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Volumn 292, Issue 3, 2007, Pages

Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: Implications for diseases in the cardiovascular system

Author keywords

Apoptotic signaling; Glutathione; Myocardial remodeling; Oxidative stress; Thiol disulfide oxidoreductases

Indexed keywords

AMINO ACID DERIVATIVE; APOPTOSIS SIGNAL REGULATING KINASE 1; BINDING PROTEIN; CISTEINYLPROLYLTYROSYLCYSTEINE; CISTEINYLSERYLTYROSYLCYSTEINE; CYSTEINYLGLYCYLPROLYLCYSTEINE; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE REDUCTASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; RAS PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOL DERIVATIVE; THIOREDOXIN; THIOREDOXIN BINDING PROTEIN 2; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

EID: 33847746679     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.01162.2006     Document Type: Review
Times cited : (297)

References (156)
  • 1
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathionylation of ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • Adachi T, Pimentel DR, Heibeck T, Hou X, Lee YJ, Jiang B, Ido Y, Cohen RA. S-glutathionylation of ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J Biol Chem 279: 29857-29862, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 2
    • 33750384450 scopus 로고    scopus 로고
    • Thioredoxin and ventricular remodeling
    • Ago T, Sadoshima J. Thioredoxin and ventricular remodeling. J Mol Cell Cardiol 41: 762-773, 2006.
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 762-773
    • Ago, T.1    Sadoshima, J.2
  • 3
    • 0030903691 scopus 로고    scopus 로고
    • Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues
    • Akamatsu Y, Ohno T, Hirota K, Kagoshima H, Yodoi J, Shigesada K. Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues. J Biol Chem 272: 14497-14500, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 14497-14500
    • Akamatsu, Y.1    Ohno, T.2    Hirota, K.3    Kagoshima, H.4    Yodoi, J.5    Shigesada, K.6
  • 6
    • 0031973308 scopus 로고    scopus 로고
    • Bandyopadhyay S, Starke DW, Mieyal JJ, Gronostajski RM. Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I. J. Biol Chem 273: 392-397, 1998.
    • Bandyopadhyay S, Starke DW, Mieyal JJ, Gronostajski RM. Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I. J. Biol Chem 273: 392-397, 1998.
  • 8
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyses the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins
    • Beer SM, Taylor ER, Brown SE, Dahm CC, Costa NJ, Runswick MJ, Murphy MP. Glutaredoxin 2 catalyses the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins. J Biol Chem 279: 47939-47951, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6    Murphy, M.P.7
  • 11
    • 28844497646 scopus 로고    scopus 로고
    • Extracellular human thioredoxin-1 inhibits lipopolysaccharide- induced interleukin-1beta expression in human monocyte-derived macrophages
    • Billiet L, Furman C, Larigauderi G, Copin C, Brand K, Fruchart JC, Rouis M. Extracellular human thioredoxin-1 inhibits lipopolysaccharide- induced interleukin-1beta expression in human monocyte-derived macrophages. J Biol Chem 280: 40310-40318, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 40310-40318
    • Billiet, L.1    Furman, C.2    Larigauderi, G.3    Copin, C.4    Brand, K.5    Fruchart, J.C.6    Rouis, M.7
  • 12
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Bjornstedt M, Xue J, Huang W, Akesson B, Holmgren A. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J Biol Chem 269: 29382-29384, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 29382-29384
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3    Akesson, B.4    Holmgren, A.5
  • 13
    • 0026132288 scopus 로고
    • Characterization of two thioredoxins in pig heart including a new mitochondrial protein
    • Bodenstein J, Follmann H. Characterization of two thioredoxins in pig heart including a new mitochondrial protein. Z Naturforsch [C] 46: 270-279, 1991.
    • (1991) Z Naturforsch [C] , vol.46 , pp. 270-279
    • Bodenstein, J.1    Follmann, H.2
  • 14
    • 0020582583 scopus 로고
    • Biochemistry and physiological role of methionine sulfoxide residues in proteins
    • Brot N, Weissbach H. Biochemistry and physiological role of methionine sulfoxide residues in proteins. Arch Biochem Biophys 223: 271-281, 1983.
    • (1983) Arch Biochem Biophys , vol.223 , pp. 271-281
    • Brot, N.1    Weissbach, H.2
  • 15
    • 0026799490 scopus 로고
    • Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14 - S) and its mixed disulfide with glutathione
    • Bushweller JH, Aslund F, Wüthrich K, Holmgren A. Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14 - S) and its mixed disulfide with glutathione. Biochemistry 31: 9288-9293, 1992.
