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Volumn 77, Issue 10, 2003, Pages 5547-5556

Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GAG PROTEIN; GENOMIC RNA; PROTEINASE; PROTEINASE INHIBITOR; VIRUS PROTEIN;

EID: 0038710633     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.10.5547-5556.2003     Document Type: Article
Times cited : (49)

References (78)
  • 1
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
    • Accola, M. A., B. Strack, and H. G. Gottlinger. 2000. Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain. J. Virol. 74:5395-5402.
    • (2000) J. Virol. , vol.74 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 3
    • 0029097067 scopus 로고
    • Potent inhibition of human immunodeficiency virus type 1 (HIV-1) replication by inducible expression of HIV-1 PR multimers
    • Arrigo, S. J., and K. Huffman. 1995. Potent inhibition of human immunodeficiency virus type 1 (HIV-1) replication by inducible expression of HIV-1 PR multimers. J. Virol. 69:5988-5994.
    • (1995) J. Virol. , vol.69 , pp. 5988-5994
    • Arrigo, S.J.1    Huffman, K.2
  • 4
    • 0027501033 scopus 로고
    • Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteins
    • Bennett, R. P., T. D. Nelle, and J. W. Wills. 1993. Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteins. J. Virol. 67:6487-6498.
    • (1993) J. Virol. , vol.67 , pp. 6487-6498
    • Bennett, R.P.1    Nelle, T.D.2    Wills, J.W.3
  • 5
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg, J. M., and Y. Shi. 1996. The galvanization of biology: a growing appreciation for the roles of zinc. Science 271:1081-1085.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 7
    • 0031592573 scopus 로고    scopus 로고
    • Microvesicles are a source of contaminating cellular proteins found in purified HIV-1 preparations
    • Bess, J. W., Jr., R. J. Gorelick, W. J. Bosche, L. E. Henderson, and L. O. Arthur. 1997. Microvesicles are a source of contaminating cellular proteins found in purified HIV-1 preparations. Virology 230:134-144.
    • (1997) Virology , vol.230 , pp. 134-144
    • Bess J.W., Jr.1    Gorelick, R.J.2    Bosche, W.J.3    Henderson, L.E.4    Arthur, L.O.5
  • 8
    • 0027971069 scopus 로고
    • Site-directed mutagenesis of the P2 region of the Rous sarcoma virus gag gene: Effects on Gag polyprotein processing
    • Bowles, N., D. Bonnet, F. Mulhauser, and P. F. Spahr. 1994. Site-directed mutagenesis of the P2 region of the Rous sarcoma virus gag gene: effects on Gag polyprotein processing. Virology 203:20-28.
    • (1994) Virology , vol.203 , pp. 20-28
    • Bowles, N.1    Bonnet, D.2    Mulhauser, F.3    Spahr, P.F.4
  • 9
    • 0031684590 scopus 로고    scopus 로고
    • Importance of basic residues in the nucleocapsid sequence for retrovirus Gag assembly and complementation rescue
    • Bowzard, J. B., R. P. Bennett, N. K. Krishna, S. M. Ernst, A. Rein, and J. W. Wills. 1998. Importance of basic residues in the nucleocapsid sequence for retrovirus Gag assembly and complementation rescue. J. Virol. 72:9034-9044.
    • (1998) J. Virol. , vol.72 , pp. 9034-9044
    • Bowzard, J.B.1    Bennett, R.P.2    Krishna, N.K.3    Ernst, S.M.4    Rein, A.5    Wills, J.W.6
  • 10
    • 0037223701 scopus 로고    scopus 로고
    • 2+ fingers are required for efficient reverse transcription, initial integration processes, and protection of newly synthesized viral DNA
    • 2+ fingers are required for efficient reverse transcription, initial integration processes, and protection of newly synthesized viral DNA. J. Virol. 77:1469-1480.
