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Volumn 131, Issue 3, 2007, Pages 223-230

Protein expression from synthetic genes: Selection of clones using GFP

Author keywords

Expression; GFP; Mutation; Synthetic gene

Indexed keywords

CLONING; DNA; NUCLEOTIDES; OPTIMIZATION; PROTEINS;

EID: 34548382206     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.07.725     Document Type: Article
Times cited : (10)

References (58)
  • 1
    • 0032499868 scopus 로고    scopus 로고
    • Gene synthesis by a LCR-based approach: high-level production of leptin-L54 using synthetic gene in Escherichia coli
    • Au L.C., Yang F.Y., Yang W.J., Lo S.H., and Kao C.F. Gene synthesis by a LCR-based approach: high-level production of leptin-L54 using synthetic gene in Escherichia coli. Biochem. Biophys. Res. Commun. 248 (1998) 200-203
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 200-203
    • Au, L.C.1    Yang, F.Y.2    Yang, W.J.3    Lo, S.H.4    Kao, C.F.5
  • 2
    • 0032810904 scopus 로고    scopus 로고
    • Overexpression of a designed 2.2 kb gene of eukaryotic phenylalanine ammonia-lyase in Escherichia coli
    • Baedeker M., and Schulz G.E. Overexpression of a designed 2.2 kb gene of eukaryotic phenylalanine ammonia-lyase in Escherichia coli. FEBS Lett. 457 (1999) 57-60
    • (1999) FEBS Lett. , vol.457 , pp. 57-60
    • Baedeker, M.1    Schulz, G.E.2
  • 3
    • 0036612858 scopus 로고    scopus 로고
    • Synthesis and bacterial expression of a gene encoding the heme domain of assimilatory nitrate reductase
    • Barber M.J., Desai S.K., Marohnic C.C., Hernandez H.H., and Pollock V.V. Synthesis and bacterial expression of a gene encoding the heme domain of assimilatory nitrate reductase. Arch. Biochem. Biophys. 402 (2002) 38-50
    • (2002) Arch. Biochem. Biophys. , vol.402 , pp. 38-50
    • Barber, M.J.1    Desai, S.K.2    Marohnic, C.C.3    Hernandez, H.H.4    Pollock, V.V.5
  • 4
    • 0025166071 scopus 로고
    • Inhibition by dopamine of (Na(+)+K+)ATPase activity in neostriatal neurons through D1 and D2 dopamine receptor synergism
    • Bertorello A.M., Hopfield J.F., Aperia A., and Greengard P. Inhibition by dopamine of (Na(+)+K+)ATPase activity in neostriatal neurons through D1 and D2 dopamine receptor synergism. Nature 347 (1990) 386-388
    • (1990) Nature , vol.347 , pp. 386-388
    • Bertorello, A.M.1    Hopfield, J.F.2    Aperia, A.3    Greengard, P.4
  • 6
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell R.C., and Joyce G.F. Randomization of genes by PCR mutagenesis. PCR Methods Appl. 2 (1992) 28-33
    • (1992) PCR Methods Appl. , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 8
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., and Prasher D.C. Green fluorescent protein as a marker for gene expression. Science 263 (1994) 802-805
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 9
    • 0034792333 scopus 로고    scopus 로고
    • Synthetic gene technology: applications to ancestral gene reconstruction and structure-function studies of receptors
    • Chang B.S., Kazmi M.A., and Sakmar T.P. Synthetic gene technology: applications to ancestral gene reconstruction and structure-function studies of receptors. Methods Enzymol. 343 (2002) 274-294
    • (2002) Methods Enzymol. , vol.343 , pp. 274-294
    • Chang, B.S.1    Kazmi, M.A.2    Sakmar, T.P.3
  • 10
    • 33244490497 scopus 로고    scopus 로고
    • Codon optimization of Candida rugosa lip1 gene for improving expression in Pichia pastoris and biochemical characterization of the purified recombinant LIP1 lipase
    • Chang S.W., Lee G.C., and Shaw J.F. Codon optimization of Candida rugosa lip1 gene for improving expression in Pichia pastoris and biochemical characterization of the purified recombinant LIP1 lipase. J. Agric. Food Chem. 54 (2006) 815-822
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 815-822
    • Chang, S.W.1    Lee, G.C.2    Shaw, J.F.3
