메뉴 건너뛰기




Volumn 250, Issue 1, 1998, Pages 106-117

Assaying for structural variation in the parvovirus capsid and its role in infection

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE;

EID: 0032505630     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9352     Document Type: Article
Times cited : (87)

References (72)
  • 1
    • 0021241157 scopus 로고
    • Aleutian disease virus, a parvovirus, is proteolytically degraded duringin vivo
    • Aasted B., Race R. E., Bloom M. E. Aleutian disease virus, a parvovirus, is proteolytically degraded duringin vivo. J. Virol. 51:1984;7-13.
    • (1984) J. Virol. , vol.51 , pp. 7-13
    • Aasted, B.1    Race, R.E.2    Bloom, M.E.3
  • 4
    • 0028813844 scopus 로고
    • Peptides derived from the unique region of B19 parvovirus minor capsid protein elicit neutralizing antibodies in rabbits
    • Anderson S., Momoeda M., Kawase M., Kajigaya S., Young N. S. Peptides derived from the unique region of B19 parvovirus minor capsid protein elicit neutralizing antibodies in rabbits. Virology. 206:1995;626-632.
    • (1995) Virology , vol.206 , pp. 626-632
    • Anderson, S.1    Momoeda, M.2    Kawase, M.3    Kajigaya, S.4    Young, N.S.5
  • 5
    • 0030600141 scopus 로고    scopus 로고
    • Endosomal proteolysis of internalized proteins
    • Authier F., Posner B. I., Bergeron J. J. M. Endosomal proteolysis of internalized proteins. FEBS Lett. 389:1996;55-60.
    • (1996) FEBS Lett. , vol.389 , pp. 55-60
    • Authier, F.1    Posner, B.I.2    Bergeron, J.J.M.3
  • 6
    • 0030999547 scopus 로고    scopus 로고
    • Mutations in reovirus outer-capsid protein ς3 selected during persistent infections of L cells confer resistance to protease inhibitor E64
    • Baer G. S., Dermody T. S. Mutations in reovirus outer-capsid protein ς3 selected during persistent infections of L cells confer resistance to protease inhibitor E64. J. Virol. 71:1997;4921-4928.
    • (1997) J. Virol. , vol.71 , pp. 4921-4928
    • Baer, G.S.1    Dermody, T.S.2
  • 7
    • 0025767163 scopus 로고
    • Parvoviral target cell specificity: Acquisition of fibrotropism by a mutant of the lymphotropic strain of minute virus of mice involves multiple amino acid substitutions within the capsid
    • Ball-Goodrich L. J., Moir R. D., Tattersall P. Parvoviral target cell specificity: acquisition of fibrotropism by a mutant of the lymphotropic strain of minute virus of mice involves multiple amino acid substitutions within the capsid. Virology. 184:1991;175-186.
    • (1991) Virology , vol.184 , pp. 175-186
    • Ball-Goodrich, L.J.1    Moir, R.D.2    Tattersall, P.3
  • 8
    • 0026736515 scopus 로고
    • Two amino acid substitutions within the capsid are coordinately required for acquisition of fibrotropism by the lymphotropic strain of minute virus of mice
    • Ball-Goodrich L. J., Tattersall P. Two amino acid substitutions within the capsid are coordinately required for acquisition of fibrotropism by the lymphotropic strain of minute virus of mice. J. Virol. 66:1992;3415-3423.
    • (1992) J. Virol. , vol.66 , pp. 3415-3423
    • Ball-Goodrich, L.J.1    Tattersall, P.2
  • 9
    • 0026524911 scopus 로고
    • Infectious entry pathway for canine parvovirus
    • Basak S., Turner H. Infectious entry pathway for canine parvovirus. Virology. 186:1992;368-376.
    • (1992) Virology , vol.186 , pp. 368-376
    • Basak, S.1    Turner, H.2
  • 10
    • 0029873185 scopus 로고    scopus 로고
    • Genome organization of the Kresse strain of porcine parvovirus: Identification of the allotropic determinant and comparison with those of NADL-2 and field isolates
    • Bergeron J., Hebert B., Tijssen P. Genome organization of the Kresse strain of porcine parvovirus: identification of the allotropic determinant and comparison with those of NADL-2 and field isolates. J. Virol. 70:1996;2508-2515.
