메뉴 건너뛰기




Volumn 4, Issue 2, 2014, Pages 181-187

Aspartame induces alteration in electrolytes homeostasis of immune organs in wistar albino rats

Author keywords

Aspartame; ATPases; Immune organs; Oxidative stress; Protein carbonyl; Protein thiol

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALPHA TOCOPHEROL; ASPARTAME; CARBONYL DERIVATIVE; FOLIC ACID; FREE RADICAL; LIPID PEROXIDE; METHANOL; THIOL PROTEINASE;

EID: 84901609784     PISSN: 22105239     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bionut.2013.12.006     Document Type: Article
Times cited : (4)

References (60)
  • 1
    • 0035701818 scopus 로고    scopus 로고
    • Aspartame: scientific evaluation in the post marketing period
    • Butchko H.H., Stargel W.W. Aspartame: scientific evaluation in the post marketing period. Regul Toxicol Pharmacol 2001, 34:221-233.
    • (2001) Regul Toxicol Pharmacol , vol.34 , pp. 221-233
    • Butchko, H.H.1    Stargel, W.W.2
  • 2
    • 0036203427 scopus 로고    scopus 로고
    • Cytotoxic effects of methanol, formaldehyde and formate on dissociated rat thymocytes: a possibility of Aspartame toxicity
    • Oyama Y., Sakai H., Arata T., et al. Cytotoxic effects of methanol, formaldehyde and formate on dissociated rat thymocytes: a possibility of Aspartame toxicity. Cell Biol Toxicol 2002, 18:43-50.
    • (2002) Cell Biol Toxicol , vol.18 , pp. 43-50
    • Oyama, Y.1    Sakai, H.2    Arata, T.3
  • 3
    • 0022585363 scopus 로고
    • Serum methanol concentrations in rats and in men after a single dose of Aspartame
    • Davoli E. Serum methanol concentrations in rats and in men after a single dose of Aspartame. Food Chem Toxicol 1986, 24:187-189.
    • (1986) Food Chem Toxicol , vol.24 , pp. 187-189
    • Davoli, E.1
  • 4
    • 33644775132 scopus 로고
    • Aspartame metabolism in animals
    • Marcel Dekker, L.D. Stegink, L.J. Filer (Eds.)
    • Oppermann J.A. Aspartame metabolism in animals. Aspartame, physiology and biochemistry 1984, 141-159. Marcel Dekker. L.D. Stegink, L.J. Filer (Eds.).
    • (1984) Aspartame, physiology and biochemistry , pp. 141-159
    • Oppermann, J.A.1
  • 5
    • 0025890083 scopus 로고
    • Metabolism of Aspartame and its L-phenylalanine methyl ester decomposition product by porcine gut
    • Burgert S.L., Andersen D.W., Stegink L.D., et al. Metabolism of Aspartame and its L-phenylalanine methyl ester decomposition product by porcine gut. Metabolism 1991, 40:612.
    • (1991) Metabolism , vol.40 , pp. 612
    • Burgert, S.L.1    Andersen, D.W.2    Stegink, L.D.3
  • 6
    • 79960265284 scopus 로고    scopus 로고
    • Metabolism and pharmacokinetics of radio labeled Aspartame in normal subjects
    • Boca Raton, New York, London, Tokyo, [CRC], C. Tschanz, H.H. Butchko, W.W. Stargel, F.N. Kotsonis (Eds.)
    • Karim A., Burns T. Metabolism and pharmacokinetics of radio labeled Aspartame in normal subjects. The clinical evaluation of a food additive. Assessment of Aspartame 1996, 57-66. Boca Raton, New York, London, Tokyo, [CRC]. C. Tschanz, H.H. Butchko, W.W. Stargel, F.N. Kotsonis (Eds.).
    • (1996) The clinical evaluation of a food additive. Assessment of Aspartame , pp. 57-66
    • Karim, A.1    Burns, T.2
  • 7
    • 0019508178 scopus 로고
    • Blood methanol concentrations in normal adult subjects administered abuse doses of Aspartame
    • Stegink L.D., Brummel M.C., McMartin K.E., et al. Blood methanol concentrations in normal adult subjects administered abuse doses of Aspartame. J Toxicol Environ Health 1981, 7:281-290.
    • (1981) J Toxicol Environ Health , vol.7 , pp. 281-290
    • Stegink, L.D.1    Brummel, M.C.2    McMartin, K.E.3
  • 9
    • 84862598603 scopus 로고
    • Membrane thiol disulfide status in glucose-6-phosphate dehydrogenase deficient red cells. Relationship to cellular glutathione
    • Kosawer N.J., Zipser Y., Faltin Z. Membrane thiol disulfide status in glucose-6-phosphate dehydrogenase deficient red cells. Relationship to cellular glutathione. Biochim Biophys Acta 1991, 1058:152-160.
