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Volumn 49, Issue 3, 2010, Pages 343-346

Between nitros(yl)ation and nitration: Regulation of thioredoxin-1 in myocardial ischemia/reperfusion injury

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS SIGNAL REGULATING KINASE 1; CYCLOSPORIN A; LINSIDOMINE; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; THIOREDOXIN 1; THIOREDOXIN INTERACTING PROTEIN;

EID: 77955279147     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2010.06.001     Document Type: Editorial
Times cited : (5)

References (61)
  • 1
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 1989, 264:13963-13966.
    • (1989) J Biol Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 2
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J., Arner E.S. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 2001, 31:1287-1312.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 3
    • 0036290861 scopus 로고    scopus 로고
    • Thioredoxin superfamily and thioredoxin-inducing agents
    • Hirota K., Nakamura H., Masutani H., Yodoi J. Thioredoxin superfamily and thioredoxin-inducing agents. Ann N Y Acad Sci 2002, 957:189-199.
    • (2002) Ann N Y Acad Sci , vol.957 , pp. 189-199
    • Hirota, K.1    Nakamura, H.2    Masutani, H.3    Yodoi, J.4
  • 4
    • 0035943725 scopus 로고    scopus 로고
    • Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa
    • Miranda-Vizuete A., Ljung J., Damdimopoulos A.E., et al. Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa. J Biol Chem 2001, 276:31567-31574.
    • (2001) J Biol Chem , vol.276 , pp. 31567-31574
    • Miranda-Vizuete, A.1    Ljung, J.2    Damdimopoulos, A.E.3
  • 6
    • 0029939584 scopus 로고    scopus 로고
    • A novel promoter sequence is involved in the oxidative stress-induced expression of the adult T-cell leukemia-derived factor (ADF)/human thioredoxin (Trx) gene
    • Taniguchi Y., Taniguchi-Ueda Y., Mori K., Yodoi J. A novel promoter sequence is involved in the oxidative stress-induced expression of the adult T-cell leukemia-derived factor (ADF)/human thioredoxin (Trx) gene. Nucleic Acids Res 1996, 24:2746-2752.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2746-2752
    • Taniguchi, Y.1    Taniguchi-Ueda, Y.2    Mori, K.3    Yodoi, J.4
  • 7
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren A. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 1995, 3:239-243.
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 8
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae H.Z., Chung S.J., Rhee S.G. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 1994, 269:27670-27678.
    • (1994) J Biol Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 9
    • 77955270298 scopus 로고    scopus 로고
    • Nitrative inactivation of thioredoxin-1 increases vulnerability of diabetic hearts to ischemia/reperfusion injury
    • Yin T., Hou R., Liu S., Lau W.B., Wang H., Tao L. Nitrative inactivation of thioredoxin-1 increases vulnerability of diabetic hearts to ischemia/reperfusion injury. J Mol Cell Cardiol 2010.
    • (2010) J Mol Cell Cardiol
    • Yin, T.1    Hou, R.2    Liu, S.3    Lau, W.B.4    Wang, H.5    Tao, L.6
  • 10
    • 0034685659 scopus 로고    scopus 로고
    • A possible interaction of thioredoxin with VDUP1 in HeLa cells detected in a yeast two-hybrid system
    • Yamanaka H., Maehira F., Oshiro M., et al. A possible interaction of thioredoxin with VDUP1 in HeLa cells detected in a yeast two-hybrid system. Biochem Biophys Res Commun 2000, 271:796-800.
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 796-800
    • Yamanaka, H.1    Maehira, F.2    Oshiro, M.3
  • 11
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • Liu H., Nishitoh H., Ichijo H., Kyriakis J.M. Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol Cell Biol 2000, 20:2198-2208.
    • (2000) Mol Cell Biol , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 12
    • 0037188936 scopus 로고    scopus 로고
    • Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner
    • Liu Y., Min W. Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner. Circ Res 2002, 90:1259-1266.
    • (2002) Circ Res , vol.90 , pp. 1259-1266
    • Liu, Y.1    Min, W.2
  • 13
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M., Nishitoh H., Fujii M., et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 1998, 17:2596-2606.
    • (1998) EMBO J , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3
  • 14
    • 0033618398 scopus 로고    scopus 로고
    • Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression
    • Nishiyama A., Matsui M., Iwata S., et al. Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression. J Biol Chem 1999, 274:21645-21650.
