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Volumn 356, Issue 5, 2006, Pages 1180-1192

During the early phase of HIV-1 DNA synthesis, nucleocapsid protein directs hybridization of the TAR complementary sequences via the ends of their double-stranded stem

Author keywords

Fluorescence; HIV NCp7; Hybridization; Kinetics; TAR

Indexed keywords

COMPLEMENTARY DNA; DOUBLE STRANDED DNA; FLUORESCENT DYE; NUCLEOCAPSID PROTEIN; SINGLE STRANDED DNA;

EID: 32044464549     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.12.038     Document Type: Article
Times cited : (64)

References (58)
  • 1
    • 0030047819 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 reverse transcriptase and early events in reverse transcription
    • E.J. Arts, and M.A. Wainberg Human immunodeficiency virus type 1 reverse transcriptase and early events in reverse transcription Advan. Virus Res. 46 1996 97 163
    • (1996) Advan. Virus Res. , vol.46 , pp. 97-163
    • Arts, E.J.1    Wainberg, M.A.2
  • 2
    • 0028057881 scopus 로고
    • Transactivation of the minus-strand DNA transfer by nucleocapsid protein during reverse transcription of the retroviral genome
    • B. Allain, M. Lapadat-Tapolsky, C. Berlioz, and J.L. Darlix Transactivation of the minus-strand DNA transfer by nucleocapsid protein during reverse transcription of the retroviral genome EMBO J. 13 1994 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
    • 0027367521 scopus 로고
    • Trans-activation of the 5′ to 3′ viral DNA strand transfer by nucleocapsid protein during reverse transcription of HIV1 RNA
    • J.L. Darlix, A. Vincent, C. Gabus, H. de Rocquigny, and B. Roques Trans-activation of the 5′ to 3′ viral DNA strand transfer by nucleocapsid protein during reverse transcription of HIV1 RNA C.R. Acad. Sci. III 316 1993 763 771
    • (1993) C.R. Acad. Sci. III , vol.316 , pp. 763-771
    • Darlix, J.L.1    Vincent, A.2    Gabus, C.3    De Rocquigny, H.4    Roques, B.5
  • 4
    • 0032491180 scopus 로고    scopus 로고
    • Actinomycin D inhibition of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase and nucleocapsid protein
    • W.R. Davis, S. Gabbara, D. Hupe, and J.A. Peliska Actinomycin D inhibition of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase and nucleocapsid protein Biochemistry 37 1998 14213 14221
    • (1998) Biochemistry , vol.37 , pp. 14213-14221
    • Davis, W.R.1    Gabbara, S.2    Hupe, D.3    Peliska, J.A.4
  • 5
    • 0028836727 scopus 로고
    • Human immunodeficiency virus nucleocapsid protein stimulates strand transfer from internal regions of heteropolymeric RNA templates
    • J.J. DeStefano Human immunodeficiency virus nucleocapsid protein stimulates strand transfer from internal regions of heteropolymeric RNA templates Arch. Virol. 140 1995 1775 1789
    • (1995) Arch. Virol. , vol.140 , pp. 1775-1789
    • Destefano, J.J.1
  • 6
    • 0031007620 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA
    • J. Guo, L.E. Henderson, J. Bess, B. Kane, and J.G. Levin Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA J. Virol. 71 1997 5178 5188
    • (1997) J. Virol. , vol.71 , pp. 5178-5188
    • Guo, J.1    Henderson, L.E.2    Bess, J.3    Kane, B.4    Levin, J.G.5
  • 7
    • 0033803461 scopus 로고    scopus 로고
    • Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer
    • J. Guo, T. Wu, J. Anderson, B.F. Kane, D.G. Johnson, and R.J. Gorelick Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer J. Virol. 74 2000 8980 8988
    • (2000) J. Virol. , vol.74 , pp. 8980-8988
    • Guo, J.1    Wu, T.2    Anderson, J.3    Kane, B.F.4    Johnson, D.G.5    Gorelick, R.J.6
  • 8
    • 6344294990 scopus 로고    scopus 로고
