메뉴 건너뛰기




Volumn 58, Issue 2, 2009, Pages 171-177

Differential expression of surface glycoconjugates on Entamoeba histolytica and Entamoeba dispar

Author keywords

Entamoeba dispar; Entamoeba histolytica; Glycoconjugates; Protozoa; Surface properties; Virulence

Indexed keywords

GALACTOSAMINE; GLYCOCONJUGATE; LECTIN; MANNOSE; N ACETYL ALPHA GALACTOSAMINE; UNCLASSIFIED DRUG; N ACETYLGALACTOSAMINE;

EID: 67349098551     PISSN: 13835769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.parint.2009.02.003     Document Type: Article
Times cited : (7)

References (45)
  • 1
    • 33845423619 scopus 로고    scopus 로고
    • Transcriptomic comparison of two Entamoeba histolytica strains with defined virulence phenotypes identifies new virulence factor candidates and key differences in the expression patterns of cysteine proteases, lectin light chains, and calmodulin
    • Davis P.H., Schulze J., and Stanley Jr. S.L. Transcriptomic comparison of two Entamoeba histolytica strains with defined virulence phenotypes identifies new virulence factor candidates and key differences in the expression patterns of cysteine proteases, lectin light chains, and calmodulin. Mol Biochem Parasitol 151 (2007) 118-128
    • (2007) Mol Biochem Parasitol , vol.151 , pp. 118-128
    • Davis, P.H.1    Schulze, J.2    Stanley Jr., S.L.3
  • 2
    • 0020045984 scopus 로고
    • Biochemical homogeneity of Entamoeba histolytica isolates, especially those from liver abscess
    • Sargeaunt P.G., Jackson T.F., and Simjee A. Biochemical homogeneity of Entamoeba histolytica isolates, especially those from liver abscess. Lancet 1 (1982) 1386-1388
    • (1982) Lancet , vol.1 , pp. 1386-1388
    • Sargeaunt, P.G.1    Jackson, T.F.2    Simjee, A.3
  • 4
    • 33846369588 scopus 로고    scopus 로고
    • Comparison of the proteome profiles of Entamoeba histolytica and its close but non-pathogenic relative Entamoeba dispar
    • Leitsch D., Wilson I.B., Paschinger K., and Duchene M. Comparison of the proteome profiles of Entamoeba histolytica and its close but non-pathogenic relative Entamoeba dispar. Wien Klin Wochenschr 118 (2006) 37-41
    • (2006) Wien Klin Wochenschr , vol.118 , pp. 37-41
    • Leitsch, D.1    Wilson, I.B.2    Paschinger, K.3    Duchene, M.4
  • 5
    • 20444482805 scopus 로고    scopus 로고
    • Entamoeba histolytica: the serine-rich gene polymorphism-based genetic variability of clinical isolates from Georgia
    • Simonishvili S., Tsanava S., Sanadze K., Chlikadze R., Miskalishvili A., Lomkatsi N., et al. Entamoeba histolytica: the serine-rich gene polymorphism-based genetic variability of clinical isolates from Georgia. Exp Parasitol 110 (2005) 313-317
    • (2005) Exp Parasitol , vol.110 , pp. 313-317
    • Simonishvili, S.1    Tsanava, S.2    Sanadze, K.3    Chlikadze, R.4    Miskalishvili, A.5    Lomkatsi, N.6
  • 6
    • 33748486043 scopus 로고    scopus 로고
    • Comparative proteomic analysis of two Entamoeba histolytica strains with different virulence phenotypes identifies peroxiredoxin as an important component of amoebic virulence
    • Davis P.H., Zhang X., Guo J., Townsend R.R., and Stanley Jr. S.L. Comparative proteomic analysis of two Entamoeba histolytica strains with different virulence phenotypes identifies peroxiredoxin as an important component of amoebic virulence. Mol Microbiol 61 (2006) 1523-1532
    • (2006) Mol Microbiol , vol.61 , pp. 1523-1532