    • (1996) J. Virol. , vol.70 , pp. 2508-2515
    • Bergeron, J.1    Hebert, B.2    Tijssen, P.3
  • 11
    • 0019029910 scopus 로고
    • Establishment of a canine cell line: Derivation, characterization and viral spectrum
    • Binn L. N., Marchwicki R. H., Stephenson E. H. Establishment of a canine cell line: derivation, characterization and viral spectrum. Am. J. Vet. Res. 41:1980;855-860.
    • (1980) Am. J. Vet. Res. , vol.41 , pp. 855-860
    • Binn, L.N.1    Marchwicki, R.H.2    Stephenson, E.H.3
  • 12
    • 0027197653 scopus 로고
    • Characterization of chimeric full-length molecular clones of Aleutian mink disease parvovirus (ADV): Identification of a determinant governing replication of ADV in cell culture
    • Bloom M. E., Berry B. D., Wei W., Perryman S., Wolfinbarger J. B. Characterization of chimeric full-length molecular clones of Aleutian mink disease parvovirus (ADV): identification of a determinant governing replication of ADV in cell culture. J. Virol. 67:1993;5976-5988.
    • (1993) J. Virol. , vol.67 , pp. 5976-5988
    • Bloom, M.E.1    Berry, B.D.2    Wei, W.3    Perryman, S.4    Wolfinbarger, J.B.5
  • 14
    • 0031985001 scopus 로고    scopus 로고
    • Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry
    • Bothner B., Dong X. F., Bibbs L., Johnson J. E., Siuzdak G. Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry. J. Biol. Chem. 273:1998;673-676.
    • (1998) J. Biol. Chem. , vol.273 , pp. 673-676
    • Bothner, B.1    Dong, X.F.2    Bibbs, L.3    Johnson, J.E.4    Siuzdak, G.5
  • 15
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough P. A., Hughson F. M., Skehel J. J., Wiley D. C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature. 371:1994;37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 16
    • 0028856089 scopus 로고
    • Peptide vaccine against canine parvovirus: Identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence
    • Casal J. I., Langeveld J. P., Cortes E., Schaaper W. W., van Dijk E., Vela C., Kamstrup S., Meloen R. H. Peptide vaccine against canine parvovirus: identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence. J. Virol. 69:1995;7274-7277.
    • (1995) J. Virol. , vol.69 , pp. 7274-7277
    • Casal, J.I.1    Langeveld, J.P.2    Cortes, E.3    Schaaper, W.W.4    Van Dijk, E.5    Vela, C.6    Kamstrup, S.7    Meloen, R.H.8
  • 17
    • 0026495801 scopus 로고
    • Multiple amino acids in the capsid structure of canine parvovirus coordinately determine the canine host range and specific antigenic and hemagglutination properties
    • Chang S. F., Sgro J. Y., Parrish C. R. Multiple amino acids in the capsid structure of canine parvovirus coordinately determine the canine host range and specific antigenic and hemagglutination properties. J. Virol. 66:1992;6858-6567.
    • (1992) J. Virol. , vol.66 , pp. 6858-6567
    • Chang, S.F.1    Sgro, J.Y.2    Parrish, C.R.3
  • 18
    • 0027194071 scopus 로고
    • Structure, sequence, and function correlations among parvoviruses
    • Chapman M. S., Rossmann M. G. Structure, sequence, and function correlations among parvoviruses. Virology. 194:1993;491-508.
    • (1993) Virology , vol.194 , pp. 491-508
    • Chapman, M.S.1    Rossmann, M.G.2
  • 19
    • 0029643956 scopus 로고
    • Single-stranded DNA-protein interactions in canine parvovirus
    • Chapman M. S., Rossmann M. G. Single-stranded DNA-protein interactions in canine parvovirus. Structure. 3:1995;151-162.
