메뉴 건너뛰기




Volumn 78, Issue 7, 1996, Pages 639-653

Dimerization of retroviral genomic RNAs: Structural and functional implications

Author keywords

Dimerization; Packaging; Retrovirus; RNA structure

Indexed keywords

VIRUS RNA;

EID: 0029909841     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(96)80010-1     Document Type: Article
Times cited : (118)

References (138)
  • 1
    • 0001002170 scopus 로고
    • Retroviridae and their replication
    • B.N. Fields, Knipe D.M. New York: Raven Press, Ltd
    • Coffin JM. Retroviridae and their replication. Fields BN, Knipe DM. Virology. 1990;1437-1500 Raven Press, Ltd, New York.
    • (1990) Virology , pp. 1437-1500
    • Coffin, J.M.1
  • 2
    • 0015579727 scopus 로고
    • Evidence for 30-40S RNA as precursor of the 60-70 S RNA of Rous sarcoma virus
    • Canaani E, Helm KVD, Duesberg P. Evidence for 30-40S RNA as precursor of the 60-70 S RNA of Rous sarcoma virus. Proc Natl Acad Sci USA. 72:1973;401-405.
    • (1973) Proc Natl Acad Sci USA , vol.72 , pp. 401-405
    • Canaani, E.1    Helm, K.V.D.2    Duesberg, P.3
  • 3
    • 0016269599 scopus 로고
    • Evidence for crossing-over between avian tumor viruses based on analysis of viral RNAs
    • Beemon K, Duesberg P, Vogt P. Evidence for crossing-over between avian tumor viruses based on analysis of viral RNAs. Proc Natl Acad Sci USA. 71:1974;4254-4258.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4254-4258
    • Beemon, K.1    Duesberg, P.2    Vogt, P.3
  • 5
    • 0014964654 scopus 로고
    • Viral RNA-dependent DNA polymerase
    • Baltimore D. Viral RNA-dependent DNA polymerase. Nature. 226:1970;209-211.
    • (1970) Nature , vol.226 , pp. 209-211
    • Baltimore, D.1
  • 6
    • 84966408881 scopus 로고
    • RNA-dependent DNA polymerase in virions of RSV
    • Temin HM, Mizutani S. RNA-dependent DNA polymerase in virions of RSV. Nature. 226:1970;211-213.
    • (1970) Nature , vol.226 , pp. 211-213
    • Temin, H.M.1    Mizutani, S.2
  • 7
    • 0020320936 scopus 로고
    • Form and function of retroviral proviruses
    • Varmus HE. Form and function of retroviral proviruses. Science. 216:1982;812-820.
    • (1982) Science , vol.216 , pp. 812-820
    • Varmus, H.E.1
  • 8
    • 0017078219 scopus 로고
    • Mapping of poly (A) sequences in the electron microscope reveals unusual structure of type C oncornavirus RNA molecules
    • Bender W, Davidson N. Mapping of poly (A) sequences in the electron microscope reveals unusual structure of type C oncornavirus RNA molecules. Cell. 7:1976;595-607.
    • (1976) Cell , vol.7 , pp. 595-607
    • Bender, W.1    Davidson, N.2
  • 10
    • 0019352256 scopus 로고
    • Secondary structural features in the 70 S RNAs of Moloney murine leukemia and Rous sarcoma viruses as observed by electron microscopy
    • Murti KG, Bondurant M, Tereba A. Secondary structural features in the 70 S RNAs of Moloney murine leukemia and Rous sarcoma viruses as observed by electron microscopy. J Virol. 37:1981;411-419.
    • (1981) J Virol , vol.37 , pp. 411-419
    • Murti, K.G.1    Bondurant, M.2    Tereba, A.3
  • 11
    • 0026096904 scopus 로고
    • Human immunodeficiency virus as a prototypic complex retrovirus
    • Cullen BR. Human immunodeficiency virus as a prototypic complex retrovirus. J Virol. 65:1991;1053-1056.
    • (1991) J Virol , vol.65 , pp. 1053-1056
    • Cullen, B.R.1
  • 12
    • 2642650984 scopus 로고
    • Structure and molecular weight of the 60-70S RNA and the 30-40S RNA of Rous sarcoma virus
    • Mangel WF, Delius H, Duesberg PH. Structure and molecular weight of the 60-70S RNA and the 30-40S RNA of Rous sarcoma virus. Proc Natl Acad Sci USA. 71:1974;4541-4545.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4541-4545
    • Mangel, W.F.1    Delius, H.2    Duesberg, P.H.3
  • 14
  • 15
    • 0018178279 scopus 로고
    • High-molecular weight RNAs of AKR, NZB and wild mouse viruses and avian reticuloendotheliosis virus all have similar dimer structures
    • Bender W, Chien YH, Chattopadkyay S, Vogt PK, Gardner MB, Davidson N. High-molecular weight RNAs of AKR, NZB and wild mouse viruses and avian reticuloendotheliosis virus all have similar dimer structures. J Virol. 25:1978;888-896.
    • (1978) J Virol , vol.25 , pp. 888-896
    • Bender, W.1    Chien, Y.H.2    Chattopadkyay, S.3    Vogt, P.K.4    Gardner, M.B.5    Davidson, N.6
  • 16
  • 17
    • 0016695830 scopus 로고
    • Structure of B77 sarcoma virus RNA: Stabilization of RNA after packaging
    • Stoltzfus CM, Snyder PN. Structure of B77 sarcoma virus RNA: stabilization of RNA after packaging. J Virol. 16:1975;1161-1170.
    • (1975) J Virol , vol.16 , pp. 1161-1170
    • Stoltzfus, C.M.1    Snyder, P.N.2
  • 18
    • 0025598002 scopus 로고
    • Cis-elements and trans-acting factors involved in the RNA dimerization of HIV-1
    • Darlix J-L, Gabus C, Nugeyre MT, Clavel F, Barré-Sinoussi F. Cis-elements and trans-acting factors involved in the RNA dimerization of HIV-1. J Mol Biol. 216:1990;689-699.
    • (1990) J Mol Biol , vol.216 , pp. 689-699
    • Darlix J-L1    Gabus, C.2    Nugeyre, M.T.3    Clavel, F.4    Barré-Sinoussi, F.5
  • 19
    • 0025266663 scopus 로고
    • Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus
    • Aldovini A, Young RA. Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus. J Virol. 64:1990;1920-1926.
    • (1990) J Virol , vol.64 , pp. 1920-1926
    • Aldovini, A.1    Young, R.A.2
  • 20
    • 0025043509 scopus 로고
    • A mutant of HIV-1 with reduced RNA packaging and abnormal particle morphology
    • Clavel F, Orenstein JM. A mutant of HIV-1 with reduced RNA packaging and abnormal particle morphology. J Virol. 64:1990;5230-5234.
    • (1990) J Virol , vol.64 , pp. 5230-5234
    • Clavel, F.1    Orenstein, J.M.2
  • 21
    • 0024320772 scopus 로고
    • Identification of a sequence required for efficient packaging of HIV-1 RNA into virions
    • Lever A, Gottlinger H, Haseltine W, Sodroski J. Identification of a sequence required for efficient packaging of HIV-1 RNA into virions. J Virol. 63:1989;4085-4087.
    • (1989) J Virol , vol.63 , pp. 4085-4087
    • Lever, A.1    Gottlinger, H.2    Haseltine, W.3    Sodroski, J.4
  • 23
    • 0028333978 scopus 로고
    • Dimerization of human immunodeficiency virus type 1 RNA involves sequences located upstream of the splice donor site
    • Marquet R, Paillart J-C, Skripkin E, Ehresmann C, Ehresmann B. Dimerization of human immunodeficiency virus type 1 RNA involves sequences located upstream of the splice donor site. Nucleic Acids Res. 22:1994;145-151.
