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Volumn 77, Issue 1, 2010, Pages 1-5

Pneumococcal microbial surface components recognizing adhesive matrix molecules targeting of the extracellular matrix

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FIBRONECTIN; PLASMINOGEN; PROTEIN PAVB; UNCLASSIFIED DRUG; MEMBRANE PROTEIN; VIRULENCE FACTOR;

EID: 77953977960     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07190.x     Document Type: Note
Times cited : (35)

References (41)
  • 1
    • 0020557001 scopus 로고
    • Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells
    • Andersson, B., Dahmen, J., Frejd, T., Leffler, H., Magnusson, G., Noori, G., et al. (1983) Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells. J Exp Med 158 : 559 570.
    • (1983) J Exp Med , vol.158 , pp. 559-570
    • Andersson, B.1    Dahmen, J.2    Frejd, T.3    Leffler, H.4    Magnusson, G.5    Noori, G.6
  • 2
    • 34247485877 scopus 로고    scopus 로고
    • E-cadherin is a receptor for the common protein pneumococcal surface adhesin A (PsaA) of Streptococcus pneumoniae
    • Anderton, J.M., Rajam, G., Romero-Steiner, S., Summer, S., Kowalczyk, A.P., Carlone, G.M., et al. (2007) E-cadherin is a receptor for the common protein pneumococcal surface adhesin A (PsaA) of Streptococcus pneumoniae. Microb Pathog 42 : 225 236.
    • (2007) Microb Pathog , vol.42 , pp. 225-236
    • Anderton, J.M.1    Rajam, G.2    Romero-Steiner, S.3    Summer, S.4    Kowalczyk, A.P.5    Carlone, G.M.6
  • 3
    • 34250333853 scopus 로고    scopus 로고
    • PH-dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids
    • Antikainen, J., Kuparinen, V., Lahteenmaki, K. Korhonen, T.K. (2007) pH-dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids. J Bacteriol 189 : 4539 4543.
    • (2007) J Bacteriol , vol.189 , pp. 4539-4543
    • Antikainen, J.1    Kuparinen, V.2    Lahteenmaki, K.3    Korhonen, T.K.4
  • 4
    • 39149114768 scopus 로고    scopus 로고
    • Streptococcus pneumoniae choline-binding protein e interaction with plasminogen/plasmin stimulates migration across the extracellular matrix
    • Attali, C., Frolet, C., Durmort, C., Offant, J., Vernet, T. Di, A.M. (2008) Streptococcus pneumoniae choline-binding protein E interaction with plasminogen/plasmin stimulates migration across the extracellular matrix. Infect Immun 76 : 466 476.
    • (2008) Infect Immun , vol.76 , pp. 466-476
    • Attali, C.1    Frolet, C.2    Durmort, C.3    Offant, J.4    Vernet, T.5    Di, A.M.6
  • 5
    • 34548667697 scopus 로고    scopus 로고
    • Fibrinolysis and host response in bacterial infections
    • Bergmann, S. Hammerschmidt, S. (2007) Fibrinolysis and host response in bacterial infections. Thromb Haemost 98 : 512 520.
    • (2007) Thromb Haemost , vol.98 , pp. 512-520
    • Bergmann, S.1    Hammerschmidt, S.2
  • 6
    • 0034931519 scopus 로고    scopus 로고
    • Alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann, S., Rohde, M., Chhatwal, G.S. Hammerschmidt, S. (2001) alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40 : 1273 1287.
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 7
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae
    • Bergmann, S., Wild, D., Diekmann, O., Frank, R., Bracht, D., Chhatwal, G.S., et al. (2003) Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol Microbiol 49 : 411 423.
    • (2003) Mol Microbiol , vol.49 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3    Frank, R.4    Bracht, D.5    Chhatwal, G.S.6
  • 8
    • 23744464766 scopus 로고    scopus 로고
    • The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration
    • Bergmann, S., Rohde, M., Preissner, K.T. Hammerschmidt, S. (2005) The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration. Thromb Haemost 94 : 304 311.
    • (2005) Thromb Haemost , vol.94 , pp. 304-311
    • Bergmann, S.1    Rohde, M.2    Preissner, K.T.3    Hammerschmidt, S.4
  • 9
    • 61949389320 scopus 로고    scopus 로고
    • Integrin-linked kinase is required for vitronectin-mediated internalization of Streptococcus pneumoniae by host cells
    • Bergmann, S., Lang, A., Rohde, M., Agarwal, V., Rennemeier, C., Grashoff, C., et al. (2009) Integrin-linked kinase is required for vitronectin-mediated internalization of Streptococcus pneumoniae by host cells. J Cell Sci 122 : 256 267.
