메뉴 건너뛰기




Volumn 302, Issue 2, 2002, Pages 420-432

Substitution of two residues in the measles virus nucleoprotein results in an impaired self-association

Author keywords

Binding sites; Electron microscopy; Measles virus; morbillivirus; Nucleocapsid; Nucleoproteins; Paramyxoviridae; Phosphoproteins; Point mutation; Protein protein interactions

Indexed keywords

GENOMIC RNA; PHOSPHOPROTEIN; VIRUS NUCLEOPROTEIN;

EID: 0036441105     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2002.1634     Document Type: Article
Times cited : (78)

References (59)
  • 1
    • 0029926011 scopus 로고    scopus 로고
    • Domains of the measles virus N protein required for binding to P protein and self-assembly
    • Bankamp, B., Horikami, S. M., Thompson, P. D., Huber, M., Billeter, M., and Moyer, S. A. (1996). Domains of the measles virus N protein required for binding to P protein and self-assembly. Virology 216, 272-277.
    • (1996) Virology , vol.216 , pp. 272-277
    • Bankamp, B.1    Horikami, S.M.2    Thompson, P.D.3    Huber, M.4    Billeter, M.5    Moyer, S.A.6
  • 2
    • 0025033250 scopus 로고
    • Localization of nucleocapsid associated polypeptides in measles virus-infected cells by immunogold labelling after resin embedding
    • Bohn, W., Ciampor, F., Rutter, R., and Mannweiler, K. (1990). Localization of nucleocapsid associated polypeptides in measles virus-infected cells by immunogold labelling after resin embedding. Arch. Virol. 114, 53-64.
    • (1990) Arch. Virol. , vol.114 , pp. 53-64
    • Bohn, W.1    Ciampor, F.2    Rutter, R.3    Mannweiler, K.4
  • 3
    • 0024825088 scopus 로고
    • High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
    • Brinkmann, U., Mattes, R. E., and Buckel, P. (1989). High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene 85, 109-114.
    • (1989) Gene , vol.85 , pp. 109-114
    • Brinkmann, U.1    Mattes, R.E.2    Buckel, P.3
  • 4
    • 0028094123 scopus 로고
    • Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution
    • Brizzard, B. L., Chubet, R. G., and Vizard, D. L. (1994). Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution. Biotechniques 16, 730-735.
    • (1994) Biotechniques , vol.16 , pp. 730-735
    • Brizzard, B.L.1    Chubet, R.G.2    Vizard, D.L.3
  • 5
    • 0027994818 scopus 로고
    • The carboxy-terminal domain of Sendai virus nucleocapsid protein is involved in complex formation between phosphoprotein and nucleocapsid-like particles
    • Buchholz, C. J., Retzler, C., Homann, H. E., and Neubert, W. J. (1994). The carboxy-terminal domain of Sendai virus nucleocapsid protein is involved in complex formation between phosphoprotein and nucleocapsid-like particles. Virology 204, 770-776.
    • (1994) Virology , vol.204 , pp. 770-776
    • Buchholz, C.J.1    Retzler, C.2    Homann, H.E.3    Neubert, W.J.4
  • 6
    • 0027260606 scopus 로고
    • The conserved N-terminal region of Sendai virus nucleocapsid protein NP is required for nucleocapsid assembly
    • Buchholz, C. J., Spehner, D., Drillien, R., Neubert, W. J., and Homann, H. E. (1993). The conserved N-terminal region of Sendai virus nucleocapsid protein NP is required for nucleocapsid assembly. J. Virol. 67, 5803-5812.
    • (1993) J. Virol. , vol.67 , pp. 5803-5812
    • Buchholz, C.J.1    Spehner, D.2    Drillien, R.3    Neubert, W.J.4    Homann, H.E.5
  • 7
    • 0024535057 scopus 로고
    • Expression of measles virus nucleoprotein in Escherichia coli: Use of deletion mutants to locate the antigenic sites
    • Buckland, R., Giraudon, P., and Wild, F. (1989). Expression of measles virus nucleoprotein in Escherichia coli: Use of deletion mutants to locate the antigenic sites. J. Gen. Virol. 70, 435-441.
