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Volumn 36, Issue 3, 2008, Pages 885-896

Probing dynamics of HIV-1 nucleocapsid protein/target hexanucleotide complexes by 2-aminopurine

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOPURINE; ADENINE; ALANINE; CHAPERONE; CYTOSINE; GUANINE; LEUCINE; NUCLEOCAPSID PROTEIN; OLIGONUCLEOTIDE; PHENYLALANINE; THYMINE; TRYPTOPHAN;

EID: 39449116929     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm1109     Document Type: Article
Times cited : (50)

References (67)
  • 1
    • 0034565966 scopus 로고    scopus 로고
    • Nucleocapsid protein of human immunodeficiency virus as a model protein with chaperoning functions and as a target for antiviral drugs
    • Darlix,J.L., Cristofari,O., Rau,M., Pechoux,C., Berthoux,L. and Roques,B. (2000) Nucleocapsid protein of human immunodeficiency virus as a model protein with chaperoning functions and as a target for antiviral drugs. Adv. Pharmacol., 48, 345-372.
    • (2000) Adv. Pharmacol , vol.48 , pp. 345-372
    • Darlix, J.L.1    Cristofari, O.2    Rau, M.3    Pechoux, C.4    Berthoux, L.5    Roques, B.6
  • 2
    • 0028904512 scopus 로고
    • RNA secondary structure and binding sites for gag gene products in the 5′, packaging signal of human immunodeficiency virus type 1
    • Clever,J., Sassetti,C. and Parslow,T.G. (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
  • 3
    • 0026628854 scopus 로고
    • Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingers
    • De Rocquigny,H., Gabus,C., Vincent,A., Fournie-Zaluski,M.C., Roques,B, and Darlix,J.L. (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    Fournie-Zaluski, M.C.4    Roques, B.5    Darlix, J.L.6
  • 4
    • 2942594259 scopus 로고    scopus 로고
    • The chaperoning and assistance roles of the HIV-1 nucleocapsid protein in proviral DNA synthesis and maintenance
    • Bampi,C., Jacquenet,S., Lener,D., Decimo,D. and Darlix,J.L. (2004) The chaperoning and assistance roles of the HIV-1 nucleocapsid protein in proviral DNA synthesis and maintenance. Int. J. Biochem. Cell Biol. 36, 1668-1686.
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , pp. 1668-1686
    • Bampi, C.1    Jacquenet, S.2    Lener, D.3    Decimo, D.4    Darlix, J.L.5
  • 5
    • 20344368389 scopus 로고    scopus 로고
    • How retroviruses select their genomes
    • D'Souza,V. and Summers,M.F. (2005) How retroviruses select their genomes. Nat. Rev. Microbiol., 3, 643-655.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 643-655
    • D'Souza, V.1    Summers, M.F.2
  • 6
    • 0027220120 scopus 로고
    • Mapping of functionally important residues of a cysteine-histidine box in the human immunodeficiency virus type 1 nucleocapsid protein
    • Dorfman,T., Luban,J., Goff,S.P., Haseltine,W.A. and Gottlinger,H.G. (1993) Mapping of functionally important residues of a cysteine-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.A.4    Gottlinger, H.G.5
  • 7
    • 0033616530 scopus 로고    scopus 로고
    • Strict conservation of the retroviral nucleocapsid protein zinc finger is strongly influenced by its role in viral infection processes: Characterization of HIV-1 particles containing mutant nucleocapsid zinc-coordinating sequences
    • Gorelick,R.J., Gagliardi,T.D., Bosche,W.J., Wiltrout,T.A., Coren,L.V., Chabot,D.J., Lifson,J.D., Henderson,L.E. and Arthur,L.O. (1999) Strict conservation of the retroviral nucleocapsid protein zinc finger is strongly influenced by its role in viral infection processes: characterization of HIV-1 particles containing mutant nucleocapsid zinc-coordinating sequences. Virology, 256, 92-104.
