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Volumn 28, Issue 3, 2005, Pages 187-195

Unity in organisation and regulation of catabolic operons in Lactobacillus plantarum, Lactococcus lactis and Listeria monocytogenes

Author keywords

Catabolite responsive element (CRE); Comparative genomics; Global regulation; Lactobacillus plantarum; Lactococcus lactis; Listeria monocytogenes; Operon organisation

Indexed keywords

CARRIER PROTEIN; DISACCHARIDE; LACTOSE; MALTOSE; MONOSACCHARIDE; REGULATOR PROTEIN; SUGAR; SUGAR ALCOHOL; SUGAR TRANSPORT PROTEIN; TREHALOSE; UNCLASSIFIED DRUG;

EID: 16244417206     PISSN: 07232020     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.syapm.2004.11.004     Document Type: Article
Times cited : (29)

References (54)
  • 2
    • 0035900670 scopus 로고    scopus 로고
    • Trehalose 6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactcoccus lactis
    • U. Andersson, F. Levander, and P. Rådström Trehalose 6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactcoccus lactis J. Biol. Chem. 276 2001 42707 42718
    • (2001) J. Biol. Chem. , vol.276 , pp. 42707-42718
    • Andersson, U.1    Levander, F.2    Rådström, P.3
  • 3
    • 34248390126 scopus 로고    scopus 로고
    • Physiological function of the maltose operon regulator, MalR, in Lactococcus lactis
    • U. Andersson, and P. Rådström Physiological function of the maltose operon regulator, MalR, in Lactococcus lactis BMC Microbiol. 2 2002 28
    • (2002) BMC Microbiol. , vol.2 , pp. 28
    • Andersson, U.1    Rådström, P.2
  • 4
    • 0027467385 scopus 로고
    • Sugar uptake and involved enzymatic activities by yeasts and lactic acid bacteria: Their relationship with bread-making quality
    • B. Antuna, and M.A. Martinez-Anaya Sugar uptake and involved enzymatic activities by yeasts and lactic acid bacteria their relationship with bread-making quality Int. J. Microbiol. 18 1993 191 200
    • (1993) Int. J. Microbiol. , vol.18 , pp. 191-200
    • Antuna, B.1    Martinez-Anaya, M.A.2
  • 5
    • 0031877016 scopus 로고    scopus 로고
    • Combining evidence using p-values: Application to sequence homology searches
    • T.L. Bailey, and M. Gribskov Combining evidence using p-values application to sequence homology searches Bioinformatics 14 1998 48 54
    • (1998) Bioinformatics , vol.14 , pp. 48-54
    • Bailey, T.L.1    Gribskov, M.2
  • 6
    • 0027992516 scopus 로고
    • BglR Protein, which belongs to the BglG family of transcriptional antiterminators, is involved in β-glucoside utilization in Lactococcus lactis
    • J. Bardowski, S.D. Ehrlich, and A. Chopin BglR Protein, which belongs to the BglG family of transcriptional antiterminators, is involved in β-glucoside utilization in Lactococcus lactis J. Bacteriol. 176 1994 5681 5685
    • (1994) J. Bacteriol. , vol.176 , pp. 5681-5685
    • Bardowski, J.1    Ehrlich, S.D.2    Chopin, A.3
  • 8
    • 0032839731 scopus 로고    scopus 로고
    • The bvr locus of Listeria monocytogenes mediates virulence gene expression by β-glucosides
    • K. Brehm, M.T. Ripio, J. Kreft, and J.A. Vazquez-Boland The bvr locus of Listeria monocytogenes mediates virulence gene expression by β-glucosides J. Bacteriol. 181 1999 5024 5032