    • (2003) J. Virol. , vol.77 , pp. 1469-1480
    • Buckman, J.S.1    Bosche, W.J.2    Gorelick, R.J.3
  • 11
    • 0029815034 scopus 로고    scopus 로고
    • Lack of integrase can markedly affect human immunodeficiency virus type 1 particle production in the presence of an active viral protease
    • Bukovsky, A., and H. Gottlinger. 1996. Lack of integrase can markedly affect human immunodeficiency virus type 1 particle production in the presence of an active viral protease. J. Virol. 70:6820-6825.
    • (1996) J. Virol. , vol.70 , pp. 6820-6825
    • Bukovsky, A.1    Gottlinger, H.2
  • 12
    • 0032874018 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsiddimer interface and the basic region of matrix protein
    • Burniston, M. T., A. Cimarelli, J. Colgan, S. P. Curtis, and J. Luban. 1999. Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsiddimer interface and the basic region of matrix protein. J. Virol. 73:8527-8540.
    • (1999) J. Virol. , vol.73 , pp. 8527-8540
    • Burniston, M.T.1    Cimarelli, A.2    Colgan, J.3    Curtis, S.P.4    Luban, J.5
  • 13
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell, S., and A. Rein. 1999. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J. Virol. 73:2270-2279.
    • (1999) J. Virol. , vol.73 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 14
    • 0030947591 scopus 로고    scopus 로고
    • In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: Identification of the p10 domain as a morphological determinant in the formation of spherical particles
    • Campbell, S., and V. M. Vogt. 1997. In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles. J. Virol. 71:4425-4435.
    • (1997) J. Virol. , vol.71 , pp. 4425-4435
    • Campbell, S.1    Vogt, V.M.2
  • 15
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell, S., and V. M. Vogt. 1995. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J. Virol. 69:6487-6497.
    • (1995) J. Virol. , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 16
    • 0028916064 scopus 로고
    • Sequence requirements for encapsidation of deletion mutants and chimeras of human immunodeficiency virus type 1 Gag precursor into retrovirus-like particles
    • Carriere, C., B. Gay, N. Chazal, N. Morin, and P. Boulanger. 1995. Sequence requirements for encapsidation of deletion mutants and chimeras of human immunodeficiency virus type 1 Gag precursor into retrovirus-like particles. J. Virol. 69:2366-2377.
    • (1995) J. Virol. , vol.69 , pp. 2366-2377
    • Carriere, C.1    Gay, B.2    Chazal, N.3    Morin, N.4    Boulanger, P.5
  • 17
    • 0032776165 scopus 로고    scopus 로고
    • Coupled integration of human immunodeficiency virus type 1 cDNA ends by purified integrase in vitro: Stimulation by the viral nucleocapsid protein
    • Carteau, S., R. J. Gorelick, and F. D. Bushman. 1999. Coupled integration of human immunodeficiency virus type 1 cDNA ends by purified integrase in vitro: stimulation by the viral nucleocapsid protein. J. Virol. 73:6670-6679.
    • (1999) J. Virol. , vol.73 , pp. 6670-6679
    • Carteau, S.1    Gorelick, R.J.2    Bushman, F.D.3
  • 18
    • 0036091692 scopus 로고    scopus 로고
    • Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus
    • Chertova, E., J. W. Bess, Jr., B. J. Crise, R. C. Sowder II, T. M. Schaden, J. M. Hilburn, J. A. Hoxie, R. E. Benveniste, J. D. Lifson, L. E. Henderson, and L. O. Arthur. 2002. Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus. J. Virol. 76:5315-5325.
    • (2002) J. Virol. , vol.76 , pp. 5315-5325
    • Chertova, E.1    Bess J.W., Jr.2    Crise, B.J.3    Sowder R.C. II4    Schaden, T.M.5    Hilburn, J.M.6    Hoxie, J.A.7    Benveniste, R.E.8    Lifson, J.D.9    Henderson, L.E.10    Arthur, L.O.11
  • 19
    • 0033941571 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 virion density is not determined by nucleocapsid basic residues
    • Cimarelli, A., and J. Luban. 2000. Human immunodeficiency virus type 1 virion density is not determined by nucleocapsid basic residues. J. Virol. 74:6734-6740.
