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Bot., 51, 2053, 10.1093\u002Fjexbot\u002F51.353.2053\nHaseeb, 2013, Delphinidin inhibits IL-1beta-induced activation of NF-kappab by modulating the phosphorylation of IRAK-1(Ser376) in human articular chondrocytes, Rheumatology, 52, 998, 10.1093\u002Frheumatology\u002Fkes363\nLivak, 2001, Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method, Methods, 25, 402, 10.1006\u002Fmeth.2001.1262\nFriesner, 2006, Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes, J. Med. Chem., 49, 6177, 10.1021\u002Fjm051256o\nBarbosa, 2003, Improved and simple micro assay for sulfated glycosaminoglycans quantification in biological extracts and its use in skin and muscle tissue studies, Glycobiology, 13, 647, 10.1093\u002Fglycob\u002Fcwg082\nSchmitz, 2010, Basic methods in histopathology of joint tissues, Osteoarth. Cart., 18, S113, 10.1016\u002Fj.joca.2010.05.026\nT. Kaneko, H. Chiba, N. Horie, T. Kato, M. Kobayashi, K. Hashimoto, K. Kusama, H. Sakagami, Effect of Scutellariae radix ingredients on prostaglandin E(2) production and COX-2 expression by LPS-activated macrophage, In Vivo, 23(4), 2009, 577–81.\nKhan, 2017, Dataset of wogonin, a natural flavonoid on the viability and activation of NF-κB and MAPKs in IL-1β-stimulated human OA chondrocytes, Data Brief, 10.1016\u002Fj.dib.2017.03.054\nAttur, 2008, Prostaglandin E2 exerts catabolic effects in osteoarthritis cartilage: evidence for signaling via the EP4 receptor, J. Immunol., 181, 5082, 10.4049\u002Fjimmunol.181.7.5082\nVuolteenaho, 2007, The role of nitric oxide in osteoarthritis, Scand. J. Rheumatol., 36, 247, 10.1080\u002F03009740701483014\nLepetsos, 2016, ROS\u002Foxidative stress signaling in osteoarthritis, Biochim. Biophys. Acta, 1862\nPoulet, 2016, Targeting oxidative stress to reduce osteoarthritis, Arthritis Res. 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Commun., 377, 1195, 10.1016\u002Fj.bbrc.2008.10.156\nCai, 2009, Neuroprotective effects of hydrogen saline in neonatal hypoxia-ischemia rat model, Brain Res., 1256, 129, 10.1016\u002Fj.brainres.2008.11.048\nNi, 2001, New anti-monocyte chemoattractant protein-1 gene therapy attenuates atherosclerosis in apolipoprotein E-knockout mice, Circulation, 103, 2096, 10.1161\u002F01.CIR.103.16.2096\nBoullier, 2006, Minimally oxidized LDL offsets the apoptotic effects of extensively oxidized LDL and free cholesterol in macrophages, Arterioscler. Thromb. Vasc. Biol., 26, 1169, 10.1161\u002F01.ATV.0000210279.97308.9a\nAyaori, 2006, Glucocorticoid receptor regulates ATP-binding cassette transporter-A1 expression and apolipoprotein-mediated cholesterol efflux from macrophages, Arterioscler. Thromb. Vasc. Biol., 26, 163, 10.1161\u002F01.ATV.0000193513.29074.52\nIuliano, 1996, Protection of low density lipoprotein oxidation at chemical and cellular level by the antioxidant drug dipyridamole, Br. J. Pharmacol., 119, 1438, 10.1111\u002Fj.1476-5381.1996.tb16056.x\nSchuyler, 2011, Insulin treatment attenuates diabetes-increased atherosclerotic intimal lesions and matrix metalloproteinase 9 expression in apolipoprotein E-deficient mice, J. Endocrinol., 210, 37, 10.1530\u002FJOE-10-0420\nFalk, 1995, Coronary plaque disruption, Circulation, 92, 657, 10.1161\u002F01.CIR.92.3.657\nDietel, 2013, Decreased numbers of regulatory T cells are associated with human atherosclerotic lesion vulnerability and inversely correlate with infiltrated mature dendritic cells, Atherosclerosis, 230, 92, 10.1016\u002Fj.atherosclerosis.2013.06.014\nTabas, 2010, Macrophage death and defective inflammation resolution in atherosclerosis, Nat. Rev. Immunol., 10, 36, 10.1038\u002Fnri2675\nTsukano, 2010, The endoplasmic reticulum stress-C\u002FEBP homologous protein pathway-mediated apoptosis in macrophages contributes to the instability of atherosclerotic plaques, Arterioscler. Thromb. Vasc. Biol., 30, 1925, 10.1161\u002FATVBAHA.110.206094\nLi, 2012, Hepcidin destabilizes atherosclerotic plaque via overactivating macrophages after erythrophagocytosis, Arterioscler. Thromb. Vasc. Biol., 32, 1158, 10.1161\u002FATVBAHA.112.246108\nMadamanchi, 2005, Oxidative stress and vascular disease, Arterioscler. Thromb. Vasc. Biol., 25, 29, 10.1161\u002F01.ATV.0000150649.39934.13\nTian, 2007, The endothelial cell-produced antiangiogenic cytokine vascular endothelial growth inhibitor induces dendritic cell maturation, J. Immunol., 179, 3742, 10.4049\u002Fjimmunol.179.6.3742\nTran, 2012, TGF-beta: the sword, the wand, and the shield of FOXP3(+) regulatory T cells, J. Mol. Cell. Biol., 4, 29, 10.1093\u002Fjmcb\u002Fmjr033\nYao, 2013, Activating transcription factor 6 mediates oxidized LDL-induced cholesterol accumulation and apoptosis in macrophages by up-regulating CHOP expression, J. Atheroscler. Thromb., 20, 94, 10.5551\u002Fjat.13425\nScull, 2011, Mechanisms of ER stress-induced apoptosis in atherosclerosis, Arterioscler. Thromb. Vasc. Biol., 31, 2792, 10.1161\u002FATVBAHA.111.224881\nThorp, 2009, Reduced apoptosis and plaque necrosis in advanced atherosclerotic lesions of Apoe-\u002F- and Ldlr-\u002F- mice lacking CHOP, Cell Metab., 9, 474, 10.1016\u002Fj.cmet.2009.03.003\nTabas, 2009, Macrophage apoptosis in atherosclerosis: consequences on plaque progression and the role of endoplasmic reticulum stress, Antioxid. Redox Signaling, 11, 2333, 10.1089\u002Fars.2009.2469\nSeimon, 2009, Mechanisms and consequences of macrophage apoptosis in atherosclerosis, J. 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Cell Physiol., 281, C1819, 10.1152\u002Fajpcell.2001.281.6.C1819\nWorkman, 2002, Hsp90 as a new therapeutic target for cancer therapy, Expert Opin. Biol. Ther., 2, 3, 10.1517\u002F14712598.2.1.3\nAgatsuma, 2002, Halohydrin and oxime derivatives of radicicol, Bioorg. Med. Chem., 10, 3445, 10.1016\u002FS0968-0896(02)00260-2\nRosser, 2000, Ligand interactions in the adenosine nucleotide-binding domain of the hsp90 chaperone, grp94. I. Evidence for allosteric regulation of ligand binding, J. Biol. Chem., 275, 22798, 10.1074\u002Fjbc.M001477200\nRoe, 1999, Structural basis for inhibition of the hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin, J. Med. Chem., 42, 260, 10.1021\u002Fjm980403y\nBillecke, 2002, Hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase, J. Biol. Chem., 277, 20504, 10.1074\u002Fjbc.M201940200\nPillay, 1996, Radicicol inhibits tyrosine phosphorylation of the mitotic src substrate sam68 and retards subsequent exit from mitosis of src-transformed cells, Cell Growth Differ., 7, 1487\nSharma, 2001, Ucs15a, a nonkinase inhibitor of src signal transduction, Oncogene, 20, 2068, 10.1038\u002Fsj.onc.1204296\nPritchard, 1995, Low-density lipoprotein increases endothelial cell nitric oxide synthase generation of superoxide anion, Circ. Res., 77, 510, 10.1161\u002F01.RES.77.3.510\nPritchard, 2002, Native low-density lipoprotein induces endothelial nitric oxide synthase dysfunction, Free Radic. Biol. Med., 33, 52, 10.1016\u002FS0891-5849(02)00851-1\nBraman, 1989, Nanogram nitrite and nitrate determination in environmental and biological materials by vanadium (iii) reduction with chemiluminescence detection, Anal. Chem., 61, 2715, 10.1021\u002Fac00199a007\nLiu, 1996, Palmitoylation of endothelial nitric oxide synthase is necessary for optimal stimulated release of nitric oxide, Biochemistry, 35, 13277, 10.1021\u002Fbi961720e\nPritchard, 2001, Heat shock protein 90 mediates the balance of nitric oxide and superoxide anion from endothelial nitric oxide synthase, J. Biol. Chem., 276, 17621, 10.1074\u002Fjbc.C100084200\nFontana, 2002, Domain mapping studies reveal that the m domain of hsp90 serves as a molecular scaffold to regulate akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release, Circ. Res., 90, 866, 10.1161\u002F01.RES.0000016837.26733.BE\nBenchekroun, 1994, Free radical formation by ansamycin benzoquinone in human breast tumor cells, Free Radic. Biol. Med., 17, 191, 10.1016\u002F0891-5849(94)90074-4\nDikalov, 2002, Geldanamycin leads to superoxide formation by enzymatic and nonenzymatic redox cycling, J. Biol. 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Photomed., 8, 236",{},{"id":18,"text":1374,"url":18,"identifiers":1375},"Pauling, 1991, Effect of ascorbic acid on incidence of spontaneous mammary tumors and UV-light-induced skin tumors in mice, Am. J. Clin. Nutr., 54, 1252S, 10.1093\u002Fajcn\u002F54.6.1252s",{"doi":1376},"10.1093\u002Fajcn\u002F54.6.1252s",{"id":18,"text":1378,"url":18,"identifiers":1379},"Jurkiewicz, 1995, Effect of topically applied tocopherol on ultraviolet radiation-mediated free radical damage in skin, J. Invest. Dermatol., 104, 484, 10.1111\u002F1523-1747.ep12605921",{"doi":1380},"10.1111\u002F1523-1747.ep12605921",{"id":18,"text":1382,"url":18,"identifiers":1383},"Burton, 1981, Autoxidation of biological molecules. I. The antioxidant activity of vitamin E and related chain-breaking phenolic antioxidants in vitro., J. Am. Chem. Soc., 103, 6472, 10.1021\u002Fja00411a035",{"doi":1384},"10.1021\u002Fja00411a035",{"id":18,"text":1386,"url":18,"identifiers":1387},"Traber, 1994, Determinants of plasma vitamin E concentrations, Free Radic. Biol. Med., 16, 229, 10.1016\u002F0891-5849(94)90148-1",{"doi":1388},"10.1016\u002F0891-5849(94)90148-1",{"id":18,"text":1390,"url":18,"identifiers":1391},"Burton, 1982, First proof that vitamin E is major lipid-soluble, chain-breaking antioxidant in human blood plasma., Lancet, 8292, 3",{},{"id":18,"text":1393,"url":18,"identifiers":1394},"Burton, 1983, Is vitamin E the only lipid-soluble, chain-breaking antioxidant in human blood plasma and erythrocyte membranes?, Arch. Biochem. Biophys., 221, 281, 10.1016\u002F0003-9861(83)90145-5",{"doi":1395},"10.1016\u002F0003-9861(83)90145-5",{"id":18,"text":1397,"url":18,"identifiers":1398},"Kagan, 1992, Recycling of vitamin E in human low density lipoproteins, J. Lipid Res., 33, 385, 10.1016\u002FS0022-2275(20)41529-9",{"doi":1399},"10.1016\u002FS0022-2275(20)41529-9",{"id":18,"text":1401,"url":18,"identifiers":1402},"Esterbauer, 1992, The role of lipid peroxidation and antioxidants in oxidative modification of LDL, Free Radic. Biol. Med., 13, 341, 10.1016\u002F0891-5849(92)90181-F",{"doi":1403},"10.1016\u002F0891-5849(92)90181-F",{"id":18,"text":1405,"url":18,"identifiers":1406},"Behrens, 1987, Mechanisms of absorption, transport and tissue uptake of RRR-α-tocopherol and d-γ-tocopherol in the white rat., J. Nutr., 117, 1562, 10.1093\u002Fjn\u002F117.9.1562",{"doi":1407},"10.1093\u002Fjn\u002F117.9.1562",{"id":18,"text":1409,"url":18,"identifiers":1410},"Handelman, 1994, Human adipose α-tocopherol and γ-tocopherol kinetics during and after 1 y of α-tocopherol supplementation, Am. J. Clin. Nutr., 59, 1025, 10.1093\u002Fajcn\u002F59.5.1025",{"doi":1411},"10.1093\u002Fajcn\u002F59.5.1025",{"id":18,"text":1413,"url":18,"identifiers":1414},"Peake, 1977, α- and γ-Tocopherols in the rat: In vitro and in vivo tissue uptake and metabolism, J. Nutr., 101, 1615, 10.1093\u002Fjn\u002F101.12.1615",{"doi":1415},"10.1093\u002Fjn\u002F101.12.1615",{"id":18,"text":1417,"url":18,"identifiers":1418},"Hayes, 1993, Differences in the plasma transport and tissue concentrations of tocopherols and tocotrienols: Observations in humans and hamsters, Proc. Soc. Exp. Biol. Med., 202, 353, 10.3181\u002F00379727-202-43546",{"doi":1419},"10.3181\u002F00379727-202-43546",{"id":18,"text":1421,"url":18,"identifiers":1422},"Serbinova, 1991, Free radical recycling and intramembrane mobility in the antioxidant properties of alpha-tocopherol and alpha-tocotrienol, Free Radic. Biol. Med., 10, 263, 10.1016\u002F0891-5849(91)90033-Y",{"doi":1423},"10.1016\u002F0891-5849(91)90033-Y",{"id":18,"text":1425,"url":18,"identifiers":1426},"Traber, 1996, Vitamin E in humans: Demand and delivery, Annu. Rev. Nutr., 16, 321, 10.1146\u002Fannurev.nu.16.070196.001541",{"doi":1427},"10.1146\u002Fannurev.nu.16.070196.001541",{"id":18,"text":1429,"url":18,"identifiers":1430},"Dupuis, 1984, In vivo relationship between horny layer reservoir effect and percutaneous absorption in human and rat, J. Invest. Dermatol., 82, 353, 10.1111\u002F1523-1747.ep12260677",{"doi":1431},"10.1111\u002F1523-1747.ep12260677",{"id":18,"text":1433,"url":18,"identifiers":1434},"Podda, 1996, Simultaneous determination of tissue tocopherols, tocotrienols, ubiquinols and ubiquinones, J. Lipid Res., 37, 893, 10.1016\u002FS0022-2275(20)37587-8",{"doi":1435},"10.1016\u002FS0022-2275(20)37587-8",{"id":18,"text":1437,"url":18,"identifiers":1438},"Burton, 1985, A mild, rapid, and efficient method of lipid extraction for use in determining vitamin E\u002Flipid ratios, Lipids, 20, 29, 10.1007\u002FBF02534359",{"doi":1439},"10.1007\u002FBF02534359",{"id":18,"text":1441,"url":18,"identifiers":1442},"Lang, 1986, Simultaneous determination of tocopherols, ubiquinols, and ubiquinones in blood, plasma, tissue homogenates, and subcellular fractions., Anal. Biochem., 157, 106, 10.1016\u002F0003-2697(86)90203-4",{"doi":1443},"10.1016\u002F0003-2697(86)90203-4",{"id":18,"text":1445,"url":18,"identifiers":1446},"Yamamoto, 