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Volumn 363, Issue 5, 2006, Pages 867-877

Rapid Kinetics of Protein-Nucleic Acid Interaction is a Major Component of HIV-1 Nucleocapsid Protein's Nucleic Acid Chaperone Function

Author keywords

DNA cooperativity; DNA melting; nucleic acid chaperone; nucleocapsid protein; single molecule DNA stretching

Indexed keywords

CHAPERONE; MUTANT PROTEIN; NUCLEIC ACID; NUCLEOCAPSID PROTEIN; SINGLE STRANDED DNA; ZINC FINGER PROTEIN;

EID: 33750016312     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.08.070     Document Type: Article
Times cited : (76)

References (65)
  • 1
    • 0029585377 scopus 로고
    • First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses
    • Darlix J.-L., Lapadat-Tapolsky M., de Rocquigny H., and Roques B.P. 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-Tapolsky, M.2    de Rocquigny, H.3    Roques, B.P.4
  • 2
    • 23144448275 scopus 로고    scopus 로고
    • Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism
    • Elsevier (Ed), Academic Press
    • Levin J.G., Guo J., Rouzina I., and Musier-Forsyth K. Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism. In: Elsevier (Ed). Progress in Nucleic Acid Research and Molecular Biology vol. 80 (2005), Academic Press 217-286
    • (2005) Progress in Nucleic Acid Research and Molecular Biology , vol.80 , pp. 217-286
    • Levin, J.G.1    Guo, J.2    Rouzina, I.3    Musier-Forsyth, K.4
  • 3
    • 0031679786 scopus 로고    scopus 로고
    • Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication
    • Rein A., Henderson L.E., and Levin J.G. Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication. Trends Biochem. Sci. 23 (1998) 297-301
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 297-301
    • Rein, A.1    Henderson, L.E.2    Levin, J.G.3
  • 4
    • 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., Bowers M.A., Sowder II R.C., Serabyn S.A., Johnson D.G., Bess Jr. J.W., et al. 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
  • 5
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • Coffin J.M., Hughes S.H., and Varmus H. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Swanstrom R., and Wills J. Synthesis, assembly, and processing of viral proteins. In: Coffin J.M., Hughes S.H., and Varmus H. (Eds). Retroviruses (1997), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 263-334
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.2
  • 6
    • 0003151659 scopus 로고
    • Retroviral virions and genomes
    • Coffin J.M., Hughes S.H., and Varmus H.E. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Vogt V.M. Retroviral virions and genomes. In: Coffin J.M., Hughes S.H., and Varmus H.E. (Eds). Retroviruses (1987), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 27-70
    • (1987) Retroviruses , pp. 27-70
    • Vogt, V.M.1
  • 7
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell S., and Vogt V.M. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J. Virol. 69 (1995) 6487-6497
    • (1995) J. Virol. , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 8
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell S., and Rein A. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J. Virol. 73 (1999) 2270-2279
    • (1999) J. Virol. , vol.73 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 11
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag D. RNA chaperones and the RNA folding problem. J. Biol. Chem. 270 (1995) 20871-20874
    • (1995) J. Biol. Chem. , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 12
    • 0037188887 scopus 로고    scopus 로고
    • RNA chaperones exist and DEAD box proteins get a life
    • Lorsch J.R. RNA chaperones exist and DEAD box proteins get a life. Cell 109 (2002) 797-800
    • (2002) Cell , vol.109 , pp. 797-800
    • Lorsch, J.R.1
  • 13
    • 0028129970 scopus 로고
    • DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein
    • Tsuchihashi Z., and Brown P.O. DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein. J. Virol. 68 (1994) 5863-5870
    • (1994) J. Virol. , vol.68 , pp. 5863-5870
    • Tsuchihashi, Z.1    Brown, P.O.2
  • 14
    • 1642298257 scopus 로고    scopus 로고
    • Mechanistic insights into the kinetics of HIV-1 nucleocapsid protein-facilitated tRNA annealing to the primer binding site
