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Volumn 74, Issue 9, 2000, Pages 4302-4309

Nucleic acid-dependent cross-linking of the nucleocapsid protein of Sindbis virus

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEIC ACID; NUCLEOCAPSID PROTEIN;

EID: 0033995285     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.9.4302-4309.2000     Document Type: Article
Times cited : (39)

References (30)
  • 4
    • 0026419333 scopus 로고
    • Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion
    • Choi, H.-K., L. Tong, W. Minor, P. Dumas, U. Boege, M. G. Rossmann, and G. Wengler. 1991. Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. Nature 354:37-43.
    • (1991) Nature , vol.354 , pp. 37-43
    • Choi, H.-K.1    Tong, L.2    Minor, W.3    Dumas, P.4    Boege, U.5    Rossmann, M.G.6    Wengler, G.7
  • 5
    • 0026419333 scopus 로고
    • Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion
    • Choi, H. K., L. Tong, W. Minor, P. Dumas, U. Boege, M. G. Rossmann, and G. Wengler. 1991. Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. Nature (London) 354:37-43.
    • (1991) Nature (London) , vol.354 , pp. 37-43
    • Choi, H.K.1    Tong, L.2    Minor, W.3    Dumas, P.4    Boege, U.5    Rossmann, M.G.6    Wengler, G.7
  • 6
    • 0023197762 scopus 로고
    • Organization of the Sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents
    • Coombs, K., and D. T. Brown. 1987. Organization of the Sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents. J. Mol. Biol. 195:359-371.
    • (1987) J. Mol. Biol. , vol.195 , pp. 359-371
    • Coombs, K.1    Brown, D.T.2
  • 7
    • 0023324281 scopus 로고
    • Topological organization of Sindbis virus capsid protein in isolated nucleocapsids
    • Coombs, K., and D. T. Brown. 1987. Topological organization of Sindbis virus capsid protein in isolated nucleocapsids. Virus Res. 7:131-149.
    • (1987) Virus Res. , vol.7 , pp. 131-149
    • Coombs, K.1    Brown, D.T.2
  • 8
    • 0024535279 scopus 로고
    • Form-determining functions in Sindbis virus nucleocapsids: Nucleosomelike organization of the nucleocapsid
    • Coombs, K. M., and D. T. Brown. 1989. Form-determining functions in Sindbis virus nucleocapsids: nucleosomelike organization of the nucleocapsid. J. Virol. 63:883-891.
    • (1989) J. Virol. , vol.63 , pp. 883-891
    • Coombs, K.M.1    Brown, D.T.2
  • 9
    • 0029823070 scopus 로고    scopus 로고
    • Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding
    • Forsell, K., G. Griffiths, and H. Garoff. 1996. Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding. EMBO J. 15:6495-6505.
    • (1996) EMBO J. , vol.15 , pp. 6495-6505
    • Forsell, K.1    Griffiths, G.2    Garoff, H.3
  • 10
    • 0028983047 scopus 로고
    • Structure-function relation of the NH2-terminal domain of the Semliki Forest virus capsid protein
    • Forsell, K., M. Suomalainen, and H. Garoff. 1995. Structure-function relation of the NH2-terminal domain of the Semliki Forest virus capsid protein. J. Virol. 69:1556-1563.
    • (1995) J. Virol. , vol.69 , pp. 1556-1563
    • Forsell, K.1    Suomalainen, M.2    Garoff, H.3
  • 11
    • 0029052283 scopus 로고
    • Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex
    • Fuller, S. D., J. A. Berriman, S. J. Butcher, and B. E. Gowen. 1995. Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex. Cell 81:715-725.
    • (1995) Cell , vol.81 , pp. 715-725
    • Fuller, S.D.1    Berriman, J.A.2    Butcher, S.J.3    Gowen, B.E.4
  • 12
    • 0017077952 scopus 로고
    • Biological activity of in vitro synthesized protein: Binding of Semliki Forest virus capsid protein to the large ribosomal subunit
    • Glanville, N., and J. Ulmanen. 1976. Biological activity of in vitro synthesized protein: binding of Semliki Forest virus capsid protein to the large ribosomal subunit. Biochem. Biophys. Res. Commun. 71:393-399.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 393-399
    • Glanville, N.1    Ulmanen, J.2
  • 14
    • 0023707298 scopus 로고
    • In vitro assembly of the outer shell of bacteriophage ø6 nucleocapsid
    • Ktistakis, N. T., C.-Y. Kao, and D. Lang. 1988. In vitro assembly of the outer shell of bacteriophage ø6 nucleocapsid. Virology 166:91-102.
    • (1988) Virology , vol.166 , pp. 91-102
    • Ktistakis, N.T.1    Kao, C.-Y.2    Lang, D.3
  • 15
    • 0027989589 scopus 로고
    • Mutations in an exposed domain of Sindbis virus capsid protein result in the production of noninfectious virions and morphological variants
    • Lee, H., and D. T. Brown. 1994. Mutations in an exposed domain of Sindbis virus capsid protein result in the production of noninfectious virions and morphological variants. Virology 202:390-400.
    • (1994) Virology , vol.202 , pp. 390-400
    • Lee, H.1    Brown, D.T.2
  • 16
    • 0030585119 scopus 로고    scopus 로고
    • Identification of a protein binding site on the surface of the alphavirus nucleocapsid protein and its implication in virus assembly
    • Lee, S., K. E. Owen, H. K. Choi, H. Lee, G. Lu, G. Wengler, D. T. Brown, M. G. Rossmann, and R. J. Kuhn. 1996. Identification of a protein binding site on the surface of the alphavirus nucleocapsid protein and its implication in virus assembly. Structure 4:531-541.
    • (1996) Structure , vol.4 , pp. 531-541
