquid chromatography","volume":"312","author":"Pastore","year":"2003","journal-title":"Anal. Biochem"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"e55512","DOI":"10.1371\/journal.pone.0055512","article-title":"Prediction of S-glutathionylation sites based on protein sequences","volume":"8","author":"Sun","year":"2013","journal-title":"PLoS One"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1016\/j.yjmcc.2005.08.010","article-title":"Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle","volume":"39","author":"Sanchez","year":"2005","journal-title":"J. Mol. Cell Cardiol"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1093\/cvr\/cvm011","article-title":"Exercise and tachycardia increase NADPH oxidase and ryanodine receptor-2 activity: Possible role in cardioprotection","volume":"77","author":"Sanchez","year":"2008","journal-title":"Cardiovasc. Res"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1161\/HYPERTENSIONAHA.107.100214","article-title":"Apocynin is not an inhibitor of vascular NADPH oxidases but an antioxidant","volume":"51","author":"Heumuller","year":"2008","journal-title":"Hypertension"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"553","DOI":"10.2741\/3705","article-title":"Modulation of cardiac ryanodine receptor activity by ROS and RNS","volume":"16","author":"Donoso","year":"2011","journal-title":"Front. Biosci"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.ceca.2005.06.033","article-title":"Modulating sarco(endo)plasmic reticulum Ca2+ ATPase 2 (SERCA2) activity: Cell biological implications","volume":"38","author":"Vangheluwe","year":"2005","journal-title":"Cell Calcium"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/S0143-4160(03)00126-X","article-title":"Ca2+ transport ATPase isoforms SERCA2a and SERCA2b are targeted to the same sites in the murine heart","volume":"34","author":"Vangheluwe","year":"2003","journal-title":"Cell Calcium"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.tcm.2006.02.001","article-title":"Nitric-oxide-induced vasodilatation: Regulation by physiologic S-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase","volume":"16","author":"Cohen","year":"2006","journal-title":"Trends Cardiovasc. Med"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1152\/ajpheart.01073.2010","article-title":"Effect of protein S-glutathionylation on Ca2+ homeostasis in cultured aortic endothelial cells","volume":"300","author":"Lock","year":"2011","journal-title":"Am. J. Physiol. Heart Circ. Physiol"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1161\/CIRCRESAHA.108.188441","article-title":"Nitroxyl activates SERCA in cardiac myocytes via glutathiolation of cysteine 674","volume":"104","author":"Lancel","year":"2009","journal-title":"Circ. Res"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1038\/nature09599","article-title":"S-glutathionylation uncouples eNOS and regulates its cellular and vascular function","volume":"468","author":"Chen","year":"2010","journal-title":"Nature"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1089\/ars.2011.3904","article-title":"S-glutathionylation reshapes our understanding of endothelial nitric oxide synthase uncoupling and nitric oxide\/reactive oxygen species-mediated signaling","volume":"14","author":"Zweier","year":"2011","journal-title":"Antioxid. Redox Signal"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1146\/annurev.biochem.71.102201.141218","article-title":"Biochemistry of Na, K-ATPase","volume":"71","author":"Kaplan","year":"2002","journal-title":"Annu. Rev.Biochem"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"2999","DOI":"10.1113\/jphysiol.2013.252817","article-title":"Protein kinase-dependent oxidative regulation of the cardiac Na+-K+ pump: Evidence from in vivo and in vitro modulation of cell signaling","volume":"591","author":"Galougahi","year":"2013","journal-title":"J. Physiol"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1146\/annurev.physiol.65.092101.142558","article-title":"Structure and mechanism of Na, K-ATPase: Functional sites and their interactions","volume":"65","author":"Jorgensen","year":"2003","journal-title":"Annu. Rev. Physiol"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"874","DOI":"10.1016\/S0008-6363(02)00841-6","article-title":"[Na+], handling in the failing human heart","volume":"57","author":"Pieske","year":"2003","journal-title":"Cardiovasc. Res"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1016\/S0008-6363(02)00735-6","article-title":"Intracellular Na in animal models of hypertrophy and heart failure: Contractile function and arrhythmogenesis","volume":"57","author":"Pogwizd","year":"2003","journal-title":"Cardiovasc. Res"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.tcm.2010.06.002","article-title":"Reversible oxidative modification: Implications for cardiovascular physiology and pathophysiology","volume":"20","author":"Rasmussen","year":"2010","journal-title":"Trends Cardiovasc. Med"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"34190","DOI":"10.1074\/jbc.273.51.34190","article-title":"Specific Cu2+-catalyzed oxidative cleavage of Na, K-ATPase at the extracellular surface","volume":"273","author":"Shimon","year":"1998","journal-title":"J. Biol. Chem"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1161\/CIRCRESAHA.111.300408","article-title":"Oxidative regulation of the Na+ -K+ pump in cardiac physiology and pathology: Clarifying the published evidence","volume":"112","author":"Figtree","year":"2013","journal-title":"Circ. Res"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"12353","DOI":"10.1074\/jbc.M112.340893","article-title":"Susceptibility