    • (1994) Nucleic Acids Res , vol.22 , pp. 145-151
    • Marquet, R.1    Paillart J-C2    Skripkin, E.3    Ehresmann, C.4    Ehresmann, B.5
  • 24
    • 0028239204 scopus 로고
    • Identification of the primary site of human immunodeficiency virus type 1 RNA dimerization in vitro
    • Skripkin E, Paillart JC, Marquet R, Ehresmann B, Ehresmann C. Identification of the primary site of human immunodeficiency virus type 1 RNA dimerization in vitro. Proc Natl Acad Sci USA. 91:1994;4945-4949.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4945-4949
    • Skripkin, E.1    Paillart, J.C.2    Marquet, R.3    Ehresmann, B.4    Ehresmann, C.5
  • 25
    • 0027996464 scopus 로고
    • Mutational analysis of the bipartite dimer linkage structure of HIV-1 genomic RNA
    • Paillart JC, Marquet R, Skripkin E, Ehresmann B, Ehresmann C. Mutational analysis of the bipartite dimer linkage structure of HIV-1 genomic RNA. J Biol Chem. 269:1994;27486-27493.
    • (1994) J Biol Chem , vol.269 , pp. 27486-27493
    • Paillart, J.C.1    Marquet, R.2    Skripkin, E.3    Ehresmann, B.4    Ehresmann, C.5
  • 26
    • 0026647836 scopus 로고
    • The human immunodeficiency virus type-1 packaging signal and major splice donor region have a conserved stable secondary structure
    • Harrison GP, Lever AML. The human immunodeficiency virus type-1 packaging signal and major splice donor region have a conserved stable secondary structure. J Virol. 66:1992;4144-4153.
    • (1992) J Virol , vol.66 , pp. 4144-4153
    • Harrison, G.P.1    Lever, A.M.L.2
  • 27
    • 0028027708 scopus 로고
    • A 19-nucleotide sequence upstream of the 5′ major splice donor site is part of the dimerization domain of human immunodeficiency virus 1 genomic RNA
    • Laughrea M, Jetté L. A 19-nucleotide sequence upstream of the 5′ major splice donor site is part of the dimerization domain of human immunodeficiency virus 1 genomic RNA. Biochemistry. 33:1994;13464-13474.
    • (1994) Biochemistry , vol.33 , pp. 13464-13474
    • Laughrea, M.1    Jetté, L.2
  • 29
    • 0027390734 scopus 로고
    • In vitro dimerization of HIV-2 leader RNA in the absence of PuGGAPuA motifs
    • Berkhout B, Oude Essink BB, Schoneveld I. In vitro dimerization of HIV-2 leader RNA in the absence of PuGGAPuA motifs. FASEB J. 7:1993;181-187.
    • (1993) FASEB J , vol.7 , pp. 181-187
    • Berkhout, B.1    Oude Essink, B.B.2    Schoneveld, I.3
  • 30
    • 0020569116 scopus 로고
    • Deletion mutants of Moloney murine leukemia virus which lack glycosylated gag protein are replication competent
    • Schwatzberg P, Colicelli J, Goff SP. Deletion mutants of Moloney murine leukemia virus which lack glycosylated gag protein are replication competent. J Virol. 46:1983;538.
    • (1983) J Virol , vol.46 , pp. 538
    • Schwatzberg, P.1    Colicelli, J.2    Goff, S.P.3
  • 31
    • 0020582124 scopus 로고
    • Construction of a retrovirus packaging mutant and its use to produce helper-free defective retrovirus
    • Mann R, Mulligan RC, Baltimore D. Construction of a retrovirus packaging mutant and its use to produce helper-free defective retrovirus. Cell. 33:1983;153-159.
    • (1983) Cell , vol.33 , pp. 153-159
    • Mann, R.1    Mulligan, R.C.2    Baltimore, D.3
  • 32
    • 0021823925 scopus 로고
    • Varying the position of a retrovirus packaging sequence results in the encapsidation of both unspliced and spliced RNAs
    • Mann R, Baltimore D. Varying the position of a retrovirus packaging sequence results in the encapsidation of both unspliced and spliced RNAs. J Virol. 54:1985;401-407.
    • (1985) J Virol , vol.54 , pp. 401-407
    • Mann, R.1    Baltimore, D.2
  • 33
    • 0023752108 scopus 로고
    • Identification of a signal in a murine retrovirus that is sufficient for packaging of nonretroviral RNA into virions
    • Adam MA, Miller AD. Identification of a signal in a murine retrovirus that is sufficient for packaging of nonretroviral RNA into virions. J Virol. 62:1988;3802-3806.
    • (1988) J Virol , vol.62 , pp. 3802-3806
    • Adam, M.A.1    Miller, A.D.2
  • 34
    • 0023177629 scopus 로고
    • Evidence that the packaging signal of Moloney murine leukemia virus extends into the gag region
    • Bender MA, Palmer TD, Gelinas RE, Miller AD. Evidence that the packaging signal of Moloney murine leukemia virus extends into the gag region. J Virol. 61:1987;1639-1646.
    • (1987) J Virol , vol.61 , pp. 1639-1646
    • Bender, M.A.1    Palmer, T.D.2    Gelinas, R.E.3    Miller, A.D.4
  • 35
    • 0024026527 scopus 로고
    • Small finger protein of avian and murine retroviruses has nucleic acid annealing activity and positions the replication primer tRNA onto genomic RNA
    • Prats AC, Sarih L, Gabus C, Litvak S, Keith G, Darlix JL. Small finger protein of avian and murine retroviruses has nucleic acid annealing activity and positions the replication primer tRNA onto genomic RNA. EMBO J. 7:1988;1777-1783.
    • (1988) EMBO J , vol.7 , pp. 1777-1783
    • Prats, A.C.1    Sarih, L.2    Gabus, C.3    Litvak, S.4    Keith, G.5    Darlix, J.L.6
  • 36
    • 0027319732 scopus 로고
    • Two short basic sequences surrounding the zinc finger of nucleocapsid protein NCp10 of Moloney murine leukemia virus are critical for RNA annealing activity
    • de Rocquigny H, Ficheux D, Gabus C, Allain B, Fournié-Zaluski MC, Darlix JL, Roques BP. Two short basic sequences surrounding the zinc finger of nucleocapsid protein NCp10 of Moloney murine leukemia virus are critical for RNA annealing activity. Nucleic Acids Res. 21:1993;823-829.
    • (1993) Nucleic Acids Res , vol.21 , pp. 823-829
    • De Rocquigny, H.1    Ficheux, D.2    Gabus, C.3    Allain, B.4    Fournié-Zaluski, M.C.5    Darlix, J.L.6    Roques, B.P.7
  • 37
    • 0029585377 scopus 로고
    • First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses
    • Darlix JL, Lapadat-Tapolski M, de Rocquigny H, Roques BP. First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses. J Mol Biol. 254:1995;523-537.
    • (1995) J Mol Biol , vol.254 , pp. 523-537
    • Darlix, J.L.1    Lapadat-Tapolski, M.2    De Rocquigny, H.3    Roques, B.P.4
  • 40
    • 0029097230 scopus 로고
    • A short autocomplementary sequence in the 5′ leader region id responsible for dimerization of MoMuLV genomic RNA
    • Girard P-M, Bonnet-Mathonière B, Muriaux D, Paoletti J. A short autocomplementary sequence in the 5′ leader region id responsible for dimerization of MoMuLV genomic RNA. Biochemistry. 34:1995;9785-9794.