    • Davis, P.H.1    Zhang, X.2    Guo, J.3    Townsend, R.R.4    Stanley Jr., S.L.5
  • 7
    • 0032918535 scopus 로고    scopus 로고
    • Antisense inhibition of expression of cysteine proteinases affects Entamoeba histolytica-induced formation of liver abscess in hamsters
    • Ankri S., Stolarsky T., Bracha R., Padilla-Vaca F., and Mirelman D. Antisense inhibition of expression of cysteine proteinases affects Entamoeba histolytica-induced formation of liver abscess in hamsters. Infect Immun 67 (1999) 421-422
    • (1999) Infect Immun , vol.67 , pp. 421-422
    • Ankri, S.1    Stolarsky, T.2    Bracha, R.3    Padilla-Vaca, F.4    Mirelman, D.5
  • 9
    • 0020414785 scopus 로고
    • Entamoeba histolytica cytotoxin: purification, characterization, strain virulence, and protease activity
    • McGowan K., Deneke C.F., Thorne G.M., and Gorbach S.L. Entamoeba histolytica cytotoxin: purification, characterization, strain virulence, and protease activity. J Infect Dis 146 (1982) 616-625
    • (1982) J Infect Dis , vol.146 , pp. 616-625
    • McGowan, K.1    Deneke, C.F.2    Thorne, G.M.3    Gorbach, S.L.4
  • 10
    • 0031045223 scopus 로고    scopus 로고
    • Virulent and avirulent Entamoeba histolytica and E. dispar differ in their cell surface phosphorylated glycolipids
    • Moody S., Becker S., Nuchamowitz Y., and Mirelman D. Virulent and avirulent Entamoeba histolytica and E. dispar differ in their cell surface phosphorylated glycolipids. Parasitology 114 Pt 2 (1997) 95-104
    • (1997) Parasitology , vol.114 , Issue.PART 2 , pp. 95-104
    • Moody, S.1    Becker, S.2    Nuchamowitz, Y.3    Mirelman, D.4
  • 11
    • 15944400645 scopus 로고    scopus 로고
    • A lysine- and glutamic acid-rich protein, KERP1, from Entamoeba histolytica binds to human enterocytes
    • Seigneur M., Mounier J., Prevost M.C., and Guillen N. A lysine- and glutamic acid-rich protein, KERP1, from Entamoeba histolytica binds to human enterocytes. Cell Microbiol 7 (2005) 569-579
    • (2005) Cell Microbiol , vol.7 , pp. 569-579
    • Seigneur, M.1    Mounier, J.2    Prevost, M.C.3    Guillen, N.4
  • 12
    • 0015848459 scopus 로고
    • Selective agglutination of pathogenic strains of Entamoeba histolytica induced con A
    • Martinez-Palomo A., Gonzalez-Robles A., and De la Torre M. Selective agglutination of pathogenic strains of Entamoeba histolytica induced con A. Nat New Biol 245 (1973) 186-187
    • (1973) Nat New Biol , vol.245 , pp. 186-187
    • Martinez-Palomo, A.1    Gonzalez-Robles, A.2    De la Torre, M.3
  • 13
    • 0017364925 scopus 로고
    • Surface properties related to concanavalin A-induced agglutination. A comparative study of several Entamoeba strains
    • Trissl D., Martinez-Palomo A., Argüello C., de la Torre M., and de la Hoz R. Surface properties related to concanavalin A-induced agglutination. A comparative study of several Entamoeba strains. J Exp Med 145 (1977) 652-665
    • (1977) J Exp Med , vol.145 , pp. 652-665
    • Trissl, D.1    Martinez-Palomo, A.2    Argüello, C.3    de la Torre, M.4    de la Hoz, R.5
  • 14
    • 0018942558 scopus 로고
    • Cytopathogenic mechanisms of Entamoeba histolytica
    • Ravdin J.I., Croft B.Y., and Guerrant R.L. Cytopathogenic mechanisms of Entamoeba histolytica. J Exp Med 152 (1980) 377-390
    • (1980) J Exp Med , vol.152 , pp. 377-390
    • Ravdin, J.I.1    Croft, B.Y.2    Guerrant, R.L.3
