메뉴 건너뛰기




Volumn 301, Issue 5, 2011, Pages

Glycogen synthase kinase-3β is required for the induction of skeletal muscle atrophy

Author keywords

E3 ubiquitin ligase; Glucocorticoids; Insulin like growth factor i; Myosin; Proteolysis

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; ATROGIN 1; CHIR 99021; DEXAMETHASONE; GLYCOGEN SYNTHASE KINASE 3BETA; LITHIUM CHLORIDE; MUSCLE PROTEIN; MUSCLE RING FINGER 1 PROTEIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; PROTEIN KINASE B; PROTEIN SERINE THREONINE KINASE INHIBITOR; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 80054907958     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00520.2010     Document Type: Article
Times cited : (70)

References (63)
  • 1
    • 33748299477 scopus 로고    scopus 로고
    • The paradoxical pro- and anti-apoptotic actions of GSK3 in the intrinsic and extrinsic apoptosis signaling pathways
    • Beurel E, Jope RS. The paradoxical pro- and anti-apoptotic actions of GSK3 in the intrinsic and extrinsic apoptosis signaling pathways. Prog Neurobiol 79: 173-189, 2006.
    • (2006) Prog Neurobiol , vol.79 , pp. 173-189
    • Beurel, E.1    Jope, R.S.2
  • 3
    • 0036726313 scopus 로고    scopus 로고
    • Stable suppression of tumorigenicity by virus-mediated RNA interference
    • Brummelkamp TR, Bernards R, Agami R. Stable suppression of tumorigenicity by virus-mediated RNA interference. Cancer Cell 2: 243-247, 2002.
    • (2002) Cancer Cell , vol.2 , pp. 243-247
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 4
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp TR, Bernards R, Agami R. A system for stable expression of short interfering RNAs in mammalian cells. Science 296: 550-553, 2002.
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 6
    • 56449116314 scopus 로고    scopus 로고
    • Contribution of natural inhibitors to the understanding of the PI3K/PDK1/PKB pathway in the insulin-mediated intracellular signaling cascade
    • Cho JY, Park J. Contribution of natural inhibitors to the understanding of the PI3K/PDK1/PKB pathway in the insulin-mediated intracellular signaling cascade. Int J Mol Sci 9: 2217-2230, 2008.
    • (2008) Int J Mol Sci , vol.9 , pp. 2217-2230
    • Cho, J.Y.1    Park, J.2
  • 7
    • 0026647437 scopus 로고
    • Glucocorticoid-induced skeletal muscle atrophy in vitro is attenuated by mechanical stimulation
    • Chromiak JA, Vandenburgh HH. Glucocorticoid-induced skeletal muscle atrophy in vitro is attenuated by mechanical stimulation. Am J Physiol Cell Physiol 262: C1471-C1477, 1992.
    • (1992) Am J Physiol Cell Physiol , vol.262
    • Chromiak, J.A.1    Vandenburgh, H.H.2
  • 10
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 351: 95-105, 2000.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 11
    • 80054963719 scopus 로고    scopus 로고
    • No muscle atrophy without GSK- 3β focus on Glycogen synthase kinase-3β is required for the induction of skeletal muscle atrophy
    • (August 10, 2011). doi:10.1152/ajpcell.00310.2011
    • Dupont-Versteegden EE, Waters C. No muscle atrophy without GSK- 3β focus on "Glycogen synthase kinase-3β is required for the induction of skeletal muscle atrophy." Am J Physiol Cell Physiol (August 10, 2011). doi:10.1152/ajpcell.00310.2011.