of \u03b21 Na+-K+ pump subunit to glutathionylation and oxidative inhibition depends on conformational state of pump","volume":"287","author":"Liu","year":"2012","journal-title":"J. Biol. Chem"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1038\/nature06419","article-title":"Crystal structure of the sodium-potassium pump","volume":"450","author":"Morth","year":"2007","journal-title":"Nature"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1038\/nature07939","article-title":"Crystal structure of the sodium-potassium pump at 2.4 A resolution","volume":"459","author":"Shinoda","year":"2009","journal-title":"Nature"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1038\/nrm3031","article-title":"A structural overview of the plasma membrane Na+, K+-ATPase and H+ATPase ion pumps","volume":"12","author":"Morth","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"36338","DOI":"10.1074\/jbc.M604788200","article-title":"Fluorometric measurements of intermolecular distances between the alpha- and beta-subunits of the Na+\/K+-ATPase","volume":"281","author":"Dempski","year":"2006","journal-title":"J. Biol. Chem"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1016\/j.freeradbiomed.2013.06.040","article-title":"Oxidative inhibition of the vascular Na(+)-K(+) pump via NADPH oxidase-dependent \u03b2(1)-subunit glutathionylation: Implications for angiotensin II-induced vascular dysfunction","volume":"65","author":"Liu","year":"2013","journal-title":"Free Radic. Biol. Med"},{"key":"ref_100","first-page":"26","article-title":"Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary","volume":"8","author":"Johansson","year":"2007","journal-title":"Biochemistry"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1016\/S0891-5849(03)00504-5","article-title":"Actin S-glutathionylation: Evidence against a thiol-disulphide exchange mechanism","volume":"35","author":"Rossi","year":"2003","journal-title":"Free Rad. Biol. Med"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"7533","DOI":"10.1021\/bi900669m","article-title":"Impact of actin glutathionylation on the actomyosin-S1 ATPase","volume":"48","author":"Pizarro","year":"2009","journal-title":"Biochemistry"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1161\/CIRCRESAHA.111.258251","article-title":"Ranolazine improves cardiac diastolic dysfunction through modulation of myofilament calcium sensitivity","volume":"110","author":"Lovelock","year":"2012","journal-title":"Circ. Res"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1161\/CIRCRESAHA.110.231670","article-title":"In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament","volume":"108","author":"Harris","year":"2011","journal-title":"Circ. Res"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1113\/jphysiol.2011.224535","article-title":"S-glutathionylation of troponin I (fast) increases contractile apparatus Ca2+ sensitivity in fast-twitch muscle fibres of rats and humans","volume":"590","author":"Mollica","year":"2012","journal-title":"J. Physiol"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"2549","DOI":"10.1016\/S0021-9258(18)34959-7","article-title":"Proximity of sulfhydryl groups to the sites of interaction between components of the troponin complex from rabbit skeletal muscle","volume":"257","author":"Chong","year":"1982","journal-title":"J. Biol. Chem"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1152\/physrev.00015.2007","article-title":"Skeletal muscle fatigue: Cellular mechanisms","volume":"88","author":"Allen","year":"2008","journal-title":"Physiol. Rev"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1113\/jphysiol.2010.200451","article-title":"Modulation of contractile apparatus Ca2+ sensitivity and disruption of excitation-contraction coupling by S-nitrosoglutathione in rat muscle fibres","volume":"589","author":"Dutka","year":"2011","journal-title":"J. Physiol"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.abb.2011.01.017","article-title":"Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle","volume":"510","author":"Stull","year":"2011","journal-title":"Arch. Biochem. Biophys"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1111\/j.1469-7793.1998.565bn.x","article-title":"Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse","volume":"509","author":"Andrade","year":"1998","journal-title":"J. Physiol"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1113\/jphysiol.2010.199059","article-title":"Acute effects of reactive oxygen and nitrogen species on the contractile function of skeletal muscle","volume":"589","author":"Lamb","year":"2011","journal-title":"J. Physiol"},{"key":"ref_112","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"},{"key":"ref_113","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","volume":"283","author":"Hurd","year":"2008","journal-title":"J. Biol. Chem"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1016\/j.freeradbiomed.2012.05.025","article-title":"Protein thiyl radical mediates S-glutathionylation of complex I","volume":"53","author":"Kang","year":"2012","journal-title":"Free Radic. Biol. Med"},{"key":"ref_115","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"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1016\/j.bbabio.2008.04.005","article-title":"Mammalian Complex I: A regulable and vulnerable pacemaker in mitochondrial respiratory function","volume":"1777","author":"Papa","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/978-1-62703-386-2_12","article-title":"Oxidative modifications of mitochondria complex II","volume":"1005","author":"Zhang","year":"2013","journal-title":"Methods