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Volumn 394, Issue 3, 2006, Pages 657-664

L-cysteate sulpho-lyase, a widespread pyridoxal 5′-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3T

Author keywords

Cysteate dissimilation; Desulphonation; Pyridoxal 5 phosphate; Sequence comparisons; Sulphite exporter

Indexed keywords

AMINO ACIDS; AMMONIA; BACTERIA; CARBON; CELLS; DEGRADATION; GEL PERMEATION CHROMATOGRAPHY; GENES;

EID: 32344450427     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051311     Document Type: Article
Times cited : (40)

References (55)
  • 1
    • 0001551136 scopus 로고
    • The identification of amino-acids derived from cysteine in chemically modified wool
    • Consden, R., Gordon, A. H. and Martin, A. J. P. (1946) The identification of amino-acids derived from cysteine in chemically modified wool. Biochem. J. 40, 580-582
    • (1946) Biochem. J. , vol.40 , pp. 580-582
    • Consden, R.1    Gordon, A.H.2    Martin, A.J.P.3
  • 2
    • 85047691482 scopus 로고
    • Verwertung anorganischer schwefelquellen durch Staphylococcus aureus-stämme
    • Seltmann, G. and Voigt, W. (1977) Verwertung anorganischer Schwefelquellen durch Staphylococcus aureus-Stämme. Z. Allg. Mikrobiol. 17, 437-450
    • (1977) Z. Allg. Mikrobiol. , vol.17 , pp. 437-450
    • Seltmann, G.1    Voigt, W.2
  • 3
    • 0019723774 scopus 로고
    • Presence of cysteic acid in the sporangium and its metabolic pathway during sporulation of Bacillus subtilis NRRL B558
    • Koshikawa, T., Nakashio, S., Kusuyama, K., Ichikawa, T. and Kondo, M. (1981) Presence of cysteic acid in the sporangium and its metabolic pathway during sporulation of Bacillus subtilis NRRL B558. J. Gen. Microbiol. 124, 415-423
    • (1981) J. Gen. Microbiol. , vol.124 , pp. 415-423
    • Koshikawa, T.1    Nakashio, S.2    Kusuyama, K.3    Ichikawa, T.4    Kondo, M.5
  • 4
    • 0021238422 scopus 로고
    • Biosynthesis of the sulfonolipid 2-amino-3-hydroxy-15-methylhexadecane-1- sulfonic acid in the gliding bacterium Cytophaga johnsonae
    • White, R. H. (1984) Biosynthesis of the sulfonolipid 2-amino-3-hydroxy- 15-methylhexadecane-1-sulfonic acid in the gliding bacterium Cytophaga johnsonae. J. Bacteriol. 159, 42-46
    • (1984) J. Bacteriol. , vol.159 , pp. 42-46
    • White, R.H.1
  • 5
    • 0018797854 scopus 로고
    • Studies on the biosynthesis of sulfolipids in the diatom Nitzschia alba
    • Anderson, R., Kates, M. and Volcani, B. E. (1979) Studies on the biosynthesis of sulfolipids in the diatom Nitzschia alba. Biochim. Biophys. Acta 573, 557-561
    • (1979) Biochim. Biophys. Acta , vol.573 , pp. 557-561
    • Anderson, R.1    Kates, M.2    Volcani, B.E.3
  • 9
    • 0035910141 scopus 로고    scopus 로고
    • Escherichia coli utilizes methanesulfonate and L-cysteate as sole sulfur sources for growth
    • Eichhorn, E. and Leisinger, T. (2001) Escherichia coli utilizes methanesulfonate and L-cysteate as sole sulfur sources for growth. FEMS Microbiol. Lett. 205, 271-275
    • (2001) FEMS Microbiol. Lett. , vol.205 , pp. 271-275
    • Eichhorn, E.1    Leisinger, T.2
  • 10
    • 15844420095 scopus 로고    scopus 로고
    • Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA
    • Rein, U., Gueta, R., Denger, K., Ruff, J., Hollemeyer, K. and Cook, A. M. (2005) Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. Microbiology (Reading, U.K.) 151, 737-747
    • (2005) Microbiology (Reading, U.K.) , vol.151 , pp. 737-747
    • Rein, U.1    Gueta, R.2    Denger, K.3    Ruff, J.4    Hollemeyer, K.5    Cook, A.M.6
  • 11
    • 0034607799 scopus 로고    scopus 로고
    • Sulfite:Cytochrome c oxidoreductase from Thiobacillus novellus. Purification, characterization, and molecular biology of a heterodimeric member of the sulfite oxidase family