    • (1989) J. Gen. Virol. , vol.70 , pp. 435-441
    • Buckland, R.1    Giraudon, P.2    Wild, F.3
  • 8
    • 0030198563 scopus 로고    scopus 로고
    • Reexamination of the Sendai virus P protein domains required for RNA synthesis: A possible supplemental role for the P protein
    • Curran, J. (1996). Reexamination of the Sendai virus P protein domains required for RNA synthesis: A possible supplemental role for the P protein. Virology 221, 130-140.
    • (1996) Virology , vol.221 , pp. 130-140
    • Curran, J.1
  • 9
    • 0031968675 scopus 로고    scopus 로고
    • A role for the Sendai virus P protein trimer in RNA synthesis
    • Curran, J. (1998). A role for the Sendai virus P protein trimer in RNA synthesis. J. Virol. 72, 4274-4280.
    • (1998) J. Virol. , vol.72 , pp. 4274-4280
    • Curran, J.1
  • 10
    • 0027159962 scopus 로고
    • The hypervariable C-terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidation
    • Curran, J., Homann, H., Buchholz, C., Rochat, S., Neubert, W., and Kolakofsky, D. (1993). The hypervariable C-terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidation. J. Virol. 67, 4358-4364.
    • (1993) J. Virol. , vol.67 , pp. 4358-4364
    • Curran, J.1    Homann, H.2    Buchholz, C.3    Rochat, S.4    Neubert, W.5    Kolakofsky, D.6
  • 11
    • 0032651115 scopus 로고    scopus 로고
    • Replication of paramyxoviruses
    • Curran, J., and Kolakofsky, D. (1999). Replication of paramyxoviruses. Adv. Virus Res. 54, 403-422.
    • (1999) Adv. Virus Res. , vol.54 , pp. 403-422
    • Curran, J.1    Kolakofsky, D.2
  • 12
    • 0028895953 scopus 로고
    • An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication
    • Curran, J., Marq, J. B., and Kolakofsky, D. (1995). An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication. J. Virol. 69, 849-855.
    • (1995) J. Virol. , vol.69 , pp. 849-855
    • Curran, J.1    Marq, J.B.2    Kolakofsky, D.3
  • 13
    • 0028018466 scopus 로고
    • Prediction of protein secondary structure from circular dichroism spectra using artificial neural network techniques
    • Dalmas, B., Hunter, G. J., and Bannister, W. H. (1994). Prediction of protein secondary structure from circular dichroism spectra using artificial neural network techniques. Biochem. Mol. Biol. Int. 34, 17-26.
    • (1994) Biochem. Mol. Biol. Int. , vol.34 , pp. 17-26
    • Dalmas, B.1    Hunter, G.J.2    Bannister, W.H.3
  • 14
    • 0342757599 scopus 로고    scopus 로고
    • 2- and COOH-terminal domains of the P protein of human parainfluenza virus type 3 in transcription and replication
    • 2- and COOH-terminal domains of the P protein of human parainfluenza virus type 3 in transcription and replication. J. Virol. 74, 5886-5895.
    • (2000) J. Virol. , vol.74 , pp. 5886-5895
    • De, B.P.1    Hoffman, M.A.2    Choudhary, S.3    Huntley, C.C.4    Banerjee, A.K.5
  • 15
    • 0021723263 scopus 로고
    • Structural and functional analysis of Sendai virus nucleocapsid protein NP with monoclonal antibodies
    • Deshpande, K. L., and Portner, A. (1984). Structural and functional analysis of Sendai virus nucleocapsid protein NP with monoclonal antibodies. Virology 139, 32-42.
    • (1984) Virology , vol.139 , pp. 32-42
    • Deshpande, K.L.1    Portner, A.2
  • 16
    • 0024549988 scopus 로고
    • The Sendai virus nucleocapsid exists in at least four different helical states
    • Egelman, E. H., Wu, S. S., Amrein, M., Portner, A., and Murti, G. (1989). The Sendai virus nucleocapsid exists in at least four different helical states. J. Virol. 63, 2233-2243.