    • Alteration of nucleic acid structure and stability modulates the efficiency of minus-strand transfer mediated by the HIV-1 nucleocapsid protein
    • S.L. Heilman-Miller, T. Wu, and J.G. Levin Alteration of nucleic acid structure and stability modulates the efficiency of minus-strand transfer mediated by the HIV-1 nucleocapsid protein J. Biol. Chem. 279 2004 44154 44165
    • (2004) J. Biol. Chem. , vol.279 , pp. 44154-44165
    • Heilman-Miller, S.L.1    Wu, T.2    Levin, J.G.3
  • 9
    • 0000333554 scopus 로고    scopus 로고
    • Evidence for a unique mechanism of strand transfer from the transactivation response region of HIV-1
    • J.K. Kim, C. Palaniappan, W. Wu, P.J. Fay, and R.A. Bambara Evidence for a unique mechanism of strand transfer from the transactivation response region of HIV-1 J. Biol. Chem. 272 1997 16769 16777
    • (1997) J. Biol. Chem. , vol.272 , pp. 16769-16777
    • Kim, J.K.1    Palaniappan, C.2    Wu, W.3    Fay, P.J.4    Bambara, R.A.5
  • 10
    • 0031547959 scopus 로고    scopus 로고
    • Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability
    • M. Lapadat-Tapolsky, C. Gabus, M. Rau, and J.L. Darlix Possible roles of HIV-1 nucleocapsid protein in the specificity of proviral DNA synthesis and in its variability J. Mol. Biol. 268 1997 250 260
    • (1997) J. Mol. Biol. , vol.268 , pp. 250-260
    • Lapadat-Tapolsky, M.1    Gabus, C.2    Rau, M.3    Darlix, J.L.4
  • 11
    • 0029044016 scopus 로고
    • Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1
    • M. Lapadat-Tapolsky, C. Pernelle, C. Borie, and J.L. Darlix Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1 Nucl. Acids Res. 23 1995 2434 2441
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2434-2441
    • Lapadat-Tapolsky, M.1    Pernelle, C.2    Borie, C.3    Darlix, J.L.4
  • 12
    • 84937346333 scopus 로고
    • Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activity
    • J.A. Peliska, S. Balasubramanian, D.P. Giedroc, and S.J. Benkovic Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activity Biochemistry 33 1994 13817 13823
    • (1994) Biochemistry , vol.33 , pp. 13817-13823
    • Peliska, J.A.1    Balasubramanian, S.2    Giedroc, D.P.3    Benkovic, S.J.4
  • 13
    • 0029009007 scopus 로고
    • Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vitro
    • L. Rodriguez-Rodriguez, Z. Tsuchihashi, G.M. Fuentes, R.A. Bambara, and P.J. Fay Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vitro J. Biol. Chem 270 1995 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
  • 14
    • 0028113905 scopus 로고
    • Human immunodeficiency virus nucleocapsid protein accelerates strand transfer of the terminally redundant sequences involved in reverse transcription
    • J.C. You, and C.S. McHenry Human immunodeficiency virus nucleocapsid protein accelerates strand transfer of the terminally redundant sequences involved in reverse transcription J. Biol. Chem. 269 1994 31491 31495
    • (1994) J. Biol. Chem. , vol.269 , pp. 31491-31495
    • You, J.C.1    McHenry, C.S.2
  • 15
    • 0034565217 scopus 로고    scopus 로고
    • Multiple biological roles associated with the repeat (R) region of the HIV-1 RNA genome
    • B. Berkhout Multiple biological roles associated with the repeat (R) region of the HIV-1 RNA genome Advan. Pharmacol. 48 2000 29 73
    • (2000) Advan. Pharmacol. , vol.48 , pp. 29-73
    • Berkhout, B.1
  • 16
    • 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
    • L.E. Henderson, M.A. Bowers, R.C. Sowder 2nd, S.A. Serabyn, D.G. Johnson, and J.W. Bess Jr 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 1992 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
  • 17
