메뉴 건너뛰기




Volumn 389, Issue 1, 2009, Pages 183-198

Molecular Interactions between HIV-1 Integrase and the Two Viral DNA Ends within the Synaptic Complex that Mediates Concerted Integration

Author keywords

HIV 1; integrase; preintegration complex; synaptic complex

Indexed keywords

DEOXYRIBONUCLEASE I; DIMER; INTEGRASE; NUCLEOTIDE; POLYMER; TETRAMER; VIRUS DNA; VIRUS NUCLEOPROTEIN;

EID: 67349245812     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.04.007     Document Type: Article
Times cited : (38)

References (52)
  • 1
    • 0001363865 scopus 로고    scopus 로고
    • Integration
    • Coffin J.M., Hughes S., and Varmus H. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Brown P.O. Integration. In: Coffin J.M., Hughes S., and Varmus H. (Eds). Retroviruses (1997), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 161-203
    • (1997) Retroviruses , pp. 161-203
    • Brown, P.O.1
  • 2
    • 0030972160 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition
    • Miller M.D., Farnet C.M., and Bushman F.D. Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. J. Virol. 71 (1997) 5382-5390
    • (1997) J. Virol. , vol.71 , pp. 5382-5390
    • Miller, M.D.1    Farnet, C.M.2    Bushman, F.D.3
  • 3
    • 0033546149 scopus 로고    scopus 로고
    • Multiple integrase functions are required to form the native structure of the human immunodeficiency virus type I intasome
    • Chen H., Wei S.Q., and Engelman A. Multiple integrase functions are required to form the native structure of the human immunodeficiency virus type I intasome. J. Biol. Chem. 274 (1999) 17358-17364
    • (1999) J. Biol. Chem. , vol.274 , pp. 17358-17364
    • Chen, H.1    Wei, S.Q.2    Engelman, A.3
  • 4
    • 0032169780 scopus 로고    scopus 로고
    • Footprints on the viral DNA ends in moloney murine leukemia virus preintegration complexes reflect a specific association with integrase
    • Wei S.Q., Mizuuchi K., and Craigie R. Footprints on the viral DNA ends in moloney murine leukemia virus preintegration complexes reflect a specific association with integrase. Proc. Natl Acad. Sci. USA 95 (1998) 10535-10540
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 10535-10540
    • Wei, S.Q.1    Mizuuchi, K.2    Craigie, R.3
  • 5
    • 0032846188 scopus 로고    scopus 로고
    • Structure-based mutagenesis of the human immunodeficiency virus type 1 DNA attachment site: effects on integration and cDNA synthesis
    • Brown H.E., Chen H., and Engelman A. Structure-based mutagenesis of the human immunodeficiency virus type 1 DNA attachment site: effects on integration and cDNA synthesis. J. Virol. 73 (1999) 9011-9020
    • (1999) J. Virol. , vol.73 , pp. 9011-9020
    • Brown, H.E.1    Chen, H.2    Engelman, A.3
  • 6
    • 0031682564 scopus 로고    scopus 로고
    • Specific and independent recognition of U3 and U5 att sites by human immunodeficiency virus type 1 integrase in vivo
    • Masuda T., Kuroda M.J., and Harada S. Specific and independent recognition of U3 and U5 att sites by human immunodeficiency virus type 1 integrase in vivo. J. Virol. 72 (1998) 8396-8402
    • (1998) J. Virol. , vol.72 , pp. 8396-8402
    • Masuda, T.1    Kuroda, M.J.2    Harada, S.3
  • 7
    • 0034812967 scopus 로고    scopus 로고
    • Asymmetric processing of human immunodeficiency virus type 1 cDNA in vivo: implications for functional end coupling during the chemical steps of DNA transposition
    • Chen H., and Engelman A. Asymmetric processing of human immunodeficiency virus type 1 cDNA in vivo: implications for functional end coupling during the chemical steps of DNA transposition. Mol. Cell Biol. 21 (2001) 6758-6767