    • (1999) J. Bacteriol. , vol.181 , pp. 5024-5032
    • Brehm, K.1    Ripio, M.T.2    Kreft, J.3    Vazquez-Boland, J.A.4
  • 9
    • 0032838288 scopus 로고    scopus 로고
    • Transport of d-xylose in Lactobacillus pentosus, Lactobacillus casei and Lactobacillus plantarum: Evidence for a mechanism of facilitated diffusion via the phosphoenol pyruvate:mannose phosphotransferase system
    • S. Chaillou, P.H. Pouwels, and P.W. Postma Transport of d-xylose in Lactobacillus pentosus, Lactobacillus casei and Lactobacillus plantarum evidence for a mechanism of facilitated diffusion via the phosphoenol pyruvate:mannose phosphotransferase system J. Bacteriol. 181 1999 4768 4773
    • (1999) J. Bacteriol. , vol.181 , pp. 4768-4773
    • Chaillou, S.1    Pouwels, P.H.2    Postma, P.W.3
  • 10
    • 0013769718 scopus 로고
    • Metabolism of mannitol and induction of mannitol 1-phosphate dehydrogenase in Lactobacillus plantarum
    • M. Chakravorty Metabolism of mannitol and induction of mannitol 1-phosphate dehydrogenase in Lactobacillus plantarum J. Bacteriol. 87 1964 1246 1248
    • (1964) J. Bacteriol. , vol.87 , pp. 1246-1248
    • Chakravorty, M.1
  • 11
    • 0028917215 scopus 로고
    • Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria
    • J. Deutscher, E. Kuster, U. Bergstedt, V. Charrier, and W. Hillen Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria Mol. Microbiol. 15 1995 1049 1053
    • (1995) Mol. Microbiol. , vol.15 , pp. 1049-1053
    • Deutscher, J.1    Kuster, E.2    Bergstedt, U.3    Charrier, V.4    Hillen, W.5
  • 12
    • 0025634299 scopus 로고
    • Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis
    • W.M. de Vos, I. Boerrigter, R.J. van Rooyen, B. Reiche, and W. Hengstenberg Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis J. Biol. Chem. 265 1990 22554 22556
    • (1990) J. Biol. Chem. , vol.265 , pp. 22554-22556
    • De Vos, W.M.1    Boerrigter, I.2    Van Rooyen, R.J.3    Reiche, B.4    Hengstenberg, W.5
  • 13
    • 0024695501 scopus 로고
    • Structure and expression of the Lactococcus lactis gene for phospho-beta-galactosidase (lacG) in Escherichia coli and L. lactis
    • W.M. de Vos, and M.J. Gasson Structure and expression of the Lactococcus lactis gene for phospho-beta-galactosidase (lacG) in Escherichia coli and L. lactis J. Gen. Microbiol. 135 1989 1833 1846
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 1833-1846
    • De Vos, W.M.1    Gasson, M.J.2
  • 15
    • 0035919866 scopus 로고    scopus 로고
    • Regulation of pyruvate metabolism in Lactococcus lactis depends on the inbalance between catabolism and anabolism
    • C. Garrigues, M. Mercade, M. Cocaign-Bousquet, N.D. Lindley, and P. Luibiere Regulation of pyruvate metabolism in Lactococcus lactis depends on the inbalance between catabolism and anabolism Biotechnol. Bioeng. 74 2001 108 115
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 108-115
    • Garrigues, C.1    Mercade, M.2    Cocaign-Bousquet, M.3    Lindley, N.D.4    Luibiere, P.5
  • 16
    • 1642296584 scopus 로고    scopus 로고
    • Engineering Lactococcus lactis for production of mannitol: High yields from food-grade strains deficient in lactate dehydrogenase and the mannitol transport system