    • 0023755462 scopus 로고
    • The gag gene products of human immunodeficiency virus type 1: Alignment within the gag open reading frame, identification of posttranslational modifications, and evidence for alternative gag precursors
    • R.J. Mervis, N. Ahmad, E.P. Lillehoj, M.G. Raum, F.H. Salazar, H.W. Chan, and S. Venkatesan The gag gene products of human immunodeficiency virus type 1: alignment within the gag open reading frame, identification of posttranslational modifications, and evidence for alternative gag precursors J. Virol. 62 1988 3993 4002
    • (1988) J. Virol. , vol.62 , pp. 3993-4002
    • Mervis, R.J.1    Ahmad, N.2    Lillehoj, E.P.3    Raum, M.G.4    Salazar, F.H.5    Chan, H.W.6    Venkatesan, S.7
  • 18
    • 0001118596 scopus 로고    scopus 로고
    • Retroviral gene expression: Synthesis, Assembly and Processing of Viral Proteins
    • H.E. Varmus J.M. Coffin S.H. Hughes Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • R. Swanstrom, and J.W. Wills Retroviral gene expression: Synthesis, Assembly and Processing of Viral Proteins H.E. Varmus J.M. Coffin S.H. Hughes Retroviruses 1997 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 263 334
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 19
    • 0029876943 scopus 로고    scopus 로고
    • Zinc binding to the HIV-1 nucleocapsid protein: A thermodynamic investigation by fluorescence spectroscopy
    • Y. Mely, H. De Rocquigny, N. Morellet, B.P. Roques, and D. Gerard Zinc binding to the HIV-1 nucleocapsid protein: a thermodynamic investigation by fluorescence spectroscopy Biochemistry 35 1996 5175 5182
    • (1996) Biochemistry , vol.35 , pp. 5175-5182
    • Mely, Y.1    De Rocquigny, H.2    Morellet, N.3    Roques, B.P.4    Gerard, D.5
  • 20
    • 0027077686 scopus 로고
    • Nucleocapsid zinc fingers detected in retroviruses: EXAFS studies of intact viruses and the solution-state structure of the nucleocapsid protein from HIV-1
    • M.F. Summers, L.E. Henderson, M.R. Chance, J.W. Bess Jr, and T.L. South Nucleocapsid zinc fingers detected in retroviruses: EXAFS studies of intact viruses and the solution-state structure of the nucleocapsid protein from HIV-1 Protein Sci. 1 1992 563 574
    • (1992) Protein Sci. , vol.1 , pp. 563-574
    • Summers, M.F.1    Henderson, L.E.2    Chance, M.R.3    Bess Jr., J.W.4    South, T.L.5
  • 22
    • 0026749685 scopus 로고
    • Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR
    • N. Morellet, N. Jullian, H. De Rocquigny, B. Maigret, J.L. Darlix, and B.P. Roques Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR EMBO J. 11 1992 3059 3065
    • (1992) EMBO J. , vol.11 , pp. 3059-3065
    • Morellet, N.1    Jullian, N.2    De Rocquigny, H.3    Maigret, B.4    Darlix, J.L.5    Roques, B.P.6
  • 23
    • 0026042741 scopus 로고
    • Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy
    • J.G. Omichinski, G.M. Clore, K. Sakaguchi, E. Appella, and A.M. Gronenborn Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy FEBS Letters 292 1991 25 30
    • (1991) FEBS Letters , vol.292 , pp. 25-30
    • Omichinski, J.G.1    Clore, G.M.2    Sakaguchi, K.3    Appella, E.4    Gronenborn, A.M.5
  • 24
    • 0025142952 scopus 로고
    • The nucleocapsid protein isolated from HIV-1 particles binds zinc and forms retroviral-type zinc fingers
    • T.L. South, P.R. Blake, R.C. Sowder 3rd, L.O. Arthur, L.E. Henderson, and M.F. Summers The nucleocapsid protein isolated from HIV-1 particles binds zinc and forms retroviral-type zinc fingers Biochemistry 29 1990 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
  • 26
    • 0031679786 scopus 로고    scopus 로고
    • Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: Significance for viral replication