  • 15
    • 0019850043 scopus 로고
    • Role of adherence in cytopathogenic mechanisms of Entamoeba histolytica. Study with mammalian tissue culture cells and human erythrocytes
    • Ravdin J.I., and Guerrant R.L. Role of adherence in cytopathogenic mechanisms of Entamoeba histolytica. Study with mammalian tissue culture cells and human erythrocytes. J Clin Invest 68 (1981) 1305-1313
    • (1981) J Clin Invest , vol.68 , pp. 1305-1313
    • Ravdin, J.I.1    Guerrant, R.L.2
  • 16
    • 0032413133 scopus 로고    scopus 로고
    • Royal Society of Tropical Medicine and Hygiene Meeting at Manson House, London, 19 February 1998. Amoebic disease. Entamoeba histolytica and E. dispar: Comparison of molecules considered important for host tissue destruction
    • Tannich E. Royal Society of Tropical Medicine and Hygiene Meeting at Manson House, London, 19 February 1998. Amoebic disease. Entamoeba histolytica and E. dispar: comparison of molecules considered important for host tissue destruction. Trans R Soc Trop Med Hyg 1998;92:593-596.
    • (1998) Trans R Soc Trop Med Hyg , vol.92 , pp. 593-596
    • Tannich, E.1
  • 17
    • 0017846267 scopus 로고
    • A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba
    • Diamond L.S., Harlow D.R., and Cunnick C.C. A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba. Trans R Soc Trop Med Hyg 72 (1978) 431-432
    • (1978) Trans R Soc Trop Med Hyg , vol.72 , pp. 431-432
    • Diamond, L.S.1    Harlow, D.R.2    Cunnick, C.C.3
  • 18
    • 0029295951 scopus 로고
    • YI-S, a casein-free medium for axenic cultivation of Entamoeba histolytica, related Entamoeba, Giardia intestinalis and Trichomonas vaginalis
    • Diamond L.S., Clark C.G., and Cunnick C.C. YI-S, a casein-free medium for axenic cultivation of Entamoeba histolytica, related Entamoeba, Giardia intestinalis and Trichomonas vaginalis. J Eukaryot Microbiol 42 (1995) 277-278
    • (1995) J Eukaryot Microbiol , vol.42 , pp. 277-278
    • Diamond, L.S.1    Clark, C.G.2    Cunnick, C.C.3
  • 19
    • 1242270550 scopus 로고    scopus 로고
    • In vitro and in vivo interaction of Entamoeba histolytica Gal/GalNAc lectin with various target cells: an immunocytochemical analysis
    • Pacheco J., Shibayama M., Campos R., Beck D.L., Houpt E., Petri Jr. W.A., et al. In vitro and in vivo interaction of Entamoeba histolytica Gal/GalNAc lectin with various target cells: an immunocytochemical analysis. Parasitol Int 53 (2004) 35-47
    • (2004) Parasitol Int , vol.53 , pp. 35-47
    • Pacheco, J.1    Shibayama, M.2    Campos, R.3    Beck, D.L.4    Houpt, E.5    Petri Jr., W.A.6
  • 22
    • 0014645531 scopus 로고
    • High-yield preparation of isolated rat liver parenchymal cells: a biochemical and fine structural study
    • Berry M.N., and Friend D.S. High-yield preparation of isolated rat liver parenchymal cells: a biochemical and fine structural study. J Cell Biol 43 (1969) 506-520
    • (1969) J Cell Biol , vol.43 , pp. 506-520
    • Berry, M.N.1    Friend, D.S.2
  • 23
    • 40749110280 scopus 로고    scopus 로고
    • Participation of the serine-rich Entamoeba histolytica protein in amebic phagocytosis of apoptotic host cells
    • Teixeira J.E., and Huston C.D. Participation of the serine-rich Entamoeba histolytica protein in amebic phagocytosis of apoptotic host cells. Infect Immun 76 (2008) 959-966
    • (2008) Infect Immun , vol.76 , pp. 959-966
