메뉴 건너뛰기




Volumn 72, Issue 2, 1998, Pages 1324-1333

The application of a homologous recombination assay revealed amino acid residues in an LTR-retrotransposon that were critical for integration

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRASE; MUTANT PROTEIN; RNA DIRECTED DNA POLYMERASE;

EID: 0031882748     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.2.1324-1333.1998     Document Type: Article
Times cited : (27)

References (55)
  • 1
    • 0029655262 scopus 로고    scopus 로고
    • The retrotransposon Tf1 assembles virus-like particles with excess Gag relative to integrase because of a regulated degradation process
    • Atwood, A., J. Lin, and H. Levin. 1996. The retrotransposon Tf1 assembles virus-like particles with excess Gag relative to integrase because of a regulated degradation process. Mol. Cell. Biol. 16:338-346.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 338-346
    • Atwood, A.1    Lin, J.2    Levin, H.3
  • 2
    • 2642596399 scopus 로고    scopus 로고
    • Unpublished data
    • Atwood, A. Unpublished data.
    • Atwood, A.1
  • 3
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154:164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 4
    • 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
  • 5
    • 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. USA 86:2525-2529.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2525-2529
    • Brown, P.O.1    Bowerman, B.2    Varmus, H.E.3    Bishop, J.M.4
  • 6
    • 0027199982 scopus 로고
    • Association of integrase, matrix, and reverse transcriptase antigens of human immunodeficiency virus type 1 with viral nucleic acids following acute infection
    • Bukrinsky, M. I., N. Sharova, T. L. McDonald, T. Pushkarskaya, W. G. Tarpley, and M. Stevenson. 1993. Association of integrase, matrix, and reverse transcriptase antigens of human immunodeficiency virus type 1 with viral nucleic acids following acute infection. Proc. Natl. Acad. Sci. USA 90:6125-6129.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6125-6129
    • Bukrinsky, M.I.1    Sharova, N.2    McDonald, T.L.3    Pushkarskaya, T.4    Tarpley, W.G.5    Stevenson, M.6
  • 7
    • 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. USA 88:1339-1343.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1339-1343
    • Bushman, F.D.1    Craigie, R.2
  • 8
    • 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, I. Palmer, P. Wingfield, 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. USA 90:3428-3432.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Palmer, I.3    Wingfield, P.4    Craigie, R.5
  • 9
    • 0000553844 scopus 로고
    • Roles of ribonuclease H in reverse transcription
    • A. Skulka and S. Goff (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Champoux, J. 1993. Roles of ribonuclease H in reverse transcription, p. 103-117. In A. Skulka and S. Goff (ed.), Reverse transcriptase. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1993) Reverse Transcriptase , pp. 103-117
    • Champoux, J.1
  • 10
    • 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
  • 11
    • 0026082573 scopus 로고
    • Single-step selection for Ty1 element retrotransposition
    • Curcio, M. J., and D. J. Garfinkel. 1991. Single-step selection for Ty1 element retrotransposition. Proc. Natl. Acad. Sci. USA 88:936-940
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 936-940
    • Curcio, M.J.1    Garfinkel, D.J.2
  • 13
    • 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
  • 14
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other 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 other 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
  • 15
    • 0025218956 scopus 로고
    • A specific terminal structure is required for Ty1 transposition
    • Eichinger, D. J., and J. D. Boeke. 1990. A specific terminal structure is required for Ty1 transposition. Genes Dev. 4:324-330.
    • (1990) Genes Dev. , vol.4 , pp. 324-330
    • Eichinger, D.J.1    Boeke, J.D.2
  • 16
    • 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
  • 17
    • 0031004162 scopus 로고    scopus 로고
    • HIV-1 cDNA integration: Requirement of HMG I(Y) protein for function of preintegration complexes in vitro
    • Farnet, C. M., and F. D. Bushman. 1997. HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro. Cell 88:483-492.