    • (1995) Structure , vol.3 , pp. 151-162
    • Chapman, M.S.1    Rossmann, M.G.2
  • 20
    • 0025915718 scopus 로고
    • Import of simian virus 40 through nuclear pore complexes
    • Clever J., Yamada M., Kasamatsu H. Import of simian virus 40 through nuclear pore complexes. Proc. Natl. Acad. Sci. USA. 88:1991;7333-7337.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7333-7337
    • Clever, J.1    Yamada, M.2    Kasamatsu, H.3
  • 21
    • 0017200326 scopus 로고
    • The parvovirus MVM: A comparison of heavy and light particle infectivity and their density conversionin vitro.
    • Clinton G. M., Hayashi M. The parvovirus MVM: a comparison of heavy and light particle infectivity and their density conversionin vitro. Virology. 74:1976;57-63.
    • (1976) Virology , vol.74 , pp. 57-63
    • Clinton, G.M.1    Hayashi, M.2
  • 22
    • 0016529725 scopus 로고
    • The parvovirus MVM: Particles with altered structural proteins
    • Clinton G. M., Hayashi M. The parvovirus MVM: particles with altered structural proteins. Virology. 66:1975;261-267.
    • (1975) Virology , vol.66 , pp. 261-267
    • Clinton, G.M.1    Hayashi, M.2
  • 23
    • 0030993261 scopus 로고    scopus 로고
    • The NS2 polypeptide of parvovirus MVM is required for capsid assembly in murine cells
    • Cotmore S. F., Abramo A. M. Jr., Carbonell L. F., Bratton J., Tattersall P. The NS2 polypeptide of parvovirus MVM is required for capsid assembly in murine cells. Virology. 231:1997;267-280.
    • (1997) Virology , vol.231 , pp. 267-280
    • Cotmore, S.F.1    Abramo A.M., Jr.2    Carbonell, L.F.3    Bratton, J.4    Tattersall, P.5
  • 24
    • 0023065751 scopus 로고
    • The autonomously replicating parvoviruses of vertebrates
    • Cotmore S. F., Tattersall P. The autonomously replicating parvoviruses of vertebrates. Adv. Virus Res. 33:1987;91-174.
    • (1987) Adv. Virus Res. , vol.33 , pp. 91-174
    • Cotmore, S.F.1    Tattersall, P.2
  • 25
    • 0024409384 scopus 로고
    • A genome-linked copy of the NS-1 polypeptide is located on the outside of infectious parvovirus particles
    • Cotmore S. F., Tattersall P. A genome-linked copy of the NS-1 polypeptide is located on the outside of infectious parvovirus particles. J. Virol. 63:1989;3902-3911.
    • (1989) J. Virol. , vol.63 , pp. 3902-3911
    • Cotmore, S.F.1    Tattersall, P.2
  • 26
    • 0028883978 scopus 로고
    • The adenovirus protease is required for virus entry into cells
    • Cotten M., Weber J. M. The adenovirus protease is required for virus entry into cells. Virology. 213:1995;494-502.
    • (1995) Virology , vol.213 , pp. 494-502
    • Cotten, M.1    Weber, J.M.2
  • 27
    • 0027320799 scopus 로고
    • Protein conformational changes in virus-cell fusion
    • Doms R. W. Protein conformational changes in virus-cell fusion. Methods Enzymol. 221:1993b;63-83.
    • (1993) Methods Enzymol. , vol.221 , pp. 63-83
    • Doms, R.W.1
  • 28
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms R. W., Lamb R. A., Rose J. K., Helenius A. Folding and assembly of viral membrane proteins. Virology. 193:1993a;545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 29
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supermolecular structure and protein conformation: Analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden K. A., Wang G., Yeager M., Nibert M. L., Coombs K. M., Furlong D. B., Fields B. N., Baker T. S. Early steps in reovirus infection are associated with dramatic changes in supermolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Exp. Med. 122:1993;1023-1041.