1987, Detection and characterization of lipid hydroperoxides at picomole levels by high-performance liquid chromatography, Anal. Biochem., 160, 7, 10.1016\u002F0003-2697(87)90606-3",{"doi":1447},"10.1016\u002F0003-2697(87)90606-3",{"id":18,"text":1449,"url":18,"identifiers":1450},"Yamamoto, 1990, Assay of lipid hydroperoxides using high-performance liquid chromatography with isoluminal chemiluminescence detection, Methods Enzymol., 186, 371, 10.1016\u002F0076-6879(90)86130-N",{"doi":1451},"10.1016\u002F0076-6879(90)86130-N",{"id":18,"text":1453,"url":18,"identifiers":1454},"Suarna, 1993, Comparative antioxidant activity of tocotrienols and other natural lipid-soluble antioxidants in a homogeneous system, and in rat and human lipoproteins, Biochim. Biophys. Acta, 1166, 163, 10.1016\u002F0005-2760(93)90092-N",{"doi":1455},"10.1016\u002F0005-2760(93)90092-N",{"id":18,"text":1457,"url":18,"identifiers":1458},"Norkus, 1993, Uptake and bioconversion of alpha-tocopheryl acetate to alpha-tocopherol in skin of hairless mice, Photochem. Photobiol., 57, 613, 10.1111\u002Fj.1751-1097.1993.tb02926.x",{"doi":1459},"10.1111\u002Fj.1751-1097.1993.tb02926.x",{"id":18,"text":1461,"url":18,"identifiers":1462},"Stocker, 1991, Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does alpha-tocopherol, Proc. Natl. Acad. Sci. USA, 88, 1646, 10.1073\u002Fpnas.88.5.1646",{"doi":1463},"10.1073\u002Fpnas.88.5.1646",{"id":18,"text":1465,"url":18,"identifiers":1466},"Niki, 1993, Chemistry and biochemistry of vitamin E and coenzyme Q as antioxidants, 13",{},{"id":18,"text":1468,"url":18,"identifiers":1469},"Kontush, 1995, Antioxidative activity of ubiquinol 10 at physiologic concentrations in human low density lipoprotein, Biochim. Biophys. Acta, 1258, 177, 10.1016\u002F0005-2760(95)00115-S",{"doi":1470},"10.1016\u002F0005-2760(95)00115-S",{"id":18,"text":1359,"url":18,"identifiers":1472},{"doi":1361},{"id":1474,"createTime":1475,"updateTime":1476,"relativeEntities":1477,"slug":1478,"properties":1479,"entityType":102,"verifyStatus":103,"verifyTime":1488,"verifyNote":105,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1489,"fullTextUrl":18,"authors":1490,"publicationType":144,"publisherRelationship":1573,"citationCount":19,"citationInfo":1619,"publishDate":1621,"publishYear":192,"citationAnalyzeStatus":195,"lastCitationAnalyze":1622,"indexDatabases":1623,"openAccess":18,"references":18,"isForceReanalyzing":198},"beab02b1-ac4a-4ad6-8138-aa1451655cc6","2024-01-04T07:30:22.920+00:00","2026-08-13T10:41:33.617+00:00",[],"Fluorescent-probes-for-the-detection-of-nitroxyl-HNO-",{"title":1480,"gsPaper":1482,"references":1484,"doi":1486},{"EN":1481},"Fluorescent probes for the detection of nitroxyl (HNO)",{"VOID":1483},"[\"17235779820756074334\"]",{"VOID":1485},"Doctorovich, 2016\nMiranda, 2005, The chemistry of nitroxyl (HNO) and implications in biology, Coord. Chem. Rev., 249, 433, 10.1016\u002Fj.ccr.2004.08.010\nFukuto, 2005, The physiological chemistry and biological activity of nitroxyl (HNO): the neglected, misunderstood, and enigmatic nitrogen oxide, Chem. Res. Toxicol., 18, 790, 10.1021\u002Ftx0496800\nIrvine, 2008, Nitroxyl (HNO): the Cinderella of the nitric oxide story, Trends Pharmacol. Sci., 29, 601, 10.1016\u002Fj.tips.2008.08.005\nPaolocci, 2009, The shy Angeli and his elusive creature: the HNO route to vasodilation,American journal of physiology, Heart Circ. Physiol., 296, H1217, 10.1152\u002Fajpheart.00243.2009\nShafirovich, 2002, Nitroxyl and its anion in aqueous solutions: spin states, protic equilibria, and reactivities toward oxygen and nitric oxide, Proc. Natl. Acad. Sci. USA, 99, 7340, 10.1073\u002Fpnas.112202099\nHughes, 1999, Synthesis, chemistry, and applications of nitroxyl ion releasers sodium trioxodinitrate or Angeli's salt and Piloty's acid, Methods Enzymol., 301, 279, 10.1016\u002FS0076-6879(99)01092-7\nCline, 2011, Detection of nitroxyl (HNO) by membrane inlet mass spectrometry, Free Radic. Biol. Med., 50, 1274, 10.1016\u002Fj.freeradbiomed.2011.02.008\nAizawa, 2013, Piloty's acid derivative with improved nitroxyl-releasing characteristics, Bioorg. Med. Chem. Lett., 23, 2340, 10.1016\u002Fj.bmcl.2013.02.062\nSirsalmath, 2013, The pH of HNO donation is modulated by ring substituents in Piloty's acid derivatives: azanone donors at biological pH, J. Inorg. Biochem., 118, 134, 10.1016\u002Fj.jinorgbio.2012.10.008\nGuthrie, 2015, \"Catch-and-release\" of HNO with pyrazolones, J. Org. Chem., 80, 1338, 10.1021\u002Fjo502330w\nGuthrie, 2015, Curtailing the hydroxylaminobarbituric acid-hydantoin rearrangement to favor HNO generation, J. Org. Chem., 80, 1349, 10.1021\u002Fjo5023316\nGuthrie, 2012, Development of N-substituted hydroxylamines as efficient nitroxyl (HNO) donors, J. Am. Chem. Soc., 134, 1962, 10.1021\u002Fja2103923\nZeng, 2004, Nitroxyl (HNO) release from new functionalized N-hydroxyurea-derived acyl nitroso-9,10-dimethylanthracene cycloadducts, Bioorg. Med. Chem. Lett., 14, 5565, 10.1016\u002Fj.bmcl.2004.08.062\nDonzelli, 2013, Pharmacological characterization of 1-nitrosocyclohexyl acetate, a long-acting nitroxyl donor that shows vasorelaxant and antiaggregatory effects, J. Pharmacol. Exp. Ther., 344, 339, 10.1124\u002Fjpet.112.199836\nHolland, 2013, Enzymatic generation of the NO\u002FHNO-releasing IPA\u002FNO anion at controlled rates in physiological media using beta-galactosidase, Nitric Oxide: Biol. Chem., 35, 131, 10.1016\u002Fj.niox.2013.10.003\nBasudhar, 2013, Synthesis and chemical and biological comparison of nitroxyl- and nitric oxide-releasing diazeniumdiolate-based aspirin derivatives, J. Med. Chem., 56, 7804, 10.1021\u002Fjm400196q\nBharadwaj, 2014, Analysis of the HNO and NO donating properties of alicyclic amine diazeniumdiolates, Nitric Oxide: Biol. Chem., 42, 70, 10.1016\u002Fj.niox.2014.08.013\nAndrei, 2010, Dual mechanisms of HNO generation by a nitroxyl prodrug of the diazeniumdiolate (NONOate) class, J. Am. Chem. Soc., 132, 16526, 10.1021\u002Fja106552p\nNakagawa, 2013, Controlled release of HNO from chemical donors for biological applications, J. Inorg. Biochem., 118, 187, 10.1016\u002Fj.jinorgbio.2012.10.004\nAdachi, 2008, Photoactivatable HNO-releasing compounds using the retro-Diels-Alder reaction, Chem. Commun., 5149, 10.1039\u002Fb811985f\nFukuto, 2009, Nitroxyl (HNO) signaling, Free Radic. Biol. Med., 47, 1318, 10.1016\u002Fj.freeradbiomed.2009.06.014\nLiochev, 2003, The mode of decomposition of Angeli's salt (Na2N2O3) and the effects thereon of oxygen, nitrite, superoxide dismutase, and glutathione, Free Radic. Biol. Med., 34, 1399, 10.1016\u002FS0891-5849(03)00111-4\nSmulik, 2014, Nitroxyl (HNO) reacts with molecular oxygen and forms peroxynitrite at physiological pH. Biological Implications, J. Biol. Chem., 289, 35570, 10.1074\u002Fjbc.M114.597740\nMiranda, 2003, A biochemical rationale for the discrete behavior of nitroxyl and nitric oxide in the cardiovascular system, Proc. Natl. Acad. Sci. USA, 100, 9196, 10.1073\u002Fpnas.1430507100\nMurphy, 1991, Reversible conversion of nitroxyl anion to nitric oxide by superoxide dismutase, Proc. Natl. Acad. Sci. USA, 88, 10860, 10.1073\u002Fpnas.88.23.10860\nLiochev, 2001, Copper,zinc superoxide dismutase as a univalent NO(-) oxidoreductase and as a dichlorofluorescin peroxidase, J. Biol. Chem., 276, 35253, 10.1074\u002Fjbc.M104237200\nLiochev, 2002, Nitroxyl (NO-): a substrate for superoxide dismutase, Arch. Biochem. Biophys., 402, 166, 10.1016\u002FS0003-9861(02)00074-7\nBazylinski, 1985, Metmyoglobin and methemoglobin as efficient traps for nitrosyl hydride (nitroxyl) in neutral aqueous-aolution, J. Am. Chem. Soc., 107, 7982, 10.1021\u002Fja00312a031\nDoyle, 1988, Oxidation and reduction of hemoproteins by trioxodinitrate(II) - the role of nitrosyl hydride and nitrite, J. Am. Chem. Soc., 110, 593, 10.1021\u002Fja00210a047\nMiranda, 2001, Unique oxidative mechanisms for the reactive nitrogen oxide species, nitroxyl anion, J. Biol. Chem., 276, 1720, 10.1074\u002Fjbc.M006174200\nMiranda, 2002, Further evidence for distinct reactive intermediates from nitroxyl and peroxynitrite: effects of buffer composition on the chemistry of Angeli's salt and synthetic peroxynitrite, Arch. Biochem. Biophys., 401, 134, 10.1016\u002FS0003-9861(02)00031-0\nKirsch, 2002, Formation of peroxynitrite from reaction of nitroxyl anion with molecular oxygen, J. Biol. Chem., 277, 13379, 10.1074\u002Fjbc.M108079200\nFukuto, 1992, Chemical oxidation of N-hydroxyguanidine compounds. Release of nitric oxide, nitroxyl and possible relationship to the mechanism of biological nitric oxide generation, Biochem. Pharmacol., 43, 607, 10.1016\u002F0006-2952(92)90584-6\nSchmidt, 1996, No ·NO from NO synthase, Proc. Natl. Acad. Sci. USA, 93, 14492, 10.1073\u002Fpnas.93.25.14492\nPufahl, 1995, Hydrogen peroxide-supported oxidation of NG-hydroxy-L-arginine by nitric oxide synthase, Biochemistry, 34, 1930, 10.1021\u002Fbi00006a014\nHobbs, 1994, Formation of free nitric oxide from l-arginine by nitric oxide synthase: direct enhancement of generation by superoxide dismutase, Proc. Natl. Acad. Sci. USA, 91, 10992, 10.1073\u002Fpnas.91.23.10992\nAdak, 2000, Arginine conversion to nitroxide by tetrahydrobiopterin-free neuronal nitric-oxide synthase. Implications for mechanism, J. Biol. Chem., 275, 33554, 10.1074\u002Fjbc.M004337200\nTantillo, 2000, Theoretical studies on N-hydroxy-L-arginine and derived radicals: implications for the mechanism of nitric oxide synthase, J. Am. Chem. Soc., 122, 536, 10.1021\u002Fja991876c\nPagliaro, 2003, Differential biological effects of products of nitric oxide (NO) synthase: it is not enough to say NO, Life Sci., 73, 2137, 10.1016\u002FS0024-3205(03)00593-9\nNiketic, 1999, Exposure of Mn and FeSODs, but not Cu\u002FZnSOD, to NO leads to nitrosonium and nitroxyl ions generation which cause enzyme modification and inactivation: an in vitro study, Free Radic. Biol. Med., 27, 992, 10.1016\u002FS0891-5849(98)00256-1\nSharpe, 1998, Reactions of nitric oxide with mitochondrial cytochrome c: a novel mechanism for the formation of nitroxyl anion and peroxynitrite, Biochem. J., 332, 9, 10.1042\u002Fbj3320009\nSaleem, 2004, Xanthine oxidase converts nitric oxide to nitroxyl that inactivates the enzyme, Biochem. Biophys. Res. Commun., 315, 455, 10.1016\u002Fj.bbrc.2004.01.081\nPoderoso, 1999, The reaction of nitric oxide with ubiquinol: kinetic properties and biological significance, Free Radic. Biol. Med., 26, 925, 10.1016\u002FS0891-5849(98)00277-9\nKirsch, 2009, New insights into the S-nitrosothiol-ascorbate reaction. The formation of nitroxyl, Org. Biomol. Chem., 7, 1954, 10.1039\u002Fb901046g\nWong, 1998, Reaction between S-nitrosothiols and thiols: generation of nitroxyl (HNO) and subsequent chemistry, Biochemistry, 37, 5362, 10.1021\u002Fbi973153g\nEberhardt, 2014, H2S and NO cooperatively regulate vascular tone by activating a neuroendocrine HNO-TRPA1-CGRP signalling pathway, Nat. Commun., 5, 4381, 10.1038\u002Fncomms5381\nFilipovic, 2012, Chemical characterization of the smallest S-nitrosothiol, HSNO; cellular cross-talk of H2S and S-nitrosothiols, J. Am. Chem. Soc., 134, 12016, 10.1021\u002Fja3009693\nFilipovic, 2013, Beyond H2S and NO interplay: hydrogen sulfide and nitroprusside react directly to give nitroxyl (HNO). A new pharmacological source of HNO, J. Med. Chem., 56, 1499, 10.1021\u002Fjm3012036\nHamer, 2015, Discussing endogenous NO(*)\u002FHNO interconversion aided by phenolic drugs and vitamins, Inorg. Chem., 54, 9342, 10.1021\u002Facs.inorgchem.5b01347\nSuarez, 2015, Nitric oxide is reduced to HNO by proton-coupled nucleophilic attack by ascorbate, tyrosine, and other alcohols. A new route to HNO in biological media?, J. Am. Chem. Soc., 137, 4720, 10.1021\u002Fja512343w\nSuarez, 2017, HNO is produced by the reaction of NO with thiols, J. Am. Chem. Soc., 139, 14483, 10.1021\u002Fjacs.7b06968\nSuarez, 2013, Time-resolved electrochemical quantification of azanone (HNO) at low nanomolar level, Anal. Chem., 85, 10262, 10.1021\u002Fac402134b\nRoyzen, 2013, Physical and structural properties of [Cu(BOT1)Cl]Cl, a fluorescent imaging probe for HNO, J. Inorg. Biochem., 118, 162, 10.1016\u002Fj.jinorgbio.2012.08.025\nRosenthal, 2010, Direct detection of nitroxyl in aqueous solution using a tripodal copper(II) BODIPY complex, J. Am. Chem. Soc., 132, 5536, 10.1021\u002Fja909148v\nZhou, 2011, Visualization of nitroxyl in living cells by a chelated copper(II) coumarin complex, Org. Lett., 13, 1290, 10.1021\u002Fol103077q\nKim, 2016, Achieving reversible sensing of nitroxyl by tuning the ligand environment of azamacrocyclic copper(II) complexes, J. Am. Chem. Soc., 138, 1804, 10.1021\u002Fjacs.5b12825\nRivera-Fuentes, 2015, Metal-based optical probes for live cell imaging of nitroxyl (HNO), Acc. Chem. Res., 48, 2927, 10.1021\u002Facs.accounts.5b00388\nBari, 2003, Fast nitroxyl trapping by ferric porphyrins, J. Am. Chem. Soc., 125, 15272, 10.1021\u002Fja036370f\nAlvarez, 2014, Redox potential determines the reaction mechanism of HNO donors with Mn and Fe porphyrins: defining the better