    • (1992) Biochemistry , vol.31 , pp. 9288-9293
    • Bushweller, J.H.1    Aslund, F.2    Wüthrich, K.3    Holmgren, A.4
  • 17
    • 0034714319 scopus 로고    scopus 로고
    • Acute cadmium exposure inactivates thioltransferase (glutaredoxin) inhibits intracellular reduction of protein-glutathionyl-mixed disulfides and initiates apoptosis
    • Chrestensen CA, Starke DW, Mieyal JJ. Acute cadmium exposure inactivates thioltransferase (glutaredoxin) inhibits intracellular reduction of protein-glutathionyl-mixed disulfides and initiates apoptosis. J Biol Chem 275: 26556-26565, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 26556-26565
    • Chrestensen, C.A.1    Starke, D.W.2    Mieyal, J.J.3
  • 19
    • 0035877650 scopus 로고    scopus 로고
    • Glutaredoxin protects cerebellar granulae neurons from dopamine-induced apoptosis by dual activation of the Ras-phosphoinositide 3-kinase and Jun N-terminal kinase pathway
    • Daily D, Vlamis-Gardikas A, Offen D, Mittelmann L, Melamed E, Holmgren A, Barzilai A. Glutaredoxin protects cerebellar granulae neurons from dopamine-induced apoptosis by dual activation of the Ras-phosphoinositide 3-kinase and Jun N-terminal kinase pathway. J Biol Chem 276: 21618-21626, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 21618-21626
    • Daily, D.1    Vlamis-Gardikas, A.2    Offen, D.3    Mittelmann, L.4    Melamed, E.5    Holmgren, A.6    Barzilai, A.7
  • 20
    • 0035847101 scopus 로고    scopus 로고
    • Glutaredoxin protects cerebellar granulae neurons from dopamine-induced apoptosis by activating NF-kappaB via Ref-1
    • Daily D, Vlamis-Gardikas A, Offen D, Mittelmann L, Melamed E, Holmgren A, Barzilai A. Glutaredoxin protects cerebellar granulae neurons from dopamine-induced apoptosis by activating NF-kappaB via Ref-1. J Biol Chem 276: 1335-1344, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 1335-1344
    • Daily, D.1    Vlamis-Gardikas, A.2    Offen, D.3    Mittelmann, L.4    Melamed, E.5    Holmgren, A.6    Barzilai, A.7
  • 21
    • 1542514717 scopus 로고    scopus 로고
    • Thioredoxin regulation of ischemic preconditioning
    • Das D. Thioredoxin regulation of ischemic preconditioning. Antioxid Redox Signal 6: 405-412, 2004.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 405-412
    • Das, D.1
  • 22
    • 0027312173 scopus 로고
    • Molecular adaption of cellular defenses following preconditioning of the heart by repeated ischemia
    • Das D, Engelman RM, Kimura Y. Molecular adaption of cellular defenses following preconditioning of the heart by repeated ischemia. Cardiovasc Res 27: 578-584, 1993.
    • (1993) Cardiovasc Res , vol.27 , pp. 578-584
    • Das, D.1    Engelman, R.M.2    Kimura, Y.3
  • 24
    • 0030851732 scopus 로고    scopus 로고
    • Davis DA, Newcomb FM, Starke DW, Ott DE, Mieyal JJ, Yarchoan R. Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. J Biol Chem 272: 25935-42590, 1997.
    • Davis DA, Newcomb FM, Starke DW, Ott DE, Mieyal JJ, Yarchoan R. Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. J Biol Chem 272: 25935-42590, 1997.
  • 25
    • 0036773760 scopus 로고    scopus 로고
    • Prevention of apoptosis by deferoxamine during 4 hours of cold cardioplegia and reperfusion: In vitro study of isolated working rat heart model
    • Dobsak P, Siegelova J, Wolf JE, Rochette L, Eicher JC, Vasku J, Kuchtickova S, Horky M. Prevention of apoptosis by deferoxamine during 4 hours of cold cardioplegia and reperfusion: in vitro study of isolated working rat heart model. Pathophysiology 9: 27-32, 2002.
    • (2002) Pathophysiology , vol.9 , pp. 27-32
    • Dobsak, P.1    Siegelova, J.2    Wolf, J.E.3    Rochette, L.4    Eicher, J.C.5    Vasku, J.6    Kuchtickova, S.7    Horky, M.8
  • 26
    • 33646108133 scopus 로고    scopus 로고
    • Status of some free radical scavenging enzymes in the blood of myocardial infarction patients
    • Dwivedi VK, Chandra M, Misra PC, Misra A, Misra MK. Status of some free radical scavenging enzymes in the blood of myocardial infarction patients. J Enzyme Inhib Med Chem 21: 43-46, 2006.
    • (2006) J Enzyme Inhib Med Chem , vol.21 , pp. 43-46
    • Dwivedi, V.K.1    Chandra, M.2    Misra, P.C.3    Misra, A.4    Misra, M.K.5
  • 30
    • 0037293568 scopus 로고    scopus 로고
    • Nitric oxide superoxide and peroxynitrite in myocardial ischemia-reperfusion injury and preconditioning
    • Ferdinandy P, Schulz R. Nitric oxide superoxide and peroxynitrite in myocardial ischemia-reperfusion injury and preconditioning. Br J Pharmacol 138: 532-543, 2003.
    • (2003) Br J Pharmacol , vol.138 , pp. 532-543
    • Ferdinandy, P.1    Schulz, R.2
  • 32
    • 0035821279 scopus 로고    scopus 로고
    • Pathophysiology of chronic heart failure
    • Francis GS. Pathophysiology of chronic heart failure. Am J Med 110: 37S-46S, 2001.
    • (2001) Am J Med , vol.110
    • Francis, G.S.1
  • 34
    • 33746921195 scopus 로고    scopus 로고
    • Oxidative stress in hepatic ischemia-reperfusion injury: The role of antioxidants and iron chelating compounds
    • Galaris D, Barbouti A, Korantzopoulos P. Oxidative stress in hepatic ischemia-reperfusion injury: the role of antioxidants and iron chelating compounds. Curr Pharm Des 12: 2875-2890, 2006.
