메뉴 건너뛰기




Volumn 52, Issue 38, 2013, Pages 6712-6723

Redox modulation of endothelial nitric oxide synthase by glutaredoxin-1 through reversible oxidative post-translational modification

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIAL NITRIC OXIDE SYNTHASE; ENDOTHELIAL NITRIC-OXIDE SYNTHASE (ENOS); GENE SILENCING; GLUTATHIONE DISULFIDE; POST-TRANSLATIONAL MODIFICATIONS; REDOX REGULATION; TANDEM MASS SPECTROMETRY; VASCULAR FUNCTIONS;

EID: 84884860926     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400404s     Document Type: Article
Times cited : (55)

References (48)
  • 1
    • 0021063422 scopus 로고
    • Endothelium-dependent relaxation in rat aorta may be mediated through cyclic GMP-dependent protein phosphorylation
    • Rapoport, R. M., Draznin, M. B., and Murad, F. (1983) Endothelium-dependent relaxation in rat aorta may be mediated through cyclic GMP-dependent protein phosphorylation Nature 306, 174-176
    • (1983) Nature , vol.306 , pp. 174-176
    • Rapoport, R.M.1    Draznin, M.B.2    Murad, F.3
  • 2
    • 0023912670 scopus 로고
    • Vascular endothelial cells synthesize nitric oxide from l -arginine
    • Palmer, R. M., Ashton, D. S., and Moncada, S. (1988) Vascular endothelial cells synthesize nitric oxide from l -arginine Nature 333, 664-666
    • (1988) Nature , vol.333 , pp. 664-666
    • Palmer, R.M.1    Ashton, D.S.2    Moncada, S.3
  • 3
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt, D. S., Hwang, P. M., Glatt, C. E., Lowenstein, C., Reed, R. R., and Snyder, S. H. (1991) Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase Nature 351, 714-718
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 5
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., and Freeman, B. A. (1990) Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide Proc. Natl. Acad. Sci. U.S.A. 87, 1620-1624
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 6
    • 0036089571 scopus 로고    scopus 로고
    • Reactive oxygen species, mitochondria, and NAD(P)H oxidases in the development and progression of heart failure
    • Sorescu, D. and Griendling, K. K. (2002) Reactive oxygen species, mitochondria, and NAD(P)H oxidases in the development and progression of heart failure Congestive Heart Failure 8, 132-140
    • (2002) Congestive Heart Failure , vol.8 , pp. 132-140
    • Sorescu, D.1    Griendling, K.K.2
  • 7
    • 0030096995 scopus 로고    scopus 로고
    • Reactive oxygen species and vascular signal transduction mechanisms
    • Wolin, M. S. (1996) Reactive oxygen species and vascular signal transduction mechanisms Microcirculation 3, 1-17
    • (1996) Microcirculation , vol.3 , pp. 1-17
    • Wolin, M.S.1
  • 8
    • 0031577442 scopus 로고    scopus 로고
    • Tetrahydrobiopterin regulates superoxide and nitric oxide generation by recombinant endothelial nitric oxide synthase
    • Wever, R. M., van Dam, T., van Rijn, H. J., de Groot, F., and Rabelink, T. J. (1997) Tetrahydrobiopterin regulates superoxide and nitric oxide generation by recombinant endothelial nitric oxide synthase Biochem. Biophys. Res. Commun. 237, 340-344
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 340-344
    • Wever, R.M.1    Van Dam, T.2    Van Rijn, H.J.3    De Groot, F.4    Rabelink, T.J.5
  • 9
    • 0032475865 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent and tetrahydrobiopterin regulatory process
    • 2+/calmodulin- dependent and tetrahydrobiopterin regulatory process J. Biol. Chem. 273, 25804-25808
    • (1998) J. Biol. Chem. , vol.273 , pp. 25804-25808
    • Xia, Y.1    Tsai, A.L.2    Berka, V.3    Zweier, J.L.4
  • 11
    • 14844327786 scopus 로고    scopus 로고
    • Endogenous methylarginines modulate superoxide as well as nitric oxide generation from neuronal nitric-oxide synthase: Differences in the effects of monomethyl- and dimethylarginines in the presence and absence of tetrahydrobiopterin
    • Cardounel, A. J., Xia, Y., and Zweier, J. L. (2005) Endogenous methylarginines modulate superoxide as well as nitric oxide generation from neuronal nitric-oxide synthase: Differences in the effects of monomethyl- and dimethylarginines in the presence and absence of tetrahydrobiopterin J. Biol. Chem. 280, 7540-7549
    • (2005) J. Biol. Chem. , vol.280 , pp. 7540-7549
    • Cardounel, A.J.1    Xia, Y.2    Zweier, J.L.3
  • 13
    • 0030711684 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of endothelial cell dysfunction