traps, Inorg. Chem., 53, 7351, 10.1021\u002Fic5007082\nWrobel, 2014, A fast and selective near-infrared fluorescent sensor for multicolor imaging of biological nitroxyl (HNO), J. Am. Chem. Soc., 136, 4697, 10.1021\u002Fja500315x\nMarti, 2005, Discrimination of nitroxyl and nitric oxide by water-soluble Mn(III) porphyrins, J. Am. Chem. Soc., 127, 4680, 10.1021\u002Fja044632n\nZhou, 2012, Nitroxyl induced fluorescence enhancement via reduction of a copper (II) coumarin-ester complex: its application for bioimaging in vivo, Sens. Actuators B Chem., 174, 414, 10.1016\u002Fj.snb.2012.08.067\nJohnson, 2013, Quantitative detection of nitroxyl upon trapping with glutathione and labeling with a specific fluorogenic reagent, Free Radic. Biol. Med., 63, 476, 10.1016\u002Fj.freeradbiomed.2013.05.011\nJohnson, 2014, Glutathione sulfinamide serves as a selective, endogenous biomarker for nitroxyl after exposure to therapeutic levels of donors, Free Radic. Biol. Med., 76, 299, 10.1016\u002Fj.freeradbiomed.2014.07.022\nReisz, 2009, Reductive phosphine-mediated ligation of nitroxyl (HNO), Org. Lett., 11, 2719, 10.1021\u002Fol900914s\nKawai, 2013, A reductant-resistant and metal-free fluorescent probe for nitroxyl applicable to living cells, J. Am. Chem. Soc., 135, 12690, 10.1021\u002Fja404757s\nMao, 2014, A highly sensitive and reductant-resistant fluorescent probe for nitroxyl in aqueous solution and serum, Chem. Commun., 50, 5790, 10.1039\u002Fc4cc01440e\nJing, 2014, Visualization of nitroxyl (HNO) in vivo via a lysosome-targetable near-infrared fluorescent probe, Chem. Commun., 50, 14253, 10.1039\u002FC4CC07561G\nMiao, 2015, A selective phosphine-based fluorescent probe for nitroxyl in living cells, Bioorg. Med. Chem. Lett., 25, 16, 10.1016\u002Fj.bmcl.2014.11.041\nZheng, 2015, A two-photon fluorescent turn-on probe for nitroxyl (HNO) and its bioimaging application in living tissues, Chem. Commun., 51, 5754, 10.1039\u002FC4CC10382C\nZhang, 2015, A FRET-based ratiometric fluorescent probe for nitroxyl detection in living cells, ACS Appl. Mater. Interfaces, 7, 5438, 10.1021\u002Fam508987v\nLiu, 2014, A fast-response, highly sensitive and selective fluorescent probe for the ratiometric imaging of nitroxyl in living cells, Chem. Commun., 50, 6013, 10.1039\u002Fc4cc00980k\nLiu, 2015, A near-infrared fluorescent probe for the selective detection of HNO in living cells and in vivo, Analyst, 140, 4576, 10.1039\u002FC5AN00759C\nReisz, 2011, Rapid and selective nitroxyl (HNO) trapping by phosphines: kinetics and new aqueous ligations for HNO detection and quantitation, J. Am. Chem. Soc., 133, 11675, 10.1021\u002Fja203652z\nShoeman, 1998, The reaction of nitroxyl (HNO) with nitrosobenzene gives cupferron (N-nitrosophenylhydroxylamine), Nitric Oxide: Biol. Chem., 2, 66, 10.1006\u002Fniox.1998.0166\nWardman, 2007, Fluorescent and luminescent probes for measurement of oxidative and nitrosative species in cells and tissues: progress, pitfalls, and prospects, Free Radic. Biol. Med., 43, 995, 10.1016\u002Fj.freeradbiomed.2007.06.026\nKalyanaraman, 2012, Measuring reactive oxygen and nitrogen species with fluorescent probes: challenges and limitations, Free Radic. Biol. Med., 52, 1, 10.1016\u002Fj.freeradbiomed.2011.09.030\nWinterbourn, 2014, The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells, Biochim. Biophys. Acta, 1840, 730, 10.1016\u002Fj.bbagen.2013.05.004\nDebowska, 2015, Toward selective detection of reactive oxygen and nitrogen species with the use of fluorogenic probes--Limitations, progress, and perspectives, Pharmacol. Rep., 67, 756, 10.1016\u002Fj.pharep.2015.03.016\nKalyanaraman, 2017, Recent developments in detection of superoxide radical anion and hydrogen peroxide: opportunities, challenges, and implications in redox signaling, Arch. Biochem. Biophys., 617, 38, 10.1016\u002Fj.abb.2016.08.021\nHardy, 2017, Detection and characterization of reactive oxygen and nitrogen species in biological systems by monitoring species-specific products, Antioxid. Redox Signal.\nRezende, 2017, Detection of hydrogen peroxide with fluorescent dyes, Antioxid. Redox Signal.\nZielonka, 2012, Global profiling of reactive oxygen and nitrogen species in biological systems: high-throughput real-time analyses, J. Biol. Chem., 287, 2984, 10.1074\u002Fjbc.M111.309062\nDoctorovich, 2014, How to find an HNO needle in a (bio)-chemical haystack, 58, 145\nMiao, 2017, Phosphine-based HNO Detection, 225\nRen, 2017, Fluorescent Probes for HNO Detection, 207\nMiao, 2016, Recent advances in the chemical biology of nitroxyl (HNO) detection and generation, Nitric Oxide: Biol. Chem., 57, 1, 10.1016\u002Fj.niox.2016.04.006\nNelli, 2000, Oxidation of nitroxyl anion to nitric oxide by copper ions, Br. J. Pharmacol., 131, 356, 10.1038\u002Fsj.bjp.0703550\nTennyson, 2007, Selective fluorescence detection of nitroxyl over nitric oxide in buffered aqueous solution using a conjugated metallopolymer, Polyhedron, 26, 4625, 10.1016\u002Fj.poly.2007.04.003\nYang, 2015, The fluorescence regulation mechanism of the paramagnetic metal in a biological HNO sensor, Chem. Commun., 51, 9616, 10.1039\u002FC5CC00787A\nMichael, 2014, HNO\u002FNO conversion mechanisms of Cu-based HNO probes with implications for Cu,Zn-SOD, J. Phys. Chem. Lett., 5, 1022, 10.1021\u002Fjz5002902\nLv, 2016, Surfactant-modulated discriminative sensing of HNO and H2S with a Cu2+-complex-based fluorescent probe, Tetrahedron, 72, 5495, 10.1016\u002Fj.tet.2016.07.039\nSasakura, 2011, Development of a highly selective fluorescence probe for hydrogen sulfide, J. Am. Chem. Soc., 133, 18003, 10.1021\u002Fja207851s\nHou, 2012, A retrievable and highly selective fluorescent probe for monitoring sulfide and imaging in living cells, Inorg. Chem., 51, 2454, 10.1021\u002Fic2024082\nQu, 2013, A red fluorescent turn-on probe for hydrogen sulfide and its application in living cells, Chem. Commun., 49, 7510, 10.1039\u002Fc3cc44128h\nSantos-Figueroa, 2014, Highly selective fluorescence detection of hydrogen sulfide by using an anthracene-functionalized cyclam–CuII complex, Eur. J. Inorg. Chem., 2014, 41, 10.1002\u002Fejic.201301306\nApfel, 2013, Detection of nitric oxide and nitroxyl with benzoresorufin-based fluorescent sensors, Inorg. Chem., 52, 3285, 10.1021\u002Fic302793w\nLim, 2006, Direct nitric oxide detection in aqueous solution by copper(II) fluorescein complexes, J. Am. Chem. Soc., 128, 14364, 10.1021\u002Fja064955e\nPluth, 2011, Seminaphthofluorescein-based fluorescent probes for imaging nitric oxide in live cells, Inorg. Chem., 50, 9385, 10.1021\u002Fic200986v\nLoas, 2017, Direct ratiometric detection of nitric oxide with Cu(II)-based fluorescent probes, J. Mater. Chem. B, 5, 8929, 10.1039\u002FC7TB02666H\nSun, 2016, A water-soluble copper(II) complex for the selective fluorescence detection of nitric oxide\u002Fnitroxyl and imaging in living cells, ChemPlusChem, 81, 30, 10.1002\u002Fcplu.201500436\nLoas, 2015, Solid-phase synthesis provides a modular, lysine-based platform for fluorescent discrimination of nitroxyl and biological thiols, Chem. Sci., 6, 4131, 10.1039\u002FC5SC00880H\nAskew, 1995, Catalysis by Cu2+ of nitric oxide release from S-nitrosothiols (RSNO), J. Chem. Soc. Perkin, 2, 741, 10.1039\u002Fp29950000741\nSingh, 1996, Mechanism of nitric oxide release from S-nitrosothiols, J. Biol. Chem., 271, 18596, 10.1074\u002Fjbc.271.31.18596\nWilliams, 1996, S-nitrosothiols and role of metal ions in decomposition to nitric oxide, Methods Enzymol., 268, 299, 10.1016\u002FS0076-6879(96)68032-X\nBurg, 2000, The reaction mechanism of nitrosothiols with copper(I), J. Biol. Inorg. Chem., 5, 213, 10.1007\u002Fs007750050365\nMezyk, 1996, Rate constant determination for the reaction of hydroxyl and glutathione thiyl radicals with glutathione in aqueous solution, J. Phys. Chem., 100, 8861, 10.1021\u002Fjp9535553\nFolkes, 2004, Kinetics of the reaction between nitric oxide and glutathione: implications for thiol depletion in cells, Free Radic. Biol. Med., 37, 549, 10.1016\u002Fj.freeradbiomed.2004.05.012\nAravindakumar, 2002, Kinetics of the anaerobic reaction of nitric oxide with cysteine, glutathione and cysteine-containing proteins: implications for in vivo[space]S-nitrosation, Journal of the Chemical Society, Perkin Trans., 2, 663, 10.1039\u002Fb107273k\nHaake, 1972, Zur desoxygenierung von tritylthionitrit, Tetrahedron Lett., 33, 3405, 10.1016\u002FS0040-4039(01)94056-0\nWang, 2008, Fast reductive ligation of S-nitrosothiols, Angew. Chem. Int. Ed. Engl., 47, 6598, 10.1002\u002Fanie.200801654\nZhang, 2009, An unexpected Bis-ligation of S-nitrosothiols, J. Am. Chem. Soc., 131, 3854, 10.1021\u002Fja900370y\nSaxon, 2000, Cell surface engineering by a modified Staudinger reaction, Science, 287, 2007, 10.1126\u002Fscience.287.5460.2007\nSmulik-Izydorczyk, 2017, A kinetic study on the reactivity of azanone (HNO) toward its selected scavengers: insight into its chemistry and detection, Nitric Oxide: Biol. Chem., 69, 61, 10.1016\u002Fj.niox.2017.05.003\nJackson, 2009, Kinetic feasibility of nitroxyl reduction by physiological reductants and biological implications, Free Radic. Biol. Med., 47, 1130, 10.1016\u002Fj.freeradbiomed.2009.06.034\nLv, 2015, An ESIPT-based ratiometric fluorescent probe for the imaging of nitroxyl in living cells, Anal. Methods, 3883, 10.1039\u002FC5AY00531K\nLiu, 2015, A highly sensitive and reductant-resistant fluorescent chemodosimeter for the rapid detection of nitroxyl, Sens. Actuators B: Chem., 220, 727, 10.1016\u002Fj.snb.2015.06.013\nTan, 2015, Design and synthesis of near-infrared fluorescent probes for imaging of biological nitroxyl, Sci. Rep., 5, 16979, 10.1038\u002Fsrep16979\nJin, 2016, Novel fluorescent ESIPT probe based on flavone for nitroxyl in aqueous solution and serum, Sens. Actuators B Chem., 224, 209, 10.1016\u002Fj.snb.2015.09.072\nBobba, 2015, Resorufin based fluorescence ‘turn-on’ chemodosimeter probe for nitroxyl (HNO), RSC Adv., 5, 84543, 10.1039\u002FC5RA17837A\nDong, 2016, Development of green to near-infrared turn-on fluorescent probes for the multicolour imaging of nitroxyl in living systems, J. Mater. Chem. B, 4, 1263, 10.1039\u002FC5TB02073E\nLiu, 2017, A reductant-resistant ratiometric, colorimetric and far-red fluorescent probe for rapid and ultrasensitive detection of nitroxyl, J. Mater. Chem. B, 5, 3557, 10.1039\u002FC6TB03359H\nDong, 2017, Two-photon red-emissive fluorescent probe for imaging nitroxyl (HNO) in living cells and tissues, J. Mater. Chem. B, 5, 5218, 10.1039\u002FC7TB00703E\nAli, 2017, A super-resolution probe to monitor HNO levels in the endoplasmic reticulum of cells, Anal. Chem., 89, 12087, 10.1021\u002Facs.analchem.7b02567\nGong, 2016, A mitochondria-targetable near-infrared fluorescent probe for imaging nitroxyl (HNO) in living cells, Dyes Pigm., 131, 24, 10.1016\u002Fj.dyepig.2016.03.046\nSunwoo, 2017, A bioorthogonal 'turn-on' fluorescent probe for tracking mitochondrial nitroxyl formation, Chem. Commun., 53, 1723, 10.1039\u002FC6CC09082F\nRen, 2017, A targetable fluorescent probe for imaging exogenous and intracellularly formed nitroxyl in mitochondria in living cells, J. Mater. Chem. B, 5, 1954, 10.1039\u002FC6TB03388A\nZhang, 2014, A reductive ligation based fluorescent probe for S-nitrosothiols, Chem. Commun., 50, 4806, 10.1039\u002FC4CC01288G\nZhu, 2016, A FRET-based ratiometric two-photon fluorescent probe for dual-channel imaging of nitroxyl in living cells and tissues, Chem. Commun., 52, 733, 10.1039\u002FC5CC08695G\nZheng, 2016, A ratiometric fluorescent probe based on a Bodipy-Coumarin conjugate for sensing of nitroxyl in living cells, Sens. Actuators B Chem., 233, 193, 10.1016\u002Fj.snb.2016.04.053\nZhou, 2017, Ratiometric visualization of NO\u002FH2S cross-talk in living cells and tissues using a nitroxyl-responsive two-photon fluorescence probe, Anal. Chem., 89, 4587, 10.1021\u002Facs.analchem.7b00073\nLi, 2018, Single probe giving different signals towards reactive oxygen species and nitroxyl, Dyes Pigm., 148, 348, 10.1016\u002Fj.dyepig.2017.09.033\nMiao, 2016, Comparison of reductive ligation-based detection strategies for nitroxyl (HNO) and S-Nitrosothiols, ChemistryOpen, 5, 110, 10.1002\u002Fopen.201500200\nBroniowska, 2013, S-nitrosoglutathione, Biochim. Biophys. Acta, 1830, 3173, 10.1016\u002Fj.bbagen.2013.02.004\nAbu-Omar, 1995, Oxidations of ER3 (E = P, As, or Sb) by hydrogen peroxide: methylrhenium trioxide as catalyst, J. Am. Chem. Soc., 117, 272, 10.1021\u002Fja00106a030\nHan, 1998, Spectrophotometric assay for hypochlorite\u002Fhypochlorous acid using tris(2-carboxyethyl)phosphine, Microchem. J., 58, 218, 10.1006\u002Fmchj.1997.1542\nLonghi, 1962, Reactions of nitrogen(II) oxide with miscellaneous lewis bases, Inorg. Chem., 1, 768, 10.1021\u002Fic50004a011\nLim, 2002, Kinetics of the oxidation of triphenylphosphine by nitric oxide, Inorg. Chem., 41, 1026, 10.1021\u002Fic0108585\nBakac, 2009, Oxidation of a water-soluble phosphine and some spectroscopic probes with nitric oxide and nitrous acid in aqueous solutions, Inorg. Chem., 48, 6979, 10.1021\u002Fic900688g\nYamada, 