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Volumn 8, Issue 3, 2008, Pages 238-249

Strategies towards the functionalization of subtilisin E from Bacillus subtilis for wool finishing applications

Author keywords

In vitro refolding; Protein engineering; Subtilisin E; Wool hydrolysis

Indexed keywords

AGRICULTURAL PRODUCTS; AMINO ACIDS; BACTERIOLOGY; CATALYSTS; CHLORINE; ENZYMES; FIBER OPTICS; FOOD ADDITIVES; HYDROLYSIS; MOLECULAR WEIGHT; PROTEINS; SOAPS (DETERGENTS); WOOL; WOOL FIBERS; YARN;

EID: 48049103260     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.200700056     Document Type: Article
Times cited : (7)

References (56)
  • 2
    • 0033543617 scopus 로고    scopus 로고
    • Engineered Bacillus lentus subtilisins have altered flexibility
    • T. Graycar, M. Knapp, G. Ganshaw, J. Dauberman, R. Bott, Engineered Bacillus lentus subtilisins have altered flexibility, J. Mol. Biol. 1999, 292, 97-109.
    • (1999) J. Mol. Biol , vol.292 , pp. 97-109
    • Graycar, T.1    Knapp, M.2    Ganshaw, G.3    Dauberman, J.4    Bott, R.5
  • 3
    • 0026891054 scopus 로고
    • Purification of a new extracellular 90-KDa serine proteinase with isoelectric point of 3.9 from Bacillus subtilis (natto) and elucidation of its distinct mode of action
    • T. Kato, Y. Yamagata, T. Arai, E. Ichishima, Purification of a new extracellular 90-KDa serine proteinase with isoelectric point of 3.9 from Bacillus subtilis (natto) and elucidation of its distinct mode of action, Biosci. Biotechnol. Biochem. 1992, 56, 1166-1168.
    • (1992) Biosci. Biotechnol. Biochem , vol.56 , pp. 1166-1168
    • Kato, T.1    Yamagata, Y.2    Arai, T.3    Ichishima, E.4
  • 5
    • 0028644160 scopus 로고
    • Cation-induced thermal stability of an alkaline protease from a Bacillus sp
    • N. Paliwal, S. P. Singh, S. K. Garg, Cation-induced thermal stability of an alkaline protease from a Bacillus sp., Bioresource Technol. 1994, 50, 209-211.
    • (1994) Bioresource Technol , vol.50 , pp. 209-211
    • Paliwal, N.1    Singh, S.P.2    Garg, S.K.3
  • 6
    • 0001170762 scopus 로고
    • Sulfonyl fluorides as inhibitors of esterases: II. Formation and reactions of phenylmethanesulfonyl alpha-chymotrypsin
    • A. M. Gold, D. Fahrney, Sulfonyl fluorides as inhibitors of esterases: II. Formation and reactions of phenylmethanesulfonyl alpha-chymotrypsin, Biochem. 1964, 3, 783-791.
    • (1964) Biochem , vol.3 , pp. 783-791
    • Gold, A.M.1    Fahrney, D.2
  • 7
    • 0016376184 scopus 로고
    • Comparative specificity of microbial proteinases
    • K. Morihara, Comparative specificity of microbial proteinases, Adv. Enzymol. 1974, 41, 179-243.
    • (1974) Adv. Enzymol , vol.41 , pp. 179-243
    • Morihara, K.1
  • 8
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases: From a bioindustrial viewpoint
    • C. G. Kumar, H. Takagi, Microbial alkaline proteases: From a bioindustrial viewpoint, Biotechnol. Adv. 1999, 17, 561-594.
    • (1999) Biotechnol. Adv , vol.17 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 9
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: Molecular approaches and industrial applications
    • R. Gupta, Q. K. Beg, R Lorenz, Bacterial alkaline proteases: molecular approaches and industrial applications, Appl. Microbiol. Biotechnol. 2002, 59, 15-32.
    • (2002) Appl. Microbiol. Biotechnol , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.K.2    Lorenz, R.3
  • 10
    • 0021112782 scopus 로고
    • Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis
    • J. A. Wells, E. Ferrari, D. J. Henner, D. A. Estell, E. Y. Chen, Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis, Nucleic Acids Res. 1983, 11, 7911-7925.