Mol. Biol"},{"key":"ref_118","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":"ref_119","doi-asserted-by":"crossref","first-page":"3374","DOI":"10.1073\/pnas.0712145105","article-title":"A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy","volume":"105","author":"Lee","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1089\/ars.2010.3251","article-title":"Redox regulation of sirtuin-1 by Sglutathiolation","volume":"13","author":"Zee","year":"2010","journal-title":"Antioxid. Redox Signal"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"3145","DOI":"10.1096\/fj.09-151308","article-title":"SIRT1 is a redox sensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress","volume":"24","author":"Caito","year":"2010","journal-title":"FASEB J"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1210\/er.2004-0028","article-title":"Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options","volume":"26","author":"Srivastava","year":"2005","journal-title":"Endocr. Rev"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/j.cbi.2011.02.023","article-title":"Aldose reductase inhibition suppresses oxidative stress induced inflammatory disorders","volume":"191","author":"Srivastava","year":"2011","journal-title":"Chem. Biol. Interact"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.1161\/01.ATV.20.7.1745","article-title":"Involvement of aldose reductase in vascular smooth muscle cell growth and lesion formation after arterial injury","volume":"20","author":"Ruef","year":"2000","journal-title":"Arterioscler. Thromb. Vasc. Biol"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"7993","DOI":"10.1074\/jbc.274.12.7993","article-title":"Osmotic response element is required for the induction of aldose reductase by tumor necrosis factor-alpha","volume":"274","author":"Iwata","year":"1999","journal-title":"J. Biol. Chem"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1096\/fj.04-1650com","article-title":"Inhibition of aldose reductase attenuates TNF-alpha-induced expression of adhesion molecules in endothelial cells","volume":"18","author":"Ramana","year":"2004","journal-title":"FASEB J"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"33539","DOI":"10.1074\/jbc.271.52.33539","article-title":"Specifically targeted modification of human aldose reductase by physiological disulfides","volume":"271","author":"Cappiello","year":"1996","journal-title":"J. Biol. Chem"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1007\/978-1-4615-2904-0_29","article-title":"Cys298 is responsible for reversible thiol-induced variation in aldose reductase activity","volume":"328","author":"Bohren","year":"1993","journal-title":"Adv. Exp. Med. Biol"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/0167-4838(93)90258-S","article-title":"Identification of the reactive cysteine residue in human placenta aldose reductase","volume":"1164","author":"Liu","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S0009-2797(00)00286-6","article-title":"Modulation of aldose reductase activity through S-thiolation by physiological thiols","volume":"130\u2013132","author":"Cappiello","year":"2001","journal-title":"Chem. Biol. Interact"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"4371","DOI":"10.1210\/en.2007-0512","article-title":"Aldose reductase-regulated tumor necrosis factor-alpha production is essential for high glucoseinduced vascular smooth muscle cell growth","volume":"148","author":"Ramana","year":"2007","journal-title":"Endocrinology"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"15110","DOI":"10.1074\/jbc.M600837200","article-title":"Redox activation of aldose reductase in the ischemic heart","volume":"281","author":"Kaiserova","year":"2006","journal-title":"J. Biol. Chem"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"9101","DOI":"10.1074\/jbc.M709671200","article-title":"Role of nitric oxide in regulating aldose reductase activation in the ischemic heart","volume":"283","author":"Kaiserova","year":"2008","journal-title":"J. Biol. Chem"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"14704","DOI":"10.1016\/S0021-9258(18)66928-5","article-title":"Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization","volume":"261","author":"Garel","year":"1986","journal-title":"J. Biol. Chem"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"14710","DOI":"10.1016\/S0021-9258(18)66929-7","article-title":"Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in NMR spectra","volume":"261","author":"Craescu","year":"1986","journal-title":"J. Biol. Chem"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.abb.2003.10.012","article-title":"Different types of glutathionylation of hemoglobin can exist in intact erythrocytes","volume":"421","author":"Mawatari","year":"2004","journal-title":"Arch. Biochem. Biophys"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"3456","DOI":"10.1016\/j.jchromb.2009.05.020","article-title":"Hemoglobin glutathionylation can occur through cysteine sulfenic acid intermediate: Electrospray ionization LTQ-Orbitrap hybrid mass spectrometry studies","volume":"877","author":"Regazzoni","year":"2009","journal-title":"J. Chromatogr. B"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Metere, A., Iorio, E., Scorza, G., Camerini, S., Casella, M., Crescenzi, M., Minetti, M., and Pietraforte, D (2013). Carbon monoxide signaling in human red blood cells: evidence for pentose phosphate pathway activation and protein deglutathionylation. Antioxid. Redox Signal, in press.","DOI":"10.1089\/ars.2012.5102"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1172\/JCI119631","article-title":"Low concentrations of nitric oxide increase oxygen affinity of sickle erythrocytes in vitro and in vivo","volume":"100","author":"Head","year":"1997","journal-title":"J. Clin. Invest."