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Volumn 375, Issue 2, 2008, Pages 539-549

Functional complementation of nucleocapsid and late domain PTAP mutants of human immunodeficiency virus type 1 during replication

Author keywords

Complementation; HIV; Nucleocapsid; PTAP late domain; Replication

Indexed keywords

GAG PROTEIN; NUCLEOCAPSID PROTEIN; VIRUS DNA; VIRUS RNA;

EID: 43249116792     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2008.02.026     Document Type: Article
Times cited : (5)

References (84)
  • 1
    • 0033013964 scopus 로고    scopus 로고
    • Conditions for copackaging Rous sarcoma virus and murine leukemia virus Gag proteins during retroviral budding
    • Bennett R.P., and Wills J.W. Conditions for copackaging Rous sarcoma virus and murine leukemia virus Gag proteins during retroviral budding. J. Virol. 73 3 (1999) 2045-2051
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 2045-2051
    • Bennett, R.P.1    Wills, J.W.2
  • 2
    • 0026013779 scopus 로고
    • Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly
    • Bennett R.P., Rhee S., Craven R.C., Hunter E., and Wills J.W. Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly. J. Virol. 65 1 (1991) 272-280
    • (1991) J. Virol. , vol.65 , Issue.1 , pp. 272-280
    • Bennett, R.P.1    Rhee, S.2    Craven, R.C.3    Hunter, E.4    Wills, J.W.5
  • 3
    • 0027501033 scopus 로고
    • Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteins
    • Bennett R.P., Nelle T.D., and Wills J.W. Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteins. J. Virol. 67 11 (1993) 6487-6498
    • (1993) J. Virol. , vol.67 , Issue.11 , pp. 6487-6498
    • Bennett, R.P.1    Nelle, T.D.2    Wills, J.W.3
  • 4
    • 0022695021 scopus 로고
    • Potential metal-binding domains in nucleic acid binding proteins
    • Berg J.M. Potential metal-binding domains in nucleic acid binding proteins. Science 232 4749 (1986) 485-487
    • (1986) Science , vol.232 , Issue.4749 , pp. 485-487
    • Berg, J.M.1
  • 5
    • 0029134623 scopus 로고
    • Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric Gag polyproteins during RNA packaging in vivo
    • Berkowitz R.D., Ohagen A., Hoglund S., and Goff S.P. Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric Gag polyproteins during RNA packaging in vivo. J. Virol. 69 10 (1995) 6445-6456
    • (1995) J. Virol. , vol.69 , Issue.10 , pp. 6445-6456
    • Berkowitz, R.D.1    Ohagen, A.2    Hoglund, S.3    Goff, S.P.4
  • 7
    • 0027458653 scopus 로고
    • Effect of rearrangements and duplications of the Cys-His motifs of Rous sarcoma virus nucleocapsid protein
    • Bowles N.E., Damay P., and Spahr P.F. Effect of rearrangements and duplications of the Cys-His motifs of Rous sarcoma virus nucleocapsid protein. J. Virol. 67 2 (1993) 623-631
    • (1993) J. Virol. , vol.67 , Issue.2 , pp. 623-631
    • Bowles, N.E.1    Damay, P.2    Spahr, P.F.3
  • 8
    • 0031684590 scopus 로고    scopus 로고
    • Importance of basic residues in the nucleocapsid sequence for retrovirus Gag assembly and complementation rescue
    • Bowzard J.B., Bennett R.P., Krishna N.K., Ernst S.M., Rein A., and Wills J.W. Importance of basic residues in the nucleocapsid sequence for retrovirus Gag assembly and complementation rescue. J. Virol. 72 11 (1998) 9034-9044
    • (1998) J. Virol. , vol.72 , Issue.11 , 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
  • 9
  • 10
    • 0036202384 scopus 로고    scopus 로고
    • Structural and functional properties of the HIV-1 RNA-tRNA(Lys)3 primer complex annealed by the nucleocapsid protein: comparison with the heat-annealed complex
    • Brule F., Marquet R., Rong L., Wainberg M.A., Roques B.P., Le Grice S.F., Ehresmann B., and Ehresmann C. Structural and functional properties of the HIV-1 RNA-tRNA(Lys)3 primer complex annealed by the nucleocapsid protein: comparison with the heat-annealed complex. Rna 8 1 (2002) 8-15
    • (2002) Rna , vol.8 , Issue.1 , pp. 8-15
    • Brule, F.1    Marquet, R.2    Rong, L.3    Wainberg, M.A.4    Roques, B.P.5    Le Grice, S.F.6    Ehresmann, B.7    Ehresmann, C.8
  • 11
