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Volumn 70, Issue 10, 1996, Pages 7132-7142

Human immunodeficiency virus type 1 nucleocapsid protein reduces reverse transcriptase pausing at a secondary structure near the murine leukemia virus polypurine tract

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOPROTEIN; RNA DIRECTED DNA POLYMERASE;

EID: 0029794295     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.10.7132-7142.1996     Document Type: Article
Times cited : (139)

References (81)
  • 1
    • 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., and R. A. Young. 1990. Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus. J. Virol. 64:1920-1926.
    • (1990) J. Virol. , vol.64 , pp. 1920-1926
    • Aldovini, A.1    Young, R.A.2
  • 2
    • 0028057881 scopus 로고
    • Transactivation of the minus-strand DNA transfer by nucleocapsid protein during reverse transcription of the retroviral genome
    • Allain, B., M. Lapadat-Tapolsky, C. Berlioz, and J.-L. Darlix. 1994. Transactivation of the minus-strand DNA transfer by nucleocapsid protein during reverse transcription of the retroviral genome. EMBO J. 13:973-981.
    • (1994) EMBO J. , vol.13 , pp. 973-981
    • Allain, B.1    Lapadat-Tapolsky, M.2    Berlioz, C.3    Darlix, J.-L.4
  • 3
    • 0028803233 scopus 로고
    • Analysis of primer extension and the first template switch during human immunodeficiency virus reverse transcription
    • Arts, E. J., Z. Li, and M. A. Wainberg. 1995. Analysis of primer extension and the first template switch during human immunodeficiency virus reverse transcription. J. Biomed. Sci. 2:314-321.
    • (1995) J. Biomed. Sci. , vol.2 , pp. 314-321
    • Arts, E.J.1    Li, Z.2    Wainberg, M.A.3
  • 4
    • 0022695021 scopus 로고
    • Potential metal-binding domains in nucleic acid binding proteins
    • Berg, J. 1986. Potential metal-binding domains in nucleic acid binding proteins. Science 232:485-487.
    • (1986) Science , vol.232 , pp. 485-487
    • Berg, J.1
  • 5
    • 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, R. D., J. Luban, and S. P. Goff. 1993. Specific binding of human immunodeficiency virus type 1 gag polyprotein and nucleocapsid protein to viral RNAs detected by RNA mobility shift assays. J. Virol. 67:7190-7200.
    • (1993) J. Virol. , vol.67 , pp. 7190-7200
    • Berkowitz, R.D.1    Luban, J.2    Goff, S.P.3
  • 6
    • 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., Å. Ohagen, S. Höglund, and S. P. Goff. 1995. Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric Gag polyproteins during RNA packaging in vivo. J. Virol. 69:6445-6456.
    • (1995) J. Virol. , vol.69 , pp. 6445-6456
    • Berkowitz, R.D.1    Ohagen, Å.2    Höglund, S.3    Goff, S.P.4
  • 7
    • 0028355964 scopus 로고
    • Facilitation of hammerhead ribozyme catalysis by the nucleocapsid protein of HIV-1 and the heterogeneous nuclear ribonucleoprotein A1
    • Bertrand, E. L., and J. J. Rossi. 1994. Facilitation of hammerhead ribozyme catalysis by the nucleocapsid protein of HIV-1 and the heterogeneous nuclear ribonucleoprotein A1. EMBO J. 13:2904-2912.
    • (1994) EMBO J. , vol.13 , pp. 2904-2912
    • Bertrand, E.L.1    Rossi, J.J.2
  • 8
    • 0026592529 scopus 로고
    • Tightly bound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type I, and other retroviruses
    • Bess, J. W., Jr., P. J. Powell, H. J. Issaq, L. J. Schumack, M. K. Grimes, L. E. Henderson, and L. O. Arthur. 1992. Tightly bound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type I, and other retroviruses. J. Virol. 66:840-847.
    • (1992) J. Virol. , vol.66 , pp. 840-847
    • Bess Jr., 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
  • 9
    • 0000553844 scopus 로고
    • Roles of ribonuclease H in reverse transcription
    • A. M. Skalka and S. P. Goff (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Champoux, J. J. 1993. Roles of ribonuclease H in reverse transcription, p. 103-117. In A. M. Skalka and S. P. Goff (ed.), Reverse transcriptase. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1993) Reverse Transcriptase , pp. 103-117
    • Champoux, J.J.1
  • 11
    • 0038138843 scopus 로고
    • Native ribonucleoprotein is an efficient transcriptional complex of avian myeloblastosis virus
    • Chen, M.-J., C. F. Garon, and T. S. Papas. 1980. Native ribonucleoprotein is an efficient transcriptional complex of avian myeloblastosis virus. Proc. Natl. Acad. Sci. USA 77:1296-1300.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1296-1300
    • Chen, M.-J.1    Garon, C.F.2    Papas, T.S.3
  • 12
    • 0029120982 scopus 로고
    • Divalent cation modulation of the ribonuclease functions of human immunodeficiency virus reverse transcriptase
    • Cirino, N. M., C. E. Cameron, J. S. Smith, J. W. Rausch, M. J. Roth, S. J. Benkovic, and S. F. J. Le Grice. 1995. Divalent cation modulation of the ribonuclease functions of human immunodeficiency virus reverse transcriptase. Biochemistry 34:9936-9943.