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/380221a0","article-title":"S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control","volume":"380","author":"Jia","year":"1996","journal-title":"Nature"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1146\/annurev.physiol.67.060603.090918","article-title":"Chemical physiology of blood flow regulation by red blood cells: The role of nitric oxide and S-nitrosohemoglobin","volume":"67","author":"Singel","year":"2005","journal-title":"Annu. Rev. Physiol"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.jchromb.2006.12.029","article-title":"Protein glutathionylation and oxidative stress","volume":"855","author":"Niwa","year":"2007","journal-title":"J. Chromatogr. B"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/j.freeradbiomed.2006.12.012","article-title":"Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotopecoded affinity tags and mass spectrometry","volume":"42","author":"Sethuraman","year":"2007","journal-title":"Free Radic. Biol. Med"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"5134","DOI":"10.1021\/ac060525v","article-title":"Detailed map of oxidative post-translational modifications of human p21ras using Fourier transform mass spectrometry","volume":"78","author":"Zhao","year":"2006","journal-title":"Anal. Chem"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1161\/01.CIR.0000157148.59308.F5","article-title":"Alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidative modification of thiols on Ras","volume":"111","author":"Kuster","year":"2005","journal-title":"Circulation"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/hr.2010.229","article-title":"Simvastatin prevents large blood pressure variability induced aggravation of cardiac hypertrophy in hypertensive rats by inhibiting RhoA\/Ras-ERK pathways","volume":"34","author":"Takayama","year":"2011","journal-title":"Hypertens. Res"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/S1016-8478(23)17590-X","article-title":"Regulation by reversible Sglutathionylation: Molecular targets implicated in inflammatory diseases","volume":"25","author":"Shelton","year":"2008","journal-title":"Mol. Cells"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"14134","DOI":"10.1021\/bi011459o","article-title":"Glutathionylation of the p50 subunit of NF-kappaB: A mechanism for redoxinduced inhibition of DNA binding","volume":"40","author":"Klatt","year":"2001","journal-title":"Biochemistry"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"18427","DOI":"10.1074\/jbc.M610934200","article-title":"Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFkappaB","volume":"282","author":"Qanungo","year":"2007","journal-title":"J. Biol. Chem"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1016\/S0092-8674(00)81694-3","article-title":"AIkB-NF-kB structures: At the interface of inflammation control","volume":"95","author":"Baeuerle","year":"1998","journal-title":"Cell"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1089\/ars.2005.7.395","article-title":"Redox regulation of NFkappaB activation: Distinct redox regulation between the cytoplasm and the nucleus","volume":"7","author":"Kabe","year":"2005","journal-title":"Antioxid. Redox Signal"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1038\/sj.cdd.4401874","article-title":"Targeting NF-kappaB in hematologic malignancies","volume":"13","author":"Braun","year":"2006","journal-title":"Cell Death. Differ"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"33255","DOI":"10.1074\/jbc.M109.042127","article-title":"Lipid rafts and caveolin-1 coordinate interleukin-1beta (IL-1beta)-dependent activation of NFkappaB by controlling endocytosis of Nox2 and IL-1beta receptor 1 from the plasma membrane","volume":"284","author":"Oakley","year":"2009","journal-title":"J. Biol. Chem"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1089\/ars.2008.2363","article-title":"Signaling components of redox active endosomes: The redoxosomes","volume":"11","author":"Oakley","year":"2009","journal-title":"Antioxid. Redox Signal"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1089\/ars.2008.2407","article-title":"Endosomal Nox2 facilitates redox dependent induction of NF-kappa B by TNF-alpha","volume":"11","author":"Li","year":"2009","journal-title":"Antioxid. Redox Signal"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1038\/emboj.2008.28","article-title":"S-glutathionylation of IRF3 regulates IRF3-CBP interaction and activation of the IFN beta pathway","volume":"27","author":"Prinarakis","year":"2008","journal-title":"EMBO J"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"H827","DOI":"10.1152\/ajpheart.00129.2010","article-title":"Phospholemman Ser69 phosphorylation contributes to sildenafilinduced cardioprotection against reperfusion injury","volume":"299","author":"Madhani","year":"2010","journal-title":"Am. J. Physiol. Heart Circ. Physiol"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/14\/10\/20845\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T21:49:56Z","timestamp":1760219396000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/14\/10\/20845"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,10,17]]},"references-count":157,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2013,10]]}},"alternative-id":["ijms141020845"],"URL":"https:\/\/doi.org\/10.3390\/ijms141020845","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,10,17]]}}}