    • (2000) J. Virol. , vol.74 , pp. 6734-6740
    • Cimarelli, A.1    Luban, J.2
  • 20
    • 0034011267 scopus 로고    scopus 로고
    • Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA
    • Cimarelli, A., S. Sandin, S. Hoglund, and J. Luban. 2000. Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA. J. Virol. 74:3046-3057.
    • (2000) J. Virol. , vol.74 , pp. 3046-3057
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 21
    • 0032506295 scopus 로고    scopus 로고
    • The role of nucleocapsid of HIV-1 in virus assembly
    • Dawson, L., and X. F. Yu. 1998. The role of nucleocapsid of HIV-1 in virus assembly. Virology 251:141-157.
    • (1998) Virology , vol.251 , pp. 141-157
    • Dawson, L.1    Yu, X.F.2
  • 22
    • 0026762403 scopus 로고
    • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    • Ehrlich, L., B. Agresta, and C. Carter. 1992. Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro. J. Virol. 66: 4874-4883.
    • (1992) J. Virol. , vol.66 , pp. 4874-4883
    • Ehrlich, L.1    Agresta, B.2    Carter, C.3
  • 23
    • 0028363103 scopus 로고
    • Specificity and sequence requirements for interactions between various retroviral Gag proteins
    • Franke, E. K., H. E. Yuan, K. L. Bossolt, S. P. Goff, and J. Luban. 1994. Specificity and sequence requirements for interactions between various retroviral Gag proteins. J. Virol. 68:5300-5305.
    • (1994) J. Virol. , vol.68 , pp. 5300-5305
    • Franke, E.K.1    Yuan, H.E.2    Bossolt, K.L.3    Goff, S.P.4    Luban, J.5
  • 24
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: Diverse functions in the virus life cycle
    • Freed, E. O. 1998. HIV-1 gag proteins: diverse functions in the virus life cycle. Virology 251:1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 25
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed, E. O. 2002. Viral late domains. J. Virol. 76:4679-4687.
    • (2002) J. Virol. , vol.76 , pp. 4679-4687
    • Freed, E.O.1
  • 26
    • 0031614235 scopus 로고    scopus 로고
    • Recent advances and remaining problems in HIV assembly
    • Garnier, L., J. B. Bowzard, and J. W. Wills. 1998. Recent advances and remaining problems in HIV assembly. AIDS 12:S5-S16.
    • (1998) AIDS , vol.12
    • Garnier, L.1    Bowzard, J.B.2    Wills, J.W.3
  • 27
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells
    • Gheysen, D., E. Jacobs, F. de Foresta, C. Thiriart, M. Francotte, D. Thines, and M. De Wilde. 1989. Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells. Cell 59:103-112.
    • (1989) Cell , vol.59 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    De Foresta, F.3    Thiriart, C.4    Francotte, M.5    Thines, D.6    De Wilde, M.7
  • 28
    • 0017289168 scopus 로고
    • Ultrastructural studies of surface features of human normal and tumor cells in tissue culture by scanning and transmission electron microscopy
    • Gonda, M. A., S. A. Aaronson, N. Ellmore, V. H. Zeve, and K. Nagashima. 1976. Ultrastructural studies of surface features of human normal and tumor cells in tissue culture by scanning and transmission electron microscopy. J. Natl. Cancer Inst. 56:245-263.
    • (1976) J. Natl. Cancer Inst. , vol.56 , pp. 245-263
    • Gonda, M.A.1    Aaronson, S.A.2    Ellmore, N.3    Zeve, V.H.4    Nagashima, K.5
  • 30
    • 0029986494 scopus 로고    scopus 로고
    • Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid: Replacement of zinc-binding residues with other zinc-binding residues yields noninfectious particles containing genomic RNA
    • Gorelick, R. J., D. J. Chabot, D. E. Ott, T. D. Gagliardi, A. Rein, L. E. Henderson, and L. O. Arthur. 1996. Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid: replacement of zinc-binding residues with other zinc-binding residues yields noninfectious particles containing genomic RNA. J. Virol. 70:2593-2597.