    • (1995) Biochemistry , vol.34 , pp. 9785-9794
    • Girard P-M1    Bonnet-Mathonière, B.2    Muriaux, D.3    Paoletti, J.4
  • 41
    • 0004007632 scopus 로고
    • Appendix C
    • Weiss R. NY: Cold Spring Harbor Laboratory Press
    • Van Beveren C, Coffin J, Hughes S. Appendix C. Weiss R. RNA Tumor Viruses. 1984;928-939 Cold Spring Harbor Laboratory Press, NY.
    • (1984) RNA Tumor Viruses , pp. 928-939
    • Van Beveren, C.1    Coffin, J.2    Hughes, S.3
  • 42
    • 0027954398 scopus 로고
    • A small and efficient dimerization/packaging signal of rat VL30 RNA and its use in murine leukemia virus-VL30-derived vectors for gene transfer
    • Torrent C, Gabus C, Darlix JL. A small and efficient dimerization/packaging signal of rat VL30 RNA and its use in murine leukemia virus-VL30-derived vectors for gene transfer. J Virol. 68:1994;661-667.
    • (1994) J Virol , vol.68 , pp. 661-667
    • Torrent, C.1    Gabus, C.2    Darlix, J.L.3
  • 43
    • 0027959199 scopus 로고
    • Analytical study of rat retro-transposon VL30 RNA dimerization in vitro and packaging in murine leukemia virus
    • Torrent C, Bordet T, Darlix J-L. Analytical study of rat retro-transposon VL30 RNA dimerization in vitro and packaging in murine leukemia virus. J Mol Biol. 240:1994;434-444.
    • (1994) J Mol Biol , vol.240 , pp. 434-444
    • Torrent, C.1    Bordet, T.2    Darlix J-L3
  • 44
    • 0026684009 scopus 로고
    • A murine leukemia virus derived retroviral vector with a rat VL30 packaging psi sequence
    • Torrent C, Wang P, Darlix JL. A murine leukemia virus derived retroviral vector with a rat VL30 packaging psi sequence. Bone Marrow Transplant. 9:1992;143-147.
    • (1992) Bone Marrow Transplant , vol.9 , pp. 143-147
    • Torrent, C.1    Wang, P.2    Darlix, J.L.3
  • 45
    • 0028915078 scopus 로고
    • Multiple regions of barvey sarcoma virus RNA can dimerize in vitro
    • Feng Y-X, Fu W, Winter AJ, Levin JG, Rein A. Multiple regions of barvey sarcoma virus RNA can dimerize in vitro. J Virol. 69:1995;2486-2490.
    • (1995) J Virol , vol.69 , pp. 2486-2490
    • Feng Y-X1    Fu, W.2    Winter, A.J.3    Levin, J.G.4    Rein, A.5
  • 46
    • 0020594561 scopus 로고
    • Nucleotide sequence of Rous sarcoma virus
    • Schwartz DE, Tizard R, Gilbert W. Nucleotide sequence of Rous sarcoma virus. Cell. 32:1983;853-869.
    • (1983) Cell , vol.32 , pp. 853-869
    • Schwartz, D.E.1    Tizard, R.2    Gilbert, W.3
  • 47
    • 0022458033 scopus 로고
    • Control of Rous sarcoma virus RNA translation and packaging by the 5′ and 3′ untranslated sequences
    • Darlix J-L. Control of Rous sarcoma virus RNA translation and packaging by the 5′ and 3′ untranslated sequences. J Mol Biol. 189:1986;421-434.
    • (1986) J Mol Biol , vol.189 , pp. 421-434
    • Darlix J-L1
  • 48
    • 0025021014 scopus 로고
    • A study of the dimer formation of Rous sarcoma virus RNA and of its effect on viral protein synthesis in vitro
    • Bieth E, Gabus C, Darlix J-L. A study of the dimer formation of Rous sarcoma virus RNA and of its effect on viral protein synthesis in vitro. Nucleic Acids Res. 18:1990;119-127.
    • (1990) Nucleic Acids Res , vol.18 , pp. 119-127
    • Bieth, E.1    Gabus, C.2    Darlix J-L3
  • 49
    • 0022527281 scopus 로고
    • A conserved cis-acting sequence in the 5′ leader of avian sarcoma virus RNA is required for packaging
    • Katz RA, Terry RW, Skalka AM. A conserved cis-acting sequence in the 5′ leader of avian sarcoma virus RNA is required for packaging. J Virol. 59:1986;163-167.
    • (1986) J Virol , vol.59 , pp. 163-167
    • Katz, R.A.1    Terry, R.W.2    Skalka, A.M.3
  • 50
    • 0020566439 scopus 로고
    • Identification of a sequence likely to be required for avian retroviral packaging
    • Pugatsch T, Stacey DW. Identification of a sequence likely to be required for avian retroviral packaging. Virology. 128:1983;505-511.
    • (1983) Virology , vol.128 , pp. 505-511
    • Pugatsch, T.1    Stacey, D.W.2
  • 51
    • 0028879022 scopus 로고
    • A study of the dimerization of Rous sarcoma virus RNA in vitro and in vivo
    • Lear AL, Haddrick M, Heaphy S. A study of the dimerization of Rous sarcoma virus RNA in vitro and in vivo. Virology. 211:1995;47-57.
    • (1995) Virology , vol.211 , pp. 47-57
    • Lear, A.L.1    Haddrick, M.2    Heaphy, S.3
  • 52
    • 0020414647 scopus 로고
    • Encapsidation sequences for spleen necrosis virus, an avian retrovirus, are between the 5′ long terminal repeat and the start of the gag gene
    • Watanabe S, Temin HM. Encapsidation sequences for spleen necrosis virus, an avian retrovirus, are between the 5′ long terminal repeat and the start of the gag gene. Proc Natl Acad Sci USA. 79:1982;5986-5990.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5986-5990
    • Watanabe, S.1    Temin, H.M.2
  • 53
    • 0023241664 scopus 로고
    • Lack of competition results in efficient packaging of heterologous murine retroviral RNAs and reticuloendotheliosis virus encapsidation-minus RNAs by the reticuloendotheliosis virus helper cell line
    • Embretson JE, Temin HM. Lack of competition results in efficient packaging of heterologous murine retroviral RNAs and reticuloendotheliosis virus encapsidation-minus RNAs by the reticuloendotheliosis virus helper cell line. J Virol. 61:1987;2675-2683.
    • (1987) J Virol , vol.61 , pp. 2675-2683
    • Embretson, J.E.1    Temin, H.M.2
  • 54
    • 0026448586 scopus 로고
    • Analytical study of avian reticuloendotheliosis virus dimeric RNA generated in vivo and in vitro
    • Darlix J-L, Gabus C, Allain B. Analytical study of avian reticuloendotheliosis virus dimeric RNA generated in vivo and in vitro. J Virol. 66:1992;7245-7252.
    • (1992) J Virol , vol.66 , pp. 7245-7252
    • Darlix J-L1    Gabus, C.2    Allain, B.3
  • 55
    • 0027952631 scopus 로고
    • A double hairpin structure is necessary for the efficient encapsidation of spleen necrosis virus retroviral RNA
    • Yang S, Temin HM. A double hairpin structure is necessary for the efficient encapsidation of spleen necrosis virus retroviral RNA. EMBO J. 13:1994;713-726.
    • (1994) EMBO J , vol.13 , pp. 713-726
    • Yang, S.1    Temin, H.M.2
  • 56
    • 0025723524 scopus 로고
    • Bovine leukemia virus matrix-associated protein MA (p15): Further processing and formation of a specific complex with the dimer of the 5′-terminal genomic RNA fragment
    • Katoh I, Kyushiki H, Sakamoto Y, Ikawa Y, Yoshinaka Y. Bovine leukemia virus matrix-associated protein MA (p15): further processing and formation of a specific complex with the dimer of the 5′-terminal genomic RNA fragment. J Virol. 65:1991;6845-6855.