    • (1997) Cell , vol.88 , pp. 483-492
    • Farnet, C.M.1    Bushman, F.D.2
  • 18
    • 0025053617 scopus 로고
    • Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences?
    • Fayet, O., P. Raymond, P. Polard, M. F. Prère, 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    Raymond, P.2    Polard, P.3    Prère, M.F.4    Chandler, M.5
  • 19
    • 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
  • 20
    • 0024562759 scopus 로고
    • Introduction of functional artificial introns into the naturally intronless ura4 gene of Schizosaccharomyces pombe
    • Gatermann, K. B., A. Hoffmann, G. H. Rosenberg, and N. F. Kaufer. 1989. Introduction of functional artificial introns into the naturally intronless ura4 gene of Schizosaccharomyces pombe. Mol. Cell. Biol. 9:1526-1535.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1526-1535
    • Gatermann, K.B.1    Hoffmann, A.2    Rosenberg, G.H.3    Kaufer, N.F.4
  • 21
    • 0022484140 scopus 로고
    • Murine leukemia virus pol gene products: Analysis with antisera generated against reverse transcriptase and endonuclease fusion proteins expressed in Escherichia coli
    • Hu, S. C., D. L. Court, M. Zweig, and J. G. Levin. 1986. Murine leukemia virus pol gene products: analysis with antisera generated against reverse transcriptase and endonuclease fusion proteins expressed in Escherichia coli. J. Virol. 60:267-274.
    • (1986) J. Virol. , vol.60 , pp. 267-274
    • Hu, S.C.1    Court, D.L.2    Zweig, M.3    Levin, J.G.4
  • 22
    • 2642604727 scopus 로고
    • Computer analysis of retroviral pol genes: Assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes
    • Johnson, M. S., M. A. McClure, D. F. Feng, J. Gray, and R. F. Doolittle. 1986. Computer analysis of retroviral pol genes: assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes. Proc. Natl. Acad. Sci. USA 83:7648-7652.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7648-7652
    • Johnson, M.S.1    McClure, M.A.2    Feng, D.F.3    Gray, J.4    Doolittle, R.F.5
  • 23
    • 0021368076 scopus 로고
    • Method for determining whether a gene of Escherichia coli is essential: Application to the pola gene
    • Joyce, C. M., and N. Grindley. 1984. Method for determining whether a gene of Escherichia coli is essential: application to the polA gene. J. Bacteriol. 158:636-643.
    • (1984) J. Bacteriol. , vol.158 , pp. 636-643
    • Joyce, C.M.1    Grindley, N.2
  • 24
    • 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
  • 26
    • 0026035178 scopus 로고
    • Retroviral integrase domains: DNA binding and the recognition of LTR sequences
    • Erratum, 25:1358
    • Khan, E., J. P. 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. (Erratum, 25:1358.)
    • (1991) Nucleic Acids Res. , vol.19 , pp. 851-860
    • Khan, E.1    Mack, J.P.2    Katz, R.A.3    Kulkosky, J.4    Skalka, A.M.5
  • 27
    • 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
  • 28
    • 0027470432 scopus 로고
    • Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions in vitro
    • Leavitt, A. D., L. Shiue, and H. E. Varmus. 1993. Site-directed mutagenesis of HIV-1 integrase demonstrates differential effects on integrase functions 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
  • 29
    • 0029033912 scopus 로고
    • A novel mechanism of self-primed reverse transcription defines a new family of retroelements
    • Levin, H. L. 1995. A novel mechanism of self-primed reverse transcription defines a new family of retroelements. Mol. Cell. Biol. 15:3310-3317.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3310-3317
    • Levin, H.L.1
  • 30
    • 0029831105 scopus 로고    scopus 로고
    • An unusual mechanism of self-primed reverse transcription requires the RNase H domain of reverse transcriptase to cleave an RNA duplex
    • Levin, H. L. 1996. An unusual mechanism of self-primed reverse transcription requires the RNase H domain of reverse transcriptase to cleave an RNA duplex. Mol. Cell. Biol. 16:5645-5654.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5645-5654
    • Levin, H.L.1
  • 31
    • 0026525450 scopus 로고
    • Demonstration of retrotransposition of the Tf1 element in fission yeast
    • Levin, H. L., and J. D. Boeke. 1992. Demonstration of retrotransposition of the Tf1 element in fission yeast. EMBO J. 11:1145-1153.
