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Volumn 69, Issue 7, 1995, Pages 4440-4452

Effects on DNA synthesis and translocation caused by mutations in the RNase H domain of Moloney murine leukemia virus reverse transcriptase

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEASE H; RNA DIRECTED DNA POLYMERASE;

EID: 0029055878     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.69.7.4440-4452.1995     Document Type: Article
Times cited : (39)

References (70)
  • 1
    • 0028057881 scopus 로고
    • Trans-activation of the minus strand DNA transfer by nucleocapsid protein during reverse transcription of the retroviral genome
    • Allain, B., M. Lapadat-Tapolsky, C. Berlioz, and J.-L. Darlix. 1994. Trans-activation of the minus strand DNA transfer by nucleocapsid protein during reverse transcription of the retroviral genome. EMBO J. 13:973-981.
    • (1994) EMBO J. , vol.13 , pp. 973-981
    • Allain, B.1    Lapadat-Tapolsky, M.2    Berlioz, C.3    Darlix, J.-L.4
  • 2
    • 0014964654 scopus 로고
    • RNA-dependent DNA polymerase in virions of RNA tumor viruses
    • Baltimore, D. 1970. RNA-dependent DNA polymerase in virions of RNA tumor viruses. Nature (London) 226:1209-1211.
    • (1970) Nature (London) , vol.226 , pp. 1209-1211
    • Baltimore, D.1
  • 3
    • 0027441816 scopus 로고
    • HIV-1 reverse transcriptase: Polymerization properties of the p51 homodimer compared to the p66/p51 heterodimer
    • Bavand, M. R., R. Wagner, and T. J. Richmond. 1993. HIV-1 reverse transcriptase: polymerization properties of the p51 homodimer compared to the p66/p51 heterodimer. Biochemistry 32:10543-10552.
    • (1993) Biochemistry , vol.32 , pp. 10543-10552
    • Bavand, M.R.1    Wagner, R.2    Richmond, T.J.3
  • 4
    • 0027257467 scopus 로고
    • RNase H activity of reverse transcriptases on substrates derived from the 5′ end of retroviral genome
    • Ben-Artzi, H., E. Zeelon, B. Amit, A. Wortzel, M. Gorecki, and A. Panet. 1993. RNase H activity of reverse transcriptases on substrates derived from the 5′ end of retroviral genome. J. Biol. Chem. 268:16465-16471.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16465-16471
    • Ben-Artzi, H.1    Zeelon, E.2    Amit, B.3    Wortzel, A.4    Gorecki, M.5    Panet, A.6
  • 5
    • 0027453514 scopus 로고
    • Nuclease activities of Moloney murine leukemia virus reverse transcriptase: Mutants with altered substrate specificities
    • Blain, S. W., and S. P. Goff. 1993. Nuclease activities of Moloney murine leukemia virus reverse transcriptase: mutants with altered substrate specificities. J. Biol. Chem. 268:23585-23592.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23585-23592
    • Blain, S.W.1    Goff, S.P.2
  • 7
    • 0019352790 scopus 로고
    • Viral DNA synthesized in vitro by avian retrovirus particles permeabilized with melittin. II. Evidence of a strand displacement mechanism in plus-strand synthesis
    • Boone, L. R. and A. M. Skalka. 1981. Viral DNA synthesized in vitro by avian retrovirus particles permeabilized with melittin. II. Evidence of a strand displacement mechanism in plus-strand synthesis. J. Virol. 37:117-126.
    • (1981) J. Virol. , vol.37 , pp. 117-126
    • Boone, L.R.1    Skalka, A.M.2
  • 8
    • 0026496655 scopus 로고
    • Mutational analysis of the fingers domain of human immunodeficiency virus type 1 reverse transcriptase
    • Boyer, P. L., A. L. Ferris, and S. H. Hughes. 1992. Mutational analysis of the fingers domain of human immunodeficiency virus type 1 reverse transcriptase. J. Virol. 66:7533-7537.