    • (2006) Curr Pharm Des , vol.12 , pp. 2875-2890
    • Galaris, D.1    Barbouti, A.2    Korantzopoulos, P.3
  • 35
    • 0029973142 scopus 로고    scopus 로고
    • Selenocysteine identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase corresponds to TGA in the human placental gene
    • Gladyshev VN, Jeang KT, Stadtman TC. Selenocysteine identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase corresponds to TGA in the human placental gene. Proc Natl Acad Sci USA 93: 6146-6151, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6146-6151
    • Gladyshev, V.N.1    Jeang, K.T.2    Stadtman, T.C.3
  • 37
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina SA, Mieyal JJ. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32: 3368-3376, 1993.
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 38
    • 0142055950 scopus 로고    scopus 로고
    • Oxidative stress and cardiovascular injury. Part I: Basic mechanisms and in vivo monitoring of ROS
    • Griendling KK, Fitzgerald GA. Oxidative stress and cardiovascular injury. Part I: basic mechanisms and in vivo monitoring of ROS. Circulation 108: 1912-1916, 2003.
    • (2003) Circulation , vol.108 , pp. 1912-1916
    • Griendling, K.K.1    Fitzgerald, G.A.2
  • 39
    • 0021962337 scopus 로고
    • Proof that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxin
    • Grippo JF, Holmgren A, Pratt WB. Proof that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxin. J Biol Chem 260: 93-97, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 93-97
    • Grippo, J.F.1    Holmgren, A.2    Pratt, W.B.3
  • 40
    • 0025676018 scopus 로고
    • Reoxigenation injury and antioxidant protection: A tale of two paradoxes
    • Gutteridge JMC, Halliwell B. Reoxigenation injury and antioxidant protection: a tale of two paradoxes. Arch Biochem Biophys 283: 223-226, 1990.
    • (1990) Arch Biochem Biophys , vol.283 , pp. 223-226
    • Gutteridge, J.M.C.1    Halliwell, B.2
  • 42
    • 0030838711 scopus 로고    scopus 로고
    • Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator
    • Hayashi S, Hajiro-Nakanishi K, Makino Y, Eguchi H, Yodoi J, Tanaka H. Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator. Nucleic Acids Res 25: 4035-4040, 1997.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4035-4040
    • Hayashi, S.1    Hajiro-Nakanishi, K.2    Makino, Y.3    Eguchi, H.4    Yodoi, J.5    Tanaka, H.6
  • 43
    • 0027217531 scopus 로고
    • Oxidoreductive regulation of nuclear factor kappa-B. Involvement of a cellular reducing catalyst thioredoxin
    • Hayashi T, Uedo Y, Okamato T. Oxidoreductive regulation of nuclear factor kappa-B. Involvement of a cellular reducing catalyst thioredoxin. J Biol Chem 268: 11380-11388, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 11380-11388
    • Hayashi, T.1    Uedo, Y.2    Okamato, T.3
  • 44
    • 0030936568 scopus 로고    scopus 로고
    • AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1
    • Hirota K, Matsui M, Iwata S, Nishiyama A, Mori K, Yodoi J. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci USA 94: 3633-3638, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3633-3638
    • Hirota, K.1    Matsui, M.2    Iwata, S.3    Nishiyama, A.4    Mori, K.5    Yodoi, J.6
  • 47
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 264: 13963-13966, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 48
    • 2042476756 scopus 로고
    • Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione
    • Holmgren A. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc Natl Acad Sci USA 73: 2275-2279, 1976.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 49
    • 0018080325 scopus 로고
    • Glutathione-dependent enzyme reactions of the phage T4 ribonucleotide reductase system
    • Holmgren A. Glutathione-dependent enzyme reactions of the phage T4 ribonucleotide reductase system. J Biol Chem 253: 7424-7430, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 7424-7430
    • Holmgren, A.1
  • 50
    • 0018786716 scopus 로고
    • Glutathione-dependent synthesis of deoxyribonucleotides. Characterisation of the enzymatic mechanism of Escherichia coli glutaredoxin
    • Holmgren A. Glutathione-dependent synthesis of deoxyribonucleotides. Characterisation of the enzymatic mechanism of Escherichia coli glutaredoxin. J Biol Chem 254: 3672-3678, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 3672-3678
    • Holmgren, A.1
  • 52
    • 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 3: 239-243, 1995.
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 53
    • 0018196480 scopus 로고
    • Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay
    • Holmgren A, Luthman M. Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay. Biochemistry 17: 4071-4077, 1978.
    • (1978) Biochemistry , vol.17 , pp. 4071-4077
    • Holmgren, A.1    Luthman, M.2
  • 57
    • 8844228265 scopus 로고    scopus 로고
    • Elevated circulating levels of thioredoxin and stress in chronic heart failure
    • Jekell A, Hossain A, Alehagen U, Dahlstrom U, Rosen A. Elevated circulating levels of thioredoxin and stress in chronic heart failure. Eur J Heart Fail 6: 883-890, 2004.
    • (2004) Eur J Heart Fail , vol.6 , pp. 883-890
    • Jekell, A.1    Hossain, A.2    Alehagen, U.3    Dahlstrom, U.4    Rosen, A.5
  • 59
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • Johansson C, Lillig CH, Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J Biol Chem 279: 7537-7543, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 61
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis GB, Holmgren A. Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J Biol Chem 255: 10261-10265, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 10261-10265
    • Kallis, G.B.1    Holmgren, A.2
  • 65
    • 0033578759 scopus 로고    scopus 로고
    • The immune system in viral myocarditis: Maintaining the balance
    • Knowlton KV, Badorff C. The immune system in viral myocarditis: maintaining the balance. Circ Res 99: 559-561, 1999.