    • Am J Physiol Cell Physiol
    • Dupont-Versteegden, E.E.1    Waters, C.2
  • 12
    • 23944509740 scopus 로고    scopus 로고
    • GSK-3beta inhibitors reduce protein degradation in muscles from septic rats and in dexamethasone-treated myotubes
    • Evenson AR, Fareed MU, Menconi MJ, Mitchell JC, Hasselgren PO. GSK-3beta inhibitors reduce protein degradation in muscles from septic rats and in dexamethasone-treated myotubes. Int J Biochem Cell Biol 37: 2226-2238, 2005.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 2226-2238
    • Evenson, A.R.1    Fareed, M.U.2    Menconi, M.J.3    Mitchell, J.C.4    Hasselgren, P.O.5
  • 13
    • 22144453941 scopus 로고    scopus 로고
    • Protein breakdown in muscle from burned rats is blocked by insulin-like growth factor i and glycogen synthase kinase-3beta inhibitors
    • Fang CH, Li BG, James JH, King JK, Evenson AR, Warden GD, Hasselgren PO. Protein breakdown in muscle from burned rats is blocked by insulin-like growth factor i and glycogen synthase kinase-3beta inhibitors. Endocrinology 146: 3141-3149, 2005.
    • (2005) Endocrinology , vol.146 , pp. 3141-3149
    • Fang, C.H.1    Li, B.G.2    James, J.H.3    King, J.K.4    Evenson, A.R.5    Warden, G.D.6    Hasselgren, P.O.7
  • 14
    • 77951487050 scopus 로고    scopus 로고
    • Signaling pathways perturbing muscle mass
    • Glass DJ. Signaling pathways perturbing muscle mass. Curr Opin Clin Nutr Metab Care 13: 225-229, 2010.
    • (2010) Curr Opin Clin Nutr Metab Care , vol.13 , pp. 225-229
    • Glass, D.J.1
  • 15
    • 23944456384 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and atrophy signaling pathways
    • Glass DJ. Skeletal muscle hypertrophy and atrophy signaling pathways. Int J Biochem Cell Biol 37: 1974-1984, 2005.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 1974-1984
    • Glass, D.J.1
  • 16
    • 45949101825 scopus 로고    scopus 로고
    • Myofibrillar protein turnover: The proteasome and the calpains
    • Goll DE, Neti G, Mares SW, Thompson VF. Myofibrillar protein turnover: the proteasome and the calpains. J Anim Sci 86: E19-E35, 2008.
    • (2008) J Anim Sci , vol.86
    • Goll, D.E.1    Neti, G.2    Mares, S.W.3    Thompson, V.F.4
  • 18
    • 0035967897 scopus 로고    scopus 로고
    • Regulation of GSK-3: A cellular multiprocessor
    • Harwood AJ. Regulation of GSK-3: a cellular multiprocessor. Cell 105: 821-824, 2001.
    • (2001) Cell , vol.105 , pp. 821-824
    • Harwood, A.J.1
  • 20
    • 0035164533 scopus 로고    scopus 로고
    • Muscle cachexia: Current concepts of intracellular mechanisms and molecular regulation
    • Hasselgren PO, Fischer JE. Muscle cachexia: current concepts of intracellular mechanisms and molecular regulation. Ann Surg 233: 9-17, 2001.
    • (2001) Ann Surg , vol.233 , pp. 9-17
    • Hasselgren, P.O.1    Fischer, J.E.2
  • 21
    • 0028899142 scopus 로고
    • Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures
    • Hong DH, Forsberg NE. Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures. Mol Cell Endocrinol 108: 199-209, 1995.
    • (1995) Mol Cell Endocrinol , vol.108 , pp. 199-209
    • Hong, D.H.1    Forsberg, N.E.2
  • 22
    • 34247857681 scopus 로고    scopus 로고
    • A prospective study of decline in fat free mass and skeletal muscle strength in chronic obstructive pulmonary disease
    • Hopkinson NS, Tennant RC, Dayer MJ, Swallow EB, Hansel TT, Moxham J, Polkey MI. A prospective study of decline in fat free mass and skeletal muscle strength in chronic obstructive pulmonary disease. Respir Res 8: 25, 2007.
    • (2007) Respir Res , vol.8 , pp. 25
    • Hopkinson, N.S.1    Tennant, R.C.2    Dayer, M.J.3    Swallow, E.B.4    Hansel, T.T.5    Moxham, J.6    Polkey, M.I.7
  • 23
    • 70349658713 scopus 로고    scopus 로고
    • Endogenous glucocorticoids and impaired insulin signaling are both required to stimulate muscle wasting under pathophysiological conditions in mice
    • Hu Z, Wang H, Lee IH, Du J, Mitch WE. Endogenous glucocorticoids and impaired insulin signaling are both required to stimulate muscle wasting under pathophysiological conditions in mice. J Clin Invest 119: 3059-3069, 2009.
