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Volumn 79, Issue 6, 2005, Pages 3822-3830

Complementarity in the supramolecular design of arenaviruses and retroviruses revealed by electron cryomicroscopy and image analysis

Author keywords

[No Author keywords available]

Indexed keywords

GENOMIC RNA; PHOSPHOLIPID; STRUCTURAL PROTEIN; VIRUS GLYCOPROTEIN; VIRUS NUCLEOPROTEIN; VIRUS PROTEIN; VIRUS SPIKE PROTEIN;

EID: 14744278960     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.6.3822-3830.2005     Document Type: Article
Times cited : (73)

References (51)
  • 1
    • 0022263256 scopus 로고
    • Electron microscopy of influenza virus. A comparison of negatively stained and ice-embedded particles
    • Booy, F. P., R. W. H. Ruigrok, and E. F. J. van Bruggen. 1985. Electron microscopy of influenza virus. A comparison of negatively stained and ice-embedded particles. J. Mol. Biol. 184:667-676.
    • (1985) J. Mol. Biol. , vol.184 , pp. 667-676
    • Booy, F.P.1    Ruigrok, R.W.H.2    Van Bruggen, E.F.J.3
  • 2
    • 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. 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.M.1
  • 3
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • Briggs, J. G., T. Wilk, R. Welker, H.-G. Kraüsslich, and S. D. Fuller. 2003. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J. 22:1707-1715.
    • (2003) EMBO J. , vol.22 , pp. 1707-1715
    • Briggs, J.G.1    Wilk, T.2    Welker, R.3    Kraüsslich, H.-G.4    Fuller, S.D.5
  • 4
    • 0002244194 scopus 로고
    • Glycoproteins of the arenaviruses
    • M. S. Salvato (ed.), Plenum Press, New York, N.Y.
    • Burns, J. W., and M. J. Buchmeier. 1993. Glycoproteins of the arenaviruses, p. 17-35. In M. S. Salvato (ed.), The Arenaviridae. Plenum Press, New York, N.Y.
    • (1993) The Arenaviridae , pp. 17-35
    • Burns, J.W.1    Buchmeier, M.J.2
  • 5
    • 0025908807 scopus 로고
    • Protein-protein interactions in lymphocytic choriomeningitis virus
    • Burns, J. W., and M. J. Buchmeier. 1991. Protein-protein interactions in lymphocytic choriomeningitis virus. Virology 183:620-629.
    • (1991) Virology , vol.183 , pp. 620-629
    • Burns, J.W.1    Buchmeier, M.J.2
  • 6
    • 0026788442 scopus 로고
    • Structure of the Escherichia coli ATP synthase and role of the gamma and epsilon subunits in coupling catalytic site and proton channeling functions
    • Capaldi, R. A., R. Aggeler, E. P. Gogol, and S. Wilkens. 1992. Structure of the Escherichia coli ATP synthase and role of the gamma and epsilon subunits in coupling catalytic site and proton channeling functions. J. Bioenerg. Biomembr. 24:435-439.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 435-439
    • Capaldi, R.A.1    Aggeler, R.2    Gogol, E.P.3    Wilkens, S.4
  • 7
    • 0036281854 scopus 로고    scopus 로고
    • Characterization of the arenavirus RING finger Z protein regions required for Z-mediated inhibition of viral RNA synthesis
    • Cornu, T. I., and J. C. de la Torre. 2002. Characterization of the arenavirus RING finger Z protein regions required for Z-mediated inhibition of viral RNA synthesis. J. Virol. 76:6678-6688.
    • (2002) J. Virol. , vol.76 , pp. 6678-6688
    • Cornu, T.I.1    De La Torre, J.C.2
  • 8
    • 0034855641 scopus 로고    scopus 로고
    • RING finger Z protein of lymphocytic choriomeningitis virus (LCMV) inhibits transcription and RNA replication of an LCMV S-segment minigenome
    • Cornu, T. I., and J. C. de la Torre. 2001. RING finger Z protein of lymphocytic choriomeningitis virus (LCMV) inhibits transcription and RNA replication of an LCMV S-segment minigenome. J. Virol. 75:9415-9426.
