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Volumn 1792, Issue 3, 2009, Pages 190-200

Lipid induced overexpression of NF-κB in skeletal muscle cells is linked to insulin resistance

Author keywords

Free fatty acid; Insulin resistance; Insulin signaling; NF B; PKCe open

Indexed keywords

CALPHOSTIN C; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIPID; PALMITIC ACID; PROTEIN KINASE C EPSILON; SMALL INTERFERING RNA; SN 50; TRANSCRIPTION FACTOR RELA;

EID: 61549096874     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2008.11.014     Document Type: Article
Times cited : (48)

References (59)
  • 1
    • 0035979775 scopus 로고    scopus 로고
    • Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of IKKβ
    • Yuan M., Konstantopoulos N., and Lee J. Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of IKKβ. Science 293 (2001) 1673-1677
    • (2001) Science , vol.293 , pp. 1673-1677
    • Yuan, M.1    Konstantopoulos, N.2    Lee, J.3
  • 2
    • 0035411587 scopus 로고    scopus 로고
    • Role of the NF-κB pathway in the pathogenesis of human disease states
    • Yamamoto Y., and Gaynor R.B. Role of the NF-κB pathway in the pathogenesis of human disease states. Curr. Mol. Med. 1 (2001) 287-296
    • (2001) Curr. Mol. Med. , vol.1 , pp. 287-296
    • Yamamoto, Y.1    Gaynor, R.B.2
  • 4
    • 0027218865 scopus 로고
    • Interaction between glucose and free fatty acid metabolism in human skeletal muscle
    • Kelley D.E., Mokan M., Simoneau J.A., and Mandarino L.J. Interaction between glucose and free fatty acid metabolism in human skeletal muscle. J. Clin. Invest. 92 (1993) 91-98
    • (1993) J. Clin. Invest. , vol.92 , pp. 91-98
    • Kelley, D.E.1    Mokan, M.2    Simoneau, J.A.3    Mandarino, L.J.4
  • 5
    • 0028342686 scopus 로고
    • Mechanisms of fatty acid-induced inhibition of glucose uptake
    • Boden G., Chen X., Ruiz J., White J.V., and Rossetti L. Mechanisms of fatty acid-induced inhibition of glucose uptake. J. Clin. Invest. 93 (1994) 2438-2446
    • (1994) J. Clin. Invest. , vol.93 , pp. 2438-2446
    • Boden, G.1    Chen, X.2    Ruiz, J.3    White, J.V.4    Rossetti, L.5
  • 6
    • 0033927667 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance
    • Shulman G.I. Cellular mechanisms of insulin resistance. J. Clin. Invest. 106 (2000) 171-176
    • (2000) J. Clin. Invest. , vol.106 , pp. 171-176
    • Shulman, G.I.1
  • 7
    • 0034611791 scopus 로고    scopus 로고
    • Obesity as a medical problem
    • Kopelman P.G. Obesity as a medical problem. Nature 404 (2000) 635-643
    • (2000) Nature , vol.404 , pp. 635-643
    • Kopelman, P.G.1
  • 11
    • 0035405847 scopus 로고    scopus 로고
    • Effect of acute changes of plasma free fatty acids on intramyocellular fat content and insulin resistance in healthy subjects
    • Boden G., Lebed B., Schatz M., Homko C., and Lemieux S. Effect of acute changes of plasma free fatty acids on intramyocellular fat content and insulin resistance in healthy subjects. Diabetes 50 (2001) 1612-1617
    • (2001) Diabetes , vol.50 , pp. 1612-1617
    • Boden, G.1    Lebed, B.2    Schatz, M.3    Homko, C.4    Lemieux, S.5
  • 12
    • 0031753812 scopus 로고    scopus 로고
    • Five-hour fatty acid elevation increases muscle lipids and impairs glycogen synthesis in the rat
