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Volumn 265, Issue 1, 1999, Pages 145-151

Purification and properties of a basic endo-β-1,6-glucanase (BGN16.1) from the antagonistic fungus Trichoderma harzianum

Author keywords

glucanases; Antagonism; Fungal cell wall; Trichoderma

Indexed keywords

BETA GLUCAN HYDROLASE; CELLULASE; CHITIN; POLYSACCHARIDE;

EID: 0033215006     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00698.x     Document Type: Article
Times cited : (55)

References (51)
  • 1
    • 0003007762 scopus 로고
    • Fungal cell walls: A review
    • (Kuhn, P.J., Trinci, A.P.J., Jung, M.J., Goosey, M.W. & Copping, L.G., eds). Springer-Verlag, Heidelberg
    • 1. Peberdy, J.F. (1990) Fungal cell walls: a review. In Biochemistry of Cell Walls and Membranes in Fungi (Kuhn, P.J., Trinci, A.P.J., Jung, M.J., Goosey, M.W. & Copping, L.G., eds). pp. 5-24. Springer-Verlag, Heidelberg.
    • (1990) Biochemistry of Cell Walls and Membranes in Fungi , pp. 5-24
    • Peberdy, J.F.1
  • 2
    • 0027439791 scopus 로고
    • Purification and properties of three (1,3)-β-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)
    • 2. Hrmova, M. & Fincher, G.B. (1993) Purification and properties of three (1,3)-β-D-glucanase isoenzymes from young leaves of barley (Hordeum vulgare). Biochem. J. 289, 453-461.
    • (1993) Biochem. J. , vol.289 , pp. 453-461
    • Hrmova, M.1    Fincher, G.B.2
  • 3
    • 0000052863 scopus 로고
    • β-D-1,3-Glucanases in fungi
    • 3. Reese, E.T. & Mandels, M. (1959) β-D-1,3-Glucanases in fungi. Can. J. Microbiol. 5, 173-185.
    • (1959) Can. J. Microbiol. , vol.5 , pp. 173-185
    • Reese, E.T.1    Mandels, M.2
  • 4
    • 0001581521 scopus 로고
    • Biological function of 'pathogenesis-related' proteins: Four PR proteins of tobacco have β-1,3-glucanase activity
    • 4. Kauffmann, S., Legrand, M., Geoffrey, P. & Fritig, B. (1987) Biological function of 'pathogenesis-related' proteins: four PR proteins of tobacco have β-1,3-glucanase activity. EMBO J. 11, 3209-3212.
    • (1987) EMBO J. , vol.11 , pp. 3209-3212
    • Kauffmann, S.1    Legrand, M.2    Geoffrey, P.3    Fritig, B.4
  • 5
    • 0027409809 scopus 로고
    • Purification and characterization of the Saccharomyces cerevisiae BGL2 gene product, a cell wall endo-β-1,3-glucanase
    • 5. Mrsa, V., Klebl, F. & Tanner, W. (1993) Purification and characterization of the Saccharomyces cerevisiae BGL2 gene product, a cell wall endo-β-1,3-glucanase. J. Bacteriol. 175, 2102-2106.
    • (1993) J. Bacteriol. , vol.175 , pp. 2102-2106
    • Mrsa, V.1    Klebl, F.2    Tanner, W.3
  • 6
    • 0026578808 scopus 로고
    • Three N-terminal domains of β-1,3-glucanase A1 are involved in binding to insoluble β-1,3-glucan
    • 6. Watanabe, T., Oyanagi, W., Suzuki, K., Ohnishi, K. & Tanaka, H. (1992) Three N-terminal domains of β-1,3-glucanase A1 are involved in binding to insoluble β-1,3-glucan. J. Bacteriol. 174, 186-190.