  • 11
    • 32644478232 scopus 로고    scopus 로고
    • Enhanced soluble protein expression using two new fusion tags
    • Chatterjee D.K., and Esposito D. Enhanced soluble protein expression using two new fusion tags. Protein Expr. Purif. 46 (2006) 122-129
    • (2006) Protein Expr. Purif. , vol.46 , pp. 122-129
    • Chatterjee, D.K.1    Esposito, D.2
  • 12
    • 0033936027 scopus 로고    scopus 로고
    • High-level expression of active HIV-1 integrase from a synthetic gene in human cells
    • Cherepanov P., Pluymers W., Claeys A., Proost P., De Clercq E., and Debyser Z. High-level expression of active HIV-1 integrase from a synthetic gene in human cells. Faseb J. 14 (2000) 1389-1399
    • (2000) Faseb J. , vol.14 , pp. 1389-1399
    • Cherepanov, P.1    Pluymers, W.2    Claeys, A.3    Proost, P.4    De Clercq, E.5    Debyser, Z.6
  • 14
    • 0020649604 scopus 로고
    • The tac promoter: a functional hybrid derived from the trp and lac promoters
    • de Boer H.A., Comstock L.J., and Vasser M. The tac promoter: a functional hybrid derived from the trp and lac promoters. Proc. Natl. Acad. Sci. USA 80 (1983) 21-25
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 21-25
    • de Boer, H.A.1    Comstock, L.J.2    Vasser, M.3
  • 17
    • 0027213871 scopus 로고
    • A method for synthesizing genes and cDNAs by the polymerase chain reaction
    • Di Donato A., de Nigris M., Russo N., Di Biase S., and D'Alessio G. A method for synthesizing genes and cDNAs by the polymerase chain reaction. Anal. Biochem. 212 (1993) 291-293
    • (1993) Anal. Biochem. , vol.212 , pp. 291-293
    • Di Donato, A.1    de Nigris, M.2    Russo, N.3    Di Biase, S.4    D'Alessio, G.5
  • 18
    • 0024995923 scopus 로고
    • A rapid method for the construction of synthetic genes using the polymerase chain reaction
    • Dillon P.J., and Rosen C.A. A rapid method for the construction of synthetic genes using the polymerase chain reaction. Biotechniques 9 298 (1990) 300
    • (1990) Biotechniques , vol.9 , Issue.298 , pp. 300
    • Dillon, P.J.1    Rosen, C.A.2
  • 19
    • 13244265563 scopus 로고    scopus 로고
    • Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression
    • Dyson M.R., Shadbolt S.P., Vincent K.J., Perera R.L., and McCafferty J. Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression. BMC Biotechnol. 4 (2004) 32
    • (2004) BMC Biotechnol. , vol.4 , pp. 32
    • Dyson, M.R.1    Shadbolt, S.P.2    Vincent, K.J.3    Perera, R.L.4    McCafferty, J.5
  • 20
    • 0034687723 scopus 로고    scopus 로고
    • High-level expression and mutagenesis of recombinant human phosphatidylcholine transfer protein using a synthetic gene: evidence for a C-terminal membrane binding domain
    • Feng L., Chan W.W., Roderick S.L., and Cohen D.E. High-level expression and mutagenesis of recombinant human phosphatidylcholine transfer protein using a synthetic gene: evidence for a C-terminal membrane binding domain. Biochemistry 39 (2000) 15399-15409
    • (2000) Biochemistry , vol.39 , pp. 15399-15409
    • Feng, L.1    Chan, W.W.2    Roderick, S.L.3    Cohen, D.E.4
  • 21
    • 0343471377 scopus 로고    scopus 로고
    • Modification of a PCR-based site-directed mutagenesis method
    • Fisher C.L., and Pei G.K. Modification of a PCR-based site-directed mutagenesis method. Biotechniques 23 570/571 (1997) 574
    • (1997) Biotechniques , vol.23 , Issue.570-571 , pp. 574
    • Fisher, C.L.1    Pei, G.K.2
  • 23
    • 0014323182 scopus 로고
    • Studies on polynucleotides, 88. Enzymatic joining of chemically synthesized segments corresponding to the gene for alanine-Trna
    • Gupta N.K., Ohtsuka E., Sgaramella V., Buchi H., Kumar A., Weber H., and Khorana H.G. Studies on polynucleotides, 88. Enzymatic joining of chemically synthesized segments corresponding to the gene for alanine-Trna. Proc. Natl. Acad. Sci. USA 60 (1968) 1338-1344