2006, In vivo detection of free radicals induced by diethylnitrosamine in rat liver tissue, Free Radic. Biol. Med., 40, 2040, 10.1016\u002Fj.freeradbiomed.2006.01.031\nBorbat, 2001, Electron spin resonance in studies of membranes and proteins, Science, 291, 266, 10.1126\u002Fscience.291.5502.266\nDavis, 2011, Magnetic resonance imaging of organic contrast agents in mice: capturing the whole-body redox landscape, Free Radic. Biol. Med., 50, 459, 10.1016\u002Fj.freeradbiomed.2010.11.028\nEmoto, 2013, Novel ascorbic acid-resistive nitroxide in a lipid emulsion: an efficient brain imaging contrast agent for MRI of small rodents, Neurosci. Lett., 546, 11, 10.1016\u002Fj.neulet.2013.04.044\nSoule, 2007, Therapeutic and clinical applications of nitroxide compounds, Antioxid. Redox Signal., 9, 1731, 10.1089\u002Fars.2007.1722\nSamuni, 2013, The use of cyclic nitroxide radicals as HNO scavengers, J. Inorg. Biochem., 118, 155, 10.1016\u002Fj.jinorgbio.2012.10.002\nCline, 2011, Detection of nitroxyl (HNO) by a prefluorescent probe, J. Phys. Org. Chem., 24, 993, 10.1002\u002Fpoc.1871\nMatsuoka, 2016, Fluorescence probe for the convenient and sensitive detection of ascorbic acid, J. Clin. Biochem. Nutr., 58, 16, 10.3164\u002Fjcbn.15-105\nPino, 2017, NitroxylFluor: a thiol-based fluorescent probe for live-cell imaging of nitroxyl, J. Am. Chem. Soc., 10.1021\u002Fjacs.7b11471\nLozinsky, 1999, Dual fluorophore-nitroxide probes for analysis of vitamin C in biological liquids, J. Biochem. Biophys. Methods, 38, 29, 10.1016\u002FS0165-022X(98)00029-3\nParkhomyuk-Ben Arye, 2002, Stilbene photochrome-fluorescence-spin molecules: covalent immobilization on silica plate and applications as redox and viscosity probes, J. Biochem. Biophys. Methods, 51, 1, 10.1016\u002FS0165-022X(01)00234-2\nCoenjarts, 2003, Mapping photogenerated radicals in thin polymer films: fluorescence imaging using a prefluorescent radical probe, J. Am. Chem. Soc., 125, 620, 10.1021\u002Fja028835s\nAliaga, 2003, A new method to study antioxidant capability: hydrogen transfer from phenols to a prefluorescent nitroxide, Org. Lett., 5, 4145, 10.1021\u002Fol035589w\nAliaga, 2008, Hydrogen-transfer reactions from phenols to TEMPO prefluorescent probes in micellar systems, Org. Lett., 10, 2147, 10.1021\u002Fol800446c\nHirosawa, 2012, A TEMPO-conjugated fluorescent probe for monitoring mitochondrial redox reactions, Chem. Commun., 48, 4845, 10.1039\u002Fc2cc30603d\nSato, 2008, Synthesis and properties of umbelliferone-nitroxide radical hybrid compounds as fluorescence and spin-label probes, Spectrochim. Acta A, 70, 799, 10.1016\u002Fj.saa.2007.09.015\nYapici, 2012, New rhodamine nitroxide based fluorescent probes for intracellular hydroxyl radical identification in living cells, Org. Lett., 14, 50, 10.1021\u002Fol202816m\nCao, 2013, Visualizing the changes in the cellular redox environment using a novel profluorescent rhodamine nitroxide probe, New J. Chem., 37, 2991, 10.1039\u002Fc3nj00674c\nYang, 2015, A sensitive and selective chemosensor for ascorbic acid based on a fluorescent nitroxide switch, Talanta, 132, 191, 10.1016\u002Fj.talanta.2014.08.066\nAliaga, 2015, TEMPO-attached pre-fluorescent probes based on pyridinium fluorophores, J. Fluoresc., 25, 979, 10.1007\u002Fs10895-015-1579-0\nLiras, 2016, Nitroxide amide-BODIPY probe behavior in fibroblasts analyzed by advanced fluorescence microscopy, Org. Biomol. Chem., 14, 4023, 10.1039\u002FC6OB00533K\nNagy, 1990, Determination of metals in solution by chelate formation with intramolecular luminescence-quenched spin-labelled reagents, Analyst, 115, 839, 10.1039\u002Fan9901500839\nPou, 1993, A fluorophore-containing nitroxide as a probe to detect superoxide and hydroxyl radical generated by stimulated neutrophils, Anal. Biochem., 212, 85, 10.1006\u002Fabio.1993.1295\nMedvedeva, 2004, Dual fluorophore-nitronyl probe for investigation of superoxide dynamics and antioxidant status of biological systems, J. Photochem. Photobiol. A Chem., 163, 45, 10.1016\u002FS1010-6030(03)00430-1\nMicallef, 2005, The application of a novel profluorescent nitroxide to monitor thermo-oxidative degradation of polypropylene, Polym. Degrad. Stabil., 89, 427, 10.1016\u002Fj.polymdegradstab.2005.01.030\nKeddie, 2005, Synthesis of profluorescent isoindoline nitroxides via palladium-catalysed Heck alkenylation, Org. Biomol. Chem., 3, 2593, 10.1039\u002Fb504354a\nBlinco, 2007, The first example of an azaphenalene profluoreseent nitroxide, Eur. J. Org. Chem., 28, 4638, 10.1002\u002Fejoc.200700545\nSato, 2009, Synthesis and spectral properties of polymethine-cyanine dye–nitroxide radical hybrid compounds for use as fluorescence probes to monitor reducing species and radicals, Spectrochim. Acta Part A: Mol. Biomol. Spectrosc., 71, 2030, 10.1016\u002Fj.saa.2008.07.045\nAhn, 2012, Two-photon fluorescence microscopy imaging of cellular oxidative stress using profluorescent nitroxides, J. Am. Chem. Soc., 134, 4721, 10.1021\u002Fja210315x\nMatsuoka, 2012, Rapid and convenient detection of ascorbic acid using a fluorescent nitroxide switch, Free Radic. Biol. 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training protects the heart against ischemia-reperfusion injury: A central role for mitochondria?",{"VOID":1634},"[\"16548938025462283287\"]",{"VOID":1636},"Benjamin, 2018, American heart association council on epidemiology and prevention statistics committee and stroke statistics subcommittee, heart disease and stroke statistics-2018 update: a report from the American heart association, Circulation, 137, e67, 10.1161\u002FCIR.0000000000000558\nThompson Paul, 2003, Exercise and physical activity in the prevention and treatment of atherosclerotic cardiovascular disease, Circulation, 107, 3109, 10.1161\u002F01.CIR.0000075572.40158.77\nBrinks, 2016, Lifestyle modification in secondary prevention, Am. J. Lifestyle Med., 11, 137, 10.1177\u002F1559827616651402\nNystoriak, 2018, Cardiovascular effects and benefits of exercise, Front. Cardiovasc. Med., 5, 10.3389\u002Ffcvm.2018.00135\nQuindry, 2017, Exercise-induced cardioprotection and the therapeutic potential of RIPC, J. Cardiovasc. Pharmacol. Therapeut., 22, 397, 10.1177\u002F1074248417715005\nEjlersen, 2017, Prognostic impact of physical activity prior to myocardial infarction: case fatality and subsequent risk of heart failure and death, Eur. J. Prev. Cardiol., 24, 1112, 10.1177\u002F2047487317702046\nKwong, 2015, Physiological and pathological roles of the mitochondrial permeability transition pore in the heart, Cell Metabol., 21, 206, 10.1016\u002Fj.cmet.2014.12.001\nConley, 2016, Mitochondria to motion: optimizing oxidative phosphorylation to improve exercise performance, J. Exp. Biol., 219, 243, 10.1242\u002Fjeb.126623\nFiorenza, 2019, High-intensity exercise training enhances mitochondrial oxidative phosphorylation efficiency in a temperature-dependent manner in human skeletal muscle: implications for exercise performance, FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol., 33, 8976\nHood, 2009, Appl. Physiol. Nutr. Metabol., 34, 465, 10.1139\u002FH09-045\nWang, 2015, Exercise prevents cardiac injury and improves mitochondrial biogenesis in advanced diabetic cardiomyopathy with PGC-1α and akt activation, Cell. Physiol. Biochem., 35, 2159, 10.1159\u002F000374021\nFrench, 2008, Exercise-induced protection against myocardial apoptosis and necrosis: MnSOD, calcium-handling proteins, and calpain, FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol., 22, 2862\nHamilton, 2003, Exercise, antioxidants, and HSP72: protection against myocardial ischemia\u002Freperfusion, Free Radic. Biol. Med., 34, 800, 10.1016\u002FS0891-5849(02)01431-4\nOng, 2015, The mitochondrial permeability transition pore and its role in myocardial ischemia reperfusion injury, J. Mol. Cell. Cardiol., 78, 23, 10.1016\u002Fj.yjmcc.2014.11.005\nChouchani, 2016, A unifying mechanism for mitochondrial superoxide production during ischemia-reperfusion injury, Cell Metabol., 23, 254, 10.1016\u002Fj.cmet.2015.12.009\nCadenas, 2018, ROS and redox signaling in myocardial ischemia-reperfusion injury and cardioprotection, Free Radic. Biol. Med., 117, 76, 10.1016\u002Fj.freeradbiomed.2018.01.024\nHom, 2009, Morphological dynamics of mitochondria — a special emphasis on cardiac muscle cells, J. Mol. Cell. Cardiol., 46, 811, 10.1016\u002Fj.yjmcc.2009.02.023\nBonora, 2019, Targeting mitochondria for cardiovascular disorders: therapeutic potential and obstacles, Nat. Rev. Cardiol., 16, 33, 10.1038\u002Fs41569-018-0074-0\nOng, 2010, Mitochondrial morphology and cardiovascular disease, Cardiovasc. Res., 88, 16, 10.1093\u002Fcvr\u002Fcvq237\nBoengler, 2009, Presence of connexin 43 in subsarcolemmal, but not in interfibrillar cardiomyocyte mitochondria, Basic Res. Cardiol., 104, 141, 10.1007\u002Fs00395-009-0007-5\nHeinzel Frank, 2005, Impairment of diazoxide-induced formation of reactive oxygen species and loss of cardioprotection in connexin 43 deficient mice, Circ. Res., 97, 583, 10.1161\u002F01.RES.0000181171.65293.65\nDenuc, 2016, New protein–protein interactions of mitochondrial connexin 43 in mouse heart, J. Cell Mol. Med., 20, 794, 10.1111\u002Fjcmm.12792\nBoengler, 2017, Mitochondria and ageing: role in heart, skeletal muscle and adipose tissue, J. Cachexia Sarcopenia Muscle., 8, 349, 10.1002\u002Fjcsm.12178\nRodríguez-Sinovas, 2018, Mitochondrial Cx43, an important component of cardiac preconditioning, Biochim. Biophys. Acta BBA - Biomembr., 1860, 174, 10.1016\u002Fj.bbamem.2017.06.011\nBarth, 1992, Ultrastructural quantitation of mitochondria and myofilaments in cardiac muscle from 10 different animal species including man, J. Mol. Cell. Cardiol., 24, 669, 10.1016\u002F0022-2828(92)93381-S\nVentura-Clapier, 2011, Bioenergetics of the failing heart, Biochim. Biophys. Acta, 1813, 1360, 10.1016\u002Fj.bbamcr.2010.09.006\nDoenst, 2013, Cardiac metabolism in heart failure - implications beyond ATP production, Circ. Res., 113, 709, 10.1161\u002FCIRCRESAHA.113.300376\nEdoardo, 2018, Calcium signaling and reactive oxygen species in mitochondria, Circ. Res., 122, 1460, 10.1161\u002FCIRCRESAHA.118.310082\nDenton, 2009, Regulation of mitochondrial dehydrogenases by calcium ions, Biochim. Biophys. Acta BBA - Bioenerg., 1787, 1309, 10.1016\u002Fj.bbabio.2009.01.005\nGriffiths, 2009, Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells, Biochim. Biophys. Acta, 1787, 1324, 10.1016\u002Fj.bbabio.2009.01.019\nHarisseh, 2019, A modified calcium retention capacity assay clarifies the roles of extra-and intracellular calcium pools in mitochondrial permeability transition pore opening, J. Biol. Chem., 294, 15282, 10.1074\u002Fjbc.RA119.009477\nZorov, 2014, Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release, Physiol. Rev., 94, 909, 10.1152\u002Fphysrev.00026.2013\nDedkova, 2013, Mitochondria-mediated cardioprotection by trimetazidine in rabbit heart failure, J. Mol. Cell. Cardiol., 59, 41, 10.1016\u002Fj.yjmcc.2013.01.016\nSantos, 2016, Redox signaling in the cardiomyocyte: from physiology to failure, Int. J. Biochem. Cell Biol., 74, 145, 10.1016\u002Fj.biocel.2016.03.002\nYoule, 2008, The BCL-2 protein family: opposing activities that mediate cell death, Nat. Rev. Mol. Cell Biol., 9, 47, 10.1038\u002Fnrm2308\nManeechote, 2017, Roles of mitochondrial dynamics modulators in cardiac ischaemia\u002Freperfusion injury, J. Cell Mol. Med., 21, 2643, 10.1111\u002Fjcmm.13330\nMorciano, 2017, Mechanistic role of mPTP in ischemia-reperfusion injury, 169\nConsolini, 2017, Mitochondrial bioenergetics during ischemia and reperfusion, Adv. Exp. Med. Biol., 982, 141, 10.1007\u002F978-3-319-55330-6_8\nGörlach, 2015, Calcium and ROS: a mutual interplay, Redox Biol, 6, 260, 10.1016\u002Fj.redox.2015.08.010\nHajnóczky, 2006, Mitochondrial calcium signalling and cell death: approaches for assessing the role of mitochondrial Ca2+ uptake in apoptosis, Cell Calcium, 40, 553, 10.1016\u002Fj.ceca.2006.08.016\nZorov, 2000, Reactive oxygen species (ROS)-induced ROS release: a new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes, J. Exp. Med., 192, 1001, 10.1084\u002Fjem.192.7.1001\nChouchani, 2014, Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS, Nature, 515, 431, 10.1038\u002Fnature13909\nChen, 2006, Reversible blockade of electron transport during ischemia protects mitochondria and decreases myocardial injury following reperfusion, J. Pharmacol. Exp. Therapeut., 319, 1405, 10.1124\u002Fjpet.106.110262\nOvize, 2010, Cardiovasc. Res., 87, 406, 10.1093\u002Fcvr\u002Fcvq129\nLim, 2011, Mitochondrial cyclophilin-D as a potential therapeutic target for post-myocardial infarction heart failure, J. Cell Mol. Med., 15, 2443, 10.1111\u002Fj.1582-4934.2010.01235.x\nWaldmeier, 2002, Inhibition of the mitochondrial permeability transition by the nonimmunosuppressive cyclosporin derivative NIM811, Mol. Pharmacol., 62, 22, 10.1124\u002Fmol.62.1.22\nMewton, 2015, CIRCUS Study Investigators, Rationale and design of the Cyclosporine to ImpRove Clinical oUtcome in ST-elevation myocardial infarction patients (the CIRCUS trial), Am. Heart J., 169, 758, 10.1016\u002Fj.ahj.2015.02.020\nCung, 2015, Cyclosporine before PCI in patients with acute myocardial infarction, N. Engl. J. Med., 373, 1021, 10.1056\u002FNEJMoa1505489\nPowers, 2014, Mechanisms of exercise-induced cardioprotection, Physiol. Bethesda Md, 29, 27\nFulghum, 2018, Metabolic mechanisms of exercise-induced cardiac remodeling, Front. Cardiovasc. Med., 5, 10.3389\u002Ffcvm.2018.00127\nHuertas, 2019, Stay fit, stay young: mitochondria in movement: the role of exercise in the new mitochondrial paradigm, Oxid. Med. Cell. Longev., 10.1155\u002F2019\u002F7058350\nHwang, 2013, Mitochondrial dynamics in the heart as a novel therapeutic target for cardioprotection, Chonnam Med. J., 49, 101, 10.4068\u002Fcmj.2013.49.3.101\nStanley, 2005, Myocardial substrate metabolism in the normal and failing heart, Physiol. Rev., 85, 1093, 10.1152\u002Fphysrev.00006.2004\nMihaylova, 2011, The AMPK signalling pathway coordinates cell growth, autophagy and metabolism, Nat. Cell Biol., 13, 1016, 10.1038\u002Fncb2329\nCantó, 2009, AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity, Nature, 458, 1056, 10.1038\u002Fnature07813\nKahn, 2005, AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism, Cell Metabol., 1, 15, 10.1016\u002Fj.cmet.2004.12.003\nTowler, 2007, AMP-activated protein kinase in metabolic control and insulin signaling, Circ. Res., 100, 328, 10.1161\u002F01.RES.0000256090.42690.05\nChatham, 2002, Lactate – the forgotten fuel!, J. Physiol., 542, 10.1113\u002Fjphysiol.2002.020974\nGoodwin, 2000, Improved energy homeostasis of the heart in the metabolic state of exercise, Am. J. Physiol.