    • Hargittai M.R.S., Gorelick R.J., Rouzina I., and Musier-Forsyth K. 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.S.1    Gorelick, R.J.2    Rouzina, I.3    Musier-Forsyth, K.4
  • 15
    • 0030018941 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus nucleocapsid protein with a structure mimicking a replication intermediate. Effects on stability, reverse transcriptase binding, and strand transfer
    • DeStefano J.J. Interaction of human immunodeficiency virus nucleocapsid protein with a structure mimicking a replication intermediate. Effects on stability, reverse transcriptase binding, and strand transfer. J. Biol. Chem. 271 (1996) 16350-16356
    • (1996) J. Biol. Chem. , vol.271 , pp. 16350-16356
    • DeStefano, J.J.1
  • 16
    • 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 seqeunces
    • Driscoll M.D., and Hughes S.H. 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 seqeunces. J. Virol. 74 (2000) 8785-8792
    • (2000) J. Virol. , vol.74 , pp. 8785-8792
    • Driscoll, M.D.1    Hughes, S.H.2
  • 17
    • 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
    • Heilman-Miller S., Wu T., and Levin J.G. 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.1    Wu, T.2    Levin, J.G.3
  • 18
    • 0027411503 scopus 로고
    • Retroviral nucleocapsid proteins possess potent nucleic acid strand renaturation activity
    • Dib-Hajj F., Khan R., and Giedroc D.P. Retroviral nucleocapsid proteins possess potent nucleic acid strand renaturation activity. Protein Sci. 2 (1993) 231-243
    • (1993) Protein Sci. , vol.2 , pp. 231-243
    • Dib-Hajj, F.1    Khan, R.2    Giedroc, D.P.3
  • 19
    • 0028113905 scopus 로고
    • Human immunodeficiency virus nucleocapsid protein accelerates strand transfer of the terminally redundant sequences involved in reverse transcription
    • You J.C., and McHenry C.S. 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
  • 20
    • 0036226153 scopus 로고    scopus 로고
    • Subtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid protein
    • Guo J., Wu T., Kane B.F., Johnson D.G., Henderson L.E., Gorelick R.J., and Levin J.G. Subtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid protein. J. Virol. 76 (2002) 4370-4378
    • (2002) J. Virol. , vol.76 , pp. 4370-4378
    • Guo, J.1    Wu, T.2    Kane, B.F.3    Johnson, D.G.4    Henderson, L.E.5    Gorelick, R.J.6    Levin, J.G.7
  • 21
    • 0041732006 scopus 로고    scopus 로고
    • Differing roles of the N- and C-terminal zinc fingers in human immunodefficency virus nucleocapsid protein-enhanced nucleic acid annealing
    • Heath M., Derebail S.S., Gorelick R.J., and DeStefano J.J. Differing roles of the N- and C-terminal zinc fingers in human immunodefficency virus nucleocapsid protein-enhanced nucleic acid annealing. J. Biol. Chem. 278 (2003) 30755-30763
    • (2003) J. Biol. Chem. , vol.278 , pp. 30755-30763
    • Heath, M.1    Derebail, S.S.2    Gorelick, R.J.3    DeStefano, J.J.4
  • 22
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • De Guzman R.N., Wu Z.R., Stalling C.C., Pappalardo L., Borer P.N., and Summers M.F. 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
  • 23
    • 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
    • Bernacchi S., Stoylov S.P., Piemont E., Ficheux D., Roques B., Darlix J.L., and Mely Y. 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.P.2    Piemont, E.3    Ficheux, D.4    Roques, B.5    Darlix, J.L.6    Mely, Y.7
  • 24
    • 0344443358 scopus 로고    scopus 로고
    • DNA condensation by the nucleocapsid protein of HIV-1: a mechanism ensuring DNA protection
    • Krishnamoorthy G., Roques B., Darlix J.-L., and Mely Y. 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
  • 26
    • 0033593039 scopus 로고    scopus 로고
    • Nucleic acid sequence discrimination by the HIV-1 nucleocapsid protein NCp7: a fluorescence study
    • Vuilleumier C., Bombarda E., Morellet N., Gerard D., Roques B.P., and Mely Y. Nucleic acid sequence discrimination by the HIV-1 nucleocapsid protein NCp7: a fluorescence study. Biochemistry 38 (1999) 16816-16825
    • (1999) Biochemistry , vol.38 , pp. 16816-16825
    • Vuilleumier, C.1    Bombarda, E.2    Morellet, N.3    Gerard, D.4    Roques, B.P.5    Mely, Y.6
  • 27
    • 0033583086 scopus 로고    scopus 로고
    • Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: elucidation of the structural determinants for function
    • Urbaneja M.A., Kane B.P., Johnson D.G., Gorelick R.J., Henderson L.E., and Casas-Finet J.R. Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: elucidation of the structural determinants for function. J. Mol. Biol. 287 (1999) 59-75
    • (1999) J. Mol. Biol. , vol.287 , pp. 59-75
    • Urbaneja, M.A.1    Kane, B.P.2    Johnson, D.G.3    Gorelick, R.J.4    Henderson, L.E.5    Casas-Finet, J.R.6
  • 28
    • 0034636984 scopus 로고    scopus 로고
    • NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the Psi-RNA packaging signal: implications for genome recognition
    • Amarasinghe G.K., Guzman R.N.D., Turner R.B., Chancellor K.J., Wu Z.R., and Summers M.F. NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the Psi-RNA packaging signal: implications for genome recognition. J. Mol. Biol. 301 (2000) 491-511
    • (2000) J. Mol. Biol. , vol.301 , pp. 491-511
    • Amarasinghe, G.K.1    Guzman, R.N.D.2    Turner, R.B.3    Chancellor, K.J.4    Wu, Z.R.5    Summers, M.F.6
  • 29
    • 16644394128 scopus 로고    scopus 로고
    • Secondary structure and secondary structure dynamics of DNA hairpins complexed with HIV-1 NC protein
    • Cosa G., Harbron E.J., Zeng Y., Liu H.W., O'Connor D.B., Eta-Hosokawa C., et al. 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
  • 30
    • 0037459094 scopus 로고    scopus 로고
    • Destabilization of the HIV-1 complementary sequence of TAR by the nucleocapsid protein through activation of conformational fluctuations
    • Azoulay J., Clamme J.-P., Darlix J.L., Roques B.P., and Mely Y. 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
  • 31
    • 0033582291 scopus 로고    scopus 로고
    • Intra-tRNA distance measurements for nucleocapsid proteindependent tRNA unwinding during priming of HIV reverse transcription
    • Chan B., Weidemaier K., Yip W.T., Barbara P.F., and Musier-Forsyth K. Intra-tRNA distance measurements for nucleocapsid proteindependent tRNA unwinding during priming of HIV reverse transcription. Proc. Natl Acad. Sci. USA 96 (1999) 459-464
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 459-464
    • Chan, B.1    Weidemaier, K.2    Yip, W.T.3    Barbara, P.F.4    Musier-Forsyth, K.5
  • 32
    • 0035812603 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein zinc finger structures induce tRNALys,3 tertiary structural changes but are not critical for primer/template annealing
    • Hargittai M.R.S., Mangla A.T., Gorelick R.J., and Musier-Forsyth K. HIV-1 nucleocapsid protein zinc finger structures induce tRNALys,3 tertiary structural changes but are not critical for primer/template annealing. J. Mol. Biol. 312 (2001) 985-997
    • (2001) J. Mol. Biol. , vol.312 , pp. 985-997
    • Hargittai, M.R.S.1    Mangla, A.T.2    Gorelick, R.J.3    Musier-Forsyth, K.4
  • 33
    • 0037260333 scopus 로고    scopus 로고
    • Nucleic acid conformational changes essential for HIV-1 nucleocapsid protein-mediated inhibition of self-priming in minus-strand transfer
    • Hong M., Harbron E., O'Connor D., Guo J., Barbara P.F., Levin J.G., and Musier-Forsyth K. 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.1    Harbron, E.2    O'Connor, D.3    Guo, J.4    Barbara, P.F.5    Levin, J.G.6    Musier-Forsyth, K.7
  • 34
    • 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
    • Beltz H., Azoulay J., Bernacchi S., Clamme J.P., Ficheux D., Roques B., et al. 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
  • 35
    • 0036600949 scopus 로고    scopus 로고
    • Force spectroscopy of single DNA and RNA molecules
    • Williams M.C., and Rouzina I. Force spectroscopy of single DNA and RNA molecules. Curr. Opin. Struct. Biol. 12 (2002) 330-336
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 330-336
    • Williams, M.C.1    Rouzina, I.2
  • 36
    • 0035144565 scopus 로고    scopus 로고
    • The effect of pH on the overstretching transition of dsDNA: evidence of force-induced DNA melting
    • Williams M.C., Wenner J.R., Rouzina I., and Bloomfield V.A. The effect of pH on the overstretching transition of dsDNA: evidence of force-induced DNA melting. Biophys. J. 80 (2001) 874-881
    • (2001) Biophys. J. , vol.80 , pp. 874-881
    • Williams, M.C.1    Wenner, J.R.2    Rouzina, I.3    Bloomfield, V.A.4
