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Volumn 2, Issue 7, 2000, Pages 793-801

Signaling and invasin-promoted uptake via integrin receptors

Author keywords

Integrin; Invasin; Receptor; Signalling; Yersinia

Indexed keywords

FOCAL ADHESION KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; INTEGRIN RECEPTOR; INVASIN;

EID: 0033920740     PISSN: 12864579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1286-4579(00)90364-2     Document Type: Review
Times cited : (98)

References (50)
  • 1
    • 0030790687 scopus 로고    scopus 로고
    • Common themes in microbial pathogenicity revisited
    • Finlay B.B., Falkow S. Common themes in microbial pathogenicity revisited. Microbiol. Mol. Biol. Rev. 28:1997;136-169.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.28 , pp. 136-169
    • Finlay, B.B.1    Falkow, S.2
  • 2
    • 0032974532 scopus 로고    scopus 로고
    • Rupture of the intestinal epithelial barrier and mucosal invasion by Shigella flexneri
    • Sansonetti P.J., Tran Van Nhieu G., Egile C. Rupture of the intestinal epithelial barrier and mucosal invasion by Shigella flexneri. Clin. Infect. Dis. 30:1999;466-475.
    • (1999) Clin. Infect. Dis. , vol.30 , pp. 466-475
    • Sansonetti, P.J.1    Tran Van Nhieu, G.2    Egile, C.3
  • 3
    • 0031717496 scopus 로고    scopus 로고
    • Macrophage-dependent induction of the Salmonella pathogenicity island 2 type III secretion system and its role in intracellular survival
    • Cirillo D.M., Valdivia R.H., Monack D.M., Falkow S. Macrophage-dependent induction of the Salmonella pathogenicity island 2 type III secretion system and its role in intracellular survival. Mol. Microbiol. 65:1998;175-188.
    • (1998) Mol. Microbiol. , vol.65 , pp. 175-188
    • Cirillo, D.M.1    Valdivia, R.H.2    Monack, D.M.3    Falkow, S.4
  • 4
    • 0030845121 scopus 로고    scopus 로고
    • Invasin-dependent and invasin-independent pathways for translocation of Yersinia pseudotuberculosis across the Peyer's patch intestinal epithelium
    • Marra A., Isberg R.R. Invasin-dependent and invasin-independent pathways for translocation of Yersinia pseudotuberculosis across the Peyer's patch intestinal epithelium. Infect. Immun. 90:1997;3412-3421.
    • (1997) Infect. Immun , vol.90 , pp. 3412-3421
    • Marra, A.1    Isberg, R.R.2
  • 5
    • 0027182029 scopus 로고
    • Yersinia enterocolitica invasin: A primary role in the initiation of infection
    • Pepe J.C., Miller V.L. Yersinia enterocolitica invasin: a primary role in the initiation of infection. Proc. Natl. Acad. Sci. USA. 63:1993;6473-6477.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.63 , pp. 6473-6477
    • Pepe, J.C.1    Miller, V.L.2
  • 6
    • 0028807421 scopus 로고
    • Pathogenesis of defined invasion mutants of Yersinia enterocolitica in a BALB/c mouse model of infection
    • Pepe J.C., Wachtel M.R., Wagar E., Miller V.L. Pathogenesis of defined invasion mutants of Yersinia enterocolitica in a BALB/c mouse model of infection. Infect. Immun. 10:1995;4837-4848.
    • (1995) Infect. Immun. , vol.10 , pp. 4837-4848
    • Pepe, J.C.1    Wachtel, M.R.2    Wagar, E.3    Miller, V.L.4
  • 7
    • 0031002852 scopus 로고    scopus 로고
    • Yersinia enterocolitica: The charisma continues
    • Bottone E.J. Yersinia enterocolitica: the charisma continues. Clin. Microbiol. Rev. 18:1997;257-276.