    • (1989) J. Virol. , vol.63 , pp. 2233-2243
    • Egelman, E.H.1    Wu, S.S.2    Amrein, M.3    Portner, A.4    Murti, G.5
  • 17
    • 0030963748 scopus 로고    scopus 로고
    • Assembly of recombinant Newcastle disease virus nucleocapsid protein into nucleocapsid-like structures is inhibited by the phosphoprotein
    • Errington, W., and Emmerson, P. T. (1997). Assembly of recombinant Newcastle disease virus nucleocapsid protein into nucleocapsid-like structures is inhibited by the phosphoprotein. J. Gen. Virol. 78, 2335-2339.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2335-2339
    • Errington, W.1    Emmerson, P.T.2
  • 18
    • 0014711995 scopus 로고
    • Observations on the structure of the nucleocapsids of some paramyxoviruses
    • Finch, J. T., and Gibbs, A. J. (1970). Observations on the structure of the nucleocapsids of some paramyxoviruses. J. Gen. Virol. 6, 141-150.
    • (1970) J. Gen. Virol. , vol.6 , pp. 141-150
    • Finch, J.T.1    Gibbs, A.J.2
  • 19
    • 0027166165 scopus 로고
    • Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structures
    • Fooks, A. R., Stephenson, J. R., Warnes, A., Dowsett, A. B., Rima, B. K., and Wilkinson, G. W. (1993). Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structures. J. Gen. Virol. 74, 1439-1444.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1439-1444
    • Fooks, A.R.1    Stephenson, J.R.2    Warnes, A.3    Dowsett, A.B.4    Rima, B.K.5    Wilkinson, G.W.6
  • 20
    • 0030464460 scopus 로고    scopus 로고
    • SEAVIEW and PHYLO_WIN: Two graphic tools for sequence alignment and molecular phylogeny
    • Galtier, N., Gouy, M., and Gautier, C. (1996). SEAVIEW and PHYLO_WIN: Two graphic tools for sequence alignment and molecular phylogeny. Comput. Appl. Biosci. 12, 543-548.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 543-548
    • Galtier, N.1    Gouy, M.2    Gautier, C.3
  • 21
    • 0024211670 scopus 로고
    • Mapping of antigenic domains of Sendai virus nucleocapsid protein expressed in Escherichia coli
    • Gill, D. S., Takai, S., Portner, A., and Kingsbury, D. W. (1988). Mapping of antigenic domains of Sendai virus nucleocapsid protein expressed in Escherichia coli. J. Virol. 62, 4805-4808.
    • (1988) J. Virol. , vol.62 , pp. 4805-4808
    • Gill, D.S.1    Takai, S.2    Portner, A.3    Kingsbury, D.W.4
  • 22
    • 0023896289 scopus 로고
    • Antigenic analysis of African measles virus field isolates: Identification and localisation of one conserved and two variable epitope sites on the NP protein
    • Giraudon, P., Jacquier, M. F., and Wild, T. F. (1988). Antigenic analysis of African measles virus field isolates: Identification and localisation of one conserved and two variable epitope sites on the NP protein. Virus Res. 10, 137-152.
    • (1988) Virus Res. , vol.10 , pp. 137-152
    • Giraudon, P.1    Jacquier, M.F.2    Wild, T.F.3
  • 23
    • 0027315126 scopus 로고
    • Conformational maturation of measles virus nucleocapsid protein
    • Gombart, A. F., Hirano, A., and Wong, T. C. (1993). Conformational maturation of measles virus nucleocapsid protein. J. Virol. 67, 4133-4141.
    • (1993) J. Virol. , vol.67 , pp. 4133-4141
    • Gombart, A.F.1    Hirano, A.2    Wong, T.C.3
  • 24
    • 0001010466 scopus 로고    scopus 로고
    • Measles virus
    • (B. N. Fields, D. M. Knipe, and P. M. Howley, Eds.), 4th ed. Lippincott-Raven, Philadelphia, PA
    • Griffin, D. E. (2001). Measles virus. In "Fields Virology" (B. N. Fields, D. M. Knipe, and P. M. Howley, Eds.), 4th ed., pp. 1401-1441. Lippincott-Raven, Philadelphia, PA.
