메뉴 건너뛰기




Volumn 41, Issue 1, 2018, Pages 67-73

The cell biology of the thyroid-disrupting mechanism of dichlorodiphenyltrichloroethane (DDT)

Author keywords

Dichlorodiphenyltrichloroethane; Extracellular vesicle; Graves disease; TSH receptor

Indexed keywords

CHLORPHENOTANE; THYROTROPIN RECEPTOR; PESTICIDE;

EID: 85021149160     PISSN: 03914097     EISSN: 17208386     Source Type: Journal    
DOI: 10.1007/s40618-017-0716-9     Document Type: Review
Times cited : (20)

References (53)
  • 1
    • 85010902340 scopus 로고    scopus 로고
    • Thyroid disruption by perfluorooctane sulfonate (PFOS) and perfluorooctanoate (PFOA)
    • COI: 1:CAS:528:DC%2BC28XhvVOnsLbP, PID: 27837466
    • Coperchini F, Awwad O, Rotondi M, Santini F, Imbriani M, Chiovato L (2017) Thyroid disruption by perfluorooctane sulfonate (PFOS) and perfluorooctanoate (PFOA). J Endocrinol Invest 40:105–121
    • (2017) J Endocrinol Invest , vol.40 , pp. 105-121
    • Coperchini, F.1    Awwad, O.2    Rotondi, M.3    Santini, F.4    Imbriani, M.5    Chiovato, L.6
  • 2
    • 0015781847 scopus 로고
    • A century of DDT
    • COI: 1:CAS:528:DyaE3sXkvVyis7Y%3D, PID: 4578152
    • Metcalf RL (1973) A century of DDT. J Agric Food Chem 21:511–519
    • (1973) J Agric Food Chem , vol.21 , pp. 511-519
    • Metcalf, R.L.1
  • 4
    • 84911478314 scopus 로고    scopus 로고
    • Impact of endocrine-disrupting chemicals on thyroid function and brain development
    • COI: 1:CAS:528:DC%2BC2cXhslOksrnN
    • Ibhazehiebo K, Koibuchi N (2014) Impact of endocrine-disrupting chemicals on thyroid function and brain development. Expert Rev Endocrinol Metab 9:579–591
    • (2014) Expert Rev Endocrinol Metab , vol.9 , pp. 579-591
    • Ibhazehiebo, K.1    Koibuchi, N.2
  • 5
    • 75149142140 scopus 로고    scopus 로고
    • Evidence for thyroid endocrine disruption in wild fish in San Francisco Bay, California, USA. Relationships to contaminant exposures
    • COI: 1:CAS:528:DC%2BC3cXhtlWktrc%3D, PID: 19939474
    • Brar NK, Waggoner C, Reyes JA, Fairey R, Kelley KM (2010) Evidence for thyroid endocrine disruption in wild fish in San Francisco Bay, California, USA. Relationships to contaminant exposures. Aquat Toxicol 96:203–215
    • (2010) Aquat Toxicol , vol.96 , pp. 203-215
    • Brar, N.K.1    Waggoner, C.2    Reyes, J.A.3    Fairey, R.4    Kelley, K.M.5
  • 6
    • 84892675179 scopus 로고    scopus 로고
    • Association between serum levels of organochlorine pesticides and sex hormones in adults living in a heavily contaminated area in Brazil
    • COI: 1:CAS:528:DC%2BC2cXhtFOiu7o%3D, PID: 23972672
    • Freire C, Koifman RJ, Sarcinelli PN, Rosa AC, Clapauch R, Koifman S (2014) Association between serum levels of organochlorine pesticides and sex hormones in adults living in a heavily contaminated area in Brazil. Int J Hyg Environ Health 217:370–378
    • (2014) Int J Hyg Environ Health , vol.217 , pp. 370-378
    • Freire, C.1    Koifman, R.J.2    Sarcinelli, P.N.3    Rosa, A.C.4    Clapauch, R.5    Koifman, S.6
  • 7
    • 84859512034 scopus 로고    scopus 로고
    • Thyroid effects of endocrine disrupting chemicals
    • COI: 1:CAS:528:DC%2BC38XlsFCkurw%3D, PID: 21939731
    • Boas M, Feldt-Rasmussen U, Main KM (2012) Thyroid effects of endocrine disrupting chemicals. Mol Cell Endocrinol 355:240–248