    • (2009) J Clin Invest , vol.119 , pp. 3059-3069
    • Hu, Z.1    Wang, H.2    Lee, I.H.3    Du, J.4    Mitch, W.E.5
  • 25
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitinproteasome pathway in muscle atrophy?
    • Jagoe RT, Goldberg AL. What do we really know about the ubiquitinproteasome pathway in muscle atrophy? Curr Opin Clin Nutr Metab Care 4: 183-190, 2001.
    • (2001) Curr Opin Clin Nutr Metab Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 26
    • 77951044429 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase inhibitor(LY294002) induces apoptosis of human nasopharyngeal carcinoma in vitro and in vivo
    • Jiang H, Fan D, Zhou G, Li X, Deng H. Phosphatidylinositol 3-kinase inhibitor(LY294002) induces apoptosis of human nasopharyngeal carcinoma in vitro and in vivo. J Exp Clin Cancer Res 29: 34, 2010.
    • (2010) J Exp Clin Cancer Res , vol.29 , pp. 34
    • Jiang, H.1    Fan, D.2    Zhou, G.3    Li, X.4    Deng, H.5
  • 27
    • 0042379932 scopus 로고    scopus 로고
    • Lithium and GSK-3: One inhibitor, two inhibitory actions, multiple outcomes
    • Jope RS. Lithium and GSK-3: one inhibitor, two inhibitory actions, multiple outcomes. Trends Pharmacol Sci 24: 441-443, 2003.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 441-443
    • Jope, R.S.1
  • 30
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres E, Amini AR, Amini AA, Griffiths J, Martin FJ, Wei Y, Lin HC, Yancopoulos GD, Glass DJ. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 280: 2737-2744, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6    Lin, H.C.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 31
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
    • Lecker SH, Solomon V, Mitch WE, Goldberg AL. Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J Nutr 129: 227S-237S, 1999.
    • (1999) J Nutr , vol.129
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 32
    • 23944504285 scopus 로고    scopus 로고
    • Insulin-like growth factor-I inhibits dexamethasone-induced proteolysis in cultured L6 myotubes through PI3K/Akt/GSK-3beta and PI3K/Akt/mTOR-dependent mechanisms
    • Li BG, Hasselgren PO, Fang CH. Insulin-like growth factor-I inhibits dexamethasone-induced proteolysis in cultured L6 myotubes through PI3K/Akt/GSK-3beta and PI3K/Akt/mTOR-dependent mechanisms. Int J Biochem Cell Biol 37: 2207-2216, 2005.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 2207-2216
    • Li, B.G.1    Hasselgren, P.O.2    Fang, C.H.3
  • 33
    • 0026006653 scopus 로고
    • Activation of the ubiquitin- ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy
    • Medina R, Wing SS, Haas A, Goldberg AL. Activation of the ubiquitin- ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy. Biomed Biochim Acta 50: 347-356, 1991.
    • (1991) Biomed Biochim Acta , vol.50 , pp. 347-356
    • Medina, R.1    Wing, S.S.2    Haas, A.3    Goldberg, A.L.4
  • 35
    • 54849413378 scopus 로고    scopus 로고
    • Dexamethasone and corticosterone induce similar, but not identical, muscle wasting responses in cultured L6 and C2C12 myotubes
    • Menconi M, Gonnella P, Petkova V, Lecker S, Hasselgren PO. Dexamethasone and corticosterone induce similar, but not identical, muscle wasting responses in cultured L6 and C2C12 myotubes. J Cell Biochem 105: 353-364, 2008.
    • (2008) J Cell Biochem , vol.105 , pp. 353-364
    • Menconi, M.1    Gonnella, P.2    Petkova, V.3    Lecker, S.4    Hasselgren, P.O.5
  • 36
    • 0027185342 scopus 로고
    • Time course of the response of myofibrillar and sarcoplasmic protein metabolism to unweighting of the soleus muscle
    • Munoz KA, Satarug S, Tischler ME. Time course of the response of myofibrillar and sarcoplasmic protein metabolism to unweighting of the soleus muscle. Metabolism 42: 1006-1012, 1993.