    • Chalkley S.M., Hettiarachchi M., Chisholm D.J., and Kraegen E.W. Five-hour fatty acid elevation increases muscle lipids and impairs glycogen synthesis in the rat. Metabolism 47 (1998) 1121-1126
    • (1998) Metabolism , vol.47 , pp. 1121-1126
    • Chalkley, S.M.1    Hettiarachchi, M.2    Chisholm, D.J.3    Kraegen, E.W.4
  • 13
    • 0345086474 scopus 로고    scopus 로고
    • Free fatty acid-induced insulin resistance is associated with activation of protein kinase C theta and alterations in the insulin signaling cascade
    • Griffin M.E., Marcucci M.J., Cline G.W., Bell K., Barucci N., Lee D., Goodyear L.J., Kraegen E.W., White M.F., and Shulman G.I. Free fatty acid-induced insulin resistance is associated with activation of protein kinase C theta and alterations in the insulin signaling cascade. Diabetes 48 (1999) 1270-1274
    • (1999) Diabetes , vol.48 , pp. 1270-1274
    • Griffin, M.E.1    Marcucci, M.J.2    Cline, G.W.3    Bell, K.4    Barucci, N.5    Lee, D.6    Goodyear, L.J.7    Kraegen, E.W.8    White, M.F.9    Shulman, G.I.10
  • 14
    • 0036300538 scopus 로고    scopus 로고
    • Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IκBα
    • Itani S.I., Ruderman N.B., Schmieder F., and Boden G. Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IκBα. Diabetes 51 (2002) 2005-2011
    • (2002) Diabetes , vol.51 , pp. 2005-2011
    • Itani, S.I.1    Ruderman, N.B.2    Schmieder, F.3    Boden, G.4
  • 15
    • 0031014830 scopus 로고    scopus 로고
    • Role of fatty acids in the pathogenesis of insulin resistance and NIDDM
    • Boden G. Role of fatty acids in the pathogenesis of insulin resistance and NIDDM. Diabetes 46 (1997) 3-10
    • (1997) Diabetes , vol.46 , pp. 3-10
    • Boden, G.1
  • 16
    • 8844255630 scopus 로고    scopus 로고
    • Free fatty acids in obesity and type2 diabetes: defining their role in the development of insulin resistance and beta-cell dysfunction
    • Boden G., and Shulman G.I. Free fatty acids in obesity and type2 diabetes: defining their role in the development of insulin resistance and beta-cell dysfunction. Eur. J. Clin. Invest. 32 (2002) 14-23
    • (2002) Eur. J. Clin. Invest. , vol.32 , pp. 14-23
    • Boden, G.1    Shulman, G.I.2
  • 17
    • 0035857020 scopus 로고    scopus 로고
    • New drug targets for type 2 diabetes and the metabolic syndrome
    • Moller D.E. New drug targets for type 2 diabetes and the metabolic syndrome. Nature 414 (2002) 821-827
    • (2002) Nature , vol.414 , pp. 821-827
    • Moller, D.E.1
  • 18
    • 0032829745 scopus 로고    scopus 로고
    • Overnight lowering of free fatty acids with Acipimox improves insulin resistance and glucose tolerance in obese diabetic and nondiabetic subjects
    • Santomauro A.T., Boden G., Silva M.E., Rocha D.M., Santos R.F., Ursich M.J., Strassmann P.G., and Wajchenburg B.L. Overnight lowering of free fatty acids with Acipimox improves insulin resistance and glucose tolerance in obese diabetic and nondiabetic subjects. Diabetes 48 (1999) 1836-1841
    • (1999) Diabetes , vol.48 , pp. 1836-1841
    • Santomauro, A.T.1    Boden, G.2    Silva, M.E.3    Rocha, D.M.4    Santos, R.F.5    Ursich, M.J.6    Strassmann, P.G.7    Wajchenburg, B.L.8
  • 21
    • 4744344777 scopus 로고    scopus 로고
    • Fatty acid-induced insulin resistance in L6 myotubes is prevented by inhibition of activation and nuclear localization of Nuclear Factor κB