    • (2012) Mol Cell Endocrinol , vol.355 , pp. 240-248
    • Boas, M.1    Feldt-Rasmussen, U.2    Main, K.M.3
  • 8
    • 84864462348 scopus 로고    scopus 로고
    • Allosteric modulators of rhodopsin-like G protein-coupled receptors: opportunities in drug development
    • PID: 22728155
    • Müller CE, Schiedel AC, Baqi Y (2012) Allosteric modulators of rhodopsin-like G protein-coupled receptors: opportunities in drug development. Pharmacol Ther 135:292–315
    • (2012) Pharmacol Ther , vol.135 , pp. 292-315
    • Müller, C.E.1    Schiedel, A.C.2    Baqi, Y.3
  • 9
    • 84870754593 scopus 로고    scopus 로고
    • Update in TSH receptor agonists and antagonists
    • COI: 1:CAS:528:DC%2BC38XhvVCgt7vM, PID: 23019348
    • Gershengorn MC, Neumann S (2012) Update in TSH receptor agonists and antagonists. J Clin Endocrinol Metab 97:4287–4292
    • (2012) J Clin Endocrinol Metab , vol.97 , pp. 4287-4292
    • Gershengorn, M.C.1    Neumann, S.2
  • 10
    • 85019221329 scopus 로고    scopus 로고
    • Allosteric modulators of the class A G protein coupled receptors
    • COI: 1:CAS:528:DC%2BC2sXmvVehsrg%3D, PID: 27236557
    • Tschammer N (2016) Allosteric modulators of the class A G protein coupled receptors. Adv Exp Med Biol 917:185–207
    • (2016) Adv Exp Med Biol , vol.917 , pp. 185-207
    • Tschammer, N.1
  • 14
    • 79955603057 scopus 로고    scopus 로고
    • The insecticide 1,1,1-trichloro-2,2-bis(p-chlorophenyl) ethane (DDT) alters the membrane raft location of the TSH receptor stably expressed in Chinese hamster ovary cells
    • PID: 21466821
    • De Gregorio F, Pellegrino M, Picchietti S, Belardinelli MC, Taddei AR, Fausto AM, Rossi M, Maggio R, Giorgi F (2011) The insecticide 1,1,1-trichloro-2,2-bis(p-chlorophenyl) ethane (DDT) alters the membrane raft location of the TSH receptor stably expressed in Chinese hamster ovary cells. Toxicol Appl Pharmacol 253:121–129
    • (2011) Toxicol Appl Pharmacol , vol.253 , pp. 121-129
    • De Gregorio, F.1    Pellegrino, M.2    Picchietti, S.3    Belardinelli, M.C.4    Taddei, A.R.5    Fausto, A.M.6    Rossi, M.7    Maggio, R.8    Giorgi, F.9
  • 15
    • 79955713826 scopus 로고    scopus 로고
    • Thyroid-stimulating hormone receptor activity after internalization
    • COI: 1:CAS:528:DC%2BC3MXmtVyksro%3D
    • Calebiro D (2011) Thyroid-stimulating hormone receptor activity after internalization. Annales des Endocrinologie (Paris) 72:64–67
    • (2011) Annales des Endocrinologie (Paris) , vol.72 , pp. 64-67
    • Calebiro, D.1
  • 16
    • 84988329619 scopus 로고    scopus 로고
    • Semiotic tools for multilevel cell communication
    • Giorgi F, Auletta G (2016) Semiotic tools for multilevel cell communication. Biosemiotics 9:365–382
    • (2016) Biosemiotics , vol.9 , pp. 365-382
    • Giorgi, F.1    Auletta, G.2
  • 18
    • 79955717583 scopus 로고    scopus 로고
    • Extrathyroidal expression of TSH receptor
    • COI: 1:CAS:528:DC%2BC3MXmtVyksrg%3D
    • Williams GR (2011) Extrathyroidal expression of TSH receptor. Ann Endocrinol (Paris) 72:68–73
    • (2011) Ann Endocrinol (Paris) , vol.72 , pp. 68-73
    • Williams, G.R.1
  • 20
    • 0028224772 scopus 로고
    • The human thyrotropin receptor activates G-proteins Gs and Gq/11
    • COI: 1:CAS:528:DyaK2cXjtFKht74%3D, PID: 8188646