-Heart Circ. Physiol., 279, H1490, 10.1152\u002Fajpheart.2000.279.4.H1490\nPerry, 2017, Mitochondrial adaptations to exercise in human skeletal muscle: a possible role for cristae density as a determinant of muscle fitness, J. Physiol., 595, 2773, 10.1113\u002FJP273549\nTuomainen, 2017, The role of cardiac energy metabolism in cardiac hypertrophy and failure, Exp. Cell Res., 360, 12, 10.1016\u002Fj.yexcr.2017.03.052\nVettor, 2014, Exercise training boosts eNOS-dependent mitochondrial biogenesis in mouse heart: role in adaptation of glucose metabolism, Am. J. Physiol.-Endocrinol. Metab., 306, E519, 10.1152\u002Fajpendo.00617.2013\nDobrzyn, 2013, Expression of lipogenic genes is upregulated in the heart with exercise training-induced but not pressure overload-induced left ventricular hypertrophy, Am. J. Physiol. Endocrinol. Metab., 304, E1348, 10.1152\u002Fajpendo.00603.2012\nCastro, 2013, Cardiac molecular-acclimation mechanisms in response to swimming-induced exercise in Atlantic salmon, PloS One, 8, 10.1371\u002Fjournal.pone.0055056\nBonen, 2001, The expression of lactate transporters (MCT1 and MCT4) in heart and muscle, Eur. J. Appl. Physiol., 86, 6, 10.1007\u002Fs004210100516\nCoven, 2003, Physiological role of AMP-activated protein kinase in the heart: graded activation during exercise, Am. J. Physiol. Endocrinol. Metab., 285, E629, 10.1152\u002Fajpendo.00171.2003\nMarsin, 2000, Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia, Curr. Biol. CB., 10, 1247, 10.1016\u002FS0960-9822(00)00742-9\nHafstad, 2011, High intensity interval training alters substrate utilization and reduces oxygen consumption in the heart, J. Appl. Physiol. Bethesda Md 1985, 111, 1235\nGreggio, 2017, Enhanced respiratory chain supercomplex formation in response to exercise in human skeletal muscle, Cell Metabol., 25, 301, 10.1016\u002Fj.cmet.2016.11.004\nHuertas, 2017, Antioxidant effect of exercise: exploring the role of the mitochondrial complex I superassembly, Redox Biol, 13, 477, 10.1016\u002Fj.redox.2017.07.009\nZhang, 1997, Relationships between myocardial bioenergetic and left ventricular function in hearts with volume-overload hypertrophy, Circulation, 96, 334, 10.1161\u002F01.CIR.96.1.334\nSpencer, 1997, Function and bioenergetics in isolated perfused trained rat hearts, Am. J. Physiol., 272, H409\nFenning, 2003, Cardiac adaptation to endurance exercise in rats, Mol. Cell. Biochem., 251, 51, 10.1023\u002FA:1025465412329\nStuewe, 2000, Exercise training enhances glycolytic and oxidative enzymes in canine ventricular myocardium, J. Mol. Cell. Cardiol., 32, 903, 10.1006\u002Fjmcc.2000.1131\nWu, 2011, The unfolded protein response mediates adaptation to exercise in skeletal muscle through a PGC-1α\u002FATF6α complex, Cell Metabol., 13, 160, 10.1016\u002Fj.cmet.2011.01.003\nYan, 2012, Exercise training-induced regulation of mitochondrial quality, Exerc. Sport Sci. Rev., 40, 159, 10.1097\u002FJES.0b013e3182575599\nArcos, 1968, Changes in ultrastructure and respiratory control in mitochondria of rat heart hypertrophied by exercise, Exp. Mol. Pathol., 8, 49, 10.1016\u002F0014-4800(68)90005-1\nOscai, 1971, Effects of exercise on cardiac weight and mitochondria in male and female rats, Am. J. Physiol., 220, 1944, 10.1152\u002Fajplegacy.1971.220.6.1944\nDworatzek, 2014, Sex differences in exercise-induced physiological myocardial hypertrophy are modulated by oestrogen receptor beta, Cardiovasc. Res., 102, 418, 10.1093\u002Fcvr\u002Fcvu065\nCoronado, 2018, Physiological mitochondrial fragmentation is a normal cardiac adaptation to increased energy demand, Circ. Res., 122, 282, 10.1161\u002FCIRCRESAHA.117.310725\nMoore, 2019, The impact of exercise on mitochondrial dynamics and the role of Drp1 in exercise performance and training adaptations in skeletal muscle, Mol. Metab., 21, 51, 10.1016\u002Fj.molmet.2018.11.012\nHuertas, 2019, Human muscular mitochondrial fusion in athletes during exercise, Faseb. J., 33, 12087, 10.1096\u002Ffj.201900365RR\nJia, 2019, Postinfarction exercise training alleviates cardiac dysfunction and adverse remodeling via mitochondrial biogenesis and SIRT1\u002FPGC-1α\u002FPI3K\u002FAkt signaling, J. Cell. Physiol., 234, 23705, 10.1002\u002Fjcp.28939\nGhahremani, 2018, Mitochondrial dynamics as an underlying mechanism involved in aerobic exercise training-induced cardioprotection against ischemia-reperfusion injury, Life Sci., 213, 102, 10.1016\u002Fj.lfs.2018.10.035\nLi, 2016, Acute exercise-induced mitochondrial stress triggers an inflammatory response in the myocardium via NLRP3 inflammasome activation with mitophagy, Oxid. Med. Cell. Longev., 2016\nPowers, 2014, Exercise-induced improvements in myocardial antioxidant capacity: the antioxidant players and cardioprotection, Free Radic. Res., 48, 43, 10.3109\u002F10715762.2013.825371\nDone, 2016, Nrf2 mediates redox adaptations to exercise, Redox Biol, 10, 191, 10.1016\u002Fj.redox.2016.10.003\nKretzschmar, 1993, Aging, training and exercise. A review of effects on plasma glutathione and lipid peroxides, Sports Med. Auckl. NZ., 15, 196, 10.2165\u002F00007256-199315030-00005\nNikolaidis, 2012, Redox biology of exercise: an integrative and comparative consideration of some overlooked issues, J. Exp. Biol., 215, 1615, 10.1242\u002Fjeb.067470\nVenditti, 2014, Vitamin E supplementation modifies adaptive responses to training in rat skeletal muscle, Free Radic. Res., 48, 1179, 10.3109\u002F10715762.2014.937341\nMuthusamy, 2012, Acute exercise stress activates Nrf2\u002FARE signaling and promotes antioxidant mechanisms in the myocardium, Free Radic. Biol. Med., 52, 366, 10.1016\u002Fj.freeradbiomed.2011.10.440\nWang, 2016, Acute exercise stress promotes Ref1\u002FNrf2 signalling and increases mitochondrial antioxidant activity in skeletal muscle, Exp. Physiol., 101, 410, 10.1113\u002FEP085493\nShanmugam, 2019, Exercise mediated Nrf2 signaling protects the myocardium from isoproterenol-induced pathological remodeling, Front. Cardiovasc. Med., 6, 68, 10.3389\u002Ffcvm.2019.00068\nHancock, 2018, Myocardial NADPH oxidase-4 regulates the physiological response to acute exercise, ELife, 7, 10.7554\u002FeLife.41044\nAgo, 2010, Upregulation of Nox4 by hypertrophic stimuli promotes apoptosis and mitochondrial dysfunction in cardiac myocytes, Circ. Res., 106, 1253, 10.1161\u002FCIRCRESAHA.109.213116\nKasai, 2020, Regulation of Nrf2 by mitochondrial reactive oxygen species in physiology and pathology, Biomolecules, 10, 320, 10.3390\u002Fbiom10020320\nDone, 2016, Nrf2 mediates redox adaptations to exercise, Redox Biol, 10, 191, 10.1016\u002Fj.redox.2016.10.003\nCrilly, 2016, The role of Nrf2 in skeletal muscle contractile and mitochondrial function, J. Appl. Physiol. Bethesda Md 1985, 121, 730\nYamashita, 1999, Exercise provides direct biphasic cardioprotection via manganese superoxide dismutase activation, J. Exp. Med., 189, 1699, 10.1084\u002Fjem.189.11.1699\nJi, 2004, Acute exercise activates nuclear factor (NF)-kappaB signaling pathway in rat skeletal muscle, FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol., 18, 1499\nLima-Cabello, 2010, Eccentric exercise induces nitric oxide synthase expression through nuclear factor-kappaB modulation in rat skeletal muscle, J. Appl. Physiol. Bethesda Md 1985, 108, 575\nBalan, 2011, Acute exercise activates myocardial nuclear factor kappa B, Cell Stress Chaperones, 16, 105, 10.1007\u002Fs12192-010-0217-7\nPala, 2016, Coenzyme Q10 supplementation modulates NFκB and Nrf2 pathways in exercise training, J. Sports Sci. Med., 15, 196\nZoll, 2003, Preserved response of mitochondrial function to short-term endurance training in skeletal muscle of heart transplant recipients, J. Am. Coll. Cardiol., 42, 126, 10.1016\u002FS0735-1097(03)00499-6\nBowles, 1994, Exercise training improves metabolic response after ischemia in isolated working rat heart, J. Appl. Physiol. Bethesda Md 1985, 76, 1608\nAlleman, 2016, Exercise-induced protection against reperfusion arrhythmia involves stabilization of mitochondrial energetics, Am. J. Physiol. Heart Circ. Physiol., 310, H1360, 10.1152\u002Fajpheart.00858.2015\nAscensão, 2006, Effects of endurance training and acute doxorubicin treatment on rat heart mitochondrial alterations induced by in vitro anoxia-reoxygenation, Cardiovasc. Toxicol., 6, 159, 10.1385\u002FCT:6:3:159\nTao, 2015, Exercise training protects against acute myocardial infarction via improving myocardial energy metabolism and mitochondrial biogenesis, Cell. Physiol. Biochem. Int. J. Exp. Cell. Physiol. Biochem. Pharmacol., 37, 162, 10.1159\u002F000430342\nHalestrap, 2004, Mitochondrial permeability transition pore opening during myocardial reperfusion--a target for cardioprotection, Cardiovasc. Res., 61, 372, 10.1016\u002FS0008-6363(03)00533-9\nBernardi, 2015, The mitochondrial permeability transition pore: molecular nature and role as a target in cardioprotection, J. Mol. Cell. Cardiol., 78, 100, 10.1016\u002Fj.yjmcc.2014.09.023\nStarnes, 2007, Exercise training decreases rat heart mitochondria free radical generation but does not prevent Ca2+-induced dysfunction, J. Appl. Physiol., 102, 1793, 10.1152\u002Fjapplphysiol.00849.2006\nMarcil, 2006, Exercise training induces respiratory substrate-specific decrease in Ca2+-induced permeability transition pore opening in heart mitochondria, Am. J. Physiol. Heart Circ. Physiol., 290, H1549, 10.1152\u002Fajpheart.00913.2005\nPons, 2013, Regular treadmill exercise restores cardioprotective signaling pathways in obese mice independently from improvement in associated co-morbidities, J. Mol. Cell. Cardiol., 54, 82, 10.1016\u002Fj.yjmcc.2012.11.010\nGross, 1999, Sarcolemmal versus mitochondrial ATP-sensitive K+ channels and myocardial preconditioning, Circ. Res., 84, 973, 10.1161\u002F01.RES.84.9.973\nGarlid, 1997, Cardioprotective effect of diazoxide and its interaction with mitochondrial ATP-sensitive K+ channels. Possible mechanism of cardioprotection, Circ. Res., 81, 1072, 10.1161\u002F01.RES.81.6.1072\nQuindry, 2012, Ischemia reperfusion injury, KATP channels, and exercise-induced cardioprotection against apoptosis, J. Appl. Physiol., 113, 498, 10.1152\u002Fjapplphysiol.00957.2011\nLoor, 2011, Mitochondrial oxidant stress triggers cell death in simulated ischemia-reperfusion, Biochim. Biophys. Acta, 1813, 1382, 10.1016\u002Fj.bbamcr.2010.12.008\nZweier, 1987, Direct measurement of free radical generation following reperfusion of ischemic myocardium, Proc. Natl. Acad. Sci. U.S.A., 84, 1404, 10.1073\u002Fpnas.84.5.1404\nKorge, 2017, Reactive oxygen species production induced by pore opening in cardiac mitochondria: the role of complex II, J. Biol. Chem., 292 (24), 9896, 10.1074\u002Fjbc.M116.768325\nHansford, 1997, Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age, J. Bioenerg. Biomembr., 29, 89, 10.1023\u002FA:1022420007908\nMurphy, 2008, Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury, Physiol. Rev., 88, 581, 10.1152\u002Fphysrev.00024.2007\nMyung, 2013, Korean Meta-Analysis Study Group, Efficacy of vitamin and antioxidant supplements in prevention of cardiovascular disease: systematic review and meta-analysis of randomised controlled trials, BMJ, 346, f10, 10.1136\u002Fbmj.f10\nMaroz, 2009, Reactivity of ubiquinone and ubiquinol with superoxide and the hydroperoxyl radical: implications for in vivo antioxidant activity, Free Radic. Biol. Med., 46, 105, 10.1016\u002Fj.freeradbiomed.2008.09.033\nAdlam, 2005, Targeting an antioxidant to mitochondria decreases cardiac ischemia-reperfusion injury, Faseb. J., 19, 1088, 10.1096\u002Ffj.05-3718com\nKihlström, 1990, Protection effect of endurance training against reoxygenation-induced injuries in rat heart, J. Appl. Physiol. Bethesda Md 1985, 68, 1672\nLee, 2012, Exercise protects cardiac mitochondria against ischemia-reperfusion injury, Med. Sci. Sports Exerc., 44, 397, 10.1249\u002FMSS.0b013e318231c037\nJudge, 2005, Exercise by lifelong voluntary wheel running reduces subsarcolemmal and interfibrillar mitochondrial hydrogen peroxide production in the heart, Am. J. Physiol.