    • (1993) J. Exp. Med. , vol.122 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 30
    • 0027138758 scopus 로고
    • Endosomal proteolysis precedes ricin A-chain toxicity in macrophages
    • Fiani M. L., Blum J. S., Stahl P. D. Endosomal proteolysis precedes ricin A-chain toxicity in macrophages. Arch. Biochem. Biophys. 307:1993;225-230.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 225-230
    • Fiani, M.L.1    Blum, J.S.2    Stahl, P.D.3
  • 31
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks C. E., Hogle J. M. Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding. J. Virol. 64:1990;1934-1945.
    • (1990) J. Virol. , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 32
    • 0029052283 scopus 로고
    • Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex
    • Fuller S. D., Berriman J. A., Butcher S. J., Gowen B. E. Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex. Cell. 81:1995;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
  • 33
    • 0029983628 scopus 로고    scopus 로고
    • The role of adenovirus protease in virus entry into cells
    • Greber U. F., Webster P., Weber J., Helenius A. The role of adenovirus protease in virus entry into cells. EMBO J. 15:1996;1766-1777.
    • (1996) EMBO J. , vol.15 , pp. 1766-1777
    • Greber, U.F.1    Webster, P.2    Weber, J.3    Helenius, A.4
  • 34
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • Greber U. F., Willetts M., Webster P., Helenius A. Stepwise dismantling of adenovirus 2 during entry into cells. Cell. 75:1993;477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 35
    • 0028240924 scopus 로고
    • Mapping of determinants of the host range for canine cells in the genome of canine parvovirus using canine parvovirus/mink enteritis virus chimeric viruses
    • Horiuchi M., Goto H., Ishiguro N., Shinagawa M. Mapping of determinants of the host range for canine cells in the genome of canine parvovirus using canine parvovirus/mink enteritis virus chimeric viruses. J. Gen. Virol. 75:1994;1319-1328.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1319-1328
    • Horiuchi, M.1    Goto, H.2    Ishiguro, N.3    Shinagawa, M.4
  • 36
    • 0026683689 scopus 로고
    • Characterization of the stage(s) in the virus replication cycle at which the host-cell specificity of the feline parvovirus subgroup is regulated in canine cells
    • Horiuchi M., Ishiguro N., Goto H., Shinagawa M. Characterization of the stage(s) in the virus replication cycle at which the host-cell specificity of the feline parvovirus subgroup is regulated in canine cells. Virology. 189:1992;600-608.
    • (1992) Virology , vol.189 , pp. 600-608
    • Horiuchi, M.1    Ishiguro, N.2    Goto, H.3    Shinagawa, M.4
  • 37
    • 0029162017 scopus 로고
    • Most of the VP1 unique region of B19 parvovirus is on the capsid surface
    • Kawase M., Momoeda M., Young N. S., Kajigaya S. Most of the VP1 unique region of B19 parvovirus is on the capsid surface. Virology. 211:1995;359-366.
    • (1995) Virology , vol.211 , pp. 359-366
    • Kawase, M.1    Momoeda, M.2    Young, N.S.3    Kajigaya, S.4
  • 38
    • 0028040536 scopus 로고
    • Mapping of antigenic domains in poliovirus VP1 involved in structural rearrangements during virus morphogenesis and antigenic alterations of the virion
    • Ketterlinus R., Wiegers K. Mapping of antigenic domains in poliovirus VP1 involved in structural rearrangements during virus morphogenesis and antigenic alterations of the virion. Virology. 204:1994;27-37.
    • (1994) Virology , vol.204 , pp. 27-37
    • Ketterlinus, R.1    Wiegers, K.2
  • 40
    • 0027532370 scopus 로고
    • Role of maturation cleavage in infectivity of picornaviruses: Activation of an infectosome
    • Lee W.-M., Monroe S. S., Rueckert R. R. Role of maturation cleavage in infectivity of picornaviruses: activation of an infectosome. J. Virol. 67:1993;2110-2122.
