메뉴 건너뛰기




Volumn 85, Issue 10, 2011, Pages 4654-4666

Sequential deletion of the integrase (Gag-Pol) carboxyl terminus reveals distinct phenotypic classes of defective HIV-1

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRASE;

EID: 79955398402     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02374-10     Document Type: Article
Times cited : (40)

References (83)
  • 1
    • 46949098038 scopus 로고    scopus 로고
    • Anti-infectives: Clinical progress of HIV-1 integrase inhibitors
    • Al-Mawsawi, L. Q., R. I. Al-Safi, and N. Neamati. 2008. Anti-infectives: clinical progress of HIV-1 integrase inhibitors. Expert Opin. Emerg. Drugs 13:213-225.
    • (2008) Expert Opin. Emerg. Drugs , vol.13 , pp. 213-225
    • Al-Mawsawi, L.Q.1    Al-Safi, R.I.2    Neamati, N.3
  • 2
    • 34250369626 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 1 integrase with cellular nuclear import receptor importin 7 and its impact on viral replication
    • Ao, Z., et al. 2007. Interaction of human immunodeficiency virus type 1 integrase with cellular nuclear import receptor importin 7 and its impact on viral replication. J. Biol. Chem. 282:13456-13467.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13456-13467
    • Ao, Z.1
  • 3
    • 0032567350 scopus 로고    scopus 로고
    • Structural determinants of metal-induced conformational changes in HIV-1 integrase
    • Asante-Appiah, E., S. H. Seeholzer, and A. M. Skalka. 1998. Structural determinants of metal-induced conformational changes in HIV-1 integrase. J. Biol. Chem. 273:35078-35087.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35078-35087
    • Asante-Appiah, E.1    Seeholzer, S.H.2    Skalka, A.M.3
  • 4
    • 0030922072 scopus 로고    scopus 로고
    • A metal-induced conformational change and activation of HIV-1 integrase
    • Asante-Appiah, E., and A. M. Skalka. 1997. A metal-induced conformational change and activation of HIV-1 integrase. J. Biol. Chem. 272:16196-16205.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16196-16205
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0029815034 scopus 로고    scopus 로고
    • Lack of integrase can markedly affect human immunodeficiency virus type 1 particle production in the presence of an active viral protease
    • Bukovsky, A., and H. Gottlinger. 1996. Lack of integrase can markedly affect human immunodeficiency virus type 1 particle production in the presence of an active viral protease. J. Virol. 70:6820-6825.
    • (1996) J. Virol. , vol.70 , pp. 6820-6825
    • Bukovsky, A.1    Gottlinger, H.2
  • 7
    • 0026655897 scopus 로고
    • Structural implications of spectroscopic characterization of a putative zinc finger peptide from HIV-1 integrase
    • Burke, C. J., et al. 1992. Structural implications of spectroscopic characterization of a putative zinc finger peptide from HIV-1 integrase. J. Biol. Chem. 267:9639-9644.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9639-9644
    • Burke, C.J.1
  • 8
    • 0030986376 scopus 로고    scopus 로고
    • Solution structure of the N-terminal zinc binding domain of HIV-1 integrase
    • Cai, M., et al. 1997. Solution structure of the N-terminal zinc binding domain of HIV-1 integrase. Nat. Struct. Biol. 4:567-577.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 567-577
    • Cai, M.1
  • 9
    • 0347949560 scopus 로고    scopus 로고
    • Incorporation of Pol into human immunodeficiency virus type 1 Gag virus-like particles occurs independently of the upstream Gag domain in Gag-Pol
    • Cen, S., et al. 2004. Incorporation of Pol into human immunodeficiency virus type 1 Gag virus-like particles occurs independently of the upstream Gag domain in Gag-Pol. J. Virol. 78:1042-1049.
    • (2004) J. Virol. , vol.78 , pp. 1042-1049
    • Cen, S.1
  • 10
    • 27144463461 scopus 로고    scopus 로고
    • Acetylation of HIV-1 integrase by p300 regulates viral integration
    • Cereseto, A., et al. 2005. Acetylation of HIV-1 integrase by p300 regulates viral integration. EMBO J. 24:3070-3081.
