메뉴 건너뛰기




Volumn 3, Issue 2, 2015, Pages

Reverse transcription of retroviruses and LTR retrotransposons

Author keywords

[No Author keywords available]

Indexed keywords

RETROPOSON; RNA DIRECTED DNA POLYMERASE;

EID: 84943382672     PISSN: None     EISSN: 21650497     Source Type: Journal    
DOI: 10.1128/microbiolspec.MDNA3-0027-2014     Document Type: Article
Times cited : (43)

References (240)
  • 1
    • 0002296754 scopus 로고    scopus 로고
    • Reverse transcriptase and the generation of retroviral DNA
    • Coffin JM, Hughes SH, Varmus HE (ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Telesnitsky A, Goff, G.P. 1997. Reverse transcriptase and the generation of retroviral DNA, p. 121-160. In Coffin JM, Hughes SH, Varmus HE (ed), Retroviruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1997) Retroviruses , pp. 121-160
    • Telesnitsky, A.1    Goff, G.P.2
  • 2
    • 58149133507 scopus 로고    scopus 로고
    • Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition
    • Sarafianos SG, Marchand B, Das K, Himmel DM, Parniak MA, Hughes SH, Arnold E. 2009. Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition. J Mol Biol 385:693-713.
    • (2009) J Mol Biol , vol.385 , pp. 693-713
    • Sarafianos, S.G.1    Marchand, B.2    Das, K.3    Himmel, D.M.4    Parniak, M.A.5    Hughes, S.H.6    Arnold, E.7
  • 3
    • 84903895598 scopus 로고    scopus 로고
    • HIV-1 Reverse Transcription
    • Bushman FD, Nabel GJ, Swanstrom R (ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hu W, Hughes SH. 2012. HIV-1 Reverse Transcription, p. 37-58. In Bushman FD, Nabel GJ, Swanstrom R (ed), HIV from Biology to Prevention and Treatment. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2012) HIV from Biology to Prevention and Treatment , pp. 37-58
    • Hu, W.1    Hughes, S.H.2
  • 4
    • 0003543882 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Skalka AM, GoffSP. 1993. Reverse Transcriptase. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1993) Reverse Transcriptase
    • Skalka, A.M.1    Goff, S.P.2
  • 5
    • 0018716671 scopus 로고
    • A detailed model of reverse transcription and tests of crucial aspects
    • Gilboa E, Mitra SW, GoffS, Baltimore D. 1979. A detailed model of reverse transcription and tests of crucial aspects. Cell 18:93-100.
    • (1979) Cell , vol.18 , pp. 93-100
    • Gilboa, E.1    Mitra, S.W.2    Goff, S.3    Baltimore, D.4
  • 6
    • 0018220356 scopus 로고
    • Mapping unintegrated avian sarcoma virus DNA: termini of linear DNA bear 300 nucleotides present once or twice in two species of circular DNA
    • Shank PR, Hughes SH, Kung HJ, Majors JE, Quintrell N, Guntaka RV, Bishop JM, Varmus HE. 1978. Mapping unintegrated avian sarcoma virus DNA: termini of linear DNA bear 300 nucleotides present once or twice in two species of circular DNA. Cell 15:1383-1395.
    • (1978) Cell , vol.15 , pp. 1383-1395
    • Shank, P.R.1    Hughes, S.H.2    Kung, H.J.3    Majors, J.E.4    Quintrell, N.5    Guntaka, R.V.6    Bishop, J.M.7    Varmus, H.E.8
  • 7
    • 0018224936 scopus 로고
    • Proviruses of avian sarcoma virus are terminally redundant, co-extensive with unintegrated linear DNA and integrated at many sites
    • Hughes SH, Shank PR, Spector DH, Kung HJ, Bishop JM, Varmus HE, Vogt PK, Breitman ML. 1978. Proviruses of avian sarcoma virus are terminally redundant, co-extensive with unintegrated linear DNA and integrated at many sites. Cell 15:1397-1410.
    • (1978) Cell , vol.15 , pp. 1397-1410
    • Hughes, S.H.1    Shank, P.R.2    Spector, D.H.3    Kung, H.J.4    Bishop, J.M.5    Varmus, H.E.6    Vogt, P.K.7    Breitman, M.L.8
  • 9
    • 0033031015 scopus 로고    scopus 로고
    • The yeast retrotransposon Ty5 uses the anticodon stem-loop of the initiator methionine tRNA as a primer for reverse transcription
    • Ke N, Gao X, Keeney JB, Boeke JD, Voytas DF. 1999. The yeast retrotransposon Ty5 uses the anticodon stem-loop of the initiator methionine tRNA as a primer for reverse transcription. RNA 5:929-938.
    • (1999) RNA , vol.5 , pp. 929-938
    • Ke, N.1    Gao, X.2    Keeney, J.B.3    Boeke, J.D.4    Voytas, D.F.5
  • 10
    • 0031741741 scopus 로고    scopus 로고
    • Reverse transcription of a self-primed retrotransposon requires an RNA structure similar to the U5-IR stem-loop of retroviruses
    • Lin JH, Levin HL. 1998. Reverse transcription of a self-primed retrotransposon requires an RNA structure similar to the U5-IR stem-loop of retroviruses. Mol Cell Biol 18:6859-6869.
    • (1998) Mol Cell Biol , vol.18 , pp. 6859-6869
    • Lin, J.H.1    Levin, H.L.2
  • 11
    • 0030019943 scopus 로고    scopus 로고
    • Specific initiation and switch to elongation of human immunodeficiency virus type 1 reverse transcription require the post-transcriptional modifications of primer tRNA3Lys
    • Isel C, Lanchy JM, Le Grice SF, Ehresmann C, Ehresmann B, Marquet R. 1996. Specific initiation and switch to elongation of human immunodeficiency virus type 1 reverse transcription require the post-transcriptional modifications of primer tRNA3Lys. EMBO J 15:917-924.