    • (1992) EMBO J. , vol.11 , pp. 1145-1153
    • Levin, H.L.1    Boeke, J.D.2
  • 32
    • 0027369451 scopus 로고
    • Novel gene expression mechanism in a fission yeast retroelement: Tf1 proteins are derived from a single primary translation product
    • Erratum, 13: 1494, 1994
    • Levin, H. L., D. C. Weaver, and J. D. Boeke. 1993. Novel gene expression mechanism in a fission yeast retroelement: Tf1 proteins are derived from a single primary translation product. EMBO J. 12:4885-1895. (Erratum, 13: 1494, 1994.)
    • (1993) EMBO J. , vol.12 , pp. 4885-11895
    • Levin, H.L.1    Weaver, D.C.2    Boeke, J.D.3
  • 33
    • 0025226543 scopus 로고
    • Two related families of retrotransposons from Schizosaccharomyces pombe
    • Levin, H. L., D. C. Weaver, and J. D. Boeke. 1990. Two related families of retrotransposons from Schizosaccharomyces pombe. Mol. Cell. Biol. 10:6791-6798.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6791-6798
    • Levin, H.L.1    Weaver, D.C.2    Boeke, J.D.3
  • 34
    • 0031059711 scopus 로고    scopus 로고
    • A complex structure in the mRNA of Tf1 is recognized and cleaved to generate the primer of reverse transcription
    • Lin, J., and H. Levin. 1997. A complex structure in the mRNA of Tf1 is recognized and cleaved to generate the primer of reverse transcription. Genes Dev. 11:270-285.
    • (1997) Genes Dev. , vol.11 , pp. 270-285
    • Lin, J.1    Levin, H.2
  • 35
    • 0027450385 scopus 로고
    • Reverse transcription of R2Bm RNA is primed by a nick at the chromosomal target site: A mechanism for non-LTR retrotransposition
    • Luan, D. D., M. H. Korman, J. L. Jakubczak, and T. H. Eickbush. 1993. Reverse transcription of R2Bm RNA is primed by a nick at the chromosomal target site: a mechanism for non-LTR retrotransposition. Cell 72:595-605.
    • (1993) Cell , vol.72 , pp. 595-605
    • Luan, D.D.1    Korman, M.H.2    Jakubczak, J.L.3    Eickbush, T.H.4
  • 36
    • 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
  • 37
    • 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
  • 38
    • 0030972160 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes: Studies of organization and composition
    • Miller, M. D., C. M. Farnet, and F. D. Bushman. 1997. Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. J. Virol. 71:5382-5390.
    • (1997) J. Virol. , vol.71 , pp. 5382-5390
    • Miller, M.D.1    Farnet, C.M.2    Bushman, F.D.3
  • 39
    • 0028201743 scopus 로고
    • Expression and partial purification of enzymatically active recombinant Ty1 integrase in Saccharomyces cerevisiae
    • Moore, S. P., and D. J. Garfinkel. 1994. Expression and partial purification of enzymatically active recombinant Ty1 integrase in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 91:1843-1847.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1843-1847
    • Moore, S.P.1    Garfinkel, D.J.2
  • 40
    • 0029023845 scopus 로고
    • Substrate specificity of Ty1 integrase
    • Moore, S. P., M. Powers, and D. J. Garfinkel. 1995. Substrate specificity of Ty1 integrase. J. Virol. 69:4683-4692.
    • (1995) J. Virol. , vol.69 , pp. 4683-4692
    • Moore, S.P.1    Powers, M.2    Garfinkel, D.J.3
  • 41
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno, S., A. Klar, and P. Nurse. 1991. Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194:795-823.