    • Harrison, D. G. (1997) Cellular and molecular mechanisms of endothelial cell dysfunction J. Clin. Invest. 100, 2153-2157
    • (1997) J. Clin. Invest. , vol.100 , pp. 2153-2157
    • Harrison, D.G.1
  • 15
    • 78649778002 scopus 로고    scopus 로고
    • Diazeniumdiolate mediated nitrosative stress alters nitric oxide homeostasis through intracellular calcium and S-glutathionylation of nitric oxide synthetase
    • Manevich, Y., Townsend, D. M., Hutchens, S., and Tew, K. D. (2010) Diazeniumdiolate mediated nitrosative stress alters nitric oxide homeostasis through intracellular calcium and S-glutathionylation of nitric oxide synthetase PLoS One 5, e14151
    • (2010) PLoS One , vol.5 , pp. 14151
    • Manevich, Y.1    Townsend, D.M.2    Hutchens, S.3    Tew, K.D.4
  • 16
    • 80052968360 scopus 로고    scopus 로고
    • Nitroglycerin-induced endothelial dysfunction and tolerance involve adverse phosphorylation and S-glutathionylation of endothelial nitric oxide synthase: Beneficial effects of therapy with the AT1 receptor blocker telmisartan
    • Knorr, M., Hausding, M., Kroller-Schuhmacher, S., Steven, S., Oelze, M., Heeren, T., Scholz, A., Gori, T., Wenzel, P., Schulz, E., Daiber, A., and Munzel, T. (2011) Nitroglycerin-induced endothelial dysfunction and tolerance involve adverse phosphorylation and S-glutathionylation of endothelial nitric oxide synthase: Beneficial effects of therapy with the AT1 receptor blocker telmisartan Arterioscler., Thromb., Vasc. Biol. 31, 2223-2231
    • (2011) Arterioscler., Thromb., Vasc. Biol. , vol.31 , pp. 2223-2231
    • Knorr, M.1    Hausding, M.2    Kroller-Schuhmacher, S.3    Steven, S.4    Oelze, M.5    Heeren, T.6    Scholz, A.7    Gori, T.8    Wenzel, P.9    Schulz, E.10    Daiber, A.11    Munzel, T.12
  • 18
    • 0035800858 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation
    • Okamoto, T., Akaike, T., Sawa, T., Miyamoto, Y., van der Vliet, A., and Maeda, H. (2001) Activation of matrix metalloproteinases by peroxynitrite- induced protein S-glutathiolation via disulfide S-oxide formation J. Biol. Chem. 276, 29596-29602
    • (2001) J. Biol. Chem. , vol.276 , pp. 29596-29602
    • Okamoto, T.1    Akaike, T.2    Sawa, T.3    Miyamoto, Y.4    Van Der Vliet, A.5    Maeda, H.6
  • 19
    • 2542486403 scopus 로고    scopus 로고
    • Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue
    • Reddy, S., Jones, A. D., Cross, C. E., Wong, P. S., and Van Der Vliet, A. (2000) Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue Biochem. J. 347 (Part 3) 821-827
    • (2000) Biochem. J. , vol.347 , Issue.PART 3 , pp. 821-827
    • Reddy, S.1    Jones, A.D.2    Cross, C.E.3    Wong, P.S.4    Van Der Vliet, A.5
  • 20
    • 31044455445 scopus 로고    scopus 로고
    • Redox modifications of protein-thiols: Emerging roles in cell signaling
    • Biswas, S., Chida, A. S., and Rahman, I. (2006) Redox modifications of protein-thiols: Emerging roles in cell signaling Biochem. Pharmacol. 71, 551-564
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 551-564
    • Biswas, S.1    Chida, A.S.2    Rahman, I.3
  • 21
    • 79954608953 scopus 로고    scopus 로고
    • S-glutathionylation reshapes our understanding of endothelial nitric oxide synthase uncoupling and nitric oxide/reactive oxygen species-mediated signaling
    • Zweier, J. L., Chen, C. A., and Druhan, L. J. (2011) S-glutathionylation reshapes our understanding of endothelial nitric oxide synthase uncoupling and nitric oxide/reactive oxygen species-mediated signaling Antioxid. Redox Signaling 14, 1769-1775
    • (2011) Antioxid. Redox Signaling , vol.14 , pp. 1769-1775
    • Zweier, J.L.1    Chen, C.A.2    Druhan, L.J.3
  • 22
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of protein function by glutathionylation
    • Ghezzi, P. (2005) Regulation of protein function by glutathionylation Free Radical Res. 39, 573-580
    • (2005) Free Radical Res. , vol.39 , pp. 573-580
    • Ghezzi, P.1
  • 23
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes, A. P. and Holmgren, A. (2004) Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system Antioxid. Redox Signaling 6, 63-74
    • (2004) Antioxid. Redox Signaling , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 24
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton, M. D., Chock, P. B., and Mieyal, J. J. (2005) Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation Antioxid. Redox Signaling 7, 348-366
    • (2005) Antioxid. Redox Signaling , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 25