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M., and Ratner L. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl. Acad. Sci. U. S. A. 87 2 (1990) 523-527
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , Issue.2 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 12
    • 0037223701 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid Zn(2+) fingers are required for efficient reverse transcription, initial integration processes, and protection of newly synthesized viral DNA
    • Buckman J.S., Bosche W.J., and Gorelick R.J. Human immunodeficiency virus type 1 nucleocapsid Zn(2+) fingers are required for efficient reverse transcription, initial integration processes, and protection of newly synthesized viral DNA. J. Virol. 77 2 (2003) 1469-1480
    • (2003) J. Virol. , vol.77 , Issue.2 , pp. 1469-1480
    • Buckman, J.S.1    Bosche, W.J.2    Gorelick, R.J.3
  • 13
    • 0035025888 scopus 로고    scopus 로고
    • A quantitative assay for HIV DNA integration in vivo
    • Butler S.L., Hansen M.S., and Bushman F.D. A quantitative assay for HIV DNA integration in vivo. Nat. Med. 7 5 (2001) 631-634
    • (2001) Nat. Med. , vol.7 , Issue.5 , pp. 631-634
    • Butler, S.L.1    Hansen, M.S.2    Bushman, F.D.3
  • 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 he formation of spherical particles
    • Campbell S., and Vogt V.M. In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in he formation of spherical particles. J. Virol. 71 6 (1997) 4425-4435
    • (1997) J. Virol. , vol.71 , Issue.6 , pp. 4425-4435
    • Campbell, S.1    Vogt, V.M.2
  • 15
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell S., and Rein A. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J. Virol. 73 3 (1999) 2270-2279
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 16
    • 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., Gorelick R.J., and Bushman F.D. Coupled integration of human immunodeficiency virus type 1 cDNA ends by purified integrase in vitro: stimulation by the viral nucleocapsid protein. J. Virol. 73 8 (1999) 6670-6679
    • (1999) J. Virol. , vol.73 , Issue.8 , pp. 6670-6679
    • Carteau, S.1    Gorelick, R.J.2    Bushman, F.D.3
  • 17
    • 0033761894 scopus 로고    scopus 로고
    • Roles of Pr55(gag) and NCp7 in tRNA(3) (Lys) genomic placement and the initiation step of reverse transcription in human immunodeficiency virus type 1
    • Cen S., Khorchid A., Gabor J., Rong L., Wainberg M.A., and Kleiman L. Roles of Pr55(gag) and NCp7 in tRNA(3) (Lys) genomic placement and the initiation step of reverse transcription in human immunodeficiency virus type 1. J. Virol. 74 22 (2000) 10796-10800
    • (2000) J. Virol. , vol.74 , Issue.22 , pp. 10796-10800
    • Cen, S.1    Khorchid, A.2    Gabor, J.3    Rong, L.4    Wainberg, M.A.5    Kleiman, L.6
  • 18
    • 0032826503 scopus 로고    scopus 로고
    • The nucleocapsid domain is responsible for the ability of spleen necrosis virus (SNV) Gag polyprotein to package both SNV and murine leukemia virus RNA
    • Certo J.L., Kabdulov T.O., Paulson M.L., Anderson J.A., and Hu W.S. The nucleocapsid domain is responsible for the ability of spleen necrosis virus (SNV) Gag polyprotein to package both SNV and murine leukemia virus RNA. J. Virol. 73 11 (1999) 9170-9177
    • (1999) J. Virol. , vol.73 , Issue.11 , pp. 9170-9177
    • Certo, J.L.1    Kabdulov, T.O.2    Paulson, M.L.3    Anderson, J.A.4    Hu, W.S.5
  • 19
    • 28844506638 scopus 로고    scopus 로고
    • Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding
    • Chen C., Vincent O., Jin J., Weisz O.A., and Montelaro R.C. Functions of early (AP-2) and late (AIP1/ALIX) endocytic proteins in equine infectious anemia virus budding. J. Biol. Chem. 280 49 (2005) 40474-40480
    • (2005) J. Biol. Chem. , vol.280 , Issue.49 , pp. 40474-40480
    • Chen, C.1    Vincent, O.2    Jin, J.3    Weisz, O.A.4    Montelaro, R.C.5
  • 20
    • 23844524271 scopus 로고    scopus 로고
    • Highly sensitive SIV plasma viral load assay: practical considerations, realistic performance expectations, and application to reverse engineering of vaccines for AIDS