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 42
    • 0026081040 scopus 로고
    • Defining nucleic acid-binding properties of avian retrovirus integrase by deletion analysis
    • Mumm, S. R., and D. P. Grandgenett. 1991. Defining nucleic acid-binding properties of avian retrovirus integrase by deletion analysis. J. Virol. 65: 1160-1167.
    • (1991) J. Virol. , vol.65 , pp. 1160-1167
    • Mumm, S.R.1    Grandgenett, D.P.2
  • 43
    • 0030964781 scopus 로고    scopus 로고
    • Substituting a conserved residue of the ribonuclease H domain alters substrate hydrolysis by retroviral reverse transcriptase
    • Rausch, J. W., and S. F. Le Grice. 1997. Substituting a conserved residue of the ribonuclease H domain alters substrate hydrolysis by retroviral reverse transcriptase. J. Biol. Chem. 272:8602-8610.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8602-8610
    • Rausch, J.W.1    Le Grice, S.F.2
  • 45
    • 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
  • 46
    • 0025309894 scopus 로고
    • Tn552, a novel transposable element from Staphylococcus aureus
    • Rowland, S. J., and K. G. 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.2
  • 47
    • 0026634793 scopus 로고
    • The N-terminal region of HIV-1 integrase is required for integration activity, but not for DNA-binding
    • Schauer, M., and A. Billich. 1992. The N-terminal region of HIV-1 integrase is required for integration activity, but not for DNA-binding. Biochem. Biophys. Res. Commun. 185:874-880.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 874-880
    • Schauer, M.1    Billich, A.2
  • 48
    • 0027939848 scopus 로고
    • Efficient homologous recombination of Ty1 element cDNA when integration is blocked
    • Sharon, G., T. J. Burkett, and D. J. Garfinkel. 1994. Efficient homologous recombination of Ty1 element cDNA when integration is blocked. Mol. Cell. Biol. 14:6540-6551.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6540-6551
    • Sharon, G.1    Burkett, T.J.2    Garfinkel, D.J.3
  • 49
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: From cloned gene to mutant yeast
    • Sikorski, R. S., and J. D. Boeke. 1990. In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol. 194:302-318.
    • (1990) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1    Boeke, J.D.2
  • 50
    • 0003543882 scopus 로고
    • Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
    • Skalka, A. M., and S. P. Goff (ed.). 1993. Reverse transcriptase. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
    • (1993) Reverse Transcriptase
    • Skalka, A.M.1    Goff, S.P.2
  • 51
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 52
    • 0025775488 scopus 로고
    • DNA binding properties of the integrase proteins of human immunodeficiency viruses types 1 and 2
    • van Gent, D. C., Y. Elgersma, M. W. Bolk, C. Vink, and R. H. Plasterk. 1991. DNA binding properties of the integrase proteins 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.3    Vink, C.4    Plasterk, R.H.5
  • 53
    • 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. USA 89:9598-9602.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9598-9602
    • Van Gent, D.C.1    Groeneger, A.A.2    Plasterk, R.H.3
  • 54
    • 0002915381 scopus 로고
    • American Society for Microbiology, Washington, D.C.
    • Varmus, H., and P. Brown (ed.). 1989. Retroviruses. American Society for Microbiology, Washington, D.C.
    • (1989) Retroviruses
    • Varmus, H.1    Brown, P.2
  • 55
    • 0029162089 scopus 로고
    • Group II intron mobility occurs by target DNA-primed reverse transcription
    • Zimmerly, S., H. Guo, P. S. Perlman, and A. M. Lambowitz. 1993. Group II intron mobility occurs by target DNA-primed reverse transcription. Cell 82:545-554.
    • (1993) Cell , vol.82 , pp. 545-554
    • Zimmerly, S.1    Guo, H.2    Perlman, P.S.3    Lambowitz, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.