메뉴 건너뛰기




Volumn 11, Issue 2, 1993, Pages 187-193

A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; GROWTH FACTOR; THIOREDOXIN;

EID: 14744292185     PISSN: 0733222X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0293-187     Document Type: Article
Times cited : (836)

References (63)
  • 1
    • 0020480282 scopus 로고
    • Characterization of translation initiation sites in E. coli
    • Stormo, G. D., Schneider, T. D. and Gold, L. 1982. Characterization of translation initiation sites in E. coli. Nucl. Acids Res. 10:2971-2996.
    • (1982) Nucl. Acids Res , vol.10 , pp. 2971-2996
    • Stormo, G.D.1    Schneider, T.D.2    Gold, L.3
  • 2
    • 0024811752 scopus 로고
    • Genetics of proteolysis in Escherichia coli
    • Gottesman, S. 1989. Genetics of proteolysis in Escherichia coli. Annu. Rev. Genet. 23:163-198.
    • (1989) Annu. Rev. Genet , vol.23 , pp. 163-198
    • Gottesman, S.1
  • 3
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • Schein, C. H, 1989. Production of soluble recombinant proteins in bacteria. Bio/Technology 7:1141-1149.
    • (1989) Bio/Technology , vol.7 , pp. 1141-1149
    • Schein, C.H.1
  • 4
    • 0024371647 scopus 로고
    • Protein folding intermediates and inclusion body formation
    • Mitraki, A. and King, J. 1989. Protein folding intermediates and inclusion body formation. Bio/Technology 7:690-697.
    • (1989) Bio/Technology , vol.7 , pp. 690-697
    • Mitraki, A.1    King, J.2
  • 6
    • 0025370459 scopus 로고
    • Engineering Escherichia coli to secrete heterologous gene products
    • Stader, J. A. and Silhavy, T. J. 1990. Engineering Escherichia coli to secrete heterologous gene products. Methods in Enzymol. 165:166-187.
    • (1990) Methods in Enzymol , vol.165 , pp. 166-187
    • Stader, J.A.1    Silhavy, T.J.2
  • 7
    • 0022981351 scopus 로고
    • Localization of inclusion bodies in Escherichia coli overproducing β-lactamase or alkaline phosphatase
    • Georgiou, G., Telford, J. N., Shuler, M. L. and Wilson, D. B. 1986. Localization of inclusion bodies in Escherichia coli overproducing β-lactamase or alkaline phosphatase. Appl. Environ. Microbiol. 52:1157-1161.
    • (1986) Appl. Environ. Microbiol , vol.52 , pp. 1157-1161
    • Georgiou, G.1    Telford, J.N.2    Shuler, M.L.3    Wilson, D.B.4
  • 8
    • 0025123399 scopus 로고
    • Folding and aggregation of β-lactamase in the periplasmic space of Es herichia coli
    • Bowden, G. A. and Giorgiou, G. 1990. Folding and aggregation of β-lactamase in the periplasmic space of Es herichia coli. J. Biol. Chem. 265:16760-16766.
    • (1990) J. Biol. Chem , vol.265 , pp. 16760-16766
    • Bowden, G.A.1    Giorgiou, G.2
  • 9
    • 0020980522 scopus 로고
    • Easy identification of cDNA clones
    • Ruther, U. and Muller-Hill, B. 1983. Easy identification of cDNA clones. EMBO J. 2:1791-1794.
    • (1983) EMBO J , vol.2 , pp. 1791-1794
    • Ruther, U.1    Muller-Hill, B.2
  • 10
    • 0025287633 scopus 로고
    • Expression as trpE fusion
    • Yansura, D. G. 1990. Expression as trpE fusion. Methods in Enzymol. 165:161-166.
    • (1990) Methods in Enzymol , vol.165 , pp. 161-166
    • Yansura, D.G.1
  • 11
    • 0022053837 scopus 로고
    • Immobilization and purification of enzymes with staphylococcal protein A gene fusion vectors
    • Nilsson, B., Abrahmsen, L. and Uhlen, M. 1985. Immobilization and purification of enzymes with staphylococcal protein A gene fusion vectors. EMBO J. 4:1075-1080.