    • (1999) J Biol Chem , vol.274 , pp. 21645-21650
    • Nishiyama, A.1    Matsui, M.2    Iwata, S.3
  • 15
    • 3142751251 scopus 로고    scopus 로고
    • Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein
    • Schulze P.C., Yoshioka J., Takahashi T., He Z., King G.L., Lee R.T. Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein. J Biol Chem 2004, 279:30369-30374.
    • (2004) J Biol Chem , vol.279 , pp. 30369-30374
    • Schulze, P.C.1    Yoshioka, J.2    Takahashi, T.3    He, Z.4    King, G.L.5    Lee, R.T.6
  • 16
    • 10644245123 scopus 로고    scopus 로고
    • Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1
    • Hwang C.Y., Ryu Y.S., Chung M.S., et al. Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1. Oncogene 2004, 23:8868-8875.
    • (2004) Oncogene , vol.23 , pp. 8868-8875
    • Hwang, C.Y.1    Ryu, Y.S.2    Chung, M.S.3
  • 17
    • 0035895885 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: role of thioredoxin in NF-kappaB activation
    • Das K.C. c-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: role of thioredoxin in NF-kappaB activation. J Biol Chem 2001, 276:4662-4670.
    • (2001) J Biol Chem , vol.276 , pp. 4662-4670
    • Das, K.C.1
  • 18
    • 36048960679 scopus 로고    scopus 로고
    • Nuclear redox-signaling is essential for apoptosis inhibition in endothelial cells-important role for nuclear thioredoxin-1
    • Schroeder P., Popp R., Wiegand B., Altschmied J., Haendeler J. Nuclear redox-signaling is essential for apoptosis inhibition in endothelial cells-important role for nuclear thioredoxin-1. Arterioscler Thromb Vasc Biol 2007, 27:2325-2331.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2325-2331
    • Schroeder, P.1    Popp, R.2    Wiegand, B.3    Altschmied, J.4    Haendeler, J.5
  • 19
    • 0023821864 scopus 로고
    • Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • Crompton M., Ellinger H., Costi A. Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem J 1988, 255:357-360.
    • (1988) Biochem J , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 20
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines C.P., Kaiser R.A., Purcell N.H., et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 2005, 434:658-662.
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3
  • 21
    • 77951294419 scopus 로고    scopus 로고
    • Cyclosporine A at reperfusion reduces infarct size in pigs
    • Skyschally A., Schulz R., Heusch G. Cyclosporine A at reperfusion reduces infarct size in pigs. Cardiovasc Drugs Ther 2010, 24:85-87.
    • (2010) Cardiovasc Drugs Ther , vol.24 , pp. 85-87
    • Skyschally, A.1    Schulz, R.2    Heusch, G.3
  • 22
    • 57149142916 scopus 로고    scopus 로고
    • Cardiac myocyte-specific expression of inducible nitric oxide synthase protects against ischemia/reperfusion injury by preventing mitochondrial permeability transition
    • West M.B., Rokosh G., Obal D., et al. Cardiac myocyte-specific expression of inducible nitric oxide synthase protects against ischemia/reperfusion injury by preventing mitochondrial permeability transition. Circulation 2008, 118:1970-1978.
    • (2008) Circulation , vol.118 , pp. 1970-1978
    • West, M.B.1    Rokosh, G.2    Obal, D.3
  • 23
    • 18344418791 scopus 로고    scopus 로고
    • The nitric oxide hypothesis of late preconditioning
    • Bolli R., Dawn B., Tang X.L., et al. The nitric oxide hypothesis of late preconditioning. Basic Res Cardiol 1998, 93:325-338.
    • (1998) Basic Res Cardiol , vol.93 , pp. 325-338
    • Bolli, R.1    Dawn, B.2    Tang, X.L.3
  • 24
    • 1142285456 scopus 로고    scopus 로고
    • Nitric oxide in myocardial ischemia/reperfusion injury
    • Schulz R., Kelm M., Heusch G. Nitric oxide in myocardial ischemia/reperfusion injury. Cardiovasc Res 2004, 61:402-413.
    • (2004) Cardiovasc Res , vol.61 , pp. 402-413
    • Schulz, R.1    Kelm, M.2    Heusch, G.3
  • 25
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium
    • Murry C.E., Jennings R.B., Reimer K.A. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 1986, 74:1124-1136.