    • P. Gaspar, A.R. Neves, A. Ramos, M.J. Gasson, C.A. Shearman, and H. Santos Engineering Lactococcus lactis for production of mannitol high yields from food-grade strains deficient in lactate dehydrogenase and the mannitol transport system Appl. Environ. Microbiol. 70 2004 1466 1474
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1466-1474
    • Gaspar, P.1    Neves, A.R.2    Ramos, A.3    Gasson, M.J.4    Shearman, C.A.5    Santos, H.6
  • 17
    • 0020600404 scopus 로고
    • Plasmid complement of Streptococcus lactis NCDO712 and other lactic streptococci after protoplast-induced curing
    • M.J. Gasson Plasmid complement of Streptococcus lactis NCDO712 and other lactic streptococci after protoplast-induced curing J. Bacteriol. 154 1983 1 9
    • (1983) J. Bacteriol. , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 18
    • 0031752047 scopus 로고    scopus 로고
    • Physiological response of Lactobacillus plantarum to salt and electrolyte stress
    • E. Glaasker, F.S. Tjan, P.F. Ter Steeg, W.N. Konings, and B. Poolman Physiological response of Lactobacillus plantarum to salt and electrolyte stress J. Bacteriol. 180 1998 4718 4723
    • (1998) J. Bacteriol. , vol.180 , pp. 4718-4723
    • Glaasker, E.1    Tjan, F.S.2    Ter Steeg, P.F.3    Konings, W.N.4    Poolman, B.5
  • 20
    • 0034103223 scopus 로고    scopus 로고
    • Arabinose fermentation by Lactobacillus plantarum in sourdough with added pentosans and α,α-l-arabinofuranosidase: A tool to increase the production of acetic acid
    • M. Gobbetti, P. Lavermicocca, F. Minervini, M. de Angelis, and A. Corsetti Arabinose fermentation by Lactobacillus plantarum in sourdough with added pentosans and α,α-l-arabinofuranosidase a tool to increase the production of acetic acid J. Appl. Microbiol. 88 2000 317 324
    • (2000) J. Appl. Microbiol. , vol.88 , pp. 317-324
    • Gobbetti, M.1    Lavermicocca, P.2    Minervini, F.3    De Angelis, M.4    Corsetti, A.5
  • 21
    • 0032365969 scopus 로고    scopus 로고
    • Genetics of galactose utilisation via the Leloir pathway in lactic acid bacteria
    • B. Grossiord, E.E. Vaughan, E. Luesink, and W.M. de Vos Genetics of galactose utilisation via the Leloir pathway in lactic acid bacteria Lait 78 1998 77 84
    • (1998) Lait , vol.78 , pp. 77-84
    • Grossiord, B.1    Vaughan, E.E.2    Luesink, E.3    De Vos, W.M.4
  • 22
    • 0036694219 scopus 로고    scopus 로고
    • Gene regulation in Lactococcus lactis: The gap between predicted and characterized regulators
    • E. Guédon, E. Jamet, and P. Renault Gene regulation in Lactococcus lactis the gap between predicted and characterized regulators Ant. van Leeuweuh 82 2002 93 112
    • (2002) Ant. Van Leeuweuh , vol.82 , pp. 93-112
    • Guédon, E.1    Jamet, E.2    Renault, P.3
  • 23
  • 24
    • 0030057004 scopus 로고    scopus 로고
    • The role of CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis
    • T.M. Henkin The role of CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis FEMS Microbiol. Lett. 135 1996 9 15
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 9-15
    • Henkin, T.M.1
  • 25
    • 0028907495 scopus 로고
    • Catabolite repression in Bacillus subtilis: A global regulatory mechanism for the Gram-positive bacteria?