    • (2001) J. Virol. , vol.75 , pp. 9415-9426
    • Cornu, T.I.1    De La Torre, J.C.2
  • 9
    • 0029042344 scopus 로고
    • Kinetics and pH dependence of acid-induced structural changes in the lymphocytic choriomeningitis virus glycoprotein complex
    • Di Simone, C., and M. J. Buchmeier. 1995. Kinetics and pH dependence of acid-induced structural changes in the lymphocytic choriomeningitis virus glycoprotein complex. Virology 209:3-9.
    • (1995) Virology , vol.209 , pp. 3-9
    • Di Simone, C.1    Buchmeier, M.J.2
  • 10
    • 0028241840 scopus 로고
    • Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike
    • Di Simone, C., M. A. Zandonatti, and M. J. Buchmeier. 1994. Acidic pH triggers LCMV membrane fusion activity and conformational change in the glycoprotein spike. Virology 198:455-465.
    • (1994) Virology , vol.198 , pp. 455-465
    • Di Simone, C.1    Zandonatti, M.A.2    Buchmeier, M.J.3
  • 12
    • 0346242739 scopus 로고    scopus 로고
    • Identification of Lassa virus glycoprotein signal peptide as a transacting maturation factor
    • Eichler, R., O. Lenz, T. Strecker, M. Eickmann, H. D. Klenk, and W. Garten. 2003. Identification of Lassa virus glycoprotein signal peptide as a transacting maturation factor. EMBO Rep. 4:1084-1088.
    • (2003) EMBO Rep. , vol.4 , pp. 1084-1088
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Eickmann, M.4    Klenk, H.D.5    Garten, W.6
  • 13
    • 1842478088 scopus 로고    scopus 로고
    • Lassa virus glycoprotein signal peptide displays a novel topology with an extended endoplasmic reticulum-luminal region
    • Eichler, R., O. Lenz, T. Strecker, M. Eickmann, H. D. Klenk, and W. Garten. 2004. Lassa virus glycoprotein signal peptide displays a novel topology with an extended endoplasmic reticulum-luminal region. J. Biol. Chem. 279:12293-12299.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12293-12299
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Eickmann, M.4    Klenk, H.D.5    Garten, W.6
  • 14
    • 0037434923 scopus 로고    scopus 로고
    • Signal peptide of Lassa virus glycoprotein GP-C exhibits an unusual length
    • Eichler, R., O. Lenz, T. Strecker, and W. Garten. 2003. Signal peptide of Lassa virus glycoprotein GP-C exhibits an unusual length. FEBS Lett. 538: 203-206.
    • (2003) FEBS Lett. , vol.538 , pp. 203-206
    • Eichler, R.1    Lenz, O.2    Strecker, T.3    Garten, W.4
  • 15
    • 1442299797 scopus 로고    scopus 로고
    • Characterization of the Lassa virus matrix protein Z: Electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP)
    • Eichler, R., T. Strecker, L. Kolesnikova, J. ter Meulen, W. Weissenhorn, S. Becker, H. D. Klenk, W. Garten, and O. Lenz. 2004. Characterization of the Lassa virus matrix protein Z: electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP). Virus Res. 100:249-255.
    • (2004) Virus Res. , vol.100 , pp. 249-255
    • Eichler, R.1    Strecker, T.2    Kolesnikova, L.3    Ter Meulen, J.4    Weissenhorn, W.5    Becker, S.6    Klenk, H.D.7    Garten, W.8    Lenz, O.9
  • 16
    • 0142242233 scopus 로고    scopus 로고
    • Long-lived signal peptide of lymphocytic choriomeningitis virus glycoprotein pGP-C
    • Froeschke, M., M. Basler, M. Groettrup, and B. Dobberstein. 2003. Long-lived signal peptide of lymphocytic choriomeningitis virus glycoprotein pGP-C. J. Biol. Chem. 278:41914-41920.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41914-41920
    • Froeschke, M.1    Basler, M.2    Groettrup, M.3    Dobberstein, B.4
  • 17
    • 0028047505 scopus 로고
    • Fine structure of influenza A virus observed by electron cryo-microscopy
    • Fujiyoshi, Y., N. P. Kume, K. Sakata, and S. B. Sato. 1994. Fine structure of influenza A virus observed by electron cryo-microscopy. EMBO J. 13:318-326.
    • (1994) EMBO J. , vol.13 , pp. 318-326
    • Fujiyoshi, Y.1    Kume, N.P.2    Sakata, K.3    Sato, S.B.4
  • 18
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • Fuller, S. D., T. Wilk, B. E. Gowen, H. G. Kraüsslich, and V. M. Vogt. 1997. Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr. Biol. 7:729-738.
