메뉴 건너뛰기




Volumn 6, Issue 1, 2011, Pages

Biophysical characterization of the olfactomedin domain of Myocilin, an extracellular matrix protein implicated in inherited forms of glaucoma

Author keywords

[No Author keywords available]

Indexed keywords

BETA CRYSTALLIN; CHYMOTRYPSIN A; GAMMA CRYSTALLIN; GLYCOSAMINOGLYCAN; MALTOSE BINDING PROTEIN; MYOCILIN; MYOCILIN OLFACTOMEDIN DOMAIN PROTEIN; SCLEROPROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG; CYTOSKELETON PROTEIN; EYE PROTEIN; GLYCOPROTEIN; OLFACTOMEDIN; TRABECULAR MESHWORK-INDUCED GLUCOCORTICOID RESPONSE PROTEIN;

EID: 79551529083     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0016347     Document Type: Article
Times cited : (32)

References (53)
  • 1
    • 64249133288 scopus 로고    scopus 로고
    • Glaucoma-associated myocilin: A better understanding but much more to learn
    • Resch Z, Fautsch M (2009) Glaucoma-associated myocilin: A better understanding but much more to learn. Exp Eye Res 88: 704-712.
    • (2009) Exp Eye Res , vol.88 , pp. 704-712
    • Resch, Z.1    Fautsch, M.2
  • 2
    • 0036202868 scopus 로고    scopus 로고
    • Distribution of myocilin and extracellular matrix components in the juxtacanalicular tissue of human eyes
    • Ueda J, Wentz-Hunter K, Yue BY (2002) Distribution of myocilin and extracellular matrix components in the juxtacanalicular tissue of human eyes. Invest Ophthalmol Vis Sci 43: 1068-1076.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 1068-1076
    • Ueda, J.1    Wentz-Hunter, K.2    Yue, B.Y.3
  • 3
    • 0034442691 scopus 로고    scopus 로고
    • Immunohistochemical localization of MYOC/TIGR protein in the trabecular tissue of normal and glaucomatous eyes
    • Tawara A, Okada Y, Kubota T, Suzuki Y, Taniguchi F, et al. (2000) Immunohistochemical localization of MYOC/TIGR protein in the trabecular tissue of normal and glaucomatous eyes. Curr Eye Res 21: 934-943.
    • (2000) Curr Eye Res , vol.21 , pp. 934-943
    • Tawara, A.1    Okada, Y.2    Kubota, T.3    Suzuki, Y.4    Taniguchi, F.5
  • 4
    • 0036140397 scopus 로고    scopus 로고
    • In vitro localization of TIGR/MYOC in trabecular meshwork extracellular matrix and binding to fibronectin
    • Filla MS, Liu X, Nguyen TD, Polansky JR, Brandt CR, et al. (2002) In vitro localization of TIGR/MYOC in trabecular meshwork extracellular matrix and binding to fibronectin. Invest Ophthalmol Vis Sci 43: 151-161.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 151-161
    • Filla, M.S.1    Liu, X.2    Nguyen, T.D.3    Polansky, J.R.4    Brandt, C.R.5
  • 5
    • 2642562995 scopus 로고    scopus 로고
    • Extracellular myocilin affects activity of human trabecular meshwork cells
    • Wentz-Hunter K, Kubota R, Shen X, Yue B (2004) Extracellular myocilin affects activity of human trabecular meshwork cells. J Cell Physiol 200: 45-52.
    • (2004) J Cell Physiol , vol.200 , pp. 45-52
    • Wentz-Hunter, K.1    Kubota, R.2    Shen, X.3    Yue, B.4
  • 7
    • 0034780081 scopus 로고    scopus 로고
    • Targeted disruption of the myocilin gene (myoc) suggests that human glaucoma-causing mutations are gain of function
    • Kim BS, Savinova OV, Reedy MV, Martin J, Lun Y, et al. (2001) Targeted disruption of the myocilin gene (myoc) suggests that human glaucoma-causing mutations are gain of function. Mol Cell Biol 21: 7707-7713.
