메뉴 건너뛰기




Volumn 11, Issue 3, 1997, Pages 371-382

Disruption of the terminal base pairs of retroviral DNA during integration

Author keywords

DNA distortion; end processing; Recombination; retroviral integration

Indexed keywords

INTEGRASE; POLYNUCLEOTIDE; VIRUS DNA;

EID: 0031050297     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.11.3.371     Document Type: Article
Times cited : (76)

References (72)
  • 1
    • 0028317055 scopus 로고
    • Identification of residues in the Mu transposase essential for catalysis
    • Baker, T.A. and L. Luo. 1994. Identification of residues in the Mu transposase essential for catalysis. Proc. Natl. Acad. Sci. 91: 6654-6658.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 6654-6658
    • Baker, T.A.1    Luo, L.2
  • 3
    • 0023647997 scopus 로고
    • Correct integration of retroviral DNA in vitro
    • Brown, P.O., B. Bowerman, H.E. Varmus, and J.M. Bishop. 1987. Correct integration of retroviral DNA in vitro. Cell 49: 347-356.
    • (1987) Cell , vol.49 , pp. 347-356
    • Brown, P.O.1    Bowerman, B.2    Varmus, H.E.3    Bishop, J.M.4
  • 4
    • 0040896601 scopus 로고
    • Retroviral integration: Structure of the initial covalent product and its precursor, and a role for the viral in protein
    • Brown, P.O., B. Bowerman, H.E. Varmus, and J.M. Bishop. 1989. Retroviral integration: Structure of the initial covalent product and its precursor, and a role for the viral IN protein. Proc. Natl Acad. Sci. 86: 2525-2529.
    • (1989) Proc. Natl Acad. Sci. , vol.86 , pp. 2525-2529
    • Brown, P.O.1    Bowerman, B.2    Varmus, H.E.3    Bishop, J.M.4
  • 5
    • 0028865574 scopus 로고
    • Catalytic domain of the avian sarcoma virus integrase: High resolution structure defines ordered active site and a hound metal cofactor
    • Bujacz, G., M. Jaskolski, J. Alexandratos, A. Wlodawer, G Merkel, R.A. Katz, and A.M. Skalka. 1995. Catalytic domain of the avian sarcoma virus integrase: High resolution structure defines ordered active site and a hound metal cofactor. J. Mol. Biol. 253: 333-346.
    • (1995) J. Mol. Biol. , vol.253 , pp. 333-346
    • Bujacz, G.1    Jaskolski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5    Katz, R.A.6    Skalka, A.M.7
  • 6
    • 0026034790 scopus 로고
    • Activities of human immunodeficiency virus (HIV) integration protein in vitro: Specific cleavage and integration of HIV DNA
    • Bushman, F.D. and R. Craigie. 1991. Activities of human immunodeficiency virus (HIV) integration protein in vitro: Specific cleavage and integration of HIV DNA. Proc. Natl. Acad. Sci. 88: 1339-1343.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 1339-1343
    • Bushman, F.D.1    Craigie, R.2
  • 7
    • 0027456715 scopus 로고
    • Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding
    • Bushman, F.D., A. Engelman, and R. Craigie. 1993. Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding. Proc. Natl. Acad. Sci. 90: 3428-3432.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Craigie, R.3
  • 8
    • 0028225959 scopus 로고
    • Human immunodeficiency virus type 1 integrase: Effect on viral replication of mutations at highly conserved residues
    • Cannon, P.M., W. Wilson, E. Byles, S.M. Kingsman, and A.J. Kingsman. 1994. Human immunodeficiency virus type 1 integrase: Effect on viral replication of mutations at highly conserved residues. J. Virol. 68: 4768-4775.
    • (1994) J. Virol. , vol.68 , pp. 4768-4775
    • Cannon, P.M.1    Wilson, W.2    Byles, E.3    Kingsman, S.M.4    Kingsman, A.J.5
  • 9
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus
    • Chow, S.A., K. Vincent, V. Ellison, and P.O. Brown. 1992. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science 255: 723-726.
    • (1992) Science , vol.255 , pp. 723-726
    • Chow, S.A.1    Vincent, K.2    Ellison, V.3    Brown, P.O.4
  • 10
    • 0022318818 scopus 로고
    • Mutants and pseudorevertants of Moloney murine leukemia virus with alterations at the integration site
    • Colicelli, J. and S.P. Goff. 1985. Mutants and pseudorevertants of Moloney murine leukemia virus with alterations at the integration site. Cell 42: 573-580.