    • (1986) Circulation , vol.74 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 26
    • 0037623908 scopus 로고    scopus 로고
    • Inhibition of myocardial injury by ischemic postconditioning during reperfusion: comparison with ischemic preconditioning
    • Zhao Z.Q., Corvera J.S., Halkos M.E., et al. Inhibition of myocardial injury by ischemic postconditioning during reperfusion: comparison with ischemic preconditioning. Am J Physiol Heart Circ Physiol 2003, 285:H579-H588.
    • (2003) Am J Physiol Heart Circ Physiol , vol.285
    • Zhao, Z.Q.1    Corvera, J.S.2    Halkos, M.E.3
  • 28
    • 77249107745 scopus 로고    scopus 로고
    • Remote ischaemic conditioning before hospital admission, as a complement to angioplasty, and effect on myocardial salvage in patients with acute myocardial infarction: a randomised trial
    • Botker H.E., Kharbanda R., Schmidt M.R., et al. Remote ischaemic conditioning before hospital admission, as a complement to angioplasty, and effect on myocardial salvage in patients with acute myocardial infarction: a randomised trial. Lancet 2010, 375:727-734.
    • (2010) Lancet , vol.375 , pp. 727-734
    • Botker, H.E.1    Kharbanda, R.2    Schmidt, M.R.3
  • 29
    • 33646072198 scopus 로고    scopus 로고
    • Postconditioning: reduction of reperfusion-induced injury
    • Zhao Z.Q., Vinten-Johansen J. Postconditioning: reduction of reperfusion-induced injury. Cardiovasc Res 2006, 70:200-211.
    • (2006) Cardiovasc Res , vol.70 , pp. 200-211
    • Zhao, Z.Q.1    Vinten-Johansen, J.2
  • 30
    • 41149145607 scopus 로고    scopus 로고
    • Pathophysiology of myocardial infarction: protection by ischemic pre- and postconditioning
    • Skyschally A., Schulz R., Heusch G. Pathophysiology of myocardial infarction: protection by ischemic pre- and postconditioning. Herz 2008, 33:88-100.
    • (2008) Herz , vol.33 , pp. 88-100
    • Skyschally, A.1    Schulz, R.2    Heusch, G.3
  • 31
    • 0038279860 scopus 로고    scopus 로고
    • Thioredoxin redox signaling in the ischemic heart: an insight with transgenic mice overexpressing Trx1
    • Turoczi T., Chang V.W., Engelman R.M., Maulik N., Ho Y.S., Das D.K. Thioredoxin redox signaling in the ischemic heart: an insight with transgenic mice overexpressing Trx1. J Mol Cell Cardiol 2003, 35:695-704.
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 695-704
    • Turoczi, T.1    Chang, V.W.2    Engelman, R.M.3    Maulik, N.4    Ho, Y.S.5    Das, D.K.6
  • 32
    • 50849100393 scopus 로고    scopus 로고
    • Sustained cardioprotection: exploring unconventional modalities
    • Peart J.N., Headrick J.P. Sustained cardioprotection: exploring unconventional modalities. Vascul Pharmacol 2008, 49:63-70.
    • (2008) Vascul Pharmacol , vol.49 , pp. 63-70
    • Peart, J.N.1    Headrick, J.P.2
  • 33
    • 33947681723 scopus 로고    scopus 로고
    • Ischemic preconditioning triggers nuclear translocation of thioredoxin and its interaction with Ref-1 potentiating a survival signal through the PI-3-kinase-Akt pathway
    • Malik G., Gorbounov N., Das S., et al. Ischemic preconditioning triggers nuclear translocation of thioredoxin and its interaction with Ref-1 potentiating a survival signal through the PI-3-kinase-Akt pathway. Antioxid Redox Signal 2006, 8:2101-2109.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 2101-2109
    • Malik, G.1    Gorbounov, N.2    Das, S.3
  • 34
    • 0345737283 scopus 로고    scopus 로고
    • Signal transduction through nuclear factor kappa B in ischemia-reperfusion and heart failure
    • Valen G. Signal transduction through nuclear factor kappa B in ischemia-reperfusion and heart failure. Basic Res Cardiol 2004, 99:1-7.
    • (2004) Basic Res Cardiol , vol.99 , pp. 1-7
    • Valen, G.1
  • 35
    • 57949097756 scopus 로고    scopus 로고
    • Innate immunity and myocardial adaptation to ischemia
    • Valeur H.S., Valen G. Innate immunity and myocardial adaptation to ischemia. Basic Res Cardiol 2009, 104:22-32.