    • (1999) Virology , vol.256 , pp. 92-104
    • Gorelick, R.J.1    Gagliardi, T.D.2    Bosche, W.J.3    Wiltrout, T.A.4    Coren, L.V.5    Chabot, D.J.6    Lifson, J.D.7    Henderson, L.E.8    Arthur, L.O.9
  • 8
    • 0033803461 scopus 로고    scopus 로고
    • Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer
    • Guo,J., Wu,T., Anderson,J., Kane,B.F., Johnson,D.G., Gorelick,R.J., Henderson,L.E. and Levin,J.G. (2000) Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minus- and plus-strand transfer. J. Virol., 74, 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    Henderson, L.E.7    Levin, J.G.8
  • 9
    • 0028858759 scopus 로고
    • The central globular domain of the nucleocapsid protein of human immunodeficiency virus type 1 is critical for virion structure and infectivity
    • Ottmann,M., Gabus,C. and Darlix,J.L. (1995) The central globular domain of the nucleocapsid protein of human immunodeficiency virus type 1 is critical for virion structure and infectivity. J. Virol., 69 1778-1784.
    • (1995) J. Virol , vol.69 , pp. 1778-1784
    • Ottmann, M.1    Gabus, C.2    Darlix, J.L.3
  • 10
    • 2242469712 scopus 로고    scopus 로고
    • De GuzmanR.N., Wu,Z.R., Stalling,C.C., Pappalardo,L., Borer,P.N. and Summers,M.F. (1998) Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science, 279, 384-388.
    • De GuzmanR.N., Wu,Z.R., Stalling,C.C., Pappalardo,L., Borer,P.N. and Summers,M.F. (1998) Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science, 279, 384-388.
  • 11
    • 0032561130 scopus 로고    scopus 로고
    • Morellet,N., Demene,H., Teilleux,V., Huynh-Dinh,T., de Rocquigny,H., Fournie-Zaluski.M.C. and Roques,B.P. (1998) Structure of the complex between the HIV-1 nucleocapsid protein NCp7 and the single-stranded pentanucleotide d(ACGCC). J. Mol. Biol., 283, 419-434.
    • Morellet,N., Demene,H., Teilleux,V., Huynh-Dinh,T., de Rocquigny,H., Fournie-Zaluski.M.C. and Roques,B.P. (1998) Structure of the complex between the HIV-1 nucleocapsid protein NCp7 and the single-stranded pentanucleotide d(ACGCC). J. Mol. Biol., 283, 419-434.
  • 12
    • 0034716939 scopus 로고    scopus 로고
    • NMR structure of stem-loop SL2 of the HIV-1 psi RNA packaging signal reveals a novel A-U-A base-triple platform
    • Amarasinghe,G.K., De Guzman,R.N., Turner,R.B. and Summers,M.F. (2000) NMR structure of stem-loop SL2 of the HIV-1 psi RNA packaging signal reveals a novel A-U-A base-triple platform. J. Mol. Biol., 299 145-156.
    • (2000) J. Mol. Biol , vol.299 , pp. 145-156
    • Amarasinghe, G.K.1    De Guzman, R.N.2    Turner, R.B.3    Summers, M.F.4
  • 13
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair
    • Walker,J.R., Corpina,R.A. and Goldberg,J. (2001) Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature, 412, 607-614.
    • (2001) Nature , vol.412 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 14
    • 0034161571 scopus 로고    scopus 로고
    • Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing
    • Mazin,A.V., Zaitseva,E., Sung,P. and Kowalczykowski,S.C. (2000) Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing. EMBO J., 19, 1148-1156.
    • (2000) EMBO J , vol.19 , pp. 1148-1156
    • Mazin, A.V.1    Zaitseva, E.2    Sung, P.3    Kowalczykowski, S.C.4
  • 15
    • 31944446215 scopus 로고    scopus 로고
    • Resolving the motional modes that code for RNA adaptation
    • Zhang,Q., Sun,X., Watt,E.D. and Al-Hashimi,H.M. (2006) Resolving the motional modes that code for RNA adaptation. Science, 311, 653-656.
    • (2006) Science , vol.311 , pp. 653-656
    • Zhang, Q.1    Sun, X.2    Watt, E.D.3    Al-Hashimi, H.M.4
  • 16
    • 0036898865 scopus 로고    scopus 로고
    • Single-molecule fluorescence of nucleic acids
    • Mollova,E.T. (2002) Single-molecule fluorescence of nucleic acids. Curr. Opin. Chem. Biol., 6, 823-828.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 823-828
    • Mollova, E.T.1
  • 17
    • 0014669561 scopus 로고    scopus 로고
    • Ward,D.C., Reich,E. and Stryer,L. (1969) Fluorescence studies of nucleotides and polynucleotides. I. Formycin, 2-aminopurine riboside, 2,6-diaminopurine riboside, and their derivatives. J. Biol. Chem., 244, 1228-1237.