    • (1992) J. Bacteriol. , vol.174 , pp. 186-190
    • Watanabe, T.1    Oyanagi, W.2    Suzuki, K.3    Ohnishi, K.4    Tanaka, H.5
  • 7
    • 0027332216 scopus 로고
    • Purification and characterization of four extracellular 1,3-β-glucanases of Botrytis cinerea
    • 7. Stahmann, K.P., Schimz, K.L. & Sahm, H. (1993) Purification and characterization of four extracellular 1,3-β-glucanases of Botrytis cinerea. J. Gen. Microbiol. 139, 2833-2840.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2833-2840
    • Stahmann, K.P.1    Schimz, K.L.2    Sahm, H.3
  • 8
    • 0000991087 scopus 로고
    • Purification and characterization of an endo-1,3-β-D-glucanase from Trichoderma longibrachiatum
    • 8. Tangarone, B., Royer, J.C. & Nakas, J.P. (1989) Purification and characterization of an endo-1,3-β-D-glucanase from Trichoderma longibrachiatum. Appl. Environ. Microbiol. 55, 177-184.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 177-184
    • Tangarone, B.1    Royer, J.C.2    Nakas, J.P.3
  • 9
    • 0348058184 scopus 로고    scopus 로고
    • Purification and characterization of an endo-β-1,3-glucanase from Trichoderma harzianum
    • 9. Noronha, E.F. & Ulhoa, C.J. (1996) Purification and characterization of an endo-β-1,3-glucanase from Trichoderma harzianum. Can. J. Microbiol. 42, 1039-1044.
    • (1996) Can. J. Microbiol. , vol.42 , pp. 1039-1044
    • Noronha, E.F.1    Ulhoa, C.J.2
  • 10
    • 0028970716 scopus 로고
    • A novel endo-β-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum
    • 10. de la Cruz, J., Pintor-Toro, J.A., Benítez, T., Llobell, A. & Romero, L.C. (1995) A novel endo-β-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum. J. Bacteriol. 177, 6937-6945.
    • (1995) J. Bacteriol. , vol.177 , pp. 6937-6945
    • De La Cruz, J.1    Pintor-Toro, J.A.2    Benítez, T.3    Llobell, A.4    Romero, L.C.5
  • 12
    • 0028987555 scopus 로고
    • Purification and characterization of an endo-β-1,6-glucanase from Trichoderma harzianum related to its mycoparasitism
    • 12. de la Cruz, J., Pintor-Toro, J.A., Benítez, T. & Llobell, A. (1995) Purification and characterization of an endo-β-1,6-glucanase from Trichoderma harzianum related to its mycoparasitism. J. Bacteriol. 177, 1864-1987.
    • (1995) J. Bacteriol. , vol.177 , pp. 1864-1987
    • De La Cruz, J.1    Pintor-Toro, J.A.2    Benítez, T.3    Llobell, A.4
  • 14
    • 0009677249 scopus 로고
    • A β-1,6-glucan 6-glucanohydrolase from Gibberelia fijikuroi
    • 14. Shibata, Y. & Fujimbara, T. (1973) A β-1,6-glucan 6-glucanohydrolase from Gibberelia fijikuroi. J. Ferment. Technol. 51, 216-226.
    • (1973) J. Ferment. Technol. , vol.51 , pp. 216-226
    • Shibata, Y.1    Fujimbara, T.2
  • 15
    • 0017282677 scopus 로고
    • Lysis of yeast cell walls. Lytic β-1,6-glucanase from Bacillus circulans WL-12
    • 15. Rombouts, F.M. & Phaff, H.J. (1976) Lysis of yeast cell walls. Lytic β-1,6-glucanase from Bacillus circulans WL-12. Eur. J. Biochem. 63, 109-120.