    • (1985) EMBO J , vol.4 , pp. 1075-1080
    • Nilsson, B.1    Abrahmsen, L.2    Uhlen, M.3
  • 12
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transierase
    • Smith, D. B. and Johnson, K. S. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transierase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 13
    • 0024215242 scopus 로고
    • An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein
    • Maina, C. V., Riggs, P. D., Grandea, A. G., Slatko, B. E., Moran, L. S., Tagliamonte, J. A., McReynolds, L. A. and di Guan, C. 1988. An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein. Gene 74:365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.3    Slatko, B.E.4    Moran, L.S.5    Tagliamonte, J.A.6    McReynolds, L.A.7    di Guan, C.8
  • 15
    • 0021256117 scopus 로고
    • Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12
    • Lunn, C. A., Kathju, S., Wallace, B. J., Kushner, S. R. and Pigiet, V. 1984. Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12. J. Biol. Chem. 259:10469-10474.
    • (1984) J. Biol. Chem , vol.259 , pp. 10469-10474
    • Lunn, C.A.1    Kathju, S.2    Wallace, B.J.3    Kushner, S.R.4    Pigiet, V.5
  • 16
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 angstroms resolution
    • Katti, S. K., LeMaster, D. M. and Eklund, H. 1990. Crystal structure of thioredoxin from Escherichia coli at 1.68 angstroms resolution. J. Mol. Biol. 212:167-184.
    • (1990) J. Mol. Biol , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 17
    • 0014346151 scopus 로고
    • Areas of adhesion between wall and membrane of Escherichia coli
    • Bayer, M. E. 1968. Areas of adhesion between wall and membrane of Escherichia coli. J. Gen. Microbiol. 53:395-404.
    • (1968) J. Gen. Microbiol , vol.53 , pp. 395-404
    • Bayer, M.E.1
  • 18
    • 0020448702 scopus 로고
    • Localization of thioredoxin from Escherichia coli in an eosmotically sensitive compartment
    • Lunn, C. A. and Pigiet, V. P. 1982. Localization of thioredoxin from Escherichia coli in an eosmotically sensitive compartment. J. Biol. Chem. 257:11424-11430.
    • (1982) J. Biol. Chem , vol.257 , pp. 11424-11430
    • Lunn, C.A.1    Pigiet, V.P.2
  • 19
    • 0023198037 scopus 로고
    • Characterization of disulfide bonds in recombinant proteins: Reduced human interleukin 2 in inclusion bodies and its oxidative refolding
    • Tsuji, T., Nakagawa, R., Sugimoto, N. and Fukuhara, K-I. 1987. Characterization of disulfide bonds in recombinant proteins: reduced human interleukin 2 in inclusion bodies and its oxidative refolding. Biochemistry 26:3129-3134.
    • (1987) Biochemistry , vol.26 , pp. 3129-3134
    • Tsuji, T.1    Nakagawa, R.2    Sugimoto, N.3    Fukuhara, K.-I.4
  • 21
    • 0023943656 scopus 로고
    • Expression, renaturation and purification of recombinant human interleukin 4 from Escherichia coli
    • van Kimmenade, A., Bond, M. W., Schumacher, J. H., Laquoi, C. and Kastelein, R. A. 1988. Expression, renaturation and purification of recombinant human interleukin 4 from Escherichia coli. Eur. J. Biochem. 173:109-114.
    • (1988) Eur. J. Biochem , vol.173 , pp. 109-114
    • van Kimmenade, A.1    Bond, M.W.2    Schumacher, J.H.3    Laquoi, C.4    Kastelein, R.A.5
  • 22
    • 0025859083 scopus 로고
    • Single-step purification and structural characterization of human interleukin-6 produced in Escherichia coli from a T7 RNA polymerase expression vector
    • Arcone, R, Pucci, P., Zapacosta, F., Fontaine, V., Malorni, A., Marino, G. and Ciliberto, G. 1991. Single-step purification and structural characterization of human interleukin-6 produced in Escherichia coli from a T7 RNA polymerase expression vector. Eur. J. Biochem. 198:541-547.
    • (1991) Eur. J. Biochem , vol.198 , pp. 541-547
    • Arcone, R.1    Pucci, P.2    Zapacosta, F.3    Fontaine, V.4    Malorni, A.5    Marino, G.6    Ciliberto, G.7
  • 23
    • 0025065459 scopus 로고
    • Primary structure and functional expression of rat and human stem cell factor DNAs
    • Martin, F. H., Suggs, S. V., Langley, K. E., Lu, H. S. et al. 1990. Primary structure and functional expression of rat and human stem cell factor DNAs. Cell 63:203-211.
