메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

1-Anilino-8-Naphthalene Sulfonate (ANS) Is Not a Desirable Probe for Determining the Molten Globule State of Chymopapain

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACRYLAMIDE; CHYMOPAPAIN; TRYPTOPHAN;

EID: 84870556608     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050633     Document Type: Article
Times cited : (41)

References (52)
  • 1
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima K, (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6: 87-103.
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 2
    • 0030473296 scopus 로고    scopus 로고
    • Kinetic intermediates in the formation of the cytochrome c molten globule
    • Colon W, Roder H, (1996) Kinetic intermediates in the formation of the cytochrome c molten globule. Nat Struct Biol 3: 1019-1025.
    • (1996) Nat Struct Biol , vol.3 , pp. 1019-1025
    • Colon, W.1    Roder, H.2
  • 3
    • 21144446625 scopus 로고    scopus 로고
    • Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins
    • Mok KH, Nagashima T, Day IJ, Hore PJ, Dobson CM, (2005) Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins. Proc Natl Acad Sci U S A 102: 8899-8904.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8899-8904
    • Mok, K.H.1    Nagashima, T.2    Day, I.J.3    Hore, P.J.4    Dobson, C.M.5
  • 4
    • 33344473937 scopus 로고    scopus 로고
    • The denatured state under native conditions: a non-native-like collapsed state of N-PGK
    • Reed MA, Jelinska C, Syson K, Cliff MJ, Splevins A, et al. (2006) The denatured state under native conditions: a non-native-like collapsed state of N-PGK. J Mol Biol 357: 365-372.
    • (2006) J Mol Biol , vol.357 , pp. 365-372
    • Reed, M.A.1    Jelinska, C.2    Syson, K.3    Cliff, M.J.4    Splevins, A.5
  • 5
    • 79959326174 scopus 로고    scopus 로고
    • Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion
    • Meinhold DW, Wright PE, (2011) Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion. Proc Natl Acad Sci U S A 108: 9078-9083.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9078-9083
    • Meinhold, D.W.1    Wright, P.E.2
  • 6
    • 79958852717 scopus 로고    scopus 로고
    • Conformational folding and stability of the HET-C2 glycolipid transfer protein fold: does a molten globule-like state regulate activity?
    • Kenoth R, Kamlekar RK, Simanshu DK, Gao Y, Malinina L, et al. (2011) Conformational folding and stability of the HET-C2 glycolipid transfer protein fold: does a molten globule-like state regulate activity? Biochemistry 50: 5163-5171.
    • (2011) Biochemistry , vol.50 , pp. 5163-5171
    • Kenoth, R.1    Kamlekar, R.K.2    Simanshu, D.K.3    Gao, Y.4    Malinina, L.5
  • 7
    • 84864643787 scopus 로고    scopus 로고
    • Characterization of molten globule PopB in absence and presence of its chaperone PcrH
    • Dey S, Basu A, Datta S, (2012) Characterization of molten globule PopB in absence and presence of its chaperone PcrH. Protein J 31: 401-416.
    • (2012) Protein J , vol.31 , pp. 401-416
    • Dey, S.1    Basu, A.2    Datta, S.3
  • 8
    • 84861904641 scopus 로고    scopus 로고
    • A functional loop spanning distant domains of glutaminyl-tRNA synthetase also stabilizes a molten globule state
    • Saha R, Dasgupta S, Banerjee R, Mitra-Bhattacharyya A, Soll D, et al. (2012) A functional loop spanning distant domains of glutaminyl-tRNA synthetase also stabilizes a molten globule state. Biochemistry 51: 4429-4437.
    • (2012) Biochemistry , vol.51 , pp. 4429-4437
    • Saha, R.1    Dasgupta, S.2    Banerjee, R.3    Mitra-Bhattacharyya, A.4    Soll, D.5
  • 9
    • 0036153595 scopus 로고    scopus 로고
    • Characterization of a partially folded intermediate of stem bromelain at low pH
    • Haq SK, Rasheedi S, Khan RH, (2002) Characterization of a partially folded intermediate of stem bromelain at low pH. Eur J Biochem 269: 47-52.