    • (1976) Eur. J. Biochem. , vol.63 , pp. 109-120
    • Rombouts, F.M.1    Phaff, H.J.2
  • 16
    • 85004579791 scopus 로고
    • Purification and some properties of an endo-β-1,6-glucanase from Neurospora crassa
    • 16. Hiura, N., Nakajima, T. & Matsuda, K. (1987) Purification and some properties of an endo-β-1,6-glucanase from Neurospora crassa. Agric. Biol. Chem. 51, 3315-3321.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 3315-3321
    • Hiura, N.1    Nakajima, T.2    Matsuda, K.3
  • 17
    • 0029844533 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular (l→6)-β-glucanase from the filamentous fungus Acremonium persicinum
    • 17. Pitson, S.M., Seviour, R.J., McDougall, B.M., Stone, B.A. & Sadek, M. (1996) Purification and characterization of an extracellular (l→6)-β-glucanase from the filamentous fungus Acremonium persicinum. Biochem. J. 316, 841-846.
    • (1996) Biochem. J. , vol.316 , pp. 841-846
    • Pitson, S.M.1    Seviour, R.J.2    McDougall, B.M.3    Stone, B.A.4    Sadek, M.5
  • 19
    • 0002096967 scopus 로고
    • Trichoderma and Gliocladium: Biology, ecology and potential for biocontrol
    • 19. Papavizas, G.C. (1985) Trichoderma and Gliocladium: biology, ecology and potential for biocontrol. Annu. Rev. Phytopathol. 23, 23-54.
    • (1985) Annu. Rev. Phytopathol. , vol.23 , pp. 23-54
    • Papavizas, G.C.1
  • 21
    • 0000330438 scopus 로고
    • Degradation of plant pathogenic fungi by Trichoderma harzianum
    • 21. Elad, Y., Chet, I. & Henis, Y. (1982) Degradation of plant pathogenic fungi by Trichoderma harzianum. Can. J. Microbiol. 28, 719-725.
    • (1982) Can. J. Microbiol. , vol.28 , pp. 719-725
    • Elad, Y.1    Chet, I.2    Henis, Y.3
  • 22
    • 0025880428 scopus 로고
    • Regulation of chitinase synthesis in Trichoderma harzianum
    • 22. Ulhoa, C.J. & Peberdy, J.F. (1991) Regulation of chitinase synthesis in Trichoderma harzianum. J. Gen. Microbiol. 137, 2163-2169.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2163-2169
    • Ulhoa, C.J.1    Peberdy, J.F.2
  • 24
    • 0023982028 scopus 로고
    • Fractionation of extracellular enzymes from a mycoparasitic strain of Trichoderma harzianum
    • 24. Ridout, C.J., Coley-Smith, J.R. & Lynch, J.M. (1988) Fractionation of extracellular enzymes from a mycoparasitic strain of Trichoderma harzianum. Enzyme Microb. Technol. 10, 180-187.
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 180-187
    • Ridout, C.J.1    Coley-Smith, J.R.2    Lynch, J.M.3
  • 25
    • 0027245389 scopus 로고
    • Molecular characterization of the proteinase-encoding gene, prb1, related to mycoparasitism by Trichoderma harzianum
    • 25. Geremía, R., Goldman, G.H., Jacobs, D., Ardiles, W., Vila, S.B., van Montagu, M. & Herrera-Estrella, A. (1993) Molecular characterization of the proteinase-encoding gene, prb1, related to mycoparasitism by Trichoderma harzianum. Mol. Microbiol. 8, 603-613.
    • (1993) Mol. Microbiol. , vol.8 , pp. 603-613
    • Geremía, R.1    Goldman, G.H.2    Jacobs, D.3    Ardiles, W.4    Vila, S.B.5    Van Montagu, M.6    Herrera-Estrella, A.7
  • 26
    • 0014243809 scopus 로고
    • Cell wall chemistry, morphogenesis and taxonomy
    • 26. Bartnicki-García, S. (1968) Cell wall chemistry, morphogenesis and taxonomy. Annu. Rev. Microbiol. 22, 87-109.