    • (1993) J. Virol. , vol.67 , pp. 2110-2122
    • Lee, W.-M.1    Monroe, S.S.2    Rueckert, R.R.3
  • 43
    • 0025219313 scopus 로고
    • Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62
    • Lobigs M., Garoff H. Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62. J. Virol. 64:1990;1233-1240.
    • (1990) J. Virol. , vol.64 , pp. 1233-1240
    • Lobigs, M.1    Garoff, H.2
  • 44
    • 0029887665 scopus 로고    scopus 로고
    • Protease-induced infectivity of hepatitis B virus for a human hepatoblastoma cell line
    • Lu X., Block T. M., Gerlich W. H. Protease-induced infectivity of hepatitis B virus for a human hepatoblastoma cell line. J. Virol. 70:1996;2277-2285.
    • (1996) J. Virol. , vol.70 , pp. 2277-2285
    • Lu, X.1    Block, T.M.2    Gerlich, W.H.3
  • 45
    • 0024534779 scopus 로고
    • Virus entry into animal cells
    • Marsh M., Helenius A. Virus entry into animal cells. Adv. Virus Res. 36:1989;107-151.
    • (1989) Adv. Virus Res. , vol.36 , pp. 107-151
    • Marsh, M.1    Helenius, A.2
  • 47
    • 0026327392 scopus 로고
    • An endogenous MDCK lysosomal membrane glycoprotein in targeted basolaterally before delivery to lysosomes
    • Nabi I. R., Le Bivic A. L., Fambrough D., Rodriguez-Boulan E. An endogenous MDCK lysosomal membrane glycoprotein in targeted basolaterally before delivery to lysosomes. J. Cell Biol. 115:1991;1573-1584.
    • (1991) J. Cell Biol. , vol.115 , pp. 1573-1584
    • Nabi, I.R.1    Le Bivic, A.L.2    Fambrough, D.3    Rodriguez-Boulan, E.4
  • 48
    • 0019468712 scopus 로고
    • Infectious process of the parvovirus H-I: Correlation of protein content, particle density, and viral infectivity
    • Paradiso P. R. Infectious process of the parvovirus H-I: correlation of protein content, particle density, and viral infectivity. J. Virol. 39:1981;800-807.
    • (1981) J. Virol. , vol.39 , pp. 800-807
    • Paradiso, P.R.1
  • 49
    • 0020460257 scopus 로고
    • Canine parvovirus: A biochemical and ultrastructural characterization
    • Paradiso P. R., Rhode S. L., Singer I. I. Canine parvovirus: a biochemical and ultrastructural characterization. J. Gen. Virol. 62:1982;113-125.
    • (1982) J. Gen. Virol. , vol.62 , pp. 113-125
    • Paradiso, P.R.1    Rhode, S.L.2    Singer, I.I.3
  • 50
    • 0021231590 scopus 로고
    • Mapping of the amino terminus of the H-1 parvovirus major capsid protein
    • Paradiso P. R., Williams K. R., Costantino R. L. Mapping of the amino terminus of the H-1 parvovirus major capsid protein. J. Virol. 52:1984;77-81.
    • (1984) J. Virol. , vol.52 , pp. 77-81
    • Paradiso, P.R.1    Williams, K.R.2    Costantino, R.L.3
  • 51
    • 0030782148 scopus 로고    scopus 로고
    • Canine parvovirus host range is determined by the specific conformation of an additional region of the capsid
    • Parker J. S. L., Parrish C. R. Canine parvovirus host range is determined by the specific conformation of an additional region of the capsid. J. Virol. 71:1997;9214-9222.
    • (1997) J. Virol. , vol.71 , pp. 9214-9222
    • Parker, J.S.L.1    Parrish, C.R.2
  • 52
    • 0025177661 scopus 로고
    • Emergence, natural history, and variation of canine, mink, and feline parvoviruses
    • Parrish C. R. Emergence, natural history, and variation of canine, mink, and feline parvoviruses. Adv. Virus Res. 38:1990;403-450.