    • (1992) J. Virol. , vol.66 , pp. 7533-7537
    • Boyer, P.L.1    Ferris, A.L.2    Hughes, S.H.3
  • 9
    • 0000553844 scopus 로고
    • Roles of ribonuclease H in reverse transcription
    • A.-M. Skalka and S. P. Goff (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Champoux, J. J. 1993. Roles of ribonuclease H in reverse transcription, p. 103-118 In A.-M. Skalka and S. P. Goff (ed.), Reverse transcriptase. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1993) Reverse Transcriptase , pp. 103-118
    • Champoux, J.J.1
  • 10
    • 0023734473 scopus 로고
    • Novel non-templated nucleotide addition reactions catalyzed by procaryotic and eucaryotic DNA polymerases
    • Clark, J. M. 1988. Novel non-templated nucleotide addition reactions catalyzed by procaryotic and eucaryotic DNA polymerases. Nucleic Acids Res. 16:9677-9686.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9677-9686
    • Clark, J.M.1
  • 11
    • 0017682918 scopus 로고
    • Terminal redundancy and the origin of replication of Rous sarcoma virus RNA
    • Coffin, J. M., and W. A. Haseltine. 1977. Terminal redundancy and the origin of replication of Rous sarcoma virus RNA. Proc. Natl. Acad. Sci. USA 74:1908-1912.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 1908-1912
    • Coffin, J.M.1    Haseltine, W.A.2
  • 12
    • 0024278041 scopus 로고
    • Sequence and spacing requirements of a retrovirus integration site
    • Colicelli, J., and S. P. Goff. 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
    • Colicelli, J.1    Goff, S.P.2
  • 13
    • 0017803621 scopus 로고
    • Unwinding-like activity associated with avian retrovirus RNA-directed DNA polymerase
    • Collett, M. S., J. P. Leis, M. S. Smith, and A. J. Faras. 1978. Unwinding-like activity associated with avian retrovirus RNA-directed DNA polymerase. J. Virol. 26:498-509.
    • (1978) J. Virol. , vol.26 , pp. 498-509
    • Collett, M.S.1    Leis, J.P.2    Smith, M.S.3    Faras, A.J.4
  • 14
    • 0025084228 scopus 로고
    • Ribonuclease H: From discovery to 3D structure
    • Crouch, R. J. 1990. Ribonuclease H: from discovery to 3D structure. New Biol. 2:771-777.
    • (1990) New Biol. , vol.2 , pp. 771-777
    • Crouch, R.J.1
  • 15
    • 0025908083 scopus 로고
    • Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
    • Davies, J. F., II, Z. Hostomska, Z. Hostomsky, S. R. Jorden, and D. A. Matthews. 1991. Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase. Science 252:88-95.
    • (1991) Science , vol.252 , pp. 88-95
    • Davies II, J.F.1    Hostomska, Z.2    Hostomsky, Z.3    Jorden, S.R.4    Matthews, D.A.5
  • 16
    • 0027328663 scopus 로고
    • Parameters that influence the binding of human immunodeficiency virus reverse transcriptase to nucleic acid structures
    • DeStefano, J. J., R. A. Bambara, and P. J. Fay. 1993. Parameters that influence the binding of human immunodeficiency virus reverse transcriptase to nucleic acid structures. Biochemistry 32:6908-6915.
    • (1993) Biochemistry , vol.32 , pp. 6908-6915
    • DeStefano, J.J.1    Bambara, R.A.2    Fay, P.J.3
  • 17
    • 0025912708 scopus 로고
    • Polymerization and RNase H activities of the reverse transcriptases from avian myeloblastosis, human immunodeficiency, and Moloney murine leukemia viruses are functionally uncoupled
    • DeStefano, J. J., R. G. Buiser, L. M. Mallaber, T. W. Myers, R. A. Bambara, and P. J. Fay. 1991. Polymerization and RNase H activities of the reverse transcriptases from avian myeloblastosis, human immunodeficiency, and Moloney murine leukemia viruses are functionally uncoupled. J. Biol. Chem. 266:7423-7431.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7423-7431
    • DeStefano, J.J.1    Buiser, R.G.2    Mallaber, L.M.3    Myers, T.W.4    Bambara, R.A.5    Fay, P.J.6
  • 18
    • 0026646806 scopus 로고
    • Requirements for strand transfer between internal regions of heteropolymer templates by human immunodeficiency virus reverse transcriptase
    • DeStefano, J. J., L. M. Mallaber, L. Rodriguez-Rodriguez, P. J. Fay, and R. A. Bambara. 1992. Requirements for strand transfer between internal regions of heteropolymer templates by human immunodeficiency virus reverse transcriptase. J. Virol. 66:6370-6378.