    • (1995) Biochemistry , vol.34 , pp. 9936-9943
    • Cirino, N.M.1    Cameron, C.E.2    Smith, J.S.3    Rausch, J.W.4    Roth, M.J.5    Benkovic, S.J.6    Le Grice, S.F.J.7
  • 13
    • 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., C. Sassetti, and T. G. Parslow. 1995. RNA secondary structure and binding sites for gag gene products in the 5′ packaging signal of human immunodeficiency virus type 1. J. Virol. 69:2101-2109.
    • (1995) J. Virol. , vol.69 , pp. 2101-2109
    • Clever, J.1    Sassetti, C.2    Parslow, T.G.3
  • 14
    • 0023055867 scopus 로고
    • Amino acid sequence homology in gag region of reverse transcribing elements and the coat protein gene of cauliflower mosaic virus
    • Covey, S. N. 1986. Amino acid sequence homology in gag region of reverse transcribing elements and the coat protein gene of cauliflower mosaic virus. Nucleic Acids Res. 14:623-633.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 623-633
    • Covey, S.N.1
  • 15
    • 0028326844 scopus 로고
    • Specific binding of HIV-1 nucleocapsid protein to PSI RNA in vitro requires N-terminal zinc finger and flanking basic amino acid residues
    • Dannull, J., A. Surovoy, G. Jung, and K. Moelling. 1994. Specific binding of HIV-1 nucleocapsid protein to PSI RNA in vitro requires N-terminal zinc finger and flanking basic amino acid residues. EMBO J. 13:1525-1533.
    • (1994) EMBO J. , vol.13 , pp. 1525-1533
    • Dannull, J.1    Surovoy, A.2    Jung, G.3    Moelling, K.4
  • 16
    • 0025598002 scopus 로고
    • Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1
    • Darlix, J. L., C. Gabus, M.-T. Nugeyre, F. Clavel, and F. Barré-Sinoussi. 1990. Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1. J. Mol. Biol. 216:689-699.
    • (1990) J. Mol. Biol. , vol.216 , pp. 689-699
    • Darlix, J.L.1    Gabus, C.2    Nugeyre, M.-T.3    Clavel, F.4    Barré-Sinoussi, F.5
  • 17
    • 0029585377 scopus 로고
    • First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses
    • Darlix, J.-L., M. Lapadat-Tapolsky, H. de Rocquigny, and B. P. Roques. 1995. First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses. J. Mol. Biol. 254:523-537.
    • (1995) J. Mol. Biol. , vol.254 , pp. 523-537
    • Darlix, J.-L.1    Lapadat-Tapolsky, M.2    De Rocquigny, H.3    Roques, B.P.4
  • 18
    • 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., C. Gabus, A. Vincent, M.-C. Fournié-Zaluski, B. Roques, and J.-L. Darlix. 1992. 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 89:6472-6476.
    • (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.5    Darlix, J.-L.6
  • 19
    • 0028836727 scopus 로고
    • Human immunodeficiency virus nucleocapsid protein stimulates strand transfer from internal regions of heteropolymeric RNA templates
    • DeStefano, J. J. 1995. Human immunodeficiency virus nucleocapsid protein stimulates strand transfer from internal regions of heteropolymeric RNA templates. Arch. Virol. 140:1775-1789.
    • (1995) Arch. Virol. , vol.140 , pp. 1775-1789
    • DeStefano, J.J.1
  • 20
    • 0026742224 scopus 로고
    • Parameters that influence processive synthesis and site-specific termination by human immunodeficiency virus reverse transcriptase on RNA and DNA templates
    • DeStefano, J. J., R. G. Buiser, L. M. Mallaber, P. J. Fay, and R. A. Bambara. 1992. Parameters that influence processive synthesis and site-specific termination by human immunodeficiency virus reverse transcriptase on RNA and DNA templates. Biochim. Biophys. Acta 1131:270-280.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 270-280
    • DeStefano, J.J.1    Buiser, R.G.2    Mallaber, L.M.3    Fay, P.J.4    Bambara, R.A.5
  • 21
    • 0027411503 scopus 로고
    • Retroviral nucleocapsid proteins possess potent nucleic acid strand renaturation activity
    • Dib-Hajj, F., R. Khan, and D. P. Giedroc. 1993. Retroviral nucleocapsid proteins possess potent nucleic acid strand renaturation activity. Protein Sci. 2:231-243.