    • (2009) J Cell Sci , vol.122 , pp. 256-267
    • Bergmann, S.1    Lang, A.2    Rohde, M.3    Agarwal, V.4    Rennemeier, C.5    Grashoff, C.6
  • 10
    • 0037422243 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 deficiency impairs host defense mechanisms against Streptococcus pneumoniae in a mouse model of bacterial meningitis
    • Bottcher, T., Spreer, A., Azeh, I., Nau, R. Gerber, J. (2003) Matrix metalloproteinase-9 deficiency impairs host defense mechanisms against Streptococcus pneumoniae in a mouse model of bacterial meningitis. Neurosci Lett 338 : 201 204.
    • (2003) Neurosci Lett , vol.338 , pp. 201-204
    • Bottcher, T.1    Spreer, A.2    Azeh, I.3    Nau, R.4    Gerber, J.5
  • 11
    • 13844281768 scopus 로고    scopus 로고
    • Sequence analysis and characterization of a novel fibronectin-binding repeat domain from the surface of Streptococcus pneumoniae
    • Bumbaca, D., Littlejohn, J.E., Nayakanti, H., Rigden, D.J., Galperin, M.Y. Jedrzejas, M.J. (2004) Sequence analysis and characterization of a novel fibronectin-binding repeat domain from the surface of Streptococcus pneumoniae. OMICS 8 : 341 356.
    • (2004) OMICS , vol.8 , pp. 341-356
    • Bumbaca, D.1    Littlejohn, J.E.2    Nayakanti, H.3    Rigden, D.J.4    Galperin, M.Y.5    Jedrzejas, M.J.6
  • 13
    • 32244435886 scopus 로고    scopus 로고
    • Zinc metalloproteinase genes in clinical isolates of Streptococcus pneumoniae: Association of the full array with a clonal cluster comprising serotypes 8 and 11A
    • Camilli, R., Pettini, E., Grosso, M.D., Pozzi, G., Pantosti, A. Oggioni, M.R. (2006) Zinc metalloproteinase genes in clinical isolates of Streptococcus pneumoniae: association of the full array with a clonal cluster comprising serotypes 8 and 11A. Microbiology 152 : 313 321.
    • (2006) Microbiology , vol.152 , pp. 313-321
    • Camilli, R.1    Pettini, E.2    Grosso, M.D.3    Pozzi, G.4    Pantosti, A.5    Oggioni, M.R.6
  • 14
    • 2542425761 scopus 로고    scopus 로고
    • Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus
    • Carneiro, C.R., Postol, E., Nomizo, R., Reis, L.F. Brentani, R.R. (2004) Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus. Microbes Infect 6 : 604 608.
    • (2004) Microbes Infect , vol.6 , pp. 604-608
    • Carneiro, C.R.1    Postol, E.2    Nomizo, R.3    Reis, L.F.4    Brentani, R.R.5
  • 15
    • 2942718793 scopus 로고    scopus 로고
    • The three extra-cellular zinc metalloproteinases of Streptococcus pneumoniae have a different impact on virulence in mice
    • Chiavolini, D., Memmi, G., Maggi, T., Iannelli, F., Pozzi, G. Oggioni, M.R. (2003) The three extra-cellular zinc metalloproteinases of Streptococcus pneumoniae have a different impact on virulence in mice. BMC Microbiol 3 : 14.
    • (2003) BMC Microbiol , vol.3 , pp. 14
    • Chiavolini, D.1    Memmi, G.2    Maggi, T.3    Iannelli, F.4    Pozzi, G.5    Oggioni, M.R.6
  • 16
    • 0030041083 scopus 로고    scopus 로고
    • Extracellular matrix biology in the lung
    • Dunsmore, S.E. Rannels, D.E. (1996) Extracellular matrix biology in the lung. Am J Physiol 270 : L3 L27.