    • A. Rein, L.E. Henderson, and J.G. Levin Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication Trends Biochem. Sci. 23 1998 297 301
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 297-301
    • Rein, A.1    Henderson, L.E.2    Levin, J.G.3
  • 27
    • 0027479628 scopus 로고
    • Functional sites in the 5′ region of human immunodeficiency virus type 1 RNA form defined structural domains
    • F. Baudin, R. Marquet, C. Isel, J.L. Darlix, B. Ehresmann, and C. Ehresmann 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.L.4    Ehresmann, B.5    Ehresmann, C.6
  • 28
    • 0033799017 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid protein can prevent self-priming of minus-strand strong stop DNA by promoting the annealing of short oligonucleotides to hairpin sequences
    • M.D. Driscoll, and S.H. Hughes Human immunodeficiency virus type 1 nucleocapsid protein can prevent self-priming of minus-strand strong stop DNA by promoting the annealing of short oligonucleotides to hairpin sequences J. Virol. 74 2000 8785 8792
    • (2000) J. Virol. , vol.74 , pp. 8785-8792
    • Driscoll, M.D.1    Hughes, S.H.2
  • 29
    • 0031926679 scopus 로고    scopus 로고
    • Actinomycin D inhibits human immunodeficiency virus type 1 minus-strand transfer in in vitro and endogenous reverse transcriptase assays
    • J. Guo, T. Wu, J. Bess, L.E. Henderson, and J.G. Levin Actinomycin D inhibits human immunodeficiency virus type 1 minus-strand transfer in in vitro and endogenous reverse transcriptase assays J. Virol. 72 1998 6716 6724
    • (1998) J. Virol. , vol.72 , pp. 6716-6724
    • Guo, J.1    Wu, T.2    Bess, J.3    Henderson, L.E.4    Levin, J.G.5
  • 30
    • 0037489501 scopus 로고    scopus 로고
    • Secondary structure in the nucleic acid affects the rate of HIV-1 nucleocapsid-mediated strand annealing
    • M.P. Golinelli, and S.H. Hughes Secondary structure in the nucleic acid affects the rate of HIV-1 nucleocapsid-mediated strand annealing Biochemistry 42 2003 8153 8162
    • (2003) Biochemistry , vol.42 , pp. 8153-8162
    • Golinelli, M.P.1    Hughes, S.H.2
  • 31
    • 0032509267 scopus 로고    scopus 로고
    • Involvement of HIV-I nucleocapsid protein in the recruitment of reverse transcriptase into nucleoprotein complexes formed in vitro
    • D. Lener, V. Tanchou, B.P. Roques, S.F. Le Grice, and J.L. Darlix Involvement of HIV-I nucleocapsid protein in the recruitment of reverse transcriptase into nucleoprotein complexes formed in vitro J. Biol. Chem. 273 1998 33781 33786
    • (1998) J. Biol. Chem. , vol.273 , pp. 33781-33786
    • Lener, D.1    Tanchou, V.2    Roques, B.P.3    Le Grice, S.F.4    Darlix, J.L.5
  • 32
    • 0033574629 scopus 로고    scopus 로고
    • Evidence of interactions between the nucleocapsid protein NCp7 and the reverse transcriptase of HIV-1
    • S. Druillennec, A. Caneparo, H. de Rocquigny, and B.P. Roques Evidence of interactions between the nucleocapsid protein NCp7 and the reverse transcriptase of HIV-1 J. Biol. Chem. 274 1999 11283 11288
    • (1999) J. Biol. Chem. , vol.274 , pp. 11283-11288
    • Druillennec, S.1    Caneparo, A.2    De Rocquigny, H.3    Roques, B.P.4
  • 33
    • 0030962706 scopus 로고    scopus 로고
    • Mutations in HIV reverse transcriptase which alter RNase H activity and decrease strand transfer efficiency are suppressed by HIV nucleocapsid protein
    • C.E. Cameron, M. Ghosh, S.F. Le Grice, and S.J. Benkovic Mutations in HIV reverse transcriptase which alter RNase H activity and decrease strand transfer efficiency are suppressed by HIV nucleocapsid protein Proc. Natl Acad. Sci. USA 94 1997 6700 6705