    • (2005) EMBO J , vol.24 , pp. 3070-3081
    • Cereseto, A.1
  • 11
    • 0027965903 scopus 로고
    • HIV-1 reverse transcription. A termination step at the center of the genome
    • Charneau, P., et al. 1994. HIV-1 reverse transcription. A termination step at the center of the genome. J. Mol. Biol. 241:651-662.
    • (1994) J. Mol. Biol. , vol.241 , pp. 651-662
    • Charneau, P.1
  • 12
    • 0034682511 scopus 로고    scopus 로고
    • Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: A model for viral DNA binding
    • Chen, J. C., et al. 2000. Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding. Proc. Natl. Acad. Sci. U. S. A. 97:8233-8238.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8233-8238
    • Chen, J.C.1
  • 13
    • 77951859479 scopus 로고    scopus 로고
    • Integrase illuminated
    • Cherepanov, P. 2010. Integrase illuminated. EMBO Rep. 11:328.
    • (2010) EMBO Rep , vol.11 , pp. 328
    • Cherepanov, P.1
  • 14
    • 0026672676 scopus 로고
    • Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: Definition of critical amino acids involved in cell tropism
    • Chesebro, B., K. Wehrly, J. Nishio, and S. Perryman. 1992. Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: definition of critical amino acids involved in cell tropism. J. Virol. 66:6547-6554.
    • (1992) J. Virol. , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4
  • 15
    • 0036118327 scopus 로고    scopus 로고
    • Coding sequences upstream of the human immunodeficiency virus type 1 reverse transcriptase domain in Gag-Pol are not essential for incorporation of the Pr160(gag-pol) into virus particles
    • Chiu, H. C., S. Y. Yao, and C. T. Wang. 2002. Coding sequences upstream of the human immunodeficiency virus type 1 reverse transcriptase domain in Gag-Pol are not essential for incorporation of the Pr160(gag-pol) into virus particles. J. Virol. 76:3221-3231.
    • (2002) J. Virol. , vol.76 , pp. 3221-3231
    • Chiu, H.C.1    Yao, S.Y.2    Wang, C.T.3
  • 16
    • 0030659177 scopus 로고    scopus 로고
    • Presence of an inducible HIV-1 latent reservoir during highly active antiretroviral therapy
    • Chun, T. W., et al. 1997. Presence of an inducible HIV-1 latent reservoir during highly active antiretroviral therapy. Proc. Natl. Acad. Sci. U. S. A. 94:13193-13197.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13193-13197
    • Chun, T.W.1
  • 17
    • 70450273192 scopus 로고    scopus 로고
    • Biochemical and virological analysis of the 18-residue C-terminal tail of HIV-1 integrase
    • Dar, M. J., et al. 2009. Biochemical and virological analysis of the 18-residue C-terminal tail of HIV-1 integrase. Retrovirology 6:94.
    • (2009) Retrovirology , vol.6 , pp. 94
    • Dar, M.J.1
  • 18
  • 19
    • 0034824775 scopus 로고    scopus 로고
    • Mapping DNA-binding sites of HIV-1 integrase by protein footprinting
    • Dirac, A. M., and J. Kjems. 2001. Mapping DNA-binding sites of HIV-1 integrase by protein footprinting. Eur. J. Biochem. 268:743-751.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 743-751
    • Dirac, A.M.1    Kjems, J.2
  • 20
    • 35348823104 scopus 로고    scopus 로고
    • Molecular mechanisms by which human immunodeficiency virus type 1 integrase stimulates the early steps of reverse transcription
    • Dobard, C. W., M. S. Briones, and S. A. Chow. 2007. Molecular mechanisms by which human immunodeficiency virus type 1 integrase stimulates the early steps of reverse transcription. J. Virol. 81:10037-10046.
    • (2007) J. Virol. , vol.81 , pp. 10037-10046
    • Dobard, C.W.1    Briones, M.S.2    Chow, S.A.3
  • 21
    • 0026740842 scopus 로고
    • Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 IN protein in vitro
    • Drelich, M., R. Wilhelm, and J. Mous. 1992. Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 IN protein in vitro. Virology 188:459-468.
    • (1992) Virology , vol.188 , pp. 459-468
    • Drelich, M.1    Wilhelm, R.2    Mous, J.3
  • 22
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda, F., et al. 1994. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 266:1981-1986.