    • (2001) Mol Cell Biol , vol.21 , pp. 7707-7713
    • Kim, B.S.1    Savinova, O.V.2    Reedy, M.V.3    Martin, J.4    Lun, Y.5
  • 8
    • 0034020149 scopus 로고    scopus 로고
    • Truncations in the TIGR gene in individuals with and without primary open-angle glaucoma
    • Lam DS, Leung YF, Chua JK, Baum L, Fan DS, et al. (2000) Truncations in the TIGR gene in individuals with and without primary open-angle glaucoma. Invest Ophthalmol Vis Sci 41: 1386-1391.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 1386-1391
    • Lam, D.S.1    Leung, Y.F.2    Chua, J.K.3    Baum, L.4    Fan, D.S.5
  • 9
    • 33746696771 scopus 로고    scopus 로고
    • Functional analysis of the glaucomacausing TIGR/myocilin protein: Integrity of amino-terminal coiled-coil regions and olfactomedin homology domain is essential for extracellular adhesion and secretion
    • Gobeil S, Letartre L, Raymond V (2006) Functional analysis of the glaucomacausing TIGR/myocilin protein: integrity of amino-terminal coiled-coil regions and olfactomedin homology domain is essential for extracellular adhesion and secretion. Exp Eye Res 82: 1017-1029.
    • (2006) Exp Eye Res , vol.82 , pp. 1017-1029
    • Gobeil, S.1    Letartre, L.2    Raymond, V.3
  • 10
    • 33646195309 scopus 로고    scopus 로고
    • Temperature sensitive secretion of mutant myocilins
    • Vollrath D, Liu Y (2006) Temperature sensitive secretion of mutant myocilins. Exp Eye Res 82: 1030-1036.
    • (2006) Exp Eye Res , vol.82 , pp. 1030-1036
    • Vollrath, D.1    Liu, Y.2
  • 11
    • 11244280871 scopus 로고    scopus 로고
    • A synthetic chaperone corrects the trafficking defect and disease phenotype in a protein misfolding disorder
    • Yam GH-F, Zuber C, Roth J (2005) A synthetic chaperone corrects the trafficking defect and disease phenotype in a protein misfolding disorder. FASEB J 19: 12-18.
    • (2005) FASEB J , vol.19 , pp. 12-18
    • Yam, G.H.-F.1    Zuber, C.2    Roth, J.3
  • 12
    • 68349098938 scopus 로고    scopus 로고
    • Correction of the disease phenotype of myocilin-causing glaucoma by a natural osmolyte
    • Jia L-Y, Gong B, Pang C-P, Huang Y, Lam DS-C, et al. (2009) Correction of the disease phenotype of myocilin-causing glaucoma by a natural osmolyte. Invest Ophthalmol Vis Sci 50: 3743-3749.
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 3743-3749
    • Jia, L.-Y.1    Gong, B.2    Pang, C.-P.3    Huang, Y.4    Lam, D.S.-C.5
  • 13
    • 77952847409 scopus 로고    scopus 로고
    • Rescue of glaucoma-causing mutant myocilin thermal stability by chemical chaperones
    • Burns JN, Orwig SD, Harris JL, Watkins JD, Vollrath D, et al. (2010) Rescue of glaucoma-causing mutant myocilin thermal stability by chemical chaperones. ACS Chem Biol 5: 477-487.
    • (2010) ACS Chem Biol , vol.5 , pp. 477-487
    • Burns, J.N.1    Orwig, S.D.2    Harris, J.L.3    Watkins, J.D.4    Vollrath, D.5
  • 14
    • 33646165968 scopus 로고    scopus 로고
    • The identification of myocilinassociated proteins in the human trabecular meshwork
    • Fautsch MP, Vrabel AM, Johnson DH (2006) The identification of myocilinassociated proteins in the human trabecular meshwork. Exp Eye Res 82: 1046-1052.
    • (2006) Exp Eye Res , vol.82 , pp. 1046-1052
    • Fautsch, M.P.1    Vrabel, A.M.2    Johnson, D.H.3
  • 15
    • 12344256073 scopus 로고    scopus 로고
    • Myocilin binding to Hep II domain of fibronectin inhibits cell spreading and incorporation of paxillin into focal adhesions
    • Peters DM, Herbert K, Biddick B, Peterson JA (2005) Myocilin binding to Hep II domain of fibronectin inhibits cell spreading and incorporation of paxillin into focal adhesions. Exp Cell Res 303: 218-228.
    • (2005) Exp Cell Res , vol.303 , pp. 218-228
    • Peters, D.M.1    Herbert, K.2    Biddick, B.3    Peterson, J.A.4
  • 16
    • 58149328927 scopus 로고    scopus 로고
    • Myocilin promotes substrate adhesion, spreading and formation of focal contacts in podocytes and mesangial cells
    • Goldwich A, Scholz M, Tamm ER (2009) Myocilin promotes substrate adhesion, spreading and formation of focal contacts in podocytes and mesangial cells. Histochem Cell Biol 131: 167-180.