    • Kappler, U., Bennett, B., Rethmeier, J., Schwarz, G., Deutzmann, R., McEwan, A. G. and Dahl, C. (2000) Sulfite:Cytochrome c oxidoreductase from Thiobacillus novellus. Purification, characterization, and molecular biology of a heterodimeric member of the sulfite oxidase family. J. Biol. Chem. 275, 13202-13212
    • (2000) J. Biol. Chem. , vol.275 , pp. 13202-13212
    • Kappler, U.1    Bennett, B.2    Rethmeier, J.3    Schwarz, G.4    Deutzmann, R.5    McEwan, A.G.6    Dahl, C.7
  • 14
    • 1942473591 scopus 로고    scopus 로고
    • Enzymes and genes of taurine and isethionate dissimilation in Paracoccus denitrificans
    • Brüggemann, C., Denger, K., Cook, A. M. and Ruff, J. (2004) Enzymes and genes of taurine and isethionate dissimilation in Paracoccus denitrificans. Microbiology (Reading, U.K.) 150, 805-816
    • (2004) Microbiology (Reading, U.K.) , vol.150 , pp. 805-816
    • Brüggemann, C.1    Denger, K.2    Cook, A.M.3    Ruff, J.4
  • 15
    • 0022311120 scopus 로고
    • D-Cysteine desulfhydrase of Escherichia coll. Purification and characterization
    • Nagasawa, T., Ishii, T., Kumagai, H. and Yamarja, H. (1985) D-Cysteine desulfhydrase of Escherichia coll. Purification and characterization. Eur. J. Biochem. 153, 541-551
    • (1985) Eur. J. Biochem. , vol.153 , pp. 541-551
    • Nagasawa, T.1    Ishii, T.2    Kumagai, H.3    Yamarja, H.4
  • 16
    • 0035798673 scopus 로고    scopus 로고
    • Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine
    • Soutourina, J., Blanquet, S. and Plateau, P. (2001) Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to D-cysteine. J. Biol. Chem. 276, 40864-40872
    • (2001) J. Biol. Chem. , vol.276 , pp. 40864-40872
    • Soutourina, J.1    Blanquet, S.2    Plateau, P.3
  • 17
    • 0242489307 scopus 로고    scopus 로고
    • Glycolytic breakdown of sulfoquinovose in bacteria: A missing link in the sulfur cycle
    • Roy, A. B., Hewlins, M. J. E., Ellis, A. J., Harwood, J. L. and White, G. F. (2003) Glycolytic breakdown of sulfoquinovose in bacteria: a missing link in the sulfur cycle. Appl. Environ. Microbiol. 69, 6434-6441
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 6434-6441
    • Roy, A.B.1    Hewlins, M.J.E.2    Ellis, A.J.3    Harwood, J.L.4    White, G.F.5
  • 18
    • 0025817783 scopus 로고
    • Illegitimate integration of non-replicative vectors in the genome of Rhodococcus fascians upon electrotransformation as an insertional mutagenesis system
    • Desomer, J., Crespi, M. and Van Montagu, M. (1991) Illegitimate integration of non-replicative vectors in the genome of Rhodococcus fascians upon electrotransformation as an insertional mutagenesis system. Mol. Microbiol. 5, 2115-2124
    • (1991) Mol. Microbiol. , vol.5 , pp. 2115-2124
    • Desomer, J.1    Crespi, M.2    Van Montagu, M.3
  • 19
    • 0030980121 scopus 로고    scopus 로고
    • Taurine reduction in anaerobic respiration of Bilophila wadsworthia RZATAU
    • Laue, H., Denger, K. and Cook, A. M. (1997) Taurine reduction in anaerobic respiration of Bilophila wadsworthia RZATAU. Appl. Environ. Microbiol. 63, 2016-2021
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2016-2021
    • Laue, H.1    Denger, K.2    Cook, A.M.3
  • 20
    • 0030830082 scopus 로고    scopus 로고
    • Fermentation of cysteate by a sulfate-reducing bacterium
    • Laue, H., Denger, K. and Cook, A. M. (1997) Fermentation of cysteate by a sulfate-reducing bacterium. Arch. Microbiol. 168, 210-214
    • (1997) Arch. Microbiol. , vol.168 , pp. 210-214
    • Laue, H.1    Denger, K.2    Cook, A.M.3
  • 21
    • 0342683869 scopus 로고    scopus 로고
    • Microbulbifer hydrolyticus gen. nov., sp. nov., and Marinobacterium georgiense gen. nov., sp. nov., two marine bacteria from a lignin-rich pulp mill waste enrichment community