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1
  • 23
    • 0029145047 scopus 로고
    • The DNA-binding domain of HIV-1 integrase has an SH3-like fold
    • Eijkelenboom, A. P., et al. 1995. The DNA-binding domain of HIV-1 integrase has an SH3-like fold. Nat. Struct. Biol. 2:807-810.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 807-810
    • Eijkelenboom, A.P.1
  • 24
    • 0032791840 scopus 로고    scopus 로고
    • Refined solution structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase
    • Eijkelenboom, A. P., et al. 1999. Refined solution structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase. Proteins 36:556-64.
    • (1999) Proteins , vol.36 , pp. 556-564
    • Eijkelenboom, A.P.1
  • 25
    • 0032617446 scopus 로고    scopus 로고
    • In vivo analysis of retroviral integrase structure and function
    • Engelman, A. 1999. In vivo analysis of retroviral integrase structure and function. Adv. Virus Res. 52:411-426.
    • (1999) Adv. Virus Res. , vol.52 , pp. 411-426
    • Engelman, A.1
  • 26
    • 0027179694 scopus 로고
    • Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex
    • Engelman, A., F. D. Bushman, and R. Craigie. 1993. Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex. EMBO J. 12:3269-3275.
    • (1993) EMBO J , vol.12 , pp. 3269-3275
    • Engelman, A.1    Bushman, F.D.2    Craigie, R.3
  • 27
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro
    • Engelman, A., and R. Craigie. 1992. Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro. J. Virol. 66:6361-6369.
    • (1992) J. Virol. , vol.66 , pp. 6361-6369
    • Engelman, A.1    Craigie, R.2
  • 28
    • 0028915128 scopus 로고
    • Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication
    • Engelman, A., G. Englund, J. M. Orenstein, M. A. Martin, and R. Craigie. 1995. Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication. J. Virol. 69:2729-2736.
    • (1995) J. Virol. , vol.69 , pp. 2729-2736
    • Engelman, A.1    Englund, G.2    Orenstein, J.M.3    Martin, M.A.4    Craigie, R.5
  • 29
    • 0028067324 scopus 로고
    • The core and carboxyl-terminal domains of the integrase protein of human immunodeficiency virus type 1 each contribute to nonspecific DNA binding
    • Engelman, A., A. B. Hickman, and R. Craigie. 1994. The core and carboxyl-terminal domains of the integrase protein of human immunodeficiency virus type 1 each contribute to nonspecific DNA binding. J. Virol. 68:5911-5917.
    • (1994) J. Virol. , vol.68 , pp. 5911-5917
    • Engelman, A.1    Hickman, A.B.2    Craigie, R.3
  • 30
    • 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 R. Craigie. 1998. Sequence specificity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interaction. EMBO J. 17:5832-5843.
    • (1998) EMBO J , vol.17 , pp. 5832-5843
    • Esposito, D.1    Craigie, R.2
  • 31
    • 14244264128 scopus 로고    scopus 로고
    • HIV-1 integrase crosslinked oligomers are active in vitro
    • Faure, A., et al. 2005. HIV-1 integrase crosslinked oligomers are active in vitro. Nucleic Acids Res. 33:977-986.
    • (2005) Nucleic Acids Res , vol.33 , pp. 977-986
    • Faure, A.1
  • 32
    • 0030792182 scopus 로고    scopus 로고
    • Complementation of integrase function in HIV-1 virions
    • Fletcher, T. M., III, et al. 1997. Complementation of integrase function in HIV-1 virions. EMBO J. 16:5123-5138.
    • (1997) EMBO J , vol.16 , pp. 5123-5138
    • Fletcher III, T.M.1
  • 33
    • 0035796559 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 integrase: Arrangement of protein domains in active cDNA complexes
    • Gao, K., S. L. Butler, and F. Bushman. 2001. Human immunodeficiency virus type 1 integrase: arrangement of protein domains in active cDNA complexes. EMBO J. 20:3565-3576.