    • (1991) Biochim Biophys Acta , vol.1058 , pp. 152-160
    • Kosawer, N.J.1    Zipser, Y.2    Faltin, Z.3
  • 10
    • 0003027669 scopus 로고
    • Properties and functions
    • Transport ATPases:
    • Stekhoren M.A., Bonting S.L., Transport ATPases: Properties and functions. Physiol Rev 1981, 61:1-76.
    • (1981) Physiol Rev , vol.61 , pp. 1-76
    • Stekhoren, M.A.1    Bonting, S.L.2
  • 12
    • 2942572700 scopus 로고    scopus 로고
    • Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?
    • Halliwell B., Whiteman M. Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?. Br J Pharmacol 2004, 142:231-255.
    • (2004) Br J Pharmacol , vol.142 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 13
    • 0032569827 scopus 로고    scopus 로고
    • Evidence of oxidative stress in mdx mouse muscle: studies of the pre-necrotic state
    • Disatnik M.H., Dhawan J., Yu Y., et al. Evidence of oxidative stress in mdx mouse muscle: studies of the pre-necrotic state. J Neurol Sci 1998, 161:77-84.
    • (1998) J Neurol Sci , vol.161 , pp. 77-84
    • Disatnik, M.H.1    Dhawan, J.2    Yu, Y.3
  • 14
    • 34249908644 scopus 로고    scopus 로고
    • Low intensity training decreases markers of oxidative stress in skeletal muscle of mdx mice
    • Kaczor J.J., Hall J.E., Payne E., et al. Low intensity training decreases markers of oxidative stress in skeletal muscle of mdx mice. Free Radic Biol Med 2007, 43:145-154.
    • (2007) Free Radic Biol Med , vol.43 , pp. 145-154
    • Kaczor, J.J.1    Hall, J.E.2    Payne, E.3
  • 15
    • 54049086602 scopus 로고    scopus 로고
    • Oxidative stress as a therapeutic target during muscle wasting: considering the complex interactions
    • Arthur P.G., Grounds M.D., Shavlakadze T. Oxidative stress as a therapeutic target during muscle wasting: considering the complex interactions. Curr Opin Clin Nutr Metab Care 2008, 11:408-416.
    • (2008) Curr Opin Clin Nutr Metab Care , vol.11 , pp. 408-416
    • Arthur, P.G.1    Grounds, M.D.2    Shavlakadze, T.3
  • 16
    • 73649141725 scopus 로고    scopus 로고
    • Detecting changes in the thiol redox state of proteins following a decrease in oxygen concentration using a dual labeling technique
    • Lui J.K., Lipscombe R., Arthur P.G. Detecting changes in the thiol redox state of proteins following a decrease in oxygen concentration using a dual labeling technique. J Proteome Res 2010, 9:383-392.
    • (2010) J Proteome Res , vol.9 , pp. 383-392
    • Lui, J.K.1    Lipscombe, R.2    Arthur, P.G.3
  • 18
    • 0024519936 scopus 로고
    • Thenen Methotrexate effects on folate status and the deoxyuridine suppression test in rats
    • Ming H., Wang S.Y., Craig A., et al. Thenen Methotrexate effects on folate status and the deoxyuridine suppression test in rats. Nut Res 1989, 9:431-444.
    • (1989) Nut Res , vol.9 , pp. 431-444
    • Ming, H.1    Wang, S.Y.2    Craig, A.3
  • 19
    • 46649108278 scopus 로고    scopus 로고
    • Opinion of the Scientific Panel on Food Additives, Flavourings, Processing Aids and Materials in contact with Food (AFC) on a request from the Commission related to a new long-term carcinogenicity study on Aspartame. Question number EFSA-Q-2005-122. Adopted on 3 May 2006
    • European Food Safety Authority (EFSA)
    • European Food Safety Authority (EFSA) Opinion of the Scientific Panel on Food Additives, Flavourings, Processing Aids and Materials in contact with Food (AFC) on a request from the Commission related to a new long-term carcinogenicity study on Aspartame. Question number EFSA-Q-2005-122. Adopted on 3 May 2006. EFSA J 2006, 356:1-44.
    • (2006) EFSA J , vol.356 , pp. 1-44
  • 20
    • 0017115609 scopus 로고
    • Methanol in poisoning folate-deficient rats
    • Maker A.B., Tephly T.R. Methanol in poisoning folate-deficient rats. Nature 1976, 261:715-716.