    • (1993) Protein Sci. , vol.2 , pp. 231-243
    • Dib-Hajj, F.1    Khan, R.2    Giedroc, D.P.3
  • 22
    • 0027220120 scopus 로고
    • Mapping of functionally important residues of a cysteinc-histidine box in the human immunodeficiency virus type 1 nucleocapsid protein
    • Dorfman, T., J. Luban, S. P. Goff, W. Haseltine, and H. G. Göttlinger. 1993. Mapping of functionally important residues of a cysteinc-histidine box in the human immunodeficiency virus type 1 nucleocapsid protein. J. Virol. 67:6159-6169.
    • (1993) J. Virol. , vol.67 , pp. 6159-6169
    • Dorfman, T.1    Luban, J.2    Goff, S.P.3    Haseltine, W.4    Göttlinger, H.G.5
  • 23
    • 0025155072 scopus 로고
    • Point mutations in the proximal Cys-His box of Rous sarcoma virus nucleocapsid protein
    • Dupraz, P., S. Oertle, C. Méric, P. Damay, and P.-F. Spahr. 1990. Point mutations in the proximal Cys-His box of Rous sarcoma virus nucleocapsid protein. J. Virol. 64:4978-4987.
    • (1990) J. Virol. , vol.64 , pp. 4978-4987
    • Dupraz, P.1    Oertle, S.2    Méric, C.3    Damay, P.4    Spahr, P.-F.5
  • 24
    • 0026765458 scopus 로고
    • Specificity of Rous sarcoma virus nucleocapsid protein in genomic RNA packaging
    • Dupraz, P., and P.-F. Spahr. 1992. Specificity of Rous sarcoma virus nucleocapsid protein in genomic RNA packaging. J. Virol. 66:4662-4670.
    • (1992) J. Virol. , vol.66 , pp. 4662-4670
    • Dupraz, P.1    Spahr, P.-F.2
  • 26
    • 0015730617 scopus 로고
    • Isolation of a ribonucleoprotein structure from oncornaviruses
    • Fleissner, E., and E. Tress. 1973. Isolation of a ribonucleoprotein structure from oncornaviruses. J. Virol. 12:1612-1615.
    • (1973) J. Virol. , vol.12 , pp. 1612-1615
    • Fleissner, E.1    Tress, E.2
  • 27
    • 0028338652 scopus 로고
    • Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protcasedefective virions
    • Fu, W., R. J. Gorelick, and A. Rein. 1994. Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protcasedefective virions. J. Virol. 68:5013-5018.
    • (1994) J. Virol. , vol.68 , pp. 5013-5018
    • Fu, W.1    Gorelick, R.J.2    Rein, A.3
  • 28
    • 0027176378 scopus 로고
    • Maturation of dimeric viral RNA of Moloney murine leukemia virus
    • Fu, W., and A. Rein. 1993. Maturation of dimeric viral RNA of Moloney murine leukemia virus. J. Virol. 67:5443-5449.
    • (1993) J. Virol. , vol.67 , pp. 5443-5449
    • Fu, W.1    Rein, A.2
  • 29
    • 0025924750 scopus 로고
    • Reverse transcriptase : RNase H from the human immunodeficiency virus. Relationship of the DNA polymerase and RNA hydrolysis activities
    • Furfine, E. S., and J. E. Reardon. 1991. Reverse transcriptase : RNase H from the human immunodeficiency virus. Relationship of the DNA polymerase and RNA hydrolysis activities. J. Biol. Chem. 266:406-412.
    • (1991) J. Biol. Chem. , vol.266 , pp. 406-412
    • Furfine, E.S.1    Reardon, J.E.2
  • 30
    • 0026448638 scopus 로고
    • Human immunodeficiency virus type 1 reverse transcriptase: Spatial and temporal relationship between the polymerase and RNase H activities
    • Gopalakrishnan, V., J. A. Pelisku, and S. J. Benkovic. 1992. Human immunodeficiency virus type 1 reverse transcriptase: spatial and temporal relationship between the polymerase and RNase H activities. Proc. Natl. Acad. Sci. USA 89:10763-10767.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10763-10767
    • Gopalakrishnan, V.1    Pelisku, J.A.2    Benkovic, S.J.3
  • 31
    • 0029986494 scopus 로고    scopus 로고
    • Genetic analysis of the zinc linger in the Moloney murine leukemia virus nucleocapsid domain: Replacement of zinccoordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA
    • Gorelick, R. J., D. J. Chabot, D. E. Ott, T. D. Gagliardi, A. Rein, L. E. Henderson, and L. O. Arthur. 1996. Genetic analysis of the zinc linger in the Moloney murine leukemia virus nucleocapsid domain: replacement of zinccoordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA. J. Virol. 70:2593-2597.