    • (2009) Histochem Cell Biol , vol.131 , pp. 167-180
    • Goldwich, A.1    Scholz, M.2    Tamm, E.R.3
  • 17
    • 0032857679 scopus 로고    scopus 로고
    • Identification of the region in the N-terminal domain responsible for the cytoplasmic localization of Myoc/Tigr and its association with microtubules
    • Mertts M, Garfield S, Tanemoto K, Tomarev SI (1999) Identification of the region in the N-terminal domain responsible for the cytoplasmic localization of Myoc/Tigr and its association with microtubules. Lab Invest 79: 1237-1245.
    • (1999) Lab Invest , vol.79 , pp. 1237-1245
    • Mertts, M.1    Garfield, S.2    Tanemoto, K.3    Tomarev, S.I.4
  • 18
    • 34948890141 scopus 로고    scopus 로고
    • Characterization of the intracellular proteolytic cleavage of myocilin and identification of calpain II as a myocilin-processing protease
    • Sanchez-Sanchez F, Martinez-Redondo F, Aroca-Aguilar JD, Coca-Prados M, Escribano J (2007) Characterization of the intracellular proteolytic cleavage of myocilin and identification of calpain II as a myocilin-processing protease. J Biol Chem 282: 27810-27824.
    • (2007) J Biol Chem , vol.282 , pp. 27810-27824
    • Sanchez-Sanchez, F.1    Martinez-Redondo, F.2    Aroca-Aguilar, J.D.3    Coca-Prados, M.4    Escribano, J.5
  • 19
    • 0036023494 scopus 로고    scopus 로고
    • Myocilin and glaucoma: Facts and ideas
    • Tamm ER (2002) Myocilin and glaucoma: facts and ideas. Prog Retin Eye Res 21: 395-428.
    • (2002) Prog Retin Eye Res , vol.21 , pp. 395-428
    • Tamm, E.R.1
  • 20
    • 73049100386 scopus 로고    scopus 로고
    • Olfactomedin domain-containing proteins: Possible mechanisms of action and functions in normal development and pathology
    • Tomarev SI, Nakaya N (2009) Olfactomedin domain-containing proteins: possible mechanisms of action and functions in normal development and pathology. Mol Neurobiol 40: 122-138.
    • (2009) Mol Neurobiol , vol.40 , pp. 122-138
    • Tomarev, S.I.1    Nakaya, N.2
  • 21
    • 64249133695 scopus 로고    scopus 로고
    • The role of proteolytic cellular systems in trabecular meshwork homeostasis
    • Liton PB, Gonzalez P, Epstein DL (2009) The role of proteolytic cellular systems in trabecular meshwork homeostasis. Exp Eye Res 88: 724-728.
    • (2009) Exp Eye Res , vol.88 , pp. 724-728
    • Liton, P.B.1    Gonzalez, P.2    Epstein, D.L.3
  • 22
    • 0030978479 scopus 로고    scopus 로고
    • Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein
    • Ganesh C, Shah AN, Swaminathan CP, Surolia A, Varadarajan R (1997) Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein. Biochemistry 36: 5020-5028.
    • (1997) Biochemistry , vol.36 , pp. 5020-5028
    • Ganesh, C.1    Shah, A.N.2    Swaminathan, C.P.3    Surolia, A.4    Varadarajan, R.5
  • 23
    • 41049089213 scopus 로고    scopus 로고
    • Extracellular matrix in the trabecular meshwork
    • Acott TS, Kelley MJ (2008) Extracellular matrix in the trabecular meshwork. Exp Eye Res 86: 543-561.
    • (2008) Exp Eye Res , vol.86 , pp. 543-561
    • Acott, T.S.1    Kelley, M.J.2
  • 24
    • 18744379471 scopus 로고    scopus 로고
    • Reconstitution of trabecular meshwork GAGs: Influence of hyaluronic acid and chondroitin sulfate on flow rates
    • Knepper PA, Fadel JR, Miller AM, Goossens W, Choi J, et al. (2005) Reconstitution of trabecular meshwork GAGs: influence of hyaluronic acid and chondroitin sulfate on flow rates. J Glaucoma 14: 230-238.
    • (2005) J Glaucoma , vol.14 , pp. 230-238
    • Knepper, P.A.1    Fadel, J.R.2    Miller, A.M.3    Goossens, W.4    Choi, J.5
  • 25
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy Server
    • In: Walker JM, ed, Totowa, NJ: Humana Press
    • Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, et al. (2005) Protein identification and analysis tools on the ExPASy Server. In: Walker JM, ed. The proteomics Protocol Handbook. Totowa, NJ: Humana Press. pp 571-607.