    • (1996) Am J Physiol , vol.270
    • Dunsmore, S.E.1    Rannels, D.E.2
  • 17
    • 31844450829 scopus 로고    scopus 로고
    • Adherence molecules of pathogenic pneumococci
    • Hammerschmidt, S. (2006) Adherence molecules of pathogenic pneumococci. Curr Opin Microbiol 9 : 12 20.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 12-20
    • Hammerschmidt, S.1
  • 18
  • 19
    • 0034786512 scopus 로고    scopus 로고
    • The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence
    • Holmes, A.R., McNab, R., Millsap, K.W., Rohde, M., Hammerschmidt, S., Mawdsley, J.L., et al. (2001) The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence. Mol Microbiol 41 : 1395 1408.
    • (2001) Mol Microbiol , vol.41 , pp. 1395-1408
    • Holmes, A.R.1    McNab, R.2    Millsap, K.W.3    Rohde, M.4    Hammerschmidt, S.5    Mawdsley, J.L.6
  • 20
    • 33749250965 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases protects mice from ascending infection and chronic disease manifestations resulting from urogenital Chlamydia muridarum infection
    • Imtiaz, M.T., Schripsema, J.H., Sigar, I.M., Kasimos, J.N. Ramsey, K.H. (2006) Inhibition of matrix metalloproteinases protects mice from ascending infection and chronic disease manifestations resulting from urogenital Chlamydia muridarum infection. Infect Immun 74 : 5513 5521.
    • (2006) Infect Immun , vol.74 , pp. 5513-5521
    • Imtiaz, M.T.1    Schripsema, J.H.2    Sigar, I.M.3    Kasimos, J.N.4    Ramsey, K.H.5
  • 21
    • 77954014575 scopus 로고    scopus 로고
    • PavB is a surface-exposed adhesin of Streptococcus pneumoniae contributing to nasopharyngeal colonization adn airways infections
    • Jensch, I., Gamez, G., Rothe, M., Ebert, S., Fulde, M., Somplatzki, D., et al. (2010) PavB is a surface-exposed adhesin of Streptococcus pneumoniae contributing to nasopharyngeal colonization adn airways infections. Mol Microbiol 77 : 22 43.
    • (2010) Mol Microbiol , vol.77 , pp. 22-43
    • Jensch, I.1    Gamez, G.2    Rothe, M.3    Ebert, S.4    Fulde, M.5    Somplatzki, D.6
  • 22
    • 0026876114 scopus 로고
    • Binding of laminin, type IV collagen, and vitronectin by Streptococcus pneumoniae
    • Kostrzynska, M. Wadstrom, T. (1992) Binding of laminin, type IV collagen, and vitronectin by Streptococcus pneumoniae. Zentralbl Bakteriol 277 : 80 83.
    • (1992) Zentralbl Bakteriol , vol.277 , pp. 80-83
    • Kostrzynska, M.1    Wadstrom, T.2
  • 23
    • 60549109675 scopus 로고    scopus 로고
    • Local and systemic responses in matrix metalloproteinase 8-deficient mice during Porphyromonas gingivalis-induced periodontitis
    • Kuula, H., Salo, T., Pirila, E., Tuomainen, A.M., Jauhiainen, M., Uitto, V.J., et al. (2009) Local and systemic responses in matrix metalloproteinase 8-deficient mice during Porphyromonas gingivalis-induced periodontitis. Infect Immun 77 : 850 859.
    • (2009) Infect Immun , vol.77 , pp. 850-859
    • Kuula, H.1    Salo, T.2    Pirila, E.3    Tuomainen, A.M.4    Jauhiainen, M.5    Uitto, V.J.6
  • 24
    • 28844504495 scopus 로고    scopus 로고
    • Pneumococcal phosphorylcholine esterase, Pce, contains a metal binuclear center that is essential for substrate binding and catalysis
    • Lagartera, L., Gonzalez, A., Hermoso, J.A., Saiz, J.L., Garcia, P., Garcia, J.L., et al. (2005) Pneumococcal phosphorylcholine esterase, Pce, contains a metal binuclear center that is essential for substrate binding and catalysis. Protein Sci 14 : 3013 3024.
    • (2005) Protein Sci , vol.14 , pp. 3013-3024
    • Lagartera, L.1    Gonzalez, A.2    Hermoso, J.A.3    Saiz, J.L.4    Garcia, P.5    Garcia, J.L.6
  • 25
    • 74049156843 scopus 로고    scopus 로고
    • Empyema hospitalizations increased in US children despite pneumococcal conjugate vaccine
    • Li, S.-T.T. Tancredi, D.J. (2009) Empyema hospitalizations increased in US children despite pneumococcal conjugate vaccine. Pediatrics 125 : 26 33.