    • (2002) Eur J Biochem , vol.269 , pp. 47-52
    • Haq, S.K.1    Rasheedi, S.2    Khan, R.H.3
  • 10
    • 51849098535 scopus 로고    scopus 로고
    • Formation of a molten globule like state in bovine serum albumin at alkaline pH
    • Sen P, Ahmad B, Khan RH, (2008) Formation of a molten globule like state in bovine serum albumin at alkaline pH. Eur Biophys J 37: 1303-1308.
    • (2008) Eur Biophys J , vol.37 , pp. 1303-1308
    • Sen, P.1    Ahmad, B.2    Khan, R.H.3
  • 11
    • 34447549197 scopus 로고    scopus 로고
    • Studies of the molten globule state of ferredoxin: structural characterization and implications on protein folding and iron-sulfur center assembly
    • Leal SS, Gomes CM, (2007) Studies of the molten globule state of ferredoxin: structural characterization and implications on protein folding and iron-sulfur center assembly. Proteins 68: 606-616.
    • (2007) Proteins , vol.68 , pp. 606-616
    • Leal, S.S.1    Gomes, C.M.2
  • 12
    • 0034283781 scopus 로고    scopus 로고
    • Hydrogen exchange study of canine milk lysozyme: stabilization mechanism of the molten globule
    • Kobashigawa Y, Demura M, Koshiba T, Kumaki Y, Kuwajima K, et al. (2000) Hydrogen exchange study of canine milk lysozyme: stabilization mechanism of the molten globule. Proteins 40: 579-589.
    • (2000) Proteins , vol.40 , pp. 579-589
    • Kobashigawa, Y.1    Demura, M.2    Koshiba, T.3    Kumaki, Y.4    Kuwajima, K.5
  • 13
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB, (1995) Molten globule and protein folding. Adv Protein Chem 47: 83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 14
    • 0034612339 scopus 로고    scopus 로고
    • Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA
    • Schonbrunn E, Eschenburg S, Luger K, Kabsch W, Amrhein N, (2000) Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc Natl Acad Sci U S A 97: 6345-6349.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6345-6349
    • Schonbrunn, E.1    Eschenburg, S.2    Luger, K.3    Kabsch, W.4    Amrhein, N.5
  • 15
    • 67651033247 scopus 로고    scopus 로고
    • Characterization of acid-induced molten globule like state of ficin
    • Devaraj KB, Kumar PR, Prakash V, (2009) Characterization of acid-induced molten globule like state of ficin. Int J Biol Macromol 45: 248-254.
    • (2009) Int J Biol Macromol , vol.45 , pp. 248-254
    • Devaraj, K.B.1    Kumar, P.R.2    Prakash, V.3
  • 16
    • 77953543617 scopus 로고    scopus 로고
    • More stable structure of wheat germ lipase at low pH than its native state
    • Ahmad E, Fatima S, Khan MM, Khan RH, (2010) More stable structure of wheat germ lipase at low pH than its native state. Biochimie 92: 885-893.
    • (2010) Biochimie , vol.92 , pp. 885-893
    • Ahmad, E.1    Fatima, S.2    Khan, M.M.3    Khan, R.H.4
  • 17
    • 65349090914 scopus 로고    scopus 로고
    • Conformational stability and multistate unfolding of poly(A)-specific ribonuclease
    • He GJ, Zhang A, Liu WF, Cheng Y, Yan YB, (2009) Conformational stability and multistate unfolding of poly(A)-specific ribonuclease. FEBS J 276: 2849-2860.
    • (2009) FEBS J , vol.276 , pp. 2849-2860
    • He, G.J.1    Zhang, A.2    Liu, W.F.3    Cheng, Y.4    Yan, Y.B.5
  • 18
    • 79961026029 scopus 로고    scopus 로고
    • Equilibrium unfolding of A. niger RNase: pH dependence of chemical and thermal denaturation
    • Kumar GR, Sharma A, Kumari M, Jagannadham MV, Debnath M, (2011) Equilibrium unfolding of A. niger RNase: pH dependence of chemical and thermal denaturation. Eur Biophys J 40: 923-935.