-Regul. Integr. Comp. Physiol., 289, R1564, 10.1152\u002Fajpregu.00396.2005\nKavazis, 2009, Exercise training induces a cardioprotective phenotype and alterations in cardiac subsarcolemmal and intermyofibrillar mitochondrial proteins, Am. J. Physiol.-Heart Circ. Physiol., 297, H144, 10.1152\u002Fajpheart.01278.2008\nHamilton, 2004, MnSOD antisense treatment and exercise-induced protection against arrhythmias, Free Radic. Biol. Med., 37, 1360, 10.1016\u002Fj.freeradbiomed.2004.07.025\nKwon\nFrasier, 2011, Exercise-induced cardiac preconditioning: how exercise protects your achy-breaky heart, J. Appl. Physiol. Bethesda Md 1985, 111, 905\nFrasier, 2013, Redox-dependent increases in glutathione reductase and exercise preconditioning: role of NADPH oxidase and mitochondria, Cardiovasc. Res., 98, 47, 10.1093\u002Fcvr\u002Fcvt009\nSantos, 2011, Redox signaling in cardiac myocytes, Free Radic. Biol. Med., 50, 777, 10.1016\u002Fj.freeradbiomed.2011.01.003\nBellinger, 2008, Remodeling of ryanodine receptor complex causes “leaky” channels: a molecular mechanism for decreased exercise capacity, Proc. Natl. Acad. Sci. U.S.A., 105, 2198, 10.1073\u002Fpnas.0711074105\nChakouri, 2018, Stress-induced protein S-glutathionylation and phosphorylation crosstalk in cardiac sarcomeric proteins - impact on heart function, Int. J. Cardiol., 258, 207, 10.1016\u002Fj.ijcard.2017.12.004\nZima, 2006, Redox regulation of cardiac calcium channels and transporters, Cardiovasc. Res., 71, 310, 10.1016\u002Fj.cardiores.2006.02.019\nAndre, 2013, Subendocardial increase in reactive oxygen species production affects regional contractile function in ischemic heart failure, Antioxidants Redox Signal., 18, 1009, 10.1089\u002Fars.2012.4534\nHandy, 2012, Redox regulation of mitochondrial function, Antioxidants Redox Signal., 16, 1323, 10.1089\u002Fars.2011.4123\nChouchani, 2013, Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I, Nat. Med., 19, 753, 10.1038\u002Fnm.3212\nSun, 2015, Ischaemic preconditioning preferentially increases protein S-nitrosylation in subsarcolemmal mitochondria, Cardiovasc. Res., 106, 227, 10.1093\u002Fcvr\u002Fcvv044\nAmanakis, 2020, Cysteine 202 of Cyclophilin D is a site of multiple post-translational modifications and plays a role in cardioprotection, Cardiovasc Res\nS.W. Taylor, E. Fahy, J. Murray, R.A. Capaldi, S.S. Ghosh, Oxidative Post-translational Modification of Tryptophan Residues in Cardiac Mitochondrial Proteins, J. Biol. Chem. 278 (2003) 19587–19590. https:\u002F\u002Fdoi.org\u002F10.1074\u002Fjbc.C300135200.\nMailloux, 2014, Glutaredoxin-2 is required to control oxidative phosphorylation in cardiac muscle by mediating deglutathionylation reactions, J. Biol. Chem., 289 (21), 14812, 10.1074\u002Fjbc.M114.550574\nMargaritelis, 2020, Redox basis of exercise physiology, Redox Biol, 101499, 10.1016\u002Fj.redox.2020.101499\nZampieri, 2016, Physical exercise in aging human skeletal muscle increases mitochondrial calcium uniporter expression levels and affects mitochondria dynamics, Phys. Rep., 4\nKemi, 2008, Exercise-induced changes in calcium handling in left ventricular cardiomyocytes, Front. Biosci. J. Virtual Libr., 13, 356, 10.2741\u002F2685\nKemi, 2010, Mechanisms of exercise-induced improvements in the contractile apparatus of the mammalian myocardium, Acta Physiol. Oxf. Engl., 199, 425, 10.1111\u002Fj.1748-1716.2010.02132.x\nKemi, 2004, Aerobic fitness is associated with cardiomyocyte contractile capacity and endothelial function in exercise training and detraining, Circulation, 109, 2897, 10.1161\u002F01.CIR.0000129308.04757.72\nKemi, 2008, Myocardial sarcoplasmic reticulum Ca2+ ATPase function is increased by aerobic interval training, Eur. J. Cardiovasc. Prev. Rehabil. Off. J. Eur. Soc. Cardiol. Work. Groups Epidemiol. Prev. Card. Rehabil. Exerc. Physiol., 15, 145\nFrench, 2006, Ischemia-reperfusion-induced calpain activation and SERCA2a degradation are attenuated by exercise training and calpain inhibition, Am. J. Physiol. Heart Circ. Physiol., 290, H128, 10.1152\u002Fajpheart.00739.2005\nMagalhães, 2014, Modulation of cardiac mitochondrial permeability transition and apoptotic signaling by endurance training and intermittent hypobaric hypoxia, Int. J. Cardiol., 173, 40, 10.1016\u002Fj.ijcard.2014.02.011\nLejay, 2019, Critical limb ischaemia exacerbates mitochondrial dysfunction in ApoE–\u002F– mice compared with ApoE+\u002F+ mice, but N-acetyl cysteine still confers protection, Eur. J. Vasc. Endovasc. Surg., 58, 576, 10.1016\u002Fj.ejvs.2019.03.028\nda Silva, 2015, Attenuation of Ca2+ homeostasis, oxidative stress, and mitochondrial dysfunctions in diabetic rat heart: insulin therapy or aerobic exercise?, J. Appl. Physiol. Bethesda Md 1985, 119, 148\nShore, 1977, Two fractions of rough endoplasmic reticulum from rat liver. I. Recovery of rapidly sedimenting endoplasmic reticulum in association with mitochondria, J. Cell Biol., 72, 714, 10.1083\u002Fjcb.72.3.714\nOropeza-Almazán, 2017, Small interfering RNA targeting mitochondrial calcium uniporter improves cardiomyocyte cell viability in hypoxia\u002Freoxygenation injury by reducing calcium overload, Oxid. Med. Cell. Longev., 2017, 5750897, 10.1155\u002F2017\u002F5750897\nSeidlmayer, 2015, Distinct mPTP activation mechanisms in ischaemia–reperfusion: contributions of Ca2+, ROS, pH, and inorganic polyphosphate, Cardiovasc. Res., 106, 237, 10.1093\u002Fcvr\u002Fcvv097\nRasmussen, 2015, Inhibition of MCU forces extramitochondrial adaptations governing physiological and pathological stress responses in heart, Proc. Natl. Acad. Sci. U.S.A., 112, 9129, 10.1073\u002Fpnas.1504705112\nLuongo, 2015, The mitochondrial calcium uniporter matches energetic supply with cardiac workload during stress and modulates permeability transition, Cell Rep., 12, 23, 10.1016\u002Fj.celrep.2015.06.017\nZhou, 2018, ER–mitochondria microdomains in cardiac ischemia–reperfusion injury: a fresh perspective, Front. Physiol., 9, 10.3389\u002Ffphys.2018.00755\nO’Dell, 1991, Tests of the roles of two diffusible substances in long-term potentiation: evidence for nitric oxide as a possible early retrograde messenger, Proc. Natl. Acad. Sci. U.S.A., 88, 11285, 10.1073\u002Fpnas.88.24.11285\nRapoport, 1983, Agonist-induced endothelium-dependent relaxation in rat thoracic aorta may be mediated through cGMP, Circ. Res., 52, 352, 10.1161\u002F01.RES.52.3.352\nMaiorana, 2003, Exercise and the nitric oxide vasodilator system, Sports Med., 33, 1013, 10.2165\u002F00007256-200333140-00001\nMeziat, 2019, Exercise training restores eNOS activation in the perivascular adipose tissue of obese rats: impact on vascular function, Nitric Oxide, 86, 63, 10.1016\u002Fj.niox.2019.02.009\nCalvert John, 2011, Exercise protects against myocardial ischemia–reperfusion injury via stimulation of β3-adrenergic receptors and increased nitric oxide signaling: role of nitrite and nitrosothiols, Circ. Res., 108, 1448, 10.1161\u002FCIRCRESAHA.111.241117\nFarah, 2013, Exercise-induced cardioprotection: a role for eNOS uncoupling and NO metabolites, Basic Res. Cardiol., 108, 389, 10.1007\u002Fs00395-013-0389-2\nWang, 2017, Aerobic exercise protects against pressure overload-induced cardiac dysfunction and hypertrophy via β3-AR-nNOS-NO activation, PloS One, 12\nInserte, 2015, The cGMP\u002FPKG pathway as a common mediator of cardioprotection: translatability and mechanism, Br. J. Pharmacol., 172, 1996, 10.1111\u002Fbph.12959\nSun, 2013, Essential role of nitric oxide in acute ischemic preconditioning: S-Nitros(yl)ation versus sGC\u002FcGMP\u002FPKG signaling?, Free Radic. Biol. Med., 54, 105, 10.1016\u002Fj.freeradbiomed.2012.09.005\nMethner, 2013, Protection through postconditioning or a mitochondria-targeted S-nitrosothiol is unaffected by cardiomyocyte-selective ablation of protein kinase G, Basic Res. Cardiol., 108, 337, 10.1007\u002Fs00395-013-0337-1\nPenna, 2014, Protein S-nitrosylation in preconditioning and postconditioning, Exp. Biol. Med., 239, 647, 10.1177\u002F1535370214522935\nSun, 2010, Protein S-nitrosylation and cardioprotection, Circ. Res., 106, 285, 10.1161\u002FCIRCRESAHA.109.209452\nChouchani, 2017, Identification and quantification of protein S-nitrosation by nitrite in the mouse heart during ischemia, J. Biol. Chem., 292, 14486, 10.1074\u002Fjbc.M117.798744\nBrookes, 2004, Calcium, ATP, and ROS: a mitochondrial love-hate triangle, Am. J. Physiol. Cell Physiol., 287, C817, 10.1152\u002Fajpcell.00139.2004\nWang, 2005, Nitric oxide donors protect murine myocardium against infarction via modulation of mitochondrial permeability transition, Am. J. Physiol.-Heart Circ. Physiol., 288, H1290, 10.1152\u002Fajpheart.00796.2004\nBorutaite, 2006, S-nitrosothiol inhibition of mitochondrial complex I causes a reversible increase in mitochondrial hydrogen peroxide production, Biochim. Biophys. Acta BBA - Bioenerg., 1757, 562, 10.1016\u002Fj.bbabio.2006.02.014\nMethner, 2014, Mitochondria selective S-nitrosation by mitochondria-targeted S-nitrosothiol protects against post-infarct heart failure in mouse hearts, Eur. J. Heart Fail., 16, 712, 10.1002\u002Fejhf.100\nPrime, 2009, A mitochondria-targeted S-nitrosothiol modulates respiration, nitrosates thiols, and protects against ischemia-reperfusion injury, Proc. Natl. Acad. Sci. Unit. States Am., 106, 10764, 10.1073\u002Fpnas.0903250106\nErusalimsky, 2007, Nitric oxide and mitochondrial signaling: from physiology to pathophysiology, Arterioscler. Thromb. Vasc. Biol., 27, 2524, 10.1161\u002FATVBAHA.107.151167\nKohr, 2011, Characterization of potential S-nitrosylation sites in the myocardium, Am. J. Physiol. Heart Circ. Physiol., 300, H1327, 10.1152\u002Fajpheart.00997.2010\nBibli, 2019, Nitroglycerine limits infarct size through S-nitrosation of cyclophilin D: a novel mechanism for an old drug, Cardiovasc. Res., 115, 625, 10.1093\u002Fcvr\u002Fcvy222\nLacza, 2009, Mitochondrial nitric oxide synthase: current concepts and controversies, Front. Biosci. Landmark Ed., 14, 4436, 10.2741\u002F3539\nGao, 2004, Docking of endothelial nitric oxide synthase (eNOS) to the mitochondrial outer membrane A PENTABASIC amino acid sequence IN the autoinhibitory domain OF eNOS targets A proteinase K-cleavable peptide ON the cytoplasmic face OF mitochondria, J. Biol. Chem., 279, 15968, 10.1074\u002Fjbc.M308504200\nSun, 2012, Disruption of caveolae blocks ischemic preconditioning-mediated S-nitrosylation of mitochondrial proteins, Antioxidants Redox Signal., 16, 45, 10.1089\u002Fars.2010.3844\nFarah, 2015, NO better way to protect the heart during ischemia–reperfusion: to be in the right place at the right time, Front. Pediatr., 3, 10.3389\u002Ffped.2015.00006\nTatarkova, 2019, Tyrosine nitration of mitochondrial proteins during myocardial ischemia and reperfusion, J. Physiol. Biochem., 75, 217, 10.1007\u002Fs13105-019-00683-7\nKleindienst, 2016, Exercise does not activate the β3 adrenergic receptor–eNOS pathway, but reduces inducible NOS expression to protect the heart of obese diabetic mice, Basic Res. Cardiol., 111, 40, 10.1007\u002Fs00395-016-0559-0\nHall, 2014, Mitochondrial fusion and fission proteins: novel therapeutic targets for combating cardiovascular disease, Br. J. Pharmacol., 171, 1890, 10.1111\u002Fbph.12516\nSuárez-Rivero, 2016, Mitochondrial dynamics in mitochondrial diseases, Diseases, 5, 10.3390\u002Fdiseases5010001\nBrady, 2006, Proapoptotic BCL-2 family members and mitochondrial dysfunction during ischemia\u002Freperfusion injury, a study employing cardiac HL-1 cells and GFP biosensors, Biochim. Biophys. Acta, 1757, 667, 10.1016\u002Fj.bbabio.2006.04.011\nManeechote, 2018, Differential temporal inhibition of mitochondrial fission by Mdivi-1 exerts effective cardioprotection in cardiac ischemia\u002Freperfusion injury, Clin. Sci. Lond. Engl. 1979, 132, 1669\nSharp, 2014, Dynamin-related protein 1 (Drp1)-mediated diastolic dysfunction in myocardial ischemia-reperfusion injury: therapeutic benefits of Drp1 inhibition to reduce mitochondrial fission, FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol., 28, 316\nVásquez‐Trincado, 2016, Mitochondrial dynamics, mitophagy and cardiovascular disease, J. Physiol., 594, 509, 10.1113\u002FJP271301\nOng, 2010, Inhibiting mitochondrial fission protects the heart against ischemia\u002Freperfusion injury, Circulation, 121, 2012, 10.1161\u002FCIRCULATIONAHA.109.906610\nOng, 2012, New roles for mitochondria in cell death in the reperfused myocardium, Cardiovasc. Res., 94, 190, 10.1093\u002Fcvr\u002Fcvr312\nDong, 2016, Inhibition of mitochondrial fission as a molecular target for cardioprotection: critical importance of the timing of treatment, Basic Res. Cardiol., 111, 59, 10.1007\u002Fs00395-016-0578-x\nDing, 2018, Inhibition of drp1-mediated mitochondrial fission protects diabetic heart against ischemia-reperfusion injury, Diabetes, 67, 10.2337\u002Fdb18-408-P\nSharp, 2015, Inhibition of the mitochondrial fission protein Drp1 improves survival in a murine cardiac arrest model, Crit. Care Med., 43, e38, 10.1097\u002FCCM.0000000000000817\nStutzman, 2015, Mdivi-1, a novel mitochondrial fission inhibitor, exerts cardioprotective effects in myocardial ischemia\u002Freperfusion (MI\u002FR) injury, Faseb. J., 29, 10.1096\u002Ffasebj.29.1_supplement.1049.1\nHom, 2010, Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes, Biochim. Biophys. Acta, 1797, 913, 10.1016\u002Fj.bbabio.2010.03.018\nChen, 2008, Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria, Am. J. Physiol.