    • (1992) J. Virol. , vol.66 , pp. 6370-6378
    • DeStefano, J.J.1    Mallaber, L.M.2    Rodriguez-Rodriguez, L.3    Fay, P.J.4    Bambara, R.A.5
  • 19
    • 0027256313 scopus 로고
    • Rapid kinetic analysis of a point mutant of HIV-1 reverse transcriptase lacking ribonuclease H activity
    • Dudding, L. R., and V. Mizrahi. 1993. Rapid kinetic analysis of a point mutant of HIV-1 reverse transcriptase lacking ribonuclease H activity. Biochemistry 32:6116-6120.
    • (1993) Biochemistry , vol.32 , pp. 6116-6120
    • Dudding, L.R.1    Mizrahi, V.2
  • 20
    • 0026342152 scopus 로고
    • Analysis of the RNA-and DNA-dependent DNA polymerase activities of point mutants of HIV-1 reverse transcriptase lacking ribonuclease H activity
    • Dudding, L. R., N. C. Nkabinde, and V. Mizrahi. 1991. Analysis of the RNA-and DNA-dependent DNA polymerase activities of point mutants of HIV-1 reverse transcriptase lacking ribonuclease H activity. Biochemistry 30:10498-10506.
    • (1991) Biochemistry , vol.30 , pp. 10498-10506
    • Dudding, L.R.1    Nkabinde, N.C.2    Mizrahi, V.3
  • 21
    • 0026664173 scopus 로고
    • When retroviral reverse transcriptases reach the end of their RNA templates
    • Fu, T.-B., and J. Taylor. 1992. When retroviral reverse transcriptases reach the end of their RNA templates. J. Virol. 66:4271-4278.
    • (1992) J. Virol. , vol.66 , pp. 4271-4278
    • Fu, T.-B.1    Taylor, J.2
  • 22
    • 0002565136 scopus 로고
    • Involvement of nucleocapsids in reverse transcription: A general phenomenon?
    • Fuetterer, J., and T. Hohn. 1987. Involvement of nucleocapsids in reverse transcription: a general phenomenon? Trends Biochem. Sci. 12:92-95.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 92-95
    • Fuetterer, J.1    Hohn, T.2
  • 23
    • 0025924750 scopus 로고
    • Reverse transcriptase-RNase H from the human immunodeficiency virus: Relationship of the DNA polymerase and RNA hydrolysis activities
    • Furfine, E. S., and J. E. Reardon. 1991. Reverse transcriptase-RNase H from the human immunodeficiency virus: relationship of the DNA polymerase and RNA hydrolysis activities. J. Biol. Chem. 266:406-412.
    • (1991) J. Biol. Chem. , vol.266 , pp. 406-412
    • Furfine, E.S.1    Reardon, J.E.2
  • 24
    • 0025810354 scopus 로고
    • Reverse-transcriptase-associated RNase H activity mediates template switching during reverse transcription in vitro
    • Garces, J., and R. Wittek, 1991. Reverse-transcriptase-associated RNase H activity mediates template switching during reverse transcription in vitro. Proc. R. Soc. Lond. Ser. B Biol. Sci. 243:235-239.
    • (1991) Proc. R. Soc. Lond. Ser. B Biol. Sci. , vol.243 , pp. 235-239
    • Garces, J.1    Wittek, R.2
  • 25
    • 0018716671 scopus 로고
    • A detailed model of reverse transcription and tests of crucial aspects
    • Gilboa, E., S. W. Mitra, S. P. Goff, and D. Baltimore. 1980. A detailed model of reverse transcription and tests of crucial aspects. Cell 18:93-100.