    • (1997) Clin. Microbiol. Rev. , vol.18 , pp. 257-276
    • Bottone, E.J.1
  • 9
    • 0025250067 scopus 로고
    • Multiple β1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells
    • Isberg R.R., Leong J.M. Multiple β1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells. Cell. 69:1990;861-871.
    • (1990) Cell , vol.69 , pp. 861-871
    • Isberg, R.R.1    Leong, J.M.2
  • 10
    • 0026770377 scopus 로고
    • Integrins: Versatility, Modulation, Signaling in Cell Adhesion
    • Hynes R.O. Integrins: Versatility, Modulation, Signaling in Cell Adhesion. Cell. 66:1992;11-25.
    • (1992) Cell , vol.66 , pp. 11-25
    • Hynes, R.O.1
  • 11
    • 0031913037 scopus 로고    scopus 로고
    • M-cell surface b1 integrin expression and invasin-mediated targeting of Yersinia pseudotuberculosis to mouse Peyer's patch M cells
    • Clark M.A., Hirst B.H., Jepson M.A. M-cell surface b1 integrin expression and invasin-mediated targeting of Yersinia pseudotuberculosis to mouse Peyer's patch M cells. Infect. Immun. 62:1998;1237-1243.
    • (1998) Infect. Immun. , vol.62 , pp. 1237-1243
    • Clark, M.A.1    Hirst, B.H.2    Jepson, M.A.3
  • 13
    • 0030978909 scopus 로고    scopus 로고
    • The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, the associated accumulation of these proteins in peripheral focal adhesions
    • Persson C., Carballeira N., Wolf-Watz H., Fallman M. The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, the associated accumulation of these proteins in peripheral focal adhesions. EMBO J. 16:1997;2307-2318.
    • (1997) EMBO J. , vol.16 , pp. 2307-2318
    • Persson, C.1    Carballeira, N.2    Wolf-Watz, H.3    Fallman, M.4
  • 14
    • 0030913232 scopus 로고    scopus 로고
    • Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
    • Black D.S., Bliska J.B. Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J. 13:1997;2730-2744.
    • (1997) EMBO J. , vol.13 , pp. 2730-2744
    • Black, D.S.1    Bliska, J.B.2
  • 15
    • 0029421061 scopus 로고
    • Translocation of the Yersinia YopE and YopH virulence proteins into target cells is mediated by YopB and YopD
    • Rosqvist R., Persson C., Hakansson S., Nordfeldt R., Wolf-Watz H. Translocation of the Yersinia YopE and YopH virulence proteins into target cells is mediated by YopB and YopD. Contrib. Microbiol. Immunol. 65:1995;230-234.
    • (1995) Contrib. Microbiol. Immunol. , vol.65 , pp. 230-234
    • Rosqvist, R.1    Persson, C.2    Hakansson, S.3    Nordfeldt, R.4    Wolf-Watz, H.5
  • 16
    • 0031031294 scopus 로고    scopus 로고
    • Identification of a family of intimins common to Escherichia coli causing attaching-effacing lesions in rabbits, humans, swine
    • Agin T.S., Wolf M.K. Identification of a family of intimins common to Escherichia coli causing attaching-effacing lesions in rabbits, humans, swine. Infect. Immun. 65:1997;320-326.
    • (1997) Infect. Immun. , vol.65 , pp. 320-326
    • Agin, T.S.1    Wolf, M.K.2
  • 17
    • 1842376874 scopus 로고    scopus 로고
    • Intimin-dependent binding of enteropathogenic Escherichia coli to host cells triggers novel signaling events, including tyrosine phosphorylation of phospholipase C-gamma1
    • Kenny B., Finlay B.B. Intimin-dependent binding of enteropathogenic Escherichia coli to host cells triggers novel signaling events, including tyrosine phosphorylation of phospholipase C-gamma1. Infect. Immun. 9:1997;2528-2536.