    • (1990) Adv. Virus Res. , vol.38 , pp. 403-450
    • Parrish, C.R.1
  • 53
    • 0025826498 scopus 로고
    • Mapping specific functions in the capsid structure of canine parvovirus and feline panleukopenia virus using infectious plasmid clones
    • Parrish C. R. Mapping specific functions in the capsid structure of canine parvovirus and feline panleukopenia virus using infectious plasmid clones. Virology. 183:1991;195-205.
    • (1991) Virology , vol.183 , pp. 195-205
    • Parrish, C.R.1
  • 54
    • 0001634993 scopus 로고
    • The emergence and evolution of canine parvovirus: An example of recent host range mutation
    • Parrish C. R. The emergence and evolution of canine parvovirus: an example of recent host range mutation. Semin. Virol. 5:1994;121-132.
    • (1994) Semin. Virol. , vol.5 , pp. 121-132
    • Parrish, C.R.1
  • 55
    • 0029188724 scopus 로고
    • The adeno-associated virus Rep78 protein is covalently linked to viral DNA in a preformed virion
    • Prasad K.-M. R., Trempe J. P. The adeno-associated virus Rep78 protein is covalently linked to viral DNA in a preformed virion. Virology. 214:1995;360-370.
    • (1995) Virology , vol.214 , pp. 360-370
    • Prasad, K.-M.R.1    Trempe, J.P.2
  • 56
    • 0028229815 scopus 로고
    • Uncoating of human rhinovirus serotype 2 from late endosomes
    • Prchla E., Kuechler E., Blaas D., Fuchs R. Uncoating of human rhinovirus serotype 2 from late endosomes. J. Virol. 68:1994;3713-3723.
    • (1994) J. Virol. , vol.68 , pp. 3713-3723
    • Prchla, E.1    Kuechler, E.2    Blaas, D.3    Fuchs, R.4
  • 57
    • 0027328068 scopus 로고
    • Defect in entry and altered pathogenicity of a polyoma virus mutant blocked in VP2 myristylation
    • Sahli R., Freund R., Dubensky T., Garcxea R., Bronson R., Benjamin T. Defect in entry and altered pathogenicity of a polyoma virus mutant blocked in VP2 myristylation. Virology. 192:1993;142-153.
    • (1993) Virology , vol.192 , pp. 142-153
    • Sahli, R.1    Freund, R.2    Dubensky, T.3    Garcxea, R.4    Bronson, R.5    Benjamin, T.6
  • 58
    • 0029795282 scopus 로고    scopus 로고
    • Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus
    • Stiasny K., Allison S. L., Marchler-Bauer A., Kunz C., Heinz F. X. Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. J. Virol. 70:1996;8142-8147.
    • (1996) J. Virol. , vol.70 , pp. 8142-8147
    • Stiasny, K.1    Allison, S.L.2    Marchler-Bauer, A.3    Kunz, C.4    Heinz, F.X.5
  • 59
    • 0028290887 scopus 로고
    • Two dominant neutralizing antigenic determinants of canine parvovirus are found on the threefold spike of the virus capsid
    • Strassheim M. L., Gruenberg A., Veijalainen P., Sgro J.-Y., Parrish C. R. Two dominant neutralizing antigenic determinants of canine parvovirus are found on the threefold spike of the virus capsid. Virology. 198:1994;175-184.
    • (1994) Virology , vol.198 , pp. 175-184
    • Strassheim, M.L.1    Gruenberg, A.2    Veijalainen, P.3    Sgro, J.-Y.4    Parrish, C.R.5
  • 60
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle
    • Sturzenbecker L. J., Nibert M., Furlong D., Fields B. N. Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle. J. Virol. 61:1987;2351-2361.
    • (1987) J. Virol. , vol.61 , pp. 2351-2361
    • Sturzenbecker, L.J.1    Nibert, M.2    Furlong, D.3    Fields, B.N.4
  • 61
    • 0017107506 scopus 로고
    • Three structural polypeptides coded for by minute virus of mice, a parvovirus
    • Tattersall P., Cawte P. J., Shatkin A. J., Ward D. C. Three structural polypeptides coded for by minute virus of mice, a parvovirus. J. Virol. 20:1976;273-289.
