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Volumn 137, Issue 1, 2008, Pages 112-121

Structural and functional analysis of virus factories purified from Rabbit vesivirus-infected Vero cells

Author keywords

Caliciviridae; Rabbit vesivirus; Replication complex; Virus factories

Indexed keywords

CALNEXIN; MICROCOCCAL NUCLEASE; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 2AB; NONSTRUCTURAL PROTEIN 2C; NONSTRUCTURAL PROTEIN 3A; NONSTRUCTURAL PROTEIN 3B; NONSTRUCTURAL PROTEIN 3CD; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 50049083226     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2008.06.009     Document Type: Article
Times cited : (4)

References (47)
  • 2
    • 41649089011 scopus 로고    scopus 로고
    • Nucleotidylylation of the VPg protein of a human norovirus by its proteinase-polymerase precursor protein
    • Belliot G., Sosnovtsev S.V., Chang K.O., McPhie P., and Green K.Y. Nucleotidylylation of the VPg protein of a human norovirus by its proteinase-polymerase precursor protein. Virology 374 (2008) 33-49
    • (2008) Virology , vol.374 , pp. 33-49
    • Belliot, G.1    Sosnovtsev, S.V.2    Chang, K.O.3    McPhie, P.4    Green, K.Y.5
  • 3
    • 0026519212 scopus 로고
    • Structural and functional characterization of the poliovirus replication complex
    • Bienz K., Egger D., Pfister T., and Troxler M. Structural and functional characterization of the poliovirus replication complex. J. Virol. 66 (1992) 2740-2747
    • (1992) J. Virol. , vol.66 , pp. 2740-2747
    • Bienz, K.1    Egger, D.2    Pfister, T.3    Troxler, M.4
  • 4
    • 0037047595 scopus 로고    scopus 로고
    • Chemical synthesis of poliovirus cDNA: generation of infectious virus in the absence of natural template
    • Cello J., Paul A.V., and Wimmer E. Chemical synthesis of poliovirus cDNA: generation of infectious virus in the absence of natural template. Science 297 (2002) 1016-1018
    • (2002) Science , vol.297 , pp. 1016-1018
    • Cello, J.1    Paul, A.V.2    Wimmer, E.3
  • 5
    • 13744258250 scopus 로고    scopus 로고
    • Reverse genetics system for porcine enteric calicivirus, a prototype sapovirus in the Caliciviridae
    • Chang K.O., Sosnovtsev S.S., Belliot G., Wang Q., Saif L.J., and Green K.Y. Reverse genetics system for porcine enteric calicivirus, a prototype sapovirus in the Caliciviridae. J. Virol. 79 (2005) 1409-1416
    • (2005) J. Virol. , vol.79 , pp. 1409-1416
    • Chang, K.O.1    Sosnovtsev, S.S.2    Belliot, G.3    Wang, Q.4    Saif, L.J.5    Green, K.Y.6
  • 6
    • 34547557616 scopus 로고    scopus 로고
    • Recovery of genetically defined murine norovirus in tissue culture by using a fowlpox virus expressing T7 RNA polymerase
    • Chaudhry Y., Skinner M.A., and Goodfellow I.G. Recovery of genetically defined murine norovirus in tissue culture by using a fowlpox virus expressing T7 RNA polymerase. J. Gen. Virol. 88 (2007) 2091-2100
    • (2007) J. Gen. Virol. , vol.88 , pp. 2091-2100
    • Chaudhry, Y.1    Skinner, M.A.2    Goodfellow, I.G.3
  • 7
    • 0031017971 scopus 로고    scopus 로고
    • The molecular biology of caliciviruses
    • Clarke I.N., and Lambden P.R. The molecular biology of caliciviruses. J. Gen. Virol. 78 Pt 2 (1997) 291-301
    • (1997) J. Gen. Virol. , vol.78 , Issue.PART 2 , pp. 291-301
    • Clarke, I.N.1    Lambden, P.R.2
  • 8
    • 0033919961 scopus 로고    scopus 로고
    • Formation of the poliovirus replication complex requires coupled viral translation, vesicle production, and viral RNA synthesis
    • Egger D., Teterina N., Ehrenfeld E., and Bienz K. Formation of the poliovirus replication complex requires coupled viral translation, vesicle production, and viral RNA synthesis. J. Virol. 74 (2000) 6570-6580
    • (2000) J. Virol. , vol.74 , pp. 6570-6580