    • C.J. Hueck, and W. Hillen Catabolite repression in Bacillus subtilis a global regulatory mechanism for the Gram-positive bacteria? Mol. Microbiol. 15 1995 395 401
    • (1995) Mol. Microbiol. , vol.15 , pp. 395-401
    • Hueck, C.J.1    Hillen, W.2
  • 26
    • 0033616714 scopus 로고    scopus 로고
    • Horizontal gene transfer among genomes: The complexity hypothesis
    • R. Jain, M.C. Rivera, and J.A. Lake Horizontal gene transfer among genomes the complexity hypothesis Proc Natl. Acad. Sci. USA 96 1999 3801 3806
    • (1999) Proc Natl. Acad. Sci. USA , vol.96 , pp. 3801-3806
    • Jain, R.1    Rivera, M.C.2    Lake, J.A.3
  • 28
    • 0025259130 scopus 로고
    • Same-day identification scheme for colonies of Listeria monocytogenes
    • R.V. Lachica Same-day identification scheme for colonies of Listeria monocytogenes Appl. Environ. Microbiol. 56 1990 1166 1168
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1166-1168
    • Lachica, R.V.1
  • 29
    • 0028882594 scopus 로고
    • A system to generate chromosomal mutations in Lactococcus lactis which allows fast analysis of targeted genes
    • J. Law, G. Buist, A. Haandrikman, J. Kok, G. Venema, and K. Leenhouts A system to generate chromosomal mutations in Lactococcus lactis which allows fast analysis of targeted genes J. Bacteriol. 177 1995 7011 7018
    • (1995) J. Bacteriol. , vol.177 , pp. 7011-7018
    • Law, J.1    Buist, G.2    Haandrikman, A.3    Kok, J.4    Venema, G.5    Leenhouts, K.6
  • 30
    • 0035486814 scopus 로고    scopus 로고
    • The physiological role of β-phosphoglucomutase in Lactococcus lactis
    • F. Levander, U. Andersson, and P. Rådström The physiological role of β-phosphoglucomutase in Lactococcus lactis Appl. Environ. Microbiol. 67 2001 4546 4553
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4546-4553
    • Levander, F.1    Andersson, U.2    Rådström, P.3
  • 31
    • 0032990409 scopus 로고    scopus 로고
    • Characterization of the divergent sacBK and sacAR operons, involved in sucrose utilization by Lactococcus lactis
    • E.J. Luesink, J.D. Marugg, O.P. Kuipers, and W.M. de Vos Characterization of the divergent sacBK and sacAR operons, involved in sucrose utilization by Lactococcus lactis J. Bacteriol. 181 1999 1924 1926
    • (1999) J. Bacteriol. , vol.181 , pp. 1924-1926
    • Luesink, E.J.1    Marugg, J.D.2    Kuipers, O.P.3    De Vos, W.M.4
  • 32
    • 0022627074 scopus 로고
    • Cloning, expression and location of the Streptococcus lactis gene for phospho-β-d-galactosidase
    • S. Maeda, and M.J. Gasson Cloning, expression and location of the Streptococcus lactis gene for phospho-β-d-galactosidase J. Gen. Microbiol. 132 1986 331 340
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 331-340
    • Maeda, S.1    Gasson, M.J.2
  • 33
    • 0031780571 scopus 로고    scopus 로고
    • Expression of the bglH gene of Lactobacillus plantarum is controlled by carbon catabolite repression
    • R. Marasco, L. Muscariello, M. Varcanonti, M. De Felice, and M. Sacco Expression of the bglH gene of Lactobacillus plantarum is controlled by carbon catabolite repression J. Bacteriol. 180 1998 3400 3404
    • (1998) J. Bacteriol. , vol.180 , pp. 3400-3404
    • Marasco, R.1    Muscariello, L.2    Varcanonti, M.3    De Felice, M.4    Sacco, M.5
  • 34
    • 0034607640 scopus 로고    scopus 로고
    • A physical and functional analysis of the newly identified bglGPT operon of Lactobacillus plantarum
    • R. Marasco, I. Salatiello, M. De Felice, and M. Sacco A physical and functional analysis of the newly identified bglGPT operon of Lactobacillus plantarum FEMS Microbiol. Lett. 186 2000 269 273