    • (1980) Cell , vol.18 , pp. 93-100
    • Gilboa, E.1    Mitra, S.W.2    Goff, S.P.3    Baltimore, D.4
  • 26
    • 0024999452 scopus 로고
    • Retroviral reverse transcriptase: Synthesis, structure and function
    • Goff, S. P. 1990. Retroviral reverse transcriptase: synthesis, structure and function. J. Acquired Immune Defic. Syndr. 3:817-831.
    • (1990) J. Acquired Immune Defic. Syndr. , vol.3 , pp. 817-831
    • Goff, S.P.1
  • 27
    • 0019507492 scopus 로고
    • Isolation and properties of Moloney murine leukemia virus mutants: Use of a rapid assay for release of virion reverse transcriptase
    • Goff, S. P., P. Traktman, and D. Baltimore. 1981. Isolation and properties of Moloney murine leukemia virus mutants: use of a rapid assay for release of virion reverse transcriptase. J. Virol. 38:239-248.
    • (1981) J. Virol. , vol.38 , pp. 239-248
    • Goff, S.P.1    Traktman, P.2    Baltimore, D.3
  • 28
    • 0023798826 scopus 로고
    • Two dominant acting selectable markers for gene transfer in mammalian cells
    • Hartman, S. C., and R. C. Mulligan. 1988. Two dominant acting selectable markers for gene transfer in mammalian cells. Proc. Natl. Acad. Sci. USA 85:8047-8051.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8047-8051
    • Hartman, S.C.1    Mulligan, R.C.2
  • 29
    • 0014202537 scopus 로고
    • Selective extraction of polyoma DNA from infected mouse cell cultures
    • Hirt, B. 1967. Selective extraction of polyoma DNA from infected mouse cell cultures. J. Mol. Biol. 106:365-369.
    • (1967) J. Mol. Biol. , vol.106 , pp. 365-369
    • Hirt, B.1
  • 30
    • 0022484140 scopus 로고
    • Murine leukemia virus pol gene products: Analysis with antisera generated against reverse transcriptase and endonuciease 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 endonuciease 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
  • 31
    • 0025635705 scopus 로고
    • Retroviral recombination and reverse transcription
    • Hu, W.-S., and H. M. Temin. 1990. Retroviral recombination and reverse transcription. Science 250:1227-1233.
    • (1990) Science , vol.250 , pp. 1227-1233
    • Hu, W.-S.1    Temin, H.M.2
  • 32
    • 0024519430 scopus 로고
    • Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching
    • Huber, H. E., J. M. McCoy, J. S. Seehra, and C. C. Richardson. 1989. Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching. J. Biol. Chem. 264:4669-4678.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4669-4678
    • Huber, H.E.1    McCoy, J.M.2    Seehra, J.S.3    Richardson, C.C.4
  • 33
    • 0025314263 scopus 로고
    • Processing the primer for plus strand DNA synthesis by human immunodeficiency virus 1 reverse transcriptase
    • Huber, H. E., and C. C. Richardson. 1990. Processing the primer for plus strand DNA synthesis by human immunodeficiency virus 1 reverse transcriptase. J. Biol. Chem. 265:10565-10573.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10565-10573
    • Huber, H.E.1    Richardson, C.C.2
  • 34
    • 0025775810 scopus 로고
    • HIV reverse transcriptase structure-function relationships
    • Jacobo-Molina, A., and E. Arnold. 1991. HIV reverse transcriptase structure-function relationships. Biochemistry 30:6354-6361.
    • (1991) Biochemistry , vol.30 , pp. 6354-6361
    • Jacobo-Molina, A.1    Arnold, E.2
  • 36
    • 0028147389 scopus 로고
    • One retroviral RNA is sufficient for synthesis of viral DNA
    • Jones, J. S., R. W. Allan, and H. M. Temin. 1994. One retroviral RNA is sufficient for synthesis of viral DNA. J. Virol. 68:207-216.