    • (1983) Nucleic Acids Res , vol.11 , pp. 7911-7925
    • Wells, J.A.1    Ferrari, E.2    Henner, D.J.3    Estell, D.A.4    Chen, E.Y.5
  • 11
    • 0021337529 scopus 로고
    • Replacement of the Bacillus subtilis subtilisin structural gene with an in vitro-derived deletion mutation
    • M. L. Stahl, E. Ferrari, Replacement of the Bacillus subtilis subtilisin structural gene with an in vitro-derived deletion mutation, J. Bacteriol. 1984, 158, 411-418.
    • (1984) J. Bacteriol , vol.158 , pp. 411-418
    • Stahl, M.L.1    Ferrari, E.2
  • 12
    • 0022848673 scopus 로고
    • Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis
    • S. L. Wong, R. H. Doi, Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis, J. Biol. Chem. 1986, 261, 10176-10181.
    • (1986) J. Biol. Chem , vol.261 , pp. 10176-10181
    • Wong, S.L.1    Doi, R.H.2
  • 13
    • 0023644876 scopus 로고
    • Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli
    • H. Ikemura, H. Takagi, M. Inouye, Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli, J. Biol. Chem. 1987, 262, 7859-7864.
    • (1987) J. Biol. Chem , vol.262 , pp. 7859-7864
    • Ikemura, H.1    Takagi, H.2    Inouye, M.3
  • 14
    • 0023722280 scopus 로고
    • In vitro processing of pro-subtilisin produced in Escherichia coli
    • H. Ikemura, M. Inouye, In vitro processing of pro-subtilisin produced in Escherichia coli, J. Biol. Chem. 1988, 263, 12959-12963.
    • (1988) J. Biol. Chem , vol.263 , pp. 12959-12963
    • Ikemura, H.1    Inouye, M.2
  • 15
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
    • X. Zhu, Y. Ohta, F. Jordon, M. Inouye, Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process, Nature (London) 1989, 339, 483-484.
    • (1989) Nature (London) , vol.339 , pp. 483-484
    • Zhu, X.1    Ohta, Y.2    Jordon, F.3    Inouye, M.4
  • 17
    • 0028067179 scopus 로고
    • Autoprocessing of pro-thiol-subtilisin E in which the active site serine residue-221 was altered to cysteine
    • Y. Li, M. Inouye, Autoprocessing of pro-thiol-subtilisin E in which the active site serine residue-221 was altered to cysteine, J. Biol. Chem. 1994, 269, 4169-4174.
    • (1994) J. Biol. Chem , vol.269 , pp. 4169-4174
    • Li, Y.1    Inouye, M.2
  • 18
    • 0035976917 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Propeptide release modulates activation precision of pro-subtilisin
    • Y. Yabuta, H. Takagi, M. Inouye, U. Shinde, Folding pathway mediated by an intramolecular chaperone: Propeptide release modulates activation precision of pro-subtilisin, J. Biol. Chem. 2001, 276, 44427-44434.
    • (2001) J. Biol. Chem , vol.276 , pp. 44427-44434
    • Yabuta, Y.1    Takagi, H.2    Inouye, M.3    Shinde, U.4
  • 19
    • 0028846035 scopus 로고
    • Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding: Refolding and inhibitory abilities of propeptide mutants
    • Y. Li, Z. Hu, F. Jordan, M. Inouye, Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding: refolding and inhibitory abilities of propeptide mutants, J. Biol. Chem. 1995, 270, 25127-25132.
    • (1995) J. Biol. Chem , vol.270 , pp. 25127-25132
    • Li, Y.1    Hu, Z.2    Jordan, F.3    Inouye, M.4
  • 20
    • 0034596066 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked
    • X. Fu, M. Inouye, U. Shinde, Folding pathway mediated by an intramolecular chaperone: The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked, J. Biol. Chem. 2000, 275, 16871-16878.
    • (2000) J. Biol. Chem , vol.275 , pp. 16871-16878
    • Fu, X.1    Inouye, M.2    Shinde, U.3
  • 21
    • 0032553556 scopus 로고    scopus 로고
    • The crystal structure of an autoprocessed Ser221 Cys-subtilisin E-propeptide complex at 2.0 A resolution
    • S. C. Jain, U. Shinde, Y. Li, M. Inouye, H. M. Berman, The crystal structure of an autoprocessed Ser221 Cys-subtilisin E-propeptide complex at 2.0 A resolution, J. Mol. Biol. 1998, 284, 137-144.