    • (1990) Cell , vol.63 , pp. 203-211
    • Martin, F.H.1    Suggs, S.V.2    Langley, K.E.3    Lu, H.S.4
  • 24
    • 0024318891 scopus 로고
    • Renaturation and purification of biologically active recombinant human macrophage colony-stimulating factor expressed in E. coli
    • Halenbeck, R., Kawasaki, E., Wrin, J. and Koths, K. 1989. Renaturation and purification of biologically active recombinant human macrophage colony-stimulating factor expressed in E. coli. Bio/Technology 7:710-715.
    • (1989) Bio/Technology , vol.7 , pp. 710-715
    • Halenbeck, R.1    Kawasaki, E.2    Wrin, J.3    Koths, K.4
  • 25
    • 0011889163 scopus 로고
    • Localization of thioredoxin, thioredoxin reductase and ribonucleotide reductase in cells: Immunohistochcmical aspects
    • Holmgren, A., Branden, C.-L, Jornvall, H., and Sjoberg, B.-M. (Eds.). Raven Press, New York
    • Hansson, H.-A., Holmgren, A., Rozell, B. and Stemme, S. 1986. Localization of thioredoxin, thioredoxin reductase and ribonucleotide reductase in cells: immunohistochcmical aspects, p. 177-187. In: Thioredoxin and Glutaredoxin Systems: Structure and Function. Holmgren, A., Branden, C.-L, Jornvall, H., and Sjoberg, B.-M. (Eds.). Raven Press, New York.
    • (1986) Thioredoxin and Glutaredoxin Systems: Structure and Function , pp. 177-187
    • Hansson, H.-A.1    Holmgren, A.2    Rozell, B.3    Stemme, S.4
  • 26
    • 0015239936 scopus 로고
    • Purification and specificity of porcine enterokinase
    • Maroux, S., Baratti, J. and Desnuelle, P. 1971. Purification and specificity of porcine enterokinase. J. Biol. Chem. 246:5031-5039.
    • (1971) J. Biol. Chem , vol.246 , pp. 5031-5039
    • Maroux, S.1    Baratti, J.2    Desnuelle, P.3
  • 28
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott, J. K. and Smith, G. P. 1990. Searching for peptide ligands with an epitope library. Scicncc 249:386-390.
    • (1990) Scicncc , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 29
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman, J. C., Ellis, L., Blacher, R. W., Roth, R. A. and Rutter, W. J. 1985. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317:267-270.
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 30
    • 0023687758 scopus 로고
    • Molecular cloning and complete amino-acid sequence of form-I phosphoinositidc- specific phospholipase C
    • Bennett, C. F., Balcarek, J. M., Varrichio, A. and Crooke, S. T. 1988. Molecular cloning and complete amino-acid sequence of form-I phosphoinositidc- specific phospholipase C. Nature 334:268-270.
    • (1988) Nature , vol.334 , pp. 268-270
    • Bennett, C.F.1    Balcarek, J.M.2    Varrichio, A.3    Crooke, S.T.4
  • 31
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
    • Mazzarella, R. A., Srinivasan, M., Haugejorden, S. M. and Green, M. 1990. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J. Biol. Chem, 265:1094-1101.
    • (1990) J. Biol. Chem , vol.265 , pp. 1094-1101
    • Mazzarella, R.A.1    Srinivasan, M.2    Haugejorden, S.M.3    Green, M.4
  • 32
    • 84966193022 scopus 로고
    • Heat-shock proteins and their potential uses for pharmaceutical protein production in microorganisms
    • Part B. T. Ahern and M. Manning (Eds.) Plenum Press, New York
    • McCoy, J. M. 1992. Heat-shock proteins and their potential uses for pharmaceutical protein production in microorganisms. In: Stability of Protein Pharmaceuticals, Part B. T. Ahern and M. Manning (Eds.) Plenum Press, New York.
    • (1992) Stability of Protein Pharmaceuticals
    • McCoy, J.M.1
  • 34
    • 0023892436 scopus 로고
    • Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature
    • Schein, C. H. and Noteborn, M. H. M, 1988. Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature. Bio/Technology 6:291-294.
    • (1988) Bio/Technology , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, M.H.M.2
  • 35
    • 0025303732 scopus 로고
    • Human recombinant interleukin-1β isolated from Escheri chia coli by simple osmotic shock
    • Joseph-Liauzum, E., Leplatois, P., Legoux, R., Gucrverno, V., Marchese, E. and Ferrara, P. 1990. Human recombinant interleukin-1β isolated from Escheri chia coli by simple osmotic shock. Gene 86:291-295.