    • (1994) J. Virol. , vol.68 , pp. 207-216
    • Jones, J.S.1    Allan, R.W.2    Temin, H.M.3
  • 38
    • 0026095261 scopus 로고
    • Importance of the positive charge cluster in Escherichia coli ribonuclease Hl for the effective binding of substrate
    • Kanaya, S., C. Katsuda-Nakai, and M. Ikehara. 1991. Importance of the positive charge cluster in Escherichia coli ribonuclease Hl for the effective binding of substrate. J. Biol. Chem. 266:11621-11627.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11621-11627
    • Kanaya, S.1    Katsuda-Nakai, C.2    Ikehara, M.3
  • 40
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt, L. A., J. Wang, J. M. Friedman, P. A. Rice, and T. A. Sieitz. 1992. Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256:1783-1790.
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Sieitz, T.A.5
  • 41
    • 0027258736 scopus 로고
    • Interaction between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle
    • Lapadat-Tapolsky, M., H. De Rocquigny, D. van Gent, B. Roques, R. Plasterk, and J.-L. Darlix. 1993. Interaction between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle. Nucleic Acids Res. 21:831-839.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 831-839
    • Lapadat-Tapolsky, M.1    De Rocquigny, H.2    Van Gent, D.3    Roques, B.4    Plasterk, R.5    Darlix, J.-L.6
  • 42
    • 0026030093 scopus 로고
    • Relationship of avian retrovirus DNA synthesis to integration in vitro
    • Lee, Y. M. H., and J. M. Coffin. 1991. Relationship of avian retrovirus DNA synthesis to integration in vitro. Mol. Cell. Biol. 11:1419-1430.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1419-1430
    • Lee, Y.M.H.1    Coffin, J.M.2
  • 43
    • 0021958611 scopus 로고
    • Reverse transcription of retroviral genomes: Mutations in the terminal repeats
    • Lobel, L. I., and S. P. Goff. 1985. Reverse transcription of retroviral genomes: mutations in the terminal repeats. J. Virol. 53:447-455.
    • (1985) J. Virol. , vol.53 , pp. 447-455
    • Lobel, L.I.1    Goff, S.P.2
  • 44
    • 0025112945 scopus 로고
    • Template switching by reverse transcriptase during DNA synthesis
    • Luo, B., and J. Taylor. 1990. Template switching by reverse transcriptase during DNA synthesis. J. Virol. 64:4321-4328.
    • (1990) J. Virol. , vol.64 , pp. 4321-4328
    • Luo, B.1    Taylor, J.2
  • 45
    • 0014322388 scopus 로고
    • Enhancement of the infectivity of simian virus 40 deoxyribonucleic acid with diethylaminoethyl-dextran
    • McCutchan, J. H., and J. S. Pagano. 1968. Enhancement of the infectivity of simian virus 40 deoxyribonucleic acid with diethylaminoethyl-dextran. J. Natl. Cancer Inst. 41:351-357.
    • (1968) J. Natl. Cancer Inst. , vol.41 , pp. 351-357
    • McCutchan, J.H.1    Pagano, J.S.2
  • 46
    • 0025882254 scopus 로고
    • Structural models of ribonuelease H domains in reverse transcriptases from retroviruses
    • Nakamura, H., K. Katayanagi, K. Morikawa, and M. Ikehara. 1991. Structural models of ribonuelease H domains in reverse transcriptases from retroviruses. Nucleic Acids Res. 19:1817-1823.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1817-1823
    • Nakamura, H.1    Katayanagi, K.2    Morikawa, K.3    Ikehara, M.4
  • 48
    • 0024434124 scopus 로고
    • Intrinsic properties of reverse transcriptase in reverse transcription: Associated RNase H is essentially regarded as an endonuclease
    • Oyama, F., R. Kikuchi, R. J. Crouch, and T. Uchida. 1989. Intrinsic properties of reverse transcriptase in reverse transcription: associated RNase H is essentially regarded as an endonuclease. J. Biol. Chem. 264:18808-18817.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18808-18817
    • Oyama, F.1    Kikuchi, R.2    Crouch, R.J.3    Uchida, T.4
  • 49
    • 0024297783 scopus 로고
    • Ordered interstrand and intrastrand DNA transfer during reverse transcription
    • Panganiban, A. T., and D. Fiore. 1988. Ordered interstrand and intrastrand DNA transfer during reverse transcription. Science 241:1064-1069.