    • (1996) J. Virol. , vol.70 , pp. 2593-2597
    • Gorelick, R.J.1    Chabot, D.J.2    Ott, D.E.3    Gagliardi, T.D.4    Rein, A.5    Henderson, L.E.6    Arthur, L.O.7
  • 31
    • 0033616530 scopus 로고    scopus 로고
    • Strict conservation of the retroviral nucleocapsid protein zinc finger is strongly influenced by its role in viral infection processes: Characterization of HIV-1 particles containing mutant nucleocapsid zinc-coordinating sequences
    • Gorelick, R. J., T. D. Gagliardi, W. J. Bosche, T. A. Wiltrout, L. V. Coren, D. J. Chabot, J. D. Lifson, L. E. Henderson, and L. O. Arthur. 1999. Strict conservation of the retroviral nucleocapsid protein zinc finger is strongly influenced by its role in viral infection processes: characterization of HIV-1 particles containing mutant nucleocapsid zinc-coordinating sequences. Virology 256:92-104.
    • (1999) Virology , vol.256 , pp. 92-104
    • Gorelick, R.J.1    Gagliardi, T.D.2    Bosche, W.J.3    Wiltrout, T.A.4    Coren, L.V.5    Chabot, D.J.6    Lifson, J.D.7    Henderson, L.E.8    Arthur, L.O.9
  • 32
    • 0024110320 scopus 로고
    • Point mutants of Moloney murine leukemia virus that fail to package viral RNA: Evidence for specific RNA recognition by a "zinc finger-like" protein sequence
    • Gorelick, R. J., L. E. Henderson, J. P. Hanser, and A. Rein. 1988. Point mutants of Moloney murine leukemia virus that fail to package viral RNA: evidence for specific RNA recognition by a "zinc finger-like" protein sequence. Proc. Natl. Acad. Sci. USA 85:8420-8424.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8420-8424
    • Gorelick, R.J.1    Henderson, L.E.2    Hanser, J.P.3    Rein, A.4
  • 33
    • 0025283822 scopus 로고
    • Noninfectious human immunodeficiency virus type 1 mutants deficient in genomic RNA
    • Gorelick, R. J., S. M. Nigida, J. W. Bess, Jr., L. E. Henderson, L. O. Arthur, and A. Rein. 1990. Noninfectious human immunodeficiency virus type 1 mutants deficient in genomic RNA. J. Virol. 64:3207-3211.
    • (1990) J. Virol. , vol.64 , pp. 3207-3211
    • Gorelick, R.J.1    Nigida, S.M.2    Bess J.W., Jr.3    Henderson, L.E.4    Arthur, L.O.5    Rein, A.6
  • 34
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Gottlinger, H. G., J. G. Sodroski, and W. A. Haseltine. 1989. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 86:5781-5785.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 35
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham, F. L., and A. J. van der Eb. 1973. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52:456-467.
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van der Eb, A.J.2
  • 36
    • 0031954466 scopus 로고    scopus 로고
    • Nterminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
    • Gross, I., H. Hohenberg, C. Huckhagel, and H. G. Krausslich. 1998. Nterminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J. Virol. 72:4798-4810.
    • (1998) J. Virol. , vol.72 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckhagel, C.3    Krausslich, H.G.4
  • 37
    • 0030682425 scopus 로고    scopus 로고
    • In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus
    • Gross, I., H. Hohenberg, and H. G. Krausslich. 1997. In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus. Eur. J. Biochem. 249:592-600.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 592-600
    • Gross, I.1    Hohenberg, H.2    Krausslich, H.G.3
  • 38
    • 0033803461 scopus 로고    scopus 로고
    • Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer
    • Guo, J., T. Wu, J. Anderson, B. F. Kane, D. G. Johnson, R. J. Gorelick, L. E. Henderson, and J. G. Levin. 2000. Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer. J. Virol. 74:8980-8988.
