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Volumn 45, Issue 51, 2006, Pages 15444-15457

In vitro biosynthesis of violacein from L-tryptophan by the enzymes VioA-E from Chromobacterium violaceum

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOBACTERIUM VIOLACEUM; CHROMOPYRROLIC ACIDS; FLAVIN DEPENDENT OXYGENASES; PROVIOLACEIN;

EID: 33845934004     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061998z     Document Type: Article
Times cited : (140)

References (54)
  • 3
    • 0003355098 scopus 로고
    • Incorporation of C14-labeled substrates into violacein
    • Demoss, R. D., and Evans, N. R. (1960) Incorporation of C14-labeled substrates into violacein, J. Bacteriol. 79, 729-733.
    • (1960) J. Bacteriol , vol.79 , pp. 729-733
    • Demoss, R.D.1    Evans, N.R.2
  • 4
    • 0001261716 scopus 로고
    • Biosynthesis of violacein: A novel rearrangement in tryptophan metabolism with a 1,2-shift of the inodle ring
    • Hoshino, T., Kondo, T., Uchiyama, T., and Ogasawara, N. (1987) Biosynthesis of violacein: a novel rearrangement in tryptophan metabolism with a 1,2-shift of the inodle ring, Agric. Biol. Chem. 51, 965-968.
    • (1987) Agric. Biol. Chem , vol.51 , pp. 965-968
    • Hoshino, T.1    Kondo, T.2    Uchiyama, T.3    Ogasawara, N.4
  • 5
    • 0003468279 scopus 로고
    • Matiere colarante se formant dans la cole de farine
    • Boisbaudran, L. D. (1882) Matiere colarante se formant dans la cole de farine, Compt. Rend. 94, 562.
    • (1882) Compt. Rend , vol.94 , pp. 562
    • Boisbaudran, L.D.1
  • 6
    • 2542454687 scopus 로고    scopus 로고
    • Genetic analysis of violacein biosynthesis by Chromobacterium violaceum
    • Antonio, R. V., and Creczynski-Pasa, T. B. (2004) Genetic analysis of violacein biosynthesis by Chromobacterium violaceum, Genet. Mol. Res. 3, 85-91.
    • (2004) Genet. Mol. Res , vol.3 , pp. 85-91
    • Antonio, R.V.1    Creczynski-Pasa, T.B.2
  • 7
    • 0000114258 scopus 로고
    • Bacterial chemistry-II: Antimicrobial photoproduct from pigment of Chromobacterium violaceum
    • Duran, N., Erazo, S., and Campos, V. (1983) Bacterial chemistry-II: antimicrobial photoproduct from pigment of Chromobacterium violaceum, An. Acad. Bras. Cienc. 55, 231-234.
    • (1983) An. Acad. Bras. Cienc , vol.55 , pp. 231-234
    • Duran, N.1    Erazo, S.2    Campos, V.3
  • 8
    • 0034805976 scopus 로고    scopus 로고
    • Chromobacterium violaceum: A review of pharmacological and industiral perspectives
    • Duran, N., and Menck, C. F. (2001) Chromobacterium violaceum: a review of pharmacological and industiral perspectives, Crit. Rev. Microbiol 27, 201-222.
    • (2001) Crit. Rev. Microbiol , vol.27 , pp. 201-222
    • Duran, N.1    Menck, C.F.2
  • 9
    • 0002272044 scopus 로고
    • Violacein, an antibiotic pigment produced by Chromobacterium violaceum
    • Lichstein, H. C., and Van de Sand, V. F. (1945) Violacein, an antibiotic pigment produced by Chromobacterium violaceum, J. Infect. Dis. 76, 47-51.