    • (1999) Circ Res , vol.99 , pp. 559-561
    • Knowlton, K.V.1    Badorff, C.2
  • 67
    • 14944371448 scopus 로고    scopus 로고
    • Alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidative modification of thiols on Ras
    • Kuster GM, Pimentel DR, Adachi T, Ido Y, Brenner DA, Cohen RA, Liao R, Siwik DA, Colucci WS. Alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidative modification of thiols on Ras. Circulation 111: 1192-1198, 2005.
    • (2005) Circulation , vol.111 , pp. 1192-1198
    • Kuster, G.M.1    Pimentel, D.R.2    Adachi, T.3    Ido, Y.4    Brenner, D.A.5    Cohen, R.A.6    Liao, R.7    Siwik, D.A.8    Colucci, W.S.9
  • 68
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin the hydrogen donor from Escherichia coli
    • Laurent TC, Moore EC, Reichard P. Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin the hydrogen donor from Escherichia coli. J Biol Chem 239: 3436-3444, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 69
    • 0032563204 scopus 로고    scopus 로고
    • Purification molecular cloning and characterization of TRP32 a novel thioredoxin-related mammalian protein of 32 kDa
    • Lee KK, Murakawa M, Takahashi S, Tsubuki S, Kawashima S, Sakamaki K, Yonehara S. Purification molecular cloning and characterization of TRP32 a novel thioredoxin-related mammalian protein of 32 kDa. J Biol Chem 273: 19160-19166, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 19160-19166
    • Lee, K.K.1    Murakawa, M.2    Takahashi, S.3    Tsubuki, S.4    Kawashima, S.5    Sakamaki, K.6    Yonehara, S.7
  • 70
    • 0028630777 scopus 로고
    • Tissue iron overload and mechanisms of iron-catalyzed oxidative injury
    • Lesnefsky EJ. Tissue iron overload and mechanisms of iron-catalyzed oxidative injury. Adv Exp Med Biol 366: 129-146, 1994.
    • (1994) Adv Exp Med Biol , vol.366 , pp. 129-146
    • Lesnefsky, E.J.1
  • 71
    • 0025286817 scopus 로고
    • Elevated circulating levels of tumor necrosis factor in servere chronic heart failure
    • Levine B, Kalman J, Mayer L, Fillit HM, Packer M. Elevated circulating levels of tumor necrosis factor in servere chronic heart failure. N Engl J Med 323: 236-341, 1990.
    • (1990) N Engl J Med , vol.323 , pp. 236-341
    • Levine, B.1    Kalman, J.2    Mayer, L.3    Fillit, H.M.4    Packer, M.5
  • 74
    • 4444337091 scopus 로고    scopus 로고
    • Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells towards doxorubicin and phenylarsine oxide
    • Lillig CH, Lönn ME, Enoksson M, Fernandes AP, Holmgren A. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells towards doxorubicin and phenylarsine oxide. Proc Natl Acad Sci USA 101: 13227-13232, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13227-13232
    • Lillig, C.H.1    Lönn, M.E.2    Enoksson, M.3    Fernandes, A.P.4    Holmgren, A.5
  • 75
    • 0032543374 scopus 로고    scopus 로고
    • Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: Catalysis by glutaredoxin
    • Lind C, Gerdes R, Schuppe-Koistinen I, Cotgreave IA. Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. Biochem Biophys Res Commun 247: 481-486, 1998.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 481-486
    • Lind, C.1    Gerdes, R.2    Schuppe-Koistinen, I.3    Cotgreave, I.A.4
  • 76
    • 2942555274 scopus 로고    scopus 로고
    • Cellular and plasma levels of human glutaredoxin 1 and 2 detected by sensitive ELISA systems
    • Lundberg M, Fernandes AP, Kumar S, Holmgren A. Cellular and plasma levels of human glutaredoxin 1 and 2 detected by sensitive ELISA systems. Biochem Biophys Res Commun 319: 801-809, 2004.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 801-809
    • Lundberg, M.1    Fernandes, A.P.2    Kumar, S.3    Holmgren, A.4
  • 78
    • 0028901726 scopus 로고
    • Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase
    • Lundstrom-Ljung J, Holmgren A. Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase. J Biol Chem 270: 7822-7828, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 7822-7828
    • Lundstrom-Ljung, J.1    Holmgren, A.2
  • 79
    • 0020488534 scopus 로고
    • Rat liver thioredoxin and thioredoxin reductase: Purification and characterization
    • Luthman M, Holmgren A. Rat liver thioredoxin and thioredoxin reductase: Purification and characterization. Biochemistry 21: 6628-6633, 1982.
    • (1982) Biochemistry , vol.21 , pp. 6628-6633
    • Luthman, M.1    Holmgren, A.2
  • 81
    • 0029165589 scopus 로고
    • Thioredoxin - a fold for all reasons
    • Martin JL. Thioredoxin - a fold for all reasons. Structure 3: 245-250, 1995.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 83
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kappa-B by reducing a disulfide bond involving cysteine 62
    • Matthews JR, Wakasugi N, Virelizier JL, Yodoi J, Hay RT. Thioredoxin regulates the DNA binding activity of NF-kappa-B by reducing a disulfide bond involving cysteine 62. Nucleic Acids Res 20: 3821-3830, 1992.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.L.3    Yodoi, J.4    Hay, R.T.5
  • 84
    • 0033066832 scopus 로고    scopus 로고
    • Differential regulation of BCL-2 AP-1 and NF-kB on cardiomyocyte apoptosis during myocardial ischemic stress adaption
    • Maulik N, Sasaki H, Addya S, Das D. Differential regulation of BCL-2 AP-1 and NF-kB on cardiomyocyte apoptosis during myocardial ischemic stress adaption. FEBS Lett 443: 331-336, 2000.