    • (1985) Cell , vol.42 , pp. 573-580
    • Colicelli, J.1    Goff, S.P.2
  • 11
    • 0024278041 scopus 로고
    • Sequence and spacing requirements of a retrovirus integration site
    • _. 1988. Sequence and spacing requirements of a retrovirus integration site. J. Mol Biol. 199: 47-59.
    • (1988) J. Mol Biol. , vol.199 , pp. 47-59
  • 12
    • 0025031786 scopus 로고
    • The in protein of Moloney murine leukemia virus processes the viral DNA ends and accomplishes their integration in vitro
    • Craigie, R., T. Fujiwara, and F. Bushman. 1990. The IN protein of Moloney murine leukemia virus processes the viral DNA ends and accomplishes their integration in vitro. Cell 62: 829-837.
    • (1990) Cell , vol.62 , pp. 829-837
    • Craigie, R.1    Fujiwara, T.2    Bushman, F.3
  • 13
    • 0342452981 scopus 로고
    • A mutant murine leukemia virus with a single missense codon in pol is defective in a function affecting integration
    • Donehower, L.A. and H.E. Varmus. 1984. A mutant murine leukemia virus with a single missense codon in pol is defective in a function affecting integration. Proc. Natl. Acad. Sci. 81: 6461-6465.
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , pp. 6461-6465
    • Donehower, L.A.1    Varmus, H.E.2
  • 14
    • 0028908767 scopus 로고
    • Characterization of recombinant murine leukemia virus integrase
    • Dotan, I., B.P. Scottoline, T.S. Heuer and P.O. Brown. 1995. Characterization of recombinant murine leukemia virus integrase. J. Virol. 69: 456-468.
    • (1995) J. Virol. , vol.69 , pp. 456-468
    • Dotan, I.1    Scottoline, B.P.2    Heuer, T.S.3    Brown, P.O.4
  • 15
    • 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
  • 16
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to polynucleotidyl transferases
    • Dyda, F., A.B. Hickman, T.M. Jenkins, A. Engelman, R. Craigie, and D.R. Davies. 1994. Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to polynucleotidyl transferases. Science 266: 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
  • 17
    • 0028239062 scopus 로고
    • A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro
    • Ellison, V. and P.O. Brown. 1994. A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro. Proc. Natl. Acad. Sci. 91: 7316-7320.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 7316-7320
    • Ellison, V.1    Brown, P.O.2
  • 18
    • 0028888455 scopus 로고
    • An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active dimer
    • Ellison, V., J. Gerton, K.A. Vincent, and P.O. Brown. 1995. An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active dimer. J. Biol. Chem. 270: 3320-3326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3320-3326
    • Ellison, V.1    Gerton, J.2    Vincent, K.A.3    Brown, P.O.4
  • 19
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficency virus type 1 integrase function in vitro
    • Engelman, A. and R. Craigie. 1992. Identification of conserved amino acid residues critical for human immunodeficency 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
  • 20
    • 0026330796 scopus 로고
    • HIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer
    • Engelman, A., K. Mizuuchi, and R. Craigie. 1991. HIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer. Cell 67:1211-1221.
    • (1991) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigie, R.3
  • 21
    • 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
  • 22
    • 0028915128 scopus 로고
    • Multiple effects of mutations in human immunodeficiency virus 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 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
  • 23
    • 0025053617 scopus 로고
    • Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences?
    • Fayet, O., P. Ramond, P. Polard, M.F. Prere, and M. Chandler. 1990. Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences? Mol Microbiol. 4: 1771-1777.
    • (1990) Mol Microbiol. , vol.4 , pp. 1771-1777
    • Fayet, O.1    Ramond, P.2    Polard, P.3    Prere, M.F.4    Chandler, M.5
  • 24
    • 0025184912 scopus 로고
    • Removal of 3′-OH-terminal nucleotides from blunt ended long terminal repeat termini by the avian retrovirus integration protein
    • Fitzgerald, M.L., A.C. Vora, and D.P. Grandgenett. 1990. Removal of 3′-OH-terminal nucleotides from blunt ended long terminal repeat termini by the avian retrovirus integration protein. J. Virol. 64: 5656-5659.