    • (2001) EMBO J , vol.20 , pp. 3565-3576
    • Gao, K.1    Butler, S.L.2    Bushman, F.3
  • 34
    • 0032483022 scopus 로고    scopus 로고
    • Three new structures of the core domain of HIV-1 integrase: An active site that binds magnesium
    • Goldgur, Y., et al. 1998. Three new structures of the core domain of HIV-1 integrase: an active site that binds magnesium. Proc. Natl. Acad. Sci. U. S. A. 95:9150-9154.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9150-9154
    • Goldgur, Y.1
  • 35
    • 33747330377 scopus 로고    scopus 로고
    • Relationship between the oligomeric status of HIV-1 integrase on DNA and enzymatic activity
    • Guiot, E., et al. 2006. Relationship between the oligomeric status of HIV-1 integrase on DNA and enzymatic activity. J. Biol. Chem. 281:22707-22719.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22707-22719
    • Guiot, E.1
  • 36
    • 33744908820 scopus 로고    scopus 로고
    • Identification of a novel human immunodeficiency virus type 1 integrase interactor, Gemin2, that facilitates efficient viral cDNA synthesis in vivo
    • Hamamoto, S., H. Nishitsuji, T. Amagasa, M. Kannagi, and T. Masuda. 2006. Identification of a novel human immunodeficiency virus type 1 integrase interactor, Gemin2, that facilitates efficient viral cDNA synthesis in vivo. J. Virol. 80:5670-5677.
    • (2006) J. Virol. , vol.80 , pp. 5670-5677
    • Hamamoto, S.1    Nishitsuji, H.2    Amagasa, T.3    Kannagi, M.4    Masuda, T.5
  • 37
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare, S., S. S. Gupta, E. Valkov, A. Engelman, and P. Cherepanov. 2010. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 464:232-236.
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 38
    • 78650533230 scopus 로고    scopus 로고
    • Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance
    • Hare, S., et al. 2010. Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. Proc. Natl. Acad. Sci. U. S. A. 107: 20057-20062.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 20057-20062
    • Hare, S.1
  • 39
    • 0029562273 scopus 로고
    • Characterization of the DNA-binding activity of HIV-1 integrase using a filter binding assay
    • Haugan, I. R., B. M. Nilsen, S. Worland, L. Olsen, and D. E. Helland. 1995. Characterization of the DNA-binding activity of HIV-1 integrase using a filter binding assay. Biochem. Biophys. Res. Commun. 217:802-810.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 802-810
    • Haugan, I.R.1    Nilsen, B.M.2    Worland, S.3    Olsen, L.4    Helland, D.E.5
  • 40
    • 0034723439 scopus 로고    scopus 로고
    • Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells
    • Hazuda, D. J., et al. 2000. Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells. Science 287:646-650.
    • (2000) Science , vol.287 , pp. 646-650
    • Hazuda, D.J.1
  • 41
    • 2342648913 scopus 로고    scopus 로고
    • Interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase proteins
    • Hehl, E. A., P. Joshi, G. V. Kalpana, and V. R. Prasad. 2004. Interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase proteins. J. Virol. 78:5056-5067.
    • (2004) J. Virol. , vol.78 , pp. 5056-5067
    • Hehl, E.A.1    Joshi, P.2    Kalpana, G.V.3    Prasad, V.R.4
  • 42
    • 0030875813 scopus 로고    scopus 로고
    • Mapping features of HIV-1 integrase near selected sites on viral and target DNA molecules in an active enzymeDNA complex by photo-cross-linking
    • Heuer, T. S., and P. O. Brown. 1997. Mapping features of HIV-1 integrase near selected sites on viral and target DNA molecules in an active enzymeDNA complex by photo-cross-linking. Biochemistry 36:10655-10665.
    • (1997) Biochemistry , vol.36 , pp. 10655-10665
    • Heuer, T.S.1    Brown, P.O.2
  • 43
    • 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 P. O. Brown. 1998. Photo-cross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex. Biochemistry 37:6667-6678.
    • (1998) Biochemistry , vol.37 , pp. 6667-6678
    • Heuer, T.S.1    Brown, P.O.2
  • 44
    • 0029980485 scopus 로고    scopus 로고
    • A soluble active mutant of HIV-1 integrase: Involvement of both the core and carboxyl-terminal domains in multimerization
    • Jenkins, T. M., A. Engelman, R. Ghirlando, and R. Craigie. 1996. A soluble active mutant of HIV-1 integrase: involvement of both the core and carboxyl-terminal domains in multimerization. J. Biol. Chem. 271:7712-7718.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.4
  • 45
    • 0030828521 scopus 로고    scopus 로고
    • Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking
    • Jenkins, T. M., D. Esposito, A. Engelman, and R. Craigie. 1997. Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking. EMBO J. 16:6849-6859.