    • (2001) Mol. Cell Biol. , vol.21 , pp. 6758-6767
    • Chen, H.1    Engelman, A.2
  • 8
    • 85158002042 scopus 로고    scopus 로고
    • Retroviral DNA Integration
    • Craig N.L., Craigie R., Gellert M., and Lambowitz A.M. (Eds), ASM Press, Washington, DC
    • Craigie R. Retroviral DNA Integration. In: Craig N.L., Craigie R., Gellert M., and Lambowitz A.M. (Eds). Mobile DNA II (2002), ASM Press, Washington, DC 613-630
    • (2002) Mobile DNA II , pp. 613-630
    • Craigie, R.1
  • 9
    • 33645864066 scopus 로고    scopus 로고
    • Retroviral DNA integration-mechanism and consequences
    • Lewinski M.K., and Bushman F.D. Retroviral DNA integration-mechanism and consequences. Adv. Genet. 55 (2005) 147-181
    • (2005) Adv. Genet. , vol.55 , pp. 147-181
    • Lewinski, M.K.1    Bushman, F.D.2
  • 11
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases
    • Dyda F., Hickman A.B., Jenkins T.M., Engelman A., Craigie R., and Davies D.R. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 266 (1994) 1981-1986
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 12
    • 0037126629 scopus 로고    scopus 로고
    • Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein
    • Wang J.Y., Ling H., Yang W., and Craigie R. Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein. EMBO J. 20 (2001) 7333-7343
    • (2001) EMBO J. , vol.20 , pp. 7333-7343
    • Wang, J.Y.1    Ling, H.2    Yang, W.3    Craigie, R.4
  • 13
    • 0035796559 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 integrase: arrangement of protein domains in active cDNA complexes
    • Gao K., Butler S.L., and Bushman F. Human immunodeficiency virus type 1 integrase: arrangement of protein domains in active cDNA complexes. EMBO J. 20 (2001) 3565-3576
    • (2001) EMBO J. , vol.20 , pp. 3565-3576
    • Gao, K.1    Butler, S.L.2    Bushman, F.3
  • 14
    • 0032510707 scopus 로고    scopus 로고
    • Photo-cross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex
    • Heuer T.S., and Brown P.O. Photo-cross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex. Biochemistry 37 (1998) 6667-6678
    • (1998) Biochemistry , vol.37 , pp. 6667-6678
    • Heuer, T.S.1    Brown, P.O.2
  • 15
    • 22144463200 scopus 로고    scopus 로고
    • Model of full-length HIV-1 integrase complexed with viral DNA as template for anti-HIV drug design
    • Karki R.G., Tang Y., Burke Jr. T.R., and Nicklaus M.C. Model of full-length HIV-1 integrase complexed with viral DNA as template for anti-HIV drug design. J. Comput. Aided Mol. Des. 18 (2004) 739-760
    • (2004) J. Comput. Aided Mol. Des. , vol.18 , pp. 739-760
    • Karki, R.G.1    Tang, Y.2    Burke Jr., T.R.3    Nicklaus, M.C.4
  • 16
    • 0037234457 scopus 로고    scopus 로고
    • Modeling HIV-1 integrase complexes based on their hydrodynamic properties
    • Podtelezhnikov A.A., Gao K., Bushman F.D., and McCammon J.A. Modeling HIV-1 integrase complexes based on their hydrodynamic properties. Biopolymers 68 (2003) 110-120
    • (2003) Biopolymers , vol.68 , pp. 110-120
    • Podtelezhnikov, A.A.1    Gao, K.2    Bushman, F.D.3    McCammon, J.A.4
  • 17
    • 41949095115 scopus 로고    scopus 로고
    • Subunit-specific protein footprinting reveals significant structural rearrangements and a role for N-terminal Lys-14 of HIV-1 Integrase during viral DNA binding
    • Zhao Z., McKee C.J., Kessl J.J., Santos W.L., Daigle J.E., Engelman A., et al. Subunit-specific protein footprinting reveals significant structural rearrangements and a role for N-terminal Lys-14 of HIV-1 Integrase during viral DNA binding. J. Biol. Chem. 283 (2008) 5632-5641