    • (1990) J. Virol. , vol.64 , pp. 5656-5659
    • Fitzgerald, M.L.1    Vora, A.C.2    Grandgenett, D.P.3
  • 25
    • 0023687763 scopus 로고
    • Retroviral DNA integration: Structure of an integration intermediate
    • Fujiwara, T. and K. Mizuuchi. 1988. Retroviral DNA integration: Structure of an integration intermediate. Cell 54: 497-504.
    • (1988) Cell , vol.54 , pp. 497-504
    • Fujiwara, T.1    Mizuuchi, K.2
  • 26
    • 0027102597 scopus 로고
    • Genetics of retroviral integration
    • Goff, S.P. 1992. Genetics of retroviral integration. Annu. Rev. Genet. 26: 527-544.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 527-544
    • Goff, S.P.1
  • 27
    • 0022262309 scopus 로고
    • Mutants of the Rous sarcoma virus reverse transcriptase gene arc defective in early replication events
    • Hippenmeyer, P.J. and D.P. Grandgenett. 1985. Mutants of the Rous sarcoma virus reverse transcriptase gene arc defective in early replication events. J. Biol. Chem 260: 8250-8256.
    • (1985) J. Biol. Chem , vol.260 , pp. 8250-8256
    • Hippenmeyer, P.J.1    Grandgenett, D.P.2
  • 29
    • 0025011051 scopus 로고
    • The avian retroviral in protein is both necessary and sufficient for integrative recombination in vitro
    • Katz, R.A., G. Merkel, J. Kulkosky, J. Leis, and A.M. Skalka. 1990. The avian retroviral IN protein is both necessary and sufficient for integrative recombination in vitro. Cell 63 87-95.
    • (1990) Cell , vol.63 , pp. 87-95
    • Katz, R.A.1    Merkel, G.2    Kulkosky, J.3    Leis, J.4    Skalka, A.M.5
  • 30
    • 0028237180 scopus 로고
    • In vitro activities of purified visna virus integrase
    • Katzman, M. and M. Sudol. 1994. In vitro activities of purified visna virus integrase. J. Virol. 68: 3558-3569.
    • (1994) J. Virol. , vol.68 , pp. 3558-3569
    • Katzman, M.1    Sudol, M.2
  • 31
    • 0026035178 scopus 로고
    • Retroviral integrase domains: DNA binding and the recognition of LTR sequences
    • Khan, E., J.P.G. Mack, R.A. Katz, J. Kulkosky, and A.M. Skalka. 1991. Retroviral integrase domains: DNA binding and the recognition of LTR sequences. Nucleic Acids Res. 19: 851-860.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 851-860
    • Khan, E.1    Mack, J.P.G.2    Katz, R.A.3    Kulkosky, J.4    Skalka, A.M.5
  • 32
    • 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.G. Mack, and A.M. Skala. 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.G.4    Skala, A.M.5
  • 33
    • 0026072804 scopus 로고
    • Substrate specificity of recombinant human immunodeficiency virus integrase
    • LaFemina, R.L., P.L. Callahan, and M.G. Cordingley. 1991. Substrate specificity of recombinant human immunodeficiency virus integrase. J. Virol. 65: 5624-5630.
    • (1991) J. Virol. , vol.65 , pp. 5624-5630
    • LaFemina, R.L.1    Callahan, P.L.2    Cordingley, M.G.3
  • 34
    • 0026459411 scopus 로고
    • Requirement of active human immunodeficiency virus type 1 integrase enzyme for productive infection of human T-lymphoid cells
    • LaFemina, R.L., C.L. Schneider, H.L. Robbins, P.L. Callahan, K. LeGrow, E. Roth, W.A. Schleif, and E.L. Emini. 1992. Requirement of active human immunodeficiency virus type 1 integrase enzyme for productive infection of human T-lymphoid cells. J. Virol. 66: 7414-7419.
    • (1992) J. Virol. , vol.66 , pp. 7414-7419
    • LaFemina, R.L.1    Schneider, C.L.2    Robbins, H.L.3    Callahan, P.L.4    Legrow, K.5    Roth, E.6    Schleif, W.A.7    Emini, E.L.8
  • 35
    • 0025850374 scopus 로고
    • Structural aspects of a higher order nucleoprotein complex: Induction of an altered DNA structure at the Mu-host junction in the Mu type 1 transpososome
    • Lavoie, B.D., B.S. Chan, R.G. Allison, and G. Chaconas. 1991. Structural aspects of a higher order nucleoprotein complex: Induction of an altered DNA structure at the Mu-host junction in the Mu type 1 transpososome. EMBO J. 10:3051-3059.