    • (2001) Fields Virology , pp. 1401-1441
    • Griffin, D.E.1
  • 25
    • 0035196816 scopus 로고    scopus 로고
    • Sendai virus genome synthesis and assembly are coupled: A possible mechanism to promote viral RNA polymerase processivity
    • Gubbay, O., Curran, J., and Kolakofsky, D. (2001). Sendai virus genome synthesis and assembly are coupled: A possible mechanism to promote viral RNA polymerase processivity. J. Gen. Virol. 82, 2895-2903.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2895-2903
    • Gubbay, O.1    Curran, J.2    Kolakofsky, D.3
  • 26
    • 0028803809 scopus 로고
    • 2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself
    • 2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself. J. Gen. Virol. 76, 2863-2867.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2863-2867
    • Harty, R.N.1    Palese, P.2
  • 27
    • 0018847901 scopus 로고
    • Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: Reversible coiling and uncoiling induced by changes in salt concentration
    • Heggeness, M. H., Scheid, A., and Choppin, P. W. (1980). Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: Reversible coiling and uncoiling induced by changes in salt concentration. Proc. Natl. Acad. Sci. USA 77, 2631-2635.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2631-2635
    • Heggeness, M.H.1    Scheid, A.2    Choppin, P.W.3
  • 28
    • 0019501692 scopus 로고
    • The relationship of conformational changes in the Sendai virus nucleocapsid to proteolytic cleavage of the NP polypeptide
    • Heggeness, M. H., Scheid, A., and Choppin, P. W. (1981). The relationship of conformational changes in the Sendai virus nucleocapsid to proteolytic cleavage of the NP polypeptide. Virology 114, 555-562.
    • (1981) Virology , vol.114 , pp. 555-562
    • Heggeness, M.H.1    Scheid, A.2    Choppin, P.W.3
  • 29
    • 0026688539 scopus 로고
    • The matrix proteins of neurovirulent subacute sclerosing panencephalitis virus and its acute measles virus progenitor are functionally different
    • Hirano, A., Wang, A. H., Gombart, A. F., and Wong, T. C. (1992). The matrix proteins of neurovirulent subacute sclerosing panencephalitis virus and its acute measles virus progenitor are functionally different. Proc. Natl. Acad. Sci. USA 89, 8745-8749.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8745-8749
    • Hirano, A.1    Wang, A.H.2    Gombart, A.F.3    Wong, T.C.4
  • 30
    • 0026070510 scopus 로고
    • Sendai virus protein-protein interactions studied by a protein-blotting protein-overlay technique: Mapping of domains on NP protein required for binding to P protein
    • Homann, H. E., Willenbrink, W., Buchholz, C. J., and Neubert, W. J. (1991). Sendai virus protein-protein interactions studied by a protein-blotting protein-overlay technique: Mapping of domains on NP protein required for binding to P protein. J. Virol. 65, 1304-1309.
    • (1991) J. Virol. , vol.65 , pp. 1304-1309
    • Homann, H.E.1    Willenbrink, W.2    Buchholz, C.J.3    Neubert, W.J.4
  • 31
    • 0026747768 scopus 로고
    • Complexes of Sendai virus NP-P and P-L proteins are required for defective interfering particle genome replication in vitro
    • Horikami, S. M., Curran, J., Kolakofsky, D., and Moyer, S. A. (1992). Complexes of Sendai virus NP-P and P-L proteins are required for defective interfering particle genome replication in vitro. J. Virol. 66, 4901-4908.