    • Cline A.N., Bess J.W., Piatak Jr. M., and Lifson J.D. Highly sensitive SIV plasma viral load assay: practical considerations, realistic performance expectations, and application to reverse engineering of vaccines for AIDS. J. Med. Primatol. 34 5-6 (2005) 303-312
    • (2005) J. Med. Primatol. , vol.34 , Issue.5-6 , pp. 303-312
    • Cline, A.N.1    Bess, J.W.2    Piatak Jr., M.3    Lifson, J.D.4
  • 21
    • 0029015825 scopus 로고
    • Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein
    • Craven R.C., Leure-duPree A.E., Weldon Jr. R.A., and Wills J.W. Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein. J. Virol. 69 7 (1995) 4213-4227
    • (1995) J. Virol. , vol.69 , Issue.7 , pp. 4213-4227
    • Craven, R.C.1    Leure-duPree, A.E.2    Weldon Jr., R.A.3    Wills, J.W.4
  • 22
    • 0037154214 scopus 로고    scopus 로고
    • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function
    • Demirov D.G., Ono A., Orenstein J.M., and Freed E.O. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc. Natl. Acad. Sci. U. S. A. 99 2 (2002) 955-960
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.2 , pp. 955-960
    • Demirov, D.G.1    Ono, A.2    Orenstein, J.M.3    Freed, E.O.4
  • 23
    • 0036133283 scopus 로고    scopus 로고
    • The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner
    • Demirov D.G., Orenstein J.M., and Freed E.O. The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner. J. Virol. 76 1 (2002) 105-117
    • (2002) J. Virol. , vol.76 , Issue.1 , pp. 105-117
    • Demirov, D.G.1    Orenstein, J.M.2    Freed, E.O.3
  • 24
    • 0346373724 scopus 로고    scopus 로고
    • A novel fluorescence resonance energy transfer assay demonstrates that the human immunodeficiency virus type 1 Pr55Gag I domain mediates Gag-Gag interactions
    • Derdowski A., Ding L., and Spearman P. A novel fluorescence resonance energy transfer assay demonstrates that the human immunodeficiency virus type 1 Pr55Gag I domain mediates Gag-Gag interactions. J. Virol. 78 3 (2004) 1230-1242
    • (2004) J. Virol. , vol.78 , Issue.3 , pp. 1230-1242
    • Derdowski, A.1    Ding, L.2    Spearman, P.3
  • 25
    • 0033060752 scopus 로고    scopus 로고
    • Proline residues in human immunodeficiency virus type 1 p6(Gag) exert a cell type-dependent effect on viral replication and virion incorporation of Pol proteins
    • Dettenhofer M., and Yu X.F. Proline residues in human immunodeficiency virus type 1 p6(Gag) exert a cell type-dependent effect on viral replication and virion incorporation of Pol proteins. J. Virol. 73 6 (1999) 4696-4704
    • (1999) J. Virol. , vol.73 , Issue.6 , pp. 4696-4704
    • Dettenhofer, M.1    Yu, X.F.2
  • 27
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • DuBridge R.B., Tang P., Hsia H.C., Leong P.M., Miller J.H., and Calos M.P. Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Mol. Cell. Biol. 7 1 (1987) 379-387
    • (1987) Mol. Cell. Biol. , vol.7 , Issue.1 , pp. 379-387
    • DuBridge, R.B.1    Tang, P.2    Hsia, H.C.3    Leong, P.M.4    Miller, J.H.5    Calos, M.P.6
  • 28
    • 33847355934 scopus 로고    scopus 로고
    • Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding
    • Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I., and Hill C.P. Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell 128 5 (2007) 841-852
    • (2007) Cell , vol.128 , Issue.5 , pp. 841-852
    • Fisher, R.D.1    Chung, H.Y.2    Zhai, Q.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 29
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: diverse functions in the virus life cycle
    • Freed E.O. HIV-1 gag proteins: diverse functions in the virus life cycle. Virology 251 1 (1998) 1-15
    • (1998) Virology , vol.251 , Issue.1 , pp. 1-15
    • Freed, E.O.1
  • 30
    • 0029655514 scopus 로고    scopus 로고
    • Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions
    • Freed E.O., and Martin M.A. Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions. J. Virol. 70 1 (1996) 341-351
    • (1996) J. Virol. , vol.70 , Issue.1 , pp. 341-351
    • Freed, E.O.1    Martin, M.A.2
  • 31
    • 0001469617 scopus 로고    scopus 로고
    • "Retroviridae: the retroviruses and their replication."