    • (1991) EMBO J. , vol.10 , pp. 3051-3059
    • Lavoie, B.D.1    Chan, B.S.2    Allison, R.G.3    Chaconas, G.4
  • 36
    • 0026537415 scopus 로고
    • Both substrate and target oligonucleotide sequences affect in vitro integration mediated by human immunodeficiency virus type 1 integrase protein produced in Saccharomyces cerevisiae
    • Leavitt, A.D., R.B. Rose, and H.E. Varmus. 1992. Both substrate and target oligonucleotide sequences affect in vitro integration mediated by human immunodeficiency virus type 1 integrase protein produced in Saccharomyces cerevisiae. J. Virol. 66: 2359-2368.
    • (1992) J. Virol. , vol.66 , pp. 2359-2368
    • Leavitt, A.D.1    Rose, R.B.2    Varmus, H.E.3
  • 37
    • 0027470432 scopus 로고
    • Site-directed mutagenesis of HIV-1 integrase demonstrate differential effects on integrase in vitro
    • Leavitt, A.D., L. Shiue, and H.E. Varmus. 1993. Site-directed mutagenesis of HIV-1 integrase demonstrate differential effects on integrase in vitro. J. Biol. Chem. 268: 2113-2119.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2113-2119
    • Leavitt, A.D.1    Shiue, L.2    Varmus, H.E.3
  • 38
    • 0024292414 scopus 로고
    • Characterization of base-pair opening in deoxynucleotide duplexes using catalyzed exchange of the imino proton
    • Leroy, J.L., M. Kochoyan, T. Huynh-Dinh, and M. Geuron. 1988. Characterization of base-pair opening in deoxynucleotide duplexes using catalyzed exchange of the imino proton. J. Mol. Biol. 16: 223-237.
    • (1988) J. Mol. Biol. , vol.16 , pp. 223-237
    • Leroy, J.L.1    Kochoyan, M.2    Huynh-Dinh, T.3    Geuron, M.4
  • 39
    • 0026799383 scopus 로고
    • Polynucleotidyl transfer reactions in transpositional DNA recombination
    • Mizuuchi, K. 1992. Polynucleotidyl transfer reactions in transpositional DNA recombination. J. Biol. Chem. 267: 21273-21276.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21273-21276
    • Mizuuchi, K.1
  • 40
    • 0026737976 scopus 로고
    • Kinetics and energetics of base-Pair opening in 5′-d(CGCGAATTCGCG)-3′ and a substituted dodecamer containing G-T mismatches
    • Moe, J.G. and I.M. Russu. 1992. Kinetics and energetics of base-Pair opening in 5′-d(CGCGAATTCGCG)-3′ and a substituted dodecamer containing G-T mismatches. Biochemistry 31: 8421-8428.
    • (1992) Biochemistry , vol.31 , pp. 8421-8428
    • Moe, J.G.1    Russu, I.M.2
  • 41
    • 0028067639 scopus 로고
    • DNA bending creates favored sites for retroviral integration: An explanation for preferred insertion sites in nucleosomes
    • Muller, H.-P. and H.E. Varmus. 1994. DNA bending creates favored sites for retroviral integration: An explanation for preferred insertion sites in nucleosomes. EMBO J. 13: 4707-4714.
    • (1994) EMBO J. , vol.13 , pp. 4707-4714
    • Muller, H.-P.1    Varmus, H.E.2
  • 42
    • 0027327513 scopus 로고
    • Endonucleolytic cleavage and DNA-joining activities of the integration protein of human foamy virus
    • Pahl, A. and RM. Flugel. 1993. Endonucleolytic cleavage and DNA-joining activities of the integration protein of human foamy virus. J. Virol. 67: 5426-5434.
    • (1993) J. Virol. , vol.67 , pp. 5426-5434
    • Pahl, A.1    Flugel, R.M.2
  • 43
    • 0021022185 scopus 로고
    • The terminal nucleotides of retrovirus DNA are required for integration but not virus production
    • Panganiban, A.T. and H.M. Temin. 1983. The terminal nucleotides of retrovirus DNA are required for integration but not virus production. Nature 306: 155-160.