    • (1992) J. Virol. , vol.66 , pp. 4901-4908
    • Horikami, S.M.1    Curran, J.2    Kolakofsky, D.3    Moyer, S.A.4
  • 32
    • 0028931697 scopus 로고
    • Structure, transcription, and replication of measles virus
    • Horikami, S. M., and Moyer, S. A. (1995). Structure, transcription, and replication of measles virus. Curr. Top. Microbiol. Immunol. 191, 35-50.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.191 , pp. 35-50
    • Horikami, S.M.1    Moyer, S.A.2
  • 33
    • 0030586736 scopus 로고    scopus 로고
    • The Sendai virus V protein interacts with the NP protein to regulate viral genome RNA replication
    • Horikami, S. M., Smallwood, S., and Moyer, S. A. (1996). The Sendai virus V protein interacts with the NP protein to regulate viral genome RNA replication. Virology 222, 383-390.
    • (1996) Virology , vol.222 , pp. 383-390
    • Horikami, S.M.1    Smallwood, S.2    Moyer, S.A.3
  • 34
    • 0032539578 scopus 로고    scopus 로고
    • The structural aspects of limited proteolysis of native proteins
    • Hubbard, S. J. (1998). The structural aspects of limited proteolysis of native proteins. Biochim. Biophys. Acta 1382, 191-206.
    • (1998) Biochim. Biophys. Acta , vol.1382 , pp. 191-206
    • Hubbard, S.J.1
  • 35
    • 0002635460 scopus 로고    scopus 로고
    • Proteolysis of native proteins as a structural probe
    • (R. J. Beynon and J. D. Bond, Eds.), 2nd ed. Oxford Univ. Press, Oxford, NY
    • Hubbard, S. J., Beynon, R. J. (2001). Proteolysis of native proteins as a structural probe. In "Proteolytic Enzymes" (R. J. Beynon and J. D. Bond, Eds.), 2nd ed., pp. 233-264. Oxford Univ. Press, Oxford, NY.
    • (2001) Proteolytic Enzymes , pp. 233-264
    • Hubbard, S.J.1    Beynon, R.J.2
  • 37
    • 0036299393 scopus 로고    scopus 로고
    • The measles virus phosphoprotein N-terminal domain (PNT) belongs to the natively unfolded class of proteins
    • Karlin, D., Longhi, S., Receveur, V., and Canard, B. (2002). The measles virus phosphoprotein N-terminal domain (PNT) belongs to the natively unfolded class of proteins. Virology 296, 251-262.
    • (2002) Virology , vol.296 , pp. 251-262
    • Karlin, D.1    Longhi, S.2    Receveur, V.3    Canard, B.4
  • 38
    • 0031924057 scopus 로고    scopus 로고
    • Identification of a region of the rabies virus N protein involved in direct binding to the viral RNA
    • Kouznetzoff, A., Buckle, M., and Tordo, N. (1998). Identification of a region of the rabies virus N protein involved in direct binding to the viral RNA. J. Gen. Virol. 79, 1005-1013.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1005-1013
    • Kouznetzoff, A.1    Buckle, M.2    Tordo, N.3
  • 39
    • 0001178028 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • (B. N. Fields, D. M. Knipe, and P. M. Howley, Eds.), 4th ed. Lippincott-Raven, Philadelphia, PA
    • Lamb, R. A., and Kolakofsky, D. (2001). Paramyxoviridae: The viruses and their replication. In "Fields Virology" (B. N. Fields, D. M. Knipe, and P. M. Howley, Eds.), 4th ed., pp. 1305-1340. Lippincott-Raven, Philadelphia, PA.
    • (2001) Fields Virology , pp. 1305-1340
    • Lamb, R.A.1    Kolakofsky, D.2
  • 40
    • 0031055574 scopus 로고    scopus 로고
    • Protein interaction domains of the measles virus nucleocapsid protein (NP)
    • Liston, P., Batal, R., DiFlumeri, C., and Briedis, D. J. (1997). Protein interaction domains of the measles virus nucleocapsid protein (NP). Arch. Virol. 142, 305-321.
    • (1997) Arch. Virol. , vol.142 , pp. 305-321
    • Liston, P.1    Batal, R.2    DiFlumeri, C.3    Briedis, D.J.4
  • 41
    • 0028846589 scopus 로고
    • Protein interactions entered into by the measles virus P, V, and C proteins
    • Liston, P., DiFlumeri, C., and Briedis, D. J. (1995). Protein interactions entered into by the measles virus P, V, and C proteins. Virus Res. 38, 241-259.