    • Egger, D.1    Teterina, N.2    Ehrenfeld, E.3    Bienz, K.4
  • 9
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • Egger D., Wolk B., Gosert R., Bianchi L., Blum H.E., Moradpour D., and Bienz K. Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J. Virol. 76 (2002) 5974-5984
    • (2002) J. Virol. , vol.76 , pp. 5974-5984
    • Egger, D.1    Wolk, B.2    Gosert, R.3    Bianchi, L.4    Blum, H.E.5    Moradpour, D.6    Bienz, K.7
  • 10
    • 0141507081 scopus 로고    scopus 로고
    • Replication of hepatitis C virus RNA occurs in a membrane-bound replication complex containing nonstructural viral protins and RNA
    • El-Hage N., and Luo G. Replication of hepatitis C virus RNA occurs in a membrane-bound replication complex containing nonstructural viral protins and RNA. J. Gen. Virol. 84 (2003) 2761-2769
    • (2003) J. Gen. Virol. , vol.84 , pp. 2761-2769
    • El-Hage, N.1    Luo, G.2
  • 11
    • 0142092456 scopus 로고    scopus 로고
    • Membrane requirements for uridylylation of the poliovirus VPg protein and viral RNA synthesis in vitro
    • Fogg M.H., Teterina N.L., and Ehrenfeld E. Membrane requirements for uridylylation of the poliovirus VPg protein and viral RNA synthesis in vitro. J. Virol. 77 (2003) 11408-11416
    • (2003) J. Virol. , vol.77 , pp. 11408-11416
    • Fogg, M.H.1    Teterina, N.L.2    Ehrenfeld, E.3
  • 12
    • 18144402819 scopus 로고    scopus 로고
    • Stimulation of poliovirus synthesis in a HeLa cell-free in vitro translation-RNA replication system by viral protein 3CD(pro)
    • Franco D., Pathak H.B., Cameron C.E., Rombaut B., Wimmer E., and Paul A.V. Stimulation of poliovirus synthesis in a HeLa cell-free in vitro translation-RNA replication system by viral protein 3CD(pro). J. Virol. 79 (2005) 6358-6367
    • (2005) J. Virol. , vol.79 , pp. 6358-6367
    • Franco, D.1    Pathak, H.B.2    Cameron, C.E.3    Rombaut, B.4    Wimmer, E.5    Paul, A.V.6
  • 13
    • 0024237292 scopus 로고
    • Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes
    • Froshauer S., Kartenbeck J., and Helenius A. Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes. J. Cell Biol. 107 (1988) 2075-2086
    • (1988) J. Cell Biol. , vol.107 , pp. 2075-2086
    • Froshauer, S.1    Kartenbeck, J.2    Helenius, A.3
  • 15
    • 0345144016 scopus 로고    scopus 로고
    • Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons
    • Gosert R., Egger D., Lohmann V., Bartenschlager R., Blum H.E., Bienz K., and Moradpour D. Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons. J. Virol. 77 (2003) 5487-5492
    • (2003) J. Virol. , vol.77 , pp. 5487-5492
    • Gosert, R.1    Egger, D.2    Lohmann, V.3    Bartenschlager, R.4    Blum, H.E.5    Bienz, K.6    Moradpour, D.7
  • 16
    • 0036196634 scopus 로고    scopus 로고
    • RNA replication of mouse hepatitis virus takes place at double-membrane vesicles
    • Gosert R., Kanjanahaluethai A., Egger D., Bienz K., and Baker S.C. RNA replication of mouse hepatitis virus takes place at double-membrane vesicles. J. Virol. 76 (2002) 3697-3708
    • (2002) J. Virol. , vol.76 , pp. 3697-3708
    • Gosert, R.1    Kanjanahaluethai, A.2    Egger, D.3    Bienz, K.4    Baker, S.C.5
  • 17
    • 34548415971 scopus 로고    scopus 로고
    • Caliciviridae: The Noroviruses
    • Knipe D.M., and Howley P.M. (Eds), Lippincott Williams & Wilkins, Philadelphia
    • Green K.Y. Caliciviridae: The Noroviruses. In: Knipe D.M., and Howley P.M. (Eds). Field's Virology (2007), Lippincott Williams & Wilkins, Philadelphia 949-979
    • (2007) Field's Virology , pp. 949-979
    • Green, K.Y.1
  • 19
    • 0030052692 scopus 로고    scopus 로고
    • Detection of the ORF3 polypeptide of feline calicivirus in infected cells and evidence for its expression from a single, functionally bicistronic, subgenomic mRNA