    • (2008) J. Biol. Chem. , vol.283 , pp. 5632-5641
    • Zhao, Z.1    McKee, C.J.2    Kessl, J.J.3    Santos, W.L.4    Daigle, J.E.5    Engelman, A.6
  • 18
    • 2942553781 scopus 로고    scopus 로고
    • Structure and function of HIV-1 integrase
    • Chiu T.K., and Davies D.R. Structure and function of HIV-1 integrase. Curr. Top. Med. Chem. 4 (2004) 965-977
    • (2004) Curr. Top. Med. Chem. , vol.4 , pp. 965-977
    • Chiu, T.K.1    Davies, D.R.2
  • 19
    • 85135598185 scopus 로고    scopus 로고
    • A three dimensional model of the human immunodeficiency virus type 1 integration complex
    • Wielens J., Crosby I., and Chalmers D. A three dimensional model of the human immunodeficiency virus type 1 integration complex. J. Comput. Aided Mol. Des. 18 (2005) 1-17
    • (2005) J. Comput. Aided Mol. Des. , vol.18 , pp. 1-17
    • Wielens, J.1    Crosby, I.2    Chalmers, D.3
  • 20
    • 58149091892 scopus 로고    scopus 로고
    • Defining the DNA substrate binding sites on HIV-1 integrase
    • Dolan J., Chen A., Weber I.T., Harrison R.W., and Leis J. Defining the DNA substrate binding sites on HIV-1 integrase. J. Mol. Biol. 385 (2009) 568-579
    • (2009) J. Mol. Biol. , vol.385 , pp. 568-579
    • Dolan, J.1    Chen, A.2    Weber, I.T.3    Harrison, R.W.4    Leis, J.5
  • 23
    • 33645285267 scopus 로고    scopus 로고
    • Retroviral DNA integration: reaction pathway and critical intermediates
    • Li M., Mizuuchi M., Burke Jr. T.R., and Craigie R. Retroviral DNA integration: reaction pathway and critical intermediates. EMBO J. 25 (2006) 1295-1304
    • (2006) EMBO J. , vol.25 , pp. 1295-1304
    • Li, M.1    Mizuuchi, M.2    Burke Jr., T.R.3    Craigie, R.4
  • 24
    • 36049049062 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type-1 concerted integration by strand transfer inhibitors which recognize a transient structural intermediate
    • Pandey K.K., Bera S., Zahm J., Vora A., Stillmock K., Hazuda D., et al. Inhibition of human immunodeficiency virus type-1 concerted integration by strand transfer inhibitors which recognize a transient structural intermediate. J. Virol. 81 (2007) 12189-12199
    • (2007) J. Virol. , vol.81 , pp. 12189-12199
    • Pandey, K.K.1    Bera, S.2    Zahm, J.3    Vora, A.4    Stillmock, K.5    Hazuda, D.6
  • 25
    • 50949119501 scopus 로고    scopus 로고
    • Mechanisms of human immunodeficiency virus type-1 concerted integration as related to strand transfer inhibition and drug resistance
    • Zahm J.A., Bera S., Pandey K.K., Vora A., Stillmock K., Hazuda D., et al. Mechanisms of human immunodeficiency virus type-1 concerted integration as related to strand transfer inhibition and drug resistance. Antimicrob. Agents Chemother. 52 (2008) 3358-3368
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 3358-3368
    • Zahm, J.A.1    Bera, S.2    Pandey, K.K.3    Vora, A.4    Stillmock, K.5    Hazuda, D.6
  • 26
    • 34247128760 scopus 로고    scopus 로고
    • Transcriptional coactivator LEDGF/p75 modulates human immunodeficiency virus type 1 integrase-mediated concerted integration
    • Pandey K.K., Sinha S., and Grandgenett D.P. Transcriptional coactivator LEDGF/p75 modulates human immunodeficiency virus type 1 integrase-mediated concerted integration. J. Virol. 81 (2007) 3969-3979
    • (2007) J. Virol. , vol.81 , pp. 3969-3979
    • Pandey, K.K.1    Sinha, S.2    Grandgenett, D.P.3
  • 27
    • 27944468727 scopus 로고    scopus 로고
    • Synaptic complex formation of two retrovirus DNA attachment sites by integrase: a fluorescence energy transfer study