    • (1945) J. Infect. Dis , vol.76 , pp. 47-51
    • Lichstein, H.C.1    Van de Sand, V.F.2
  • 11
    • 33845961562 scopus 로고    scopus 로고
    • May, G, Brummer, B, and Ott, H. Treatment of prophylaxis of polio and herpes virus infections comprises admin, of 3-(1,2-dihydro-5-(5-hydroxy-1H- indol-3-yl)-2-oxo-3H-pyrrole-3-ylidene)-1,3-dihydro-2H-indol-2-one. Ger OffenDE 3935066, 25 April, 1991
    • May, G., Brummer, B., and Ott, H. Treatment of prophylaxis of polio and herpes virus infections comprises admin, of 3-(1,2-dihydro-5-(5-hydroxy-1H- indol-3-yl)-2-oxo-3H-pyrrole-3-ylidene)-1,3-dihydro-2H-indol-2-one. Ger OffenDE 3935066, 25 April, 1991.
  • 13
    • 33644867406 scopus 로고    scopus 로고
    • Violacein synergistically increases 5-fluorouracil cytotoxicity, induces apoptosis and inhibits Akt-mediated signal transduction in human colorectal cancer cells
    • Kodach, L. L., Bos, C. L., Duran, N., Peppelenbosch, M. P., Ferreira, C. V., and Hardwick, J. C. (2006) Violacein synergistically increases 5-fluorouracil cytotoxicity, induces apoptosis and inhibits Akt-mediated signal transduction in human colorectal cancer cells, Carcinogenesis 27, 508-516.
    • (2006) Carcinogenesis , vol.27 , pp. 508-516
    • Kodach, L.L.1    Bos, C.L.2    Duran, N.3    Peppelenbosch, M.P.4    Ferreira, C.V.5    Hardwick, J.C.6
  • 14
    • 0345269812 scopus 로고    scopus 로고
    • Violacein and its beta-cyclodextrin complexes induce apoptosis and differentiation in HL60 cells
    • Melo, P. S., Justo, G. Z., de Azevedo, M. B., Duran, N., and Haun, M. (2003) Violacein and its beta-cyclodextrin complexes induce apoptosis and differentiation in HL60 cells, Toxicology 186, 217-225.
    • (2003) Toxicology , vol.186 , pp. 217-225
    • Melo, P.S.1    Justo, G.Z.2    de Azevedo, M.B.3    Duran, N.4    Haun, M.5
  • 20
    • 0024624735 scopus 로고
    • Bacterial chemistry-III: Preliminary studies on trypanosomal activities of Chromobacterium violaceum products
    • Duran, N., Campos, V., Riveros, R., Joyas, A., Pereira, M. F., and Haun, M. (1989) Bacterial chemistry-III: preliminary studies on trypanosomal activities of Chromobacterium violaceum products, An. Acad. Bras. Cienc. 61, 31-36.
    • (1989) An. Acad. Bras. Cienc , vol.61 , pp. 31-36
    • Duran, N.1    Campos, V.2    Riveros, R.3    Joyas, A.4    Pereira, M.F.5    Haun, M.6
  • 21
    • 0034812079 scopus 로고    scopus 로고
    • Antileishmanial activity of the violacein extracted from Chromobacterium violaceum
    • Leon, L. L., Miranda, C. C., De Souza, A. O., and Duran, N. (2001) Antileishmanial activity of the violacein extracted from Chromobacterium violaceum, J. Antimicrob. Chemother. 48, 449-450.
    • (2001) J. Antimicrob. Chemother , vol.48 , pp. 449-450
    • Leon, L.L.1    Miranda, C.C.2    De Souza, A.O.3    Duran, N.4
  • 22
    • 0037863996 scopus 로고    scopus 로고
    • Evaluation of the antiulcerogenic activity of violacein and its modulation by the inclusion complexation with beta-cyclodextrin
    • Duran, N., Justo, G. Z., Melo, P. S., De Azevedo, M. B., Brito, A. R., Almeida, A. B., and Haun, M. (2003) Evaluation of the antiulcerogenic activity of violacein and its modulation by the inclusion complexation with beta-cyclodextrin, Can. J. Physiol. Pharmacol. 81, 387-396.