    • Sinha S., Perdomo G., Brown N.F., and O'Doherty R.M. Fatty acid-induced insulin resistance in L6 myotubes is prevented by inhibition of activation and nuclear localization of Nuclear Factor κB. J. Biol. Chem. 279 (2004) 41294-41301
    • (2004) J. Biol. Chem. , vol.279 , pp. 41294-41301
    • Sinha, S.1    Perdomo, G.2    Brown, N.F.3    O'Doherty, R.M.4
  • 22
    • 14644427890 scopus 로고    scopus 로고
    • Local and systemic insulin resistance resulting from hepatic activation of IKK-β and NF-κB
    • Cai D., Yuan M., Frantz D.F., Melendez P.A., Hansen L., Lee J., and Shoelson S.E. Local and systemic insulin resistance resulting from hepatic activation of IKK-β and NF-κB. Nat. Med. 11 (2005) 183-190
    • (2005) Nat. Med. , vol.11 , pp. 183-190
    • Cai, D.1    Yuan, M.2    Frantz, D.F.3    Melendez, P.A.4    Hansen, L.5    Lee, J.6    Shoelson, S.E.7
  • 23
    • 33751163999 scopus 로고    scopus 로고
    • The NF-κB pathway
    • Moynagh P.N. The NF-κB pathway. J. Cell Sci. 118 (2005) 4389-4392
    • (2005) J. Cell Sci. , vol.118 , pp. 4389-4392
    • Moynagh, P.N.1
  • 24
    • 24944473034 scopus 로고    scopus 로고
    • NF-κB controls the global proinflammatory response in endothelial cells: evidence for the regulation of a pro-atherogenic program
    • Kempe S., Kestler H., Lasar A., and Wirth T. NF-κB controls the global proinflammatory response in endothelial cells: evidence for the regulation of a pro-atherogenic program. Nucleic Acids Res. 33 (2005) 165308-165319
    • (2005) Nucleic Acids Res. , vol.33 , pp. 165308-165319
    • Kempe, S.1    Kestler, H.2    Lasar, A.3    Wirth, T.4
  • 25
    • 1842526076 scopus 로고    scopus 로고
    • Active repression of antiapoptotic gene expression by RelA(p65) NF-κB
    • Campbell J.K., Rocha S., and Perkins D.N. Active repression of antiapoptotic gene expression by RelA(p65) NF-κB. Mol. Cell 13 (2004) 853-865
    • (2004) Mol. Cell , vol.13 , pp. 853-865
    • Campbell, J.K.1    Rocha, S.2    Perkins, D.N.3
  • 26
    • 29044447292 scopus 로고    scopus 로고
    • Free fatty acids produce insulin resistance and activate the proinflammatory Nuclear Factor-κB pathway in rat liver
    • Boden G., She P., Mozzoli M., Cheung P., Gumireddy K., Reddy P., Xiang X., Luo Z., and Ruderman N. Free fatty acids produce insulin resistance and activate the proinflammatory Nuclear Factor-κB pathway in rat liver. Diabetes 54 (2005) 3458-3465
    • (2005) Diabetes , vol.54 , pp. 3458-3465
    • Boden, G.1    She, P.2    Mozzoli, M.3    Cheung, P.4    Gumireddy, K.5    Reddy, P.6    Xiang, X.7    Luo, Z.8    Ruderman, N.9
  • 27
    • 33644680390 scopus 로고    scopus 로고
    • Conjugated linoleic acid promotes human adipocyte insulin resistance through NFκB-dependent cytokine production
    • Chung S., Brown J.M., Provo J.N., Hopkins R., and Mclntosh M.K. Conjugated linoleic acid promotes human adipocyte insulin resistance through NFκB-dependent cytokine production. J. Biol. Chem. 280 (2005) 38445-38456
    • (2005) J. Biol. Chem. , vol.280 , pp. 38445-38456
    • Chung, S.1    Brown, J.M.2    Provo, J.N.3    Hopkins, R.4    Mclntosh, M.K.5
  • 28
    • 22144498471 scopus 로고    scopus 로고
    • Palmitate-induced interleukin 6 production is mediated by protein kinase C and Nuclear-factor κB activation and leads to Glucose transporter 4 down-regulation in skeletal muscle cells