    • Bera S., Vora A.C., Chiu R., Heyduk T., and Grandgenett D.P. Synaptic complex formation of two retrovirus DNA attachment sites by integrase: a fluorescence energy transfer study. Biochemistry 44 (2005) 15106-15114
    • (2005) Biochemistry , vol.44 , pp. 15106-15114
    • Bera, S.1    Vora, A.C.2    Chiu, R.3    Heyduk, T.4    Grandgenett, D.P.5
  • 28
    • 0036085517 scopus 로고    scopus 로고
    • Principles and biophysical applications of lanthanide-based probes
    • Selvin P.R. Principles and biophysical applications of lanthanide-based probes. Annu. Rev. Biophys. Biomol. Struct. 31 (2002) 275-302
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 275-302
    • Selvin, P.R.1
  • 29
    • 36048938734 scopus 로고    scopus 로고
    • Distance determination in proteIN-DNA complexes using fluorescence resonance energy transfer
    • Didenko V.V. (Ed), Humana Press, Totowa, NJ
    • Lorenz M., and Diekmann S. Distance determination in proteIN-DNA complexes using fluorescence resonance energy transfer. In: Didenko V.V. (Ed). Methods in Molecular Biology vol. 335 (2006), Humana Press, Totowa, NJ 243-256
    • (2006) Methods in Molecular Biology , vol.335 , pp. 243-256
    • Lorenz, M.1    Diekmann, S.2
  • 30
    • 15244360525 scopus 로고    scopus 로고
    • Architecture of recombination intermediates visualized by in-gel FRET of lambda integrase-Holliday junction-arm DNA complexes
    • Radman-Livaja M., Biswas T., Mierke D., and Landy A. Architecture of recombination intermediates visualized by in-gel FRET of lambda integrase-Holliday junction-arm DNA complexes. Proc. Natl Acad. Sci. USA 102 (2005) 3913-3920
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3913-3920
    • Radman-Livaja, M.1    Biswas, T.2    Mierke, D.3    Landy, A.4
  • 31
    • 0035088065 scopus 로고    scopus 로고
    • DNase protection analysis of retrovirus integrase at the viral DNA ends for full-site integration in vitro
    • Vora A., and Grandgenett D.P. DNase protection analysis of retrovirus integrase at the viral DNA ends for full-site integration in vitro. J. Virol. 75 (2001) 3556-3567
    • (2001) J. Virol. , vol.75 , pp. 3556-3567
    • Vora, A.1    Grandgenett, D.P.2
  • 32
    • 23844491860 scopus 로고    scopus 로고
    • Processing of viral DNA ends channels the HIV-1 integration reaction to concerted integration
    • Li M., and Craigie R. Processing of viral DNA ends channels the HIV-1 integration reaction to concerted integration. J. Biol. Chem. 280 (2005) 29334-29339
    • (2005) J. Biol. Chem. , vol.280 , pp. 29334-29339
    • Li, M.1    Craigie, R.2
  • 33
    • 0034723439 scopus 로고    scopus 로고
    • Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells
    • Hazuda D.J., Felock P., Witmer M., Wolfe A., Stillmock K., Grobler J.A., et al. Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells. Science 287 (2000) 646-650
    • (2000) Science , vol.287 , pp. 646-650
    • Hazuda, D.J.1    Felock, P.2    Witmer, M.3    Wolfe, A.4    Stillmock, K.5    Grobler, J.A.6
  • 34
    • 0031050297 scopus 로고    scopus 로고
    • Disruption of the terminal base pairs of retroviral DNA during integration
    • Scottoline B.P., Chow S., Ellison V., and Brown P.O. Disruption of the terminal base pairs of retroviral DNA during integration. Genes Dev. 11 (1997) 371-382
    • (1997) Genes Dev. , vol.11 , pp. 371-382
    • Scottoline, B.P.1    Chow, S.2    Ellison, V.3    Brown, P.O.4
  • 35
    • 0032189652 scopus 로고    scopus 로고
    • Sequence specificity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interaction