    • (1968) Proc. Natl. Acad. Sci. USA , vol.60 , pp. 1338-1344
    • Gupta, N.K.1    Ohtsuka, E.2    Sgaramella, V.3    Buchi, H.4    Kumar, A.5    Weber, H.6    Khorana, H.G.7
  • 24
    • 0037855845 scopus 로고    scopus 로고
    • Expression in Pichia pastoris and purification of a membrane-acting immunotoxin based on a synthetic gene coding for the Bacillus thuringiensis Cyt2Aa1 toxin
    • Gurkan C., and Ellar D.J. Expression in Pichia pastoris and purification of a membrane-acting immunotoxin based on a synthetic gene coding for the Bacillus thuringiensis Cyt2Aa1 toxin. Protein Expr. Purif. 29 (2003) 103-116
    • (2003) Protein Expr. Purif. , vol.29 , pp. 103-116
    • Gurkan, C.1    Ellar, D.J.2
  • 25
    • 0041589240 scopus 로고    scopus 로고
    • Expression of the Bacillus thuringiensis Cyt2Aa1 toxin in Pichia pastoris using a synthetic gene construct
    • Gurkan C., and Ellar D.J. Expression of the Bacillus thuringiensis Cyt2Aa1 toxin in Pichia pastoris using a synthetic gene construct. Biotechnol. Appl. Biochem. 38 (2003) 25-33
    • (2003) Biotechnol. Appl. Biochem. , vol.38 , pp. 25-33
    • Gurkan, C.1    Ellar, D.J.2
  • 26
    • 0032030138 scopus 로고    scopus 로고
    • Codon optimization of the gene encoding a domain from human type 1 neurofibromin protein results in a threefold improvement in expression level in Escherichia coli
    • Hale R.S., and Thompson G. Codon optimization of the gene encoding a domain from human type 1 neurofibromin protein results in a threefold improvement in expression level in Escherichia coli. Protein Expr. Purif. 12 (1998) 185-188
    • (1998) Protein Expr. Purif. , vol.12 , pp. 185-188
    • Hale, R.S.1    Thompson, G.2
  • 27
    • 0037095730 scopus 로고    scopus 로고
    • DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis
    • Hoover D.M., and Lubkowski J. DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis. Nucleic Acids Res. 30 (2002) e43
    • (2002) Nucleic Acids Res. , vol.30
    • Hoover, D.M.1    Lubkowski, J.2
  • 28
    • 33646089874 scopus 로고    scopus 로고
    • Codon optimization, expression, and characterization of an internalizing anti-ErbB2 single-chain antibody in Pichia pastoris
    • Hu S., Li L., Qiao J., Guo Y., Cheng L., and Liu J. Codon optimization, expression, and characterization of an internalizing anti-ErbB2 single-chain antibody in Pichia pastoris. Protein Expr. Purif. 47 (2006) 249-257
    • (2006) Protein Expr. Purif. , vol.47 , pp. 249-257
    • Hu, S.1    Li, L.2    Qiao, J.3    Guo, Y.4    Cheng, L.5    Liu, J.6
  • 29
    • 5344243810 scopus 로고    scopus 로고
    • High-level expression of the neutralizing epitope of porcine epidemic diarrhea virus by a tobacco mosaic virus-based vector
    • Kang T.J., Kang K.H., Kim J.A., Kwon T.H., Jang Y.S., and Yang M.S. High-level expression of the neutralizing epitope of porcine epidemic diarrhea virus by a tobacco mosaic virus-based vector. Protein Expr. Purif. 38 (2004) 129-135
    • (2004) Protein Expr. Purif. , vol.38 , pp. 129-135
    • Kang, T.J.1    Kang, K.H.2    Kim, J.A.3    Kwon, T.H.4    Jang, Y.S.5    Yang, M.S.6
  • 30
    • 8144226497 scopus 로고    scopus 로고
    • Total synthesis of long DNA sequences: synthesis of a contiguous 32-kb polyketide synthase gene cluster
    • Kodumal S.J., Patel K.G., Reid R., Menzella H.G., Welch M., and Santi D.V. Total synthesis of long DNA sequences: synthesis of a contiguous 32-kb polyketide synthase gene cluster. Proc. Natl. Acad. Sci. USA 101 (2004) 15573-15578
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15573-15578
    • Kodumal, S.J.1    Patel, K.G.2    Reid, R.3    Menzella, H.G.4    Welch, M.5    Santi, D.V.6
  • 31
    • 0033963277 scopus 로고    scopus 로고
    • From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase
    • Lehmann M., Kostrewa D., Wyss M., Brugger R., D'Arcy A., Pasamontes L., and van Loon A.P. From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. Protein Eng. 13 (2000) 49-57