    • Teixeira, J.E.1    Huston, C.D.2
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76 (1979) 4350-4354
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 25
    • 0029052976 scopus 로고
    • Calorimetric analysis of the binding of lectins with overlapping carbohydrate-binding ligand specificities
    • Chervenak M.C., and Toone E.J. Calorimetric analysis of the binding of lectins with overlapping carbohydrate-binding ligand specificities. Biochemistry 34 (1995) 5685-5695
    • (1995) Biochemistry , vol.34 , pp. 5685-5695
    • Chervenak, M.C.1    Toone, E.J.2
  • 26
    • 0034851060 scopus 로고    scopus 로고
    • Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition process
    • Barre A., Bourne Y., Van Damme E.J., Peumans W.J., and Rouge P. Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition process. Biochimie 83 (2001) 645-651
    • (2001) Biochimie , vol.83 , pp. 645-651
    • Barre, A.1    Bourne, Y.2    Van Damme, E.J.3    Peumans, W.J.4    Rouge, P.5
  • 27
    • 0033593246 scopus 로고    scopus 로고
    • Crystal structure of a dimeric mannose-specific agglutinin from garlic: quaternary association and carbohydrate specificity
    • Chandra N.R., Ramachandraiah G., Bachhawat K., Dam T.K., Surolia A., and Vijayan M. Crystal structure of a dimeric mannose-specific agglutinin from garlic: quaternary association and carbohydrate specificity. J Mol Biol 285 (1999) 1157-1168
    • (1999) J Mol Biol , vol.285 , pp. 1157-1168
    • Chandra, N.R.1    Ramachandraiah, G.2    Bachhawat, K.3    Dam, T.K.4    Surolia, A.5    Vijayan, M.6
  • 28
    • 0018948310 scopus 로고
    • Attachment and short-term maintenance of motility and viability of Entamoeba histolytica in a defined medium
    • Gillin F.D., and Diamond L.S. Attachment and short-term maintenance of motility and viability of Entamoeba histolytica in a defined medium. J Protozool 27 (1980) 220-225
    • (1980) J Protozool , vol.27 , pp. 220-225
    • Gillin, F.D.1    Diamond, L.S.2
  • 29
    • 0024286486 scopus 로고
    • Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb
    • Shibuya N., Goldstein I.J., Van Damme E.J., and Peumans W.J. Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb. J Biol Chem 263 (1988) 728-734
    • (1988) J Biol Chem , vol.263 , pp. 728-734
    • Shibuya, N.1    Goldstein, I.J.2    Van Damme, E.J.3    Peumans, W.J.4
  • 30
    • 0019572737 scopus 로고
    • Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins
    • Debray H., Decout D., Strecker G., Spik G., and Montreuil J. Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins. Eur J Biochem 117 (1981) 41-55
    • (1981) Eur J Biochem , vol.117 , pp. 41-55
    • Debray, H.1    Decout, D.2    Strecker, G.3    Spik, G.4    Montreuil, J.5
  • 31
    • 0017227759 scopus 로고
    • Purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity
    • Allen A.K., Desai N.N., and Neuberger A. Purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity. Biochem J 155 (1976) 127-135
    • (1976) Biochem J , vol.155 , pp. 127-135
    • Allen, A.K.1    Desai, N.N.2    Neuberger, A.3
  • 32
    • 0027314952 scopus 로고
    • X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 A resolution
    • Rini J.M., Hardman K.D., Einspahr H., Suddath F.L., and Carver J.P. X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 A resolution. J Biol Chem 268 (1993) 10126-10132