    • (2000) J. Virol. , vol.74 , pp. 8980-8988
    • Guo, J.1    Wu, T.2    Anderson, J.3    Kane, B.F.4    Johnson, D.G.5    Gorelick, R.J.6    Henderson, L.E.7    Levin, J.G.8
  • 39
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: Tailor-made genes using polymerase chain reaction
    • Horton, R. M., Z. Cai, S. N. Ho, and L. R. Pease. 1990. Gene splicing by overlap extension: tailor-made genes using polymerase chain reaction. Bio-Techniques 8:528-535.
    • (1990) Bio-Techniques , vol.8 , pp. 528-535
    • Horton, R.M.1    Cai, Z.2    Ho, S.N.3    Pease, L.R.4
  • 40
    • 0028971135 scopus 로고
    • Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69:6810-6818.
    • (1995) J. Virol. , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 41
    • 0036827828 scopus 로고    scopus 로고
    • Nucleic acid-independent retrovirus assembly can be driven by dimerization
    • Johnson, M. C., H. M. Scobie, Y. M. Ma, and V. M. Vogt. 2002. Nucleic acid-independent retrovirus assembly can be driven by dimerization. J. Virol. 76:11177-11185.
    • (2002) J. Virol. , vol.76 , pp. 11177-11185
    • Johnson, M.C.1    Scobie, H.M.2    Ma, Y.M.3    Vogt, V.M.4
  • 42
    • 0027101766 scopus 로고
    • Distinct signals in human immunodeficiency virus type 1 Pr55 necessary for RNA binding and particle formation
    • Jowett, J. B., D. J. Hockley, M. V. Nermut, and I. M. Jones. 1992. Distinct signals in human immunodeficiency virus type 1 Pr55 necessary for RNA binding and particle formation. J. Gen. Virol. 73:3079-3086.
    • (1992) J. Gen. Virol. , vol.73 , pp. 3079-3086
    • Jowett, J.B.1    Hockley, D.J.2    Nermut, M.V.3    Jones, I.M.4
  • 43
    • 0027971826 scopus 로고
    • Human immunodeficiency virus type 1 virions composed of unprocessed Gag and Gag-Pol precursors are capable of reverse transcribing viral genomic RNA
    • Kaplan, A. H., P. Krogstad, D. J. Kempf, D. W. Norbeck, and R. Swanstrom. 1994. Human immunodeficiency virus type 1 virions composed of unprocessed Gag and Gag-Pol precursors are capable of reverse transcribing viral genomic RNA. Antimicrob. Agents Chemother. 38:2929-2933.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2929-2933
    • Kaplan, A.H.1    Krogstad, P.2    Kempf, D.J.3    Norbeck, D.W.4    Swanstrom, R.5
  • 44
    • 0027932364 scopus 로고
    • The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency
    • Kaplan, A. H., M. Manchester, and R. Swanstrom. 1994. The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency. J. Virol. 68:6782-6786.
    • (1994) J. Virol. , vol.68 , pp. 6782-6786
    • Kaplan, A.H.1    Manchester, M.2    Swanstrom, R.3
  • 45
    • 0025828543 scopus 로고
    • HIV-1 gag proteins are processed in two cellular compartments
    • Kaplan, A. H., and R. Swanstrom. 1991. HIV-1 gag proteins are processed in two cellular compartments. Proc. Natl. Acad. Sci. USA 88:4528-4532.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4528-4532
    • Kaplan, A.H.1    Swanstrom, R.2
  • 46
    • 0027214941 scopus 로고
    • Overexpression of the HIV-1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles
    • Karacostas, V., E. J. Wolffe, K. Nagashima, M. A. Gonda, and B. Moss. 1993. Overexpression of the HIV-1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles. Virology 193:661-671.