    • (1983) Nature , vol.306 , pp. 155-160
    • Panganiban, A.T.1    Temin, H.M.2
  • 44
    • 0342466800 scopus 로고
    • The retrovirus pol gene encodes a product required for DNA integration: Identification of a retrovirus int locus
    • _. 1984. The retrovirus pol gene encodes a product required for DNA integration: Identification of a retrovirus int locus. Proc. Natl Acad Sci. 81: 7885-7889.
    • (1984) Proc. Natl Acad Sci. , vol.81 , pp. 7885-7889
  • 45
    • 0028928168 scopus 로고
    • Bacterial transposases and retroviral integrases
    • Polard, P. and M. Chandler. 1995. Bacterial transposases and retroviral integrases. Mol. Microbiol. 15: 13-23.
    • (1995) Mol. Microbiol. , vol.15 , pp. 13-23
    • Polard, P.1    Chandler, M.2
  • 46
    • 0028264042 scopus 로고
    • Human immunodeficiency virus integrase directs integration to sites of severe DNA distortion within the nucleosome core
    • Pruss, D., F.D. Bushman, and A.P. Wolffe. 1994a. Human immunodeficiency virus integrase directs integration to sites of severe DNA distortion within the nucleosome core. Proc. Natl Acad. Sci. 91: 5913-5917.
    • (1994) Proc. Natl Acad. Sci. , vol.91 , pp. 5913-5917
    • Pruss, D.1    Bushman, F.D.2    Wolffe, A.P.3
  • 47
    • 0028125005 scopus 로고
    • The influence of DNA and nucleosome structure on integration events directed by HIV integrase
    • Pruss, D., R. Reeves, F.D. Bushman, and A.P. Wolffe. 1994b. The influence of DNA and nucleosome structure on integration events directed by HIV integrase. J. Biol. Chem. 269: 25031-25041.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25031-25041
    • Pruss, D.1    Reeves, R.2    Bushman, F.D.3    Wolffe, A.P.4
  • 48
    • 0026696624 scopus 로고
    • Nucleosomes, DNA-binding proteins, and DNA sequence modulate retroviral integration target site selection
    • Pryciak, P.M. and H.E. Varmus. 1992. Nucleosomes, DNA-binding proteins, and DNA sequence modulate retroviral integration target site selection. Cell 69: 769-780.
    • (1992) Cell , vol.69 , pp. 769-780
    • Pryciak, P.M.1    Varmus, H.E.2
  • 49
    • 0029891597 scopus 로고    scopus 로고
    • Distinct DNA sequence and structure requirements for the two sites of V(D)J recombination signal cleavage
    • Ramsden, D.A., J.F. McBlane, D.C. van Gent, and M. Gellert. 1996. Distinct DNA sequence and structure requirements for the two sites of V(D)J recombination signal cleavage. EMBO J. 15: 3197-3206.
    • (1996) EMBO J. , vol.15 , pp. 3197-3206
    • Ramsden, D.A.1    McBlane, J.F.2    Van Gent, D.C.3    Gellert, M.4
  • 50
    • 0029129435 scopus 로고
    • Structure of the bacteriophage Mu transposase core: A common structural motif for DNA transposition and retroviral integration
    • Rice, P.A. and K. Mizuuchi. 1995. Structure of the bacteriophage Mu transposase core: A common structural motif for DNA transposition and retroviral integration. Cell 82: 209-220.
    • (1995) Cell , vol.82 , pp. 209-220
    • Rice, P.A.1    Mizuuchi, K.2
  • 51
    • 0024340289 scopus 로고
    • Structure of the termini of DNA intermediates in the integration of retroviral DNA: Dependence on in function and terminal DNA sequence
    • Roth, M.J., P.L. Schwartzberg, and S.P. Goff. 1989. Structure of the termini of DNA intermediates in the integration of retroviral DNA: Dependence on IN function and terminal DNA sequence. Cell 58: 47-54
    • (1989) Cell , vol.58 , pp. 47-54
    • Roth, M.J.1    Schwartzberg, P.L.2    Goff, S.P.3
  • 52
    • 0025309894 scopus 로고
    • Tn552, a novel transposable element from Staphylococcus aureus
    • Rowland, S.J. and K.G.H. Dyke. 1990. Tn552, a novel transposable element from Staphylococcus aureus. Mol Microbiol. 4: 961-975.