    • (1993) Metabolism , vol.42 , pp. 1006-1012
    • Munoz, K.A.1    Satarug, S.2    Tischler, M.E.3
  • 37
    • 19344372609 scopus 로고    scopus 로고
    • Response of the ubiquitin-proteasome pathway to changes in muscle activity
    • Reid MB. Response of the ubiquitin-proteasome pathway to changes in muscle activity. Am J Physiol Regul Integr Comp Physiol 288: R1423-R1431, 2005.
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.288
    • Reid, M.B.1
  • 38
    • 0033546439 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
    • Rena G, Guo S, Cichy SC, Unterman TG, Cohen P. Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J Biol Chem 274: 17179-17183, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 17179-17183
    • Rena, G.1    Guo, S.2    Cichy, S.C.3    Unterman, T.G.4    Cohen, P.5
  • 41
    • 0034805180 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 by competition for magnesium
    • Ryves WJ, Harwood AJ. Lithium inhibits glycogen synthase kinase-3 by competition for magnesium. Biochem Biophys Res Commun 280: 720-725, 2001.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 720-725
    • Ryves, W.J.1    Harwood, A.J.2
  • 42
    • 4544293878 scopus 로고    scopus 로고
    • IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
    • Sacheck JM, Ohtsuka A, McLary SC, Goldberg AL. IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. Am J Physiol Endocrinol Metab 287: E591-E601, 2004.
    • (2004) Am J Physiol Endocrinol Metab , vol.287
    • Sacheck, J.M.1    Ohtsuka, A.2    McLary, S.C.3    Goldberg, A.L.4
  • 45
    • 42449133390 scopus 로고    scopus 로고
    • Mechanisms of glucocorticoidinduced myopathy
    • Schakman O, Gilson H, Thissen JP. Mechanisms of glucocorticoidinduced myopathy. J Endocrinol 197: 1-10, 2008.
    • (2008) J Endocrinol , vol.197 , pp. 1-10
    • Schakman, O.1    Gilson, H.2    Thissen, J.P.3
  • 46
    • 0033679673 scopus 로고    scopus 로고
    • 4E-BP1 and S6K1: Translational integration sites for nutritional and hormonal information in muscle
    • Shah OJ, Anthony JC, Kimball SR, Jefferson LS. 4E-BP1 and S6K1: translational integration sites for nutritional and hormonal information in muscle. Am J Physiol Endocrinol Metab 279: E715-E729, 2000.
    • (2000) Am J Physiol Endocrinol Metab , vol.279
    • Shah, O.J.1    Anthony, J.C.2    Kimball, S.R.3    Jefferson, L.S.4
  • 47
    • 51649094129 scopus 로고    scopus 로고
    • Dexamethasone-induced apoptotic mechanisms in myeloma cells investigated by analysis of mutant glucocorticoid receptors
    • Sharma S, Lichtenstein A. Dexamethasone-induced apoptotic mechanisms in myeloma cells investigated by analysis of mutant glucocorticoid receptors. Blood 112: 1338-1345, 2008.
    • (2008) Blood , vol.112 , pp. 1338-1345
    • Sharma, S.1    Lichtenstein, A.2
  • 49
    • 33644849468 scopus 로고    scopus 로고
    • Quantification of hormone-induced atrophy of large myotubes from C2C12 and L6 cells: Atrophy-inducible and atrophy-resistant C2C12 myotubes
    • Sultan KR, Henkel B, Terlou M, Haagsman HP. Quantification of hormone-induced atrophy of large myotubes from C2C12 and L6 cells: atrophy-inducible and atrophy-resistant C2C12 myotubes. Am J Physiol Cell Physiol 290: C650-C659, 2006.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Sultan, K.R.1    Henkel, B.2    Terlou, M.3    Haagsman, H.P.4
  • 53
    • 38049134604 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 suppresses myogenic differentiation through negative regulation of NFATc3
    • Van der Velden JL, Schols AM, Willems J, Kelders MC, Langen RC. Glycogen synthase kinase 3 suppresses myogenic differentiation through negative regulation of NFATc3. J Biol Chem 283: 358-366, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 358-366
    • van der Velden, J.L.1    Schols, A.M.2    Willems, J.3    Kelders, M.C.4    Langen, R.C.5
  • 54
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • research0034
    • Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, Speleman F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 3: research0034, 2002.