    • David P.M.H., and Knipes M. (Eds), Lippincott William and Wilkins, Piladelphia, PA, USA II
    • Freed E.O., and Martin M.A. "Retroviridae: the retroviruses and their replication.". In: David P.M.H., and Knipes M. (Eds). Fields Virology. fifth ed. II (2007), Lippincott William and Wilkins, Piladelphia, PA, USA II
    • (2007) Fields Virology. fifth ed. , vol.II
    • Freed, E.O.1    Martin, M.A.2
  • 32
    • 31144437880 scopus 로고    scopus 로고
    • Effects of Gag mutation and processing on retroviral dimeric RNA maturation
    • Fu W., Dang Q., Nagashima K., Freed E.O., Pathak V.K., and Hu W.S. Effects of Gag mutation and processing on retroviral dimeric RNA maturation. J. Virol. 80 3 (2006) 1242-1249
    • (2006) J. Virol. , vol.80 , Issue.3 , pp. 1242-1249
    • Fu, W.1    Dang, Q.2    Nagashima, K.3    Freed, E.O.4    Pathak, V.K.5    Hu, W.S.6
  • 34
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells
    • Gheysen D., Jacobs E., de Foresta F., Thiriart C., Francotte M., Thines D., and De Wilde M. Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells. Cell 59 1 (1989) 103-112
    • (1989) Cell , vol.59 , Issue.1 , 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
  • 35
    • 40449094896 scopus 로고    scopus 로고
    • "Retroviridae: the retroviruses and their replication."
    • David P.M.H., and Knipes M. (Eds), Lippincott William and Wilkins, Piladelphia, PA, USA II
    • Goff S.P. "Retroviridae: the retroviruses and their replication.". In: David P.M.H., and Knipes M. (Eds). Fields Virology. fifth ed. II (2007), Lippincott William and Wilkins, Piladelphia, PA, USA II
    • (2007) Fields Virology. fifth ed. , vol.II
    • Goff, S.P.1
  • 36
    • 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., Henderson L.E., Hanser J.P., and Rein A. 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. U. S. A. 85 22 (1988) 8420-8424
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , Issue.22 , pp. 8420-8424
    • Gorelick, R.J.1    Henderson, L.E.2    Hanser, J.P.3    Rein, A.4
  • 38
    • 0027197020 scopus 로고
    • The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent
    • Gorelick R.J., Chabot D.J., Rein A., Henderson L.E., and Arthur L.O. The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent. J. Virol. 67 7 (1993) 4027-4036
    • (1993) J. Virol. , vol.67 , Issue.7 , pp. 4027-4036
    • Gorelick, R.J.1    Chabot, D.J.2    Rein, A.3    Henderson, L.E.4    Arthur, L.O.5
  • 39
    • 0029986494 scopus 로고    scopus 로고
    • Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid domain: replacement of zinc-coordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA
    • Gorelick R.J., Chabot D.J., Ott D.E., Gagliardi T.D., Rein A., Henderson L.E., and Arthur L.O. Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid domain: replacement of zinc-coordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA. J. Virol. 70 4 (1996) 2593-2597
    • (1996) J. Virol. , vol.70 , Issue.4 , 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
  • 41
    • 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., Gagliardi T.D., Bosche W.J., Wiltrout T.A., Coren L.V., Chabot D.J., Lifson J.D., Henderson L.E., and Arthur L.O. 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 1 (1999) 92-104
    • (1999) Virology , vol.256 , Issue.1 , 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
  • 42
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Gottlinger H.G., Sodroski J.G., and Haseltine W.A. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. U. S. A. 86 15 (1989) 5781-5785
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , Issue.15 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 43
    • 0041732006 scopus 로고    scopus 로고
    • Differing roles of the N- and C-terminal zinc fingers in human immunodeficiency virus nucleocapsid protein-enhanced nucleic acid annealing
    • Heath M.J., Derebail S.S., Gorelick R.J., and DeStefano J.J. Differing roles of the N- and C-terminal zinc fingers in human immunodeficiency virus nucleocapsid protein-enhanced nucleic acid annealing. J. Biol. Chem. 278 33 (2003) 30755-30763
    • (2003) J. Biol. Chem. , vol.278 , Issue.33 , pp. 30755-30763
    • Heath, M.J.1    Derebail, S.S.2    Gorelick, R.J.3    DeStefano, J.J.4
  • 44
    • 35348892063 scopus 로고    scopus 로고