    • (1990) Mol Microbiol. , vol.4 , pp. 961-975
    • Rowland, S.J.1    Dyke, K.G.H.2
  • 54
    • 0029096898 scopus 로고
    • The phage Mu transpososome core: DNA requirements for assembly and funcion
    • Savilahti, H., P.A. Rice, and K. Mizuuchi. 1995. The phage Mu transpososome core: DNA requirements for assembly and funcion. EMBO J. 14: 4893-4903.
    • (1995) EMBO J. , vol.14 , pp. 4893-4903
    • Savilahti, H.1    Rice, P.A.2    Mizuuchi, K.3
  • 55
    • 0021729809 scopus 로고
    • Construction and analysis of deletion mutations in the pol gene of Moloney murine leukemia virus: A new viral function required for productive infection
    • Schwartzberg, P.J., J. Colicelli, and S.P. Goff. 1984. Construction and analysis of deletion mutations in the pol gene of Moloney murine leukemia virus: A new viral function required for productive infection. Cell 37: 1043-1052.
    • (1984) Cell , vol.37 , pp. 1043-1052
    • Schwartzberg, P.J.1    Colicelli, J.2    Goff, S.P.3
  • 56
    • 0343250277 scopus 로고
    • Molecular model for the transposition of bacteriophage Mu and other transposable elements
    • Shapiro, J. 1979. Molecular model for the transposition of bacteriophage Mu and other transposable elements. Proc. Natl. Acad. Sci. 76: 1933-1937.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 1933-1937
    • Shapiro, J.1
  • 57
    • 0025366844 scopus 로고
    • Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity
    • Sherman, P.A. and J.A. Fyfe. 1990. Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity. J. Virol. 87: 5119-5123.
    • (1990) J. Virol. , vol.87 , pp. 5119-5123
    • Sherman, P.A.1    Fyfe, J.A.2
  • 58
    • 0026693410 scopus 로고
    • Human immunodeficiency virus type 1 integration protein: DNA cleaving activity
    • Sherman, P.A., M.L. Dickenson, and J.A. Fyfe. 1992. Human immunodeficiency virus type 1 integration protein: DNA cleaving activity. J. Virol. 66: 3593-3601.
    • (1992) J. Virol. , vol.66 , pp. 3593-3601
    • Sherman, P.A.1    Dickenson, M.L.2    Fyfe, J.A.3
  • 59
    • 0027997840 scopus 로고
    • Integrase mutants of human immmunodeficiency virus type 1 wth a specific defect in integration
    • Taddeo, B., W.A. Haseltine, and C.M. Farnet. 1994. Integrase mutants of human immmunodeficiency virus type 1 wth a specific defect in integration. J. Virol. 68: 8401-8405.
    • (1994) J. Virol. , vol.68 , pp. 8401-8405
    • Taddeo, B.1    Haseltine, W.A.2    Farnet, C.M.3
  • 60
    • 0028089732 scopus 로고
    • DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein
    • van den Ent, F.M., C. Vink, and R.H. Plasterk. 1994. DNA substrate requirements for different activities of the human immunodeficiency virus type 1 integrase protein. J. Virol. 68: 7825-7832.
    • (1994) J. Virol. , vol.68 , pp. 7825-7832
    • Van Den Ent, F.M.1    Vink, C.2    Plasterk, R.H.3
  • 61
    • 0025775488 scopus 로고
    • DNA binding properties of the integrase of human immunodeficiency viruses types 1 and 2
    • van Gent, D.C., Y. Elgersma, M.W.J. Bolk, C. Vink, and R.H.A. Plasterk. 1991. DNA binding properties of the integrase of human immunodeficiency viruses types 1 and 2. Nucleic Acids Res. 19: 3821-3827.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3821-3827
    • Van Gent, D.C.1    Elgersma, Y.2    Bolk, M.W.J.3    Vink, C.4    Plasterk, R.H.A.5
  • 62
    • 0026668776 scopus 로고
    • Mutational analyis of the integrase protein of human immunodeficiency virus type 2
    • van Gent, D.C., A.A.M. Oude Groeneger, and R.H.A. Plasterk 1992. Mutational analyis of the integrase protein of human immunodeficiency virus type 2. Proc. Natl. Acad. Sci. 89: 9598-9602.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 9598-9602
    • Van Gent, D.C.1    Oude Groeneger, A.A.M.2    Plasterk, R.H.A.3
  • 63
    • 0027246609 scopus 로고
    • Complementation between HIV integrase proteins mutated in different domains
    • van Gent, D.C., C. Vink, A.A.M. Oude Groeneger, and R.H.A. Plasterk. 1993. Complementation between HIV integrase proteins mutated in different domains. EMBO J. 12: 3261-3268.