    • Herbert T.P., Brierley I., and Brown T.D. Detection of the ORF3 polypeptide of feline calicivirus in infected cells and evidence for its expression from a single, functionally bicistronic, subgenomic mRNA. J. Gen. Virol. 77 Pt 1 (1996) 123-127
    • (1996) J. Gen. Virol. , vol.77 , Issue.PART 1 , pp. 123-127
    • Herbert, T.P.1    Brierley, I.2    Brown, T.D.3
  • 20
    • 0031579246 scopus 로고    scopus 로고
    • Hepatitis C virus NS5B protein is a membrane-associated phosphoprotein with a predominantly perinuclear localization
    • Hwang S.B., Park K.J., Kim Y.S., Sung Y.C., and Lai M.M. Hepatitis C virus NS5B protein is a membrane-associated phosphoprotein with a predominantly perinuclear localization. Virology 227 (1997) 439-446
    • (1997) Virology , vol.227 , pp. 439-446
    • Hwang, S.B.1    Park, K.J.2    Kim, Y.S.3    Sung, Y.C.4    Lai, M.M.5
  • 21
    • 31644445841 scopus 로고    scopus 로고
    • Analysis of protein-protein interactions in the feline calicivirus replication complex
    • Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., and Goodfellow I.G. Analysis of protein-protein interactions in the feline calicivirus replication complex. J. Gen. Virol. 87 (2006) 363-368
    • (2006) J. Gen. Virol. , vol.87 , pp. 363-368
    • Kaiser, W.J.1    Chaudhry, Y.2    Sosnovtsev, S.V.3    Goodfellow, I.G.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0040353989 scopus 로고    scopus 로고
    • Expression of enzymatically active rabbit hemorrhagic disease virus RNA-dependent RNA polymerase in Escherichia coli
    • López Vázquez A., Martin Alonso J.M., Casais R., Boga J.A., and Parra F. Expression of enzymatically active rabbit hemorrhagic disease virus RNA-dependent RNA polymerase in Escherichia coli. J. Virol. 72 (1998) 2999-3004
    • (1998) J. Virol. , vol.72 , pp. 2999-3004
    • López Vázquez, A.1    Martin Alonso, J.M.2    Casais, R.3    Boga, J.A.4    Parra, F.5
  • 24
    • 0035958885 scopus 로고    scopus 로고
    • Identification of the amino acid residue involved in rabbit hemorrhagic disease virus VPg uridylylation
    • Machín A., Martin Alonso J.M., and Parra F. Identification of the amino acid residue involved in rabbit hemorrhagic disease virus VPg uridylylation. J. Biol. Chem. 276 (2001) 27787-27792
    • (2001) J. Biol. Chem. , vol.276 , pp. 27787-27792
    • Machín, A.1    Martin Alonso, J.M.2    Parra, F.3
  • 25
    • 0033761980 scopus 로고    scopus 로고
    • ATP binding and ATPase activities associated with recombinant rabbit hemorrhagic disease virus 2C-like polypeptide
    • Marin M.S., Casais R., Alonso J.M., and Parra F. ATP binding and ATPase activities associated with recombinant rabbit hemorrhagic disease virus 2C-like polypeptide. J. Virol. 74 (2000) 10846-10851
    • (2000) J. Virol. , vol.74 , pp. 10846-10851
    • Marin, M.S.1    Casais, R.2    Alonso, J.M.3    Parra, F.4
  • 27
    • 0026010247 scopus 로고
    • Genomic and subgenomic RNAs of rabbit hemorrhagic disease virus are both protein-linked and packaged into particles
    • Meyers G., Wirblich C., and Thiel H.J. Genomic and subgenomic RNAs of rabbit hemorrhagic disease virus are both protein-linked and packaged into particles. Virology 184 (1991) 677-686
    • (1991) Virology , vol.184 , pp. 677-686
    • Meyers, G.1    Wirblich, C.2    Thiel, H.J.3
  • 28
    • 0026325508 scopus 로고
    • Cell-free, de novo synthesis of poliovirus
    • Molla A., Paul A.V., and Wimmer E. Cell-free, de novo synthesis of poliovirus. Science 254 (1991) 1647-1651
    • (1991) Science , vol.254 , pp. 1647-1651
    • Molla, A.1    Paul, A.V.2    Wimmer, E.3
  • 29
    • 2342435180 scopus 로고    scopus 로고
    • Synthesis in vitro of rabbit hemorrhagic disease virus subgenomic RNA by internal initiation on (-)sense genomic RNA: mapping of a subgenomic promoter