    • (1968) Annu. Rev. Microbiol. , vol.22 , pp. 87-109
    • Bartnicki-García, S.1
  • 28
    • 0029061762 scopus 로고
    • Molecular characterization and heterologous expression of an endo-β-1,6-glucanase gene from the mycoparasitic fungus trichoderma harzianum
    • 28. Lora, J.M., de la Cruz, J., Bernítez, T., Llobell, A. & Pintor-Toro, J.A. (1995) Molecular characterization and heterologous expression of an endo-β-1,6-glucanase gene from the mycoparasitic fungus Trichoderma harzianum. Mol. Gen. Genet. 247, 639-645.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 639-645
    • Lora, J.M.1    De La Cruz, J.2    Bernítez, T.3    Llobell, A.4    Pintor-Toro, J.A.5
  • 29
    • 0016380710 scopus 로고
    • Glucanases in Schizosaccharomyces. Isolation and properties of the cell wall-associated β-1,3-glucanases
    • 29. Fleet, G.H. & Phaff, H.J. (1974) Glucanases in Schizosaccharomyces. Isolation and properties of the cell wall-associated β-1,3-glucanases. J. Biol. Chem. 249, 1717-1728.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1717-1728
    • Fleet, G.H.1    Phaff, H.J.2
  • 30
    • 33750423631 scopus 로고
    • Notes in sugar determination
    • 30. Somogyi, M. (1952) Notes in sugar determination. J. Biol. Chem. 195, 19-23.
    • (1952) J. Biol. Chem. , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 31
    • 0002440017 scopus 로고
    • Colorimetric analysis of sugars
    • 31. Nelson, N.J. (1955) Colorimetric analysis of sugars. Methods Enzymol. 3, 85-86.
    • (1955) Methods Enzymol. , vol.3 , pp. 85-86
    • Nelson, N.J.1
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • 32. Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • 33. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0033001727 scopus 로고    scopus 로고
    • Detection of β-1,6-glucanase isozymes from Trichoderma strains in sodium dodecyl sulphate-polyacrylamide gel electrophoresis and isoelectrofocusing gels
    • 34. Soler, A., de la Cruz, J. & Llobell, A. (1999) Detection of β-1,6-glucanase isozymes from Trichoderma strains in sodium dodecyl sulphate-polyacrylamide gel electrophoresis and isoelectrofocusing gels. J. Microbiol. Methods 35, 245-251.
    • (1999) J. Microbiol. Methods , vol.35 , pp. 245-251
    • Soler, A.1    De La Cruz, J.2    Llobell, A.3
  • 35
    • 0020084688 scopus 로고
    • A highly sensitive periodic acid-silver stain for 1,2-diol groups of glicoproteins and polysaccharides in polyacrylamide gels
    • 35. Dubray, G. & Bezard, G. (1982) A highly sensitive periodic acid-silver stain for 1,2-diol groups of glicoproteins and polysaccharides in polyacrylamide gels. Anal. Biochem. 119, 325-329.
    • (1982) Anal. Biochem. , vol.119 , pp. 325-329
    • Dubray, G.1    Bezard, G.2
  • 36
    • 0025975260 scopus 로고
    • Nucleotide sequence of the exo-β-1,3-glucanase-encoding gene, EXG1, of the yeast Saccharomyces cerevisiae
    • 36. Vázquez de Aldana, C.R., Correa, J., San Segundo, P., Bueno, A., Nebreda, A.R., Mendez, E. & del Rey, F. (1991) Nucleotide sequence of the exo-β-1,3-glucanase-encoding gene, EXG1, of the yeast Saccharomyces cerevisiae. Gene 97, 173-182.
    • (1991) Gene , vol.97 , pp. 173-182
    • Vázquez De Aldana, C.R.1    Correa, J.2    San Segundo, P.3    Bueno, A.4    Nebreda, A.R.5    Mendez, E.6    Del Rey, F.7
  • 37
    • 0026606338 scopus 로고
    • O-glycosilation in Aspergillus glucoamilase. Conformation and role in binding
    • 37. Williamson, G., Belshaw, N.J. & Williamson, M.P. (1992) O-glycosilation in Aspergillus glucoamilase. Conformation and role in binding. Biochem. J. 282, 423-428.