    • (2009) Basic Res Cardiol , vol.104 , pp. 22-32
    • Valeur, H.S.1    Valen, G.2
  • 36
    • 0347986778 scopus 로고    scopus 로고
    • Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy
    • Yamamoto M., Yang G., Hong C., et al. Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy. J Clin Invest 2003, 112:1395-1406.
    • (2003) J Clin Invest , vol.112 , pp. 1395-1406
    • Yamamoto, M.1    Yang, G.2    Hong, C.3
  • 37
    • 0037056109 scopus 로고    scopus 로고
    • Overexpression of thioredoxin-1 in transgenic mice attenuates adriamycin-induced cardiotoxicity
    • Shioji K., Kishimoto C., Nakamura H., et al. Overexpression of thioredoxin-1 in transgenic mice attenuates adriamycin-induced cardiotoxicity. Circulation 2002, 106:1403-1409.
    • (2002) Circulation , vol.106 , pp. 1403-1409
    • Shioji, K.1    Kishimoto, C.2    Nakamura, H.3
  • 39
    • 3843054499 scopus 로고    scopus 로고
    • Cardioprotective effects of thioredoxin in myocardial ischemia and reperfusion: role of S-nitrosylation [corrected]
    • Tao L., Gao E., Bryan N.S., et al. Cardioprotective effects of thioredoxin in myocardial ischemia and reperfusion: role of S-nitrosylation [corrected]. Proc Natl Acad Sci U S A 2004, 101:11471-11476.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 11471-11476
    • Tao, L.1    Gao, E.2    Bryan, N.S.3
  • 42
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • Haendeler J., Hoffmann J., Tischler V., Berk B.C., Zeiher A.M., Dimmeler S. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat Cell Biol 2002, 4:743-749.
    • (2002) Nat Cell Biol , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 43
    • 4143102291 scopus 로고    scopus 로고
    • Antioxidant effects of statins via S-nitrosylation and activation of thioredoxin in endothelial cells: a novel vasculoprotective function of statins
    • Haendeler J., Hoffmann J., Zeiher A.M., Dimmeler S. Antioxidant effects of statins via S-nitrosylation and activation of thioredoxin in endothelial cells: a novel vasculoprotective function of statins. Circulation 2004, 110:856-861.
    • (2004) Circulation , vol.110 , pp. 856-861
    • Haendeler, J.1    Hoffmann, J.2    Zeiher, A.M.3    Dimmeler, S.4
  • 44
    • 18444369324 scopus 로고    scopus 로고
    • Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems
    • Casagrande S., Bonetto V., Fratelli M., et al. Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems. Proc Natl Acad Sci U S A 2002, 99:9745-9749.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9745-9749
    • Casagrande, S.1    Bonetto, V.2    Fratelli, M.3
  • 46
    • 0029927487 scopus 로고    scopus 로고
    • The role of glutathione in the transport and catabolism of nitric oxide
    • Hogg N., Singh R.J., Kalyanaraman B. The role of glutathione in the transport and catabolism of nitric oxide. FEBS Lett 1996, 382:223-228.
    • (1996) FEBS Lett , vol.382 , pp. 223-228
    • Hogg, N.1    Singh, R.J.2    Kalyanaraman, B.3
  • 48
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi R., Beckman J.S., Bush K.M., Freeman B.A. Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J Biol Chem 1991, 266:4244-4250.
    • (1991) J Biol Chem , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 49
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction
    • Greenacre S.A., Ischiropoulos H. Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction. Free Radic Res 2001, 34:541-581.
    • (2001) Free Radic Res , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 50
    • 33749035991 scopus 로고    scopus 로고
    • Nitrative inactivation of thioredoxin-1 and its role in postischemic myocardial apoptosis
    • Tao L., Jiao X., Gao E., et al. Nitrative inactivation of thioredoxin-1 and its role in postischemic myocardial apoptosis. Circulation 2006, 114:1395-1402.
    • (2006) Circulation , vol.114 , pp. 1395-1402
    • Tao, L.1    Jiao, X.2    Gao, E.3
  • 51
    • 67650257495 scopus 로고    scopus 로고
    • High glucose sensitizes adult cardiomyocytes to ischaemia/reperfusion injury through nitrative thioredoxin inactivation
    • Luan R., Liu S., Yin T., et al. High glucose sensitizes adult cardiomyocytes to ischaemia/reperfusion injury through nitrative thioredoxin inactivation. Cardiovasc Res 2009, 83:294-302.