    • (2003) Can. J. Physiol. Pharmacol , vol.81 , pp. 387-396
    • Duran, N.1    Justo, G.Z.2    Melo, P.S.3    De Azevedo, M.B.4    Brito, A.R.5    Almeida, A.B.6    Haun, M.7
  • 24
    • 0023639472 scopus 로고
    • Biosynthesis of violacein: Origins of hydrogen, nitrogen and oxygen atoms in the 2-pyrrolidone nucleus
    • Hoshino, T., Takano, T., Hori, S., and Ogasawara, N. (1987) Biosynthesis of violacein: origins of hydrogen, nitrogen and oxygen atoms in the 2-pyrrolidone nucleus, Agric. Biol. Chem. 51, 2733-2741.
    • (1987) Agric. Biol. Chem , vol.51 , pp. 2733-2741
    • Hoshino, T.1    Takano, T.2    Hori, S.3    Ogasawara, N.4
  • 25
    • 33746608987 scopus 로고    scopus 로고
    • Biological formation of pyrroles: Nature's logic and enzymatic machinery
    • Walsh, C. T., Garneau-Tsodikova, S., and Howard-Jones, A. R. (2006) Biological formation of pyrroles: nature's logic and enzymatic machinery, Nat. Prod. Rep. 23, 517-531.
    • (2006) Nat. Prod. Rep , vol.23 , pp. 517-531
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Howard-Jones, A.R.3
  • 26
    • 0034151792 scopus 로고    scopus 로고
    • Biosynthesis of violacein: Intact incorporation of the tryptophan molecule on the oxindole side, with intramolecular rearrangement of the indole ring on the 5-hydroxyindole side
    • Momen, A. Z., and Hoshino, T. (2000) Biosynthesis of violacein: intact incorporation of the tryptophan molecule on the oxindole side, with intramolecular rearrangement of the indole ring on the 5-hydroxyindole side, Biosci. Biotechnol. Biochem. 64, 539-549.
    • (2000) Biosci. Biotechnol. Biochem , vol.64 , pp. 539-549
    • Momen, A.Z.1    Hoshino, T.2
  • 27
    • 0141426670 scopus 로고    scopus 로고
    • Mechanism of aromatic hydroxylation by an activated FeIV=O core in tetrahydrobiopterin- dependent hydroxylases
    • Bassan, A., Blomberg, M. R., and Siegbahn, P. E. (2003) Mechanism of aromatic hydroxylation by an activated FeIV=O core in tetrahydrobiopterin- dependent hydroxylases, Chemistry 9, 4055-4067.
    • (2003) Chemistry , vol.9 , pp. 4055-4067
    • Bassan, A.1    Blomberg, M.R.2    Siegbahn, P.E.3
  • 28
    • 0025163193 scopus 로고
    • Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis
    • Hashim, M. F., Hakamatsuka, T., Ebizuka, Y., and Sankawa, U. (1990) Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis, FEBS Lett. 271, 219-222.
    • (1990) FEBS Lett , vol.271 , pp. 219-222
    • Hashim, M.F.1    Hakamatsuka, T.2    Ebizuka, Y.3    Sankawa, U.4
  • 29
    • 33646592543 scopus 로고    scopus 로고
    • Functional genomic analysis of alkaloid biosynthesis in Hyoscyamus niger reveals a cytochrome P450 involved in littorine rearrangement
    • Li, R., Reed, D. W., Liu, E., Nowak, J., Pelcher, L. E., Page, J. E., and Covello, P. S. (2006) Functional genomic analysis of alkaloid biosynthesis in Hyoscyamus niger reveals a cytochrome P450 involved in littorine rearrangement, Chem. Biol. 13, 513-520.