    • Ward,D.C., Reich,E. and Stryer,L. (1969) Fluorescence studies of nucleotides and polynucleotides. I. Formycin, 2-aminopurine riboside, 2,6-diaminopurine riboside, and their derivatives. J. Biol. Chem., 244, 1228-1237.
  • 18
    • 0035793105 scopus 로고    scopus 로고
    • 2-Aminopurine fluorescence quenching and lifetimes: Role of base stacking
    • Jean,J.M. and Hall,K.B. (2001) 2-Aminopurine fluorescence quenching and lifetimes: Role of base stacking. Proc. Natl Acad. Sci. USA, 98 37-41.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 37-41
    • Jean, J.M.1    Hall, K.B.2
  • 19
    • 3543088541 scopus 로고    scopus 로고
    • Stacking-unstacking dynamics of oligodeoxynucleotide trimers
    • Jean,J.M. and Hall,K.B. (2004) Stacking-unstacking dynamics of oligodeoxynucleotide trimers. Biochemistry, 43, 10277-10284.
    • (2004) Biochemistry , vol.43 , pp. 10277-10284
    • Jean, J.M.1    Hall, K.B.2
  • 20
    • 0037032244 scopus 로고    scopus 로고
    • 2-Aminopurine: A probe of structural dynamics and charge transfer in DNA and DNA:RNA hybrids
    • O'Neill,M.A. and Barton,J.K. (2002) 2-Aminopurine: A probe of structural dynamics and charge transfer in DNA and DNA:RNA hybrids. J. Am. Chem. Soc., 124, 13053-13066.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 13053-13066
    • O'Neill, M.A.1    Barton, J.K.2
  • 21
    • 0037120095 scopus 로고    scopus 로고
    • Femtosecond charge transfer dynamics of a modified DNA base: 2-aminopurine in complexes with nucleotides
    • Fiebig,T., Wan,C. and Zewail,A.H. (2002) Femtosecond charge transfer dynamics of a modified DNA base: 2-aminopurine in complexes with nucleotides. Chem. Phys. Chem., 3, 781-788.
    • (2002) Chem. Phys. Chem , vol.3 , pp. 781-788
    • Fiebig, T.1    Wan, C.2    Zewail, A.H.3
  • 23
    • 4344579386 scopus 로고    scopus 로고
    • Ligand-induced changes in 2-aminopurine fluorescence as a probe for small molecule binding to HIV-1 PAR RNA
    • Bradrick,T.D. and Marino,J.P. (2004) Ligand-induced changes in 2-aminopurine fluorescence as a probe for small molecule binding to HIV-1 PAR RNA. RNA, 10, 1459-1468.
    • (2004) RNA , vol.10 , pp. 1459-1468
    • Bradrick, T.D.1    Marino, J.P.2
  • 24
    • 23944512612 scopus 로고    scopus 로고
    • Structural heterogeneity in DNA: Temperature dependence of 2-aminopurine fluorescence in dinucleotides
    • Somsen,O.J., Keukens,L.B., de Keijzer,M.N., van Hoek,A. and van Amerongen,H. (2005) Structural heterogeneity in DNA: Temperature dependence of 2-aminopurine fluorescence in dinucleotides. Chem. Phys. Chem., 6, 1622-1627.
    • (2005) Chem. Phys. Chem , vol.6 , pp. 1622-1627
    • Somsen, O.J.1    Keukens, L.B.2    de Keijzer, M.N.3    van Hoek, A.4    van Amerongen, H.5
  • 25
    • 0035969959 scopus 로고    scopus 로고
    • Probing structure and dynamics of DNA with 2-aminopurine: Effects of local environment on fluorescence
    • Rachofsky,E.L., Osman,R. and Ross,J.B. (2001) Probing structure and dynamics of DNA with 2-aminopurine: Effects of local environment on fluorescence. Biochemistry, 40, 946-956.