    • (1997) EMBO J , vol.16 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 46
    • 77957670046 scopus 로고    scopus 로고
    • Structure-based modeling of the functional HIV-1 intasome and its inhibition
    • Krishnan, L., et al. 2010. Structure-based modeling of the functional HIV-1 intasome and its inhibition. Proc. Natl. Acad. Sci. U. S. A. 107: 15910-15915.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 15910-15915
    • Krishnan, L.1
  • 47
    • 0026719238 scopus 로고
    • Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases
    • Kulkosky, J., K. S. Jones, R. A. Katz, J. P. Mack, and A. M. Skalka. 1992. Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases. Mol. Cell. Biol. 12:2331-2338.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2331-2338
    • Kulkosky, J.1    Jones, K.S.2    Katz, R.A.3    Mack, J.P.4    Skalka, A.M.5
  • 48
    • 0030030041 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 integrase mutants retain in vitro integrase activity yet fail to integrate viral DNA efficiently during infection
    • Leavitt, A. D., G. Robles, N. Alesandro, and H. E. Varmus. 1996. Human immunodeficiency virus type 1 integrase mutants retain in vitro integrase activity yet fail to integrate viral DNA efficiently during infection. J. Virol. 70:721-728.
    • (1996) J. Virol. , vol.70 , pp. 721-728
    • Leavitt, A.D.1    Robles, G.2    Alesandro, N.3    Varmus, H.E.4
  • 49
    • 33645285267 scopus 로고    scopus 로고
    • Retroviral DNA integration: Reaction pathway and critical intermediates
    • Li, M., M. Mizuuchi, T. R. Burke, Jr., and R. Craigie. 2006. Retroviral DNA integration: reaction pathway and critical intermediates. EMBO J. 25:1295- 1304.
    • (2006) EMBO J. , vol.25 , pp. 1295-1304
    • Li, M.1    Mizuuchi, M.2    Burke Jr., T.R.3    Craigie, R.4
  • 50
    • 34248391815 scopus 로고    scopus 로고
    • Incorporation of human immunodeficiency virus type 1 reverse transcriptase into virus-like particles
    • Liao, W. H., et al. 2007. Incorporation of human immunodeficiency virus type 1 reverse transcriptase into virus-like particles. J. Virol. 81:5155-5165.
    • (2007) J. Virol. , vol.81 , pp. 5155-5165
    • Liao, W.H.1
  • 51
    • 33847261670 scopus 로고    scopus 로고
    • Characterization of HIV-1 integrase N-terminal mutant viruses
    • Lloyd, A. G., Y. S. Ng, M. A. Muesing, V. Simon, and L. C. Mulder. 2007. Characterization of HIV-1 integrase N-terminal mutant viruses. Virology 360:129-135.
    • (2007) Virology , vol.360 , pp. 129-135
    • Lloyd, A.G.1    Ng, Y.S.2    Muesing, M.A.3    Simon, V.4    Mulder, L.C.5
  • 52
    • 0029116747 scopus 로고
    • Solution structure of the DNA binding domain of HIV-1 integrase
    • Lodi, P. J., et al. 1995. Solution structure of the DNA binding domain of HIV-1 integrase. Biochemistry 34:9826-9833.
    • (1995) Biochemistry , vol.34 , pp. 9826-9833
    • Lodi, P.J.1
  • 53
    • 70349320511 scopus 로고    scopus 로고
    • Natural polymorphisms of human immunodeficiency virus type 1 integrase and inherent susceptibilities to a panel of integrase inhibitors
    • Low, A., et al. 2009. Natural polymorphisms of human immunodeficiency virus type 1 integrase and inherent susceptibilities to a panel of integrase inhibitors. Antimicrob. Agents Chemother. 53:4275-4282.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 4275-4282
    • Low, A.1
  • 54
    • 23244433627 scopus 로고    scopus 로고
    • Genetic analyses of conserved residues in the carboxyl-terminal domain of human immunodeficiency virus type 1 integrase
    • Lu, R., H. Z. Ghory, and A. Engelman. 2005. Genetic analyses of conserved residues in the carboxyl-terminal domain of human immunodeficiency virus type 1 integrase. J. Virol. 79:10356-10368.