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction
    • Starke, D. W., Chock, P. B., and Mieyal, J. J. (2003) Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction J. Biol. Chem. 278, 14607-14613
    • (2003) J. Biol. Chem. , vol.278 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 26
    • 34547128886 scopus 로고    scopus 로고
    • Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFκB
    • Qanungo, S., Starke, D. W., Pai, H. V., Mieyal, J. J., and Nieminen, A. L. (2007) Glutathione supplementation potentiates hypoxic apoptosis by S-glutathionylation of p65-NFκB J. Biol. Chem. 282, 18427-18436
    • (2007) J. Biol. Chem. , vol.282 , pp. 18427-18436
    • Qanungo, S.1    Starke, D.W.2    Pai, H.V.3    Mieyal, J.J.4    Nieminen, A.L.5
  • 27
    • 51349142890 scopus 로고    scopus 로고
    • Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: Implications for intracellular roles
    • Gallogly, M. M., Starke, D. W., Leonberg, A. K., Ospina, S. M., and Mieyal, J. J. (2008) Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: Implications for intracellular roles Biochemistry 47, 11144-11157
    • (2008) Biochemistry , vol.47 , pp. 11144-11157
    • Gallogly, M.M.1    Starke, D.W.2    Leonberg, A.K.3    Ospina, S.M.4    Mieyal, J.J.5
  • 28
    • 64549106959 scopus 로고    scopus 로고
    • Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation
    • Gallogly, M. M., Starke, D. W., and Mieyal, J. J. (2009) Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation Antioxid. Redox Signaling 11, 1059-1081
    • (2009) Antioxid. Redox Signaling , vol.11 , pp. 1059-1081
    • Gallogly, M.M.1    Starke, D.W.2    Mieyal, J.J.3
  • 29
    • 84856729192 scopus 로고    scopus 로고
    • Mitochondrial thiols in antioxidant protection and redox signaling: Distinct roles for glutathionylation and other thiol modifications
    • Murphy, M. P. (2012) Mitochondrial thiols in antioxidant protection and redox signaling: Distinct roles for glutathionylation and other thiol modifications Antioxid. Redox Signaling 16, 476-495
    • (2012) Antioxid. Redox Signaling , vol.16 , pp. 476-495
    • Murphy, M.P.1
  • 30
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • Gallogly, M. M. and Mieyal, J. J. (2007) Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress Curr. Opin. Pharmacol. 7, 381-391
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 31
    • 55249112287 scopus 로고    scopus 로고
    • Phosphorylation of endothelial nitric-oxide synthase regulates superoxide generation from the enzyme
    • Chen, C. A., Druhan, L. J., Varadharaj, S., Chen, Y. R., and Zweier, J. L. (2008) Phosphorylation of endothelial nitric-oxide synthase regulates superoxide generation from the enzyme J. Biol. Chem. 283, 27038-27047
    • (2008) J. Biol. Chem. , vol.283 , pp. 27038-27047
    • Chen, C.A.1    Druhan, L.J.2    Varadharaj, S.3    Chen, Y.R.4    Zweier, J.L.5
  • 32
    • 80051698652 scopus 로고    scopus 로고
    • Superoxide induces endothelial nitric-oxide synthase protein thiyl radical formation, a novel mechanism regulating eNOS function and coupling
    • Chen, C. A., Lin, C. H., Druhan, L. J., Wang, T. Y., Chen, Y. R., and Zweier, J. L. (2011) Superoxide induces endothelial nitric-oxide synthase protein thiyl radical formation, a novel mechanism regulating eNOS function and coupling J. Biol. Chem. 286, 29098-29107
    • (2011) J. Biol. Chem. , vol.286 , pp. 29098-29107
    • Chen, C.A.1    Lin, C.H.2    Druhan, L.J.3    Wang, T.Y.4    Chen, Y.R.5    Zweier, J.L.6
  • 33
    • 77950632502 scopus 로고    scopus 로고
    • Peroxynitrite induces destruction of the tetrahydrobiopterin and heme in endothelial nitric oxide synthase: Transition from reversible to irreversible enzyme inhibition
    • Chen, W., Druhan, L. J., Chen, C. A., Hemann, C., Chen, Y. R., Berka, V., Tsai, A. L., and Zweier, J. L. (2010) Peroxynitrite induces destruction of the tetrahydrobiopterin and heme in endothelial nitric oxide synthase: Transition from reversible to irreversible enzyme inhibition Biochemistry 49, 3129-3137
    • (2010) Biochemistry , vol.49 , pp. 3129-3137
    • Chen, W.1    Druhan, L.J.2    Chen, C.A.3    Hemann, C.4    Chen, Y.R.5    Berka, V.6    Tsai, A.L.7    Zweier, J.L.8
  • 34
    • 0025787205 scopus 로고
    • Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: An FAD- and FMN-containing flavoprotein