    • Allgeier A, Offermanns S, Van Sande J, Spicher K, Schultz G, Dumont JE (1994) The human thyrotropin receptor activates G-proteins Gs and Gq/11. J Biol Chem 269:13733–13735
    • (1994) J Biol Chem , vol.269 , pp. 13733-13735
    • Allgeier, A.1    Offermanns, S.2    Van Sande, J.3    Spicher, K.4    Schultz, G.5    Dumont, J.E.6
  • 21
    • 0030471654 scopus 로고    scopus 로고
    • Cell surface protein disulfide-isomerase is involved in the shedding of human thyrotropin receptor ectodomain
    • PID: 8942642
    • Couët J, de Bernard S, Loosfelt H, Saunier B, Milgrom E, Misrahi M (1996) Cell surface protein disulfide-isomerase is involved in the shedding of human thyrotropin receptor ectodomain. Biochemistry 35:14800–14805
    • (1996) Biochemistry , vol.35 , pp. 14800-14805
    • Couët, J.1    de Bernard, S.2    Loosfelt, H.3    Saunier, B.4    Milgrom, E.5    Misrahi, M.6
  • 22
    • 0030053238 scopus 로고    scopus 로고
    • Shedding of human thyrotropin receptor ectodomain. Involvement of a matrix metalloprotease
    • PID: 8626810
    • Couët J, Sar S, Jolivet A, Hai MT, Milgrom E, Misrahi M (1996) Shedding of human thyrotropin receptor ectodomain. Involvement of a matrix metalloprotease. J Biol Chem 271:4545–4552
    • (1996) J Biol Chem , vol.271 , pp. 4545-4552
    • Couët, J.1    Sar, S.2    Jolivet, A.3    Hai, M.T.4    Milgrom, E.5    Misrahi, M.6
  • 23
    • 0031409476 scopus 로고    scopus 로고
    • Mechanisms of shedding of a soluble form of the TSH receptor
    • COI: 1:CAS:528:DyaK1cXhsFGrtbk%3D
    • Misrahi M, Couet J, Milgrom E (1997) Mechanisms of shedding of a soluble form of the TSH receptor. Ann Endocrinol (Paris) 58:365–369
    • (1997) Ann Endocrinol (Paris) , vol.58 , pp. 365-369
    • Misrahi, M.1    Couet, J.2    Milgrom, E.3
  • 24
    • 9444277288 scopus 로고    scopus 로고
    • Monomerization as a prerequisite for intramolecular cleavage and shedding of the thyrotropin receptor
    • COI: 1:CAS:528:DC%2BD2cXhtVaqu7rM, PID: 15319351
    • Latif R, Ando T, Davies TF (2004) Monomerization as a prerequisite for intramolecular cleavage and shedding of the thyrotropin receptor. Endocrinology 145:5580–5588
    • (2004) Endocrinology , vol.145 , pp. 5580-5588
    • Latif, R.1    Ando, T.2    Davies, T.F.3
  • 25
    • 36248986754 scopus 로고    scopus 로고
    • G protein-coupled receptor oligomerization provides the framework for signal discrimination
    • COI: 1:CAS:528:DC%2BD2sXhsVekt7nL, PID: 17868304
    • Maggio R, Innamorati G, Parenti M (2007) G protein-coupled receptor oligomerization provides the framework for signal discrimination. J Neurochem 103:1741–1752
    • (2007) J Neurochem , vol.103 , pp. 1741-1752
    • Maggio, R.1    Innamorati, G.2    Parenti, M.3
  • 26
    • 84962960723 scopus 로고    scopus 로고
    • Revealing G-protein-coupled receptor oligomerization at the single-molecule level through a nanoscopic lens: methods, dynamics and biological function
    • COI: 1:CAS:528:DC%2BC2MXhvFWksrfK, PID: 26509747
    • Scarselli M, Annibale P, McCormick PJ, Kolachalam S, Aringhieri S, Radenovic A, Corsini GU, Maggio R (2016) Revealing G-protein-coupled receptor oligomerization at the single-molecule level through a nanoscopic lens: methods, dynamics and biological function. FEBS J 283:1197–1217
    • (2016) FEBS J , vol.283 , pp. 1197-1217