    • The role of WWP1-Gag interaction and Gag ubiquitination in assembly and release of human T-cell leukemia virus type 1
    • Heidecker G., Lloyd P.A., Soheilian F., Nagashima K., and Derse D. The role of WWP1-Gag interaction and Gag ubiquitination in assembly and release of human T-cell leukemia virus type 1. J. Virol. 81 18 (2007) 9769-9777
    • (2007) J. Virol. , vol.81 , Issue.18 , pp. 9769-9777
    • Heidecker, G.1    Lloyd, P.A.2    Soheilian, F.3    Nagashima, K.4    Derse, D.5
  • 45
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly
    • Hill C.P., Worthylake D., Bancroft D.P., Christensen A.M., and Sundquist W.I. Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc. Natl. Acad. Sci. U. S. A. 93 7 (1996) 3099-3104
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , Issue.7 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 46
    • 0028971135 scopus 로고
    • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Huang M., Orenstein J.M., Martin M.A., and Freed E.O. p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69 11 (1995) 6810-6818
    • (1995) J. Virol. , vol.69 , Issue.11 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 47
    • 0029671218 scopus 로고    scopus 로고
    • trans-acting proteins involved in RNA encapsidation and viral assembly in human immunodeficiency virus type 1
    • Kaye J.F., and Lever A.M. trans-acting proteins involved in RNA encapsidation and viral assembly in human immunodeficiency virus type 1. J. Virol. 70 2 (1996) 880-886
    • (1996) J. Virol. , vol.70 , Issue.2 , pp. 880-886
    • Kaye, J.F.1    Lever, A.M.2
  • 48
    • 0031800763 scopus 로고    scopus 로고
    • Nonreciprocal packaging of human immunodeficiency virus type 1 and type 2 RNA: a possible role for the p2 domain of Gag in RNA encapsidation
    • Kaye J.F., and Lever A.M. Nonreciprocal packaging of human immunodeficiency virus type 1 and type 2 RNA: a possible role for the p2 domain of Gag in RNA encapsidation. J. Virol. 72 7 (1998) 5877-5885
    • (1998) J. Virol. , vol.72 , Issue.7 , pp. 5877-5885
    • Kaye, J.F.1    Lever, A.M.2
  • 49
    • 0031547959 scopus 로고    scopus 로고
    • Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability
    • Lapadat-Tapolsky M., Gabus C., Rau M., and Darlix J.L. Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability. J. Mol. Biol. 268 2 (1997) 250-260
    • (1997) J. Mol. Biol. , vol.268 , Issue.2 , pp. 250-260
    • Lapadat-Tapolsky, M.1    Gabus, C.2    Rau, M.3    Darlix, J.L.4
  • 50
    • 0032509267 scopus 로고    scopus 로고
    • Involvement of HIV-I nucleocapsid protein in the recruitment of reverse transcriptase into nucleoprotein complexes formed in vitro
    • Lener D., Tanchou V., Roques B.P., Le Grice S.F., and Darlix J.L. Involvement of HIV-I nucleocapsid protein in the recruitment of reverse transcriptase into nucleoprotein complexes formed in vitro. J. Biol. Chem. 273 50 (1998) 33781-33786
    • (1998) J. Biol. Chem. , vol.273 , Issue.50 , pp. 33781-33786
    • Lener, D.1    Tanchou, V.2    Roques, B.P.3    Le Grice, S.F.4    Darlix, J.L.5
  • 51
    • 23144448275 scopus 로고    scopus 로고
    • Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism
    • Levin J.G., Guo J., Rouzina I., and Musier-Forsyth K. Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism. Prog. Nucleic Acid Res. Mol. Biol. 80 (2005) 217-286
    • (2005) Prog. Nucleic Acid Res. Mol. Biol. , vol.80 , pp. 217-286
    • Levin, J.G.1    Guo, J.2    Rouzina, I.3    Musier-Forsyth, K.4
  • 52
    • 0028800265 scopus 로고
    • A leucine triplet repeat sequence (LXX)4 in p6gag is important for Vpr incorporation into human immunodeficiency virus type 1 particles
    • Lu Y.L., Bennett R.P., Wills J.W., Gorelick R., and Ratner L. A leucine triplet repeat sequence (LXX)4 in p6gag is important for Vpr incorporation into human immunodeficiency virus type 1 particles. J. Virol. 69 11 (1995) 6873-6879
    • (1995) J. Virol. , vol.69 , Issue.11 , pp. 6873-6879
    • Lu, Y.L.1    Bennett, R.P.2    Wills, J.W.3    Gorelick, R.4    Ratner, L.5
  • 53
    • 0028342554 scopus 로고
    • Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
    • Mammano F., Ohagen A., Hoglund S., and Gottlinger H.G. Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis. J. Virol. 68 8 (1994) 4927-4936
    • (1994) J. Virol. , vol.68 , Issue.8 , pp. 4927-4936