    • (1990) Gene , vol.86 , pp. 291-295
    • Joseph-Liauzum, E.1    Leplatois, P.2    Legoux, R.3    Gucrverno, V.4    Marchese, E.5    Ferrara, P.6
  • 37
    • 0025365143 scopus 로고
    • Gene fusions for purpose of expression: An introduction
    • Uhlen, M. and Moks, T. 1990. Gene fusions for purpose of expression: an introduction. Methods in Enzymol. 185:129-143.
    • (1990) Methods in Enzymol , vol.185 , pp. 129-143
    • Uhlen, M.1    Moks, T.2
  • 38
    • 0019586165 scopus 로고
    • Mechanism of action of the lex A gene product
    • Brent, R. and Ptashne, M. 1981. Mechanism of action of the lex A gene product. Proc. Natl. Acad. Sci. USA 78:4204-4208.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4204-4208
    • Brent, R.1    Ptashne, M.2
  • 40
    • 0021073779 scopus 로고
    • Construction of improved M13 vectors using oligonucleotide-directed mutagenesis
    • Norrander, J., Kempe, T. and Messing, J. 1983. Construction of improved M13 vectors using oligonucleotide-directed mutagenesis. Gene 26:101-106.
    • (1983) Gene , vol.26 , pp. 101-106
    • Norrander, J.1    Kempe, T.2    Messing, J.3
  • 41
    • 0019442130 scopus 로고
    • Purified X regulatory protein ell positively activates promoters for lysogenic development
    • Shimatake, H. and Rosenberg, M. 1981. Purified X regulatory protein ell positively activates promoters for lysogenic development. Nature 292:128-132.
    • (1981) Nature , vol.292 , pp. 128-132
    • Shimatake, H.1    Rosenberg, M.2
  • 42
    • 0022474612 scopus 로고
    • Structural and functional relationships between fumarase and aspartasc
    • Woods, S. A., Miles, J. S., Roberts, R. E. and Guest, J. R. 1986. Structural and functional relationships between fumarase and aspartasc. Biochem. J. 237:547-557.
    • (1986) Biochem. J , vol.237 , pp. 547-557
    • Woods, S.A.1    Miles, J.S.2    Roberts, R.E.3    Guest, J.R.4
  • 43
    • 0023277065 scopus 로고
    • Characterization of a human multilineage- colony-stimuiating factor cDNA clone identified by a conserved non-coding sequence in mouse interleukin-3
    • Dorsscrs, L., Burger, H., Bot, F., Delwel, R., Geurts van Kessel, A., Lowen- berg, B. and Wagemaker, G. 1987. Characterization of a human multilineage- colony-stimuiating factor cDNA clone identified by a conserved non-coding sequence in mouse interleukin-3. Gene 55:115-124.
    • (1987) Gene , vol.55 , pp. 115-124
    • Dorsscrs, L.1    Burger, H.2    Bot, F.3    Delwel, R.4    Geurts van Kessel, A.5    Lowen-Berg, B.6    Wagemaker, G.7
  • 44
    • 0022801346 scopus 로고
    • Structure and expression of cDNA and genes for human interferon-beta-2, a distinct species inducible by growth-stimulatory cytokines
    • Zilberstein, A., Ruggieri, R., Korn, J. H. and Revel, M. 1986. Structure and expression of cDNA and genes for human interferon-beta-2, a distinct species inducible by growth-stimulatory cytokines. EMBO J. 5:2529-2537.
    • (1986) EMBO J , vol.5 , pp. 2529-2537
    • Zilberstein, A.1    Ruggieri, R.2    Korn, J.H.3    Revel, M.4
  • 45
    • 0022608022 scopus 로고
    • A cDNA clone used to study mRNA induciblc in human tonsillar lymphocytes by a tumor promoter
    • Obaru, K., Fukuda, M., Maeda, S. and Shimada, K. 1986. A cDNA clone used to study mRNA induciblc in human tonsillar lymphocytes by a tumor promoter. J. Biochem. 99:885-894.
    • (1986) J. Biochem , vol.99 , pp. 885-894
    • Obaru, K.1    Fukuda, M.2    Maeda, S.3    Shimada, K.4
  • 47
    • 0023126461 scopus 로고
    • Human CSF-1: Molecular cloning and expression of 4-kb cDNA encoding the urinary protein
    • Wong, G. G., Temple, P. A., Leary, A. C., Witek-Giannotti, J. S. et al. 1987. Human CSF-1: molecular cloning and expression of 4-kb cDNA encoding the urinary protein. Science 235:1504-1508.