    • (2006) Chem. Biol , vol.13 , pp. 513-520
    • Li, R.1    Reed, D.W.2    Liu, E.3    Nowak, J.4    Pelcher, L.E.5    Page, J.E.6    Covello, P.S.7
  • 31
    • 0035963668 scopus 로고    scopus 로고
    • Cloning and heterologous expression of a natural product biosynthetic gene cluster from eDNA
    • Brady, S. F., Chao, C. J., Handelsman, J., and Clardy, J. (2001) Cloning and heterologous expression of a natural product biosynthetic gene cluster from eDNA, Org. Lett. 3, 1981-1984.
    • (2001) Org. Lett , vol.3 , pp. 1981-1984
    • Brady, S.F.1    Chao, C.J.2    Handelsman, J.3    Clardy, J.4
  • 32
    • 0025832316 scopus 로고
    • Cloning and heterologous expression of the violacein biosynthesis gene cluster from Chromobacterium violaceum
    • Pemberton, J. M., Vincent, K. M., and Penfold, R. J. (1991) Cloning and heterologous expression of the violacein biosynthesis gene cluster from Chromobacterium violaceum, Curr. Microbiol. 22, 355-358.
    • (1991) Curr. Microbiol , vol.22 , pp. 355-358
    • Pemberton, J.M.1    Vincent, K.M.2    Penfold, R.J.3
  • 33
    • 0012569067 scopus 로고    scopus 로고
    • Characterization of the biosynthetic gene cluster of rebeccamycin from Lechevalieria aerocolonigenes ATCC 39243
    • Onaka, H., Taniguchi, S., Igarashi, Y., and Furumai, T. (2003) Characterization of the biosynthetic gene cluster of rebeccamycin from Lechevalieria aerocolonigenes ATCC 39243, Biosci. Biotechnol. Biochem. 67, 127-138.
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 127-138
    • Onaka, H.1    Taniguchi, S.2    Igarashi, Y.3    Furumai, T.4
  • 34
    • 0036952785 scopus 로고    scopus 로고
    • Cloning of the staurosporine biosynthetic gene cluster from Streptomyces sp. TP-A0274 and its heterologous expression in Streptomyces lividans
    • Onaka, H., Taniguchi, S., Igarashi, Y., and Furumai, T. (2002) Cloning of the staurosporine biosynthetic gene cluster from Streptomyces sp. TP-A0274 and its heterologous expression in Streptomyces lividans, J. Antibiot. (Tokyo) 55, 1063-1071.
    • (2002) J. Antibiot. (Tokyo) , vol.55 , pp. 1063-1071
    • Onaka, H.1    Taniguchi, S.2    Igarashi, Y.3    Furumai, T.4
  • 36
    • 28544449005 scopus 로고    scopus 로고
    • Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD
    • Howard-Jones, A. R., and Walsh, C. T. (2005) Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD, Biochemistry 44, 15652-15663.
    • (2005) Biochemistry , vol.44 , pp. 15652-15663
    • Howard-Jones, A.R.1    Walsh, C.T.2
  • 37
    • 0000307640 scopus 로고
    • A new metabolite of tryptophan, chromopyrrolic acid, produced by Chromobacterium violaceum
    • Hoshino, T., Kojima, Y., Hayashi, T., Uchiyama, T., and Kaneko, K. (1993) A new metabolite of tryptophan, chromopyrrolic acid, produced by Chromobacterium violaceum, Biosci. Biotech. Biochem. 57, 775-781.
    • (1993) Biosci. Biotech. Biochem , vol.57 , pp. 775-781
    • Hoshino, T.1    Kojima, Y.2    Hayashi, T.3    Uchiyama, T.4    Kaneko, K.5
  • 38
    • 37049076961 scopus 로고
    • Biosynthesis of violacein: Oxygenation at the 2-position of the indole ring and structures of proviolacein, prodeoxyviolacein and pseudoviolacein, the plausible biosynthetic intermediates of violacein and deoxyviolacein
    • Hoshino, T., Hayashi, T., and Odajima, T. (1995) Biosynthesis of violacein: oxygenation at the 2-position of the indole ring and structures of proviolacein, prodeoxyviolacein and pseudoviolacein, the plausible biosynthetic intermediates of violacein and deoxyviolacein, J. Chem. Soc. Perkin Trans. 1, 1565-1571.