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    de Preter, K.2    Pattyn, F.3    Poppe, B.4    van Roy, N.5    de Paepe, A.6    Speleman, F.7
  • 55
    • 0039700194 scopus 로고    scopus 로고
    • P70 S6 kinase-mediated protein synthesis is a critical step for vascular endothelial cell proliferation
    • Vinals F, Chambard JC, Pouyssegur J. p70 S6 kinase-mediated protein synthesis is a critical step for vascular endothelial cell proliferation. J Biol Chem 274: 26776-26782, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 26776-26782
    • Vinals, F.1    Chambard, J.C.2    Pouyssegur, J.3
  • 58
    • 77955375187 scopus 로고    scopus 로고
    • atrogin-1 affects muscle protein synthesis and degradation when energy metabolism is impaired by the antidiabetes drug berberine
    • Wang H, Liu D, Cao P, Lecker S, Hu Z. atrogin-1 affects muscle protein synthesis and degradation when energy metabolism is impaired by the antidiabetes drug berberine. Diabetes 59: 1879-1889, 2010.
    • (2010) Diabetes , vol.59 , pp. 1879-1889
    • Wang, H.1    Liu, D.2    Cao, P.3    Lecker, S.4    Hu, Z.5
  • 59
    • 0032498112 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B: Glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin
    • Welsh GI, Miller CM, Loughlin AJ, Price NT, Proud CG. Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin. FEBS Lett 421: 125-130, 1998.
    • (1998) FEBS Lett , vol.421 , pp. 125-130
    • Welsh, G.I.1    Miller, C.M.2    Loughlin, A.J.3    Price, N.T.4    Proud, C.G.5
  • 60
    • 0027460118 scopus 로고
    • Glucocorticoids activate the ATP-ubiquitindependent proteolytic system in skeletal muscle during fasting
    • Wing SS, Goldberg AL. Glucocorticoids activate the ATP-ubiquitindependent proteolytic system in skeletal muscle during fasting. Am J Physiol Endocrinol Metab 264: E668-E676, 1993.
    • (1993) Am J Physiol Endocrinol Metab , vol.264
    • Wing, S.S.1    Goldberg, A.L.2
  • 61
    • 0037401683 scopus 로고    scopus 로고
    • Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle
    • Wray CJ, Mammen JM, Hershko DD, Hasselgren PO. Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle. Int J Biochem Cell Biol 35: 698-705, 2003.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 698-705
    • Wray, C.J.1    Mammen, J.M.2    Hershko, D.D.3    Hasselgren, P.O.4
  • 62
    • 0017361716 scopus 로고
    • A myogenic cell line with altered serum requirements for differentiation
    • Yaffe D, Saxel O. A myogenic cell line with altered serum requirements for differentiation. Differentiation 7: 159-166, 1977.
    • (1977) Differentiation , vol.7 , pp. 159-166
    • Yaffe, D.1    Saxel, O.2
  • 63
    • 77951876957 scopus 로고    scopus 로고
    • IGF-1 prevents ANG II-induced skeletal muscle atrophy via Akt- and Foxodependent inhibition of the ubiquitin ligase atrogin-1 expression
    • Yoshida T, Semprun-Prieto L, Sukhanov S, Delafontaine P. IGF-1 prevents ANG II-induced skeletal muscle atrophy via Akt- and Foxodependent inhibition of the ubiquitin ligase atrogin-1 expression. Am J Physiol Heart Circ Physiol 298: H1565-H1570, 2010.
    • (2010) Am J Physiol Heart Circ Physiol , vol.298
    • Yoshida, T.1    Semprun-Prieto, L.2    Sukhanov, S.3    Delafontaine, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.