    • Morales M., Barcena J., Ramirez M.A., Boga J.A., Parra F., and Torres J.M. Synthesis in vitro of rabbit hemorrhagic disease virus subgenomic RNA by internal initiation on (-)sense genomic RNA: mapping of a subgenomic promoter. J. Biol. Chem. 279 (2004) 17013-17018
    • (2004) J. Biol. Chem. , vol.279 , pp. 17013-17018
    • Morales, M.1    Barcena, J.2    Ramirez, M.A.3    Boga, J.A.4    Parra, F.5    Torres, J.M.6
  • 30
    • 0036065127 scopus 로고    scopus 로고
    • The subgenomic RNA of feline calicivirus is packaged into viral particles during infection
    • Neill J.D. The subgenomic RNA of feline calicivirus is packaged into viral particles during infection. Virus Res. 87 (2002) 89-93
    • (2002) Virus Res. , vol.87 , pp. 89-93
    • Neill, J.D.1
  • 31
    • 0033457373 scopus 로고    scopus 로고
    • Movement and localization of RNA in the cell nucleus
    • Pederson T. Movement and localization of RNA in the cell nucleus. FASEB J. 13 Suppl. 2 (1999) S238-S242
    • (1999) FASEB J. , vol.13 , Issue.SUPPL. 2
    • Pederson, T.1
  • 32
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • Prentice E., Jerome W.G., Yoshimori T., Mizushima N., and Denison M.R. Coronavirus replication complex formation utilizes components of cellular autophagy. J. Biol. Chem. 279 (2004) 10136-10141
    • (2004) J. Biol. Chem. , vol.279 , pp. 10136-10141
    • Prentice, E.1    Jerome, W.G.2    Yoshimori, T.3    Mizushima, N.4    Denison, M.R.5
  • 33
    • 0033992516 scopus 로고    scopus 로고
    • Overview of hepatitis C virus genome structure, polyprotein processing, and protein properties
    • Reed K.E., and Rice C.M. Overview of hepatitis C virus genome structure, polyprotein processing, and protein properties. Curr. Top. Microbiol. Immunol. 242 (2000) 55-84
    • (2000) Curr. Top. Microbiol. Immunol. , vol.242 , pp. 55-84
    • Reed, K.E.1    Rice, C.M.2
  • 34
    • 0030915143 scopus 로고    scopus 로고
    • Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein
    • Schaad M.C., Jensen P.E., and Carrington J.C. Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein. EMBO J. 16 (1997) 4049-4059
    • (1997) EMBO J. , vol.16 , pp. 4049-4059
    • Schaad, M.C.1    Jensen, P.E.2    Carrington, J.C.3
  • 35
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel A., Giddings Jr. T.H., Ladinsky M.S., and Kirkegaard K. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J. Virol. 70 (1996) 6576-6588
    • (1996) J. Virol. , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings Jr., T.H.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 36
    • 0036204740 scopus 로고    scopus 로고
    • A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids
    • Schwartz M., Chen J., Janda M., Sullivan M., den B.J., and Ahlquist P. A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids. Mol. Cell 9 (2002) 505-514
    • (2002) Mol. Cell , vol.9 , pp. 505-514
    • Schwartz, M.1    Chen, J.2    Janda, M.3    Sullivan, M.4    den, B.J.5    Ahlquist, P.6
  • 37
    • 0037379425 scopus 로고    scopus 로고
    • Hepatitis C virus RNA replication occurs on a detergent-resistant membrane that cofractionates with caveolin-2
    • Shi S.T., Lee K.J., Aizaki H., Hwang S.B., and Lai M.M. Hepatitis C virus RNA replication occurs on a detergent-resistant membrane that cofractionates with caveolin-2. J. Virol. 77 (2003) 4160-4168
    • (2003) J. Virol. , vol.77 , pp. 4160-4168
    • Shi, S.T.1    Lee, K.J.2    Aizaki, H.3    Hwang, S.B.4    Lai, M.M.5
  • 38
    • 0029134714 scopus 로고
    • RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity
    • Sosnovtsev S., and Green K.Y. RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity. Virology 210 (1995) 383-390
    • (1995) Virology , vol.210 , pp. 383-390