    • Esposito D., and Craigie R. Sequence specificity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interaction. EMBO J. 17 (1998) 5832-5843
    • (1998) EMBO J. , vol.17 , pp. 5832-5843
    • Esposito, D.1    Craigie, R.2
  • 36
    • 44949212848 scopus 로고    scopus 로고
    • Modeling, analysis, and validation of a novel HIV integrase structure provide insights into the binding modes of potent integrase inhibitors
    • Chen X., Tsiang M., Yu F., Hung M., Jones G.S., Zeynalzadegan A., et al. Modeling, analysis, and validation of a novel HIV integrase structure provide insights into the binding modes of potent integrase inhibitors. J. Mol. Biol. 380 (2008) 504-519
    • (2008) J. Mol. Biol. , vol.380 , pp. 504-519
    • Chen, X.1    Tsiang, M.2    Yu, F.3    Hung, M.4    Jones, G.S.5    Zeynalzadegan, A.6
  • 37
    • 12944270496 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase
    • Espeseth A.S., Felock P., Wolfe A., Witmer M., Grobler J., Anthony N., et al. HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase. Proc. Natl Acad. Sci. USA 97 (2000) 11244-11249
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 11244-11249
    • Espeseth, A.S.1    Felock, P.2    Wolfe, A.3    Witmer, M.4    Grobler, J.5    Anthony, N.6
  • 38
    • 3843108916 scopus 로고    scopus 로고
    • A naphthyridine carboxamide provides evidence for discordant resistance between mechanistically identical inhibitors of HIV-1 integrase
    • Hazuda D.J., Anthony N.J., Gomez R.P., Jolly S.M., Wai J.S., Zhuang L., et al. A naphthyridine carboxamide provides evidence for discordant resistance between mechanistically identical inhibitors of HIV-1 integrase. Proc. Natl Acad. Sci. USA 101 (2004) 11233-11238
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11233-11238
    • Hazuda, D.J.1    Anthony, N.J.2    Gomez, R.P.3    Jolly, S.M.4    Wai, J.S.5    Zhuang, L.6
  • 39
    • 58149154667 scopus 로고    scopus 로고
    • The terminal (catalytic) adenosine of the HIV LTR controls the kinetics of binding and dissociation of HIV integrase strand transfer inhibitors
    • Langley D., Samanta H.K., Lin Z., Walker M.A., Krystal M.R., and Dicker I.B. The terminal (catalytic) adenosine of the HIV LTR controls the kinetics of binding and dissociation of HIV integrase strand transfer inhibitors. Biochemistry 47 (2008) 13481-13488
    • (2008) Biochemistry , vol.47 , pp. 13481-13488
    • Langley, D.1    Samanta, H.K.2    Lin, Z.3    Walker, M.A.4    Krystal, M.R.5    Dicker, I.B.6
  • 41
    • 18344371347 scopus 로고    scopus 로고
    • Structural organization of bacterial RNA polymerase holoenzyme and the RNA polymerase-promoter open complex
    • Mekler V., Kortkhonjia E., Mukhopadhyay J., Knight J., Revyakin A., Kapanidis A.N., et al. Structural organization of bacterial RNA polymerase holoenzyme and the RNA polymerase-promoter open complex. Cell 108 (2002) 599-614
    • (2002) Cell , vol.108 , pp. 599-614
    • Mekler, V.1    Kortkhonjia, E.2    Mukhopadhyay, J.3    Knight, J.4    Revyakin, A.5    Kapanidis, A.N.6
  • 42
    • 48249139029 scopus 로고    scopus 로고
    • The structure of cyanine 5 terminally attached to double-stranded DNA: implications for FRET studies
    • Iqbal A., Wang L., Thompson K.C., Lilley D.M., and Norman D.G. The structure of cyanine 5 terminally attached to double-stranded DNA: implications for FRET studies. Biochemistry 47 (2008) 7857-7862
    • (2008) Biochemistry , vol.47 , pp. 7857-7862
    • Iqbal, A.1    Wang, L.2    Thompson, K.C.3    Lilley, D.M.4    Norman, D.G.5
  • 43