    • Stuehr, D. J., Cho, H. J., Kwon, N. S., Weise, M. F., and Nathan, C. F. (1991) Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: An FAD- and FMN-containing flavoprotein Proc. Natl. Acad. Sci. U.S.A. 88, 7773-7777
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 7773-7777
    • Stuehr, D.J.1    Cho, H.J.2    Kwon, N.S.3    Weise, M.F.4    Nathan, C.F.5
  • 35
    • 0028884647 scopus 로고
    • Cloning, expression and characterization of human thioltransferase (glutaredoxin) in E coli
    • Chrestensen, C. A., Eckman, C. B., Starke, D. W., and Mieyal, J. J. (1995) Cloning, expression and characterization of human thioltransferase (glutaredoxin) in E. coli FEBS Lett. 374, 25-28
    • (1995) FEBS Lett. , vol.374 , pp. 25-28
    • Chrestensen, C.A.1    Eckman, C.B.2    Starke, D.W.3    Mieyal, J.J.4
  • 36
    • 0034714319 scopus 로고    scopus 로고
    • Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis
    • Chrestensen, C. A., Starke, D. W., and Mieyal, J. J. (2000) Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis J. Biol. Chem. 275, 26556-26565
    • (2000) J. Biol. Chem. , vol.275 , pp. 26556-26565
    • Chrestensen, C.A.1    Starke, D.W.2    Mieyal, J.J.3
  • 37
    • 0346749513 scopus 로고    scopus 로고
    • Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt
    • Murata, H., Ihara, Y., Nakamura, H., Yodoi, J., Sumikawa, K., and Kondo, T. (2003) Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt J. Biol. Chem. 278, 50226-50233
    • (2003) J. Biol. Chem. , vol.278 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 39
    • 84875737737 scopus 로고    scopus 로고
    • Glutathione catalysis and the reaction mechanisms of glutathione- dependent enzymes
    • Deponte, M. (2013) Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes Biochim. Biophys. Acta 1830, 3217-3266
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3217-3266
    • Deponte, M.1
  • 40
    • 0031000775 scopus 로고    scopus 로고
    • PH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • Srinivasan, U., Mieyal, P. A., and Mieyal, J. J. (1997) pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis Biochemistry 36, 3199-3206
    • (1997) Biochemistry , vol.36 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 43
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense
    • Beer, S. M., Taylor, E. R., Brown, S. E., Dahm, C. C., Costa, N. J., Runswick, M. J., and Murphy, M. P. (2004) Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense J. Biol. Chem. 279, 47939-47951
    • (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
  • 44
    • 84875709337 scopus 로고    scopus 로고
    • The fairytale of the GSSG/GSH redox potential
    • Flohe, L. (2013) The fairytale of the GSSG/GSH redox potential Biochim. Biophys. Acta 1830, 3139-3142
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3139-3142
    • Flohe, L.1
  • 45
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer, F. Q. and Buettner, G. R. (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radical Biol. Med. 30, 1191-1212
    • (2001) Free Radical Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 46
    • 79961144636 scopus 로고    scopus 로고
    • Mechanism of glutathione depletion during simulated ischemia-reperfusion of H9c2 cardiac myocytes
    • Ko, Y. E., Lee, I. H., So, H. M., Kim, H. W., and Kim, Y. H. (2011) Mechanism of glutathione depletion during simulated ischemia-reperfusion of H9c2 cardiac myocytes Free Radical Res. 45, 1074-1082
    • (2011) Free Radical Res. , vol.45 , pp. 1074-1082
    • Ko, Y.E.1    Lee, I.H.2    So, H.M.3    Kim, H.W.4    Kim, Y.H.5
  • 47
    • 0000098037 scopus 로고
    • Direct measurement of free radical generation following reperfusion of ischemic myocardium
    • Zweier, J. L., Flaherty, J. T., and Weisfeldt, M. L. (1987) Direct measurement of free radical generation following reperfusion of ischemic myocardium Proc. Natl. Acad. Sci. U.S.A. 84, 1404-1407
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 1404-1407
    • Zweier, J.L.1    Flaherty, J.T.2    Weisfeldt, M.L.3
  • 48
    • 0034886331 scopus 로고    scopus 로고
    • Glutathione supplementation and training increases myocardial resistance to ischemia-reperfusion in vivo
    • Ramires, P. R. and Ji, L. L. (2001) Glutathione supplementation and training increases myocardial resistance to ischemia-reperfusion in vivo Am. J. Physiol. 281, H679-H688
    • (2001) Am. J. Physiol. , vol.281
    • Ramires, P.R.1    Ji, L.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.