    • (1993) Virology , vol.193 , pp. 661-671
    • Karacostas, V.1    Wolffe, E.J.2    Nagashima, K.3    Gonda, M.A.4    Moss, B.5
  • 47
    • 0021846499 scopus 로고
    • Murine leukemia virus maturation: Protease region required for conversion from "immature" to "mature" core form and for virus infectivity
    • Katoh, I., Y. Yoshinaka, A. Rein, M. Shibuya, T. Odaka, and S. Oroszlan. 1985. Murine leukemia virus maturation: protease region required for conversion from "immature" to "mature" core form and for virus infectivity. Virology 145:280-292.
    • (1985) Virology , vol.145 , pp. 280-292
    • Katoh, I.1    Yoshinaka, Y.2    Rein, A.3    Shibuya, M.4    Odaka, T.5    Oroszlan, S.6
  • 48
    • 0026322839 scopus 로고
    • Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity
    • Krausslich, H. G. 1991. Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity. Proc. Natl. Acad. Sci. USA 88:3213-3217.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3213-3217
    • Krausslich, H.G.1
  • 49
    • 0028821437 scopus 로고
    • Overexpression of human immunodeficiency virus type 1 protease increases intracellular cleavage of Gag and reduces virus infectivity
    • Luukkonen, B. G., E. M. Fenyo, and S. Schwartz. 1995. Overexpression of human immunodeficiency virus type 1 protease increases intracellular cleavage of Gag and reduces virus infectivity. Virology 206:854-865.
    • (1995) Virology , vol.206 , pp. 854-865
    • Luukkonen, B.G.1    Fenyo, E.M.2    Schwartz, S.3
  • 50
    • 0036091735 scopus 로고    scopus 로고
    • Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly
    • Ma, Y. M., and V. M. Vogt. 2002. Rous sarcoma virus Gag protein-oligonucleotide interaction suggests a critical role for protein dimer formation in assembly. J. Virol. 76:5452-5462.
    • (2002) J. Virol. , vol.76 , pp. 5452-5462
    • Ma, Y.M.1    Vogt, V.M.2
  • 51
    • 9244219568 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 encapsidation site is a multipartite RNA element composed of functional hairpin structures
    • McBride, M. S., and A. T. Panganiban. 1996. The human immunodeficiency virus type 1 encapsidation site is a multipartite RNA element composed of functional hairpin structures. J. Virol. 70:2963-2973.
    • (1996) J. Virol. , vol.70 , pp. 2963-2973
    • McBride, M.S.1    Panganiban, A.T.2
  • 52
    • 0026585458 scopus 로고
    • Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells
    • Mergener, K., M. Facke, R. Welker, V. Brinkmann, H. R. Gelderblom, and H. G. Krausslich. 1992. Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells. Virology 186:25-39.
    • (1992) Virology , vol.186 , pp. 25-39
    • Mergener, K.1    Facke, M.2    Welker, R.3    Brinkmann, V.4    Gelderblom, H.R.5    Krausslich, H.G.6
  • 54
    • 0036828053 scopus 로고    scopus 로고
    • Murine leukemia virus nucleocapsid mutant particles lacking viral RNA encapsidate ribosomes
    • Muriaux, D., J. Mirro, K. Nagashima, D. Harvin, and A. Rein. 2002. Murine leukemia virus nucleocapsid mutant particles lacking viral RNA encapsidate ribosomes. J. Virol. 76:11405-11413.
    • (2002) J. Virol. , vol.76 , pp. 11405-11413
    • Muriaux, D.1    Mirro, J.2    Nagashima, K.3    Harvin, D.4    Rein, A.5
  • 56
    • 0026018243 scopus 로고
    • Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production
    • Park, J., and C. D. Morrow. 1991. Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production. J. Virol. 65:5111-5117.
    • (1991) J. Virol. , vol.65 , pp. 5111-5117
    • Park, J.1    Morrow, C.D.2
  • 57
    • 0029817879 scopus 로고    scopus 로고
    • Charged amino acid residues of human immunodeficiency virus type 1 nucleocapsid p7 protein involved in RNA packaging and infectivity
    • Poon, D. T. K., J. Wu, and A. Aldovini. 1996. Charged amino acid residues of human immunodeficiency virus type 1 nucleocapsid p7 protein involved in RNA packaging and infectivity. J. Virol. 70:6607-6616.