    • (1996) J. Virol. , vol.70 , pp. 2593-2597
    • Gorelick, R.J.1    Chabot, D.J.2    Ott, D.E.3    Gagliardi, T.D.4    Rein, A.5    Henderson, L.E.6    Arthur, L.O.7
  • 32
    • 0027197020 scopus 로고
    • The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent
    • Gorelick, R. J., D. J. Chabot, A. Rein, L. E. Henderson, and L. O. Arthur. 1993. The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent. J. Virol. 67:4027-4036.
    • (1993) J. Virol. , vol.67 , pp. 4027-4036
    • Gorelick, R.J.1    Chabot, D.J.2    Rein, A.3    Henderson, L.E.4    Arthur, L.O.5
  • 33
    • 0024110320 scopus 로고
    • Point mutants of Moloney murine leukemia virus that fail to package viral RNA: Evidence for specific RNA recognition hy a "zinc finger-like" protein sequence
    • Gorelick, R. J., L. E. Henderson, J. P. Hanser, and A. Rein. 1988. Point mutants of Moloney murine leukemia virus that fail to package viral RNA: evidence for specific RNA recognition hy a "zinc finger-like" protein sequence. Proc. Natl. Acad. Sci. USA 85:8420-8424.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8420-8424
    • Gorelick, R.J.1    Henderson, L.E.2    Hanser, J.P.3    Rein, A.4
  • 35
    • 0028956355 scopus 로고
    • Defects in primer-template binding. processive DNA synthesis, and RNase H activity associated with chimeric reverse transcriptases having the murine leukemia virus polymerase domain joined to Eschmchia coli RNase H
    • Guo, J., W. Wu, Z. Y. Yuan, K. Post, R. J. Crouch, and J. G. Levin. 1995 Defects in primer-template binding. processive DNA synthesis, and RNase H activity associated with chimeric reverse transcriptases having the murine leukemia virus polymerase domain joined to Eschmchia coli RNase H. Biochemistry 34:5018-5029.
    • (1995) Biochemistry , vol.34 , pp. 5018-5029
    • Guo, J.1    Wu, W.2    Yuan, Z.Y.3    Post, K.4    Crouch, R.J.5    Levin, J.G.6
  • 36
  • 37
    • 0026515142 scopus 로고
    • Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: Posttranslational modifications, proteolytic processings, and complete amino acid sequences
    • Henderson, L. E., M. A. Bowers, R. C. Sowder II, S. A. Serabyn, D. G. Johnson, J. W. Bess, Jr., L. O. Arthur, D. K. Bryant, and C. Fenselau. 1992 Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processings, and complete amino acid sequences. J. Virol. 66:1856-1865.
    • (1992) J. Virol. , vol.66 , pp. 1856-1865
    • Henderson, L.E.1    Bowers, M.A.2    Sowder II, R.C.3    Serabyn, S.A.4    Johnson, D.G.5    Bess Jr., J.W.6    Arthur, L.O.7    Bryant, D.K.8    Fenselau, C.9
  • 38
    • 9544246610 scopus 로고
    • Amino acid sequences of retroviral structural proteins
    • appendix F, R. Weiss, N. Teich, H. Varmus, and J. Coffin (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Henderson, L. E., T. D. Copeland, G. W. Smythers, R. C. Sowder, and S. Oroszlan. 1982. Amino acid sequences of retroviral structural proteins, appendix F, p. 1377-1382. In R. Weiss, N. Teich, H. Varmus, and J. Coffin (ed.), Molecular biology of tumor viruses. RNA tumor viruses, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1982) Molecular Biology of Tumor Viruses. RNA Tumor Viruses, 2nd Ed. , pp. 1377-1382
    • Henderson, L.E.1    Copeland, T.D.2    Smythers, G.W.3    Sowder, R.C.4    Oroszlan, S.5
  • 39
    • 0019786215 scopus 로고
    • Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses
    • Henderson, L. E., T. D. Copeland, R. C. Sowder, G. W. Smythers, and S. Oroszlan. 1981. Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses. J. Biol. Chem. 256:8400-8406.
    • (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
  • 40
    • 0021365594 scopus 로고
    • Nucleotide sequence of AKV murine leukemia virus
    • Herr, W. 1984. Nucleotide sequence of AKV murine leukemia virus. J. Virol. 49:471-478.