    • González, J. M., Mayer, F., Moran, M. A., Hudson, R. E. and Whitman, W. B. (1997) Microbulbifer hydrolyticus gen. nov., sp. nov., and Marinobacterium georgiense gen. nov., sp. nov., two marine bacteria from a lignin-rich pulp mill waste enrichment community. Int. J. Syst. Bacteriol. 47, 369-376
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 369-376
    • González, J.M.1    Mayer, F.2    Moran, M.A.3    Hudson, R.E.4    Whitman, W.B.5
  • 22
    • 0028307260 scopus 로고
    • Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain 0-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid
    • Junker, F., Field, J. A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C. L., Mason, J. R., Leisinger, T. and Cook, A. M. (1994) Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain 0-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300, 429-436
    • (1994) Biochem. J. , vol.300 , pp. 429-436
    • Junker, F.1    Field, J.A.2    Bangerter, F.3    Ramsteiner, K.4    Kohler, H.-P.5    Joannou, C.L.6    Mason, J.R.7    Leisinger, T.8    Cook, A.M.9
  • 23
    • 0030858163 scopus 로고    scopus 로고
    • Thiosulfate as a metabolic product: The bacterial fermentation of taurine
    • Denger, K., Laue, H. and Cook, A. M. (1997) Thiosulfate as a metabolic product: the bacterial fermentation of taurine. Arch. Microbiol. 168, 297-301
    • (1997) Arch. Microbiol. , vol.168 , pp. 297-301
    • Denger, K.1    Laue, H.2    Cook, A.M.3
  • 25
    • 0000012625 scopus 로고
    • Ammonia
    • (Bergmeyer, H. U., ed.), Verlag Chemie, Weinheim
    • Bergmeyer, H. U. and Beutler, H.-O. (1984) Ammonia. In Methods of Enzymic Analysis, Vol. VIII (Bergmeyer, H. U., ed.), pp. 454-461, Verlag Chemie, Weinheim
    • (1984) Methods of Enzymic Analysis , vol.8 , pp. 454-461
    • Bergmeyer, H.U.1    Beutler, H.-O.2
  • 26
    • 0035878925 scopus 로고    scopus 로고
    • Sulphoacetaldehyde sulpho-lyase (EC 4.4.1.12) from Desultonispora thiosulfatigenes: Purification, properties and primary sequence
    • Denger, K., Ruff, J., Rein, U. and Cook, A. M. (2001) Sulphoacetaldehyde sulpho-lyase (EC 4.4.1.12) from Desultonispora thiosulfatigenes: purification, properties and primary sequence. Biochem. J. 357, 581-586
    • (2001) Biochem. J. , vol.357 , pp. 581-586
    • Denger, K.1    Ruff, J.2    Rein, U.3    Cook, A.M.4
  • 27
    • 0029974571 scopus 로고    scopus 로고
    • Bacterial desulfonation of the ethanesulfonate metabolite of the chloroacetanilide herbicide metazachlor
    • Laue, H., Field, J. A. and Cook, A. M. (1996) Bacterial desulfonation of the ethanesulfonate metabolite of the chloroacetanilide herbicide metazachlor. Environ. Sci. Technol. 30, 1129-1132
    • (1996) Environ. Sci. Technol. , vol.30 , pp. 1129-1132
    • Laue, H.1    Field, J.A.2    Cook, A.M.3
  • 28
    • 0023082772 scopus 로고
    • Sulfate: Turfaidimetric and nephelometric methods
    • Sörbo, B. (1987) Sulfate: turfaidimetric and nephelometric methods. Methods Enzymol. 143, 3-6
    • (1987) Methods Enzymol. , vol.143 , pp. 3-6
    • Sörbo, B.1
  • 29
    • 0001206338 scopus 로고
    • Pyruvate
    • (Bergmeyer, H. U., ed.), Verlag Chemie, Weinheim
    • Lamprecht, W. and Heinz, F. (1984) Pyruvate. In Methods of Enzymic Analysis, Vol. 6 (Bergmeyer, H. U., ed.), pp. 570-577, Verlag Chemie, Weinheim
    • (1984) Methods of Enzymic Analysis , vol.6 , pp. 570-577
    • Lamprecht, W.1    Heinz, F.2
  • 30
    • 0014270238 scopus 로고
    • Enzymes of the mandelate pathway in bacterium N.C.I.B. 8250
    • Kennedy, S. I. T. and Fewson, C. A. (1968) Enzymes of the mandelate pathway in bacterium N.C.I.B. 8250. Biochem. J. 107, 497-506
    • (1968) Biochem. J. , vol.107 , pp. 497-506
    • Kennedy, S.I.T.1    Fewson, C.A.2
  • 31
    • 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. (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.1