    • Jove M., Planavila A., Laguna J.C., and Vazquez-Carrera M. Palmitate-induced interleukin 6 production is mediated by protein kinase C and Nuclear-factor κB activation and leads to Glucose transporter 4 down-regulation in skeletal muscle cells. Endocrinology 146 (2005) 3087-3095
    • (2005) Endocrinology , vol.146 , pp. 3087-3095
    • Jove, M.1    Planavila, A.2    Laguna, J.C.3    Vazquez-Carrera, M.4
  • 32
    • 27844520859 scopus 로고    scopus 로고
    • Inhibition of insulin receptor gene expression and insulin signaling by fatty acid: interplay of PKC isoforms therein
    • Dey D., Mukherjee M., Basu D., Datta M., Roy S.S., Bandyopadhyay A., and Bhattacharya S. Inhibition of insulin receptor gene expression and insulin signaling by fatty acid: interplay of PKC isoforms therein. Cell Physiol. Biochem. 16 (2005) 217-228
    • (2005) Cell Physiol. Biochem. , vol.16 , pp. 217-228
    • Dey, D.1    Mukherjee, M.2    Basu, D.3    Datta, M.4    Roy, S.S.5    Bandyopadhyay, A.6    Bhattacharya, S.7
  • 33
    • 34247382539 scopus 로고    scopus 로고
    • Fatty acid represses insulin receptor gene expression by impairing HMGA1 through protein kinase Ce{open}
    • Dey D., Bhattacharya A., Roy S.S., and Bhattacharya S. Fatty acid represses insulin receptor gene expression by impairing HMGA1 through protein kinase Ce{open}. Biochem. Biophys. Res. Commun. 357 (2007) 474-479
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 474-479
    • Dey, D.1    Bhattacharya, A.2    Roy, S.S.3    Bhattacharya, S.4
  • 36
    • 0037238183 scopus 로고    scopus 로고
    • Purification of two types of gonadotropin receptors from carp ovarian follicles: overlapping recognition by two different ligands
    • Basu D., and Bhattacharya S. Purification of two types of gonadotropin receptors from carp ovarian follicles: overlapping recognition by two different ligands. Gen. Comp. Endo. 129 (2002) 152-162
    • (2002) Gen. Comp. Endo. , vol.129 , pp. 152-162
    • Basu, D.1    Bhattacharya, S.2
  • 37
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase D in a soluble extract from isolated mammalian nuclei
    • Dignam J.D., Lebovitz R.M., and Roeder R.G. Accurate transcription initiation by RNA polymerase D in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11 (1983) 1475-1489
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 38
    • 0345873536 scopus 로고    scopus 로고
    • Delivery of bioactive, gel-isolated proteins into live cells
    • Taylor J.E., and Patron C.F. Delivery of bioactive, gel-isolated proteins into live cells. Electrophoresis 24 (2003) 1331-1337
    • (2003) Electrophoresis , vol.24 , pp. 1331-1337
    • Taylor, J.E.1    Patron, C.F.2
  • 40
    • 21744448372 scopus 로고    scopus 로고
    • n3 PUFA's modulate T-cell activation via protein kinase C-α and -e{open} and NF-κB signaling pathway
    • Denys A., Hicham A., and Khan N.A. n3 PUFA's modulate T-cell activation via protein kinase C-α and -e{open} and NF-κB signaling pathway. J. Lipid Res. 46 (2005) 752-758
    • (2005) J. Lipid Res. , vol.46 , pp. 752-758
    • Denys, A.1    Hicham, A.2    Khan, N.A.3
  • 41
    • 0033588253 scopus 로고    scopus 로고
    • Ceramide generation is sufficient to account for the inhibition of the insulin-stimulated PKB pathway in C2C12 skeletal muscle cells pretreated with palmitate