    • (1993) J Biol Chem , vol.268 , pp. 10126-10132
    • Rini, J.M.1    Hardman, K.D.2    Einspahr, H.3    Suddath, F.L.4    Carver, J.P.5
  • 33
    • 0032033602 scopus 로고    scopus 로고
    • Identification of significant variation in the composition of lipophosphoglycan-like molecules of E. histolytica and E. dispar
    • Moody S., Becker S., Nuchamowitz Y., and Mirelman D. Identification of significant variation in the composition of lipophosphoglycan-like molecules of E. histolytica and E. dispar. J Eukaryot Microbiol 45 (1998) 9S-12S
    • (1998) J Eukaryot Microbiol , vol.45
    • Moody, S.1    Becker, S.2    Nuchamowitz, Y.3    Mirelman, D.4
  • 34
    • 0023620359 scopus 로고
    • Use of antibodies to characterize a 220-kilodalton surface protein from Entamoeba histolytica
    • Meza I., Cazares F., Rosales-Encina J.L., Talamas-Rohana P., and Rojkind M. Use of antibodies to characterize a 220-kilodalton surface protein from Entamoeba histolytica. J Infect Dis 156 (1987) 798-805
    • (1987) J Infect Dis , vol.156 , pp. 798-805
    • Meza, I.1    Cazares, F.2    Rosales-Encina, J.L.3    Talamas-Rohana, P.4    Rojkind, M.5
  • 35
    • 0021918960 scopus 로고
    • N-Acetyl-d-galactosamine-inhibitable adherence lectin of Entamoeba histolytica. I. Partial purification and relation to amoebic virulence in vitro
    • Ravdin J.I., Murphy C.F., Salata R.A., Guerrant R.L., and Hewlett E.L. N-Acetyl-d-galactosamine-inhibitable adherence lectin of Entamoeba histolytica. I. Partial purification and relation to amoebic virulence in vitro. J Infect Dis 151 (1985) 804-815
    • (1985) J Infect Dis , vol.151 , pp. 804-815
    • Ravdin, J.I.1    Murphy, C.F.2    Salata, R.A.3    Guerrant, R.L.4    Hewlett, E.L.5
  • 36
    • 0023138352 scopus 로고
    • Localization and identification of an Entamoeba histolytica adhesin
    • Arroyo R., and Orozco E. Localization and identification of an Entamoeba histolytica adhesin. Mol Biochem Parasitol 23 (1987) 151-158
    • (1987) Mol Biochem Parasitol , vol.23 , pp. 151-158
    • Arroyo, R.1    Orozco, E.2
  • 37
    • 0023897945 scopus 로고
    • Binding, uptake, and transcytosis of ligands for mannose-specific receptors in rat liver: an electron microscopic study
    • Kempka G., and Kolb-Bachofen V. Binding, uptake, and transcytosis of ligands for mannose-specific receptors in rat liver: an electron microscopic study. Exp Cell Res 176 (1988) 38-48
    • (1988) Exp Cell Res , vol.176 , pp. 38-48
    • Kempka, G.1    Kolb-Bachofen, V.2
  • 38
    • 28044469503 scopus 로고    scopus 로고
    • The asialoglycoprotein receptor clears glycoconjugates terminating with sialic acid alpha 2,6GalNAc
    • Park E.I., Mi Y., Unverzagt C., Gabius H.J., and Baenziger J.U. The asialoglycoprotein receptor clears glycoconjugates terminating with sialic acid alpha 2,6GalNAc. Proc Natl Acad Sci U S A 102 (2005) 17125-17129
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17125-17129
    • Park, E.I.1    Mi, Y.2    Unverzagt, C.3    Gabius, H.J.4    Baenziger, J.U.5
  • 39
    • 0035135808 scopus 로고    scopus 로고
    • Carbohydrate moieties of the interstitial and glandular tissues of the amphibian Pleurodeles waltl testis shown by lectin histochemistry
    • Saez F.J., Madrid J.F., Aparicio R., Hernandez F., and Alonso E. Carbohydrate moieties of the interstitial and glandular tissues of the amphibian Pleurodeles waltl testis shown by lectin histochemistry. J Anat 198 (2001) 47-56