    • (1997) Infect. Immun. , vol.9 , pp. 2528-2536
    • Kenny, B.1    Finlay, B.B.2
  • 18
    • 0025301659 scopus 로고
    • Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein
    • Leong J.M., Fournier R.S., Isberg R.R. Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein. EMBO J. 14:1990;1979-1989.
    • (1990) EMBO J. , vol.14 , pp. 1979-1989
    • Leong, J.M.1    Fournier, R.S.2    Isberg, R.R.3
  • 19
    • 0028855422 scopus 로고
    • An aspartate residue of the Yersinia pseudotuberculosis invasin protein that is critical for integrin binding
    • Leong J.M., Morrissey P.E., Marra A., Isberg R.R. An aspartate residue of the Yersinia pseudotuberculosis invasin protein that is critical for integrin binding. EMBO J. 84:1995;422-431.
    • (1995) EMBO J. , vol.84 , pp. 422-431
    • Leong, J.M.1    Morrissey, P.E.2    Marra, A.3    Isberg, R.R.4
  • 20
    • 0030050396 scopus 로고    scopus 로고
    • A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy D.J., Aukhil I., Erickson H.P. A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell. 271:1996;155-164.
    • (1996) Cell , vol.271 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 21
    • 0029811176 scopus 로고    scopus 로고
    • A region of the Yersinia pseudotuberculosis invasin protein that contributes to high affinity binding to integrin receptors
    • Saltman L.H., Lu Y., Zaharias E.M., Isberg R.R. A region of the Yersinia pseudotuberculosis invasin protein that contributes to high affinity binding to integrin receptors. J. Biol. Chem. 269:1996;23438-23444.
    • (1996) J. Biol. Chem. , vol.269 , pp. 23438-23444
    • Saltman, L.H.1    Lu, Y.2    Zaharias, E.M.3    Isberg, R.R.4
  • 22
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota S., Nomizu M., Yamada K.M. The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J. Biol. Chem. 286:1994;24756-24761.
    • (1994) J. Biol. Chem. , vol.286 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.M.3
  • 23
    • 0033536633 scopus 로고    scopus 로고
    • Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein
    • Hamburger Z.A., Brown M.S., Isberg R.R., Bjorkman P.J. Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein. Science. 18:1999;291-295.
    • (1999) Science , vol.18 , pp. 291-295
    • Hamburger, Z.A.1    Brown, M.S.2    Isberg, R.R.3    Bjorkman, P.J.4
  • 24
    • 0033105366 scopus 로고    scopus 로고
    • A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association
    • Dersch P., Isberg R.R. A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association. EMBO J. 163:1999;1199-1213.
    • (1999) EMBO J. , vol.163 , pp. 1199-1213
    • Dersch, P.1    Isberg, R.R.2
  • 25
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis W.I., Taylor M.E., Drickamer K. The C-type lectin superfamily in the immune system. Immunol. Rev. 266:1998;19-34.
    • (1998) Immunol. Rev. , vol.266 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 26
    • 0026343041 scopus 로고
    • The Yersinia pseudotuberculosis invasin protein and human fibronectin bind to mutually exclusive sites on the a5b1 integrin receptor
    • Tran Van, Nhieu G., Isberg R.R. The Yersinia pseudotuberculosis invasin protein and human fibronectin bind to mutually exclusive sites on the a5b1 integrin receptor. J. Biol. Chem. 60:1991;24367-24375.
    • (1991) J. Biol. Chem. , vol.60 , pp. 24367-24375
    • Tran, V.1    Nhieu, G.2    Isberg, R.R.3
  • 27
    • 0026737731 scopus 로고
    • The integrin-binding domain of invasin is sufficient to allow bacterial entry into mammalian cells
    • Rankin S., Isberg R.R., Leong J.M. The integrin-binding domain of invasin is sufficient to allow bacterial entry into mammalian cells. Infect. Immun. 12:1992;3909-3912.