    • (2005) The proteomics Protocol Handbook , pp. 571-607
    • Gasteiger, E.1    Hoogland, C.2    Gattiker, A.3    Duvaud, S.4    Wilkins, M.R.5
  • 26
    • 0037436854 scopus 로고    scopus 로고
    • Expression and characterization of the olfactomedin domain of human myocilin
    • Nagy I, Trexler M, Patthy L (2003) Expression and characterization of the olfactomedin domain of human myocilin. Biochem Biophys Res Commun 302: 554-561.
    • (2003) Biochem Biophys Res Commun , vol.302 , pp. 554-561
    • Nagy, I.1    Trexler, M.2    Patthy, L.3
  • 27
    • 1642486696 scopus 로고    scopus 로고
    • Analysis of circular dichroism data
    • Greenfield NJ (2004) Analysis of circular dichroism data. Methods Enzymol 383: 282-317.
    • (2004) Methods Enzymol , vol.383 , pp. 282-317
    • Greenfield, N.J.1
  • 28
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson AD, Murphy KP (1997) Protein structure and the energetics of protein stability. Chem Rev 97: 1251-1268.
    • (1997) Chem Rev , vol.97 , pp. 1251-1268
    • Robertson, A.D.1    Murphy, K.P.2
  • 29
    • 77957967074 scopus 로고    scopus 로고
    • Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins
    • Pace CN, Huyghues-Despointes BMP, Fu HL, Takano K, Scholtz JM, et al. (2010) Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins. Protein Sci 19: 929-943.
    • (2010) Protein Sci , vol.19 , pp. 929-943
    • Pace, C.N.1    Huyghues-Despointes, B.M.P.2    Fu, H.L.3    Takano, K.4    Scholtz, J.M.5
  • 30
    • 0031932170 scopus 로고    scopus 로고
    • Favorable domain size in proteins
    • Xu D, Nussinov R (1998) Favorable domain size in proteins. Fold Des 3: 11-17.
    • (1998) Fold Des , vol.3 , pp. 11-17
    • Xu, D.1    Nussinov, R.2
  • 31
    • 0026530837 scopus 로고
    • Beta-II conformation of all-beta proteins can be distinguished from unordered form by circular dichroism
    • Wu J, Yang JT, Wu CS (1992) Beta-II conformation of all-beta proteins can be distinguished from unordered form by circular dichroism. Anal Biochem 200: 359-364.
    • (1992) Anal Biochem , vol.200 , pp. 359-364
    • Wu, J.1    Yang, J.T.2    Wu, C.S.3
  • 32
    • 0029951066 scopus 로고    scopus 로고
    • Glycosaminoglycans of the human trabecular meshwork in primary open-angle glaucoma
    • Knepper PA, Goossens W, Hvizd M, Palmberg PF (1996) Glycosaminoglycans of the human trabecular meshwork in primary open-angle glaucoma. Invest Ophthalmol Vis Sci 37: 1360-1367.
    • (1996) Invest Ophthalmol Vis Sci , vol.37 , pp. 1360-1367
    • Knepper, P.A.1    Goossens, W.2    Hvizd, M.3    Palmberg, P.F.4
  • 33
    • 34548258678 scopus 로고    scopus 로고
    • Glycosaminoglycans of the trabecular meshwork of the eye in primary juvenile glaucoma
    • Kuleshova ON, Zaidman AM, Korel AV (2007) Glycosaminoglycans of the trabecular meshwork of the eye in primary juvenile glaucoma. Bull Exp Biol Med 143: 381-384.
    • (2007) Bull Exp Biol Med , vol.143 , pp. 381-384
    • Kuleshova, O.N.1    Zaidman, A.M.2    Korel, A.V.3
  • 36
    • 23644437177 scopus 로고    scopus 로고
    • Identification and characterization of photomedins: Novel olfactomedin-domaincontaining proteins with chondroitin sulphate-E-binding activity
    • Furutani Y, Manabe R, Tsutsui K, Yamada T, Sugimoto N, et al. (2005) Identification and characterization of photomedins: novel olfactomedin-domaincontaining proteins with chondroitin sulphate-E-binding activity. Biochem J 389: 675-684.
    • (2005) Biochem J , vol.389 , pp. 675-684
    • Furutani, Y.1    Manabe, R.2    Tsutsui, K.3    Yamada, T.4    Sugimoto, N.5
  • 37
    • 35948954725 scopus 로고    scopus 로고
    • Structural features and functional domains of amassin-1, a cell-binding olfactomedin protein
    • Hillier BJ, Vacquier VD (2007) Structural features and functional domains of amassin-1, a cell-binding olfactomedin protein. Biochem Cell Biol 85: 552-562.