    • (2001) Biochemistry , vol.40 , pp. 946-956
    • Rachofsky, E.L.1    Osman, R.2    Ross, J.B.3
  • 26
    • 1642347123 scopus 로고    scopus 로고
    • Fluorescence-based approach for detecting and characterizing antibiotic-induced conformational changes in ribosomal RNA: Comparing aminoglycoside binding to prokaryotic and eukaryotic ribosomal RNA sequences
    • Kaul,M., Barbieri,C.M. and Pilch,D.S. (2004) Fluorescence-based approach for detecting and characterizing antibiotic-induced conformational changes in ribosomal RNA: Comparing aminoglycoside binding to prokaryotic and eukaryotic ribosomal RNA sequences. J. Am. Chem. Soc. 126, 3447-3453.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 3447-3453
    • Kaul, M.1    Barbieri, C.M.2    Pilch, D.S.3
  • 27
    • 28544438811 scopus 로고    scopus 로고
    • Using 2-aminopurine fluorescence to detect bacteriophage T4 DNA polymerase-DNA complexes that are important for primer extension and proofreading reactions
    • Hariharan,C. and Reha-Krantz,L.J. (2005) Using 2-aminopurine fluorescence to detect bacteriophage T4 DNA polymerase-DNA complexes that are important for primer extension and proofreading reactions. Biochemistry, 44, 15674-15684.
    • (2005) Biochemistry , vol.44 , pp. 15674-15684
    • Hariharan, C.1    Reha-Krantz, L.J.2
  • 28
    • 34250348104 scopus 로고    scopus 로고
    • Site-specific dynamics of strands in ss- and dsDNA as revealed by time-domain fluorescence of 2-aminopurine
    • Ramreddy,T., Rao,B.J. and Krishnamoorthy,G. (2007) Site-specific dynamics of strands in ss- and dsDNA as revealed by time-domain fluorescence of 2-aminopurine. J. Phys. Chem. B, 111, 5757-5766.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 5757-5766
    • Ramreddy, T.1    Rao, B.J.2    Krishnamoorthy, G.3
  • 29
    • 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. (1999) Nucleic acid sequence discrimination by the HIV-1 nucleocapsid protein NCp7: A fluorescence study. Biochemistry, 38, 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
  • 30
    • 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. (1998) Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides. J. Virol., 72, 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
  • 32
    • 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., Piemont,E., Ficheux,D., Roques,B.P., Darlix,J.L. and Mely,Y. (2002) 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, 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
  • 34
    • 0019201754 scopus 로고
    • Effect of fibrational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes
    • Lipari,G. and Szabo,A. (1980) Effect of fibrational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes. Biophys. J., 30, 489-506.
    • (1980) Biophys. J , vol.30 , pp. 489-506
    • Lipari, G.1    Szabo, A.2
  • 35
    • 0038750927 scopus 로고    scopus 로고
    • Steady-state and time-revolved fluorescence studies indicate an unusual conformation of 2-aminopurine within ATAT and TATA duplex DNA sequences
    • Rai,P., Cole,T.D., Thompson,E., Millar,D.P. and Linn,S. (2003) Steady-state and time-revolved fluorescence studies indicate an unusual conformation of 2-aminopurine within ATAT and TATA duplex DNA sequences. Nucleic Acids Res., 31, 2323-2332.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2323-2332
    • Rai, P.1    Cole, T.D.2    Thompson, E.3    Millar, D.P.4    Linn, S.5
  • 38
    • 0028128641 scopus 로고
    • Melting and premelting transitions of an oligomer measured by DNA base fluorescence and absorption
    • Xu,D., Evans,K.O. and Nordlund,T.M. (1994) Melting and premelting transitions of an oligomer measured by DNA base fluorescence and absorption. Biochemistry, 33, 9592-9599.
    • (1994) Biochemistry , vol.33 , pp. 9592-9599
    • Xu, D.1    Evans, K.O.2    Nordlund, T.M.3
  • 39
    • 0034896734 scopus 로고    scopus 로고
    • Probing the structure and dynamics of a DNA hairpin by ultrafast quenching and fluorescence depolarization
    • Larsen,O.F., van Stokkum,I.H., Gobets,B., van Grondelle,R. and van Amerongen,H. (2001) Probing the structure and dynamics of a DNA hairpin by ultrafast quenching and fluorescence depolarization. Biophys. J. 81, 1115-1126.