    • (1991) J Virol , vol.65 , pp. 6845-6855
    • Katoh, I.1    Kyushiki, H.2    Sakamoto, Y.3    Ikawa, Y.4    Yoshinaka, Y.5
  • 57
    • 0027465686 scopus 로고
    • Bovine leukemia virus RNA sequences involved in dimerization and specific gag protein binding: Close relation to the packaging sites of avian, murine, and human retroviruses
    • Katoh I, Yasunaga T, Yoshinaka Y. Bovine leukemia virus RNA sequences involved in dimerization and specific gag protein binding: close relation to the packaging sites of avian, murine, and human retroviruses. J Virol. 67:1993;1830-1839.
    • (1993) J Virol , vol.67 , pp. 1830-1839
    • Katoh, I.1    Yasunaga, T.2    Yoshinaka, Y.3
  • 58
    • 0029154036 scopus 로고
    • An RNA stem-loop structure involved in the packaging of bovine leukemia virus genomic RNA in vivo
    • Kurg A, Sommer G, Metspalu A. An RNA stem-loop structure involved in the packaging of bovine leukemia virus genomic RNA in vivo. Virology. 211:1995;434-442.
    • (1995) Virology , vol.211 , pp. 434-442
    • Kurg, A.1    Sommer, G.2    Metspalu, A.3
  • 59
    • 0029040494 scopus 로고
    • The bovine leukemia virus encapsidation signal is discontinuous and extends into the 5′ end of the gag gene
    • Mansky LM, Krueger AE, Temin HM. The bovine leukemia virus encapsidation signal is discontinuous and extends into the 5′ end of the gag gene. J Virol. 69:1995;3282-3289.
    • (1995) J Virol , vol.69 , pp. 3282-3289
    • Mansky, L.M.1    Krueger, A.E.2    Temin, H.M.3
  • 60
    • 0027479628 scopus 로고
    • Functional sites in the 5′ region of human immunodeficiency virus type-1 RNA form defined structural domains
    • Baudin F, Marquet R, Isel C, Darlix J-L, Ehresmann B, Ehresmann C. Functional sites in the 5′ region of human immunodeficiency virus type-1 RNA form defined structural domains. J Mol Biol. 229:1993;382-397.
    • (1993) J Mol Biol , vol.229 , pp. 382-397
    • Baudin, F.1    Marquet, R.2    Isel, C.3    Darlix J-L4    Ehresmann, B.5    Ehresmann, C.6
  • 61
    • 0027380689 scopus 로고
    • Mode of dimerization of HIV-1 genomic RNA
    • Awang G, Sen D. Mode of dimerization of HIV-1 genomic RNA. Biochemistry. 32:1993;11453-11457.
    • (1993) Biochemistry , vol.32 , pp. 11453-11457
    • Awang, G.1    Sen, D.2
  • 62
    • 0027533742 scopus 로고
    • Evidence for interstrand quadruplex formation in the dimerization of human immunodeficiency virus-1 genomic RNA
    • Sundquist WI, Heaphy S. Evidence for interstrand quadruplex formation in the dimerization of human immunodeficiency virus-1 genomic RNA. Proc Natl Acad Sci USA. 90:1993;3393-3397.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3393-3397
    • Sundquist, W.I.1    Heaphy, S.2
  • 63
    • 0027438808 scopus 로고
    • The multimerization state of retroviral RNA is modulated by ammonium ions and affects HIV-1 full-length cDNA synthesis in vitro
    • Weiss S, Häusl G, Famulok M, König B. The multimerization state of retroviral RNA is modulated by ammonium ions and affects HIV-1 full-length cDNA synthesis in vitro. Nucleic Acids Res. 21:1993;4879-4885.
    • (1993) Nucleic Acids Res , vol.21 , pp. 4879-4885
    • Weiss, S.1    Häusl, G.2    Famulok, M.3    König, B.4
  • 64
    • 0003200419 scopus 로고    scopus 로고
    • Localization of the dimerization initiation site of HIV-1 genomic RNA and mechanism of dimerization
    • R.H. Sarma, Sarma M.H. Albany, NY: Adenine Press. in press
    • Marquet R, Paillart J-C, Skripkin E, Ehresmann C, Ehresmann B. Localization of the dimerization initiation site of HIV-1 genomic RNA and mechanism of dimerization. Sarma RH, Sarma MH. Biological Structure and Dynamics. 1996;Adenine Press, Albany, NY. in press.
    • (1996) Biological Structure and Dynamics
    • Marquet, R.1    Paillart J-C2    Skripkin, E.3    Ehresmann, C.4    Ehresmann, B.5
  • 65
    • 0028338652 scopus 로고
    • Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protease-defective virions
    • Fu W, Gorelick RJ, Rein A. Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protease-defective virions. J Virol. 68:1994;5013-5018.
    • (1994) J Virol , vol.68 , pp. 5013-5018
    • Fu, W.1    Gorelick, R.J.2    Rein, A.3
  • 66
    • 0030019828 scopus 로고    scopus 로고
    • Kissing-loop model of HIV-1 genome dimerization: HIV-1 RNA can assume alternative dimeric forms, and all sequences upstream or downstream of hairpin 248-271 are dispensable for dimer formation
    • Laughrea M, Jetté L. Kissing-loop model of HIV-1 genome dimerization: HIV-1 RNA can assume alternative dimeric forms, and all sequences upstream or downstream of hairpin 248-271 are dispensable for dimer formation. Biochemistry. 35:1996;1589-1598.
    • (1996) Biochemistry , vol.35 , pp. 1589-1598
    • Laughrea, M.1    Jetté, L.2
  • 68
    • 0002721515 scopus 로고
    • The control of prokaryotic and eukaryotic gene expression by naturally occurring antisens RNA
    • S.T. Crooke, Lebleu B. Boca Raton: CRC Press Inc
    • Simons RW. The control of prokaryotic and eukaryotic gene expression by naturally occurring antisens RNA. Crooke ST, Lebleu B. Antisense Research and Applications. 1993;97-124 CRC Press Inc, Boca Raton.
    • (1993) Antisense Research and Applications , pp. 97-124
    • Simons, R.W.1
  • 69
    • 85041131924 scopus 로고
    • Antisens RNA control in bacteria, phage and plasmids
    • Wagner EGH, Simons RW. Antisens RNA control in bacteria, phage and plasmids. Annu Rev Microbiol. 48:1994;713-742.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 713-742
    • Wagner, E.G.H.1    Simons, R.W.2
  • 71
    • 0027267286 scopus 로고
    • Secondary structure of HIV-2 leader RNA comprising the tRNA-primer binding site
    • Berkhout B, Schoneveld I. Secondary structure of HIV-2 leader RNA comprising the tRNA-primer binding site. Nucleic Acids Res. 21:1993;1171-1178.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1171-1178
    • Berkhout, B.1    Schoneveld, I.2
  • 72
    • 0030366242 scopus 로고    scopus 로고
    • Structure and function of the human immunodeficiency virus leader RNA
    • in press
    • Berkhout B. Structure and function of the human immunodeficiency virus leader RNA. Prog Nucleic Acids Res Mol Biol. 1996;. in press.
    • (1996) Prog Nucleic Acids Res Mol Biol
    • Berkhout, B.1
  • 73
    • 0026544013 scopus 로고
    • Novel GACG-hairpin pair motif in the 5′ untranslated region of type C retrovirus related to murine leukemia virus
    • Konings DAM, Nash MA, Maizel JV, Arlinghaus RB. Novel GACG-hairpin pair motif in the 5′ untranslated region of type C retrovirus related to murine leukemia virus. J Virol. 66:1992;632-640.