    • (1984) J. Virol. , vol.49 , pp. 471-478
    • Herr, W.1
  • 41
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag, D. 1995. RNA chaperones and the RNA folding problem. J. Biol. Chem. 270:20871-20874.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 42
    • 0028216716 scopus 로고
    • An RNA chaperone activity of non-specific RNA binding proteins in hammerhead ribozyme catalysis
    • Herschlag, D., M. Khosla, Z. Tsuchihashi, and R. L. Karpel. 1994. An RNA chaperone activity of non-specific RNA binding proteins in hammerhead ribozyme catalysis. EMBO J. 13:2913-2924.
    • (1994) EMBO J. , vol.13 , pp. 2913-2924
    • Herschlag, D.1    Khosla, M.2    Tsuchihashi, Z.3    Karpel, R.L.4
  • 43
    • 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., H. De Rocquigny, B. P. Roques, and J.-L. Darlix. 1993. Basic amino acids flanking the zinc finger of Moloney murine leukemia virus nucleocapsid protein NCp10 are critical for virus infectivity. J. Virol. 67: 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
  • 44
    • 0030067973 scopus 로고    scopus 로고
    • Effect of human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein on HIV-1 reverse transcriptase activity in vitro
    • Ji, X., G. J. Klarmann, and B. D. Preston. 1996. Effect of human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein on HIV-1 reverse transcriptase activity in vitro. Biochemistry 35:132-143.
    • (1996) Biochemistry , vol.35 , pp. 132-143
    • Ji, X.1    Klarmann, G.J.2    Preston, B.D.3
  • 45
    • 0023654385 scopus 로고
    • Interactions of retroviral structural proteins with single-stranded nucleic acids
    • Karpel, R. L., L. E. Henderson, and S. Oroszlan. 1987. Interactions of retroviral structural proteins with single-stranded nucleic acids. J. Biol. Chem. 262:4961-4967.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4961-4967
    • Karpel, R.L.1    Henderson, L.E.2    Oroszlan, S.3
  • 48
    • 0027238697 scopus 로고
    • Template-directed pausing of DNA synthesis by HIV-1 reverse transcriptase during polymerization of HIV-1 sequences in vitro
    • Klarmann, G. J., C. A. Schauber, and B. D. Preston. 1993. Template-directed pausing of DNA synthesis by HIV-1 reverse transcriptase during polymerization of HIV-1 sequences in vitro. J. Biol. Chem. 268:9793-9802.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9793-9802
    • Klarmann, G.J.1    Schauber, C.A.2    Preston, B.D.3
  • 49
    • 0027964450 scopus 로고
    • Phosphorescence and optically detected magnetic resonance investigation of the binding of the nucleocapsid protein of the human immunodeficiency virus type 1 and related peptides to RNA
    • Lam, W.-C., A. H. Maki, J. R. Casas-Finet, J. W. Erickson, B. P. Kane, R. C. Sowder II, and L. E. Henderson. 1994. Phosphorescence and optically detected magnetic resonance investigation of the binding of the nucleocapsid protein of the human immunodeficiency virus type 1 and related peptides to RNA. Biochemistry 33:10693-10700.
    • (1994) Biochemistry , vol.33 , pp. 10693-10700
    • Lam, W.-C.1    Maki, A.H.2    Casas-Finet, J.R.3    Erickson, J.W.4    Kane, B.P.5    Sowder II, R.C.6    Henderson, L.E.7
  • 50
    • 0027320154 scopus 로고
    • Evidence for stacking interactions between 5-mercurated polyuridylic acid and HIV-1 p7 nucleocapsid protein obtained by phosphorescence and optically detected magnetic resonance (ODMR)
    • Lam, W.-C., A. H. Maki, J. R. Casas-Finet, J. W. Erickson, R. C. Sowder II, and L. E. Henderson. 1993. Evidence for stacking interactions between 5-mercurated polyuridylic acid and HIV-1 p7 nucleocapsid protein obtained by phosphorescence and optically detected magnetic resonance (ODMR). FEBS Lett. 328:45-48.
    • (1993) FEBS Lett. , vol.328 , pp. 45-48
    • Lam, W.-C.1    Maki, A.H.2    Casas-Finet, J.R.3    Erickson, J.W.4    Sowder II, R.C.5    Henderson, L.E.6
  • 51
    • 0027258736 scopus 로고
    • Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle
    • Lapadat-Tapolsky, M., H. De Rocquigny, D. Van Gent, B. Roques, R. Plasterk, and J.-L. Darlix. 1993. Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle. Nucleic Acids Res. 21:831-839.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 831-839
    • Lapadat-Tapolsky, M.1    De Rocquigny, H.2    Van Gent, D.3    Roques, B.4    Plasterk, R.5    Darlix, J.-L.6
  • 52
    • 0029044016 scopus 로고
    • Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1
    • Lapadat-Tapolsky, M., C. Pernelle, C. Borie, and J.-L. Darlix. 1995. Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1. Nucleic Acids Res. 23:2434-2441.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2434-2441
    • Lapadat-Tapolsky, M.1    Pernelle, C.2    Borie, C.3    Darlix, J.-L.4
  • 53
    • 0023695043 scopus 로고
    • Functional organization of the murine leukemia virus reverse transcriptase: Characterization of a bacterially expressed AKR DNA polymerase deficient in RNase H activity
    • Levin, J. G., R. J. Crouch, K. Post, S. C. Hu, D. McKelvin, M. Zweig, D. L. Court, and B. I. Gerwin. 1988. Functional organization of the murine leukemia virus reverse transcriptase: characterization of a bacterially expressed AKR DNA polymerase deficient in RNase H activity. J. Virol. 62:4376-4380.