    • (2000) FEBS Lett , vol.443 , pp. 331-336
    • Maulik, N.1    Sasaki, H.2    Addya, S.3    Das, D.4
  • 85
    • 0032537424 scopus 로고    scopus 로고
    • An essential role of NFkB in tyrosine kinase signaling of p38 MAP kinase regulation of myocardial adaption to ischemia
    • Maulik N, Sato M, Price BD, Das D. An essential role of NFkB in tyrosine kinase signaling of p38 MAP kinase regulation of myocardial adaption to ischemia. FEBS Lett 429: 365-369, 1998.
    • (1998) FEBS Lett , vol.429 , pp. 365-369
    • Maulik, N.1    Sato, M.2    Price, B.D.3    Das, D.4
  • 86
    • 0033048005 scopus 로고    scopus 로고
    • Thioltransferase overexpression increases resistance of MCF-7 cells to adriamycin
    • Meyer EB, Wells WW. Thioltransferase overexpression increases resistance of MCF-7 cells to adriamycin. Free Radic Biol Med 26: 770-776, 1999.
    • (1999) Free Radic Biol Med , vol.26 , pp. 770-776
    • Meyer, E.B.1    Wells, W.W.2
  • 88
    • 2942547764 scopus 로고    scopus 로고
    • Thioredoxin a redox-regulating protein is expressed in spontanous myocarditis in inbred strains of mice
    • Miyamoto M, Kishimoto C, Nimata M, Nakamura H, Yodoi J. Thioredoxin a redox-regulating protein is expressed in spontanous myocarditis in inbred strains of mice. Int J Cardiol 95: 315-319, 2004.
    • (2004) Int J Cardiol , vol.95 , pp. 315-319
    • Miyamoto, M.1    Kishimoto, C.2    Nimata, M.3    Nakamura, H.4    Yodoi, J.5
  • 90
    • 33645990964 scopus 로고    scopus 로고
    • Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria
    • Molina-Navarro MM, Casas C, Piedrafita L, Belli G, Herrero E. Prokaryotic and eukaryotic monothiol glutaredoxins are able to perform the functions of Grx5 in the biogenesis of Fe/S clusters in yeast mitochondria. FEBS Lett 580: 2273-2280, 2006.
    • (2006) FEBS Lett , vol.580 , pp. 2273-2280
    • Molina-Navarro, M.M.1    Casas, C.2    Piedrafita, L.3    Belli, G.4    Herrero, E.5
  • 91
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Mühlenhoff U, Gerber J, Richhardt N, Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J 22: 4815-4825, 2003.
    • (2003) EMBO J , vol.22 , pp. 4815-4825
    • Mühlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 92
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • Murray CE, Jennings RB, Reimer KA. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 74: 1124-1136, 1986.
    • (1986) Circulation , vol.74 , pp. 1124-1136
    • Murray, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 94
    • 0032078806 scopus 로고    scopus 로고
    • Measurements of plasma glutaredoxin and thioredoxin in healthy volunteers and during open-heart surgery
    • Nakamura H, Vaage J, Valen G, Padilla CA, Bjornstedt M, Holmgren A. Measurements of plasma glutaredoxin and thioredoxin in healthy volunteers and during open-heart surgery. Free Radic Biol Med 24: 1176-1186, 1998.
    • (1998) Free Radic Biol Med , vol.24 , pp. 1176-1186
    • Nakamura, H.1    Vaage, J.2    Valen, G.3    Padilla, C.A.4    Bjornstedt, M.5    Holmgren, A.6
  • 95
    • 0032827583 scopus 로고    scopus 로고
    • Mouse glutaredoxin - cDNA cloning high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2
    • Nakamura T, Ohno T, Hirota K, Nishiyama A, Nakamura H, Wada H, Yodoi J. Mouse glutaredoxin - cDNA cloning high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2. Free Radic Res 31: 357-365, 1999.
    • (1999) Free Radic Res , vol.31 , pp. 357-365
    • Nakamura, T.1    Ohno, T.2    Hirota, K.3    Nishiyama, A.4    Nakamura, H.5    Wada, H.6    Yodoi, J.7
  • 96
    • 33750907851 scopus 로고    scopus 로고
    • The role of apoptosis signal-regulating kinase 1 in cardiomycyte apoptosis
    • Nishida K, Otsu K. The role of apoptosis signal-regulating kinase 1 in cardiomycyte apoptosis. Antioxid Redox Signal 8: 1729-1736, 2006.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1729-1736
    • Nishida, K.1    Otsu, K.2
  • 98
    • 0037305881 scopus 로고    scopus 로고
    • The absence of mitochondrial thioredoxin 2 causes massive apoptosis exencephaly and early embryonic lethality in homozygous mice
    • Nonn L, Williams RR, Erickson RP, Powis G. The absence of mitochondrial thioredoxin 2 causes massive apoptosis exencephaly and early embryonic lethality in homozygous mice. Mol Cell Biol 23: 916-922, 2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 916-922
    • Nonn, L.1    Williams, R.R.2    Erickson, R.P.3    Powis, G.4
  • 100
    • 0037432192 scopus 로고    scopus 로고
    • Effect of classic preconditioning on the gene expression pattern of rat hearts: A DNA microarray study
    • Onody A, Zvara A, Hackler L, Vigh L Jr, Ferndinandy P, Puskas LB. Effect of classic preconditioning on the gene expression pattern of rat hearts: a DNA microarray study. FEBS Lett 536: 35-40, 2003.