    • (1988) Science , vol.241 , pp. 1064-1069
    • Panganiban, A.T.1    Fiore, D.2
  • 50
    • 0028088986 scopus 로고
    • Marked infidelity of human immunodeficiency virus type 1 reverse transcriptase at RNA and DNA template ends
    • Patel, P. H., and B. D. Preston. 1994. Marked infidelity of human immunodeficiency virus type 1 reverse transcriptase at RNA and DNA template ends. Proc. Natl. Acad. Sci. USA 91:549-553.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 549-553
    • Patel, P.H.1    Preston, B.D.2
  • 51
    • 0026486193 scopus 로고
    • Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase
    • Peliska, J. A., and S. J. Benkovic. 1992. Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase. Science 258:1112-1118.
    • (1992) Science , vol.258 , pp. 1112-1118
    • Peliska, J.A.1    Benkovic, S.J.2
  • 52
    • 0027158755 scopus 로고
    • Replication of the retroviral terminal repeat sequence during in vivo reverse transcription
    • Ramsey, C. A., and A. T. Panganiban. 1993. Replication of the retroviral terminal repeat sequence during in vivo reverse transcription. J. Virol. 67: 4114-4121.
    • (1993) J. Virol. , vol.67 , pp. 4114-4121
    • Ramsey, C.A.1    Panganiban, A.T.2
  • 53
    • 0017359967 scopus 로고
    • Increased length of DNA made by virions of murine leukemia virus at limiting magnesium ion concentrations
    • Rothenberg, E., and D. Baltimore. 1977. Increased length of DNA made by virions of murine leukemia virus at limiting magnesium ion concentrations. J. Virol. 21:168-178.
    • (1977) J. Virol. , vol.21 , pp. 168-178
    • Rothenberg, E.1    Baltimore, D.2
  • 56
    • 0025267173 scopus 로고
    • HIV-1 RT-associated ribonuelease H displays both endonuclease and 3′-5′ exonuclease activity
    • Schatz, O., J. Mous, and S. F. Le Grice. 1990. HIV-1 RT-associated ribonuelease H displays both endonuclease and 3′-5′ exonuclease activity. EMBO J. 9:1171-1176.
    • (1990) EMBO J. , vol.9 , pp. 1171-1176
    • Schatz, O.1    Mous, J.2    Le Grice, S.F.3
  • 57
    • 0003543882 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Skalka, A.-M., and S. P. Goff, ed. 1993. Reverse transcriptase. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1993) Reverse Transcriptase
    • Skalka, A.-M.1    Goff, S.P.2
  • 58
    • 0019457949 scopus 로고
    • The terminal redundancy of the retroviral genome facilitates chain elongation by reverse transcriptase
    • Swanstrom, R., H. E. Varmus, and J. M. Bishop. 1981. The terminal redundancy of the retroviral genome facilitates chain elongation by reverse transcriptase. J. Biol. Chem. 256:1115-1121.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1115-1121
    • Swanstrom, R.1    Varmus, H.E.2    Bishop, J.M.3
  • 59
    • 0024121540 scopus 로고
    • Domain structure of the Moloney murine leukemia virus reverse transcriptase: Mutational analysis and separate expression of the polymerase and RNase H activities
    • Tanese, N., and S. P. Goff. 1988. Domain structure of the Moloney murine leukemia virus reverse transcriptase: mutational analysis and separate expression of the polymerase and RNase H activities. Proc. Natl. Acad. Sci. USA 85:1777-1781.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1777-1781
    • Tanese, N.1    Goff, S.P.2
  • 60
    • 0025873605 scopus 로고
    • Abortive reverse transcription by mutants of Moloney murine leukemia virus deficient in the reverse transcriptase-associated RNase H function
    • Tanese, N., A. Telesnitsky, and S. P. Goff. 1991. Abortive reverse transcription by mutants of Moloney murine leukemia virus deficient in the reverse transcriptase-associated RNase H function. J. Virol. 65:4387-4397.