    • (1996) J. Virol. , vol.70 , pp. 6607-6616
    • Poon, D.T.K.1    Wu, J.2    Aldovini, A.3
  • 58
    • 0035003983 scopus 로고    scopus 로고
    • Sequencespecific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection
    • Purohit, P., S. Dupont, M. Stevenson, and M. R. Green. 2001. Sequencespecific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection. RNA 7:576-584.
    • (2001) RNA , vol.7 , pp. 576-584
    • Purohit, P.1    Dupont, S.2    Stevenson, M.3    Green, M.R.4
  • 60
    • 0031679786 scopus 로고    scopus 로고
    • Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: Significance for viral replication
    • Rein, A., L. E. Henderson, and J. G. Levin. 1998. Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication. Trends Biochem. Sci. 23:297-301.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 297-301
    • Rein, A.1    Henderson, L.E.2    Levin, J.G.3
  • 62
    • 0026043144 scopus 로고
    • Analysis of non-infectious HIV particles produced in presence of HIV proteinase inhibitor
    • Schatzl, H., H. R. Gelderblom, H. Nitschko, and K. von der Helm. 1991. Analysis of non-infectious HIV particles produced in presence of HIV proteinase inhibitor. Arch. Virol. 120:71-81.
    • (1991) Arch. Virol. , vol.120 , pp. 71-81
    • Schatzl, H.1    Gelderblom, H.R.2    Nitschko, H.3    Von der Helm, K.4
  • 64
    • 0030782150 scopus 로고    scopus 로고
    • Distinct functions and requirements for the Cys-His boxes of the human immunodeficiency virus type 1 nucleocapsid protein during RNA encapsidation and replication
    • Schwartz, M. D., D. Fiore, and A. T. Panganiban. 1997. Distinct functions and requirements for the Cys-His boxes of the human immunodeficiency virus type 1 nucleocapsid protein during RNA encapsidation and replication. J. Virol. 71:9295-9305.
    • (1997) J. Virol. , vol.71 , pp. 9295-9305
    • Schwartz, M.D.1    Fiore, D.2    Panganiban, A.T.3
  • 66
    • 0036094492 scopus 로고    scopus 로고
    • Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis
    • Strack, B., A. Calistri, and H. G. Gottlinger. 2002. Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis. J. Virol. 76:5472-5479.
    • (2002) J. Virol. , vol.76 , pp. 5472-5479
    • Strack, B.1    Calistri, A.2    Gottlinger, H.G.3
  • 67
    • 0031907134 scopus 로고    scopus 로고
    • Plasma SIV RNA viral load determination by real-time quantification of product generation in reverse transcriptase-polymerase chain reaction
    • Suryanarayana, K., T. A. Wiltrout, G. M. Vasquez, V. M. Hirsch, and J. D. Lifson. 1998. Plasma SIV RNA viral load determination by real-time quantification of product generation in reverse transcriptase-polymerase chain reaction. AIDS Res. Hum. Retrovir. 14:183-189.
    • (1998) AIDS Res. Hum. Retrovir. , vol.14 , pp. 183-189
    • Suryanarayana, K.1    Wiltrout, T.A.2    Vasquez, G.M.3    Hirsch, V.M.4    Lifson, J.D.5
  • 68
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • J. Coffin, S. Hughes, and H. Varmus (ed.). Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Swanstrom, R., and J. Wills 1997. Synthesis, assembly, and processing of viral proteins, p. 263-334. In J. Coffin, S. Hughes, and H. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.2
  • 69
    • 0003151659 scopus 로고    scopus 로고
    • Retroviral virions and genomes
    • J. Coffin, S. Hughes, and H. Varmus (ed.). Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Vogt, V. 1997. Retroviral virions and genomes, p. 27-70. In J. Coffin, S. Hughes, and H. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1997) Retroviruses , pp. 27-70
    • Vogt, V.1
  • 70
    • 0036315329 scopus 로고    scopus 로고
    • Analysis of bovine leukemia virus gag membrane targeting and late domain function
    • Wang, H., K. M. Norris, and L. M. Mansky. 2002. Analysis of bovine leukemia virus gag membrane targeting and late domain function. J. Virol. 76:8485-8493.