    • (2000) Protein Eng. , vol.13 , pp. 49-57
    • Lehmann, M.1    Kostrewa, D.2    Wyss, M.3    Brugger, R.4    D'Arcy, A.5    Pasamontes, L.6    van Loon, A.P.7
  • 32
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung D.W., Chen E., and Goeddel D.V. A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. J. Methods Cell Mol. Biol. 1 (1989) 11-15
    • (1989) J. Methods Cell Mol. Biol. , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 33
    • 0037123363 scopus 로고    scopus 로고
    • The use of synthetic genes for the expression of ciliate proteins in heterologous systems
    • Lin Y., Cheng G., Wang X., and Clark T.G. The use of synthetic genes for the expression of ciliate proteins in heterologous systems. Gene 288 (2002) 85-94
    • (2002) Gene , vol.288 , pp. 85-94
    • Lin, Y.1    Cheng, G.2    Wang, X.3    Clark, T.G.4
  • 34
    • 0026592678 scopus 로고
    • Ligation-free gene synthesis by PCR: synthesis and mutagenesis at multiple loci of a chimeric gene encoding OmpA signal peptide and hirudin
    • Majumder K. Ligation-free gene synthesis by PCR: synthesis and mutagenesis at multiple loci of a chimeric gene encoding OmpA signal peptide and hirudin. Gene 110 (1992) 89-94
    • (1992) Gene , vol.110 , pp. 89-94
    • Majumder, K.1
  • 36
    • 0033966840 scopus 로고    scopus 로고
    • Assembly and expression of a synthetic gene encoding the antigen Pfs48/45 of the human malaria parasite Plasmodium falciparum in yeast
    • Milek R.L., Stunnenberg H.G., and Konings R.N. Assembly and expression of a synthetic gene encoding the antigen Pfs48/45 of the human malaria parasite Plasmodium falciparum in yeast. Vaccine 18 (2000) 1402-1411
    • (2000) Vaccine , vol.18 , pp. 1402-1411
    • Milek, R.L.1    Stunnenberg, H.G.2    Konings, R.N.3
  • 39
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid B.G., and Flynn G.C. Chromophore formation in green fluorescent protein. Biochemistry 36 (1997) 6786-6791
    • (1997) Biochemistry , vol.36 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 40
    • 0026502381 scopus 로고
    • Dual asymmetric PCR: one-step construction of synthetic genes
    • Sandhu G.S., Aleff R.A., and Kline B.C. Dual asymmetric PCR: one-step construction of synthetic genes. Biotechniques 12 (1992) 14-16
    • (1992) Biotechniques , vol.12 , pp. 14-16
    • Sandhu, G.S.1    Aleff, R.A.2    Kline, B.C.3
  • 41
    • 13644260108 scopus 로고    scopus 로고
    • Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
    • Scheibel T. Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins. Microb. Cell Fact. 3 (2004) 14
    • (2004) Microb. Cell Fact. , vol.3 , pp. 14
    • Scheibel, T.1
  • 42
    • 0347364647 scopus 로고    scopus 로고
    • Generating a synthetic genome by whole genome assembly: phiX174 bacteriophage from synthetic oligonucleotides
    • Smith H.O., Hutchison III C.A., Pfannkoch C., and Venter J.C. Generating a synthetic genome by whole genome assembly: phiX174 bacteriophage from synthetic oligonucleotides. Proc. Natl. Acad. Sci. USA 100 (2003) 15440-15445
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15440-15445
    • Smith, H.O.1    Hutchison III, C.A.2    Pfannkoch, C.3    Venter, J.C.4
  • 43
    • 0030923727 scopus 로고    scopus 로고
    • Removal of polymerase-produced mutant sequences from PCR products
    • Smith J., and Modrich P. Removal of polymerase-produced mutant sequences from PCR products. Proc. Natl. Acad. Sci. USA 94 (1997) 6847-6850
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6847-6850
    • Smith, J.1    Modrich, P.2
  • 44
    • 0026512912 scopus 로고
    • PCR amplification of specific alleles (PASA) is a general method for rapidly detecting known single-base changes
    • Sommer S.S., Groszbach A.R., and Bottema C.D. PCR amplification of specific alleles (PASA) is a general method for rapidly detecting known single-base changes. Biotechniques 12 (1992) 82-87