    • (1992) Infect. Immun. , vol.12 , pp. 3909-3912
    • Rankin, S.1    Isberg, R.R.2    Leong, J.M.3
  • 28
    • 0027158079 scopus 로고
    • Bacterial internalization mediated by β1 chain integrins is determined by ligand affinity and receptor density
    • Tran, Van Nhieu G., Isberg R.R. Bacterial internalization mediated by β1 chain integrins is determined by ligand affinity and receptor density. EMBO J. 199:1993;1887-1895.
    • (1993) EMBO J. , vol.199 , pp. 1887-1895
    • Tran1    Van Nhieu, G.2    Isberg, R.R.3
  • 29
    • 0025858982 scopus 로고
    • Cultured human fibroblasts contain a large pool of precursor β1-integrin but lack an intracellular pool of mature subunit
    • Destrooper B., Van Leuven F., Carmeliet G., Van Den Berghe H., Cassiman J.J. Cultured human fibroblasts contain a large pool of precursor β1-integrin but lack an intracellular pool of mature subunit. Eur. J. Biochem. 1991;25-33.
    • (1991) Eur. J. Biochem. , pp. 25-33
    • Destrooper, B.1    Van Leuven, F.2    Carmeliet, G.3    Van Den Berghe, H.4    Cassiman, J.J.5
  • 30
    • 0026642556 scopus 로고
    • Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association
    • Reszka A.A., Hayashi Y., Horwitz A.F. Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association. J. Cell Biol. 268:1992.
    • (1992) J. Cell Biol. , vol.268
    • Reszka, A.A.1    Hayashi, Y.2    Horwitz, A.F.3
  • 31
    • 0027454485 scopus 로고
    • Mapping of the alpha-actinin binding site within the β1 integrin cytoplasmic domain
    • Otey C.A., Vasquez G.B., Burridge K., Erickson B.W. Mapping of the alpha-actinin binding site within the β1 integrin cytoplasmic domain. J. Biol. Chem. 130:1993;21193-21197.
    • (1993) J. Biol. Chem. , vol.130 , pp. 21193-21197
    • Otey, C.A.1    Vasquez, G.B.2    Burridge, K.3    Erickson, B.W.4
  • 32
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains
    • Schaller M.D., Otey C.A., Hildebrand J.D., Parsons J.T. Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains. J. Cell Biol. 274:1995;1181-1187.
    • (1995) J. Cell Biol. , vol.274 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 33
    • 0032590074 scopus 로고    scopus 로고
    • Interaction of the integrin β1 cytoplasmic domain with ICAP-1 protein
    • Zhang X.A., Hemler M.E. Interaction of the integrin β1 cytoplasmic domain with ICAP-1 protein. J. Biol. Chem. 271:1999;11-19.
    • (1999) J. Biol. Chem. , vol.271 , pp. 11-19
    • Zhang, X.A.1    Hemler, M.E.2
  • 34
    • 0013549674 scopus 로고    scopus 로고
    • Mutations in the cytoplasmic domain of the integrin β1 chain indicate a role for endocytosis factors in bacterial internalization
    • Tran Van, Nhieu G., Krukonis E.S., Reszka A.A., Horwitz A.F., Isberg R.R. Mutations in the cytoplasmic domain of the integrin β1 chain indicate a role for endocytosis factors in bacterial internalization. J. Biol. Chem. 15:1996;7665-7672.
    • (1996) J. Biol. Chem. , vol.15 , pp. 7665-7672
    • Tran Van1    Nhieu, G.2    Krukonis, E.S.3    Reszka, A.A.4    Horwitz, A.F.5    Isberg, R.R.6
  • 35
    • 0027352270 scopus 로고
    • Exploitation of host signal transduction pathways and cytoskeletal functions by invasive bacteria
    • Rosenshine I., Finlay B.B. Exploitation of host signal transduction pathways and cytoskeletal functions by invasive bacteria. Bioessays. 88:1993;17-24.