    • (2007) Biochem Cell Biol , vol.85 , pp. 552-562
    • Hillier, B.J.1    Vacquier, V.D.2
  • 38
    • 0344921403 scopus 로고    scopus 로고
    • Stability, homodimerization, and calcium-binding properties of a single, variant betagamma-crystallin domain of the protein absent in melanoma 1 (AIM1)
    • Rajini B, Graham C, Wistow G, Sharma Y (2003) Stability, homodimerization, and calcium-binding properties of a single, variant betagamma-crystallin domain of the protein absent in melanoma 1 (AIM1). Biochemistry 42: 4552-4559.
    • (2003) Biochemistry , vol.42 , pp. 4552-4559
    • Rajini, B.1    Graham, C.2    Wistow, G.3    Sharma, Y.4
  • 40
    • 0016307277 scopus 로고
    • A comparison of the circular dichroism spectra of the subclasses of human immunoglobulin G
    • Johnson PM, Scopes PM, Tracey BM, Watkins J (1974) A comparison of the circular dichroism spectra of the subclasses of human immunoglobulin G. Immunology 27: 27-31.
    • (1974) Immunology , vol.27 , pp. 27-31
    • Johnson, P.M.1    Scopes, P.M.2    Tracey, B.M.3    Watkins, J.4
  • 41
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • Brahms S, Brahms J (1980) Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J Mol Biol 138: 149-178.
    • (1980) J Mol Biol , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 42
    • 18844414326 scopus 로고    scopus 로고
    • High accuracy prediction of beta-turns and their types using propensities and multiple alignments
    • Fuchs PF, Alix AJ (2005) High accuracy prediction of beta-turns and their types using propensities and multiple alignments. Proteins 59: 828-839.
    • (2005) Proteins , vol.59 , pp. 828-839
    • Fuchs, P.F.1    Alix, A.J.2
  • 43
    • 0015244842 scopus 로고
    • Active site spin-labeled alpha-chymotrypsin. Guanidine hydrochloride denaturation studies using electron paramagnetic resonance and circular dichroism
    • Morrisett JD, Broomfield CA (1971) Active site spin-labeled alpha-chymotrypsin. Guanidine hydrochloride denaturation studies using electron paramagnetic resonance and circular dichroism. J Am Chem Soc 93: 7297-7304.
    • (1971) J Am Chem Soc , vol.93 , pp. 7297-7304
    • Morrisett, J.D.1    Broomfield, C.A.2
  • 44
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding R, Russell RB, Neduva V, Gibson TJ (2003) GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res 31: 3701-3708.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 46
    • 34247096110 scopus 로고    scopus 로고
    • A reference dataset for circular dichroism spectroscopy tailored for the betagamma-crystallin lens proteins
    • Evans P, Bateman OA, Slingsby C, Wallace BA (2007) A reference dataset for circular dichroism spectroscopy tailored for the betagamma-crystallin lens proteins. Exp Eye Res 84: 1001-1008.
    • (2007) Exp Eye Res , vol.84 , pp. 1001-1008
    • Evans, P.1    Bateman, O.A.2    Slingsby, C.3    Wallace, B.A.4
  • 47
    • 0023655016 scopus 로고
    • Structure and stability of gamma-crystallins. Denaturation and proteolysis behavior
    • Mandal K, Chakrabarti B, Thomson J, Siezen RJ (1987) Structure and stability of gamma-crystallins. Denaturation and proteolysis behavior. J Biol Chem 262: 8096-8102.
    • (1987) J Biol Chem , vol.262 , pp. 8096-8102
    • Mandal, K.1    Chakrabarti, B.2    Thomson, J.3    Siezen, R.J.4
  • 48
    • 33745167938 scopus 로고    scopus 로고
    • Protein-misfolding diseases and chaperone-based therapeutic approaches
    • Chaudhuri TK, Paul S (2006) Protein-misfolding diseases and chaperone-based therapeutic approaches. FEBS J 273: 1331-1349.
    • (2006) FEBS J , vol.273 , pp. 1331-1349
    • Chaudhuri, T.K.1    Paul, S.2
  • 51
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen FH, Berglund H, Vedadi M (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2: 2212-2221.
    • (2007) Nat Protoc , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 52
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Analytical Chemistry 68: 850-858.
    • (1996) Analytical Chemistry , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 53
    • 34248532415 scopus 로고    scopus 로고
    • PROMALS: Towards accurate multiple sequence alignments of distantly related proteins
    • Pei J, Grishin NV (2007) PROMALS: towards accurate multiple sequence alignments of distantly related proteins. Bioinformatics 23: 802-808.
    • (2007) Bioinformatics , vol.23 , pp. 802-808
    • Pei, J.1    Grishin, N.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.