    • Schmitz-Peiffer C., Craig D.L., and Biden T.J. Ceramide generation is sufficient to account for the inhibition of the insulin-stimulated PKB pathway in C2C12 skeletal muscle cells pretreated with palmitate. J. Biol. Chem. 274 (1999) 24202-24210
    • (1999) J. Biol. Chem. , vol.274 , pp. 24202-24210
    • Schmitz-Peiffer, C.1    Craig, D.L.2    Biden, T.J.3
  • 42
    • 33748755008 scopus 로고    scopus 로고
    • Toll-like receptor-2 is essential for the development of palmitate-induced insulin resistance in myotubes
    • Senn J.J. Toll-like receptor-2 is essential for the development of palmitate-induced insulin resistance in myotubes. J. Biol. Chem. 281 (2006) 26865-26875
    • (2006) J. Biol. Chem. , vol.281 , pp. 26865-26875
    • Senn, J.J.1
  • 43
    • 0038532298 scopus 로고    scopus 로고
    • A role for ceramide, but not diacylglycerol, in the antagonism of insulin signal transduction by saturated fatty acids
    • Chavez J.A., Knotts T.A., Wang L.P., Li G., Dobrowsky R.T., Florant G.L., and Summers S.A. A role for ceramide, but not diacylglycerol, in the antagonism of insulin signal transduction by saturated fatty acids. J. Biol. Chem. 278 (2003) 10297-10303
    • (2003) J. Biol. Chem. , vol.278 , pp. 10297-10303
    • Chavez, J.A.1    Knotts, T.A.2    Wang, L.P.3    Li, G.4    Dobrowsky, R.T.5    Florant, G.L.6    Summers, S.A.7
  • 45
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh S., and Karin M. Missing pieces in the NF-κB puzzle. Cell 109 (2002) 81-96
    • (2002) Cell , vol.109 , pp. 81-96
    • Ghosh, S.1    Karin, M.2
  • 47
    • 0030991201 scopus 로고    scopus 로고
    • The transcriptional activity of NF-Kappa B p65 is regulated by the I-Kappa B associated PKA C subunit through a cyclic-AMP independent mechanism
    • Zhong H., SuYang H., Erdjument-Bromage H., Tempst P., and Ghosh S. The transcriptional activity of NF-Kappa B p65 is regulated by the I-Kappa B associated PKA C subunit through a cyclic-AMP independent mechanism. Cell 89 (1997) 413-424
    • (1997) Cell , vol.89 , pp. 413-424
    • Zhong, H.1    SuYang, H.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 48
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-Kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the co-activator CBP/P300
    • Zhong H., Voll R..E., and Ghosh S. Phosphorylation of NF-Kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the co-activator CBP/P300. Mol. Cell. 1 (1998) 661-671
    • (1998) Mol. Cell. , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R..E.2    Ghosh, S.3
  • 49
    • 2442572230 scopus 로고    scopus 로고
    • Identification of a p65 peptide that selectively inhibits NF-κB activation induced by various inflammatory stimuli and its role in downregulation of NF-κB-mediated gene expression and up-regulation of apoptosis
    • Takada Y., Singh S., and Aggarwal B.B. Identification of a p65 peptide that selectively inhibits NF-κB activation induced by various inflammatory stimuli and its role in downregulation of NF-κB-mediated gene expression and up-regulation of apoptosis. J. Biol. Chem. 279 (2004) 15096-15104
    • (2004) J. Biol. Chem. , vol.279 , pp. 15096-15104
    • Takada, Y.1    Singh, S.2    Aggarwal, B.B.3
  • 50
    • 0031437893 scopus 로고    scopus 로고
    • Activation of nuclear transcription factor NF-κB by interleukin-1 is accompanied by casein kinase II-mediated phosphorylation of p65 subunit