    • (1993) Bioessays , vol.88 , pp. 17-24
    • Rosenshine, I.1    Finlay, B.B.2
  • 36
    • 0025972090 scopus 로고
    • Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant
    • Bliska J.B., Guan K.L., Dixon J.E., Falkow S. Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant. Proc. Natl. Acad. Sci. USA. 27:1991;1187-1191.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.27 , pp. 1187-1191
    • Bliska, J.B.1    Guan, K.L.2    Dixon, J.E.3    Falkow, S.4
  • 37
    • 0031983624 scopus 로고    scopus 로고
    • The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton
    • Fu Y., Galan J.E. The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton. Mol. Microbiol. 401:1998;359-368.
    • (1998) Mol. Microbiol. , vol.401 , pp. 359-368
    • Fu, Y.1    Galan, J.E.2
  • 38
    • 0033575956 scopus 로고    scopus 로고
    • A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu Y., Galan J.E. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature. 13:1999;293-297.
    • (1999) Nature , vol.13 , pp. 293-297
    • Fu, Y.1    Galan, J.E.2
  • 39
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist R., Magnusson K.E., Wolf W.H. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 17:1994;964-972.
    • (1994) EMBO J. , vol.17 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf, W.H.3
  • 40
    • 0031032777 scopus 로고    scopus 로고
    • Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: Involvement of the Grb2, p130cas, Nck adaptor proteins
    • Schlaepfer D.D., Broome M.A., Hunter T. Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, Nck adaptor proteins. Mol. Cell. Biol. 14:1997;1702-1713.
    • (1997) Mol. Cell. Biol. , vol.14 , pp. 1702-1713
    • Schlaepfer, D.D.1    Broome, M.A.2    Hunter, T.3
  • 41
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller M.D., Hildebrand J.D., Shannon J.D., Fox J.W., Vines R.R., Parsons J.T. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol. Cell Biol. 110:1994;1680-1688.
    • (1994) Mol. Cell Biol. , vol.110 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 42
    • 0031044781 scopus 로고    scopus 로고
    • Focal adhesion kinase: At the crossroads of signal transduction
    • Ilic D., Damsky C.H., Yamamoto T. Focal adhesion kinase: at the crossroads of signal transduction. J. Cell. Sci. 377:1997;401-407.
    • (1997) J. Cell. Sci. , vol.377 , pp. 401-407
    • Ilic, D.1    Damsky, C.H.2    Yamamoto, T.3
  • 44
    • 0032506002 scopus 로고    scopus 로고
    • Involvement of focal adhesion kinase in invasin-mediated uptake
    • Alrutz M.A., Isberg R.R. Involvement of focal adhesion kinase in invasin-mediated uptake. Proc. Natl. Acad. Sci. USA. 375:1998;13658-13663.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.375 , pp. 13658-13663
    • Alrutz, M.A.1    Isberg, R.R.2
  • 46
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon N., Hall A. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9:1997;86-92.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 47
    • 0033231935 scopus 로고    scopus 로고
    • The world according to Arp: Regulation of actin nucleation by the Arp2/3 complex
    • Welch M.D. The world according to Arp: regulation of actin nucleation by the Arp2/3 complex. Trends Cell Biol. 17:1999;423-427.
    • (1999) Trends Cell Biol. , vol.17 , pp. 423-427
    • Welch, M.D.1
  • 48
    • 0032403083 scopus 로고    scopus 로고
    • WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac
    • Miki H., Suetsugu S., Takenawa T. WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 95:1998;6932-6941.
    • (1998) EMBO J. , vol.95 , pp. 6932-6941
    • Miki, H.1    Suetsugu, S.2    Takenawa, T.3
  • 49
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Locher K.P., Rees B., Koebnik R., Mitschler A., Mouliner L., Rosenbusch J.P., Moras D. Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell. 82:1998;771-778.
    • (1998) Cell , vol.82 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Mouliner, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 50
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science. 1998;2215-2220.
    • (1998) Science , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5


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