    • (1976) Nature , vol.261 , pp. 715-716
    • Maker, A.B.1    Tephly, T.R.2
  • 21
    • 0025927934 scopus 로고
    • The toxicity of methanol
    • Tephly T.R. The toxicity of methanol. Life Sci 1991, 48:1031-1041.
    • (1991) Life Sci , vol.48 , pp. 1031-1041
    • Tephly, T.R.1
  • 22
    • 0042970421 scopus 로고
    • Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid
    • Rabinowitz J.C., Pricer W.E. Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid. J Am Chem Soc 1956, 78:5702-5704.
    • (1956) J Am Chem Soc , vol.78 , pp. 5702-5704
    • Rabinowitz, J.C.1    Pricer, W.E.2
  • 23
    • 0018843626 scopus 로고
    • Participation of dorsal hippocampus in the glucocorticoids feedback effect on adrenocortical activity
    • Feldman S., Conforti N. Participation of dorsal hippocampus in the glucocorticoids feedback effect on adrenocortical activity. Neuroendocrinology 1980, 30:52-55.
    • (1980) Neuroendocrinology , vol.30 , pp. 52-55
    • Feldman, S.1    Conforti, N.2
  • 24
    • 0001473390 scopus 로고
    • Sodium potassium activated adenosine triphosphatase and cation transport
    • Interscience Wiley, London
    • Bonting S.L. Sodium potassium activated adenosine triphosphatase and cation transport. Membrane and ion transport 1970, 1:257-263. Interscience Wiley, London.
    • (1970) Membrane and ion transport , vol.1 , pp. 257-263
    • Bonting, S.L.1
  • 25
    • 0020623732 scopus 로고
    • Purification and characterization of two forms of a low affinity Ca2+ATPase from erythrocyte membranes
    • Hjerten S., Pan H. Purification and characterization of two forms of a low affinity Ca2+ATPase from erythrocyte membranes. Biochem Biophys Acta 1983, 728:281-288.
    • (1983) Biochem Biophys Acta , vol.728 , pp. 281-288
    • Hjerten, S.1    Pan, H.2
  • 26
    • 0020060819 scopus 로고
    • A comparative study of plasma membrane Mg2+ATPase activities in normal, regenerating and malignant cells
    • Ohnishi T., Suzuki T., Suzuki Y., et al. A comparative study of plasma membrane Mg2+ATPase activities in normal, regenerating and malignant cells. Biochim Biophys Acta 1982, 684:67-74.
    • (1982) Biochim Biophys Acta , vol.684 , pp. 67-74
    • Ohnishi, T.1    Suzuki, T.2    Suzuki, Y.3
  • 27
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorous
    • Fiske C.H., Subbarow Y. The colorimetric determination of phosphorous. J Biol Chem 1925, 663:75-400.
    • (1925) J Biol Chem , vol.663 , pp. 75-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 28
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry O.H., Rosebrough N.J., Farr A.L., et al. Protein measurement with the Folin phenol reagent. J Biol Chem 1951, 193:265-275.
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3
  • 29
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H., Ohishi N., Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 1979, 95:351-358.
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 30
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidativelymodi
    • ed proteins
    • Levine R.L., Williams J.A., Stadtman E.R., et al. Carbonyl assays for determination of oxidativelymodi. ed proteins. Methods Enzymol 1994, 233:346-363.
    • (1994) Methods Enzymol , vol.233 , pp. 346-363
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3
  • 31
    • 0014428865 scopus 로고
    • Estimation of total protein bound and non proteinsuiphydryl in the tissue with Ellman's reagent
    • Sedlack J., Lindsay R.H. Estimation of total protein bound and non proteinsuiphydryl in the tissue with Ellman's reagent. Anal Biochem 1968, 25:192-205.
    • (1968) Anal Biochem , vol.25 , pp. 192-205
    • Sedlack, J.1    Lindsay, R.H.2
  • 32
    • 0021288822 scopus 로고
    • Vitamin E analysis methods for animal tissues
    • Desai I.D. Vitamin E analysis methods for animal tissues. Methods Enzymol 1984, 105:138-147.
    • (1984) Methods Enzymol , vol.105 , pp. 138-147
    • Desai, I.D.1
  • 34
    • 14644399750 scopus 로고    scopus 로고
    • Counterction of oxalate induced nitrosative stress by supplementation of L-arginine, a potent antilithic agent
    • Pragasam V., Kalaiselvi P., Sumitra K., et al. Counterction of oxalate induced nitrosative stress by supplementation of L-arginine, a potent antilithic agent. Clin Chim Acta 2005, 354:159-166.