  • 37
    • 0035072057 scopus 로고    scopus 로고
    • Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching
    • Williams M.C., Wenner J.R., Rouzina I., and Bloomfield V.A. Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching. Biophys. J. 80 (2001) 1932-1939
    • (2001) Biophys. J. , vol.80 , pp. 1932-1939
    • Williams, M.C.1    Wenner, J.R.2    Rouzina, I.3    Bloomfield, V.A.4
  • 38
    • 0036106380 scopus 로고    scopus 로고
    • Salt dependence of the elasticity and overstretching transition of single DNA molecules
    • Wenner J.R., Williams M.C., Rouzina I., and Bloomfield V.A. Salt dependence of the elasticity and overstretching transition of single DNA molecules. Biophys. J. 82 (2002) 3160-3169
    • (2002) Biophys. J. , vol.82 , pp. 3160-3169
    • Wenner, J.R.1    Williams, M.C.2    Rouzina, I.3    Bloomfield, V.A.4
  • 39
    • 0036009140 scopus 로고    scopus 로고
    • Thermodynamics of DNA interactions from single molecule stretching experiments
    • Williams M.C., Rouzina I., and Bloomfield V.A. Thermodynamics of DNA interactions from single molecule stretching experiments. Acc. Chem. Res. 35 (2002) 159-166
    • (2002) Acc. Chem. Res. , vol.35 , pp. 159-166
    • Williams, M.C.1    Rouzina, I.2    Bloomfield, V.A.3
  • 40
    • 1042298812 scopus 로고    scopus 로고
    • Mechanical measurement of single molecule binding rates: kinetics of DNA helix-destabilization by T4 gene 32 protein
    • Pant K., Karpel R.L., Rouzina I., and Williams M.C. Mechanical measurement of single molecule binding rates: kinetics of DNA helix-destabilization by T4 gene 32 protein. J. Mol. Biol. 336 (2004) 851-870
    • (2004) J. Mol. Biol. , vol.336 , pp. 851-870
    • Pant, K.1    Karpel, R.L.2    Rouzina, I.3    Williams, M.C.4
  • 41
    • 0344406718 scopus 로고    scopus 로고
    • Kinetic regulation of single DNA molecule denaturation by T4 gene 32 protein structural domains
    • Pant K., Karpel R.L., and Williams M.C. Kinetic regulation of single DNA molecule denaturation by T4 gene 32 protein structural domains. J. Mol. Biol. 327 (2003) 571-578
    • (2003) J. Mol. Biol. , vol.327 , pp. 571-578
    • Pant, K.1    Karpel, R.L.2    Williams, M.C.3
  • 42
    • 18844364649 scopus 로고    scopus 로고
    • Salt-dependent binding of T4 gene 32 protein to single and double-stranded DNA: single molecule force spectroscopy measurements
    • Pant K., Karpel R.L., and Williams M.C. Salt-dependent binding of T4 gene 32 protein to single and double-stranded DNA: single molecule force spectroscopy measurements. J. Mol. Biol. 349 (2005) 317-330
    • (2005) J. Mol. Biol. , vol.349 , pp. 317-330
    • Pant, K.1    Karpel, R.L.2    Williams, M.C.3
  • 44
    • 0037116588 scopus 로고    scopus 로고
    • Discriminating small molecule DNA binding modes by single molecule force spectroscopy
    • Krautbauer R., Pope L.H., Schrader T.E., Allen S., and Gaub H.E. Discriminating small molecule DNA binding modes by single molecule force spectroscopy. FEBS Letters 510 (2002) 154-158
    • (2002) FEBS Letters , vol.510 , pp. 154-158
    • Krautbauer, R.1    Pope, L.H.2    Schrader, T.E.3    Allen, S.4    Gaub, H.E.5
  • 45
    • 33744826236 scopus 로고    scopus 로고
    • Exploring the interaction of ruthenium(II) polypyridyl complexes with DNA using single-molecule techniques
    • Mihailovic A., Vladescu I., McCauley M., Ly E., Williams M.C., Spain E.M., and Nunez M.E. Exploring the interaction of ruthenium(II) polypyridyl complexes with DNA using single-molecule techniques. Langmuir 22 (2006) 4699-4709
    • (2006) Langmuir , vol.22 , pp. 4699-4709
    • Mihailovic, A.1    Vladescu, I.2    McCauley, M.3    Ly, E.4    Williams, M.C.5    Spain, E.M.6    Nunez, M.E.7
  • 46
    • 28844463534 scopus 로고    scopus 로고
    • Mapping the phase diagram of single DNA molecule force-induced melting in the presence of ethidium
    • Vladescu I.D., McCauley M.J., Rouzina I., and Williams M.C. Mapping the phase diagram of single DNA molecule force-induced melting in the presence of ethidium. Phys. Rev. Letters 95 (2005) 158102
    • (2005) Phys. Rev. Letters , vol.95 , pp. 158102
    • Vladescu, I.D.1    McCauley, M.J.2    Rouzina, I.3    Williams, M.C.4
  • 48
    • 4344589738 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein binds to the viral DNA initiation sequences and chaperones their kissing interactions