    • (1992) J Virol , vol.66 , pp. 632-640
    • Konings, D.A.M.1    Nash, M.A.2    Maizel, J.V.3    Arlinghaus, R.B.4
  • 74
    • 0027426883 scopus 로고
    • Conformation analysis of the 5′ leader and the gag initiation site of MoMuLV RNA and allosteric transitions induced by dimerization
    • Mougel M, Tounekti N, Darlix JL, Paoletti J, Ehresmann B, Ehresmann C. Conformation analysis of the 5′ leader and the gag initiation site of MoMuLV RNA and allosteric transitions induced by dimerization. Nucleic Acids Res. 21:1993;4677-4684.
    • (1993) Nucleic Acids Res , vol.21 , pp. 4677-4684
    • Mougel, M.1    Tounekti, N.2    Darlix, J.L.3    Paoletti, J.4    Ehresmann, B.5    Ehresmann, C.6
  • 75
    • 0025884993 scopus 로고
    • RNA secondary structure analysis of the packaging signal for Moloney murine leukemia virus
    • Alford RL, Honda S, Lawrence CB, Belmont JW. RNA secondary structure analysis of the packaging signal for Moloney murine leukemia virus. Virology. 183:1991;611-619.
    • (1991) Virology , vol.183 , pp. 611-619
    • Alford, R.L.1    Honda, S.2    Lawrence, C.B.3    Belmont, J.W.4
  • 76
    • 0026329560 scopus 로고
    • Phylogenetic and physiscal analysis of the 5′ leader RNA sequences of avian retrovirus
    • Hackett PB, Dalton MW, Johnson DP, Petersen RB. Phylogenetic and physiscal analysis of the 5′ leader RNA sequences of avian retrovirus. Nucleic Acids Res. 19:1992;6929-6934.
    • (1992) Nucleic Acids Res , vol.19 , pp. 6929-6934
    • Hackett, P.B.1    Dalton, M.W.2    Johnson, D.P.3    Petersen, R.B.4
  • 77
    • 0028953881 scopus 로고
    • Secondary structure model of Mason-pfiser monkey virus 5′ leader sequence: Identification of a structural motif common to a variety of retroviruses
    • Harrison GP, Hunter E, Lever AML. Secondary structure model of Mason-pfiser monkey virus 5′ leader sequence: identification of a structural motif common to a variety of retroviruses. J Virol. 69:1995;2175-2186.
    • (1995) J Virol , vol.69 , pp. 2175-2186
    • Harrison, G.P.1    Hunter, E.2    Lever, A.M.L.3
  • 78
    • 0003518435 scopus 로고
    • A compilation and analysis of nucleic acid and amino acid sequences
    • G. Myers, B. Korber, B.H. Hahn, K-T Jeang, J.W. Mellors, F.E. McCutchan, L.E. Henderson, & G.N. Pavlakis. Los Alamos, New Mexico, USA: Los Alamos National Laboratory
    • Myers G, Korber B, Hahn BH, Jeang K-T, Mellors JW, McCutchan FE, Henderson LE, Pavlakis GN. A compilation and analysis of nucleic acid and amino acid sequences. Human Retroviruses and AIDS. 1995;Los Alamos National Laboratory, Los Alamos, New Mexico, USA.
    • (1995) Human Retroviruses and AIDS
  • 79
    • 0019786215 scopus 로고
    • Primary structure of the low-molecular-weight nucleic acid binding proteins of murine leukemia viruses
    • Henderson LE, Copeland TD, Sowder RC, Smythers GW, Oroszlan S. Primary structure of the low-molecular-weight nucleic acid binding proteins of murine leukemia viruses. J Biol Chem. 256:1981;8400-8406.
    • (1981) J Biol Chem , vol.256 , pp. 8400-8406
    • Henderson, L.E.1    Copeland, T.D.2    Sowder, R.C.3    Smythers, G.W.4    Oroszlan, S.5
  • 80
    • 0023055867 scopus 로고
    • Amino acid sequence homology in gag region of reverse transcribing elements and the coat protein gene of cauliflower mosaic virus
    • Covey SN. Amino acid sequence homology in gag region of reverse transcribing elements and the coat protein gene of cauliflower mosaic virus. Nucleic Acids Res. 14:1986;623-633.
    • (1986) Nucleic Acids Res , vol.14 , pp. 623-633
    • Covey, S.N.1
  • 81
    • 0026171924 scopus 로고
    • Investigation of zinc-binding affinities of Moloney murine leukemia virus nucleocapsid protein and its related zinc finger and modified peptides
    • Mély Y, Cornille F, Fournié-Zaluski M-C, Darlix JL, Roques BP, Gérard D. Investigation of zinc-binding affinities of Moloney murine leukemia virus nucleocapsid protein and its related zinc finger and modified peptides. Biopolymers. 31:1991;899-906.
    • (1991) Biopolymers , vol.31 , pp. 899-906
    • Mély, Y.1    Cornille, F.2    Fournié-Zaluski M-C3    Darlix, J.L.4    Roques, B.P.5    Gérard, D.6
  • 82
    • 0026592529 scopus 로고
    • Tightly bound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type 1, and other retroviruses
    • Bess JW, Powell PJ, Issaq HJ, Schumack LJ, Grimes MK, Henderson LE, Arthur LO. Tightly bound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type 1, and other retroviruses. J Virol. 66:1992;840-847.
    • (1992) J Virol , vol.66 , pp. 840-847
    • Bess, J.W.1    Powell, P.J.2    Issaq, H.J.3    Schumack, L.J.4    Grimes, M.K.5    Henderson, L.E.6    Arthur, L.O.7
  • 83
    • 0020367716 scopus 로고
    • Binding sites of viral protein P19 onto Rous sarcoma virus RNA and possible controls of viral functions
    • Darlix JL, Spahr P-F. Binding sites of viral protein P19 onto Rous sarcoma virus RNA and possible controls of viral functions. J Mol Biol. 160:1982;147-161.
    • (1982) J Mol Biol , vol.160 , pp. 147-161
    • Darlix, J.L.1    Spahr P-F2
  • 84
    • 0021763128 scopus 로고
    • It is Rous sarcoma virus P12 and not P19 that binds tightly to Rous sarcoma virus RNA
    • Méric C, Darlix JL, Spahr PF. It is Rous sarcoma virus P12 and not P19 that binds tightly to Rous sarcoma virus RNA. J Mol Biol. 173:1984;531-538.
    • (1984) J Mol Biol , vol.173 , pp. 531-538
    • Méric, C.1    Darlix, J.L.2    Spahr, P.F.3
  • 85
    • 0026474681 scopus 로고
    • Recombinant HIV-1 nucleocapsid protein p15 produced as a fusion protein with glutathione S-transferase in Escherichia coli mediates dimerization and enhances reverse transcription of retroviral RNA
    • Weiss S, Konig B, Morikawa Y, Jones I. Recombinant HIV-1 nucleocapsid protein p15 produced as a fusion protein with glutathione S-transferase in Escherichia coli mediates dimerization and enhances reverse transcription of retroviral RNA. Gene. 121:1992;203-212.