    • (1976) J. Virol. , vol.20 , pp. 273-289
    • Tattersall, P.1    Cawte, P.J.2    Shatkin, A.J.3    Ward, D.C.4
  • 62
    • 0017353812 scopus 로고
    • Sequence homology between the structural polypeptides of minute virus of mice
    • Tattersall P., Shatkin A. J., Ward D. C. Sequence homology between the structural polypeptides of minute virus of mice. J. Mol. Biol. 111:1977;775-794.
    • (1977) J. Mol. Biol. , vol.111 , pp. 775-794
    • Tattersall, P.1    Shatkin, A.J.2    Ward, D.C.3
  • 63
    • 0030062362 scopus 로고    scopus 로고
    • Evolution of canine parvovirus involved loss and gain of feline host range
    • Truyen U., Evermann J. F., Vieler E., Parrish C. R. Evolution of canine parvovirus involved loss and gain of feline host range. Virology. 215:1996;186-189.
    • (1996) Virology , vol.215 , pp. 186-189
    • Truyen, U.1    Evermann, J.F.2    Vieler, E.3    Parrish, C.R.4
  • 64
    • 0029072670 scopus 로고
    • Evolution of the feline-subgroup parvoviruses and the control of canine host rangein vivo.
    • Truyen U., Gruenberg A., Chang S. F., Obermaier B., Veijalainen P., Parrish C. R. Evolution of the feline-subgroup parvoviruses and the control of canine host rangein vivo. J. Virol. 69:1995;4702-4710.
    • (1995) J. Virol. , vol.69 , pp. 4702-4710
    • Truyen, U.1    Gruenberg, A.2    Chang, S.F.3    Obermaier, B.4    Veijalainen, P.5    Parrish, C.R.6
  • 66
    • 0027070506 scopus 로고
    • The trypsin-sensitive RVER domain in the capsid proteins of minute virus of mice is required for efficient cell binding and viral infection but not for proteolytic processingin vivo.
    • Tullis G. E., Burger L. R., Pintel D. J. The trypsin-sensitive RVER domain in the capsid proteins of minute virus of mice is required for efficient cell binding and viral infection but not for proteolytic processingin vivo. Virology. 191:1992;846-857.
    • (1992) Virology , vol.191 , pp. 846-857
    • Tullis, G.E.1    Burger, L.R.2    Pintel, D.J.3
  • 67
    • 0025994285 scopus 로고
    • Infectious entry pathway of adenovirus type 2
    • Varga M. J., Weibull C., Everitt E. Infectious entry pathway of adenovirus type 2. J. Virol. 65:1991;6061-6070.
    • (1991) J. Virol. , vol.65 , pp. 6061-6070
    • Varga, M.J.1    Weibull, C.2    Everitt, E.3
  • 69
    • 0028142765 scopus 로고
    • Protective antibodies inhibt reovirus internalization and uncoating by intracellular proteases
    • Virgin H. W., Mann M. A., Tyler K. L. Protective antibodies inhibt reovirus internalization and uncoating by intracellular proteases. J. Virol. 68:1994;6719-6729.
    • (1994) J. Virol. , vol.68 , pp. 6719-6729
    • Virgin, H.W.1    Mann, M.A.2    Tyler, K.L.3
  • 70
  • 71
    • 0027431751 scopus 로고
    • The canine parvovirus empty capsid structure
    • Wu H., Rossmann M. G. The canine parvovirus empty capsid structure. J. Mol. Biol. 233:1993;231-244.
    • (1993) J. Mol. Biol. , vol.233 , pp. 231-244
    • Wu, H.1    Rossmann, M.G.2
  • 72
    • 0030573015 scopus 로고    scopus 로고
    • Canine parvovirus capsid structure, analyzed at 2.9 Å resolution
    • Xie Q., Chapman M. S. Canine parvovirus capsid structure, analyzed at 2.9 Å resolution. J. Mol. Biol. 264:1996;497-520.
    • (1996) J. Mol. Biol. , vol.264 , pp. 497-520
    • Xie, Q.1    Chapman, M.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.