    • (1992) Biochem. J. , vol.282 , pp. 423-428
    • Williamson, G.1    Belshaw, N.J.2    Williamson, M.P.3
  • 38
    • 0000234469 scopus 로고
    • Several 'pathogenesis-related' proteins in potato are 1,3-β-glucanases and chitinases
    • 38. Kombrink, E., Schröder, M. & Hahlbrock, K. (1988) Several 'pathogenesis-related' proteins in potato are 1,3-β-glucanases and chitinases. Proc. Natl Acad. Sci. USA 85, 782-786.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 782-786
    • Kombrink, E.1    Schröder, M.2    Hahlbrock, K.3
  • 39
    • 0023473794 scopus 로고
    • Rapid isoelectrofocusing in a vertical polyacrylamide minigel system
    • 39. Roberstson, E.F., Dannelly, H.K., Malloy, P.J. & Reeve, H.C. (1987) Rapid isoelectrofocusing in a vertical polyacrylamide minigel system. Anal. Biochem. 167, 290-294.
    • (1987) Anal. Biochem. , vol.167 , pp. 290-294
    • Roberstson, E.F.1    Dannelly, H.K.2    Malloy, P.J.3    Reeve, H.C.4
  • 40
    • 0000206650 scopus 로고
    • Enzymatic hydrolysis of yeast cell walls. I. Isolation of wall-decomposing organisms and separation and purification of lytic enzymes
    • 40. Tanaka, H. & Phaff, H.J. (1965) Enzymatic hydrolysis of yeast cell walls. I. Isolation of wall-decomposing organisms and separation and purification of lytic enzymes. J. Bacteriol. 89, 1570-1580.
    • (1965) J. Bacteriol. , vol.89 , pp. 1570-1580
    • Tanaka, H.1    Phaff, H.J.2
  • 41
    • 0027728296 scopus 로고
    • Barley pathogenesis-related proteins with fungal cell wall lytic activity inhibit the growth of yeast
    • 41. Grenier, J., Potvin, C. & Asselin, A. (1993) Barley pathogenesis-related proteins with fungal cell wall lytic activity inhibit the growth of yeast. Plant Physiol. 103, 1277-1283.
    • (1993) Plant Physiol. , vol.103 , pp. 1277-1283
    • Grenier, J.1    Potvin, C.2    Asselin, A.3
  • 43
    • 0023439754 scopus 로고
    • Expression, glycosylation and secretion of fungal hydrolases in yeast
    • 43. Yoshizumi, H. & Ashikari, T. (1987) Expression, glycosylation and secretion of fungal hydrolases in yeast. Trends Biotechnol. 5, 277-281.
    • (1987) Trends Biotechnol. , vol.5 , pp. 277-281
    • Yoshizumi, H.1    Ashikari, T.2
  • 44
    • 0023650010 scopus 로고
    • Heterogeneous glycosylation of the EXG1 gene product accounts for two extracellular exo-β-glucanases of Saccharomyces cerevisiae
    • 44. Nebreda, A.R., Vázquez de Aldana, C.R., Villa, T.G., Villanueva, J.R. & del Rey, F. (1987) Heterogeneous glycosylation of the EXG1 gene product accounts for two extracellular exo-β-glucanases of Succharomyces cerevisiae. FEBS Lett. 220, 27-30.
    • (1987) FEBS Lett. , vol.220 , pp. 27-30
    • Nebreda, A.R.1    Vázquez De Aldana, C.R.2    Villa, T.G.3    Villanueva, J.R.4    Del Rey, F.5
  • 45
    • 14744300573 scopus 로고
    • The two major xylanases from Trichoderma reesei: Characterization of both enzymes and genes
    • 45. Torronen, A., Mach, R., Messner, M., Gonzalez, R., Kalkkinen, N., Harkki, A. & Kubicek, C. (1992) The two major xylanases from Trichoderma reesei: characterization of both enzymes and genes. Biol Technol. 10, 1461-1465.