    • (2005) J. Virol. , vol.79 , pp. 10356-10368
    • Lu, R.1    Ghory, H.Z.2    Engelman, A.3
  • 55
    • 34250857925 scopus 로고    scopus 로고
    • Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation
    • Luo, K., et al. 2007. Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. J. Virol. 81:7238-7248.
    • (2007) J. Virol. , vol.81 , pp. 7238-7248
    • Luo, K.1
  • 56
    • 0001166515 scopus 로고    scopus 로고
    • Structure-based mutational analysis of the C-terminal DNA-binding domain of human immunodeficiency virus type 1 integrase: Critical residues for protein oligomerization and DNA binding
    • Lutzke, R. A., and R. H. Plasterk. 1998. Structure-based mutational analysis of the C-terminal DNA-binding domain of human immunodeficiency virus type 1 integrase: critical residues for protein oligomerization and DNA binding. J. Virol. 72:4841-4848.
    • (1998) J. Virol. , vol.72 , pp. 4841-4848
    • Lutzke, R.A.1    Plasterk, R.H.2
  • 57
    • 0028034050 scopus 로고
    • Characterization of the minimal DNA-binding domain of the HIV integrase protein
    • Lutzke, R. A., C. Vink, and R. H. Plasterk. 1994. Characterization of the minimal DNA-binding domain of the HIV integrase protein. Nucleic Acids Res. 22:4125-4131.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4125-4131
    • Lutzke, R.A.1    Vink, C.2    Plasterk, R.H.3
  • 58
    • 78149434355 scopus 로고    scopus 로고
    • The mechanism of retroviral integration from X-ray structures of its key intermediates
    • Maertens, G. N., S. Hare, and P. Cherepanov. 2010. The mechanism of retroviral integration from X-ray structures of its key intermediates. Nature 468:326-329.
    • (2010) Nature , vol.468 , pp. 326-329
    • Maertens, G.N.1    Hare, S.2    Cherepanov, P.3
  • 59
    • 0028871705 scopus 로고
    • Genetic analysis of human immunodeficiency virus type 1 integrase and the U3 att site: Unusual phenotype of mutants in the zinc finger-like domain
    • Masuda, T., V. Planelles, P. Krogstad, and I. S. Chen. 1995. Genetic analysis of human immunodeficiency virus type 1 integrase and the U3 att site: unusual phenotype of mutants in the zinc finger-like domain. J. Virol. 69: 6687-6696.
    • (1995) J. Virol. , vol.69 , pp. 6687-6696
    • Masuda, T.1    Planelles, V.2    Krogstad, P.3    Chen, I.S.4
  • 60
    • 33947713897 scopus 로고    scopus 로고
    • The N-end rule pathway for regulated proteolysis: Prokaryotic and eukaryotic strategies
    • Mogk, A., R. Schmidt, and B. Bukau. 2007. The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol. 17:165-172.
    • (2007) Trends Cell Biol , vol.17 , pp. 165-172
    • Mogk, A.1    Schmidt, R.2    Bukau, B.3
  • 61
    • 0344766077 scopus 로고    scopus 로고
    • Primary human immunodeficiency virus type 2 (HIV-2) isolates, like HIV-1 isolates, frequently use CCR5 but show promiscuity in coreceptor usage
    • Morner, A., et al. 1999. Primary human immunodeficiency virus type 2 (HIV-2) isolates, like HIV-1 isolates, frequently use CCR5 but show promiscuity in coreceptor usage. J. Virol. 73:2343-2349.
    • (1999) J. Virol. , vol.73 , pp. 2343-2349
    • Morner, A.1
  • 62
    • 34748827049 scopus 로고    scopus 로고
    • von Hippel Lindau binding protein 1-mediated degradation of integrase affects HIV-1 gene expression at a postintegration step
    • Mousnier, A., et al. 2007. von Hippel Lindau binding protein 1-mediated degradation of integrase affects HIV-1 gene expression at a postintegration step. Proc. Natl. Acad. Sci. U. S. A. 104:13615-13620.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 13615-13620
    • Mousnier, A.1
  • 63
    • 0024431684 scopus 로고
    • In vivo footprinting of a muscle specific enhancer by ligation mediated PCR
    • Mueller, P. R., and B. Wold. 1989. In vivo footprinting of a muscle specific enhancer by ligation mediated PCR. Science 246:780-786.