    • (2001) Biophys. J , vol.81 , pp. 1115-1126
    • Larsen, O.F.1    van Stokkum, I.H.2    Gobets, B.3    van Grondelle, R.4    van Amerongen, H.5
  • 40
    • 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
    • Beltz,H., Clauss,C., Piemont,E., Ficheux,D., Gorelick,R.J., Roques,B., Gabus,C., Darlix,J.L., de Rocquigny,H. et al. (2005) 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, 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    Gabus, C.7    Darlix, J.L.8    de Rocquigny, H.9
  • 41
    • 0029876943 scopus 로고    scopus 로고
    • Zinc binding to the HIV-1 nucleocapsid protein: A thermodynamic investigation by fluorescence spectroscopy
    • Mely,Y., De Rocquigny,H., Morellet,N., Roques,B.P. and Gerad,D. (1996) Zinc binding to the HIV-1 nucleocapsid protein: A thermodynamic investigation by fluorescence spectroscopy. Biochemistry, 35 5175-5182.
    • (1996) Biochemistry , vol.35 , pp. 5175-5182
    • Mely, Y.1    De Rocquigny, H.2    Morellet, N.3    Roques, B.P.4    Gerad, D.5
  • 43
    • 33750016312 scopus 로고    scopus 로고
    • Rapid kinetics of protein-nucleic acid interaction is a major component of HIV-1 nucleocapsid protein's nucleic acid chaperone function
    • Cruceanu,M., Gorelick,R.J., Musier-Forsyth,K., Rouzina,I. and Williams,M.C. (2006) Rapid kinetics of protein-nucleic acid interaction is a major component of HIV-1 nucleocapsid protein's nucleic acid chaperone function. J. Mol. Biol., 363, 867-877.
    • (2006) J. Mol. Biol , vol.363 , pp. 867-877
    • Cruceanu, M.1    Gorelick, R.J.2    Musier-Forsyth, K.3    Rouzina, I.4    Williams, M.C.5
  • 44
    • 0035814801 scopus 로고    scopus 로고
    • Phosphorescence and optically detected magnetic resonance of HIV-1 nucleocapsid protein complexes with stem-loop sequences of the genomic Psi-Tecognition element
    • Maki,A.H., Ozarowski,A., Misra,A., Urbaneja,M.A. and Casas-Finet,J.R. (2001) Phosphorescence and optically detected magnetic resonance of HIV-1 nucleocapsid protein complexes with stem-loop sequences of the genomic Psi-Tecognition element. Biochemistry, 40, 1403-1412.
    • (2001) Biochemistry , vol.40 , pp. 1403-1412
    • Maki, A.H.1    Ozarowski, A.2    Misra, A.3    Urbaneja, M.A.4    Casas-Finet, J.R.5
  • 45
    • 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
    • Amarasinghe,G.K., Zhou,J., Miskimon,M., Chancellor,K.J., McDonald,J.A., Matthews,A.G., Miller,R.R., Rouse,M.D. and Summers,M.F. (2001) 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, 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    Miller, R.R.7    Rouse, M.D.8    Summers, M.F.9
  • 46
    • 0033583086 scopus 로고    scopus 로고
    • Binding properties of the human immunodeficiency vinis 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. (1999) Binding properties of the human immunodeficiency vinis type 1 nucleocapsid protein p7 to a model RNA: elucidation of the structural determinants for function. J. Mol. Biol., 287, 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
  • 47
    • 0033020588 scopus 로고    scopus 로고
    • Time-resolved fluorescence investigation of the human immunodeficiency virus type 1 nucleocapsid protein: Influence of the binding of nucleic acids
    • Bombarda,E., Ababou,A., Vuilleumier,C., Gerard,D., Roques,B.P., Piemont,E. and Mely,Y. (1999) Time-resolved fluorescence investigation of the human immunodeficiency virus type 1 nucleocapsid protein: influence of the binding of nucleic acids. Biophys. J., 76, 1561-1570.