    • Mammano, F.1    Ohagen, A.2    Hoglund, S.3    Gottlinger, H.G.4
  • 54
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano J., Zang T., and Bieniasz P.D. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7 12 (2001) 1313-1319
    • (2001) Nat. Med. , vol.7 , Issue.12 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 55
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-I in retroviral budding
    • Martin-Serrano J., Zang T., and Bieniasz P.D. Role of ESCRT-I in retroviral budding. J. Virol. 77 8 (2003) 4794-4804
    • (2003) J. Virol. , vol.77 , Issue.8 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 56
    • 0038447097 scopus 로고    scopus 로고
    • Human cellular nucleic acid-binding protein Zn2+ fingers support replication of human immunodeficiency virus type 1 when they are substituted in the nucleocapsid protein
    • McGrath C.F., Buckman J.S., Gagliardi T.D., Bosche W.J., Coren L.V., and Gorelick R.J. Human cellular nucleic acid-binding protein Zn2+ fingers support replication of human immunodeficiency virus type 1 when they are substituted in the nucleocapsid protein. J. Virol. 77 15 (2003) 8524-8531
    • (2003) J. Virol. , vol.77 , Issue.15 , pp. 8524-8531
    • McGrath, C.F.1    Buckman, J.S.2    Gagliardi, T.D.3    Bosche, W.J.4    Coren, L.V.5    Gorelick, R.J.6
  • 57
    • 0022978019 scopus 로고
    • Rous sarcoma virus nucleic acid-binding protein p12 is necessary for viral 70S RNA dimer formation and packaging
    • Meric C., and Spahr P.F. Rous sarcoma virus nucleic acid-binding protein p12 is necessary for viral 70S RNA dimer formation and packaging. J. Virol. 60 2 (1986) 450-459
    • (1986) J. Virol. , vol.60 , Issue.2 , pp. 450-459
    • Meric, C.1    Spahr, P.F.2
  • 58
    • 0024507854 scopus 로고
    • Characterization of Moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein
    • Meric C., and Goff S.P. Characterization of Moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein. J. Virol. 63 4 (1989) 1558-1568
    • (1989) J. Virol. , vol.63 , Issue.4 , pp. 1558-1568
    • Meric, C.1    Goff, S.P.2
  • 59
    • 0023801716 scopus 로고
    • Mutations in Rous sarcoma virus nucleocapsid protein p12 (NC): deletions of Cys-His boxes
    • Meric C., Gouilloud E., and Spahr P.F. Mutations in Rous sarcoma virus nucleocapsid protein p12 (NC): deletions of Cys-His boxes. J. Virol. 62 9 (1988) 3328-3333
    • (1988) J. Virol. , vol.62 , Issue.9 , pp. 3328-3333
    • Meric, C.1    Gouilloud, E.2    Spahr, P.F.3
  • 60
    • 0034026083 scopus 로고    scopus 로고
    • Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and alpha-helix 2 of the gp41 cytoplasmic tail
    • Murakami T., and Freed E.O. Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and alpha-helix 2 of the gp41 cytoplasmic tail. J. Virol. 74 8 (2000) 3548-3554
    • (2000) J. Virol. , vol.74 , Issue.8 , pp. 3548-3554
    • Murakami, T.1    Freed, E.O.2
  • 62
    • 0032951899 scopus 로고    scopus 로고
    • Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus
    • Ono A., and Freed E.O. Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus. J. Virol. 73 5 (1999) 4136-4144
    • (1999) J. Virol. , vol.73 , Issue.5 , pp. 4136-4144
    • Ono, A.1    Freed, E.O.2
  • 63
    • 0038710633 scopus 로고    scopus 로고
    • Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant
    • Ott D.E., Coren L.V., Chertova E.N., Gagliardi T.D., Nagashima K., Sowder II R.C., Poon D.T., and Gorelick R.J. Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant. J. Virol. 77 10 (2003) 5547-5556
    • (2003) J. Virol. , vol.77 , Issue.10 , pp. 5547-5556
    • Ott, D.E.1    Coren, L.V.2    Chertova, E.N.3    Gagliardi, T.D.4    Nagashima, K.5    Sowder II, R.C.6    Poon, D.T.7    Gorelick, R.J.8
  • 64
    • 0028873674 scopus 로고
    • Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on virion particle assembly, release, and infectivity
    • Reicin A.S., Paik S., Berkowitz R.D., Luban J., Lowy I., and Goff S.P. Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on virion particle assembly, release, and infectivity. J. Virol. 69 2 (1995) 642-650
    • (1995) J. Virol. , vol.69 , Issue.2 , pp. 642-650
    • Reicin, A.S.1    Paik, S.2    Berkowitz, R.D.3    Luban, J.4    Lowy, I.5    Goff, S.P.6
  • 65
    • 0031679786 scopus 로고    scopus 로고
    • Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication
    • Rein A., Henderson L.E., and Levin J.G. Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication. Trends Biochem. Sci. 23 8 (1998) 297-301
    • (1998) Trends Biochem. Sci. , vol.23 , Issue.8 , pp. 297-301
    • Rein, A.1    Henderson, L.E.2    Levin, J.G.3
  • 66
    • 13744254540 scopus 로고    scopus 로고
    • Genetic recombination of human immunodeficiency virus type 1 in one round of viral replication: effects of genetic distance, target cells, accessory genes, and lack of high negative interference in crossover events
    • Rhodes T.D., Nikolaitchik O., Chen J., Powell D., and Hu W.S. Genetic recombination of human immunodeficiency virus type 1 in one round of viral replication: effects of genetic distance, target cells, accessory genes, and lack of high negative interference in crossover events. J. Virol. 79 3 (2005) 1666-1677
    • (2005) J. Virol. , vol.79 , Issue.3 , pp. 1666-1677
    • Rhodes, T.D.1    Nikolaitchik, O.2    Chen, J.3    Powell, D.4    Hu, W.S.5
  • 67
    • 0029009007 scopus 로고
    • Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vitro
    • Rodriguez-Rodriguez L., Tsuchihashi Z., Fuentes G.M., Bambara R.A., and Fay P.J. Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vitro. J. Biol. Chem. 270 25 (1995) 15005-15011
    • (1995) J. Biol. Chem. , vol.270 , Issue.25 , pp. 15005-15011
    • Rodriguez-Rodriguez, L.1    Tsuchihashi, Z.2    Fuentes, G.M.3    Bambara, R.A.4    Fay, P.J.5
  • 68
    • 0035861731 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein and the secondary structure of the binary complex formed between tRNA(Lys.3) and viral RNA template play different roles during initiation of (-) strand DNA reverse transcription
    • Rong L., Liang C., Hsu M., Guo X., Roques B.P., and Wainberg M.A. HIV-1 nucleocapsid protein and the secondary structure of the binary complex formed between tRNA(Lys.3) and viral RNA template play different roles during initiation of (-) strand DNA reverse transcription. J. Biol. Chem. 276 50 (2001) 47725-47732
    • (2001) J. Biol. Chem. , vol.276 , Issue.50 , pp. 47725-47732
    • Rong, L.1    Liang, C.2    Hsu, M.3    Guo, X.4    Roques, B.P.5    Wainberg, M.A.6
  • 70
    • 0031949314 scopus 로고    scopus 로고
    • The I domain is required for efficient plasma membrane binding of human immunodeficiency virus type 1 Pr55Gag
    • Sandefur S., Varthakavi V., and Spearman P. The I domain is required for efficient plasma membrane binding of human immunodeficiency virus type 1 Pr55Gag. J. Virol. 72 4 (1998) 2723-2732
    • (1998) J. Virol. , vol.72 , Issue.4 , pp. 2723-2732
    • Sandefur, S.1    Varthakavi, V.2    Spearman, P.3
  • 71
    • 0033862233 scopus 로고    scopus 로고
    • Mapping and characterization of the N-terminal I domain of human immunodeficiency virus type 1 Pr55(Gag)
    • Sandefur S., Smith R.M., Varthakavi V., and Spearman P. Mapping and characterization of the N-terminal I domain of human immunodeficiency virus type 1 Pr55(Gag). J. Virol. 74 16 (2000) 7238-7249
    • (2000) J. Virol. , vol.74 , Issue.16 , pp. 7238-7249
    • Sandefur, S.1    Smith, R.M.2    Varthakavi, V.3    Spearman, P.4
  • 72
    • 0029130067 scopus 로고
    • Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation
    • Srinivasakumar N., Hammarskjold M.L., and Rekosh D. Characterization of deletion mutations in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation. J. Virol. 69 10 (1995) 6106-6114
    • (1995) J. Virol. , vol.69 , Issue.10 , pp. 6106-6114
    • Srinivasakumar, N.1    Hammarskjold, M.L.2    Rekosh, D.3
  • 73
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B., Calistri A., Craig S., Popova E., and Gottlinger H.G. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114 6 (2003) 689-699
    • (2003) Cell , vol.114 , Issue.6 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 74
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • Coffin J.M., Hughes S.H., and Varmus H.E. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
    • Swanstrom R., and Wills J.W. Synthesis, assembly, and processing of viral proteins. In: Coffin J.M., Hughes S.H., and Varmus H.E. (Eds). Retroviruses (1997), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y 263-334
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 75