    • (1998) J. Mol. Biol , vol.284 , pp. 137-144
    • Jain, S.C.1    Shinde, U.2    Li, Y.3    Inouye, M.4    Berman, H.M.5
  • 22
    • 0024273064 scopus 로고
    • Mutant subtilisin E with enhanced protease activity obtained by site-directed mutagenesis
    • H. Takagi, Y. Morinaga, H. Ikemura, M. Inouye, Mutant subtilisin E with enhanced protease activity obtained by site-directed mutagenesis, J. Biol. Chem. 1988, 263, 19592-19596.
    • (1988) J. Biol. Chem , vol.263 , pp. 19592-19596
    • Takagi, H.1    Morinaga, Y.2    Ikemura, H.3    Inouye, M.4
  • 23
    • 0031449410 scopus 로고    scopus 로고
    • Construction of novel subtilisin E with high specificity, activity and productivity through multiple amino acid substitutions
    • H. Takagi I. Ohtsu, S. Nakamori, Construction of novel subtilisin E with high specificity, activity and productivity through multiple amino acid substitutions, Protein Eng. 1997, 10, 985-989.
    • (1997) Protein Eng , vol.10 , pp. 985-989
    • Takagi, H.1    Ohtsu, I.2    Nakamori, S.3
  • 24
    • 0035668519 scopus 로고    scopus 로고
    • Generation of a broad estereolytic subtilisin using combined molecular evolution and periplasmic expression
    • G. E. Sroga, J. S. Dordick, Generation of a broad estereolytic subtilisin using combined molecular evolution and periplasmic expression, Protein Eng. 2001, 14, 929-937.
    • (2001) Protein Eng , vol.14 , pp. 929-937
    • Sroga, G.E.1    Dordick, J.S.2
  • 25
    • 0025232324 scopus 로고
    • Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease
    • H. Takagi, T. Takahashi, H. Momose, M. Inouye, Y. Maeda, H. Matsuzawa et al., Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease, J. Biol. Chem. 1990, 265, 6674-6676.
    • (1990) J. Biol. Chem , vol.265 , pp. 6674-6676
    • Takagi, H.1    Takahashi, T.2    Momose, H.3    Inouye, M.4    Maeda, Y.5    Matsuzawa, H.6
  • 26
    • 0342316127 scopus 로고
    • Thermal stability improvement of subtilisin E with protein engineering
    • X. S. Wang, P. Z. Wang, L. Y. Kong, H. J. Ruang, Thermal stability improvement of subtilisin E with protein engineering, Chin. J. Biochem. Biophys. 1993, 25, 51-61.
    • (1993) Chin. J. Biochem. Biophys , vol.25 , pp. 51-61
    • Wang, X.S.1    Wang, P.Z.2    Kong, L.Y.3    Ruang, H.J.4
  • 28
    • 0034714147 scopus 로고    scopus 로고
    • Thermal stable and oxidation-resistant variant of subtilisin E
    • Y. Yang, L. Jiang, L. Zhu, Y. Wu, S. Yang, Thermal stable and oxidation-resistant variant of subtilisin E, J. Biotechnol. 2000, 81, 113-118.
    • (2000) J. Biotechnol , vol.81 , pp. 113-118
    • Yang, Y.1    Jiang, L.2    Zhu, L.3    Wu, Y.4    Yang, S.5
  • 29
    • 0032973026 scopus 로고    scopus 로고
    • Directed evolution converts subtilisin E into a functional equivalent of thermitase
    • H. Zhao, F. H. Arnold, Directed evolution converts subtilisin E into a functional equivalent of thermitase, Protein Eng. 1999, 12, 47-53.
    • (1999) Protein Eng , vol.12 , pp. 47-53
    • Zhao, H.1    Arnold, F.H.2
  • 30
    • 0035940087 scopus 로고    scopus 로고
    • Extremozymes for improving wool properties
    • K. Schumacher, E. Heine, H. Hocker, Extremozymes for improving wool properties, J. Biotechnol. 2001, 89, 281-288.