    • Egele C., Schaub E., Ramalanjaona N., Piemont E., Ficheux D., Roques B., et al. HIV-1 nucleocapsid protein binds to the viral DNA initiation sequences and chaperones their kissing interactions. J. Mol. Biol. 342 (2004) 453-466
    • (2004) J. Mol. Biol. , vol.342 , pp. 453-466
    • Egele, C.1    Schaub, E.2    Ramalanjaona, N.3    Piemont, E.4    Ficheux, D.5    Roques, B.6
  • 50
    • 0037173118 scopus 로고    scopus 로고
    • Specific zinc finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function
    • Williams M.C., Gorelick R.J., and Musier-Forsyth K. Specific zinc finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function. Proc. Natl Acad. Sci. USA 99 (2002) 8614-8619
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8614-8619
    • Williams, M.C.1    Gorelick, R.J.2    Musier-Forsyth, K.3
  • 51
    • 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
    • Le Cam E., Coulaud D., Delain E., Petitjean P., Roques B.P., Gérard D., et al. 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    Gérard, D.6
  • 53
    • 0028955753 scopus 로고
    • Binding of the HIV-1 nucleocapsid protein to the primer tRNA(3Lys), in vitro, is essentially not specific
    • Mely Y., de Rocquigny H., Sorinas-Jimeno M., Keith G., Roques B.P., Marquet R., and Gerard D. Binding of the HIV-1 nucleocapsid protein to the primer tRNA(3Lys), in vitro, is essentially not specific. J. Biol. Chem. 270 (1995) 1650-1656
    • (1995) J. Biol. Chem. , vol.270 , pp. 1650-1656
    • Mely, Y.1    de Rocquigny, H.2    Sorinas-Jimeno, M.3    Keith, G.4    Roques, B.P.5    Marquet, R.6    Gerard, D.7
  • 54
    • 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
    • Urbaneja M.A., Wu M., Casas-Finet J.R., and Karpel R.L. 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
  • 55
    • 0031935140 scopus 로고    scopus 로고
    • Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides
    • Fisher R.J., Rein A., Fivash M., Urbaneja M.A., Casas-Finet J.R., Medaglia M., and Henderson L.E. Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides. J. Virol. 72 (1998) 1902-1909
    • (1998) J. Virol. , vol.72 , pp. 1902-1909
    • Fisher, R.J.1    Rein, A.2    Fivash, M.3    Urbaneja, M.A.4    Casas-Finet, J.R.5    Medaglia, M.6    Henderson, L.E.7
  • 56
    • 0031447208 scopus 로고    scopus 로고
    • DNA condensation by multivalent cations
    • Bloomfield V.A. DNA condensation by multivalent cations. Biopolymers 44 (1998) 269-282
    • (1998) Biopolymers , vol.44 , pp. 269-282
    • Bloomfield, V.A.1
  • 59
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning G.S. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Quart. Rev. Biophys. 11 (1978) 179-246
    • (1978) Quart. Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 60
    • 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
    • Beltz H., Piemont E., Schaub E., Ficheux D., Roques B., Darlix J.L., and Mely Y. 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
  • 61
    • 0141866872 scopus 로고    scopus 로고
    • Steps of the acceptor invasion mechanism for HIV-1 minus strand strong stop transfer
    • Chen Y., Balakrishnan M., Roques B., and Bambara R.A. 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.3    Bambara, R.A.4
  • 63
    • 0344443680 scopus 로고    scopus 로고
    • Zinc finger-dependent HIV-1 nucleocapsid protein-TAR RNA interactions
    • Lee N., Gorelick R.J., and Musier-Forsyth K. Zinc finger-dependent HIV-1 nucleocapsid protein-TAR RNA interactions. Nucl. Acids Res. 31 (2003) 4847-4855
    • (2003) Nucl. Acids Res. , vol.31 , pp. 4847-4855
    • Lee, N.1    Gorelick, R.J.2    Musier-Forsyth, K.3
  • 64
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules
    • Smith S.B., Cui Y.J., and Bustamante C. Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules. Science 271 (1996) 795-799
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.J.2    Bustamante, C.3
  • 65
    • 33748769274 scopus 로고    scopus 로고
    • Vo, M.-N., Barany, G., Rouzina I., Musier-Forsyth, K. Mechanistic studies of mini-TAR RNA/DNA annealing in the absence and presence of HIV-1 nucleocapsid protein. J. Mol. Biol., in press. doi:10.1016/j.jmb.2006.08.039


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.