    • (2009) Pediatrics , vol.125 , pp. 26-33
    • Li, S.-T.T.1    Tancredi, D.J.2
  • 26
    • 31844451911 scopus 로고    scopus 로고
    • Multifunctional role of choline binding protein G in pneumococcal pathogenesis
    • Mann, B., Orihuela, C., Antikainen, J., Gao, G., Sublett, J., Korhonen, T.K., et al. (2006) Multifunctional role of choline binding protein G in pneumococcal pathogenesis. Infect Immun 74 : 821 829.
    • (2006) Infect Immun , vol.74 , pp. 821-829
    • Mann, B.1    Orihuela, C.2    Antikainen, J.3    Gao, G.4    Sublett, J.5    Korhonen, T.K.6
  • 27
    • 43249127583 scopus 로고    scopus 로고
    • Procoagulant activity in children with community acquired pneumonia, pleural effusion and empyema
    • Michelin, E., Snijders, D., Conte, S., Via, P.D., Tagliaferro, T., Da Dalt, L., et al. (2008) Procoagulant activity in children with community acquired pneumonia, pleural effusion and empyema. Pediatr Pulmonol 43 : 472 475.
    • (2008) Pediatr Pulmonol , vol.43 , pp. 472-475
    • Michelin, E.1    Snijders, D.2    Conte, S.3    Via, P.D.4    Tagliaferro, T.5    Da Dalt, L.6
  • 28
    • 33746637557 scopus 로고    scopus 로고
    • Identification of a Candidate Streptococcus pneumoniae core genome and regions of diversity correlated with invasive pneumococcal disease
    • Obert, C., Sublett, J., Kaushal, D., Hinojosa, E., Barton, T., Tuomanen, E.I., et al. (2006) Identification of a Candidate Streptococcus pneumoniae core genome and regions of diversity correlated with invasive pneumococcal disease. Infect Immun 74 : 4766 4777.
    • (2006) Infect Immun , vol.74 , pp. 4766-4777
    • Obert, C.1    Sublett, J.2    Kaushal, D.3    Hinojosa, E.4    Barton, T.5    Tuomanen, E.I.6
  • 29
    • 0043166893 scopus 로고    scopus 로고
    • Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia
    • Oggioni, M.R., Memmi, G., Maggi, T., Chiavolini, D., Iannelli, F. Pozzi, G. (2003) Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia. Mol Microbiol 49 : 795 805.
    • (2003) Mol Microbiol , vol.49 , pp. 795-805
    • Oggioni, M.R.1    Memmi, G.2    Maggi, T.3    Chiavolini, D.4    Iannelli, F.5    Pozzi, G.6
  • 30
    • 6944224035 scopus 로고    scopus 로고
    • Tissue-specific contributions of pneumococcal virulence factors to pathogenesis
    • Orihuela, C.J., Gao, G., Francis, K.P., Yu, J. Tuomanen, E.I. (2004) Tissue-specific contributions of pneumococcal virulence factors to pathogenesis. J Infect Dis 190 : 1661 1669.
    • (2004) J Infect Dis , vol.190 , pp. 1661-1669
    • Orihuela, C.J.1    Gao, G.2    Francis, K.P.3    Yu, J.4    Tuomanen, E.I.5
  • 31
    • 67651007158 scopus 로고    scopus 로고
    • Laminin receptor initiates bacterial contact with the blood brain barrier in experimental meningitis models
    • Orihuela, C.J., Mahdavi, J., Thornton, J., Mann, B., Wooldridge, K.G., Abouseada, N., et al. (2009) Laminin receptor initiates bacterial contact with the blood brain barrier in experimental meningitis models. J Clin Invest 119 : 1638 1646.
    • (2009) J Clin Invest , vol.119 , pp. 1638-1646
    • Orihuela, C.J.1    Mahdavi, J.2    Thornton, J.3    Mann, B.4    Wooldridge, K.G.5    Abouseada, N.6
  • 32
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw, A., Ewald, A.J. Werb, Z. (2007) Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 8 : 221 233.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-Mccaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 33
    • 77951212739 scopus 로고    scopus 로고
    • Plasminogen- and fibronectin-binding protein B is involved in the adherence of Streptococcus pneumoniae to human epithelial cells
    • Papasergi, S., Garibaldi, M., Tuscano, G., Signorino, G., Ricci, S., Peppoloni, S., et al. (2010) Plasminogen- and fibronectin-binding protein B is involved in the adherence of Streptococcus pneumoniae to human epithelial cells. J Biol Chem 285 : 7517 7524.