    • (2001) J. Biotechnol , vol.89 , pp. 281-288
    • Schumacher, K.1    Heine, E.2    Hocker, H.3
  • 31
    • 0002858849 scopus 로고    scopus 로고
    • Factors affecting the control of proteolytic enzyme reactions on wool
    • J. Shen, D. P. Bishop, E. Heine, B. Hollfelder, Factors affecting the control of proteolytic enzyme reactions on wool, J. Textile Inst. 1999, 90, 404-411.
    • (1999) J. Textile Inst , vol.90 , pp. 404-411
    • Shen, J.1    Bishop, D.P.2    Heine, E.3    Hollfelder, B.4
  • 34
    • 33745538783 scopus 로고    scopus 로고
    • New enzyme-based process direction to prevent wool shrinking without substantial tensile strength loss
    • H. B. M. Lenting, M. Schroeder, G. M. Guebitz, A. Cavaco-Paulo, J. Shen, New enzyme-based process direction to prevent wool shrinking without substantial tensile strength loss, Biotechnol. Lett. 2006, 28, 711-716.
    • (2006) Biotechnol. Lett , vol.28 , pp. 711-716
    • Lenting, H.B.M.1    Schroeder, M.2    Guebitz, G.M.3    Cavaco-Paulo, A.4    Shen, J.5
  • 35
    • 0035827597 scopus 로고    scopus 로고
    • The amino-terminal heptad repeats of the coiled-coil neck domain of pulmonary surfactant protein D are necessary for the assembly of trimeric subunits and dodecamers
    • P. Zhang, A. McAlinden, S. Li, T. Schumacher, H. Wang, S. Hu et al., The amino-terminal heptad repeats of the coiled-coil neck domain of pulmonary surfactant protein D are necessary for the assembly of trimeric subunits and dodecamers, J. Biol. Chem. 2001, 276, 19862-19870.
    • (2001) J. Biol. Chem , vol.276 , pp. 19862-19870
    • Zhang, P.1    McAlinden, A.2    Li, S.3    Schumacher, T.4    Wang, H.5    Hu, S.6
  • 36
    • 0037175005 scopus 로고    scopus 로고
    • Trimerization of the amino propeptide of type IIA procollagen using a 14-amino acid sequence derived from the coiled-coil neck domain of surfactant protein D
    • A. McAlinden, E. C. Crouch, J. G. Bann, P. Zhang, L. J. Sandell, Trimerization of the amino propeptide of type IIA procollagen using a 14-amino acid sequence derived from the coiled-coil neck domain of surfactant protein D, J. Biol. Chem. 2002, 277, 41274-41281.
    • (2002) J. Biol. Chem , vol.277 , pp. 41274-41281
    • McAlinden, A.1    Crouch, E.C.2    Bann, J.G.3    Zhang, P.4    Sandell, L.J.5
  • 37
    • 0028013677 scopus 로고
    • A covalently trapped folding intermediate of subtilisin E: Spontaneous dimerization of a prosubtilisin E Ser49Cys mutant in vivo and its autoprocessing in vitro
    • Z. Hu, X. Zhu, F. Jordan, M. Inouye, A covalently trapped folding intermediate of subtilisin E: spontaneous dimerization of a prosubtilisin E Ser49Cys mutant in vivo and its autoprocessing in vitro, Biochemistry 1994, 33 (2), 562-569.
    • (1994) Biochemistry , vol.33 , Issue.2 , pp. 562-569
    • Hu, Z.1    Zhu, X.2    Jordan, F.3    Inouye, M.4
  • 38
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • H. Inoue, H. Nojima, H. Okayama, High efficiency transformation of Escherichia coli with plasmids, Gene 1990, 96, 23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 41
    • 0030088086 scopus 로고    scopus 로고
    • Site-specific mutagenesis by using an accurate recombinant polymerase chain reaction method
    • M. Ansaldi, M. Lepelletier, V. Mejean, Site-specific mutagenesis by using an accurate recombinant polymerase chain reaction method, Anal. Biochem. 1996, 234 (1), 110-111.