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 269-273
    • Marasco, R.1    Salatiello, I.2    De Felice, M.3    Sacco, M.4
  • 35
    • 0024810767 scopus 로고
    • Selected characteristics of several strains of Lactobacillus plantarum
    • B. Mayo, C. Hardisson, and A.F. Braun Selected characteristics of several strains of Lactobacillus plantarum Microbiologia 5 1989 105 112
    • (1989) Microbiologia , vol.5 , pp. 105-112
    • Mayo, B.1    Hardisson, C.2    Braun, A.F.3
  • 36
    • 0027221824 scopus 로고
    • Identification of a phosphoenolpyruvate: Fructose phosphotransferase system (fructose 1-phosphate forming) in Listeria monocytogenes
    • W.J. Mitchell, J. Reizer, C. Herring, C. Hoischen, and M.H. Saier Jr. Identification of a phosphoenolpyruvate fructose phosphotransferase system (fructose 1-phosphate forming) in Listeria monocytogenes J. Bacteriol. 175 1993 2758 2761
    • (1993) J. Bacteriol. , vol.175 , pp. 2758-2761
    • Mitchell, W.J.1    Reizer, J.2    Herring, C.3    Hoischen, C.4    Saier Jr., M.H.5
  • 37
    • 0035404452 scopus 로고    scopus 로고
    • The functional ccpA gene is required for carbon catabolite repression in Lactobacillus plantarum
    • L. Muscariello, R. Marasco, M. De Felice, and M. Sacco The functional ccpA gene is required for carbon catabolite repression in Lactobacillus plantarum Appl. Environ. Microbiol. 67 2001 2903 2907
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2903-2907
    • Muscariello, L.1    Marasco, R.2    De Felice, M.3    Sacco, M.4
  • 38
    • 0033946783 scopus 로고    scopus 로고
    • Metabolic characterization of Lactococcus lactis deficient in lactate dehydrogenase using in vivo 13C-NMR
    • A.R. Neves, S. Ramos, C. Shearman, M.J. Gasson, J.S. Almeida, and H. Santos Metabolic characterization of Lactococcus lactis deficient in lactate dehydrogenase using in vivo 13C-NMR Eur. J. Biochem. 267 2000 3859 3868
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3859-3868
    • Neves, A.R.1    Ramos, S.2    Shearman, C.3    Gasson, M.J.4    Almeida, J.S.5    Santos, H.6
  • 39
    • 0034965154 scopus 로고    scopus 로고
    • Genetic localization and regulation of the maltose phosphorylase gene, malP, in Lactococcus lactis
    • U. Nilsson, and P. Rådström Genetic localization and regulation of the maltose phosphorylase gene, malP, in Lactococcus lactis Microbiology 147 2001 1565 1573
    • (2001) Microbiology , vol.147 , pp. 1565-1573
    • Nilsson, U.1    Rådström, P.2
  • 40
    • 0024589644 scopus 로고
    • Physiological studies of the growth and utilization of sugars by Listeria species
    • L. Pine, G.B. Malcolm, J.B. Brooks, and M.I. Duneshvar Physiological studies of the growth and utilization of sugars by Listeria species Can. J. Microbiol. 35 1989 245 254
    • (1989) Can. J. Microbiol. , vol.35 , pp. 245-254
    • Pine, L.1    Malcolm, G.B.2    Brooks, J.B.3    Duneshvar, M.I.4
  • 41
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • P.W. Postma, J.W. Lengeler, and G.R. Jacobson Phosphoenolpyruvate carbohydrate phosphotransferase systems of bacteria Microbiol. Rev. 57 1993 5435 5494
    • (1993) Microbiol. Rev. , vol.57 , pp. 5435-5494
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 42
    • 0025953961 scopus 로고
    • Development of an improved chemically defined minimal medium for Listeria monocytogenes
    • R.J. Premaratne, W.J. Lin, and E.A. Johnson Development of an improved chemically defined minimal medium for Listeria monocytogenes Appl. Environ. Microbiol. 57 1991 3046 3048
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3046-3048
    • Premaratne, R.J.1    Lin, W.J.2    Johnson, E.A.3
  • 43
    • 0028021801 scopus 로고