    • (2001) J Anat , vol.198 , pp. 47-56
    • Saez, F.J.1    Madrid, J.F.2    Aparicio, R.3    Hernandez, F.4    Alonso, E.5
  • 40
    • 49649095473 scopus 로고    scopus 로고
    • Unique Asn-linked oligosaccharides of the human pathogen Entamoeba histolytica
    • Magnelli P., Cipollo J.F., Ratner D.M., Cui J., Kelleher D., Gilmore R., et al. Unique Asn-linked oligosaccharides of the human pathogen Entamoeba histolytica. J Biol Chem 283 (2008) 18355-18364
    • (2008) J Biol Chem , vol.283 , pp. 18355-18364
    • Magnelli, P.1    Cipollo, J.F.2    Ratner, D.M.3    Cui, J.4    Kelleher, D.5    Gilmore, R.6
  • 41
    • 0026345423 scopus 로고
    • Sequence of a cysteine-rich galactose-specific lectin of Entamoeba histolytica
    • Mann B.J., Torian B.E., Vedvick T.S., and Petri Jr. W.A. Sequence of a cysteine-rich galactose-specific lectin of Entamoeba histolytica. Proc Natl Acad Sci U S A 88 (1991) 3248-3252
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3248-3252
    • Mann, B.J.1    Torian, B.E.2    Vedvick, T.S.3    Petri Jr., W.A.4
  • 42
    • 34447334535 scopus 로고    scopus 로고
    • Differential in vitro inhibitory activity against HIV-1 of alpha-(1-3)- and alpha-(1-6)-d-mannose specific plant lectins: implication for microbicide development
    • Saidi H., Nasreddine N., Jenabian M.A., Lecerf M., Schols D., Krief C., et al. Differential in vitro inhibitory activity against HIV-1 of alpha-(1-3)- and alpha-(1-6)-d-mannose specific plant lectins: implication for microbicide development. J Transl Med 5 (2007) 28
    • (2007) J Transl Med , vol.5 , pp. 28
    • Saidi, H.1    Nasreddine, N.2    Jenabian, M.A.3    Lecerf, M.4    Schols, D.5    Krief, C.6
  • 43
    • 4644227155 scopus 로고    scopus 로고
    • Mannose-specific plant lectins from the Amaryllidaceae family qualify as efficient microbicides for prevention of human immunodeficiency virus infection
    • Balzarini J., Hatse S., Vermeire K., Princen K., Aquaro S., Perno C.F., et al. Mannose-specific plant lectins from the Amaryllidaceae family qualify as efficient microbicides for prevention of human immunodeficiency virus infection. Antimicrob Agents Chemother 48 (2004) 3858-3870
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3858-3870
    • Balzarini, J.1    Hatse, S.2    Vermeire, K.3    Princen, K.4    Aquaro, S.5    Perno, C.F.6
  • 44
    • 0026020005 scopus 로고
    • Alpha-(1-3)- and alpha-(1-6)-d-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro
    • Balzarini J., Schols D., Neyts J., Van Damme E., Peumans W., and De Clercq E. Alpha-(1-3)- and alpha-(1-6)-d-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro. Antimicrob Agents Chemother 35 (1991) 410-416
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 410-416
    • Balzarini, J.1    Schols, D.2    Neyts, J.3    Van Damme, E.4    Peumans, W.5    De Clercq, E.6
  • 45
    • 0027267428 scopus 로고
    • Envelope glycoproteins of HIV-1, HIV-2, and SIV purified with Galanthus nivalis agglutinin induce strong immune responses
    • Gilljam G. Envelope glycoproteins of HIV-1, HIV-2, and SIV purified with Galanthus nivalis agglutinin induce strong immune responses. AIDS Res Hum Retrovir 9 (1993) 431-438
    • (1993) AIDS Res Hum Retrovir , vol.9 , pp. 431-438
    • Gilljam, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.