    • (1988) J. Virol. , vol.62 , pp. 4376-4380
    • Levin, J.G.1    Crouch, R.J.2    Post, K.3    Hu, S.C.4    McKelvin, D.5    Zweig, M.6    Court, D.L.7    Gerwin, B.I.8
  • 54
    • 0023874836 scopus 로고
    • Analysis of the primary structure of the long terminal repeat and the gag and pol genes of the human spumaretrovirus
    • Maurer, B., H. Bannert, G. Darai, and R. M. Flügel. 1988. Analysis of the primary structure of the long terminal repeat and the gag and pol genes of the human spumaretrovirus. J. Virol. 62:1590-1597.
    • (1988) J. Virol. , vol.62 , pp. 1590-1597
    • Maurer, B.1    Bannert, H.2    Darai, G.3    Flügel, R.M.4
  • 55
    • 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., F. Cornille, M.-C. Fournié-Zaluski, J.-L. Darlix, B. P. Roques, and D. Gerard. 1991. Investigation of zinc-binding affinities of Moloney murine leukemia virus nucleocapsid protein and its related zinc finger and modified peptides. Biopolymers 31:899-906.
    • (1991) Biopolymers , vol.31 , pp. 899-906
    • Mély, Y.1    Cornille, F.2    Fournié-Zaluski, M.-C.3    Darlix, J.-L.4    Roques, B.P.5    Gerard, D.6
  • 56
    • 0024507854 scopus 로고
    • Characterization of Moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein
    • Méric, C., and S. P. Goff. 1989. Characterization of Moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein. J. Virol. 63:1558-1568.
    • (1989) J. Virol. , vol.63 , pp. 1558-1568
    • Méric, C.1    Goff, S.P.2
  • 57
    • 0023801716 scopus 로고
    • Mutations in Rous sarcoma virus nucleocapsid protein p12 (NC): Deletions of Cys-His boxes
    • Méric, C., E. Gouilloud, and P.-F. Spahr. 1988. Mutations in Rous sarcoma virus nucleocapsid protein p12 (NC): deletions of Cys-His boxes, J. Virol. 62:3328-3333.
    • (1988) J. Virol. , vol.62 , pp. 3328-3333
    • Méric, C.1    Gouilloud, E.2    Spahr, P.-F.3
  • 58
    • 0022978019 scopus 로고
    • Rous sarcoma virus nucleic acid-binding protein p12 is necessary for viral 70S RNA dimer formation and packaging
    • Méric, C., and P.-F. Spahr. 1986. Rous sarcoma virus nucleic acid-binding protein p12 is necessary for viral 70S RNA dimer formation and packaging. J. Virol. 60:450-459.
    • (1986) J. Virol. , vol.60 , pp. 450-459
    • Méric, C.1    Spahr, P.-F.2
  • 59
    • 0022004872 scopus 로고
    • Functional analysis of reverse transcription by a frameshift pol mutant of murine leukemia virus
    • Messer, L. I., K. M. Currey, B. J. O'Neill, J. V. Maizel, Jr., J. G. Levin, and B. I. Gerwin. 1985. Functional analysis of reverse transcription by a frameshift pol mutant of murine leukemia virus. Virology 146:146-152.
    • (1985) Virology , vol.146 , pp. 146-152
    • Messer, L.I.1    Currey, K.M.2    O'Neill, B.J.3    Maizel Jr., J.V.4    Levin, J.G.5    Gerwin, B.I.6
  • 60
    • 0027986960 scopus 로고
    • Amino acid requirements of the nucleocapsid protein of HIV-1 for increasing catalytic activity of a Ki-ras ribozyme in vitro
    • Müller, G., B. Strack, J. Dannull, B. S. Sproat, A. Surovoy, G. Jung, and K. Moelling. 1994. Amino acid requirements of the nucleocapsid protein of HIV-1 for increasing catalytic activity of a Ki-ras ribozyme in vitro. J. Mol. Biol. 242:422-429.