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6700-6705
    • Cameron, C.E.1    Ghosh, M.2    Le Grice, S.F.3    Benkovic, S.J.4
  • 34
    • 0141866872 scopus 로고    scopus 로고
    • Steps of the acceptor invasion mechanism for HIV-1 minus strand strong stop transfer
    • Y. Chen, M. Balakrishnan, B.P. Roques, and R.A. Bambara Steps of the acceptor invasion mechanism for HIV-1 minus strand strong stop transfer J. Biol. Chem. 278 2003 38368 38375
    • (2003) J. Biol. Chem. , vol.278 , pp. 38368-38375
    • Chen, Y.1    Balakrishnan, M.2    Roques, B.P.3    Bambara, R.A.4
  • 35
    • 0037424356 scopus 로고    scopus 로고
    • Mechanism of minus strand strong stop transfer in HIV-1 reverse transcription
    • Y. Chen, M. Balakrishnan, B.P. Roques, P.J. Fay, and R.A. Bambara Mechanism of minus strand strong stop transfer in HIV-1 reverse transcription J. Biol. Chem. 278 2003 8006 8017
    • (2003) J. Biol. Chem. , vol.278 , pp. 8006-8017
    • Chen, Y.1    Balakrishnan, M.2    Roques, B.P.3    Fay, P.J.4    Bambara, R.A.5
  • 36
    • 0042858256 scopus 로고    scopus 로고
    • Role of the reverse transcriptase, nucleocapsid protein, and template structure in the two-step transfer mechanism in retroviral recombination
    • R.H. Roda, M. Balakrishnan, M.N. Hanson, B.M. Wohrl, S.F. Le Grice, and B.P. Roques Role of the reverse transcriptase, nucleocapsid protein, and template structure in the two-step transfer mechanism in retroviral recombination J. Biol. Chem. 278 2003 31536 31546
    • (2003) J. Biol. Chem. , vol.278 , pp. 31536-31546
    • Roda, R.H.1    Balakrishnan, M.2    Hanson, M.N.3    Wohrl, B.M.4    Le Grice, S.F.5    Roques, B.P.6
  • 37
    • 0037459094 scopus 로고    scopus 로고
    • Destabilization of the HIV-1 complementary sequence of TAR by the nucleocapsid protein through activation of conformational fluctuations
    • J. Azoulay, J.P. Clamme, J.L. Darlix, B.P. Roques, and Y. Mely Destabilization of the HIV-1 complementary sequence of TAR by the nucleocapsid protein through activation of conformational fluctuations J. Mol. Biol. 326 2003 691 700
    • (2003) J. Mol. Biol. , vol.326 , pp. 691-700
    • Azoulay, J.1    Clamme, J.P.2    Darlix, J.L.3    Roques, B.P.4    Mely, Y.5
  • 38
    • 0037453234 scopus 로고    scopus 로고
    • Impact of the terminal bulges of HIV-1 cTAR DNA on its stability and the destabilizing activity of the nucleocapsid protein NCp7
    • H. Beltz, J. Azoulay, S. Bernacchi, J.P. Clamme, D. Ficheux, and B. Roques Impact of the terminal bulges of HIV-1 cTAR DNA on its stability and the destabilizing activity of the nucleocapsid protein NCp7 J. Mol. Biol. 328 2003 95 108
    • (2003) J. Mol. Biol. , vol.328 , pp. 95-108
    • Beltz, H.1    Azoulay, J.2    Bernacchi, S.3    Clamme, J.P.4    Ficheux, D.5    Roques, B.6
  • 39
    • 0036298272 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein activates transient melting of least stable parts of the secondary structure of TAR and its complementary sequence
    • S. Bernacchi, S. Stoylov, E. Piemont, D. Ficheux, B.P. Roques, J.L. Darlix, and Y. Mely HIV-1 nucleocapsid protein activates transient melting of least stable parts of the secondary structure of TAR and its complementary sequence J. Mol. Biol. 317 2002 385 399
    • (2002) J. Mol. Biol. , vol.317 , pp. 385-399
    • Bernacchi, S.1    Stoylov, S.2    Piemont, E.3    Ficheux, D.4    Roques, B.P.5    Darlix, J.L.6    Mely, Y.7
  • 40
    • 0037260333 scopus 로고    scopus 로고
    • Nucleic acid conformational changes essential for HIV-1 nucleocapsid protein-mediated inhibition of self-priming in minus-strand transfer