    • (1992) Gene , vol.121 , pp. 203-212
    • Weiss, S.1    Konig, B.2    Morikawa, Y.3    Jones, I.4
  • 87
    • 0026628854 scopus 로고
    • Viral RNA annealing activities of human immunodeficiency virus type-1 nucleocapsid protein require only peptide domains outside the zinc fingers
    • de Rocquigny H, Gabus C, Vincent A, Fournié-Zaluski MC, Roques BP, Darlix JL. Viral RNA annealing activities of human immunodeficiency virus type-1 nucleocapsid protein require only peptide domains outside the zinc fingers. Proc Natl Acad Sci USA. 89:1992;6472-6476.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6472-6476
    • De Rocquigny, H.1    Gabus, C.2    Vincent, A.3    Fournié-Zaluski, M.C.4    Roques, B.P.5    Darlix, J.L.6
  • 88
    • 0025773436 scopus 로고
    • Viral RNA annealing activities of the nucleocapsid protein of Moloney murine leukemia virus are zinc independent
    • Prats AC, Housset V, de Billy G, Cornille F, Prats H, Roques B, Darlix JL. Viral RNA annealing activities of the nucleocapsid protein of Moloney murine leukemia virus are zinc independent. Nucleic Acids Res. 19:1991;3533-3541.
    • (1991) Nucleic Acids Res , vol.19 , pp. 3533-3541
    • Prats, A.C.1    Housset, V.2    De Billy, G.3    Cornille, F.4    Prats, H.5    Roques, B.6    Darlix, J.L.7
  • 89
    • 0027480054 scopus 로고
    • Basic amino acids flanking the zinc finger of Moloney murine leukemia virus nucleocapsid protein NCp10 are critical for virus infectivity
    • Housset V, de Rocquigny H, Roques BP, Darlix JL. Basic amino acids flanking the zinc finger of Moloney murine leukemia virus nucleocapsid protein NCp10 are critical for virus infectivity. J Virol. 67:1993;2537-2545.
    • (1993) J Virol , vol.67 , pp. 2537-2545
    • Housset, V.1    De Rocquigny, H.2    Roques, B.P.3    Darlix, J.L.4
  • 90
    • 0030019808 scopus 로고    scopus 로고
    • The in vitro ejection of zinc from human immunodeficiency virus (HIV) type 1 nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity
    • Tummino PJ, Scholten JD, Harvey P, Holler TP, Maloney L, Gogliotti R, Domagala J, Hupe D. The in vitro ejection of zinc from human immunodeficiency virus (HIV) type 1 nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity. Proc Natl Acad Sci USA. 93:1996;969-973.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 969-973
    • Tummino, P.J.1    Scholten, J.D.2    Harvey, P.3    Holler, T.P.4    Maloney, L.5    Gogliotti, R.6    Domagala, J.7    Hupe, D.8
  • 91
    • 0025941876 scopus 로고
    • Binding of the human immunodeficiency virus type 1 (HIV-1) RNA to recombinant HIV-1 gag polyprotein
    • Luban J, Goff SP. Binding of the human immunodeficiency virus type 1 (HIV-1) RNA to recombinant HIV-1 gag polyprotein. J Virol. 65:1991;3203-3212.
    • (1991) J Virol , vol.65 , pp. 3203-3212
    • Luban, J.1    Goff, S.P.2
  • 92
    • 0027496344 scopus 로고
    • Specific binding of human immunodeficiency virus type 1 gag polyprotein and nucleocapsid protein to viral RNAs detected by RNA mobility shift assays
    • Berkowitz RD, Luban J, Goff SP. Specific binding of human immunodeficiency virus type 1 gag polyprotein and nucleocapsid protein to viral RNAs detected by RNA mobility shift assays. J Virol. 67:1993;7190-7200.
    • (1993) J Virol , vol.67 , pp. 7190-7200
    • Berkowitz, R.D.1    Luban, J.2    Goff, S.P.3
  • 93
    • 0028100456 scopus 로고
    • Analysis of binding elements in the human immunodeficiency virus type 1 genomic RNA and nucleocapsid protein
    • Berkowitz RD, Goff SP. Analysis of binding elements in the human immunodeficiency virus type 1 genomic RNA and nucleocapsid protein. Virology. 202:1994;233-246.
    • (1994) Virology , vol.202 , pp. 233-246
    • Berkowitz, R.D.1    Goff, S.P.2
  • 94
    • 0028904512 scopus 로고
    • RNA secondary structure and binding sites for gag gene products in the 5′ packaging signal of human immunodeficiency virus type 1
    • Clever J, Sassetti C, Parslow TG. RNA secondary structure and binding sites for gag gene products in the 5′ packaging signal of human immunodeficiency virus type 1. J Virol. 69:1995;2101-2109.
    • (1995) J Virol , vol.69 , pp. 2101-2109
    • Clever, J.1    Sassetti, C.2    Parslow, T.G.3
  • 95
    • 0029656149 scopus 로고    scopus 로고
    • Specific binding of human immunodeficiency virus type 1 (HIV-1) gag-derived proteins to a 5′ HIV-1 genomic RNA sequence
    • Geigenmüller U, Linial ML. Specific binding of human immunodeficiency virus type 1 (HIV-1) gag-derived proteins to a 5′ HIV-1 genomic RNA sequence. J Virol. 70:1996;667-671.
    • (1996) J Virol , vol.70 , pp. 667-671
    • Geigenmüller, U.1    Linial, M.L.2
  • 96
    • 0026700526 scopus 로고
    • 2+ complex formation analysis with electrospray mass spectrometry
    • 2+ complex formation analysis with electrospray mass spectrometry. FEBS Lett. 311:1992;259-262.
    • (1992) FEBS Lett , vol.311 , pp. 259-262
    • Surovoy, A.1    Waidelich, D.2    Jung, G.3
  • 97
    • 0027324022 scopus 로고
    • Elucidation of a conserved RNA stem-loop structure in the packaging signal of human immunodeficiency virus type-1
    • Hayashi T, Ueno Y, Okamoto T. Elucidation of a conserved RNA stem-loop structure in the packaging signal of human immunodeficiency virus type-1. FEBS Lett. 327:1993;213-218.
    • (1993) FEBS Lett , vol.327 , pp. 213-218
    • Hayashi, T.1    Ueno, Y.2    Okamoto, T.3
  • 98
    • 0027176378 scopus 로고
    • Maturation of dimeric viral RNA of Moloney murine leukemia virus
    • Fu W, Rein A. Maturation of dimeric viral RNA of Moloney murine leukemia virus. J Virol. 67:1993;5443-5449.
    • (1993) J Virol , vol.67 , pp. 5443-5449
    • Fu, W.1    Rein, A.2
  • 99
    • 0015810188 scopus 로고
    • RNA metabolism of murine leukemia virus: Detection of virus-specific RNA sequences in infected and uninfected cells and identification of virus-specific messenger RNA
    • Fan H, Baltimore D. RNA metabolism of murine leukemia virus: detection of virus-specific RNA sequences in infected and uninfected cells and identification of virus-specific messenger RNA. J Mol Biol. 80:1973;93-117.
    • (1973) J Mol Biol , vol.80 , pp. 93-117
    • Fan, H.1    Baltimore, D.2
  • 100
    • 0016218492 scopus 로고
    • Deficiency of 60 to 70S RNA in murine leukemia virus particles assembled in cells treated with actinomycin D
    • Levin JG, Grimley PM, Ramseur JM, Berezesky IK. Deficiency of 60 to 70S RNA in murine leukemia virus particles assembled in cells treated with actinomycin D. J Virol. 14:1974;152-161.
    • (1974) J Virol , vol.14 , pp. 152-161
    • Levin, J.G.1    Grimley, P.M.2    Ramseur, J.M.3    Berezesky, I.K.4
  • 101
    • 0019860883 scopus 로고
    • Metabolism of viral RNA in murine leukemia virus-infected cells: Evidence for differential stability of viral message and virion precursor RNA
    • Messer LI, Levin JG, Chattopadhyay SK. Metabolism of viral RNA in murine leukemia virus-infected cells: evidence for differential stability of viral message and virion precursor RNA. J Virol. 40:1981;683-690.