    • (1989) Science , vol.246 , pp. 780-786
    • Mueller, P.R.1    Wold, B.2
  • 64
    • 0037178886 scopus 로고    scopus 로고
    • Interaction of HIV-1 integrase with DNA repair protein hRad18
    • Mulder, L. C., L. A. Chakrabarti, and M. A. Muesing. 2002. Interaction of HIV-1 integrase with DNA repair protein hRad18. J. Biol. Chem. 277: 27489-27493.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27489-27493
    • Mulder, L.C.1    Chakrabarti, L.A.2    Muesing, M.A.3
  • 65
    • 0034703066 scopus 로고    scopus 로고
    • Degradation of HIV-1 integrase by the N-end rule pathway
    • Mulder, L. C., and M. A. Muesing. 2000. Degradation of HIV-1 integrase by the N-end rule pathway. J. Biol. Chem. 275:29749-29753.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29749-29753
    • Mulder, L.C.1    Muesing, M.A.2
  • 66
    • 0029670765 scopus 로고    scopus 로고
    • Monoclonal antibodies against human immunodeficiency virus type 1 integrase: Epitope mapping and differential effects on integrase activities in vitro
    • Nilsen, B. M., et al. 1996. Monoclonal antibodies against human immunodeficiency virus type 1 integrase: epitope mapping and differential effects on integrase activities in vitro. J. Virol. 70:1580-1587.
    • (1996) J. Virol. , vol.70 , pp. 1580-1587
    • Nilsen, B.M.1
  • 67
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy, A. M., N. C. Gaddis, J. D. Choi, and M. H. Malim. 2002. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 68
    • 0026683120 scopus 로고
    • Epitope mapping of HIV-1 reverse transcriptase with monoclonal antibodies that inhibit polymerase and RNase H activities
    • Szilvay, A. M., et al. 1992. Epitope mapping of HIV-1 reverse transcriptase with monoclonal antibodies that inhibit polymerase and RNase H activities. J. Acquir. Immune Defic. Syndr. 5:647-657.
    • (1992) J. Acquir. Immune Defic. Syndr. , vol.5 , pp. 647-657
    • Szilvay, A.M.1
  • 69
    • 23344452833 scopus 로고    scopus 로고
    • A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons
    • Tasaki, T., et al. 2005. A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons. Mol. Cell. Biol. 25: 7120-7136.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7120-7136
    • Tasaki, T.1
  • 70
    • 0035914054 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase and integrase enzymes physically interact and inhibit each other
    • Tasara, T., G. Maga, M. O. Hottiger, and U. Hubscher. 2001. HIV-1 reverse transcriptase and integrase enzymes physically interact and inhibit each other. FEBS Lett. 507:39-44.
    • (2001) FEBS Lett , vol.507 , pp. 39-44
    • Tasara, T.1    Maga, G.2    Hottiger, M.O.3    Hubscher, U.4
  • 71
    • 33847657288 scopus 로고    scopus 로고
    • Posttranslational acetylation of the human immunodeficiency virus type 1 integrase carboxyl-terminal domain is dispensable for viral replication
    • Topper, M., et al. 2007. Posttranslational acetylation of the human immunodeficiency virus type 1 integrase carboxyl-terminal domain is dispensable for viral replication. J. Virol. 81:3012-3017.
    • (2007) J. Virol. , vol.81 , pp. 3012-3017
    • Topper, M.1
  • 72
    • 0033997592 scopus 로고    scopus 로고
    • Identification of critical amino acid residues in human immunodeficiency virus type 1 IN required for efficient proviral DNA formation at steps prior to integration in dividing and nondividing cells
    • Tsurutani, N., et al. 2000. Identification of critical amino acid residues in human immunodeficiency virus type 1 IN required for efficient proviral DNA formation at steps prior to integration in dividing and nondividing cells. J. Virol. 74:4795-4806.