    • (1994) J. Mol. Biol. , vol.242 , pp. 422-429
    • Müller, G.1    Strack, B.2    Dannull, J.3    Sproat, B.S.4    Surovoy, A.5    Jung, G.6    Moelling, K.7
  • 61
    • 84937346333 scopus 로고
    • Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activity
    • Peliska, J. A., S. Balasubramanian, D. P. Giedroc, and S. J. Benkovic. 1994. Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activity. Biochemistry 33:13817-13823.
    • (1994) Biochemistry , vol.33 , pp. 13817-13823
    • Peliska, J.A.1    Balasubramanian, S.2    Giedroc, D.P.3    Benkovic, S.J.4
  • 62
    • 0026486193 scopus 로고
    • Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase
    • Peliska, J. A., and S. J. Benknvic. 1992. Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase. Science 258:1112-1118.
    • (1992) Science , vol.258 , pp. 1112-1118
    • Peliska, J.A.1    Benknvic, S.J.2
  • 63
    • 0027157093 scopus 로고
    • A large deletion in the connection subdomain of murine leukemia virus reverse transcriptase or replacement of the RNase H domain with Escherichia coli RNase H results in altered polymerase and RNase H activities
    • Post, K., J. Guo, E. Kalman, T. Uchida, R. J. Crouch, and J. G. Levin. 1993. A large deletion in the connection subdomain of murine leukemia virus reverse transcriptase or replacement of the RNase H domain with Escherichia coli RNase H results in altered polymerase and RNase H activities. Biochemistry 32:5508-5517.
    • (1993) Biochemistry , vol.32 , pp. 5508-5517
    • Post, K.1    Guo, J.2    Kalman, E.3    Uchida, T.4    Crouch, R.J.5    Levin, J.G.6
  • 64
    • 0025773436 scopus 로고
    • Viral RNA annealing activities of the nucleocapsid protein of Moloney murine leukemia virus are zinc independent
    • Prats, A.-C., V. Housset, G. de Billy, F. Cornille, H. Prats, B. Roques, and J.-L. Darlix. 1991. Viral RNA annealing activities of the nucleocapsid protein of Moloney murine leukemia virus are zinc independent. Nucleic Acids Res. 19:3533-3541.
    • (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
  • 65
    • 0030013723 scopus 로고    scopus 로고
    • Inactivation of murine leukemia virus by compounds that react with the zinc finger in the viral nucleocapsid protein
    • Rein, A., D. E. Oil, J. Mirro, L. O. Arthur, W. Rice, and L. E. Henderson. 1996. Inactivation of murine leukemia virus by compounds that react with the zinc finger in the viral nucleocapsid protein. J. Virol. 70:4966-4972.
    • (1996) J. Virol. , vol.70 , pp. 4966-4972
    • Rein, A.1    Oil, D.E.2    Mirro, J.3    Arthur, L.O.4    Rice, W.5    Henderson, L.E.6
  • 67
    • 0029009007 scopus 로고
    • Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vito
    • Rodriguez-Rodriguez, L., Z. Tsuchihashi. G. M. Fuentes, R. A. Bambara, and P. J. Fay. 1995. Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vito. J. Biol. Chem. 270:15005-15011.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15005-15011
    • Rodriguez-Rodriguez, L.1    Tsuchihashi, Z.2    Fuentes, G.M.3    Bambara, R.A.4    Fay, P.J.5
  • 68
    • 0030028806 scopus 로고    scopus 로고
    • Mutations of basic amino acids of NCp7 of human immunodeficiency virus type 1 affect RNA binding in vitro
    • Schmalzbauer, E., B. Strack, J. Dannull, S. Guehmann, and K. Moelling. 1996. Mutations of basic amino acids of NCp7 of human immunodeficiency virus type 1 affect RNA binding in vitro. J. Virol. 70:771-777.
    • (1996) J. Virol. , vol.70 , pp. 771-777
    • Schmalzbauer, E.1    Strack, B.2    Dannull, J.3    Guehmann, S.4    Moelling, K.5
  • 69
    • 0025142952 scopus 로고
    • The nucleocapsid protein isolated from HIV-1 particles hinds zinc and forms retroviral-type zinc fingers
    • South, T. L., P. R. Blake, R. C. Sowder III, L. O. Arthur, L. E. Henderson, and M. F. Summers. 1990. The nucleocapsid protein isolated from HIV-1 particles hinds zinc and forms retroviral-type zinc fingers. Biochemistry 29: 7786-7789.
    • (1990) Biochemistry , vol.29 , pp. 7786-7789
    • South, T.L.1    Blake, P.R.2    Sowder III, R.C.3    Arthur, L.O.4    Henderson, L.E.5    Summers, M.F.6
  • 71
    • 0027464411 scopus 로고
    • Conformational and nucleic acid binding studies on the synthetic nucleocapsid protein of HIV-1
    • Surovoy, A., J. Dannull, K. Moelling, and G. Jung. 1993. Conformational and nucleic acid binding studies on the synthetic nucleocapsid protein of HIV-1. J. Mol. Biol. 229:94-104.