    • Purification and characterization of two phosphoglucomutases from Lactococcus lactis subsp lactis and their regulation in maltose- and glucose-utilizing cells
    • N. Qian, G.A. Stanley, B. Hahn-Hägerdal, and P. Rådström Purification and characterization of two phosphoglucomutases from Lactococcus lactis subsp lactis and their regulation in maltose- and glucose-utilizing cells J. Bacteriol. 176 1994 5304 5311
    • (1994) J. Bacteriol. , vol.176 , pp. 5304-5311
    • Qian, N.1    Stanley, G.A.2    Hahn-Hägerdal, B.3    Rådström, P.4
  • 46
    • 0035282418 scopus 로고    scopus 로고
    • Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR
    • A. Schlösser, A. Weber, and H. Schrempf Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR FEMS Microbiol. Lett. 196 2001 77 83
    • (2001) FEMS Microbiol. Lett. , vol.196 , pp. 77-83
    • Schlösser, A.1    Weber, A.2    Schrempf, H.3
  • 47
    • 0029785421 scopus 로고    scopus 로고
    • Expression of the tre operon of Bacillus subtilis 168 is regulated by the repressor TreR
    • F. Schöck, and M.K. Dahl Expression of the tre operon of Bacillus subtilis 168 is regulated by the repressor TreR J. Bacteriol. 178 1996 4576 4581
    • (1996) J. Bacteriol. , vol.178 , pp. 4576-4581
    • Schöck, F.1    Dahl, M.K.2
  • 49
    • 0019853495 scopus 로고
    • Uptake and metabolism of sucrose by Streptococcus lactis
    • J. Thompson, and B.M. Chassy Uptake and metabolism of sucrose by Streptococcus lactis J. Bacteriol. 147 1981 543 551
    • (1981) J. Bacteriol. , vol.147 , pp. 543-551
    • Thompson, J.1    Chassy, B.M.2
  • 50
    • 0025837018 scopus 로고
    • Purification and properties of fructokinase I from Lactococcus lactis: Localization of scrK on the sucrose-nisin transposon Tn5306
    • J. Thompson, D.L. Sackett, and J.A. Donkersloot Purification and properties of fructokinase I from Lactococcus lactis localization of scrK on the sucrose-nisin transposon Tn5306 J. Biol. Chem. 266 1991 22626 22633
    • (1991) J. Biol. Chem. , vol.266 , pp. 22626-22633
    • Thompson, J.1    Sackett, D.L.2    Donkersloot, J.A.3
  • 52
    • 0025052301 scopus 로고
    • Molecular cloning, transcriptional analysis, and nucleotide sequence of lacR, a gene encoding the repressor of the lactose phosphotransferase system of Lactococcus lactis
    • R.J. van Rooijen, and W.M. de Vos Molecular cloning, transcriptional analysis, and nucleotide sequence of lacR, a gene encoding the repressor of the lactose phosphotransferase system of Lactococcus lactis J. Biol. Chem. 265 1990 18499 18503
    • (1990) J. Biol. Chem. , vol.265 , pp. 18499-18503
    • Van Rooijen, R.J.1    De Vos, W.M.2
  • 53
    • 0026576556 scopus 로고
    • Characterization of the Lactococcus lactis lactose operon promoter: Contribution of flanking sequences and LacR repressor to promoter activity
    • R.J. van Rooijen, M.J. Gasson, and W.M. de Vos Characterization of the Lactococcus lactis lactose operon promoter contribution of flanking sequences and LacR repressor to promoter activity J. Bacteriol. 174 1992 2273 2280
    • (1992) J. Bacteriol. , vol.174 , pp. 2273-2280
    • Van Rooijen, R.J.1    Gasson, M.J.2    De Vos, W.M.3
  • 54
    • 0025071837 scopus 로고
    • Site-directed mutagenesis of a catabolite repression operator sequence in Bacillus subtilis
    • M.J. Weickert, and G.H. Chambliss Site-directed mutagenesis of a catabolite repression operator sequence in Bacillus subtilis Proc. Natl. Acad. Sci. USA 87 1990 6238 6242
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6238-6242
    • Weickert, M.J.1    Chambliss, G.H.2


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