    • (2011) Eur Biophys J , vol.40 , pp. 923-935
    • Kumar, G.R.1    Sharma, A.2    Kumari, M.3    Jagannadham, M.V.4    Debnath, M.5
  • 19
    • 79951514955 scopus 로고    scopus 로고
    • Pea lectin unfolding reveals a unique molten globule fragment chain
    • Sen D, Mandal DK, (2011) Pea lectin unfolding reveals a unique molten globule fragment chain. Biochimie 93: 409-417.
    • (2011) Biochimie , vol.93 , pp. 409-417
    • Sen, D.1    Mandal, D.K.2
  • 20
    • 84863241639 scopus 로고    scopus 로고
    • A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin
    • Tseng TS, Cheng CS, Chen DJ, Shih MF, Liu YN, et al. (2012) A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin. Biochem J 442: 563-572.
    • (2012) Biochem J , vol.442 , pp. 563-572
    • Tseng, T.S.1    Cheng, C.S.2    Chen, D.J.3    Shih, M.F.4    Liu, Y.N.5
  • 21
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer L, (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J Mol Biol 13: 482-495.
    • (1965) J Mol Biol , vol.13 , pp. 482-495
    • Stryer, L.1
  • 22
    • 0030070010 scopus 로고    scopus 로고
    • Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1′)anilinonaphthalene binding to intestinal fatty acid binding protein
    • Kirk WR, Kurian E, Prendergast FG, (1996) Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1′)anilinonaphthalene binding to intestinal fatty acid binding protein. Biophys J 70: 69-83.
    • (1996) Biophys J , vol.70 , pp. 69-83
    • Kirk, W.R.1    Kurian, E.2    Prendergast, F.G.3
  • 23
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis D, Lovrien R, (1998) 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys J 74: 422-429.
    • (1998) Biophys J , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 24
    • 33847659962 scopus 로고    scopus 로고
    • ANS fluorescence: potential to augment the identification of the external binding sites of proteins
    • Gasymov OK, Glasgow BJ, (2007) ANS fluorescence: potential to augment the identification of the external binding sites of proteins. Biochim Biophys Acta 1774: 403-411.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 403-411
    • Gasymov, O.K.1    Glasgow, B.J.2
  • 25
    • 2542479281 scopus 로고    scopus 로고
    • Low concentration of guanidine hydrochloride induces the formation of an aggregation-prone state in alpha-urease
    • McDuff FO, Doucet A, Beauregard M, (2004) Low concentration of guanidine hydrochloride induces the formation of an aggregation-prone state in alpha-urease. Biochem Cell Biol 82: 305-313.
    • (2004) Biochem Cell Biol , vol.82 , pp. 305-313
    • McDuff, F.O.1    Doucet, A.2    Beauregard, M.3
  • 26
    • 78649778065 scopus 로고    scopus 로고
    • Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates
    • Povarova OI, Kuznetsova IM, Turoverov KK, (2010) Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates. PLoS One 5: e15035.
    • (2010) PLoS One , vol.5
    • Povarova, O.I.1    Kuznetsova, I.M.2    Turoverov, K.K.3
  • 28
    • 0025008745 scopus 로고
    • The amino acid sequence of chymopapain from Carica papaya
    • Watson DC, Yaguchi M, Lynn KR, (1990) The amino acid sequence of chymopapain from Carica papaya. Biochem J 266: 75-81.
    • (1990) Biochem J , vol.266 , pp. 75-81
    • Watson, D.C.1    Yaguchi, M.2    Lynn, K.R.3
  • 29
    • 0017846050 scopus 로고
    • The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis
    • Carne A, Moore CH, (1978) The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis. Biochem J 173: 73-83.
    • (1978) Biochem J , vol.173 , pp. 73-83
    • Carne, A.1    Moore, C.H.2
  • 30
    • 0024551586 scopus 로고
    • Stem bromelain: amino acid sequence and implications for weak binding of cystatin
    • Ritonja A, Rowan AD, Buttle DJ, Rawlings ND, Turk V, et al. (1989) Stem bromelain: amino acid sequence and implications for weak binding of cystatin. FEBS Lett 247: 419-424.