    • 33747875746 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid zinc-finger mutations cause defects in reverse transcription and integration
    • Thomas J.A., Gagliardi T.D., Alvord W.G., Lubomirski M., Bosche W.J., and Gorelick R.J. Human immunodeficiency virus type 1 nucleocapsid zinc-finger mutations cause defects in reverse transcription and integration. Virology 353 1 (2006) 41-51
    • (2006) Virology , vol.353 , Issue.1 , pp. 41-51
    • Thomas, J.A.1    Gagliardi, T.D.2    Alvord, W.G.3    Lubomirski, M.4    Bosche, W.J.5    Gorelick, R.J.6
  • 76
    • 0028129970 scopus 로고
    • DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein
    • Tsuchihashi Z., and Brown P.O. DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein. J. Virol. 68 9 (1994) 5863-5870
    • (1994) J. Virol. , vol.68 , Issue.9 , pp. 5863-5870
    • Tsuchihashi, Z.1    Brown, P.O.2
  • 78
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler U.K., Stray K.M., Garrus J.E., and Sundquist W.I. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77 9 (2003) 5439-5450
    • (2003) J. Virol. , vol.77 , Issue.9 , pp. 5439-5450
    • von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 79
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral gag proteins
    • Wills J.W., and Craven R.C. Form, function, and use of retroviral gag proteins. Aids 5 6 (1991) 639-654
    • (1991) Aids , vol.5 , Issue.6 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 80
    • 0036101339 scopus 로고    scopus 로고
    • Functional evaluation of DC-SIGN monoclonal antibodies reveals DC-SIGN interactions with ICAM-3 do not promote human immunodeficiency virus type 1 transmission
    • Wu L., Martin T.D., Vazeux R., Unutmaz D., and KewalRamani V.N. Functional evaluation of DC-SIGN monoclonal antibodies reveals DC-SIGN interactions with ICAM-3 do not promote human immunodeficiency virus type 1 transmission. J. Virol. 76 12 (2002) 5905-5914
    • (2002) J. Virol. , vol.76 , Issue.12 , pp. 5905-5914
    • Wu, L.1    Martin, T.D.2    Vazeux, R.3    Unutmaz, D.4    KewalRamani, V.N.5
  • 81
    • 0034747798 scopus 로고    scopus 로고
    • Alteration of zinc-binding residues of simian immunodeficiency virus p8(NC) results in subtle differences in gag processing and virion maturation associated with degradative loss of mutant NC
    • Yovandich J.L., Chertova E.N., Kane B.P., Gagliardi T.D., Bess Jr. J.W., Sowder II R.C., Henderson L.E., and Gorelick R.J. Alteration of zinc-binding residues of simian immunodeficiency virus p8(NC) results in subtle differences in gag processing and virion maturation associated with degradative loss of mutant NC. J. Virol. 75 1 (2001) 115-124
    • (2001) J. Virol. , vol.75 , Issue.1 , pp. 115-124
    • Yovandich, J.L.1    Chertova, E.N.2    Kane, B.P.3    Gagliardi, T.D.4    Bess Jr., J.W.5    Sowder II, R.C.6    Henderson, L.E.7    Gorelick, R.J.8
  • 82
    • 0031901643 scopus 로고    scopus 로고
    • Mutations of the human immunodeficiency virus type 1 p6Gag domain result in reduced retention of Pol proteins during virus assembly
    • Yu X.F., Dawson L., Tian C.J., Flexner C., and Dettenhofer M. Mutations of the human immunodeficiency virus type 1 p6Gag domain result in reduced retention of Pol proteins during virus assembly. J. Virol. 72 4 (1998) 3412-3417
    • (1998) J. Virol. , vol.72 , Issue.4 , pp. 3412-3417
    • Yu, X.F.1    Dawson, L.2    Tian, C.J.3    Flexner, C.4    Dettenhofer, M.5
  • 83
    • 0029149643 scopus 로고
    • Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation
    • Zhang Y., and Barklis E. Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation. J. Virol. 69 9 (1995) 5716-5722
    • (1995) J. Virol. , vol.69 , Issue.9 , pp. 5716-5722
    • Zhang, Y.1    Barklis, E.2
  • 84
    • 0036314441 scopus 로고    scopus 로고
    • Zinc finger domain of murine leukemia virus nucleocapsid protein enhances the rate of viral DNA synthesis in vivo
    • Zhang W.H., Hwang C.K., Hu W.S., Gorelick R.J., and Pathak V.K. Zinc finger domain of murine leukemia virus nucleocapsid protein enhances the rate of viral DNA synthesis in vivo. J. Virol. 76 15 (2002) 7473-7484
    • (2002) J. Virol. , vol.76 , Issue.15 , pp. 7473-7484
    • Zhang, W.H.1    Hwang, C.K.2    Hu, W.S.3    Gorelick, R.J.4    Pathak, V.K.5


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