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0033862434 scopus 로고    scopus 로고
    • Purification, properties and primary structure of alanine dehydrogenase involved in taurine metabolism in the anaerobe Bilophila wadsworthia
    • Laue, H. and Cook, A. M. (2000) Purification, properties and primary structure of alanine dehydrogenase involved in taurine metabolism in the anaerobe Bilophila wadsworthia. Arch. Microbiol. 174, 162-167
    • (2000) Arch. Microbiol. , vol.174 , pp. 162-167
    • Laue, H.1    Cook, A.M.2
  • 34
    • 0032751653 scopus 로고    scopus 로고
    • Desulfonation of propanesulfonic acid by Comamonas acidovorans strain P53: Evidence for an alkanesulfonate sulfonatase and an atypical sulfite dehydrogenase
    • Reichenbecher, W., Kelly, D. P. and Murrell, J. C. (1999) Desulfonation of propanesulfonic acid by Comamonas acidovorans strain P53: evidence for an alkanesulfonate sulfonatase and an atypical sulfite dehydrogenase. Arch. Microbiol. 172, 387-392
    • (1999) Arch. Microbiol. , vol.172 , pp. 387-392
    • Reichenbecher, W.1    Kelly, D.P.2    Murrell, J.C.3
  • 35
    • 0037440030 scopus 로고    scopus 로고
    • Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: Purification from Alcaligenes defragrans and gene clusters in taurine degradation
    • Ruff, J., Denger, K. and Cook, A. M. (2003) Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation. Biochem. J. 369, 275-285
    • (2003) Biochem. J. , vol.369 , pp. 275-285
    • Ruff, J.1    Denger, K.2    Cook, A.M.3
  • 37
  • 38
    • 0002727505 scopus 로고
    • Biodégradation of s-triazine xenobiotics
    • Cook, A. M. (1987) Biodégradation of s-triazine xenobiotics. FEMS Microbiol. Rev. 46, 93-116
    • (1987) FEMS Microbiol. Rev. , vol.46 , pp. 93-116
    • Cook, A.M.1
  • 42
    • 1542472666 scopus 로고    scopus 로고
    • Gel chromatography as an analytical tool for characterization of size and molecular mass of proteins
    • le Maire, M., Ghasi, A. and Moller, J. V. (1996) Gel chromatography as an analytical tool for characterization of size and molecular mass of proteins. ACS Symp. Ser. 635, 36-51
    • (1996) ACS Symp. Ser. , vol.635 , pp. 36-51
    • Maire, M.1    Ghasi, A.2    Moller, J.V.3
  • 43
    • 84954948756 scopus 로고
    • Metabolism of 1-aminocyclopropane-1-carboxylic acid
    • Honma, M. and Shimomura, T. (1978) Metabolism of 1-aminocyclopropane-1- carboxylic acid. Agric. Biol. Chem. 42, 1825-1831
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 1825-1831
    • Honma, M.1    Shimomura, T.2
  • 45
    • 0023679401 scopus 로고
    • Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1
    • Nagasawa, T., Ishii, T. and Yamada, H. (1988) Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. Arch. Microbiol. 149, 413-416
    • (1988) Arch. Microbiol. , vol.149 , pp. 413-416
    • Nagasawa, T.1    Ishii, T.2    Yamada, H.3
  • 46
    • 0000976838 scopus 로고    scopus 로고
    • Metabolism of sulfonic acids and other organosulfur compounds by sulfate-reducing bacteria
    • Lie, T. L., Leadbetter, J. R. and Leadbetter, E. R. (1998) Metabolism of sulfonic acids and other organosulfur compounds by sulfate-reducing bacteria. Geomicrobiol. J. 15, 135-149
    • (1998) Geomicrobiol. J. , vol.15 , pp. 135-149
    • Lie, T.L.1    Leadbetter, J.R.2    Leadbetter, E.R.3
  • 47
    • 0345701960 scopus 로고    scopus 로고
    • Reaction of 1-amino-2-methylenecyclopropane-1-carboxylate with 1-aminocyclopropane-1-carboxylate deaminase: Analysis and mechanistic implications
    • Zhao, Z., Chen, H., Li, K., Du, W., He, S. and Liu, H. W. (2003) Reaction of 1-amino-2-methylenecyclopropane-1-carboxylate with 1-aminocyclopropane-1- carboxylate deaminase: analysis and mechanistic implications. Biochemistry 42, 2089-2103