    • (1999) Biophys. J , vol.76 , pp. 1561-1570
    • Bombarda, E.1    Ababou, A.2    Vuilleumier, C.3    Gerard, D.4    Roques, B.P.5    Piemont, E.6    Mely, Y.7
  • 48
    • 0032570327 scopus 로고    scopus 로고
    • The annealing of tRNA3Lys to human immunodeficiency virus type 1 primer binding site is critically dependent on the NCp7 zinc fingers structure
    • Remy,E., de Rocquigny,H., Petitjean,P., Muriaux,D., Theilleux,V., Paoletti,J. and Roques,B.P. (1998) The annealing of tRNA3Lys to human immunodeficiency virus type 1 primer binding site is critically dependent on the NCp7 zinc fingers structure. J. Biol. Chem., 273, 4819-4822.
    • (1998) J. Biol. Chem , vol.273 , pp. 4819-4822
    • Remy, E.1    de Rocquigny, H.2    Petitjean, P.3    Muriaux, D.4    Theilleux, V.5    Paoletti, J.6    Roques, B.P.7
  • 49
    • 0037027319 scopus 로고    scopus 로고
    • 2-Aminopurine electronic structure and fluorescence properties in DNA
    • Jean,J.M. and Hall,K.B. (2002) 2-Aminopurine electronic structure and fluorescence properties in DNA. Biochemistry, 41, 13152-13161.
    • (2002) Biochemistry , vol.41 , pp. 13152-13161
    • Jean, J.M.1    Hall, K.B.2
  • 50
    • 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. (2003) DNA condensation by the nucleocapsid protein of HIV-1: A mechanism ensuring DNA protection. Nucleic Acids Res., 31, 5425-5432.
    • (2003) Nucleic Acids Res , vol.31 , pp. 5425-5432
    • Krishnamoorthy, G.1    Roques, B.2    Darlix, J.L.3    Mely, Y.4
  • 51
    • 0030916603 scopus 로고    scopus 로고
    • Recent solution structures of RNA and its complexes with drugs, peptides and proteins
    • Ramos,A., Gubser,C.C. and Varani,G. (1997) Recent solution structures of RNA and its complexes with drugs, peptides and proteins. Curr. Opin. Struct. Biol., 7, 317-323.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 317-323
    • Ramos, A.1    Gubser, C.C.2    Varani, G.3
  • 52
    • 0035838382 scopus 로고    scopus 로고
    • Current topics in RNA-protein recognition: Control of specificity and biological function through induced fit and conformational capture
    • Leulliot,N. and Varani,G. (2001) Current topics in RNA-protein recognition: Control of specificity and biological function through induced fit and conformational capture. Biochemistry, 40, 7947-7956.
    • (2001) Biochemistry , vol.40 , pp. 7947-7956
    • Leulliot, N.1    Varani, G.2
  • 53
    • 2942739181 scopus 로고    scopus 로고
    • Structure of the His44→ Ala single point mutant of the distal finger motif of HIV-1 nucleocapsid protein: A combined NMR, molecular dynamics simulation, and fluorescence study
    • Stote,R.H., Kellenberger,E., Muller,H., Bombarda,E., Roques,B.P., Kieffer,B. and Mely,Y. (2004) Structure of the His44→ Ala single point mutant of the distal finger motif of HIV-1 nucleocapsid protein: A combined NMR, molecular dynamics simulation, and fluorescence study. Biochemistry, 43, 7687-7697.