    • (1995) Virus Res. , vol.38 , pp. 241-259
    • Liston, P.1    DiFlumeri, C.2    Briedis, D.J.3
  • 42
    • 0031575842 scopus 로고    scopus 로고
    • A highly conserved region of the Sendai virus nucleocapsid protein contributes to the NP-NP binding domain
    • Myers, T. M., Pieters, A., and Moyer, S. A. (1997). A highly conserved region of the Sendai virus nucleocapsid protein contributes to the NP-NP binding domain. Virology 229, 322-335.
    • (1997) Virology , vol.229 , pp. 322-335
    • Myers, T.M.1    Pieters, A.2    Moyer, S.A.3
  • 43
    • 0033016954 scopus 로고    scopus 로고
    • Identification of nucleocapsid protein residues required for Sendai virus nucleocapsid formation and genome replication
    • Myers, T. M., Smallwood, S., and Moyer, S. A. (1999). Identification of nucleocapsid protein residues required for Sendai virus nucleocapsid formation and genome replication. J. Gen. Virol. 80, 1383-1391.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1383-1391
    • Myers, T.M.1    Smallwood, S.2    Moyer, S.A.3
  • 44
    • 0014515705 scopus 로고
    • Development of measles virus in vitro
    • Nakai, T., Shand, F. L., and Howatson, A. F. (1969). Development of measles virus in vitro. Virology 38, 50-67.
    • (1969) Virology , vol.38 , pp. 50-67
    • Nakai, T.1    Shand, F.L.2    Howatson, A.F.3
  • 46
    • 0000163167 scopus 로고    scopus 로고
    • Rhabdoviridae: The viruses and their replication
    • (B. N. Fields, D. M. Knipe, and P. M. Howley, Eds.), 4th ed. Lippincott-Raven, Philadelphia, PA
    • Rose, J. K., and Whitt, M. A. (2001). Rhabdoviridae: The viruses and their replication. In "Fields Virology" (B. N. Fields, D. M. Knipe, and P. M. Howley, Eds.), 4th ed., pp. 1221-1241. Lippincott-Raven, Philadelphia, PA.
    • (2001) Fields Virology , pp. 1221-1241
    • Rose, J.K.1    Whitt, M.A.2
  • 47
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • Rost, B. (1996). PHD: Predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 266, 525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 48
    • 0025017126 scopus 로고
    • Separate domains of Sendai virus P protein are required for binding to viral nucleocapsids
    • Ryan, K. W., and Portner, A. (1990). Separate domains of Sendai virus P protein are required for binding to viral nucleocapsids. Virology 174, 515-521.
    • (1990) Virology , vol.174 , pp. 515-521
    • Ryan, K.W.1    Portner, A.2
  • 49
    • 0027209004 scopus 로고
    • Antibodies to paramyxovirus nucleoproteins define regions important for immunogenicity and nucleocapsid assembly
    • Ryan, K. W., Portner, A., and Murti, K. G. (1993). Antibodies to paramyxovirus nucleoproteins define regions important for immunogenicity and nucleocapsid assembly. Virology 193, 376-384.
    • (1993) Virology , vol.193 , pp. 376-384
    • Ryan, K.W.1    Portner, A.2    Murti, K.G.3
  • 50
    • 0031579250 scopus 로고    scopus 로고
    • Recombinant measles viruses defective for RNA editing and V protein synthesis are viable in cultured cells
    • Schneider, H., Kaelin, K., and Billeter, M. A. (1997). Recombinant measles viruses defective for RNA editing and V protein synthesis are viable in cultured cells. Virology 227, 314-322.
    • (1997) Virology , vol.227 , pp. 314-322
    • Schneider, H.1    Kaelin, K.2    Billeter, M.A.3
  • 51
    • 0034749347 scopus 로고    scopus 로고
    • Structure of recombinant rabies virus nucleoprotein-RNA complex and identification of the phosphoprotein binding site
    • Schoehn, G., Iseni, F., Mavrakis, M., Blondel, D., and Ruigrok, R. W. (2001). Structure of recombinant rabies virus nucleoprotein-RNA complex and identification of the phosphoprotein binding site. J. Virol. 75, 490-498.