    • Sosnovtsev, S.1    Green, K.Y.2
  • 39
    • 0034634331 scopus 로고    scopus 로고
    • Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions
    • Sosnovtsev S.V., and Green K.Y. Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions. Virology 277 (2000) 193-203
    • (2000) Virology , vol.277 , pp. 193-203
    • Sosnovtsev, S.V.1    Green, K.Y.2
  • 40
    • 0032798396 scopus 로고    scopus 로고
    • Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein
    • Sosnovtseva S.A., Sosnovtsev S.V., and Green K.Y. Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein. J. Virol. 73 (1999) 6626-6633
    • (1999) J. Virol. , vol.73 , pp. 6626-6633
    • Sosnovtseva, S.A.1    Sosnovtsev, S.V.2    Green, K.Y.3
  • 41
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles
    • Suhy D.A., Giddings Jr. T.H., and Kirkegaard K. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J. Virol. 74 (2000) 8953-8965
    • (2000) J. Virol. , vol.74 , pp. 8953-8965
    • Suhy, D.A.1    Giddings Jr., T.H.2    Kirkegaard, K.3
  • 42
    • 0020521818 scopus 로고
    • Membrane fractions active in poliovirus RNA replication contain VPg precursor polypeptides
    • Takegami T., Semler B.L., Anderson C.W., and Wimmer E. Membrane fractions active in poliovirus RNA replication contain VPg precursor polypeptides. Virology 128 (1983) 33-47
    • (1983) Virology , vol.128 , pp. 33-47
    • Takegami, T.1    Semler, B.L.2    Anderson, C.W.3    Wimmer, E.4
  • 43
    • 0035157382 scopus 로고    scopus 로고
    • Proteinase-polymerase precursor as the active form of feline calicivirus RNA-dependent RNA polymerase
    • Wei L., Huhn J.S., Mory A., Pathak H.B., Sosnovtsev S.V., Green K.Y., and Cameron C.E. Proteinase-polymerase precursor as the active form of feline calicivirus RNA-dependent RNA polymerase. J. Virol. 75 (2001) 1211-1219
    • (2001) J. Virol. , vol.75 , pp. 1211-1219
    • Wei, L.1    Huhn, J.S.2    Mory, A.3    Pathak, H.B.4    Sosnovtsev, S.V.5    Green, K.Y.6    Cameron, C.E.7
  • 44
    • 0033602697 scopus 로고    scopus 로고
    • Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes
    • Westaway E.G., Khromykh A.A., and Mackenzie J.M. Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes. Virology 258 (1999) 108-117
    • (1999) Virology , vol.258 , pp. 108-117
    • Westaway, E.G.1    Khromykh, A.A.2    Mackenzie, J.M.3
  • 45
    • 0030846512 scopus 로고    scopus 로고
    • Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures
    • Westaway E.G., Mackenzie J.M., Kenney M.T., Jones M.K., and Khromykh A.A. Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures. J. Virol. 71 (1997) 6650-6661
    • (1997) J. Virol. , vol.71 , pp. 6650-6661
    • Westaway, E.G.1    Mackenzie, J.M.2    Kenney, M.T.3    Jones, M.K.4    Khromykh, A.A.5
  • 46
    • 0028840662 scopus 로고
    • 3C-like protease of rabbit hemorrhagic-disease virus-identification of cleavage sites in the Orf1 polyprotein and analysis of cleavage specificity
    • Wirblich C., Sibilia M., Boniotti M.B., Rossi C., Thiel H.J., and Meyers G. 3C-like protease of rabbit hemorrhagic-disease virus-identification of cleavage sites in the Orf1 polyprotein and analysis of cleavage specificity. J. Virol. 69 (1995) 7159-7168
    • (1995) J. Virol. , vol.69 , pp. 7159-7168
    • Wirblich, C.1    Sibilia, M.2    Boniotti, M.B.3    Rossi, C.4    Thiel, H.J.5    Meyers, G.6
  • 47
    • 0029798532 scopus 로고    scopus 로고
    • Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies
    • Wirblich C., Thiel H.J., and Meyers G. Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies. J. Virol. 70 (1996) 7974-7983
    • (1996) J. Virol. , vol.70 , pp. 7974-7983
    • Wirblich, C.1    Thiel, H.J.2    Meyers, G.3


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