    • (2003) FEBS Lett , vol.536 , pp. 35-40
    • Onody, A.1    Zvara, A.2    Hackler, L.3    Vigh Jr, L.4    Ferndinandy, P.5    Puskas, L.B.6
  • 101
    • 11144269771 scopus 로고    scopus 로고
    • PKC mediates cyclic stretch-induced cardiac hypertrophy through rho family GTPases and mitogen-activated protein kinases in cardiomyocytes
    • Pan J, Singh US, Takahashi T, Oka Y, Palm-Leis A, Herbelin BS, Baker KM. PKC mediates cyclic stretch-induced cardiac hypertrophy through rho family GTPases and mitogen-activated protein kinases in cardiomyocytes. J Cell Physiol 202: 536-553, 2005.
    • (2005) J Cell Physiol , vol.202 , pp. 536-553
    • Pan, J.1    Singh, U.S.2    Takahashi, T.3    Oka, Y.4    Palm-Leis, A.5    Herbelin, B.S.6    Baker, K.M.7
  • 102
    • 0024743065 scopus 로고
    • The mechanisms of reduction of protein mixed disulfides (dethiolation) in cardiac tissue
    • Park EM, Thomas JA. The mechanisms of reduction of protein mixed disulfides (dethiolation) in cardiac tissue. Arch Biochem Biophys 274: 47-54, 1989.
    • (1989) Arch Biochem Biophys , vol.274 , pp. 47-54
    • Park, E.M.1    Thomas, J.A.2
  • 103
  • 105
    • 2542486403 scopus 로고    scopus 로고
    • Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue
    • Reddy S, Jones AD, Cross CE, Wong PSY, van der Vliet A. Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. Biochem J 347: 824-827, 2000.
    • (2000) Biochem J , vol.347 , pp. 824-827
    • Reddy, S.1    Jones, A.D.2    Cross, C.E.3    Wong, P.S.Y.4    van der Vliet, A.5
  • 106
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee SG, Chae HY, Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic Biol Med 38: 1543-1552, 2005.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Y.2    Kim, K.3
  • 107
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodriguez-Manzaneque MT, Tamarit J, Belli G, Ros J, Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell 13: 1109-1121, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 108
    • 0033552883 scopus 로고    scopus 로고
    • Atheriosclerosis: An inflammatory disease
    • Ross R. Atheriosclerosis: an inflammatory disease. N Engl J Med 340: 115-126, 1999.
    • (1999) N Engl J Med , vol.340 , pp. 115-126
    • Ross, R.1
  • 109
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • Rubartelli A, Bajetto A, Allavena G, Wollman E, Sitia R. Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J Biol Chem 267: 24161-24164, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 24161-24164
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia, R.5
  • 110
    • 0342275186 scopus 로고    scopus 로고
    • Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A
    • Ruoppolo M, Lundstrom-Ljung J, Talamo F, Pucci P, Marino G. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A. Biochemistry 36: 12259-12267, 1997.
    • (1997) Biochemistry , vol.36 , pp. 12259-12267
    • Ruoppolo, M.1    Lundstrom-Ljung, J.2    Talamo, F.3    Pucci, P.4    Marino, G.5
  • 111
    • 33750925507 scopus 로고    scopus 로고
    • Redox regulation of growth and death in cardiac myocytes
    • Sadoshima J. Redox regulation of growth and death in cardiac myocytes. Antioxid Redox Signal 8: 1621-1624, 2006.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1621-1624
    • Sadoshima, J.1
  • 115
    • 33847747954 scopus 로고    scopus 로고
    • Inhibition of cell growth in: Cell and tissue culture
    • Schafer FQ, Buettner GR. Inhibition of cell growth in: cell and tissue culture. Free Radic Biol Med 30: 238-239, 2001.
    • (2001) Free Radic Biol Med , vol.30 , pp. 238-239
    • Schafer, F.Q.1    Buettner, G.R.2
  • 116
    • 3142751251 scopus 로고    scopus 로고
    • Hyperglycemia promotes oxidative through inhibition of thioredoxin function by thioredoxin-interacting protein
    • Schulze PC, Yoshida J, Takahashi T, He Z, King GL, Lee RT. Hyperglycemia promotes oxidative through inhibition of thioredoxin function by thioredoxin-interacting protein. J Biol Chem 279: 30369-30374, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 30369-30374
    • Schulze, P.C.1    Yoshida, J.2    Takahashi, T.3    He, Z.4    King, G.L.5    Lee, R.T.6
  • 117
    • 0037056109 scopus 로고    scopus 로고
    • Overexpression of thioredoxin-1 in transgenic mice attenuates adriamycin-induced cardiotoxicity
    • Shioji K, Kishimoto C, Nakamura H, Masutani H, Yuan Z, Oka S, Yodoi J. Overexpression of thioredoxin-1 in transgenic mice attenuates adriamycin-induced cardiotoxicity. Circulation 106: 1403-1409, 2002.
    • (2002) Circulation , vol.106 , pp. 1403-1409
    • Shioji, K.1    Kishimoto, C.2    Nakamura, H.3    Masutani, H.4    Yuan, Z.5    Oka, S.6    Yodoi, J.7
  • 121
    • 0031000775 scopus 로고    scopus 로고
    • pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • Srinivasan U, Mieyal PA, Mieyal JJ. pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry 36: 3199-3206, 1997.