-Cell Physiol., 294, C460, 10.1152\u002Fajpcell.00211.2007\nPlotnikov, 2008, Interrelations of mitochondrial fragmentation and cell death under ischemia\u002Freoxygenation and UV-irradiation: protective effects of SkQ1, lithium ions and insulin, FEBS Lett., 582, 3117, 10.1016\u002Fj.febslet.2008.08.002\nTeixeira de Lemos, 2012, Regular physical exercise as a strategy to improve antioxidant and anti-inflammatory status: benefits in type 2 diabetes mellitus, Oxid. Med. Cell. Longev., 2012, 10.1155\u002F2012\u002F741545\nSimioni, 2018, Oxidative stress: role of physical exercise and antioxidant nutraceuticals in adulthood and aging, Oncotarget, 9, 17181, 10.18632\u002Foncotarget.24729\nJiang, 2014, Aerobic interval training attenuates mitochondrial dysfunction in rats post-myocardial infarction: roles of mitochondrial network dynamics, Int. J. Mol. Sci., 15, 5304, 10.3390\u002Fijms15045304\nTwig, 2008, Fission and selective fusion govern mitochondrial segregation and elimination by autophagy, EMBO J., 27, 433, 10.1038\u002Fsj.emboj.7601963\nKubli, 2013, Parkin protein deficiency exacerbates cardiac injury and reduces survival following myocardial infarction, J. Biol. Chem., 288, 915, 10.1074\u002Fjbc.M112.411363\nSiddall, 2013, Loss of PINK1 increases the heart’s vulnerability to ischemia-reperfusion injury, PloS One, 8, 10.1371\u002Fannotation\u002F94fd6502-4b2d-409c-8836-66fe6ebc03ab\nHamacher-Brady, 2006, Enhancing macroautophagy protects against ischemia\u002Freperfusion injury in cardiac myocytes, J. Biol. Chem., 281, 29776, 10.1074\u002Fjbc.M603783200\nLee, 2017, Potential signaling pathways of acute endurance exercise-induced cardiac autophagy and mitophagy and its possible role in cardioprotection, J. Physiol. Sci., 67, 639, 10.1007\u002Fs12576-017-0555-7\nYuan, 2018, Parkin mediates mitophagy to participate in cardioprotection induced by late exercise preconditioning but Bnip3 does not, J. Cardiovasc. Pharmacol., 71, 303, 10.1097\u002FFJC.0000000000000572\nWest, 2011, Mitochondria in innate immune responses, Nat. Rev. Immunol., 11, 389, 10.1038\u002Fnri2975\nArslan, 2011, Innate immune signaling in cardiac ischemia, Nat. Rev. Cardiol., 8, 292, 10.1038\u002Fnrcardio.2011.38\nFrangogiannis, 2012, Regulation of the inflammatory response in cardiac repair, Circ. Res., 110, 159, 10.1161\u002FCIRCRESAHA.111.243162\nGleeson, 2011, The anti-inflammatory effects of exercise: mechanisms and implications for the prevention and treatment of disease, Nat. Rev. Immunol., 11, 607, 10.1038\u002Fnri3041\nEddy, 1992, Tumor necrosis factor-α pretreatment is protective in a rat model of myocardial ischemia-reperfusion injury, Biochem. Biophys. Res. Commun., 184, 1056, 10.1016\u002F0006-291X(92)90698-K\nBoyd, 2013, Reducing the intensity and volume of interval training diminishes cardiovascular adaptation but not mitochondrial biogenesis in overweight\u002Fobese men, PloS One, 8, 10.1371\u002Fjournal.pone.0068091\nChen, 2018, Exercise training augments Sirt1-signaling and attenuates cardiac inflammation in D-galactose induced-aging rats, Aging, 10, 4166, 10.18632\u002Faging.101714\nLiao, 2015, An anti-EpCAM antibody EpAb2-6 for the treatment of colon cancer, Oncotarget, 6, 24947, 10.18632\u002Foncotarget.4453\nEltzschig, 2011, Ischemia and reperfusion--from mechanism to translation, Nat. Med., 17, 1391, 10.1038\u002Fnm.2507\nMukhopadhyay, 2012, Mitochondrial reactive oxygen species generation triggers inflammatory response and tissue injury associated with hepatic ischemia-reperfusion: therapeutic potential of mitochondrially-targeted antioxidants, Free Radic. Biol. Med., 53, 1123, 10.1016\u002Fj.freeradbiomed.2012.05.036\nOtaka, 2018, Myonectin is an exercise-induced myokine that protects the heart from ischemia-reperfusion injury, Circ. Res., 123, 1326, 10.1161\u002FCIRCRESAHA.118.313777\nSharma, 2019, Temporal dynamics of pre and post myocardial infarcted tissue with concomitant preconditioning of aerobic exercise in chronic diabetic rats, Life Sci., 225, 79, 10.1016\u002Fj.lfs.2019.03.077\nTuon, 2015, Physical training regulates mitochondrial parameters and neuroinflammatory mechanisms in an experimental model of Parkinson’s disease, Oxid. Med. Cell. Longev., 10.1155\u002F2015\u002F261809\nTang, 2016, Sirt1 and the mitochondria, Mol. Cell, 39, 87, 10.14348\u002Fmolcells.2016.2318\nMa, 2017, SIRT1 activation by resveratrol alleviates cardiac dysfunction via mitochondrial regulation in diabetic cardiomyopathy mice, Oxid. Med. Cell. Longev., 2017, 4602715, 10.1155\u002F2017\u002F4602715\nChen, 2018, Role of Parkin and endurance training on mitochondrial turnover in skeletal muscle, Skeletal Muscle, 8, 10.1186\u002Fs13395-018-0157-y\nMichelsen, 2012, Exercise-induced cardioprotection is mediated by a bloodborne, transferable factor, Basic Res. Cardiol., 107, 260, 10.1007\u002Fs00395-012-0260-x\nZhang, 2006, Kappa-opioid receptors mediate cardioprotection by remote preconditioning, Anesthesiology, 105, 550, 10.1097\u002F00000542-200609000-00019\nSuvorava, 2018, Exercise-induced cardioprotection via eNOS: a putative role of red blood cell signaling, Curr. Med. Chem., 25, 4457, 10.2174\u002F0929867325666180307112557\nFiuza-Luces, 2018, Exercise benefits in cardiovascular disease: beyond attenuation of traditional risk factors, Nat. Rev. Cardiol., 15, 731, 10.1038\u002Fs41569-018-0065-1\nMcGinnis, 2015, Interleukin-6 mediates exercise preconditioning against myocardial ischemia reperfusion injury, Am. J. Physiol. Heart Circ. Physiol., 308, H1423, 10.1152\u002Fajpheart.00850.2014\nSmart, 2006, IL-6 induces PI 3-kinase and nitric oxide-dependent protection and preserves mitochondrial function in cardiomyocytes, Cardiovasc. Res., 69, 164, 10.1016\u002Fj.cardiores.2005.08.017\nQiu, 2015, Chronic exercise training and circulating irisin in adults: a meta-analysis, Sports Med. Auckl. NZ., 45, 1577, 10.1007\u002Fs40279-014-0293-4\nWang, 2017, Irisin plays a pivotal role to protect the heart against ischemia and reperfusion injury, J. Cell. Physiol., 232, 3775, 10.1002\u002Fjcp.25857\nBei, 2017, Exercise-induced circulating extracellular vesicles protect against cardiac ischemia-reperfusion injury, Basic Res. Cardiol., 112, 38, 10.1007\u002Fs00395-017-0628-z\nWang, 2020, Exercise protects the heart against myocardial infarction through upregulation of miR-1192, Biochem. Biophys. Res. Commun., 521, 1061, 10.1016\u002Fj.bbrc.2019.11.019\nHou, 2019, Longterm exercise-derived exosomal miR-342-5p: a novel exerkine for cardioprotection, Circ. Res., 124, 1386, 10.1161\u002FCIRCRESAHA.118.314635\nWang, 2018, Involvement of brain-derived neurotrophic factor in exercise-induced cardioprotection of post-myocardial infarction rats, Int. J. Mol. Med., 42, 2867\nCrisafulli, 2004, Exercise-induced and nitroglycerin-induced myocardial preconditioning improves hemodynamics in patients with angina, Am. J. Physiol. Heart Circ. 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2018, Role of TNF-TNF receptor 2 signal in regulatory T cells and its therapeutic implications, Front. Immunol., 9, 784, 10.3389\u002Ffimmu.2018.00784","https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffimmu.2018.00784",{"mag":1919,"pmc":1920,"openalex":1921,"pm":1922,"doi":1923},"2800399031","5916970","W2800399031","29725328","10.3389\u002Ffimmu.2018.00784",{"id":18,"text":1925,"url":1926,"identifiers":1927},"Beldi, 2020, TNFR2 is a crucial hub controlling mesenchymal stem cell biological and functional properties, Front. Cell Dev. Biol., 8, 10.3389\u002Ffcell.2020.596831","https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffcell.2020.596831",{"mag":1928,"pmc":1929,"openalex":1930,"pm":1931,"doi":1932},"3107363889","7746825","W3107363889","33344453","10.3389\u002Ffcell.2020.596831",{"id":18,"text":1934,"url":1935,"identifiers":1936},"Parameswaran, 2010, Tumor necrosis factor-α signaling in macrophages, Crit. Rev. Eukaryot. Gene Expr., 20, 87, 10.1615\u002FCritRevEukarGeneExpr.v20.i2.10","https:\u002F\u002Fdoi.org\u002F10.1615\u002Fcritreveukargeneexpr.v20.i2.10",{"mag":1937,"pmc":1938,"openalex":1939,"pm":1940,"doi":1941},"1997834526","3066460","W1997834526","21133840","10.1615\u002Fcritreveukargeneexpr.v20.i2.10",{"id":18,"text":1943,"url":1944,"identifiers":1945},"Xie, 2021, TNF-α-mediated m(6)A modification of ELMO1 triggers directional migration of mesenchymal stem cell in ankylosing spondylitis, Nat. Commun., 12, 5373, 10.1038\u002Fs41467-021-25710-4","http:\u002F\u002Fdx.doi.org\u002F10.1038\u002Fs41467-021-25710-4",{"doi":1946},"10.1038\u002Fs41467-021-25710-4",{"id":18,"text":1948,"url":1949,"identifiers":1950},"Kirwin, 2021, Mechanisms underlying the therapeutic potential of mesenchymal stem cells in atherosclerosis, Regen. Med., 16, 669, 10.2217\u002Frme-2021-0024","https:\u002F\u002Fdoi.org\u002F10.2217\u002Frme-2021-0024",{"mag":1951,"openalex":1952,"pm":1953,"doi":1954},"3173732164","W3173732164","34189963","10.2217\u002Frme-2021-0024",{"id":18,"text":1956,"url":1957,"identifiers":1958},"Wajant, 2019, TNFR1 and TNFR2 in the control of the life and death balance of macrophages, Front. Cell Dev. Biol., 7, 91, 10.3389\u002Ffcell.2019.00091","https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffcell.2019.00091",{"mag":1959,"pmc":1960,"openalex":1961,"pm":1962,"doi":1963},"2947512282","6548990","W2947512282","31192209","10.3389\u002Ffcell.2019.00091",{"id":1965,"text":1966,"url":1967,"identifiers":1968},"3bafdb2e-88cf-424e-93f4-6efa47846a7e","Beldi, 2020, TNFα\u002FTNFR2 signaling pathway: an active immune checkpoint for mesenchymal stem cell immunoregulatory function, Stem Cell Res. Ther., 11, 281, 10.1186\u002Fs13287-020-01740-5","https:\u002F\u002Fstemcellres.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13287-020-01740-5",{"doi":1969},"10.1186\u002Fs13287-020-01740-5",{"id":1971,"text":1972,"url":1973,"identifiers":1974},"217af3b4-c5a3-4018-bde3-2916fb1ebd97","Boland, 2018, IFN-γ and TNF-α pre-licensing protects mesenchymal stromal cells from the pro-inflammatory effects of palmitate, Mol. Ther., 26, 860, 10.1016\u002Fj.ymthe.2017.12.013","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS152500161730610X",{"doi":1975},"10.1016\u002Fj.ymthe.2017.12.013",{"id":18,"text":1977,"url":1978,"identifiers":1979},"Hong, 2020, miR-155-5p inhibition rejuvenates aged mesenchymal stem cells and enhances cardioprotection following infarction, Aging Cell, 19, 10.1111\u002Facel.13128","https:\u002F\u002Fdoi.org\u002F10.1111\u002Facel.13128",{"mag":1980,"pmc":1981,"openalex":1982,"pm":1983,"doi":1984},"3010888780","7189985","W3010888780","32196916","10.1111\u002Facel.13128",{"id":1986,"text":1987,"url":1988,"identifiers":1989},"447939d7-ee8d-45c0-97b5-5f87dd2bd1e3","Klecker, 2017, Lipid droplets guard mitochondria during autophagy, Dev. Cell, 42, 1, 10.1016\u002Fj.devcel.2017.06.018","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1534580717305063",{"doi":1990},"10.1016\u002Fj.devcel.2017.06.018",{"id":1992,"text":1993,"url":1994,"identifiers":1995},"dcedeb22-a108-413d-bcb4-a097bf033a8d","Chen, 2020, Role of oxidative stress in the pathogenesis of nonalcoholic fatty liver disease, Free Radic. Biol. Med., 152, 116, 10.1016\u002Fj.freeradbiomed.2020.02.025","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0891584919315151",{"doi":1996},"10.1016\u002Fj.freeradbiomed.2020.02.025",{"id":18,"text":1998,"url":1999,"identifiers":2000},"Turinetto, 2016, Senescence in human mesenchymal stem cells: functional changes and implications in stem cell-based therapy, Int. J. Mol. Sci., 17, 1164, 10.3390\u002Fijms17071164","https:\u002F\u002Fdoi.org\u002F10.3390\u002Fijms17071164",{"mag":2001,"pmc":2002,"openalex":2003,"pm":2004,"doi":2005},"2494515430","4964536","W2494515430","27447618","10.3390\u002Fijms17071164",{"id":18,"text":2007,"url":2008,"identifiers":2009},"Fafián-Labora, 2019, FASN activity is important for the initial stages of the induction of senescence, Cell Death Dis., 10, 318, 