    • (1991) J. Virol. , vol.65 , pp. 4387-4397
    • Tanese, N.1    Telesnitsky, A.2    Goff, S.P.3
  • 61
    • 0026571161 scopus 로고
    • Defects in Moloney murine leukemia virus replication caused by a reverse transcriptase mutation modeled on the structure of Escherichia coli RNase H
    • Telesnitsky, A., S. W. Blain, and S. P. Goff. 1992. Defects in Moloney murine leukemia virus replication caused by a reverse transcriptase mutation modeled on the structure of Escherichia coli RNase H. J. Virol. 66:615-622.
    • (1992) J. Virol. , vol.66 , pp. 615-622
    • Telesnitsky, A.1    Blain, S.W.2    Goff, S.P.3
  • 62
    • 0027518740 scopus 로고
    • RNase H domain mutations affect the interaction between Moloney murine leukemia virus reverse transcriptase and its primer-template
    • Telesnitsky, A., and S. P. Goff. 1993. RNase H domain mutations affect the interaction between Moloney murine leukemia virus reverse transcriptase and its primer-template. Proc. Natl. Acad. Sci. USA 90:1276-1280.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1276-1280
    • Telesnitsky, A.1    Goff, S.P.2
  • 63
    • 0027382852 scopus 로고
    • Two defective forms of reverse transcriptase can complement to restore retroviral infectivity
    • Telesnitsky, A., and S. P. Goff. 1993. Two defective forms of reverse transcriptase can complement to restore retroviral infectivity. EMBO J. 12:4433-4438.
    • (1993) EMBO J. , vol.12 , pp. 4433-4438
    • Telesnitsky, A.1    Goff, S.P.2
  • 64
    • 0014964695 scopus 로고
    • RNA-directed DNA polymerase in virions of Rous sarcoma virus
    • Temin, H. M., and S. Mizutani. 1970. RNA-directed DNA polymerase in virions of Rous sarcoma virus. Nature (London) 226:1211-1213.
    • (1970) Nature (London) , vol.226 , pp. 1211-1213
    • Temin, H.M.1    Mizutani, S.2
  • 65
    • 0002915381 scopus 로고
    • Retroviruses
    • D. E. Berg and M. M. Howe (ed.), American Society for Microbiology, Washington, D.C.
    • Varmus, H. E., and P. Brown. 1989. Retroviruses, p. 55-108. In D. E. Berg and M. M. Howe (ed.), Mobile DNA. American Society for Microbiology, Washington, D.C.
    • (1989) Mobile DNA , pp. 55-108
    • Varmus, H.E.1    Brown, P.2
  • 66
    • 0017884602 scopus 로고
    • Kinetics of synthesis, structure and purification of avian sarcoma virus-specific DNA made in the cytoplasm of acutely infected cells
    • Varmus, H. E., S. Heasley, K.-J. Kung, H. Oppennann, W. C. Smith, J. M. Bishop, and P. R. Shank. 1978. Kinetics of synthesis, structure and purification of avian sarcoma virus-specific DNA made in the cytoplasm of acutely infected cells. J. Mol. Biol. 120:55-82.
    • (1978) J. Mol. Biol. , vol.120 , pp. 55-82
    • Varmus, H.E.1    Heasley, S.2    Kung, K.-J.3    Oppennann, H.4    Smith, W.C.5    Bishop, J.M.6    Shank, P.R.7
  • 68
    • 0025605872 scopus 로고
    • Ribonucleases H of retroviral and cellular origin
    • Wintersberger, U. 1990. Ribonucleases H of retroviral and cellular origin. Pharmacol Ther. 48:259-280.
    • (1990) Pharmacol Ther. , vol.48 , pp. 259-280
    • Wintersberger, U.1
  • 70
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein
    • Yang, W., W. A. Hendrickson, R. J. Crouch, and Y. Satow. 1990. Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein. Science 249:1398-1405.
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4


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