    • Scarselli, M.1    Annibale, P.2    McCormick, P.J.3    Kolachalam, S.4    Aringhieri, S.5    Radenovic, A.6    Corsini, G.U.7    Maggio, R.8
  • 27
    • 77955052967 scopus 로고    scopus 로고
    • Receptor oligomerization as a process modulating cellular semiotics
    • Giorgi F, Bruni LE, Maggio R (2010) Receptor oligomerization as a process modulating cellular semiotics. Biosemiotics 3:157–176
    • (2010) Biosemiotics , vol.3 , pp. 157-176
    • Giorgi, F.1    Bruni, L.E.2    Maggio, R.3
  • 28
    • 0033304941 scopus 로고    scopus 로고
    • Internalization and recycling pathways of the thyrotropin receptor
    • COI: 1:CAS:528:DyaK1MXms1Omt74%3D, PID: 10517676
    • Baratti-Elbaz C, Ghinea N, Lahuna O, Loosfelt H, Pichon C, Milgrom E (1999) Internalization and recycling pathways of the thyrotropin receptor. Mol Endocrinol 13:1751–1765
    • (1999) Mol Endocrinol , vol.13 , pp. 1751-1765
    • Baratti-Elbaz, C.1    Ghinea, N.2    Lahuna, O.3    Loosfelt, H.4    Pichon, C.5    Milgrom, E.6
  • 29
    • 0842334557 scopus 로고    scopus 로고
    • Upon thyrotropin binding the thyrotropin receptor is internalized and localized to endosome
    • COI: 1:CAS:528:DC%2BD2cXovFSrsg%3D%3D, PID: 14576174
    • Singh SP, McDonald D, Hope TJ, Prabhakar BS (2004) Upon thyrotropin binding the thyrotropin receptor is internalized and localized to endosome. Endocrinology 145:1003–1010
    • (2004) Endocrinology , vol.145 , pp. 1003-1010
    • Singh, S.P.1    McDonald, D.2    Hope, T.J.3    Prabhakar, B.S.4
  • 32
    • 84930857717 scopus 로고    scopus 로고
    • Minireview: role of intracellular scaffolding proteins in the regulation of endocrine G protein-coupled receptor signaling
    • Cornelia W, Ferguson SSG (2015) Minireview: role of intracellular scaffolding proteins in the regulation of endocrine G protein-coupled receptor signaling. Mol Endocrinol 29:814–830
    • (2015) Mol Endocrinol , vol.29 , pp. 814-830
    • Cornelia, W.1    Ferguson, S.S.G.2
  • 34
    • 34347257788 scopus 로고    scopus 로고
    • Lipid rafts are triage centers for multimeric and monomeric thyrotropin receptor regulation
    • COI: 1:CAS:528:DC%2BD2sXntVOgu70%3D, PID: 17412816
    • Latif R, Ando T, Davies TF (2007) Lipid rafts are triage centers for multimeric and monomeric thyrotropin receptor regulation. Endocrinology 148:3164–3175
    • (2007) Endocrinology , vol.148 , pp. 3164-3175
    • Latif, R.1    Ando, T.2    Davies, T.F.3
  • 35
    • 23944509766 scopus 로고    scopus 로고
    • Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation
    • PID: 15741221
    • Del Conde I, Shrimpton CN, Thiagarajan P, López JA (2005) Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation. Blood 106:1604–1611
    • (2005) Blood , vol.106 , pp. 1604-1611
    • Del Conde, I.1    Shrimpton, C.N.2    Thiagarajan, P.3    López, J.A.4
  • 37
    • 77952365658 scopus 로고    scopus 로고
    • Microvesicles: mediators of extracellular communication during cancer progression
    • COI: 1:CAS:528:DC%2BC3cXotFGrsLw%3D, PID: 20445011
    • Muralidharan-Chari V, Clancy JW, Sedgwick A, D’Souza-Schorey C (2010) Microvesicles: mediators of extracellular communication during cancer progression. J Cell Sci 123:1603–1611
    • (2010) J Cell Sci , vol.123 , pp. 1603-1611
    • Muralidharan-Chari, V.1    Clancy, J.W.2    Sedgwick, A.3    D’Souza-Schorey, C.4
  • 40
    • 84976347038 scopus 로고    scopus 로고