    • Bird T.A., Schooley K., Dower S.K., Hagen H., and Virca G.D. Activation of nuclear transcription factor NF-κB by interleukin-1 is accompanied by casein kinase II-mediated phosphorylation of p65 subunit. J. Biol. Chem. 272 (1997) 32606-32612
    • (1997) J. Biol. Chem. , vol.272 , pp. 32606-32612
    • Bird, T.A.1    Schooley, K.2    Dower, S.K.3    Hagen, H.4    Virca, G.D.5
  • 51
    • 0034693133 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II
    • Wang D., Westerheide S.D., Hanson J.L., and Baldwin Jr. A.S. Tumor necrosis factor alpha induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II. J. Biol. Chem. 275 (2000) 32592-32597
    • (2000) J. Biol. Chem. , vol.275 , pp. 32592-32597
    • Wang, D.1    Westerheide, S.D.2    Hanson, J.L.3    Baldwin Jr., A.S.4
  • 52
    • 0032491485 scopus 로고    scopus 로고
    • Tumor necrosis factor-dependent activation of a RelA homodimer in astrocytes
    • Wang D., and Baldwin Jr. A.S. Tumor necrosis factor-dependent activation of a RelA homodimer in astrocytes. J. Biol. Chem. 273 (1998) 29411-29416
    • (1998) J. Biol. Chem. , vol.273 , pp. 29411-29416
    • Wang, D.1    Baldwin Jr., A.S.2
  • 54
    • 0028911139 scopus 로고
    • Analysis of the role of protein kinase C-α, -e{open} and -ζ in T cell activation
    • Genot E.M., Parker P.J., and Cantrell D.A. Analysis of the role of protein kinase C-α, -e{open} and -ζ in T cell activation. J. Biol. Chem. 270 (1995) 9833-9839
    • (1995) J. Biol. Chem. , vol.270 , pp. 9833-9839
    • Genot, E.M.1    Parker, P.J.2    Cantrell, D.A.3
  • 57
    • 20444494359 scopus 로고    scopus 로고
    • A novel protein kinase C (PKCe{open}) is required for fMet-Leu-Phe-induced activation of NF-κB in human peripheral blood monocytes
    • Chen L.-Yu., Doerner A., Lehmann P.F., Huang S., Zhong G., and Pan Z.K. A novel protein kinase C (PKCe{open}) is required for fMet-Leu-Phe-induced activation of NF-κB in human peripheral blood monocytes. J. Biol. Chem. 280 (2005) 22497-22501
    • (2005) J. Biol. Chem. , vol.280 , pp. 22497-22501
    • Chen, L.-Yu.1    Doerner, A.2    Lehmann, P.F.3    Huang, S.4    Zhong, G.5    Pan, Z.K.6
  • 58
    • 0027462682 scopus 로고
    • Mutual regulation of the transcriptional activator NF-kappa B and its inhibitor I kappa B-alpha
    • Brown K., Park S., Kanno T., Franzoso G., and Siebenlist U. Mutual regulation of the transcriptional activator NF-kappa B and its inhibitor I kappa B-alpha. Proc. Nat. Aca. Sci. U. S. A. 90 (1993) 2532-2536
    • (1993) Proc. Nat. Aca. Sci. U. S. A. , vol.90 , pp. 2532-2536
    • Brown, K.1    Park, S.2    Kanno, T.3    Franzoso, G.4    Siebenlist, U.5
  • 59
    • 0011321375 scopus 로고    scopus 로고
    • Glutathione downregulates the phosphorylation of IkB: autoloop regulation of the NF-κB-mediated expression of NF-κB subunits by TNF-α in mouse muscular endothelial cells
    • Cho S., Urata Y., Iida T., Goto S., Yamaguchi M., Sumikawa K., and Kondo T. Glutathione downregulates the phosphorylation of IkB: autoloop regulation of the NF-κB-mediated expression of NF-κB subunits by TNF-α in mouse muscular endothelial cells. Biochem. Biophys. Res. Commun. 253 (1998) 104-108
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 104-108
    • Cho, S.1    Urata, Y.2    Iida, T.3    Goto, S.4    Yamaguchi, M.5    Sumikawa, K.6    Kondo, T.7


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