    • (1995) J. Chem. Soc. Perkin Trans , vol.1 , pp. 1565-1571
    • Hoshino, T.1    Hayashi, T.2    Odajima, T.3
  • 39
    • 0000557273 scopus 로고
    • Biosynthesis of Violacein: Evidence for the intermediacy of 5-hydroxy-L-tryptophan and the structure of a new pigment, oxyviolacein, produced by the metabolism of 5-hydroxytryptophan
    • Hoshino, T., and Ogasawara, N. (1990) Biosynthesis of Violacein: Evidence for the intermediacy of 5-hydroxy-L-tryptophan and the structure of a new pigment, oxyviolacein, produced by the metabolism of 5-hydroxytryptophan, Agric. Biol. Chem. 54, 2339-2346.
    • (1990) Agric. Biol. Chem , vol.54 , pp. 2339-2346
    • Hoshino, T.1    Ogasawara, N.2
  • 40
    • 33747160432 scopus 로고    scopus 로고
    • Reevaluation of the violacein biosynthetic pathway and its relationship to indolocarbazole biosynthesis
    • Sanchez, C., Brana, A. F., Mendez, C., and Salas, J. A. (2006) Reevaluation of the violacein biosynthetic pathway and its relationship to indolocarbazole biosynthesis, Chembiochem 7, 1231-1240.
    • (2006) Chembiochem , vol.7 , pp. 1231-1240
    • Sanchez, C.1    Brana, A.F.2    Mendez, C.3    Salas, J.A.4
  • 42
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation 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
  • 43
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A., and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal. Biochem. 161, 1-15.
    • (1987) Anal. Biochem , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 44
    • 0025055440 scopus 로고
    • Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
    • Haigler, B. E., and Gibson, D. T. (1990) Purification and properties of NADH-ferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816, J. Bacteriol. 172, 457-464.
    • (1990) J. Bacteriol , vol.172 , pp. 457-464
    • Haigler, B.E.1    Gibson, D.T.2
  • 45
    • 25444465451 scopus 로고    scopus 로고
    • Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis
    • Dorrestein, P. C., Yeh, E., Garneau-Tsodikova, S., Kelleher, N. L., and Walsh, C. T. (2005) Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis, Proc. Natl. Acad. Sci. U.S.A. 102, 13843-13848.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 13843-13848
    • Dorrestein, P.C.1    Yeh, E.2    Garneau-Tsodikova, S.3    Kelleher, N.L.4    Walsh, C.T.5
  • 46
    • 84981657902 scopus 로고
    • An improved cathode for the measurement of photosynthetic oxygen evolution by isolated chloroplasts
    • Delieu, T., and Walker, D. A. (1972) An improved cathode for the measurement of photosynthetic oxygen evolution by isolated chloroplasts, New Phytol. 71, 201-225.
    • (1972) New Phytol , vol.71 , pp. 201-225
    • Delieu, T.1    Walker, D.A.2
  • 47
    • 0032567402 scopus 로고    scopus 로고
    • Molecular basis for the stabilization and inhibition of 2, 3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol
    • Vaillancourt, F. H., Han, S., Fortin, P. D., Bolin, J. T., and Eltis, L. D. (1998) Molecular basis for the stabilization and inhibition of 2, 3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol, J. Biol. Chem. 273, 34887-34895.