    • (2005) Clin Chim Acta , vol.354 , pp. 159-166
    • Pragasam, V.1    Kalaiselvi, P.2    Sumitra, K.3
  • 39
    • 0019450954 scopus 로고
    • Calcium potentiates the peroxidation of erythrocytemembrane lipids
    • Jain K.S., Shohet S.B. Calcium potentiates the peroxidation of erythrocytemembrane lipids. Biochem Biophys Acta 1981, 642:46-54.
    • (1981) Biochem Biophys Acta , vol.642 , pp. 46-54
    • Jain, K.S.1    Shohet, S.B.2
  • 41
    • 84942398580 scopus 로고
    • Role of magnesium in cardiac diseases
    • Ebel H., Gunther T. Role of magnesium in cardiac diseases. J Clin Biochem 1983, 21:249.
    • (1983) J Clin Biochem , vol.21 , pp. 249
    • Ebel, H.1    Gunther, T.2
  • 42
    • 0022295756 scopus 로고
    • New perspectives on the role of magnesium in the pathophysiology of cardiovascular system.1. Clinical aspects
    • Altura B.M., Altura B.T. New perspectives on the role of magnesium in the pathophysiology of cardiovascular system.1. Clinical aspects. Magnesium 1985, 4:226.
    • (1985) Magnesium , vol.4 , pp. 226
    • Altura, B.M.1    Altura, B.T.2
  • 43
    • 7644240645 scopus 로고    scopus 로고
    • Oxidative stress a predisposing factor for renal stone formation- amelioration by vitamin E supplementation
    • Pragasam S., Jenitha V., Kalaiselvi X., et al. Oxidative stress a predisposing factor for renal stone formation- amelioration by vitamin E supplementation. Clin Chem Acta 2004, 350:57-63.
    • (2004) Clin Chem Acta , vol.350 , pp. 57-63
    • Pragasam, S.1    Jenitha, V.2    Kalaiselvi, X.3
  • 44
    • 0034911751 scopus 로고    scopus 로고
    • Effect of vitamin E, vitamin C and spirulina on the levels of membrane-bound enzymes and lipids in some organs of rats exposed to lead
    • Upasani C.D., Balaraman R. Effect of vitamin E, vitamin C and spirulina on the levels of membrane-bound enzymes and lipids in some organs of rats exposed to lead. Indian J Pharmacol 2001, 33:185-191.
    • (2001) Indian J Pharmacol , vol.33 , pp. 185-191
    • Upasani, C.D.1    Balaraman, R.2
  • 45
    • 0030598991 scopus 로고    scopus 로고
    • Thymosin protects liver and aorta from oxidative damage in atherosclerotic rabbits
    • Gokkuou C., Ademolu E., Turkolu U.M., et al. Thymosin protects liver and aorta from oxidative damage in atherosclerotic rabbits. Life Sci 1996, 59:1059-1067.
    • (1996) Life Sci , vol.59 , pp. 1059-1067
    • Gokkuou, C.1    Ademolu, E.2    Turkolu, U.M.3
  • 46
    • 0023178426 scopus 로고
    • Vitamin E protection against chemical induced injury. Maintenance of cellular protein thiols as a cytoprptective mechanism
    • Pasoe G.A., Olafsdottir K., Reed D.J. Vitamin E protection against chemical induced injury. Maintenance of cellular protein thiols as a cytoprptective mechanism. Arch Biochem Biophys 1987, 256:150-168.
    • (1987) Arch Biochem Biophys , vol.256 , pp. 150-168
    • Pasoe, G.A.1    Olafsdottir, K.2    Reed, D.J.3
  • 47
    • 43449131541 scopus 로고    scopus 로고
    • Relation of plasma protein oxidation parameters and paraoxonase activity in the ageing population
    • Cakatay U., Kayali R., Uzun H. Relation of plasma protein oxidation parameters and paraoxonase activity in the ageing population. Clin Exp Med 2008, 8:51-57.
    • (2008) Clin Exp Med , vol.8 , pp. 51-57
    • Cakatay, U.1    Kayali, R.2    Uzun, H.3
  • 48
    • 0035312208 scopus 로고    scopus 로고
    • Oxidative damage following cerebral ischemia depends on reperfusion - a biochemical study in rat
    • Nita D.A., Nita V., Spulber S., et al. Oxidative damage following cerebral ischemia depends on reperfusion - a biochemical study in rat. J Cell Mol Med 2001, 5:163-170.