    • (1997) Biochemistry , vol.36 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 126
    • 0037490142 scopus 로고    scopus 로고
    • Reversible glutathionylation of complex I increases mitochondrial superoxide formation
    • Taylor ER, Hurrell F, Shannon RJ, Lin TK, Hirst J, Murphy MP. Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J Biol Chem 278: 19603-19611, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 19603-19611
    • Taylor, E.R.1    Hurrell, F.2    Shannon, R.J.3    Lin, T.K.4    Hirst, J.5    Murphy, M.P.6
  • 127
    • 0031833126 scopus 로고    scopus 로고
    • Laminar shear stress: Mechanisms by which endothelial cells transduce an atheroprotective force
    • Traub O, Berk BC. Laminar shear stress: mechanisms by which endothelial cells transduce an atheroprotective force. Arterioscler Thromb Vasc Biol 18: 677-685, 1998.
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 677-685
    • Traub, O.1    Berk, B.C.2
  • 128
    • 33750915424 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress DNA damage and heart failure
    • Tsutsui H, Ide T, Kinugawa S. Mitochondrial oxidative stress DNA damage and heart failure. Antioxid Redox Signal 8: 1737-1744, 2006.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1737-1744
    • Tsutsui, H.1    Ide, T.2    Kinugawa, S.3
  • 129
    • 0038279860 scopus 로고    scopus 로고
    • Thioredoxin redox signaling in the ischemic heart: An insight with transgenic mice overexpressing Trx1
    • Turoczi T, Chang VW, Engelman RM, Maulik N, Ho YS, Das DK. Thioredoxin redox signaling in the ischemic heart: an insight with transgenic mice overexpressing Trx1. J Mol Cell Cardiol 35: 695-704, 2003.
    • (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
  • 131
    • 23044505674 scopus 로고    scopus 로고
    • Molecular and functional characterization of a human frataxin mutation found in hypertrophiy cardiomyopathy
    • Van Driest SL, Gakh O, Ommen SR, Isaya G, Ackerman MJ. Molecular and functional characterization of a human frataxin mutation found in hypertrophiy cardiomyopathy. Mol Genet Metab 85: 280-285, 2005.
    • (2005) Mol Genet Metab , vol.85 , pp. 280-285
    • Van Driest, S.L.1    Gakh, O.2    Ommen, S.R.3    Isaya, G.4    Ackerman, M.J.5
  • 132
    • 0027946340 scopus 로고
    • Concentration of copper zinc chromium iron and nickel in the abdominal aorta of patients deceased with coronary heart diseas
    • Vlad M, Caseanu E, Uza G, Petrescu M. Concentration of copper zinc chromium iron and nickel in the abdominal aorta of patients deceased with coronary heart diseas. J Trace Elem Electrolytes Health Dis 8: 111-114, 1994.
    • (1994) J Trace Elem Electrolytes Health Dis , vol.8 , pp. 111-114
    • Vlad, M.1    Caseanu, E.2    Uza, G.3    Petrescu, M.4
  • 133
    • 13944266092 scopus 로고    scopus 로고
    • Elevated thioredoxin after angioplasty in peripheral arterial disease
    • Wahlgren CM, Pekkari K. Elevated thioredoxin after angioplasty in peripheral arterial disease. Eur J Vasc Endovasc Surg 29: 281-286, 2005.
    • (2005) Eur J Vasc Endovasc Surg , vol.29 , pp. 281-286
    • Wahlgren, C.M.1    Pekkari, K.2
  • 135
    • 0037135621 scopus 로고    scopus 로고
    • 3-up- regulated protein-1 is a stress-responsive gene that regulates cardiomyocyte viability through interaction with thioredoxin
    • 3-up- regulated protein-1 is a stress-responsive gene that regulates cardiomyocyte viability through interaction with thioredoxin. J Biol Chem 277: 26496-26500, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 26496-26500
    • Wang, Y.1    De Keulanaer, G.W.2    Lee, R.T.3
  • 136
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells WW, Xu DP, Yang YF, Rocque PA. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J Biol Chem 265: 15361-15364, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.F.3    Rocque, P.A.4
  • 137
    • 0036735392 scopus 로고    scopus 로고
    • The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1alpha protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis
    • Welsh SJ, Bellamy WT, Briehl MM, Powis G. The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1alpha protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis. Cancer Res 62: 5089-5095, 2002.
    • (2002) Cancer Res , vol.62 , pp. 5089-5095
    • Welsh, S.J.1    Bellamy, W.T.2    Briehl, M.M.3    Powis, G.4
  • 139
    • 0034695550 scopus 로고    scopus 로고
    • Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT a novel protein kinase C-interacting protein with a thioredoxin homology domain
    • Witte S, Villalba M, Bi K, Liu Y, Isakov N, Altman A. Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT a novel protein kinase C-interacting protein with a thioredoxin homology domain. J Biol Chem 275: 1902-1909, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 1902-1909
    • Witte, S.1    Villalba, M.2    Bi, K.3    Liu, Y.4    Isakov, N.5    Altman, A.6
  • 140
    • 0034970775 scopus 로고    scopus 로고
    • MEK1/2-ERK1/2 mediates alpha1-adrenergic-stimulated hypertrophy in adult rat ventricular myocytes
    • Xiao L, Pimental DR, Amin JK, Sawyer DB, Colucci WS. MEK1/2-ERK1/2 mediates alpha1-adrenergic-stimulated hypertrophy in adult rat ventricular myocytes. J Mol Cell Cardiol 33: 779-787, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 779-787
    • Xiao, L.1    Pimental, D.R.2    Amin, J.K.3    Sawyer, D.B.4    Colucci, W.S.5
  • 144
    • 0344875019 scopus 로고    scopus 로고
    • Thioredoxin: A key regulator of cardiovascular homeostasis
    • Yamawaki H, Haendeler J, Berk BC. Thioredoxin: a key regulator of cardiovascular homeostasis. Circ Res 93: 1029-1033, 2003.