    • (1989) FEBS Lett , vol.247 , pp. 419-424
    • Ritonja, A.1    Rowan, A.D.2    Buttle, D.J.3    Rawlings, N.D.4    Turk, V.5
  • 31
    • 0032573356 scopus 로고    scopus 로고
    • Sequential unfolding of papain in molten globule state
    • Edwin F, Jagannadham MV, (1998) Sequential unfolding of papain in molten globule state. Biochem Biophys Res Commun 252: 654-660.
    • (1998) Biochem Biophys Res Commun , vol.252 , pp. 654-660
    • Edwin, F.1    Jagannadham, M.V.2
  • 32
    • 7044228278 scopus 로고    scopus 로고
    • Characterization of a partially folded intermediate of papain induced by fluorinated alcohols at low pH
    • Naeem A, Khan KA, Khan RH, (2004) Characterization of a partially folded intermediate of papain induced by fluorinated alcohols at low pH. Arch Biochem Biophys 432: 79-87.
    • (2004) Arch Biochem Biophys , vol.432 , pp. 79-87
    • Naeem, A.1    Khan, K.A.2    Khan, R.H.3
  • 33
    • 43049119004 scopus 로고    scopus 로고
    • Mechanism for stabilization of the molten globule state of papain by sodium n-alkyl sulfates: spectroscopic and calorimetric approaches
    • Chamani J, Heshmati M, (2008) Mechanism for stabilization of the molten globule state of papain by sodium n-alkyl sulfates: spectroscopic and calorimetric approaches. J Colloid Interface Sci 322: 119-127.
    • (2008) J Colloid Interface Sci , vol.322 , pp. 119-127
    • Chamani, J.1    Heshmati, M.2
  • 35
    • 38449098568 scopus 로고    scopus 로고
    • Effect of polyethylene glycols on the function and structure of thiol proteases
    • Fatima S, Khan RH, (2007) Effect of polyethylene glycols on the function and structure of thiol proteases. J Biochem 142: 65-72.
    • (2007) J Biochem , vol.142 , pp. 65-72
    • Fatima, S.1    Khan, R.H.2
  • 36
    • 33845312248 scopus 로고    scopus 로고
    • Studies on the acid unfolded and molten globule states of catalytically active stem bromelain: a comparison with catalytically inactive form
    • Ahmad B, Khan RH, (2006) Studies on the acid unfolded and molten globule states of catalytically active stem bromelain: a comparison with catalytically inactive form. J Biochem 140: 501-508.
    • (2006) J Biochem , vol.140 , pp. 501-508
    • Ahmad, B.1    Khan, R.H.2
  • 37
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen YH, Yang JT, Martinez HM, (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11: 4120-4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 38
    • 80355136403 scopus 로고    scopus 로고
    • Stereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry and bioinformatics
    • Ahmad E, Rabbani G, Zaidi N, Singh S, Rehan M, et al. (2011) Stereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry and bioinformatics. PLoS One 6: e26186.
    • (2011) PLoS One , vol.6
    • Ahmad, E.1    Rabbani, G.2    Zaidi, N.3    Singh, S.4    Rehan, M.5
  • 39
    • 29144535272 scopus 로고    scopus 로고
    • 2,2,2-trifluoroethanol-induced molten globule state of concanavalin A and energetics of 8-anilinonaphthalene sulfonate binding: calorimetric and spectroscopic investigation
    • Banerjee T, Kishore N, (2005) 2,2,2-trifluoroethanol-induced molten globule state of concanavalin A and energetics of 8-anilinonaphthalene sulfonate binding: calorimetric and spectroscopic investigation. J Phys Chem B 109: 22655-22662.
    • (2005) J Phys Chem B , vol.109 , pp. 22655-22662
    • Banerjee, T.1    Kishore, N.2
  • 40
    • 33749356802 scopus 로고    scopus 로고
    • Elucidating the binding thermodynamics of 8-anilino-1-naphthalene sulfonic acid with the A-state of alpha-lactalbumin: an isothermal titration calorimetric investigation
    • Singh SK, Kishore N, (2006) Elucidating the binding thermodynamics of 8-anilino-1-naphthalene sulfonic acid with the A-state of alpha-lactalbumin: an isothermal titration calorimetric investigation. Biopolymers 83: 205-212.