    • Lee, S.1    Owen, K.E.2    Choi, H.K.3    Lee, H.4    Lu, G.5    Wengler, G.6    Brown, D.T.7    Rossmann, M.G.8    Kuhn, R.J.9
  • 17
    • 0026684254 scopus 로고
    • Topological analysis of the hepatitis B virus core particle by cysteine-cysteine cross-linking
    • Nassal, M., A. Rieger, and O. Steinau. 1992. Topological analysis of the hepatitis B virus core particle by cysteine-cysteine cross-linking. J. Mol. Biol. 225:1013-1025.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1013-1025
    • Nassal, M.1    Rieger, A.2    Steinau, O.3
  • 18
    • 0029876709 scopus 로고    scopus 로고
    • Identification of a region in the Sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation
    • Owen, K. E., and R. J. Kuhn. 1996. Identification of a region in the Sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation. J. Virol. 70:2757-2763.
    • (1996) J. Virol. , vol.70 , pp. 2757-2763
    • Owen, K.E.1    Kuhn, R.J.2
  • 20
    • 0015752210 scopus 로고
    • Kinetics of formation of Semliki forest virus nucleocapsid
    • Söderlund, H. 1973. Kinetics of formation of Semliki Forest virus nucleocapsid. Intervirology 1:354-361.
    • (1973) Intervirology , vol.1 , pp. 354-361
    • Söderlund, H.1
  • 21
    • 0017661273 scopus 로고
    • Transient association of Semliki Forest virus capsid protein with ribosomes
    • Söderlund, H., and I. Ulmanen. 1977. Transient association of Semliki Forest virus capsid protein with ribosomes. J. Virol. 24:907-909.
    • (1977) J. Virol. , vol.24 , pp. 907-909
    • Söderlund, H.1    Ulmanen, I.2
  • 22
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • Strauss, J. H., and E. G. Strauss. 1994. The alphaviruses: gene expression, replication, and evolution. Microbiol. Rev. 58:491-562.
    • (1994) Microbiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 23
    • 0025351310 scopus 로고
    • Proteolytic dissection of Sindbis virus core protein
    • Strong, R. K., and S. C. Harrison. 1990. Proteolytic dissection of Sindbis virus core protein. J. Virol. 64:3992-3994.
    • (1990) J. Virol. , vol.64 , pp. 3992-3994
    • Strong, R.K.1    Harrison, S.C.2
  • 24
    • 0033028591 scopus 로고    scopus 로고
    • In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia coli
    • Tellinghuisen, T. L., A. E. Hamburger, B. R. Fisher, R. Ostendorp, and R. J. Kuhn. 1999. In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia coli. J. Virol. 73:5309-5319.
    • (1999) J. Virol. , vol.73 , pp. 5309-5319
    • Tellinghuisen, T.L.1    Hamburger, A.E.2    Fisher, B.R.3    Ostendorp, R.4    Kuhn, R.J.5
  • 25
    • 0028359402 scopus 로고
    • Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site
    • Weiss, B., U. Geigenmüller-Gnirke, and S. Schlesinger. 1994. Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site. Nucleic Acids Res. 22:780-786.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 780-786
    • Weiss, B.1    Geigenmüller-Gnirke, U.2    Schlesinger, S.3
  • 26
    • 0023118357 scopus 로고
    • The mode of assembly of alphavirus cores implies a mechanism for the disassembly of the cores in the early stages of infection
    • Wengler, G. 1987. The mode of assembly of alphavirus cores implies a mechanism for the disassembly of the cores in the early stages of infection. Arch. Virol. 94:1-14.
    • (1987) Arch. Virol. , vol.94 , pp. 1-14
    • Wengler, G.1
  • 27
    • 0020053676 scopus 로고
    • The core protein of the alphavirus sindbis virus assembles into core-like nucleoproteins with the viral genome RNA and with other single-stranded nucleic acids in vitro
    • Wengler, G., U. Boege, G. Wengler, H. Bischoff, and K. Wahn. 1982. The core protein of the alphavirus Sindbis virus assembles into core-like nucleoproteins with the viral genome RNA and with other single-stranded nucleic acids in vitro. Virology 118:401-410.
    • (1982) Virology , vol.118 , pp. 401-410
    • Wengler, G.1    Boege, U.2    Wengler, G.3    Bischoff, H.4    Wahn, K.5
  • 28
    • 0021357579 scopus 로고
    • Establishment and analysis of a system which allows assembly and disassembly of alphavirus core-like particles under physiological condition in vitro
    • Wengler, G., G. Wengler, U. Boege, and K. Wahn. 1984. Establishment and analysis of a system which allows assembly and disassembly of alphavirus core-like particles under physiological condition in vitro. Virology 132:401-412.
    • (1984) Virology , vol.132 , pp. 401-412
    • Wengler, G.1    Wengler, G.2    Boege, U.3    Wahn, K.4
  • 29
    • 0027054277 scopus 로고
    • Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores
    • Wengler, G., D. Würkner, and G. Wengler. 1992. Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores. Virology 191:880-888.
    • (1992) Virology , vol.191 , pp. 880-888
    • Wengler, G.1    Würkner, D.2    Wengler, G.3
  • 30
    • 0028919805 scopus 로고
    • In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in E. coli and in vitro-transcribed viral cDNA
    • Zhao, X., J. M. Fox, N. H. Olson, T. S. Baker, and M. J. Young. 1995. In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in E. coli and in vitro-transcribed viral cDNA. Virology 207:486-494.
    • (1995) Virology , vol.207 , pp. 486-494
    • Zhao, X.1    Fox, J.M.2    Olson, N.H.3    Baker, T.S.4    Young, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.