    • FRTL-5 Rat Thyroid cells release thyroglobulin sequestered in exosomes: a possible novel mechanism for thyroglobulin processing in the thyroid
    • Vlasov P, Doi SQ, Sellitti DF (2016) FRTL-5 Rat Thyroid cells release thyroglobulin sequestered in exosomes: a possible novel mechanism for thyroglobulin processing in the thyroid. J Tyroid Res 2016:9276402
    • (2016) J Tyroid Res , vol.2016 , pp. 9276402
    • Vlasov, P.1    Doi, S.Q.2    Sellitti, D.F.3
  • 41
    • 0033680962 scopus 로고    scopus 로고
    • Role of thyroglobulin endocytic pathways in the control of thyroid hormone release
    • PID: 11029276
    • Marinò M, McCluskey RT (2000) Role of thyroglobulin endocytic pathways in the control of thyroid hormone release. Am J Physiol Cell Physiol 279:C1295–C1306
    • (2000) Am J Physiol Cell Physiol , vol.279 , pp. C1295-C1306
    • Marinò, M.1    McCluskey, R.T.2
  • 42
    • 80054103916 scopus 로고    scopus 로고
    • Binding, uptake, and degradation of internalized thyroglobulin in cultured thyroid and non-thyroid cells
    • COI: 1:CAS:528:DC%2BC3MXhsVGns7rN, PID: 20959721
    • Botta R, Lisi S, Pinchera A, Taddei AR, Fausto AM, Giorgi F, Marinò M (2011) Binding, uptake, and degradation of internalized thyroglobulin in cultured thyroid and non-thyroid cells. J Endocrinol Invest 34:515–520
    • (2011) J Endocrinol Invest , vol.34 , pp. 515-520
    • Botta, R.1    Lisi, S.2    Pinchera, A.3    Taddei, A.R.4    Fausto, A.M.5    Giorgi, F.6    Marinò, M.7
  • 43
    • 84983035667 scopus 로고    scopus 로고
    • Intracellular retention of thyroglobulin in the absence of the low-density lipoprotein receptor-associated protein (RAP) is likely due to premature binding to megalin in the biosynthetic pathway
    • COI: 1:CAS:528:DC%2BC28XmvVSjtb8%3D, PID: 27094046
    • Lisi S, Botta R, Rotondo Dottore G, Leo M, Latrofa F, Vitti P, Marinò M (2016) Intracellular retention of thyroglobulin in the absence of the low-density lipoprotein receptor-associated protein (RAP) is likely due to premature binding to megalin in the biosynthetic pathway. J Endocrinol Invest 39:1039–1044
    • (2016) J Endocrinol Invest , vol.39 , pp. 1039-1044
    • Lisi, S.1    Botta, R.2    Rotondo Dottore, G.3    Leo, M.4    Latrofa, F.5    Vitti, P.6    Marinò, M.7
  • 44
    • 85019097803 scopus 로고    scopus 로고
    • Binding of thyroglobulin (Tg) to the low-density lipoprotein receptor-associated protein (RAP) during the biosynthetic pathway prevents premature Tg interactions with sortilin
    • Botta R, Lisi S, Rotondo Dottore G, Vitti P, Marinò M (2017) Binding of thyroglobulin (Tg) to the low-density lipoprotein receptor-associated protein (RAP) during the biosynthetic pathway prevents premature Tg interactions with sortilin. J Endocrinol Invest. doi: 10.1007/s40618-017-0668-0. (Epub ahead of print)
    • (2017) J Endocrinol Invest
    • Botta, R.1    Lisi, S.2    Rotondo Dottore, G.3    Vitti, P.4    Marinò, M.5
  • 45
    • 57149087260 scopus 로고    scopus 로고
    • Secretion of active membrane type 1 matrix metalloproteinase (MMP-14) into extracellular space in microvesicular exosomes
    • COI: 1:CAS:528:DC%2BD1cXhsFWgt77L, PID: 18802920
    • Hakulinen J, Sankkila L, Sugiyama N, Kaisa Lehti K, Keski-Oja J (2008) Secretion of active membrane type 1 matrix metalloproteinase (MMP-14) into extracellular space in microvesicular exosomes. J Cell Biochem 105:1211–1218