    • (1981) J Virol , vol.40 , pp. 683-690
    • Messer, L.I.1    Levin, J.G.2    Chattopadhyay, S.K.3
  • 102
    • 0023886015 scopus 로고
    • Post-transcriptional regulatory mechanisms in Escherichia coli
    • Gold L. Post-transcriptional regulatory mechanisms in Escherichia coli. Annu Rev Biochem. 57:1988;199-233.
    • (1988) Annu Rev Biochem , vol.57 , pp. 199-233
    • Gold, L.1
  • 103
    • 0005218668 scopus 로고
    • Influences of mRNA secondary structure on initiation by eukaryotic ribosomes
    • Kozak M. Influences of mRNA secondary structure on initiation by eukaryotic ribosomes. Proc Natl Acad Sci USA. 83:1986;2850-2854.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2850-2854
    • Kozak, M.1
  • 104
    • 0024414469 scopus 로고
    • Circumstances and mechanisms of inhibition of translation by secondary structure in eukaryotic mRNAs
    • Kozak M. Circumstances and mechanisms of inhibition of translation by secondary structure in eukaryotic mRNAs. Mol Cell Biol. 9:1989;5134-5142.
    • (1989) Mol Cell Biol , vol.9 , pp. 5134-5142
    • Kozak, M.1
  • 105
    • 0024986686 scopus 로고
    • Control of prokaryotic translational initiation by mRNA secondary structure
    • de Smit M, van Duin J. Control of prokaryotic translational initiation by mRNA secondary structure. Progr Nucleic Acid Res Mol Biol. 38:1990;1-35.
    • (1990) Progr Nucleic Acid Res Mol Biol , vol.38 , pp. 1-35
    • De Smit, M.1    Van Duin, J.2
  • 106
    • 0030025977 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 5′ packaging signal structure affects translation but does not function as an internal ribosome entry site structure
    • Miele G, Mouland A, Harrison GP, Cohen E, Lever AML. The human immunodeficiency virus type 1 5′ packaging signal structure affects translation but does not function as an internal ribosome entry site structure. J Virol. 70:1996;944-951.
    • (1996) J Virol , vol.70 , pp. 944-951
    • Miele, G.1    Mouland, A.2    Harrison, G.P.3    Cohen, E.4    Lever, A.M.L.5
  • 107
    • 0026760617 scopus 로고
    • Role of the open reading frames of Rous sarcoma virus leader RNA in translation and genome packaging
    • Donzé O, Spahr PF. Role of the open reading frames of Rous sarcoma virus leader RNA in translation and genome packaging. EMBO J. 11:1992;3747-3757.
    • (1992) EMBO J , vol.11 , pp. 3747-3757
    • Donzé, O.1    Spahr, P.F.2
  • 108
    • 0028925912 scopus 로고
    • The first and third uORFs in RSV leader RNA are efficiently translated: Implications for translational regulation and viral RNA packaging
    • Donzé O, Damay P, Spahr PF. The first and third uORFs in RSV leader RNA are efficiently translated: implications for translational regulation and viral RNA packaging. Nucleic Acids Res. 23:1995;861-868.
    • (1995) Nucleic Acids Res , vol.23 , pp. 861-868
    • Donzé, O.1    Damay, P.2    Spahr, P.F.3
  • 109
    • 0025295654 scopus 로고
    • Retroviral RNA packaging: Sequence requirements and implications
    • Linial ML, Miller AD. Retroviral RNA packaging: sequence requirements and implications. Curr Top Microbiol Immunol. 157:1990;125-152.
    • (1990) Curr Top Microbiol Immunol , vol.157 , pp. 125-152
    • Linial, M.L.1    Miller, A.D.2
  • 110
    • 0018236682 scopus 로고
    • An avian oncovirus mutant (SE 21Q1b) deficient in genomic RNA: Biological and biochemical characterization
    • Linial M, Medeiros E, Hayward WS. An avian oncovirus mutant (SE 21Q1b) deficient in genomic RNA: biological and biochemical characterization. Cell. 15:1978;1371-1381.
    • (1978) Cell , vol.15 , pp. 1371-1381
    • Linial, M.1    Medeiros, E.2    Hayward, W.S.3
  • 112
    • 0026632944 scopus 로고
    • RNA packaging signal of human immunodeficiency virus type-1
    • Hayashi T, Shioda T, Iwakura Y, Shibuta H. RNA packaging signal of human immunodeficiency virus type-1. Virology. 188:1992;590-599.
    • (1992) Virology , vol.188 , pp. 590-599
    • Hayashi, T.1    Shioda, T.2    Iwakura, Y.3    Shibuta, H.4
  • 113
    • 0028246961 scopus 로고
    • A short sequence upstream of the 5′ major splice site is important for encapsidation of HIV-1 genomic RNA
    • Kim HJ, Lee K, O'Rear JJ. A short sequence upstream of the 5′ major splice site is important for encapsidation of HIV-1 genomic RNA. Virology. 198:1994;336-340.
    • (1994) Virology , vol.198 , pp. 336-340
    • Kim, H.J.1    Lee, K.2    O'Rear, J.J.3
  • 114
    • 0029154824 scopus 로고
    • Human immunodeficiency virus type 2 (HIV-2): Packaging signal and associated negative regulatory element
    • Garzino-Demo A, Gallo RC, Arya SK. Human immunodeficiency virus type 2 (HIV-2): packaging signal and associated negative regulatory element. Hum Gene Ther. 6:1995;177-184.
    • (1995) Hum Gene Ther , vol.6 , pp. 177-184
    • Garzino-Demo, A.1    Gallo, R.C.2    Arya, S.K.3
  • 115
    • 0027480059 scopus 로고
    • Simian immunodeficiency virus RNA is efficiently encapsidated by HIV-1 particles
    • Rizvi TA, Panganiban AT. Simian immunodeficiency virus RNA is efficiently encapsidated by HIV-1 particles. J Virol. 67:1993;2681-2688.
    • (1993) J Virol , vol.67 , pp. 2681-2688
    • Rizvi, T.A.1    Panganiban, A.T.2
  • 116
    • 0029149643 scopus 로고
    • Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation
    • Zhang Y, Barklis E. Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation. J Virol. 69:1995;5716-5722.
    • (1995) J Virol , vol.69 , pp. 5716-5722
    • Zhang, Y.1    Barklis, E.2
  • 117
    • 0029134623 scopus 로고
    • Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric gag polyproteins during RNA packaging in vivo
    • Berkowitz RD, Ohagen A, Höglund S, Goff SP. Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric gag polyproteins during RNA packaging in vivo. J Virol. 69:1995;6445-6456.
    • (1995) J Virol , vol.69 , pp. 6445-6456
    • Berkowitz, R.D.1    Ohagen, A.2    Höglund, S.3    Goff, S.P.4
  • 118
    • 9244219568 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 encapsidation site is a multipartite RNA element composed of functional hairpin structures
    • McBride MS, Panganiban AT. The human immunodeficiency virus type 1 encapsidation site is a multipartite RNA element composed of functional hairpin structures. J Virol. 70:1996;2963-2973.
    • (1996) J Virol , vol.70 , pp. 2963-2973
    • McBride, M.S.1    Panganiban, A.T.2
  • 119
    • 0015459544 scopus 로고
    • Comparison of immature (rapide harvest) and mature Rous sarcoma virus particles
    • Cheung KS, Smith RE, Stone MP, Joklik WK. Comparison of immature (rapide harvest) and mature Rous sarcoma virus particles. Virology. 50:1972;851-864.