    • M.K. Hong, E.J. Harbron, D.B. O'Connor, J. Guo, P.F. Barbara, J.G. Levin, and K. Musier-Forsyth Nucleic acid conformational changes essential for HIV-1 nucleocapsid protein-mediated inhibition of self-priming in minus-strand transfer J. Mol. Biol. 325 2003 1 10
    • (2003) J. Mol. Biol. , vol.325 , pp. 1-10
    • Hong, M.K.1    Harbron, E.J.2    O'Connor, D.B.3    Guo, J.4    Barbara, P.F.5    Levin, J.G.6    Musier-Forsyth, K.7
  • 41
    • 20844463873 scopus 로고    scopus 로고
    • Structural determinants of HIV-1 nucleocapsid protein for cTAR DNA binding and destabilization, and correlation with inhibition of self-primed DNA synthesis
    • H. Beltz, C. Clauss, E. Piemont, D. Ficheux, R.J. Gorelick, and B. Roques Structural determinants of HIV-1 nucleocapsid protein for cTAR DNA binding and destabilization, and correlation with inhibition of self-primed DNA synthesis J. Mol. Biol. 348 2005 1113 1126
    • (2005) J. Mol. Biol. , vol.348 , pp. 1113-1126
    • Beltz, H.1    Clauss, C.2    Piemont, E.3    Ficheux, D.4    Gorelick, R.J.5    Roques, B.6
  • 42
    • 27744552000 scopus 로고    scopus 로고
    • Single-molecule FRET studies of important intermediates in the nucleocapsid protein chaperoned minus-strand transfer step in HIV-1 reverse transcription
    • H.W. Liu, G. Cosa, C.F. Landes, Y. Zeng, B.J. Kovaleski, and D.G. Mullen Single-molecule FRET studies of important intermediates in the nucleocapsid protein chaperoned minus-strand transfer step in HIV-1 reverse transcription Biophys. J. 89 2005 3470 3479
    • (2005) Biophys. J. , vol.89 , pp. 3470-3479
    • Liu, H.W.1    Cosa, G.2    Landes, C.F.3    Zeng, Y.4    Kovaleski, B.J.5    Mullen, D.G.6
  • 43
    • 0035861980 scopus 로고    scopus 로고
    • Stem-loop SL4 of the HIV-1 psi RNA packaging signal exhibits weak affinity for the nucleocapsid protein. structural studies and implications for genome recognition
    • G.K. Amarasinghe, J. Zhou, M. Miskimon, K.J. Chancellor, J.A. McDonald, and A.G. Matthews Stem-loop SL4 of the HIV-1 psi RNA packaging signal exhibits weak affinity for the nucleocapsid protein. structural studies and implications for genome recognition J. Mol. Biol. 314 2001 961 970
    • (2001) J. Mol. Biol. , vol.314 , pp. 961-970
    • Amarasinghe, G.K.1    Zhou, J.2    Miskimon, M.3    Chancellor, K.J.4    McDonald, J.A.5    Matthews, A.G.6
  • 44
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • R.N. De Guzman, Z.R. Wu, C.C. Stalling, L. Pappalardo, P.N. Borer, and M.F. Summers Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element Science 279 1998 384 388
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 46
    • 0037214624 scopus 로고    scopus 로고
    • Excitonic heterodimer formation in an HIV-1 oligonucleotide labelled with a donor-acceptor pair used for fluorescence resonance energy transfer
    • S. Bernacchi, E. Piemont, N. Potier, A. Dorsselaer, and Y. Mely Excitonic heterodimer formation in an HIV-1 oligonucleotide labelled with a donor-acceptor pair used for fluorescence resonance energy transfer Biophys. J. 84 2003 643 654
    • (2003) Biophys. J. , vol.84 , pp. 643-654
    • Bernacchi, S.1    Piemont, E.2    Potier, N.3    Dorsselaer, A.4    Mely, Y.5
  • 47
    • 1642298257 scopus 로고    scopus 로고
    • Mechanistic insights into the kinetics of HIV-1 nucleocapsid protein-facilitated tRNA annealing to the primer binding site
    • M.R. Hargittai, R.J. Gorelick, I. Rouzina, and K. Musier-Forsyth Mechanistic insights into the kinetics of HIV-1 nucleocapsid protein-facilitated tRNA annealing to the primer binding site J. Mol. Biol. 337 2004 951 968
    • (2004) J. Mol. Biol. , vol.337 , pp. 951-968
    • Hargittai, M.R.1    Gorelick, R.J.2    Rouzina, I.3    Musier-Forsyth, K.4