    • (2008) J Cell Biochem , vol.105 , pp. 1211-1218
    • Hakulinen, J.1    Sankkila, L.2    Sugiyama, N.3    Kaisa Lehti, K.4    Keski-Oja, J.5
  • 46
    • 84874377202 scopus 로고    scopus 로고
    • Extracellular vesicles: exosomes, microvesicles, and friends
    • COI: 1:CAS:528:DC%2BC3sXjtFCnsbk%3D, PID: 23420871
    • Raposo G, Stoorvogel W (2013) Extracellular vesicles: exosomes, microvesicles, and friends. J Cell Biol 200:373–383
    • (2013) J Cell Biol , vol.200 , pp. 373-383
    • Raposo, G.1    Stoorvogel, W.2
  • 47
    • 85047558390 scopus 로고    scopus 로고
    • Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3D collagen matrix
    • Masci VL, Taddei AR, Gambellini G, Giorgi F, Fausto AM (2016) Microvesicles shed from fibroblasts act as metalloproteinase carriers in a 3D collagen matrix. J Circ Biomark 5:1–11
    • (2016) J Circ Biomark , vol.5 , pp. 1-11
    • Masci, V.L.1    Taddei, A.R.2    Gambellini, G.3    Giorgi, F.4    Fausto, A.M.5
  • 48
    • 0031936373 scopus 로고    scopus 로고
    • Integrins in thyroid tissue: upregulation of a2b1 in anaplastic thyroid carcinoma
    • COI: 1:CAS:528:DyaK1cXhtVChs7k%3D, PID: 9461325
    • Dahlman T, Grimelius L, Wallin G, Rubin K, Westermark K (1998) Integrins in thyroid tissue: upregulation of a2b1 in anaplastic thyroid carcinoma. Eur J Endocrinol 138:104–112
    • (1998) Eur J Endocrinol , vol.138 , pp. 104-112
    • Dahlman, T.1    Grimelius, L.2    Wallin, G.3    Rubin, K.4    Westermark, K.5
  • 50
    • 84929575459 scopus 로고    scopus 로고
    • Targeting the thyroid-stimulating hormone receptor with small molecule ligands and antibodies
    • COI: 1:CAS:528:DC%2BC2MXovVegsLg%3D, PID: 25768836
    • Davies TF, Latif R (2015) Targeting the thyroid-stimulating hormone receptor with small molecule ligands and antibodies. Expert Opin Ther Targets 19:835–847
    • (2015) Expert Opin Ther Targets , vol.19 , pp. 835-847
    • Davies, T.F.1    Latif, R.2
  • 51
    • 84976328958 scopus 로고    scopus 로고
    • Recent advances of exosomes in immune modulation and autoimmune diseases
    • COI: 1:CAS:528:DC%2BC28XptlCrsLY%3D
    • Tan L, Wu H, Liu Y, Zhao M, Li D, Lu Q (2016) Recent advances of exosomes in immune modulation and autoimmune diseases. J Autoimmun 49:357–365
    • (2016) J Autoimmun , vol.49 , pp. 357-365
    • Tan, L.1    Wu, H.2    Liu, Y.3    Zhao, M.4    Li, D.5    Lu, Q.6
  • 52
    • 84857968441 scopus 로고    scopus 로고
    • The majority of microRNAs detectable in serum and saliva is concentrated in exosomes
    • COI: 1:CAS:528:DC%2BC38XktlSktrs%3D, PID: 22427800
    • Gallo A, Tandon M, Alevizos I, Illei GG (2012) The majority of microRNAs detectable in serum and saliva is concentrated in exosomes. PLoS One 7(3):e30679
    • (2012) PLoS One , vol.7 , Issue.3
    • Gallo, A.1    Tandon, M.2    Alevizos, I.3    Illei, G.G.4
  • 53
    • 84964798275 scopus 로고    scopus 로고
    • Exosomes: the link between GPCR activation and metastatic potential?
    • PID: 27092178
    • Isola AL, Chen S (2016) Exosomes: the link between GPCR activation and metastatic potential? Front Genet 7:56
    • (2016) Front Genet , vol.7 , pp. 56
    • Isola, A.L.1    Chen, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.