    • (1972) Virology , vol.50 , pp. 851-864
    • Cheung, K.S.1    Smith, R.E.2    Stone, M.P.3    Joklik, W.K.4
  • 121
    • 0025155072 scopus 로고
    • Point mutations in the proximal cys-his box of Rous sarcoma virus nucleocapsid protein
    • Dupraz P, Oertle S, Méric C, Damay P, Spahr PF. Point mutations in the proximal cys-his box of Rous sarcoma virus nucleocapsid protein. J Virol. 64:1990;4978-4987.
    • (1990) J Virol , vol.64 , pp. 4978-4987
    • Dupraz, P.1    Oertle, S.2    Méric, C.3    Damay, P.4    Spahr, P.F.5
  • 122
    • 0024507854 scopus 로고
    • Characterization of Moloney murine leukemia virus mutants with single amino-acid substitution in the Cys-His box of the nucleocapsid protein
    • Méric C, Goff S. Characterization of Moloney murine leukemia virus mutants with single amino-acid substitution in the Cys-His box of the nucleocapsid protein. J Virol. 63:1989;1558-1568.
    • (1989) J Virol , vol.63 , pp. 1558-1568
    • Méric, C.1    Goff, S.2
  • 123
    • 0025959787 scopus 로고
    • Sex and recombination in retroviruses
    • Temin HM. Sex and recombination in retroviruses. Trends Genet. 7:1991;71-74.
    • (1991) Trends Genet , vol.7 , pp. 71-74
    • Temin, H.M.1
  • 124
    • 0027180278 scopus 로고
    • Retrovirus variation and reverse transcription: Abnormal strand transfers result in retrovirus genetic variation
    • Temin HM. Retrovirus variation and reverse transcription: abnormal strand transfers result in retrovirus genetic variation. Proc Natl Acad Sci USA. 90:1993;6900-6903.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6900-6903
    • Temin, H.M.1
  • 125
    • 0025215849 scopus 로고
    • Reverse transcriptase and genomic variability: The accuracy of DNA replication is enzyme-specific and sequence-dependent
    • Ricchetti M, Buc H. Reverse transcriptase and genomic variability: the accuracy of DNA replication is enzyme-specific and sequence-dependent. EMBO J. 9:1990;1583-1593.
    • (1990) EMBO J , vol.9 , pp. 1583-1593
    • Ricchetti, M.1    Buc, H.2
  • 126
    • 0025635705 scopus 로고
    • Retroviral recombination and reverse transcription
    • Hu WS, Temin HM. Retroviral recombination and reverse transcription. Science. 250:1990;1227-1233.
    • (1990) Science , vol.250 , pp. 1227-1233
    • Hu, W.S.1    Temin, H.M.2
  • 127
    • 0026608762 scopus 로고
    • Homologous recombination of copackaged retroviruse RNAs during reverse transcription
    • Stuhlmann H, Berg P. Homologous recombination of copackaged retroviruse RNAs during reverse transcription. J Virol. 66:1992;2378-2388.
    • (1992) J Virol , vol.66 , pp. 2378-2388
    • Stuhlmann, H.1    Berg, P.2
  • 128
    • 0001145205 scopus 로고
    • Role of reverse transcriptase in retroviral recombination
    • New York: Cold Spring Harbor Laboratory Press
    • Hu W-S, Pathak VK, Temin HM. Role of reverse transcriptase in retroviral recombination. Reverse Transcriptase. 1993;251-274 Cold Spring Harbor Laboratory Press, New York.
    • (1993) Reverse Transcriptase , pp. 251-274
    • Hu W-S1    Pathak, V.K.2    Temin, H.M.3
  • 129
    • 0018304892 scopus 로고
    • Structure, replication and recombination of retrovirus genomes: Some unifying hypothesis
    • Coffin JM. Structure, replication and recombination of retrovirus genomes: some unifying hypothesis. J Gen Virol. 42:1979;1-26.
    • (1979) J Gen Virol , vol.42 , pp. 1-26
    • Coffin, J.M.1
  • 130
    • 0017910010 scopus 로고
    • The mechanisms for genetic recombination in the avian retroviruses
    • Hunter E. The mechanisms for genetic recombination in the avian retroviruses. Curr Top Microbiol Immunol. 79:1978;295-309.
    • (1978) Curr Top Microbiol Immunol , vol.79 , pp. 295-309
    • Hunter, E.1
  • 131
    • 0020174308 scopus 로고
    • Retroviral DNA H structures: Displacement-assimilation model of recombination
    • Junghans RP, Boone LR, Skalka AM. Retroviral DNA H structures: displacement-assimilation model of recombination. Cell. 30:1982;53-62.
    • (1982) Cell , vol.30 , pp. 53-62
    • Junghans, R.P.1    Boone, L.R.2    Skalka, A.M.3
  • 133
    • 0028147389 scopus 로고
    • One retroviral RNA is sufficient for synthesis of viral DNA
    • Jones JS, Allan RW, Temin HM. One retroviral RNA is sufficient for synthesis of viral DNA. J Virol. 68:1994;207-216.
    • (1994) J Virol , vol.68 , pp. 207-216
    • Jones, J.S.1    Allan, R.W.2    Temin, H.M.3
  • 134
    • 0024297783 scopus 로고
    • Ordered interstrand and intrastrand DNA transfer during reverse transcription
    • Panganiban A, Fiore D. Ordered interstrand and intrastrand DNA transfer during reverse transcription. Science. 241:1988;1064-1069.
    • (1988) Science , vol.241 , pp. 1064-1069
    • Panganiban, A.1    Fiore, D.2
  • 135
    • 0025112945 scopus 로고
    • Template switching by reverse transcriptase during DNA synthesis
    • Luo G, Taylor J. Template switching by reverse transcriptase during DNA synthesis. J. Virol. 64:1990;4321-4328.
    • (1990) J. Virol. , vol.64 , pp. 4321-4328
    • Luo, G.1    Taylor, J.2
  • 136
    • 0011951305 scopus 로고
    • Alternation of localisation of dimer linkage structure sequence in retroviral RNA: Little effect on replication or homologous recombination
    • Jones JS, Allan RW, Temin HM. Alternation of localisation of dimer linkage structure sequence in retroviral RNA: little effect on replication or homologous recombination. J Virol. 67:1993;3551-3558.
    • (1993) J Virol , vol.67 , pp. 3551-3558
    • Jones, J.S.1    Allan, R.W.2    Temin, H.M.3
  • 137
    • 0030053532 scopus 로고    scopus 로고
    • The recombination rate is not increased when retroviral RNA is missing an encapsidation sequence
    • Zhang J, Temin HM. The recombination rate is not increased when retroviral RNA is missing an encapsidation sequence. J Virol. 70:1996;2019-2021.
    • (1996) J Virol , vol.70 , pp. 2019-2021
    • Zhang, J.1    Temin, H.M.2
  • 138
    • 0030053312 scopus 로고    scopus 로고
    • A preferred region for recombinational patch repair in the 5′ untranslated region of primer binding site-impaired murine leukemia virus vectors
    • Mikkelsen JG, Lund AH, Kristensen KD, Duch M, Sorensen MS, Jorgensen P, Pedersen FS. A preferred region for recombinational patch repair in the 5′ untranslated region of primer binding site-impaired murine leukemia virus vectors. J Virol. 70:1996;1439-1447.
    • (1996) J Virol , vol.70 , pp. 1439-1447
    • Mikkelsen, J.G.1    Lund, A.H.2    Kristensen, K.D.3    Duch, M.4    Sorensen, M.S.5    Jorgensen, P.6    Pedersen, F.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.