    • (1997) Curr. Biol. , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Kraüsslich, H.G.4    Vogt, V.M.5
  • 19
    • 3142545672 scopus 로고    scopus 로고
    • The viral transmembrane superfamily: Possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor
    • Gallaher, W. R., C. DiSimone, and M. J. Buchmeier. 2001. The viral transmembrane superfamily: possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestor. BMC Microbiol. 1:1.
    • (2001) BMC Microbiol. , vol.1 , pp. 1
    • Gallaher, W.R.1    DiSimone, C.2    Buchmeier, M.J.3
  • 20
    • 0017721483 scopus 로고
    • Structural proteins of Tacaribe and Tamiami virions
    • Gard, G. P., A. C. Vezza, D. H. L. Bishop, and R. W. Compans. 1977. Structural proteins of Tacaribe and Tamiami virions. Virology 83:84-95.
    • (1977) Virology , vol.83 , pp. 84-95
    • Gard, G.P.1    Vezza, A.C.2    Bishop, D.H.L.3    Compans, R.W.4
  • 21
    • 0024314658 scopus 로고
    • Molecular architecture of Escherichia coli F1 adenosine triphosphatase
    • Gogol, E. P., U. Lucken, T. Bork, and R. A. Capaldi. 1989. Molecular architecture of Escherichia coli F1 adenosine triphosphatase. Biochemistry 28:4709-4716.
    • (1989) Biochemistry , vol.28 , pp. 4709-4716
    • Gogol, E.P.1    Lucken, U.2    Bork, T.3    Capaldi, R.A.4
  • 22
    • 0028372190 scopus 로고
    • Projection structures of human immunodeficiency virus type 1 (HIV-1) observed with high resolution electron cryo-microscopy
    • Tokyo
    • Goto, T., T. Ashina, Y. Fujiyoshi, N. Kume, H. Yamagishi, and M. Nakai. 1994. Projection structures of human immunodeficiency virus type 1 (HIV-1) observed with high resolution electron cryo-microscopy. J. Electron Microsc. (Tokyo) 43:16-19.
    • (1994) J. Electron Microsc. , vol.43 , pp. 16-19
    • Goto, T.1    Ashina, T.2    Fujiyoshi, Y.3    Kume, N.4    Yamagishi, H.5    Nakai, M.6
  • 23
    • 0028773889 scopus 로고
    • Volume changes on protein folding
    • Harpaz, Y., M. Gerstein, and C. Chothia. 1994. Volume changes on protein folding. Structure 2:641-649.
    • (1994) Structure , vol.2 , pp. 641-649
    • Harpaz, Y.1    Gerstein, M.2    Chothia, C.3
  • 24
    • 0023756448 scopus 로고
    • Cryoelectron microscopy of vitrified Sendai virions
    • Hosaka, Y., and T. Watabe. 1988. Cryoelectron microscopy of vitrified Sendai virions. J. Virol. Methods 22:347-349.
    • (1988) J. Virol. Methods , vol.22 , pp. 347-349
    • Hosaka, Y.1    Watabe, T.2
  • 25
    • 0021884896 scopus 로고
    • Properties and characterization of monoclonal antibodies to Tacaribe virus
    • Howard, C. R., H. Lewicki, L. Allison, M. Salter, and M. J. Buchmeier. 1985. Properties and characterization of monoclonal antibodies to Tacaribe virus. J. Gen. Virol. 66:1383-1395.
    • (1985) J. Gen. Virol. , vol.66 , pp. 1383-1395
    • Howard, C.R.1    Lewicki, H.2    Allison, L.3    Salter, M.4    Buchmeier, M.J.5
  • 26
    • 14744268458 scopus 로고
    • Structure and variation among arenaviruses
    • E. Kurstak (ed.), Academic Press, Orlando, Fla.
    • Howard, C. R., and P. R. Young. 1984. Structure and variation among arenaviruses, p. 327-341. In E. Kurstak (ed.), Applied virology. Academic Press, Orlando, Fla.
    • (1984) Applied Virology , pp. 327-341
    • Howard, C.R.1    Young, P.R.2
  • 27
    • 18144444991 scopus 로고    scopus 로고
    • Tacaribe virus Z protein interacts with the L polymerase protein to inhibit viral RNA synthesis
    • Jacamo, R., N. Lopez, M. Wilda, and M. T. Franze-Fernandez. 2003. Tacaribe virus Z protein interacts with the L polymerase protein to inhibit viral RNA synthesis. J. Virol. 77:10383-10393.