    • (2004) Biochemistry , vol.43 , pp. 7687-7697
    • Stote, R.H.1    Kellenberger, E.2    Muller, H.3    Bombarda, E.4    Roques, B.P.5    Kieffer, B.6    Mely, Y.7
  • 55
    • 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., Darlix,J.L. and Mely,Y. (2003) 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, 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    Darlix, J.L.7    Mely, Y.8
  • 56
    • 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. (2003) Destabilization of the HIV-1 complementary sequence of TAR by the nucleocapsid protein through activation of conformational fluctuations. J. Mol. Biol., 326, 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
  • 57
    • 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
    • Liu,H.W., Cosa,G., Landes,C.F., Zeng,Y., Kovaleski,B.J., Mullen,D.G., Barany,G., Musier-Forsyth,K. and Barbara,P.F. (2005) Single-molecule FRET studies of important intermediates in the nucleocapsid-protein-chaperoned minus-strand transfer step in HIV-1 reverse transcription. Biophys. J., 89, 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    Barany, G.7    Musier-Forsyth, K.8    Barbara, P.F.9
  • 58
    • 34248397617 scopus 로고    scopus 로고
    • Insights on the role of nucleic acid/protein interactions in chaperoned nucleic acid rearrangements of HIV-1 reverse transcription
    • Liu,H.W., Zeng,Y., Landes,C.F., Kim,Y.J., Zhu,Y., Ma,X., Vo,M.N., Musier-Forsyth,K. and Barbara,P.F. (2007) Insights on the role of nucleic acid/protein interactions in chaperoned nucleic acid rearrangements of HIV-1 reverse transcription. Proc. Natl Acad. Sci. USA, 104, 5261-5267.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 5261-5267
    • Liu, H.W.1    Zeng, Y.2    Landes, C.F.3    Kim, Y.J.4    Zhu, Y.5    Ma, X.6    Vo, M.N.7    Musier-Forsyth, K.8    Barbara, P.F.9
  • 59
    • 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.K., Harbron,E.J., O'Connor,D.B., Guo,J., Barbara,P.F., Levin,J.G. and Musier-Forsyth,K. (2003) Nucleic acid conformational changes essential for HIV-1 nucleocapsid protein-mediated inhibition of self-priming in minus-strand transfer. J. Mol. Biol., 325, 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
  • 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. (2004) 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, 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
  • 63
    • 35948977709 scopus 로고    scopus 로고
    • Investigating the mechanism of the nucleocapsid protein chaperoning of the second strand transfer during HIV-1 DNA synthesis
    • Ramalanjaona,N., Rocquigny,H.D., Millet,A., Ficheux,D., Darlix,J.L. and Mely,Y. (2007) Investigating the mechanism of the nucleocapsid protein chaperoning of the second strand transfer during HIV-1 DNA synthesis. J. Mol. Biol., 374, 1074-1053.
    • (2007) J. Mol. Biol , vol.374 , pp. 1074-1053
    • Ramalanjaona, N.1    Rocquigny, H.D.2    Millet, A.3    Ficheux, D.4    Darlix, J.L.5    Mely, Y.6
  • 64
    • 33748769274 scopus 로고    scopus 로고
    • Mechanistic studies of mini-TAR RNA/DNA annealing in the absence and presence of HIV-1 nucleocapsid protein
    • Vo,M.N., Barany,G., Rouzina,I. and Musier-Forsyth,K. (2006) Mechanistic studies of mini-TAR RNA/DNA annealing in the absence and presence of HIV-1 nucleocapsid protein. J. Mol. Biol., 363, 244-261.
    • (2006) J. Mol. Biol , vol.363 , pp. 244-261
    • Vo, M.N.1    Barany, G.2    Rouzina, I.3    Musier-Forsyth, K.4
  • 65
    • 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., Darlix,J.L. and Mely,Y. (2004) HIV-1 nucleocapsid protein binds to the viral DNA initiation sequences and chaperones their kissing interactions. J. Mol. Biol., 342, 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    Darlix, J.L.7    Mely, Y.8
  • 66
    • 29244449343 scopus 로고    scopus 로고
    • Investigation by fluorescence correlation spectroscopy of the chaperoning interactions of HIV-1 nucleocapsid protein with the viral DNA initiation sequences
    • Egele,C., Schaub,E., Piemont,E., de Rocquigny,H. and Mely,Y. (2005) Investigation by fluorescence correlation spectroscopy of the chaperoning interactions of HIV-1 nucleocapsid protein with the viral DNA initiation sequences. C. R. Biol., 328, 1041-1051.
    • (2005) C. R. Biol , vol.328 , pp. 1041-1051
    • Egele, C.1    Schaub, E.2    Piemont, E.3    de Rocquigny, H.4    Mely, Y.5
  • 67
    • 0037126724 scopus 로고    scopus 로고
    • Mechanism of nucleocapsid protein catalyzed structural isomerization of the dimerization initiation site of HIV-1
    • Rist,M.J. and Marino,J.P. (2002) Mechanism of nucleocapsid protein catalyzed structural isomerization of the dimerization initiation site of HIV-1. Biochemistry, 41, 14762-14770.
    • (2002) Biochemistry , vol.41 , pp. 14762-14770
    • Rist, M.J.1    Marino, J.P.2


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