    • (1993) EMBO J. , vol.12 , pp. 3261-3268
    • Van Gent, D.C.1    Vink, C.2    Oude Groeneger, A.A.M.3    Plasterk, R.H.A.4
  • 64
    • 0029967722 scopus 로고    scopus 로고
    • Initiation of V(D)J recombination: Similarities to transposition and retroviral integration
    • van Gent, D.C., K. Mizuuchi, and M. Gellert. 1996. Initiation of V(D)J recombination: similarities to transposition and retroviral integration. Science 271: 1592-1594.
    • (1996) Science , vol.271 , pp. 1592-1594
    • Van Gent, D.C.1    Mizuuchi, K.2    Gellert, M.3
  • 65
    • 0027472085 scopus 로고
    • Characterization of human immunodeficiency virus type 1 integrase expressed in Escherichia coli and analysis of variants with amino-terminal mutations
    • Vincent, K.A., V. Ellison, S.A. Chow, and P.O. Brown. 1993. Characterization of human immunodeficiency virus type 1 integrase expressed in Escherichia coli and analysis of variants with amino-terminal mutations. J. Virol. 67: 425-437.
    • (1993) J. Virol. , vol.67 , pp. 425-437
    • Vincent, K.A.1    Ellison, V.2    Chow, S.A.3    Brown, P.O.4
  • 66
    • 0027508068 scopus 로고
    • The human immunodeficiency virus integrase protein
    • Vink, C. and R.H.A. Plasterk. 1993. The human immunodeficiency virus integrase protein. Trends Genet. 9: 433-437.
    • (1993) Trends Genet. , vol.9 , pp. 433-437
    • Vink, C.1    Plasterk, R.H.A.2
  • 67
    • 0026095906 scopus 로고
    • Human immunodeficiency virus integrase protein requires a subterminal position of its viral DNA recognition sequence for efficient cleavage
    • Vink, C., D.C. van Gent, Y. Elgersma, and R.H.A. Plasterk. 1991a. Human immunodeficiency virus integrase protein requires a subterminal position of its viral DNA recognition sequence for efficient cleavage. J. Virol. 65: 4636-4644.
    • (1991) J. Virol. , vol.65 , pp. 4636-4644
    • Vink, C.1    Van Gent, D.C.2    Elgersma, Y.3    Plasterk, R.H.A.4
  • 68
    • 0026348879 scopus 로고
    • Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein
    • Vink, C., E. Yeheskiely, G.A. van der Marcl, J.H. van Bloom, and R.H.A. Plasterk. 1991b. Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein. Nucleic Acids Res. 19: 6691-6698.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6691-6698
    • Vink, C.1    Yeheskiely, E.2    Van Der Marcl, G.A.3    Van Bloom, J.H.4    Plasterk, R.H.A.5
  • 69
    • 0027210608 scopus 로고
    • Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type 1 integrase protein
    • Vink, C., A.A.M. Oude-Groeneger, and R.H.A. Plasterk. 1993. Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type 1 integrase protein. Nucleic Acids Res. 21: 1419-1425.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude-Groeneger, A.A.M.2    Plasterk, R.H.A.3
  • 70
    • 0027979130 scopus 로고
    • Activities of the feline imunodeficiency virus integrase protein produced in Escherichia coli
    • Vink, C., K.H. van der Linden, and R.H.A. Plasterk. 1994. Activities of the feline imunodeficiency virus integrase protein produced in Escherichia coli. J. Virol. 68: 1468-1474.
    • (1994) J. Virol. , vol.68 , pp. 1468-1474
    • Vink, C.1    Van Der Linden, K.H.2    Plasterk, R.H.A.3
  • 71
    • 0026622006 scopus 로고
    • Retroviral reverse transcription and integration: Progress and problems
    • Whitcomb, J.M. and S.H. Hughes. 1992. Retroviral reverse transcription and integration: Progress and problems. Annu. Rev. Cell Biol. 8: 275-306.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 275-306
    • Whitcomb, J.M.1    Hughes, S.H.2
  • 72
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.