    • (1992) Biotechniques , vol.12 , pp. 82-87
    • Sommer, S.S.1    Groszbach, A.R.2    Bottema, C.D.3
  • 45
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sorensen H.P., and Mortensen K.K. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115 (2005) 113-128
    • (2005) J. Biotechnol. , vol.115 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 46
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370 (1994) 389-391
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 47
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer W.P., Crameri A., Ha K.D., Brennan T.M., and Heyneker H.L. Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene 164 (1995) 49-53
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 48
    • 0036417167 scopus 로고    scopus 로고
    • Expression, purification, and characterization of minimized chicken riboflavin carrier protein from a synthetic gene in Escherichia coli
    • Subramanian S., Kondaiah P., and Radhakantha Adiga P. Expression, purification, and characterization of minimized chicken riboflavin carrier protein from a synthetic gene in Escherichia coli. Protein Expr. Purif. 26 (2002) 284-289
    • (2002) Protein Expr. Purif. , vol.26 , pp. 284-289
    • Subramanian, S.1    Kondaiah, P.2    Radhakantha Adiga, P.3
  • 49
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor S., and Richardson C.C. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82 (1985) 1074-1078
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 50
  • 52
    • 0022917641 scopus 로고
    • Host/vector interactions which affect the viability of recombinant phage lambda clones
    • Wertman K.F., Wyman A.R., and Botstein D. Host/vector interactions which affect the viability of recombinant phage lambda clones. Gene 49 (1986) 253-262
    • (1986) Gene , vol.49 , pp. 253-262
    • Wertman, K.F.1    Wyman, A.R.2    Botstein, D.3
  • 53
    • 0030002009 scopus 로고    scopus 로고
    • Synthesis of a modified gene encoding human ornithine transcarbamylase for expression in mammalian mitochondrial and universal translation systems: a novel approach towards correction of a genetic defect
    • Wheeler V.C., Prodromou C., Pearl L.H., Williamson R., and Coutelle C. Synthesis of a modified gene encoding human ornithine transcarbamylase for expression in mammalian mitochondrial and universal translation systems: a novel approach towards correction of a genetic defect. Gene 169 (1996) 251-255
    • (1996) Gene , vol.169 , pp. 251-255
    • Wheeler, V.C.1    Prodromou, C.2    Pearl, L.H.3    Williamson, R.4    Coutelle, C.5
  • 54
    • 0035130371 scopus 로고    scopus 로고
    • Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
    • Wigley W.C., Stidham R.D., Smith N.M., Hunt J.F., and Thomas P.J. Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein. Nat. Biotechnol. 19 (2001) 131-136
    • (2001) Nat. Biotechnol. , vol.19 , pp. 131-136
    • Wigley, W.C.1    Stidham, R.D.2    Smith, N.M.3    Hunt, J.F.4    Thomas, P.J.5
  • 57
    • 3042820410 scopus 로고    scopus 로고
    • A simple, rapid, high-fidelity and cost-effective PCR-based two-step DNA synthesis method for long gene sequences
    • Xiong A.S., Yao Q.H., Peng R.H., Li X., Fan H.Q., Cheng Z.M., and Li Y. A simple, rapid, high-fidelity and cost-effective PCR-based two-step DNA synthesis method for long gene sequences. Nucleic Acids Res. 32 (2004) e98
    • (2004) Nucleic Acids Res. , vol.32
    • Xiong, A.S.1    Yao, Q.H.2    Peng, R.H.3    Li, X.4    Fan, H.Q.5    Cheng, Z.M.6    Li, Y.7
  • 58
    • 17044455338 scopus 로고    scopus 로고
    • Two-step total gene synthesis method
    • Young L., and Dong Q. Two-step total gene synthesis method. Nucleic Acids Res. 32 (2004) e59
    • (2004) Nucleic Acids Res. , vol.32
    • Young, L.1    Dong, Q.2


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