    • (2003) Biochemistry , vol.42 , pp. 2089-2103
    • Zhao, Z.1    Chen, H.2    Li, K.3    Du, W.4    He, S.5    Liu, H.W.6
  • 48
    • 0028286455 scopus 로고
    • Critical nucleotides in the interaction of a LysR-type regulator with its target promoter region. catBC promoter activation by CatR
    • Parsek, M. R., Ye, R. W., Pun, P. and Chakrabarty, A. M. (1994) Critical nucleotides in the interaction of a LysR-type regulator with its target promoter region. catBC promoter activation by CatR. J. Bacteriol. 269, 11279-11284
    • (1994) J. Bacteriol. , vol.269 , pp. 11279-11284
    • Parsek, M.R.1    Ye, R.W.2    Pun, P.3    Chakrabarty, A.M.4
  • 49
    • 0026544125 scopus 로고
    • Conserved motifs in a divergent nod box of Azorhizobium caulinodans ORS571 reveal a common structure in promoters regulated by LysR-type proteins
    • Goethals, K., Van Montagu, M. and Holsters, M. (1992) Conserved motifs in a divergent nod box of Azorhizobium caulinodans ORS571 reveal a common structure in promoters regulated by LysR-type proteins. Proc. Natl. Acad. Sci. U.S.A. 89, 1646-1650
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 1646-1650
    • Goethals, K.1    Van Montagu, M.2    Holsters, M.3
  • 50
    • 0037134521 scopus 로고    scopus 로고
    • Identification of coenzyme M biosynthetic phosphosulfolactate synthase: A new family of sulfonate biosynthesizing enzymes
    • Graham, D. E., Xu, H. and White, R. H. (2002) Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate biosynthesizing enzymes. J. Biol. Chem. 277, 13421-13429
    • (2002) J. Biol. Chem. , vol.277 , pp. 13421-13429
    • Graham, D.E.1    Xu, H.2    White, R.H.3
  • 51
    • 0016655150 scopus 로고
    • Microbial metabolism of aryl sulphonates a reassessment of colorimetric methods for the determination of sulphite and their use in measuring desulphonation of aryl and alkylbenzene sulphonates
    • Johnston, J. B., Murray, K. and Cain, R. B. (1975) Microbial metabolism of aryl sulphonates a reassessment of colorimetric methods for the determination of sulphite and their use in measuring desulphonation of aryl and alkylbenzene sulphonates. Antonie van Leeuwenhoek 41, 493-511
    • (1975) Antonie Van Leeuwenhoek , vol.41 , pp. 493-511
    • Johnston, J.B.1    Murray, K.2    Cain, R.B.3
  • 52
    • 0031451030 scopus 로고    scopus 로고
    • Metabolism of sulfoacetate by environmental Aureobacterium sp. and Comamonas acidovorans isolates
    • King, J. E. and Quinn, J. P. (1997) Metabolism of sulfoacetate by environmental Aureobacterium sp. and Comamonas acidovorans isolates. Microbiology (Reading, U.K.) 143, 3907-3912
    • (1997) Microbiology (Reading, U.K.) , vol.143 , pp. 3907-3912
    • King, J.E.1    Quinn, J.P.2
  • 53
    • 0030739589 scopus 로고    scopus 로고
    • The role of sulfoacetaldehyde sulfo-lyase in the mineralization of isethionate by an environmental Acinetobacter isolate
    • King, J. E., Jaouhari, R. and Quinn, J. P. (1997) The role of sulfoacetaldehyde sulfo-lyase in the mineralization of isethionate by an environmental Acinetobacter isolate. Microbiology (Reading, U.K.) 143, 2339-2343
    • (1997) Microbiology (Reading, U.K.) , vol.143 , pp. 2339-2343
    • King, J.E.1    Jaouhari, R.2    Quinn, J.P.3
  • 54
    • 33645539868 scopus 로고    scopus 로고
    • The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine
    • in the press
    • 53a Weinitschke, S., Denger, K., Smits, T. M. H., Hollemeyer, K. and Cook, A. M. (2006) The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine. Microbiology (Reading, U.K.), in the press
    • (2006) Microbiology (Reading, U.K.)
    • Weinitschke, S.1    Denger, K.2    Smits, T.M.H.3    Hollemeyer, K.4    Cook, A.M.5


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