    • (1996) Anal. Biochem , vol.234 , Issue.1 , pp. 110-111
    • Ansaldi, M.1    Lepelletier, M.2    Mejean, V.3
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 1970, 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. M. Bradford, A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 44
    • 0343923413 scopus 로고    scopus 로고
    • An extremely heatstable extracellular proteinase (aeropyrolysin) from the hyperthermophilic archaeon Aeropyrum pernix K1
    • Y. Sako, P. Chavez Croocker, Y. Ishida, An extremely heatstable extracellular proteinase (aeropyrolysin) from the hyperthermophilic archaeon Aeropyrum pernix K1, FEBS Letters 1997, 415, 329-334.
    • (1997) FEBS Letters , vol.415 , pp. 329-334
    • Sako, Y.1    Chavez Croocker, P.2    Ishida, Y.3
  • 45
    • 0037199161 scopus 로고    scopus 로고
    • A strategy for in vivo screening of Subtilisin E reaction specificity in E. coli periplasm
    • G. E. Sroga, J. S. Dordick, A strategy for in vivo screening of Subtilisin E reaction specificity in E. coli periplasm, Biotechnol. Bioeng. 2002, 78, 761-769.
    • (2002) Biotechnol. Bioeng , vol.78 , pp. 761-769
    • Sroga, G.E.1    Dordick, J.S.2
  • 46
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • S. C. Makrides, Strategies for achieving high-level expression of genes in Escherichia coli, Microbiol. Rev. 1996, 60, 512-538.
    • (1996) Microbiol. Rev , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 48
    • 0021359871 scopus 로고
    • Novel high-level expression cloning vehicles: 104-fold amplification of Escherichia coli minor protein
    • Y. Masui, T. Mizuno, M. Inouye, Novel high-level expression cloning vehicles: 104-fold amplification of Escherichia coli minor protein, Nat. Biotechnol. 1984, 2, 81-85.
    • (1984) Nat. Biotechnol , vol.2 , pp. 81-85
    • Masui, Y.1    Mizuno, T.2    Inouye, M.3
  • 49
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • F. W. Studier, Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system, J. Mol. Biol. 1991, 219, 37-44.
    • (1991) J. Mol. Biol , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 51
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese Cedar pollen, Cryj2
    • K. Nishihara, M. Kanemori, M. Kitagawa, H. Yanagi, T. Yura, Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese Cedar pollen, Cryj2, in Escherichia coli, Appl. Microbiol. Biotechnol. 1998, 64, 1694-1699.
    • (1998) Escherichia coli, Appl. Microbiol. Biotechnol , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 52
    • 18144376288 scopus 로고    scopus 로고
    • Co-expression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli
    • S. G. Kim, D. H. Kweon, D. H. Lee, Y. C. Park, J. H. Seo, Co-expression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli, Protein Expr. Purif. 2005, 41, 426-432.
    • (2005) Protein Expr. Purif , vol.41 , pp. 426-432
    • Kim, S.G.1    Kweon, D.H.2    Lee, D.H.3    Park, Y.C.4    Seo, J.H.5
  • 53
    • 33745931632 scopus 로고    scopus 로고
    • A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli
    • M. Schlapschy, S. Grimm, A. Skerra, A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli, Protein Eng. Des. Sel. 2006, 19, 385-390.
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 385-390
    • Schlapschy, M.1    Grimm, S.2    Skerra, A.3
  • 54
    • 0038035426 scopus 로고    scopus 로고
    • Q. Yang, J. Xu, M. Li, X. Lei, L. An, High-level expression of a soluble snake venom enzyme, gloshedobin, in E. coli in the presence of metal ions, Biotechnol. Lett. 2003, 25, 607-610.
    • Q. Yang, J. Xu, M. Li, X. Lei, L. An, High-level expression of a soluble snake venom enzyme, gloshedobin, in E. coli in the presence of metal ions, Biotechnol. Lett. 2003, 25, 607-610.
  • 56
    • 35748986427 scopus 로고    scopus 로고
    • A sucrose-inducible promoter system for the intra- and extracellular protein production in Bacillus megaterium
    • R. Biedendieck, M. Gamer, L. Jaensch, S. Meyer, M. Rohde, W. D. Deckwer et al., A sucrose-inducible promoter system for the intra- and extracellular protein production in Bacillus megaterium, J. Biotechnol. 2007, 132, 426-430.
    • (2007) J. Biotechnol , vol.132 , pp. 426-430
    • Biedendieck, R.1    Gamer, M.2    Jaensch, L.3    Meyer, S.4    Rohde, M.5    Deckwer, W.D.6


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