    • (2010) J Biol Chem , vol.285 , pp. 7517-7524
    • Papasergi, S.1    Garibaldi, M.2    Tuscano, G.3    Signorino, G.4    Ricci, S.5    Peppoloni, S.6
  • 35
    • 67651215947 scopus 로고    scopus 로고
    • Host adhesive activities and virulence of novel fimbrial proteins of Porphyromonas gingivalis
    • Pierce, D.L., Nishiyama, S., Liang, S., Wang, M., Triantafilou, M., Triantafilou, K., et al. (2009) Host adhesive activities and virulence of novel fimbrial proteins of Porphyromonas gingivalis. Infect Immun 77 : 3294 3301.
    • (2009) Infect Immun , vol.77 , pp. 3294-3301
    • Pierce, D.L.1    Nishiyama, S.2    Liang, S.3    Wang, M.4    Triantafilou, M.5    Triantafilou, K.6
  • 36
    • 48749094614 scopus 로고    scopus 로고
    • Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge
    • Rose, L., Shivshankar, P., Hinojosa, E., Rodriguez, A., Sanchez, C.J. Orihuela, C.J. (2008) Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge. J Infect Dis 198 : 375 383.
    • (2008) J Infect Dis , vol.198 , pp. 375-383
    • Rose, L.1    Shivshankar, P.2    Hinojosa, E.3    Rodriguez, A.4    Sanchez, C.J.5    Orihuela, C.J.6
  • 37
    • 0030983804 scopus 로고    scopus 로고
    • Contribution of novel choline-binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae
    • Rosenow, C., Ryan, P., Weiser, J.N., Johnson, S., Fontan, P., Ortqvist, A., et al. (1997) Contribution of novel choline-binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae. Mol Microbiol 25 : 819 829.
    • (1997) Mol Microbiol , vol.25 , pp. 819-829
    • Rosenow, C.1    Ryan, P.2    Weiser, J.N.3    Johnson, S.4    Fontan, P.5    Ortqvist, A.6
  • 38
    • 77049248168 scopus 로고
    • Streptococcal enzymes in the treatment of pleural empyema
    • Salzberg, A.M. (1956) Streptococcal enzymes in the treatment of pleural empyema. South Med J 49 : 50 53.
    • (1956) South Med J , vol.49 , pp. 50-53
    • Salzberg, A.M.1
  • 39
    • 70350168050 scopus 로고    scopus 로고
    • The Streptococcus pneumoniae adhesin PsrP binds to Keratin 10 on lung cells
    • Shivshankar, P., Sanchez, C., Rose, L.F. Orihuela, C.J. (2009) The Streptococcus pneumoniae adhesin PsrP binds to Keratin 10 on lung cells. Mol Microbiol 73 : 663 679.
    • (2009) Mol Microbiol , vol.73 , pp. 663-679
    • Shivshankar, P.1    Sanchez, C.2    Rose, L.F.3    Orihuela, C.J.4
  • 40
    • 0037125989 scopus 로고    scopus 로고
    • Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype v Streptococcus agalactiae
    • Tettelin, H., Masignani, V., Cieslewicz, M.J., Eisen, J.A., Peterson, S., Wessels, M.R., et al. (2002) Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae. Proc Natl Acad Sci USA 99 : 12391 12396.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12391-12396
    • Tettelin, H.1    Masignani, V.2    Cieslewicz, M.J.3    Eisen, J.A.4    Peterson, S.5    Wessels, M.R.6
  • 41
    • 61349132103 scopus 로고    scopus 로고
    • PfbA, a novel plasmin- and fibronectin-binding protein of Streptococcus pneumoniae, contributes to fibronectin-dependent adhesion and antiphagocytosis
    • Yamaguchi, M., Terao, Y., Mori, Y., Hamada, S. Kawabata, S. (2008) PfbA, a novel plasmin- and fibronectin-binding protein of Streptococcus pneumoniae, contributes to fibronectin-dependent adhesion and antiphagocytosis. J Biol Chem 283 : 36272 36279.
    • (2008) J Biol Chem , vol.283 , pp. 36272-36279
    • Yamaguchi, M.1    Terao, Y.2    Mori, Y.3    Hamada, S.4    Kawabata, S.5


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