    • 0033776960 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer as a structural tool for nucleic acids
    • Lilley D.M., and Wilson T.J. Fluorescence resonance energy transfer as a structural tool for nucleic acids. Curr. Opin. Chem. Biol. 4 (2000) 507-517
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 507-517
    • Lilley, D.M.1    Wilson, T.J.2
  • 44
    • 0032617446 scopus 로고    scopus 로고
    • In vivo analysis of retroviral integrase structure and function
    • Engelman A. In vivo analysis of retroviral integrase structure and function. Adv. Virus Res. 52 (1999) 411-426
    • (1999) Adv. Virus Res. , vol.52 , pp. 411-426
    • Engelman, A.1
  • 45
    • 20744447462 scopus 로고    scopus 로고
    • Recombinant HIV-1 integrase exhibits a capacity for full-site integration in vitro that is comparable to that of purified preintegraton complexes from virus-infected cells
    • Sinha S., and Grandgenett D. Recombinant HIV-1 integrase exhibits a capacity for full-site integration in vitro that is comparable to that of purified preintegraton complexes from virus-infected cells. J. Virol. 79 (2005) 8208-8216
    • (2005) J. Virol. , vol.79 , pp. 8208-8216
    • Sinha, S.1    Grandgenett, D.2
  • 46
    • 0036118227 scopus 로고    scopus 로고
    • Efficient concerted integration by recombinant human immunodeficiency virus type 1 integrase without cellular or viral cofactors
    • Sinha S., Pursley M.H., and Grandgenett D.P. Efficient concerted integration by recombinant human immunodeficiency virus type 1 integrase without cellular or viral cofactors. J. Virol. 76 (2002) 3105-3113
    • (2002) J. Virol. , vol.76 , pp. 3105-3113
    • Sinha, S.1    Pursley, M.H.2    Grandgenett, D.P.3
  • 48
    • 0020679785 scopus 로고
    • Rhodamine-based compounds as fluorogenic substrates for serine proteinases
    • Leytus S.P., Melhado L.L., and Mangel W.F. Rhodamine-based compounds as fluorogenic substrates for serine proteinases. Biochem. J. 209 (1983) 299-307
    • (1983) Biochem. J. , vol.209 , pp. 299-307
    • Leytus, S.P.1    Melhado, L.L.2    Mangel, W.F.3
  • 49
    • 33947094704 scopus 로고
    • Absolute quantum yield determination by thermal blooming. Fluorescein
    • Brannon J.H., and Magde D. Absolute quantum yield determination by thermal blooming. Fluorescein. J. Phys. Chem. 82 (1978) 705-709
    • (1978) J. Phys. Chem. , vol.82 , pp. 705-709
    • Brannon, J.H.1    Magde, D.2
  • 50
    • 0028295796 scopus 로고
    • Resonance energy transfer: methods and applications
    • Wu P., and Brand L. Resonance energy transfer: methods and applications. Anal. Biochem. 218 (1994) 1-13
    • (1994) Anal. Biochem. , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 51
    • 0034732989 scopus 로고    scopus 로고
    • Location of cyanine-3 on double-stranded DNA: importance for fluorescence resonance energy transfer studies
    • Norman D.G., Grainger R.J., Uhrin D., and Lilley D.M. Location of cyanine-3 on double-stranded DNA: importance for fluorescence resonance energy transfer studies. Biochemistry 39 (2000) 6317-6324
    • (2000) Biochemistry , vol.39 , pp. 6317-6324
    • Norman, D.G.1    Grainger, R.J.2    Uhrin, D.3    Lilley, D.M.4
  • 52
    • 0028286320 scopus 로고
    • Folding of the multidomain human immunodeficiency virus type-I integrase
    • Grandgenett D.P., and Goodarzi G. Folding of the multidomain human immunodeficiency virus type-I integrase. Protein Sci. 3 (1994) 888-897
    • (1994) Protein Sci. , vol.3 , pp. 888-897
    • Grandgenett, D.P.1    Goodarzi, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.