    • (2003) J. Virol. , vol.77 , pp. 10383-10393
    • Jacamo, R.1    Lopez, N.2    Wilda, M.3    Franze-Fernandez, M.T.4
  • 28
    • 0035782860 scopus 로고    scopus 로고
    • The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy
    • Kingston, R. L., N. H. Olson, and V. M. Vogt. 2001. The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy. J. Struct. Biol. 136:67-80.
    • (2001) J. Struct. Biol. , vol.136 , pp. 67-80
    • Kingston, R.L.1    Olson, N.H.2    Vogt, V.M.3
  • 30
    • 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 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0017713089 scopus 로고
    • Virion-associated ribosomes are not required for the replication of Pichinde virus
    • Leung, W. C., and W. E. Rawls. 1977. Virion-associated ribosomes are not required for the replication of Pichinde virus. Virology 81:174-176.
    • (1977) Virology , vol.81 , pp. 174-176
    • Leung, W.C.1    Rawls, W.E.2
  • 32
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., P. R. Baldwin, and W. Chiu. 1999. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 33
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano, J., A. Yarovoy, D. Perez-Caballero, and P. D. Bieniasz. 2003. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl. Acad. Sci. USA 100:12414-12419.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 34
    • 0021153153 scopus 로고
    • Molecular structure determination of crystalline specimens in frozen aqueous solutions
    • Milligan, R. A., A. Brisson, and P. N. T. Unwin. 1984. Molecular structure determination of crystalline specimens in frozen aqueous solutions. Ultramicroscopy 13:1-10.
    • (1984) Ultramicroscopy , vol.13 , pp. 1-10
    • Milligan, R.A.1    Brisson, A.2    Unwin, P.N.T.3
  • 36
    • 0027364812 scopus 로고
    • Further evidence of icosahedral symmetry in human and simian immunodeficiency virus
    • Nermut, M. V., C. Grief, S. Hashmi, and D. J. Hockley. 1993. Further evidence of icosahedral symmetry in human and simian immunodeficiency virus. AIDS Res. Hum. Retroviruses 9:929-938.
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 929-938
    • Nermut, M.V.1    Grief, C.2    Hashmi, S.3    Hockley, D.J.4
  • 37
    • 0242331609 scopus 로고    scopus 로고
    • The small RING finger protein Z drives arenavirus budding: Implications for antiviral strategies
    • Perez, M., R. C. Craven, and J. C. de la Torre. 2003. The small RING finger protein Z drives arenavirus budding: implications for antiviral strategies. Proc. Natl. Acad. Sci. USA 100:12978-12983.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12978-12983
    • Perez, M.1    Craven, R.C.2    De La Torre, J.C.3
  • 38
    • 4644243004 scopus 로고    scopus 로고
    • Myristoylation of the RING finger Z protein is essential for arenavirus budding
    • Perez, M., D. L. Greenwald, and J. C. de la Torre. 2004. Myristoylation of the RING finger Z protein is essential for arenavirus budding. J. Virol. 78: 11443-11448.
    • (2004) J. Virol. , vol.78 , pp. 11443-11448
    • Perez, M.1    Greenwald, D.L.2    De La Torre, J.C.3
  • 39
    • 0029979024 scopus 로고    scopus 로고
    • The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins
    • Risco, C., I. M. Antón, L. Enjuanes, and J. L. Carrascosa. 1996. The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins. J. Virol. 70:4773-4777.
    • (1996) J. Virol. , vol.70 , pp. 4773-4777
    • Risco, C.1    Antón, I.M.2    Enjuanes, L.3    Carrascosa, J.L.4
  • 40
    • 0026538145 scopus 로고
    • Biochemical and immunological evidence that the 11 kDa zinc-binding protein of lymphocytic choriomeningitis virus is a structural component of the virus
    • Salvato, M. S., K. J. Schweighofer, J. Burns, and E. M. Shimomaye. 1992. Biochemical and immunological evidence that the 11 kDa zinc-binding protein of lymphocytic choriomeningitis virus is a structural component of the virus. Virus Res. 22:185-198.