    • (2001) J. Virol. , vol.75 , pp. 490-498
    • Schoehn, G.1    Iseni, F.2    Mavrakis, M.3    Blondel, D.4    Ruigrok, R.W.5
  • 52
    • 0031611889 scopus 로고    scopus 로고
    • The replicative complex of paramyxoviruses: Structure and function
    • Sedlmeier, R., and Neubert, W. J. (1998). The replicative complex of paramyxoviruses: Structure and function. Adv. Virus Res. 50, 101-139.
    • (1998) Adv. Virus Res. , vol.50 , pp. 101-139
    • Sedlmeier, R.1    Neubert, W.J.2
  • 53
    • 0033526504 scopus 로고    scopus 로고
    • Domains of Rinderpest virus phosphoprotein involved in interaction with itself and the nucleocapsid protein
    • Shaji, D., and Shaila, M. S. (1999). Domains of Rinderpest virus phosphoprotein involved in interaction with itself and the nucleocapsid protein. Virology 258, 415-424.
    • (1999) Virology , vol.258 , pp. 415-424
    • Shaji, D.1    Shaila, M.S.2
  • 54
    • 0030832332 scopus 로고    scopus 로고
    • The assembly of the measles virus nucleoprotein into nucleocapsid-like particles is modulated by the phosphoprotein
    • Spehner, D., Drillien, R., and Howley, P. M. (1997). The assembly of the measles virus nucleoprotein into nucleocapsid-like particles is modulated by the phosphoprotein. Virology 232, 260-268.
    • (1997) Virology , vol.232 , pp. 260-268
    • Spehner, D.1    Drillien, R.2    Howley, P.M.3
  • 55
    • 0025983571 scopus 로고
    • Assembly of nucleocapsid-like structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein
    • Spehner, D., Kirn, A., and Drillien, R. (1991). Assembly of nucleocapsid-like structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein. J. Virol. 65, 6296-6300.
    • (1991) J. Virol. , vol.65 , pp. 6296-6300
    • Spehner, D.1    Kirn, A.2    Drillien, R.3
  • 56
    • 0028345962 scopus 로고
    • The Sendai virus matrix protein appears to be recruited in the cytoplasm by the viral nucleocapsid to function in viral assembly and budding
    • Stricker, R., Mottet, G., and Roux, L. (1994). The Sendai virus matrix protein appears to be recruited in the cytoplasm by the viral nucleocapsid to function in viral assembly and budding. J. Gen. Virol. 75, 1031-1042.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1031-1042
    • Stricker, R.1    Mottet, G.2    Roux, L.3
  • 57
    • 0028040129 scopus 로고
    • Transcription inhibition and other properties of matrix proteins expressed by M genes cloned from measles viruses and diseased human brain tissue
    • Suryanarayana, K., Baczko, K., ter Meulen, V., and Wagner, R. R. (1994). Transcription inhibition and other properties of matrix proteins expressed by M genes cloned from measles viruses and diseased human brain tissue. J. Virol. 68, 1532-1543.
    • (1994) J. Virol. , vol.68 , pp. 1532-1543
    • Suryanarayana, K.1    Baczko, K.2    Ter Meulen, V.3    Wagner, R.R.4
  • 58
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994). CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 59
    • 0029143791 scopus 로고
    • Expression of the measles virus nucleoprotein gene in Escherichia coli and assembly of nucleocapsid-like structures
    • Warnes, A., Fooks, A. R., Dowsett, A. B., Wilkinson, G. W., and Stephenson, J. R. (1995). Expression of the measles virus nucleoprotein gene in Escherichia coli and assembly of nucleocapsid-like structures. Gene 160, 173-178.
    • (1995) Gene , vol.160 , pp. 173-178
    • Warnes, A.1    Fooks, A.R.2    Dowsett, A.B.3    Wilkinson, G.W.4    Stephenson, J.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.