    • (1998) J. Biol. Chem , vol.273 , pp. 34887-34895
    • Vaillancourt, F.H.1    Han, S.2    Fortin, P.D.3    Bolin, J.T.4    Eltis, L.D.5
  • 48
    • 33751261455 scopus 로고    scopus 로고
    • Studies on the biosynthesis of violacein. Part 9. Green pigments possessing tetraindole and dipyrromethene moieties, chromoviridans and deoxychromoviridans, produced by a cell free extract of Chromobacterium violaceum and their biosynthetic origins
    • Momen, A. Z., Mizuoka, T., and Hoshino, T. (1998) Studies on the biosynthesis of violacein. Part 9. Green pigments possessing tetraindole and dipyrromethene moieties, chromoviridans and deoxychromoviridans, produced by a cell free extract of Chromobacterium violaceum and their biosynthetic origins, J. Chem. Soc., Perkin Trans. 1, 3087-3092.
    • (1998) J. Chem. Soc., Perkin Trans , vol.1 , pp. 3087-3092
    • Momen, A.Z.1    Mizuoka, T.2    Hoshino, T.3
  • 50
    • 29144525471 scopus 로고    scopus 로고
    • Direct formation of chromopyrrolic acid from the indole-3-pyruvic acid by StaD, a novel hemoprotein in indolocarbazole biosynthesis
    • Asamizu, S., Kato, Y., Igarashi, Y., Tamotsu, F., and Onaka, H. (2006) Direct formation of chromopyrrolic acid from the indole-3-pyruvic acid by StaD, a novel hemoprotein in indolocarbazole biosynthesis, Tetrahedron Lett. 47, 473-475.
    • (2006) Tetrahedron Lett , vol.47 , pp. 473-475
    • Asamizu, S.1    Kato, Y.2    Igarashi, Y.3    Tamotsu, F.4    Onaka, H.5
  • 51
    • 14644432391 scopus 로고    scopus 로고
    • Molecular analysis of the rebeccamycin-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243
    • Nishizawa, T., Aldrich, C. C., and Sherman, D. H. (2005) Molecular analysis of the rebeccamycin-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243, J. Bacteriol. 187, 2084-2092.
    • (2005) J. Bacteriol , vol.187 , pp. 2084-2092
    • Nishizawa, T.1    Aldrich, C.C.2    Sherman, D.H.3
  • 52
    • 0036048808 scopus 로고    scopus 로고
    • Correlation between pigmentation and antifouling compounds produced by Pseudoalteromonas tunicata
    • Egan, S., James, S., Holmstrom, C., and Kjelleberg, S. (2002) Correlation between pigmentation and antifouling compounds produced by Pseudoalteromonas tunicata, Environ. Microbiol. 4, 433-442.
    • (2002) Environ. Microbiol , vol.4 , pp. 433-442
    • Egan, S.1    James, S.2    Holmstrom, C.3    Kjelleberg, S.4
  • 53
    • 33745963527 scopus 로고    scopus 로고
    • Flavin redox chemistry precedes substrate chlorination during the reaction of the flavin-dependent halogenase RebH
    • Yeh, E., Cole, L. J., Barr, E. W., Bollinger, J. M., Jr., Ballou, D. P., and Walsh, C. T. (2006) Flavin redox chemistry precedes substrate chlorination during the reaction of the flavin-dependent halogenase RebH, Biochemistry 45, 7904-7912.
    • (2006) Biochemistry , vol.45 , pp. 7904-7912
    • Yeh, E.1    Cole, L.J.2    Barr, E.W.3    Bollinger Jr., J.M.4    Ballou, D.P.5    Walsh, C.T.6
  • 54
    • 15244349569 scopus 로고    scopus 로고
    • Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis
    • Yeh, E., Garneau, S., and Walsh, C. T. (2005) Robust in vitro activity of RebF and RebH, a two-component reductase/halogenase, generating 7-chlorotryptophan during rebeccamycin biosynthesis, Proc. Natl. Acad. Sci. U.S.A. 102, 3960-3965.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 3960-3965
    • Yeh, E.1    Garneau, S.2    Walsh, C.T.3


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