    • (1992) Virus Res. , vol.22 , pp. 185-198
    • Salvato, M.S.1    Schweighofer, K.J.2    Burns, J.3    Shimomaye, E.M.4
  • 41
  • 42
    • 0032167614 scopus 로고    scopus 로고
    • Clathrin coats at 21 a resolution: A cellular assembly designed to recycle multiple membrane receptors
    • Smith, C. J., N. Grigorieff, and B. M. F. Pearse. 1998. Clathrin coats at 21 A resolution: a cellular assembly designed to recycle multiple membrane receptors. EMBO J. 17:4943-4953.
    • (1998) EMBO J. , vol.17 , pp. 4943-4953
    • Smith, C.J.1    Grigorieff, N.2    Pearse, B.M.F.3
  • 43
    • 0141856160 scopus 로고    scopus 로고
    • Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles
    • Erratum, 77:12927
    • Strecker, T., R. Eichler, J. ter Meulen, W. Weissenhorn, H. Dieter Klenk, W. Garten, and O. Lenz. 2003. Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles. J. Virol. 77:10700-10705. (Erratum, 77:12927.)
    • (2003) J. Virol. , vol.77 , pp. 10700-10705
    • Strecker, T.1    Eichler, R.2    Ter Meulen, J.3    Weissenhorn, W.4    Dieter Klenk, H.5    Garten, W.6    Lenz, O.7
  • 45
    • 0025880220 scopus 로고
    • Structural variation of la Crosse virions under different chemical and physical conditions
    • Wang, G. J., M. Hewlett, and W. Chiu. 1991. Structural variation of La Crosse virions under different chemical and physical conditions. Virology 184:455-459.
    • (1991) Virology , vol.184 , pp. 455-459
    • Wang, G.J.1    Hewlett, M.2    Chiu, W.3
  • 46
    • 0034864546 scopus 로고    scopus 로고
    • Specific interaction of a novel foamy virus Env leader protein with the N-terminal Gag domain
    • Wilk, T., V. Geiselhart, M. Frech, S. D. Fuller, R. M. Flügel, and M. Lochelt. 2001. Specific interaction of a novel foamy virus Env leader protein with the N-terminal Gag domain. J. Virol. 75:7995-8007.
    • (2001) J. Virol. , vol.75 , pp. 7995-8007
    • Wilk, T.1    Geiselhart, V.2    Frech, M.3    Fuller, S.D.4    Flügel, R.M.5    Lochelt, M.6
  • 48
    • 0032560502 scopus 로고    scopus 로고
    • Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: Implications for retroviral assembly mechanisms
    • Yeager, M., E. M. Wilson-Kubalek, S. G. Weiner, P. O. Brown, and A. Rein. 1998. Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms. Proc. Natl. Acad. Sci. USA 95:7299-7304.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7299-7304
    • Yeager, M.1    Wilson-Kubalek, E.M.2    Weiner, S.G.3    Brown, P.O.4    Rein, A.5
  • 49
    • 77956899724 scopus 로고
    • Arenaviridae
    • M. V. Nermut and A. C. Steven (ed.), Elsevier, New York, N.Y.
    • Young, P. R. 1987. Arenaviridae, p. 185-198. In M. V. Nermut and A. C. Steven (ed.), Animal virus structure. Elsevier, New York, N.Y.
    • (1987) Animal Virus Structure , pp. 185-198
    • Young, P.R.1
  • 50
    • 0020698274 scopus 로고
    • Fine structure analysis of Pichinde virus nucleocapsids
    • Young, P. R., and C. R. Howard. 1983. Fine structure analysis of Pichinde virus nucleocapsids. J. Gen. Virol. 64:833-842.
    • (1983) J. Gen. Virol. , vol.64 , pp. 833-842
    • Young, P.R.1    Howard, C.R.2
  • 51
    • 0035123571 scopus 로고    scopus 로고
    • Characterization of Rous sarcoma virus Gag particles assembled in vitro
    • Yu, F., S. M. Joshi, Y. M. Ma, R. L. Kingston, M. N. Simon, and V. M. Vogt. 2001. Characterization of Rous sarcoma virus Gag particles assembled in vitro. J. Virol. 75:2753-2764.
    • (2001) J. Virol. , vol.75 , pp. 2753-2764
    • Yu, F.1    Joshi, S.M.2    Ma, Y.M.3    Kingston, R.L.4    Simon, M.N.5    Vogt, V.M.6


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