    • (2006) Biopolymers , vol.83 , pp. 205-212
    • Singh, S.K.1    Kishore, N.2
  • 42
    • 0023659224 scopus 로고
    • Does the fluorescence quencher acrylamide bind to proteins?
    • Eftink MR, Ghiron CA, (1987) Does the fluorescence quencher acrylamide bind to proteins? Biochim Biophys Acta 916: 343-349.
    • (1987) Biochim Biophys Acta , vol.916 , pp. 343-349
    • Eftink, M.R.1    Ghiron, C.A.2
  • 43
    • 79955642720 scopus 로고    scopus 로고
    • The client protein p53 adopts a molten globule-like state in the presence of Hsp90
    • Park SJ, Borin BN, Martinez-Yamout MA, Dyson HJ, (2011) The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nat Struct Mol Biol 18: 537-541.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 537-541
    • Park, S.J.1    Borin, B.N.2    Martinez-Yamout, M.A.3    Dyson, H.J.4
  • 44
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: intermediates and unfolded states
    • Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR, (1994) Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry 33: 12504-12511.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 45
    • 0037203848 scopus 로고    scopus 로고
    • Native-like secondary structure of molten globules
    • Vassilenko KS, Uversky VN, (2002) Native-like secondary structure of molten globules. Biochim Biophys Acta 1594: 168-177.
    • (2002) Biochim Biophys Acta , vol.1594 , pp. 168-177
    • Vassilenko, K.S.1    Uversky, V.N.2
  • 46
    • 31444450716 scopus 로고    scopus 로고
    • Histidine aromatic interactions in proteins and protein-ligand complexes: quantum chemical study of X-ray and model structures
    • Cauët E, Rooman M, Wintjens R, Lièvin J, Biot C, (2005) Histidine aromatic interactions in proteins and protein-ligand complexes: quantum chemical study of X-ray and model structures. J Chem Theory Comput 1: 472-483.
    • (2005) J Chem Theory Comput , vol.1 , pp. 472-483
    • Cauët, E.1    Rooman, M.2    Wintjens, R.3    Lièvin, J.4    Biot, C.5
  • 48
    • 58149204226 scopus 로고    scopus 로고
    • Thermodynamic insight into the binding of ANS with salt induced molten globule state of cytochrome c
    • Sharma R, Kishore N, (2009) Thermodynamic insight into the binding of ANS with salt induced molten globule state of cytochrome c. J Chem Thermodyn 41: 342-348.
    • (2009) J Chem Thermodyn , vol.41 , pp. 342-348
    • Sharma, R.1    Kishore, N.2
  • 49
    • 36248995759 scopus 로고    scopus 로고
    • Characterization of fluorescence of ANS-tear lipocalin complex: evidence for multiple-binding modes
    • Gasymov OK, Abduragimov AR, Glasgow BJ, (2007) Characterization of fluorescence of ANS-tear lipocalin complex: evidence for multiple-binding modes. Photochem Photobiol 83: 1405-1414.
    • (2007) Photochem Photobiol , vol.83 , pp. 1405-1414
    • Gasymov, O.K.1    Abduragimov, A.R.2    Glasgow, B.J.3
  • 50
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • Ross PD, Subramanian S, (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20: 3096-3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 51
    • 4444330121 scopus 로고    scopus 로고
    • Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure
    • Manning M, Colon W, (2004) Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure. Biochemistry 43: 11248-11254.
    • (2004) Biochemistry , vol.43 , pp. 11248-11254
    • Manning, M.1    Colon, W.2
  • 52
    • 33748349224 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in initiation and propagation of protein folding
    • Dyson HJ, Wright PE, Scheraga HA, (2006) The role of hydrophobic interactions in initiation and propagation of protein folding. Proc Natl Acad Sci U S A 103: 13057-13061.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 13057-13061
    • Dyson, H.J.1    Wright, P.E.2    Scheraga, H.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.