  • 50
    • 1942457321 scopus 로고    scopus 로고
    • Role of the structure of the top half of HIV-1 cTAR DNA on the nucleic acid destabilizing activity of the nucleocapsid protein NCp7
    • H. Beltz, E. Piemont, E. Schaub, D. Ficheux, B. Roques, J.L. Darlix, and Y. Mely Role of the structure of the top half of HIV-1 cTAR DNA on the nucleic acid destabilizing activity of the nucleocapsid protein NCp7 J. Mol. Biol. 338 2004 711 723
    • (2004) J. Mol. Biol. , vol.338 , pp. 711-723
    • Beltz, H.1    Piemont, E.2    Schaub, E.3    Ficheux, D.4    Roques, B.5    Darlix, J.L.6    Mely, Y.7
  • 51
    • 0344443358 scopus 로고    scopus 로고
    • DNA condensation by the nucleocapsid protein of HIV-1: A mechanism ensuring DNA protection
    • G. Krishnamoorthy, B. Roques, J.L. Darlix, and Y. Mely DNA condensation by the nucleocapsid protein of HIV-1: a mechanism ensuring DNA protection Nucl. Acids Res. 31 2003 5425 5432
    • (2003) Nucl. Acids Res. , vol.31 , pp. 5425-5432
    • Krishnamoorthy, G.1    Roques, B.2    Darlix, J.L.3    Mely, Y.4
  • 52
    • 0032032070 scopus 로고    scopus 로고
    • Properties and growth mechanism of the ordered aggregation of a model RNA by the HIV-1 nucleocapsid protein: An electron microscopy investigation
    • E. Le Cam, D. Coulaud, E. Delain, P. Petitjean, B.P. Roques, and D. Gerard Properties and growth mechanism of the ordered aggregation of a model RNA by the HIV-1 nucleocapsid protein: an electron microscopy investigation Biopolymers 45 1998 217 229
    • (1998) Biopolymers , vol.45 , pp. 217-229
    • Le Cam, E.1    Coulaud, D.2    Delain, E.3    Petitjean, P.4    Roques, B.P.5    Gerard, D.6
  • 53
    • 0036307597 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein as a nucleic acid chaperone: Spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity
    • M.A. Urbaneja, M. Wu, J.R. Casas-Finet, and R.L. Karpel HIV-1 nucleocapsid protein as a nucleic acid chaperone: spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity J. Mol. Biol. 318 2002 749 764
    • (2002) J. Mol. Biol. , vol.318 , pp. 749-764
    • Urbaneja, M.A.1    Wu, M.2    Casas-Finet, J.R.3    Karpel, R.L.4
  • 54
    • 16644394128 scopus 로고    scopus 로고
    • Secondary structure and secondary structure dynamics of DNA hairpins complexed with HIV-1 NC protein
    • G. Cosa, E.J. Harbron, Y. Zeng, H.W. Liu, D.B. O'Connor, and C. Eta-Hosokawa Secondary structure and secondary structure dynamics of DNA hairpins complexed with HIV-1 NC protein Biophys. J. 87 2004 2759 2767
    • (2004) Biophys. J. , vol.87 , pp. 2759-2767
    • Cosa, G.1    Harbron, E.J.2    Zeng, Y.3    Liu, H.W.4    O'Connor, D.B.5    Eta-Hosokawa, C.6
  • 55
    • 0034903425 scopus 로고    scopus 로고
    • Structural features in the HIV-1 repeat region facilitate strand transfer during reverse transcription
    • B. Berkhout, N.L. Vastenhouw, B.I. Klasens, and H. Huthoff Structural features in the HIV-1 repeat region facilitate strand transfer during reverse transcription Rna 7 2001 1097 1114
    • (2001) Rna , vol.7 , pp. 1097-1114
    • Berkhout, B.1    Vastenhouw, N.L.2    Klasens, B.I.3    Huthoff, H.4
  • 57
    • 17644391796 scopus 로고    scopus 로고
    • Acceptor RNA cleavage profile supports an invasion mechanism for HIV-1 minus strand transfer
    • Y. Chen, M. Balakrishnan, B.P. Roques, and R.A. Bambara Acceptor RNA cleavage profile supports an invasion mechanism for HIV-1 minus strand transfer J. Biol. Chem. 280 2005 14443 14452
    • (2005) J. Biol. Chem. , vol.280 , pp. 14443-14452
    • Chen, Y.1    Balakrishnan, M.2    Roques, B.P.3    Bambara, R.A.4


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