    • (1992) Biol Technol. , vol.10 , pp. 1461-1465
    • Torronen, A.1    Mach, R.2    Messner, M.3    Gonzalez, R.4    Kalkkinen, N.5    Harkki, A.6    Kubicek, C.7
  • 46
    • 0016260554 scopus 로고
    • Purification and properties of an endo-β-1,6-glucanase from Rhizopus chinensis R-69
    • 46. Yamamoto, S., Kobayashi, R. & Nagasaki, S. (1974) Purification and properties of an endo-β-1,6-glucanase from Rhizopus chinensis R-69. Agric. Biol. Chem. 38, 1493-1500.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 1493-1500
    • Yamamoto, S.1    Kobayashi, R.2    Nagasaki, S.3
  • 47
    • 0028055658 scopus 로고
    • Purification, characterization, and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetyl-β-glucosaminidase from Trichoderma harzianum
    • 47. Lorito, M., Hayes, C.K., di Pietro, A., Woo, S.L. & Harman, G.E. (1994) Purification, characterization, and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetyl-β-glucosaminidase from Trichoderma harzianum. Phytopathology 84, 398-405.
    • (1994) Phytopathology , vol.84 , pp. 398-405
    • Lorito, M.1    Hayes, C.K.2    Di Pietro, A.3    Woo, S.L.4    Harman, G.E.5
  • 48
    • 0000439771 scopus 로고
    • Endochitinase from Gliocladium virens: Isolation, characterization and synergistic antifungal activity in combination with Gliotoxin
    • 48. di Pietro, A., Lorito, M., Hayes, C.K., Broadway, R.M. & Harman, G.E. (1993) Endochitinase from Gliocladium virens: isolation, characterization and synergistic antifungal activity in combination with Gliotoxin. Phytopathology 83, 308-313.
    • (1993) Phytopathology , vol.83 , pp. 308-313
    • Di Pietro, A.1    Lorito, M.2    Hayes, C.K.3    Broadway, R.M.4    Harman, G.E.5
  • 49
    • 0000101691 scopus 로고
    • Degradation of fungal cell walls by lytic enzymes from Trichoderma harzianum
    • 49. Sivan, A. & Chet, I. (1989) Degradation of fungal cell walls by lytic enzymes from Trichoderma harzianum. J. Gen. Microbiol. 135, 675-682.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 675-682
    • Sivan, A.1    Chet, I.2
  • 50
    • 0028100107 scopus 로고
    • Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics, molecular mechanisms involved in the antagonism action of Trichoderma harzianum against phytopathogenic fungi
    • 50. Schirmböck, M., Lorito, M., Wang, Y.-L., Arisan-Atac, I., Scala, F. & Kubicek, C.P. (1994) Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics, molecular mechanisms involved in the antagonism action of Trichoderma harzianum against phytopathogenic fungi. Appl. Environ. Microbiol. 60, 4364-4370.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4364-4370
    • Schirmböck, M.1    Lorito, M.2    Wang, Y.-L.3    Arisan-Atac, I.4    Scala, F.5    Kubicek, C.P.6
  • 51
    • 0028324914 scopus 로고
    • Synergistic combinations of cell wall degrading enzymes and different antifungal compounds enhances inhibition of spore germination
    • 51. Lorito, M., Peterbauer, M., Hayes, C.K., Woo, S.L. & Harman, G.E. (1994) Synergistic combinations of cell wall degrading enzymes and different antifungal compounds enhances inhibition of spore germination. Microbiology 140, 623-629.
    • (1994) Microbiology , vol.140 , pp. 623-629
    • Lorito, M.1    Peterbauer, M.2    Hayes, C.K.3    Woo, S.L.4    Harman, G.E.5


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