    • (2009) Cardiovasc Res , vol.83 , pp. 294-302
    • Luan, R.1    Liu, S.2    Yin, T.3
  • 52
    • 0035843914 scopus 로고    scopus 로고
    • Role of NADPH oxidase in the vascular hypertrophic and oxidative stress response to angiotensin II in mice
    • Wang H.D., Xu S., Johns D.G., et al. Role of NADPH oxidase in the vascular hypertrophic and oxidative stress response to angiotensin II in mice. Circ Res 2001, 88:947-953.
    • (2001) Circ Res , vol.88 , pp. 947-953
    • Wang, H.D.1    Xu, S.2    Johns, D.G.3
  • 53
    • 0029841018 scopus 로고    scopus 로고
    • Measurement of nitric oxide and peroxynitrite generation in the postischemic heart. Evidence for peroxynitrite-mediated reperfusion injury
    • Wang P., Zweier J.L. Measurement of nitric oxide and peroxynitrite generation in the postischemic heart. Evidence for peroxynitrite-mediated reperfusion injury. J Biol Chem 1996, 271:29223-29230.
    • (1996) J Biol Chem , vol.271 , pp. 29223-29230
    • Wang, P.1    Zweier, J.L.2
  • 54
    • 0032964853 scopus 로고    scopus 로고
    • Selective nitration of prostacyclin synthase and defective vasorelaxation in atherosclerotic bovine coronary arteries
    • Zou M.H., Leist M., Ullrich V. Selective nitration of prostacyclin synthase and defective vasorelaxation in atherosclerotic bovine coronary arteries. Am J Pathol 1999, 154:1359-1365.
    • (1999) Am J Pathol , vol.154 , pp. 1359-1365
    • Zou, M.H.1    Leist, M.2    Ullrich, V.3
  • 55
    • 0034939115 scopus 로고    scopus 로고
    • The role of oxidative stress in the onset and progression of diabetes and its complications: a summary of a Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society
    • Rosen P., Nawroth P.P., King G., Moller W., Tritschler H.J., Packer L. The role of oxidative stress in the onset and progression of diabetes and its complications: a summary of a Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society. Diabetes Metab Res Rev 2001, 17:189-212.
    • (2001) Diabetes Metab Res Rev , vol.17 , pp. 189-212
    • Rosen, P.1    Nawroth, P.P.2    King, G.3    Moller, W.4    Tritschler, H.J.5    Packer, L.6
  • 56
    • 0033555139 scopus 로고    scopus 로고
    • The peroxynitrite generator, SIN-1, becomes a nitric oxide donor in the presence of electron acceptors
    • Singh R.J., Hogg N., Joseph J., Konorev E., Kalyanaraman B. The peroxynitrite generator, SIN-1, becomes a nitric oxide donor in the presence of electron acceptors. Arch Biochem Biophys 1999, 361:331-339.
    • (1999) Arch Biochem Biophys , vol.361 , pp. 331-339
    • Singh, R.J.1    Hogg, N.2    Joseph, J.3    Konorev, E.4    Kalyanaraman, B.5
  • 57
    • 52049087608 scopus 로고    scopus 로고
    • Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues
    • Hashemy S.I., Holmgren A. Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues. J Biol Chem 2008, 283:21890-21898.
    • (2008) J Biol Chem , vol.283 , pp. 21890-21898
    • Hashemy, S.I.1    Holmgren, A.2
  • 58
    • 14444281569 scopus 로고    scopus 로고
    • Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways
    • Ichijo H., Nishida E., Irie K., et al. Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 1997, 275:90-94.
    • (1997) Science , vol.275 , pp. 90-94
    • Ichijo, H.1    Nishida, E.2    Irie, K.3
  • 60
    • 34147099428 scopus 로고    scopus 로고
    • A peptide inhibitor of c-Jun NH2-terminal kinase reduces myocardial ischemia-reperfusion injury and infarct size in vivo
    • Milano G., Morel S., Bonny C., et al. A peptide inhibitor of c-Jun NH2-terminal kinase reduces myocardial ischemia-reperfusion injury and infarct size in vivo. Am J Physiol Heart Circ Physiol 2007, 292:H1828-H1835.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Milano, G.1    Morel, S.2    Bonny, C.3


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