    • (2001) J Cell Mol Med , vol.5 , pp. 163-170
    • Nita, D.A.1    Nita, V.2    Spulber, S.3
  • 50
    • 0021679890 scopus 로고
    • Enhanced lysosomal phospholipid degradation and lysphospholipid production due to free radical
    • Weglicki W.B., Dickens B.F., Mak I.T. Enhanced lysosomal phospholipid degradation and lysphospholipid production due to free radical. Biochem Biophys 1984, 124:229-235.
    • (1984) Biochem Biophys , vol.124 , pp. 229-235
    • Weglicki, W.B.1    Dickens, B.F.2    Mak, I.T.3
  • 51
    • 46149102483 scopus 로고    scopus 로고
    • Protective effect of melatonin against formaldehyde- induced kidney damage in rats
    • Zararsiz I., Sarsilmaz M., Tas U., et al. Protective effect of melatonin against formaldehyde- induced kidney damage in rats. Toxicol Indian Health 2007, 23(10):573-579.
    • (2007) Toxicol Indian Health , vol.23 , Issue.10 , pp. 573-579
    • Zararsiz, I.1    Sarsilmaz, M.2    Tas, U.3
  • 52
    • 0035574844 scopus 로고    scopus 로고
    • Beta-carotene production and its role in sclerotial differentiation of Sclerotiumrolfsii
    • Georgiou C.D., Zervoudakis G., Tairis N., et al. Beta-carotene production and its role in sclerotial differentiation of Sclerotiumrolfsii. Fungal Genet Biol 2001, 34:11-20.
    • (2001) Fungal Genet Biol , vol.34 , pp. 11-20
    • Georgiou, C.D.1    Zervoudakis, G.2    Tairis, N.3
  • 53
    • 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., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 2001, 1:1191-1212.
    • (2001) Free Radic Biol Med , vol.1 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 54
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 1993, 62:797-821.
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 55
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine R., Williams J.A., Stadtman E.R., et al. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol 1994, 233:346-363.
    • (1994) Methods Enzymol , vol.233 , pp. 346-363
    • Levine, R.1    Williams, J.A.2    Stadtman, E.R.3
  • 56
    • 0025808924 scopus 로고
    • The effect of tocopherol as an antioxidant on the oxidation of membrane protein thiols induced by free radicals generated in different sites
    • Takenaka Y., Miki M., Yasuda H., et al. The effect of tocopherol as an antioxidant on the oxidation of membrane protein thiols induced by free radicals generated in different sites. Arch Biochem Biophys 1991, 285:344-350.
    • (1991) Arch Biochem Biophys , vol.285 , pp. 344-350
    • Takenaka, Y.1    Miki, M.2    Yasuda, H.3
  • 57
    • 31644450799 scopus 로고    scopus 로고
    • Synergistic protection by adenosylmethionine with vitamins C and E on liver injury induced by thioacetamide in rats
    • Ming Z., Fan Y., Yang X., et al. Synergistic protection by adenosylmethionine with vitamins C and E on liver injury induced by thioacetamide in rats. Free Radic Biol Med 2006, 40:617-624.
    • (2006) Free Radic Biol Med , vol.40 , pp. 617-624
    • Ming, Z.1    Fan, Y.2    Yang, X.3
  • 58
    • 0033063671 scopus 로고    scopus 로고
    • Protcctive role of ubiquinone in vitamin E and selenium deficient plasma membranes
    • Navarro F., Arroyo A., Vlanin S.L., et al. Protcctive role of ubiquinone in vitamin E and selenium deficient plasma membranes. Bio Factors 1999, 9:163-170.
    • (1999) Bio Factors , vol.9 , pp. 163-170
    • Navarro, F.1    Arroyo, A.2    Vlanin, S.L.3
  • 59
    • 0031306201 scopus 로고    scopus 로고
    • Ultrastructral elevation of lysosome and biochemical change in cathepsin D distribution in hepatocytes in methanol intoxication
    • Skrzydlewksa E., Szynaka B. ultrastructral elevation of lysosome and biochemical change in cathepsin D distribution in hepatocytes in methanol intoxication. Roczniki Akademii Medycznej W Bialymstoku 1997, 42:47-55.
    • (1997) Roczniki Akademii Medycznej W Bialymstoku , vol.42 , pp. 47-55
    • Skrzydlewksa, E.1    Szynaka, B.2
  • 60
    • 0037716626 scopus 로고    scopus 로고
    • Formaldehyde induced shrinkage of rat thymocyte
    • Nakao H., Umebayashi C., Nakata M., et al. Formaldehyde induced shrinkage of rat thymocyte. J Pharmacol Sci 2003, 91:83-86.
    • (2003) J Pharmacol Sci , vol.91 , pp. 83-86
    • Nakao, H.1    Umebayashi, C.2    Nakata, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.