    • (2000) J. Virol. , vol.74 , pp. 4795-4806
    • Tsurutani, N.1
  • 73
    • 0026668776 scopus 로고
    • Mutational analysis of the integrase protein of human immunodeficiency virus type 2
    • van Gent, D. C., A. A. Groeneger, and R. H. Plasterk. 1992. Mutational analysis of the integrase protein of human immunodeficiency virus type 2. Proc. Natl. Acad. Sci. U. S. A. 89:9598-9602.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 9598-9602
    • van Gent, D.C.1    Groeneger, A.A.2    Plasterk, R.H.3
  • 74
    • 0027246609 scopus 로고
    • Complementation between HIV integrase proteins mutated in different domains
    • van Gent, D. C., C. Vink, A. A. Groeneger, and R. H. Plasterk. 1993. Complementation between HIV integrase proteins mutated in different domains. EMBO J. 12:3261-3267.
    • (1993) EMBO J , vol.12 , pp. 3261-3267
    • van Gent, D.C.1    Vink, C.2    Groeneger, A.A.3    Plasterk, R.H.4
  • 75
    • 0027210608 scopus 로고
    • Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein
    • Vink, C., A. M. Oude Groeneger, and R. H. Plasterk. 1993. Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein. Nucleic Acids Res. 21:1419-1425.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude Groeneger, A.M.2    Plasterk, R.H.3
  • 76
    • 0242492858 scopus 로고    scopus 로고
    • The human polycomb group EED protein interacts with the integrase of human immunodeficiency virus type 1
    • Violot, S., et al. 2003. The human polycomb group EED protein interacts with the integrase of human immunodeficiency virus type 1. J. Virol. 77: 12507-12522.
    • (2003) J. Virol. , vol.77 , pp. 12507-12522
    • Violot, S.1
  • 77
    • 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., H. Ling, W. Yang, and R. Craigie. 2001. Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein. EMBO J. 20:7333-7343.
    • (2001) EMBO J , vol.20 , pp. 7333-7343
    • Wang, J.Y.1    Ling, H.2    Yang, W.3    Craigie, R.4
  • 78
    • 65549142692 scopus 로고    scopus 로고
    • Identifying and characterizing a functional HIV-1 reverse transcriptase-binding site on integrase
    • Wilkinson, T. A., et al. 2009. Identifying and characterizing a functional HIV-1 reverse transcriptase-binding site on integrase. J. Biol. Chem. 284: 7931-7939.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7931-7939
    • Wilkinson, T.A.1
  • 79
    • 0028924020 scopus 로고
    • Human immunodeficiency virus type 1 integrase: Effects of mutations on viral ability to integrate, direct viral gene expression from unintegrated viral DNA templates, and sustain viral propagation in primary cells
    • Wiskerchen, M., and M. A. Muesing. 1995. Human immunodeficiency virus type 1 integrase: effects of mutations on viral ability to integrate, direct viral gene expression from unintegrated viral DNA templates, and sustain viral propagation in primary cells. J. Virol. 69:376-386.
    • (1995) J. Virol. , vol.69 , pp. 376-386
    • Wiskerchen, M.1    Muesing, M.A.2
  • 80
    • 0033019033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 integrase protein promotes reverse transcription through specific interactions with the nucleo-protein reverse transcription complex
    • Wu, X., et al. 1999. Human immunodeficiency virus type 1 integrase protein promotes reverse transcription through specific interactions with the nucleo-protein reverse transcription complex. J. Virol. 73:2126-2135.
    • (1999) J. Virol. , vol.73 , pp. 2126-2135
    • Wu, X.1
  • 81
    • 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., et al. 2008. 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. 283:5632-5641.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5632-5641
    • Zhao, Z.1
  • 82
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng, R., T. M. Jenkins, and R. Craigie. 1996. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc. Natl. Acad. Sci. U. S. A. 93:13659-13664.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3
  • 83
    • 2342541832 scopus 로고    scopus 로고
    • Requirement for integrase during reverse transcription of human immunodeficiency virus type 1 and the effect of cysteine mutations of integrase on its interactions with reverse transcrip-tase
    • Zhu, K., C. Dobard, and S. A. Chow. 2004. Requirement for integrase during reverse transcription of human immunodeficiency virus type 1 and the effect of cysteine mutations of integrase on its interactions with reverse transcrip-tase. J. Virol. 78:5045-5055.
    • (2004) J. Virol. , vol.78 , pp. 5045-5055
    • Zhu, K.1    Dobard, C.2    Chow, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.