    • (2003) Circ Res , vol.93 , pp. 1029-1033
    • Yamawaki, H.1    Haendeler, J.2    Berk, B.C.3
  • 145
    • 0141506872 scopus 로고    scopus 로고
    • Chronic physiological shear stress inhibits tumor necrosis factor-induced proinflammatory responses in rabbit aorta perfused ex vivo
    • Yamawaki H, Lehoux S, Berk BC. Chronic physiological shear stress inhibits tumor necrosis factor-induced proinflammatory responses in rabbit aorta perfused ex vivo. Circulation 108: 1619-1625, 2003.
    • (2003) Circulation , vol.108 , pp. 1619-1625
    • Yamawaki, H.1    Lehoux, S.2    Berk, B.C.3
  • 146
    • 14644401702 scopus 로고    scopus 로고
    • Fluid shear stress inhibits vascular inflammation by decreasing thioredoxin-interacting protein in endothelial cell
    • Yamawaki H, Pan S, Lee RT, Berk BC. Fluid shear stress inhibits vascular inflammation by decreasing thioredoxin-interacting protein in endothelial cell. J Clin Invest 115: 733-738, 2005.
    • (2005) J Clin Invest , vol.115 , pp. 733-738
    • Yamawaki, H.1    Pan, S.2    Lee, R.T.3    Berk, B.C.4
  • 147
    • 0032497928 scopus 로고    scopus 로고
    • Reactivity of the human thioltransferase (glutaredoxin) C7S C25S C78S C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity
    • Yang Y, Jao S, Nanduri S, Starke DW, Mieyal JJ, Qin J. Reactivity of the human thioltransferase (glutaredoxin) C7S C25S C78S C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Biochemistry 37: 17145-17156, 1998.
    • (1998) Biochemistry , vol.37 , pp. 17145-17156
    • Yang, Y.1    Jao, S.2    Nanduri, S.3    Starke, D.W.4    Mieyal, J.J.5    Qin, J.6
  • 149
    • 0028037601 scopus 로고
    • Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins
    • Yoshitake S, Nanri H, Fernando MR, Minakami S. Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J Biochem 116: 42-46, 1994.
    • (1994) J Biochem , vol.116 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minakami, S.4
  • 150
    • 20444452107 scopus 로고    scopus 로고
    • Ferritin in atherosclerosis
    • You SA, Wang Q. Ferritin in atherosclerosis. Clin Chim Acta 357: 1-16, 2005.
    • (2005) Clin Chim Acta , vol.357 , pp. 1-16
    • You, S.A.1    Wang, Q.2
  • 151
    • 0029941609 scopus 로고    scopus 로고
    • Iron in human atheroma and LDL oxidation by macrophages following erythrophagocytosis
    • Yuan XM, Anders WL, Olsson AG, Brunk UT. Iron in human atheroma and LDL oxidation by macrophages following erythrophagocytosis. Atherosclerosis 124: 61-73, 1996.
    • (1996) Atherosclerosis , vol.124 , pp. 61-73
    • Yuan, X.M.1    Anders, W.L.2    Olsson, A.G.3    Brunk, U.T.4
  • 152
    • 0033597924 scopus 로고    scopus 로고
    • Mass spectrometry analysis of nitric oxide-modified caspase-3
    • Zech B, Wilm M, van Eldik R, Bruhne B. Mass spectrometry analysis of nitric oxide-modified caspase-3. J Biol Chem 274: 20931-20936, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 20931-20936
    • Zech, B.1    Wilm, M.2    van Eldik, R.3    Bruhne, B.4
  • 153
    • 2942696470 scopus 로고    scopus 로고
    • Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner
    • Zhang R, Al-Lamki R, Bai L, Streb JW, Miano JM, Bradley J, Min W. Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner. Circ Res 94: 1483-1491, 2004.
    • (2004) Circ Res , vol.94 , pp. 1483-1491
    • Zhang, R.1    Al-Lamki, R.2    Bai, L.3    Streb, J.W.4    Miano, J.M.5    Bradley, J.6    Min, W.7
  • 154
    • 0034705133 scopus 로고    scopus 로고
    • Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenylsulfide formed from the conserved cysteine-selenocysteine sequence
    • Zhong L, Arnér ESJ, Holmgren A. Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proc Natl Acad Sci USA 97: 5854-5859, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5854-5859
    • Zhong, L.1    Arnér, E.S.J.2    Holmgren, A.3
  • 155
    • 0035084272 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in postischemic myocardium
    • Zweier JL, Fertmann J, Wei G. Nitric oxide and peroxynitrite in postischemic myocardium. Antioxid Redox Signal 3: 11-12, 2001.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 11-12
    • Zweier, J.L.1    Fertmann, J.2    Wei, G.3
  • 156
    • 0000098037 scopus 로고
    • Direct measurement of free radical generation following reperfusion of ischemic myocardium
    • Zweier JL, Flaherty JT, Weisfeld ML. Direct measurement of free radical generation following reperfusion of ischemic myocardium. Proc Natl Acad Sci USA 84: 1404-1407, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1404-1407
    • Zweier, J.L.1    Flaherty, J.T.2    Weisfeld, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.