    • (2002) J. Virol. , vol.76 , pp. 8485-8493
    • Wang, H.1    Norris, K.M.2    Mansky, L.M.3
  • 71
    • 0036889123 scopus 로고    scopus 로고
    • RNA incorporation is critical for retroviral particle integrity after cell membrane assembly of Gag complexes
    • Wang, S. W., and A. Aldovini. 2002. RNA incorporation is critical for retroviral particle integrity after cell membrane assembly of Gag complexes. J. Virol. 76:11853-11865.
    • (2002) J. Virol. , vol.76 , pp. 11853-11865
    • Wang, S.W.1    Aldovini, A.2
  • 72
    • 0033958427 scopus 로고    scopus 로고
    • Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1
    • Welker, R., H. Hohenberg, U. Tessmer, C. Huckhagel, and H. G. Krausslich. 2000. Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1. J. Virol. 74:1168-1177.
    • (2000) J. Virol. , vol.74 , pp. 1168-1177
    • Welker, R.1    Hohenberg, H.2    Tessmer, U.3    Huckhagel, C.4    Krausslich, H.G.5
  • 73
    • 0037538069 scopus 로고
    • An assembly domain of the Rous sarcoma virus Gag protein required late in budding
    • Wills, J. W., C. E. Cameron, C. B. Wilson, Y. Xaing, R. P. Bennett, and J. Leis. 1994. An assembly domain of the Rous sarcoma virus Gag protein required late in budding. J. Virol. 63:4331-4343.
    • (1994) J. Virol. , vol.63 , pp. 4331-4343
    • Wills, J.W.1    Cameron, C.E.2    Wilson, C.B.3    Xaing, Y.4    Bennett, R.P.5    Leis, J.6
  • 74
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral Gag proteins
    • Wills, J. W., and R. C. Craven. 1991. Form, function, and use of retroviral Gag proteins. AIDS 5:639-654.
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 75
    • 0029793362 scopus 로고    scopus 로고
    • The zinc finger of nucleocapsid protein of Friend murine leukemia virus is critical for proviral DNA synthesis in vivo
    • Yu, Q., and J.-L. Darlix. 1996. The zinc finger of nucleocapsid protein of Friend murine leukemia virus is critical for proviral DNA synthesis in vivo. J. Virol. 70:5791-5798.
    • (1996) J. Virol. , vol.70 , pp. 5791-5798
    • Yu, Q.1    Darlix, J.-L.2
  • 76
    • 0036063661 scopus 로고    scopus 로고
    • Identification of a minimal HIV-1 gag domain sufficient for self-association
    • Zabransky, A., E. Hunter, and M. Sakalian. 2002. Identification of a minimal HIV-1 gag domain sufficient for self-association. Virology 294:141-150.
    • (2002) Virology , vol.294 , pp. 141-150
    • Zabransky, A.1    Hunter, E.2    Sakalian, M.3
  • 77
    • 0030795040 scopus 로고    scopus 로고
    • Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation
    • Zhang, Y., and E. Barklis 1997. Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation. J. Virol. 71:6765-6776.
    • (1997) J. Virol. , vol.71 , pp. 6765-6776
    • Zhang, Y.1    Barklis, E.2
  • 78
    • 0031910808 scopus 로고    scopus 로고
    • Analysis of the assembly function of the human immunodeficiency virus type 1 Gag protein nucleocapsid domain
    • Zhang, Y., H. Qian, Z. Love, and E. Barklis. 1998. Analysis of the assembly function of the human immunodeficiency virus type 1 Gag protein nucleocapsid domain. J. Virol. 72:1782-1789.
    • (1998) J. Virol. , vol.72 , pp. 1782-1789
    • Zhang, Y.1    Qian, H.2    Love, Z.3    Barklis, E.4


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