    • (1987) Science , vol.235 , pp. 1504-1508
    • Wong, G.G.1    Temple, P.A.2    Leary, A.C.3    Witek-Giannotti, J.S.4
  • 53
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Miller, J. H. 1972. Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 54
    • 0023009856 scopus 로고
    • A novel prophage independent trp regulated lambda pL expression system
    • Mieschendahl, M., Petri, T. and Hanggi, U. 1986. A novel prophage independent trp regulated lambda pL expression system. Bio/Technology 4:802-808.
    • (1986) Bio/Technology , vol.4 , pp. 802-808
    • Mieschendahl, M.1    Petri, T.2    Hanggi, U.3
  • 55
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bactcriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bactcriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 56
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-poly- acrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schagger, H. and von Jagow, G. 1987. Tricine-sodium dodecyl sulfate-poly- acrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 57
    • 0025636017 scopus 로고
    • M-O7e human leukemic factor-dependent cell line provides a rapid and sensitive bioassay for the human cytokines GM-CSF and IL-3
    • Avanzi, C. G., Brizzi, M. F., Giannotti, J., Ciarletta, A., Yang, Y.-C., Pegoraro, L. and Clark, S. C. 1990. M-O7e human leukemic factor-dependent cell line provides a rapid and sensitive bioassay for the human cytokines GM-CSF and IL-3. J. Cellular Physiol. 145:458-464.
    • (1990) J. Cellular Physiol , vol.145 , pp. 458-464
    • Avanzi, C.G.1    Brizzi, M.F.2    Giannotti, J.3    Ciarletta, A.4    Yang, Y.-C.5    Pegoraro, L.6    Clark, S.C.7
  • 58
    • 0026603456 scopus 로고
    • Recombinant human bone morphogenetic protein-2 induces osteoblastic differentiation in W-20-17 stromal cells
    • Thies, R. S., Bauduy, M., Ashton, B. A., Kurtzberg, L., Wozney, J. M. and Rosen, V. 1992. Recombinant human bone morphogenetic protein-2 induces osteoblastic differentiation in W-20-17 stromal cells. Endocrinology 130:1318-1324.
    • (1992) Endocrinology , vol.130 , pp. 1318-1324
    • Thies, R.S.1    Bauduy, M.2    Ashton, B.A.3    Kurtzberg, L.4    Wozney, J.M.5    Rosen, V.6
  • 59
    • 0021842768 scopus 로고
    • Some interleukin-3 dependent mast-cell lines also respond to interleukin-2
    • Warren, H. S., Hargreaves, J. and Happel, A. J. 1985. Some interleukin-3 dependent mast-cell lines also respond to interleukin-2. Lymphokine Res. 4:195-204.
    • (1985) Lymphokine Res , vol.4 , pp. 195-204
    • Warren, H.S.1    Hargreaves, J.2    Happel, A.J.3
  • 61
    • 0024318485 scopus 로고
    • Establishment and characterization of a unique human cell line that proliferates dependently on GM-CSF, IL-3 or erythropoietin
    • Kitamura, T., Tange, T., Chiba, S., Kuwaki, T., Mitani, K., Urabe, A. and Takaku, F. 1989. Establishment and characterization of a unique human cell line that proliferates dependently on GM-CSF, IL-3 or erythropoietin. J. Cellular Physiol. 140:323-334.
    • (1989) J. Cellular Physiol , vol.140 , pp. 323-334
    • Kitamura, T.1    Tange, T.2    Chiba, S.3    Kuwaki, T.4    Mitani, K.5    Urabe, A.6    Takaku, F.7
  • 63
    • 0024210526 scopus 로고
    • Leukaemia inhibitory factor is identical to the myeloid growth factor human interleukin for DA cells
    • Moreau, J.-F., Donaldson, D. D., Bennett, F., Witek-Giannotti, J., Clark, S. C. and Wong, G. G. 1988. Leukaemia inhibitory factor is identical to the myeloid growth factor human interleukin for DA cells. Nature 336:690-692.
    • (1988) Nature , vol.336 , pp. 690-692
    • Moreau, J.-F.1    Donaldson, D.D.2    Bennett, F.3    Witek-Giannotti, J.4    Clark, S.C.5    Wong, G.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.