10.1038\u002Fs41419-019-1550-0","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41419-019-1550-0",{"mag":2010,"pmc":2011,"openalex":2012,"pm":2013,"doi":2014},"2929830445","6453932","W2929830445","30962418","10.1038\u002Fs41419-019-1550-0",{"id":18,"text":2016,"url":2017,"identifiers":2018},"Xie, 2020, NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential, Signal Transduct. Targeted Ther., 5, 227, 10.1038\u002Fs41392-020-00311-7","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41392-020-00311-7",{"mag":2019,"pmc":2020,"openalex":2021,"pm":2022,"doi":2023},"3092621787","7539288","W3092621787","33028824","10.1038\u002Fs41392-020-00311-7",{"id":18,"text":2025,"url":2026,"identifiers":2027},"Kratz, 2021, Sirtuins as important factors in pathological states and the role of their molecular activity modulators, Int. J. Mol. Sci., 22, 630, 10.3390\u002Fijms22020630","https:\u002F\u002Fdoi.org\u002F10.3390\u002Fijms22020630",{"mag":2028,"pmc":2029,"openalex":2030,"pm":2031,"doi":2032},"3118766162","7827102","W3118766162","33435263","10.3390\u002Fijms22020630",{"id":18,"text":2034,"url":2035,"identifiers":2036},"Denu, 2017, SIRT3 enhances mesenchymal stem cell longevity and differentiation, Oxid. Med. Cell. Longev., 2017, 10.1155\u002F2017\u002F5841716","https:\u002F\u002Fdoi.org\u002F10.1155\u002F2017\u002F5841716",{"mag":2037,"pmc":2038,"openalex":2039,"pm":2040,"doi":2041},"2671520429","5499245","W2671520429","28717408","10.1155\u002F2017\u002F5841716",{"id":18,"text":2043,"url":2044,"identifiers":2045},"Oh, 2019, 17β-Estradiol protects mesenchymal stem cells against high glucose-induced mitochondrial oxidants production via Nrf2\u002FSirt3\u002FMnSOD signaling, Free Radic. Biol. Med., 130, 328, 10.1016\u002Fj.freeradbiomed.2018.11.003","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002Fj.freeradbiomed.2018.11.003",{"doi":2046},"10.1016\u002Fj.freeradbiomed.2018.11.003",{"id":2048,"text":2049,"url":2050,"identifiers":2051},"99f11b2b-40bf-4315-8736-6b60d6d3ad55","Constanze, 2020, Evidence that TNF-β suppresses osteoblast differentiation of mesenchymal stem cells and resveratrol reverses it through modulation of NF-κB, Sirt1 and Runx2, Cell Tissue Res., 381, 83, 10.1007\u002Fs00441-020-03188-8","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs00441-020-03188-8",{"doi":2052},"10.1007\u002Fs00441-020-03188-8",{"id":2054,"text":2055,"url":2056,"identifiers":2057},"4c68646b-0035-4279-8000-0006b275d4fa","Zuo, 2019, TNF-α-mediated upregulation of SOD-2 contributes to cell proliferation and cisplatin resistance in esophageal squamous cell carcinoma, Oncol. Rep., 42, 1497","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":2058},"10.1007\u002Fs10440-022-00541-7",{"id":18,"text":2060,"url":2061,"identifiers":2062},"Warren, 2019, Regulation of adaptive immune cells by sirtuins, Front. Endocrinol., 10, 466, 10.3389\u002Ffendo.2019.00466","https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffendo.2019.00466",{"mag":2063,"pmc":2064,"openalex":2065,"pm":2066,"doi":2067},"2956308291","6637536","W2956308291","31354630","10.3389\u002Ffendo.2019.00466",{"id":18,"text":2069,"url":2070,"identifiers":2071},"Denu, 2016, Effects of oxidative stress on mesenchymal stem cell biology, Oxid. Med. Cell. Longev., 10.1155\u002F2016\u002F2989076","https:\u002F\u002Fdoi.org\u002F10.1155\u002F2016\u002F2989076",{"mag":2072,"pmc":2073,"openalex":2074,"pm":2075,"doi":2076},"2433697453","4928004","W2433697453","27413419","10.1155\u002F2016\u002F2989076",{"id":18,"text":2078,"url":2079,"identifiers":2080},"Wu, 2022, TNF antagonist sensitizes synovial fibroblasts to ferroptotic cell death in collagen-induced arthritis mouse models, Nat. Commun., 13, 676, 10.1038\u002Fs41467-021-27948-4","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41467-021-27948-4",{"openalex":2081,"pm":2082,"doi":2083},"W4210367362","35115492","10.1038\u002Fs41467-021-27948-4",{"id":18,"text":2085,"url":2086,"identifiers":2087},"Grant, 2015, Fat in flames: influence of cytokines and pattern recognition receptors on adipocyte lipolysis, Am. J. Physiol. Endocrinol. Metab., 309, E205, 10.1152\u002Fajpendo.00053.2015","https:\u002F\u002Fdoi.org\u002F10.1152\u002Fajpendo.00053.2015",{"mag":2088,"openalex":2089,"pm":2090,"doi":2091},"1962531591","W1962531591","26058863","10.1152\u002Fajpendo.00053.2015",{"id":18,"text":2093,"url":2094,"identifiers":2095},"Wiley, 2021, The metabolic roots of senescence: mechanisms and opportunities for intervention, Nat. metab., 3, 1290, 10.1038\u002Fs42255-021-00483-8","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs42255-021-00483-8",{"mag":2096,"openalex":2097,"pm":2098,"doi":2099},"3206142581","W3206142581","34663974","10.1038\u002Fs42255-021-00483-8",{"id":18,"text":2101,"url":2102,"identifiers":2103},"Li, 2019, Sirt5 attenuates cisplatin-induced acute kidney injury through regulation of Nrf2\u002FHO-1 and Bcl-2, BioMed Res. Int., 2019, 10.1155\u002F2019\u002F4745132","https:\u002F\u002Fdoi.org\u002F10.1155\u002F2019\u002F4745132",{"mag":2104,"pmc":2105,"openalex":2106,"pm":2107,"doi":2108},"2985425212","6878818","W2985425212","31815138","10.1155\u002F2019\u002F4745132",{"id":2054,"text":2110,"url":2056,"identifiers":2111},"Jarc, 2019, Lipid droplets and the management of cellular stress, Yale J. Biol. Med., 92, 435",{"doi":2058},{"id":18,"text":2113,"url":2114,"identifiers":2115},"Crescenzi, 2011, NF-κB-dependent cytokine secretion controls Fas expression on chemotherapy-induced premature senescent tumor cells, Oncogene, 30, 2707, 10.1038\u002Fonc.2011.1","http:\u002F\u002Fdx.doi.org\u002F10.1038\u002Fonc.2011.1",{"doi":2116},"10.1038\u002Fonc.2011.1",{"id":18,"text":2118,"url":2119,"identifiers":2120},"Meital, 2019, Omega-3 fatty acids decrease oxidative stress and inflammation in macrophages from patients with small abdominal aortic aneurysm, Sci. Rep., 9, 10.1038\u002Fs41598-019-49362-z","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41598-019-49362-z",{"mag":2121,"pmc":2122,"openalex":2123,"pm":2124,"doi":2125},"2972749395","6736886","W2972749395","31506475","10.1038\u002Fs41598-019-49362-z",{"id":18,"text":2127,"url":2128,"identifiers":2129},"Darlington, 2001, Antioxidants and fatty acids in the amelioration of rheumatoid arthritis and related disorders, Br. J. Nutr., 85, 251, 10.1079\u002FBJN2000239","https:\u002F\u002Fdoi.org\u002F10.1079\u002Fbjn2000239",{"mag":2130,"openalex":2131,"pm":2132,"doi":2133},"2142328693","W2142328693","11299072","10.1079\u002Fbjn2000239",{"id":2135,"text":2136,"url":2137,"identifiers":2138},"ef268c94-74b7-4f9e-a4a8-1265d10cca8c","Nguyen, 2017, DGAT1-dependent lipid droplet biogenesis protects mitochondrial function during starvation-induced autophagy, Dev. Cell, 42, 9, 10.1016\u002Fj.devcel.2017.06.003","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1534580717304598",{"doi":2139},"10.1016\u002Fj.devcel.2017.06.003",{"id":18,"text":2141,"url":2142,"identifiers":2143},"Geltinger, 2020, Friend or Foe: lipid droplets as organelles for protein and lipid storage in cellular stress response, aging and disease, Molecules, 25, 10.3390\u002Fmolecules25215053","https:\u002F\u002Fdoi.org\u002F10.3390\u002Fmolecules25215053",{"mag":2144,"pmc":2145,"openalex":2146,"pm":2147,"doi":2148},"3096053618","7663626","W3096053618","33143278","10.3390\u002Fmolecules25215053",{"id":18,"text":2150,"url":2151,"identifiers":2152},"Feldman, 2013, Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins, J. Biol. Chem., 288, 31350, 10.1074\u002Fjbc.C113.511261","https:\u002F\u002Fdoi.org\u002F10.1074\u002Fjbc.c113.511261",{"mag":2153,"pmc":2154,"openalex":2155,"pm":2156,"doi":2157},"2061576857","3829447","W2061576857","24052263","10.1074\u002Fjbc.c113.511261",{"id":18,"text":2159,"url":2160,"identifiers":2161},"Chiba, 2019, Sirtuin 5 regulates proximal tubule fatty acid oxidation to protect against AKI, J. Am. Soc. Nephrol., 30, 2384, 10.1681\u002FASN.2019020163","https:\u002F\u002Fdoi.org\u002F10.1681\u002Fasn.2019020163",{"mag":2162,"pmc":2163,"openalex":2164,"pm":2165,"doi":2166},"2978876764","6900790","W2978876764","31575700","10.1681\u002Fasn.2019020163",{"id":18,"text":2168,"url":2169,"identifiers":2170},"Shi, 2018, MSCs protect endothelial cells from inflammatory injury partially by secreting STC1, Int. Immunopharm., 61, 109, 10.1016\u002Fj.intimp.2018.05.016","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.intimp.2018.05.016",{"mag":2171,"openalex":2172,"pm":2173,"doi":2174},"2806311477","W2806311477","29857240","10.1016\u002Fj.intimp.2018.05.016",{"id":2176,"text":2177,"url":2178,"identifiers":2179},"195d57c6-836c-4784-b872-207f3dfdc383","Domingues, 2019, Antioxidant-upregulated mesenchymal stem cells reduce inflammation and improve fatty liver disease in diet-induced obesity, Stem Cell Res. Ther., 10, 280, 10.1186\u002Fs13287-019-1393-8","https:\u002F\u002Fstemcellres.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13287-019-1393-8",{"doi":2180},"10.1186\u002Fs13287-019-1393-8",{"id":18,"text":2182,"url":2183,"identifiers":2184},"Grdina, 2013, A manganese superoxide dismutase (SOD2)-mediated adaptive response, Radiat. Res., 179, 115, 10.1667\u002FRR3126.2","https:\u002F\u002Fdoi.org\u002F10.1667\u002Frr3126.2",{"mag":2185,"pmc":2186,"openalex":2187,"pm":2188,"doi":2189},"2163554836","3594688","W2163554836","23237540","10.1667\u002Frr3126.2",{"id":2191,"text":2192,"url":2193,"identifiers":2194},"4a7e87c4-f95a-4952-b7bf-afbaba5aec72","Dai, 2020, Nrf2: redox and metabolic regulator of stem cell state and function, Trends Mol. Med., 26, 185, 10.1016\u002Fj.molmed.2019.09.007","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1471491419302461",{"doi":2195},"10.1016\u002Fj.molmed.2019.09.007",{"id":18,"text":2197,"url":2198,"identifiers":2199},"He, 2019, SOD2 acetylation on lysine 68 promotes stem cell reprogramming in breast cancer, Proc. Natl. Acad. Sci. U. S. A., 116, 23534, 10.1073\u002Fpnas.1902308116","https:\u002F\u002Fdoi.org\u002F10.1073\u002Fpnas.1902308116",{"mag":2200,"pmc":2201,"openalex":2202,"pm":2203,"doi":2204},"2980111553","6876149","W2980111553","31591207","10.1073\u002Fpnas.1902308116",{"id":18,"text":2206,"url":2207,"identifiers":2208},"Sun, 2019, SIRT5 promotes cisplatin resistance in ovarian cancer by suppressing DNA damage in a ROS-dependent manner via regulation of the Nrf2\u002FHO-1 pathway, Front. Oncol., 9, 754, 10.3389\u002Ffonc.2019.00754","https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffonc.2019.00754",{"mag":2209,"pmc":2210,"openalex":2211,"pm":2212,"doi":2213},"2965445632","6700301","W2965445632","31456942","10.3389\u002Ffonc.2019.00754",{"id":18,"text":2215,"url":2216,"identifiers":2217},"Luque-Campos, 2019, Mesenchymal stem cells improve rheumatoid arthritis progression by controlling memory T cell response, Front. Immunol., 10, 798, 10.3389\u002Ffimmu.2019.00798","https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffimmu.2019.00798",{"mag":2218,"pmc":2219,"openalex":2220,"pm":2221,"doi":2222},"2936335917","6477064","W2936335917","31040848","10.3389\u002Ffimmu.2019.00798",{"id":2224,"text":2225,"url":2226,"identifiers":2227},"9c3eb9ba-1b02-4435-8074-e5cf2a2bc1c5","Zhao, 2021, sTNFRII-Fc modification protects human UC-MSCs against apoptosis\u002Fautophagy induced by TNF-α and enhances their efficacy in alleviating inflammatory arthritis, Stem Cell Res. Ther., 12, 535, 10.1186\u002Fs13287-021-02602-4","https:\u002F\u002Fstemcellres.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs13287-021-02602-4",{"doi":2228},"10.1186\u002Fs13287-021-02602-4",{"id":18,"text":2230,"url":2231,"identifiers":2232},"Zhang, 2020, Sirtuin 5 deficiency increases disease severity in rats with adjuvant-induced arthritis, Cell. Mol. Immunol., 17, 1190, 10.1038\u002Fs41423-020-0380-4","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41423-020-0380-4",{"mag":2233,"pmc":2234,"openalex":2235,"pm":2236,"doi":2237},"3007664438","7784877","W3007664438","32099074","10.1038\u002Fs41423-020-0380-4",{"id":2239,"text":2240,"url":2241,"identifiers":2242},"7ba4d248-4dcf-4e17-ac57-ce373610061c","Flynn, 2007, UC blood-derived mesenchymal stromal cells: an overview, Cytotherapy, 9, 717, 10.1080\u002F14653240701584578","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1465324907701408",{"doi":2243},"10.1080\u002F14653240701584578",{"id":18,"text":2245,"url":2246,"identifiers":2247},"Secco, 2008, Multipotent stem cells from umbilical cord: cord is richer than blood, Stem Cells, 26, 146, 10.1634\u002Fstemcells.2007-0381","https:\u002F\u002Fdoi.org\u002F10.1634\u002Fstemcells.2007-0381",{"mag":2248,"openalex":2249,"pm":2250,"doi":2251},"1990758819","W1990758819","17932423","10.1634\u002Fstemcells.2007-0381",{"id":18,"text":2253,"url":2254,"identifiers":2255},"Chang, 2013, Timing of umbilical cord blood derived mesenchymal stem cells transplantation determines therapeutic efficacy in the neonatal hyperoxic lung injury, PLoS One, 8, 10.1371\u002Fjournal.pone.0052419","https:\u002F\u002Fdoi.org\u002F10.1371\u002Fjournal.pone.0052419",{"mag":2256,"pmc":2257,"openalex":2258,"pm":2259,"doi":2260},"2016671483","3549907","W2016671483","23349686","10.1371\u002Fjournal.pone.0052419"]