    • (1993) J. Mol. Biol. , vol.229 , pp. 94-104
    • Surovoy, A.1    Dannull, J.2    Moelling, K.3    Jung, G.4
  • 72
    • 0019777933 scopus 로고
    • Properties of the avian viral protein p12
    • Sykora, K. W., and K. Moelling. 1981. Properties of the avian viral protein p12. J. Gen. Virol. 55:379-391.
    • (1981) J. Gen. Virol. , vol.55 , pp. 379-391
    • Sykora, K.W.1    Moelling, K.2
  • 73
    • 0029121697 scopus 로고
    • Formation of stable and functional HIV-1 nucleoprotein complexes in vitro
    • Tanchou, V., C. Gabus, V. Rogemond, and J.-L. Darlix. 1995. Formation of stable and functional HIV-1 nucleoprotein complexes in vitro. J. Mol. Biol. 252:563-571.
    • (1995) J. Mol. Biol. , vol.252 , pp. 563-571
    • Tanchou, V.1    Gabus, C.2    Rogemond, V.3    Darlix, J.-L.4
  • 74
    • 0027518740 scopus 로고
    • RNase H domain mutations affect the interaction between Moloney murine leukemia virus reverse transcriptase and its primer-template
    • Telesnitsky, A., and S. P. Goff. 1993. RNase H domain mutations affect the interaction between Moloney murine leukemia virus reverse transcriptase and its primer-template. Proc. Natl. Acad. Sci. USA 90:1276-1280.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1276-1280
    • Telesnitsky, A.1    Goff, S.P.2
  • 75
    • 0028129970 scopus 로고
    • DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein
    • Tsuchihashi, Z., and P. O. Brown. 1994. DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein. J. Virol. 68:5863-5870.
    • (1994) J. Virol. , vol.68 , pp. 5863-5870
    • Tsuchihashi, Z.1    Brown, P.O.2
  • 76
    • 0027370258 scopus 로고
    • Protein enhancement of hammerhead ribozyme catalysis
    • Tsuchihashi, Z., M. Khosla, and D. Herschlag. 1993. Protein enhancement of hammerhead ribozyme catalysis. Science 262:99-102.
    • (1993) Science , vol.262 , pp. 99-102
    • Tsuchihashi, Z.1    Khosla, M.2    Herschlag, D.3
  • 77
    • 0000376143 scopus 로고
    • Replication of retroviruses
    • R. Weiss, N. Teich, H. Varmus, and J. Coffin (ed.). Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Varmus, H., and R. Swanstrom. 1984. Replication of retroviruses. p. 369-512. In R. Weiss, N. Teich, H. Varmus, and J. Coffin (ed.). Molecular biology of tumor viruses, RNA tumor viruses, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1984) Molecular Biology of Tumor Viruses, RNA Tumor Viruses, 2nd Ed. , pp. 369-512
    • Varmus, H.1    Swanstrom, R.2
  • 78
    • 0027246189 scopus 로고
    • The polypurine tract, PPT, of HIV as target for antisense and triple-helix-forming oligonucleotides
    • Volkmann, S., J. Dannull, and K. Moelling. 1993. The polypurine tract, PPT, of HIV as target for antisense and triple-helix-forming oligonucleotides. Biochimie 75:71-78.
    • (1993) Biochimie , vol.75 , pp. 71-78
    • Volkmann, S.1    Dannull, J.2    Moelling, K.3
  • 79
    • 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., B. Konig, Y. Morikawa, and I. Jones. 1992. 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 121:203-212.
    • (1992) Gene , vol.121 , pp. 203-212
    • Weiss, S.1    Konig, B.2    Morikawa, Y.3    Jones, I.4
  • 80
    • 0028113905 scopus 로고
    • Human immunodeficiency virus nucleocapsid protein accelerates strand transfer of the terminally redundant sequences involved in reverse transcription
    • You, J. C., and C. S. McHenry. 1994. Human immunodeficiency virus nucleocapsid protein accelerates strand transfer of the terminally redundant sequences involved in reverse transcription. J. Biol. Chem. 269:31491-31495.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31491-31495
    • You, J.C.1    McHenry, C.S.2
  • 81
    • 0029149643 scopus 로고
    • Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation
    • Zhang, Y., and E. Barklis. 1995. Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation. J. Virol. 69:5716-5722.
    • (1995) J. Virol. , vol.69 , pp. 5716-5722
    • Zhang, Y.1    Barklis, E.2


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