    • (1996) EMBO J , vol.15 , pp. 917-924
    • Isel, C.1    Lanchy, J.M.2    Le Grice, S.F.3    Ehresmann, C.4    Ehresmann, B.5    Marquet, R.6
  • 12
    • 0030449991 scopus 로고    scopus 로고
    • Binding and kinetic properties of HIV-1 reverse transcriptase markedly differ during initiation and elongation of reverse transcription
    • Lanchy JM, Ehresmann C, Le Grice SF, Ehresmann B, Marquet R. 1996. Binding and kinetic properties of HIV-1 reverse transcriptase markedly differ during initiation and elongation of reverse transcription. EMBO J 15:7178-7187.
    • (1996) EMBO J , vol.15 , pp. 7178-7187
    • Lanchy, J.M.1    Ehresmann, C.2    Le Grice, S.F.3    Ehresmann, B.4    Marquet, R.5
  • 13
    • 0027382852 scopus 로고
    • Two defective forms of reverse transcriptase can complement to restore retroviral infectivity
    • Telesnitsky A, GoffSP. 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
  • 14
    • 0034990535 scopus 로고    scopus 로고
    • Replication of phenotypically mixed human immunodeficiency virus type 1 virions containing catalytically active and catalytically inactive reverse transcriptase
    • Julias JG, Ferris AL, Boyer PL, Hughes SH. 2001. Replication of phenotypically mixed human immunodeficiency virus type 1 virions containing catalytically active and catalytically inactive reverse transcriptase. J Virol 75:6537-6546.
    • (2001) J Virol , vol.75 , pp. 6537-6546
    • Julias, J.G.1    Ferris, A.L.2    Boyer, P.L.3    Hughes, S.H.4
  • 15
    • 0035172899 scopus 로고    scopus 로고
    • In vitro analysis of human immunodeficiency virus type 1 minus-strand strong-stop DNA synthesis and genomic RNA processing
    • Driscoll MD, Golinelli MP, Hughes SH. 2001. In vitro analysis of human immunodeficiency virus type 1 minus-strand strong-stop DNA synthesis and genomic RNA processing. J Virol 75:672-686.
    • (2001) J Virol , vol.75 , pp. 672-686
    • Driscoll, M.D.1    Golinelli, M.P.2    Hughes, S.H.3
  • 16
    • 34250322690 scopus 로고    scopus 로고
    • Mechanisms that prevent template inactivation by HIV-1 reverse transcriptase RNase H cleavages
    • Purohit V, Roques BP, Kim B, Bambara RA. 2007. Mechanisms that prevent template inactivation by HIV-1 reverse transcriptase RNase H cleavages. J Biol Chem 282:12598-12609.
    • (2007) J Biol Chem , vol.282 , pp. 12598-12609
    • Purohit, V.1    Roques, B.P.2    Kim, B.3    Bambara, R.A.4
  • 17
    • 0024297783 scopus 로고
    • Ordered interstrand and intrastrand DNA transfer during reverse transcription
    • Panganiban AT, Fiore D. 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
  • 18
    • 0025635705 scopus 로고
    • Retroviral recombination and reverse transcription
    • Hu WS, Temin HM. 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
  • 19
    • 0032503218 scopus 로고    scopus 로고
    • The first strand transfer during HIV-1 reverse transcription can occur either intramolecularly or intermolecularly
    • van Wamel JL, Berkhout B. 1998. The first strand transfer during HIV-1 reverse transcription can occur either intramolecularly or intermolecularly. Virology 244:245-251.
    • (1998) Virology , vol.244 , pp. 245-251
    • van Wamel, J.L.1    Berkhout, B.2
  • 20
    • 0033045438 scopus 로고    scopus 로고
    • Reverse transcription of the yeast Ty1 retrotransposon: the mode of first strand transfer is either intermolecular or intramolecular
    • Wilhelm M, Boutabout M, Heyman T, Wilhelm FX. 1999. Reverse transcription of the yeast Ty1 retrotransposon: the mode of first strand transfer is either intermolecular or intramolecular. J Mol Biol 288:505-510.
    • (1999) J Mol Biol , vol.288 , pp. 505-510
    • Wilhelm, M.1    Boutabout, M.2    Heyman, T.3    Wilhelm, F.X.4
  • 21
    • 0026806438 scopus 로고
    • Mutations in the central polypurine tract of HIV-1 result in delayed replication
    • Hungnes O, Tjotta E, Grinde B. 1992. Mutations in the central polypurine tract of HIV-1 result in delayed replication. Virology 190:440-442.
    • (1992) Virology , vol.190 , pp. 440-442
    • Hungnes, O.1    Tjotta, E.2    Grinde, B.3
  • 22
    • 0026506252 scopus 로고
    • A second origin of DNA plusstrand synthesis is required for optimal human immunodeficiency virus replication
    • Charneau P, Alizon M, Clavel F. 1992. A second origin of DNA plusstrand synthesis is required for optimal human immunodeficiency virus replication. J Virol 66:2814-2820.
    • (1992) J Virol , vol.66 , pp. 2814-2820
    • Charneau, P.1    Alizon, M.2    Clavel, F.3
  • 23
    • 0019457949 scopus 로고
    • The terminal redundancy of the retrovirus genome facilitates chain elongation by reverse transcriptase
    • Swanstrom R, Varmus HE, Bishop JM. 1981. The terminal redundancy of the retrovirus 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
  • 24
    • 0032561343 scopus 로고    scopus 로고
    • The nature of human immunodeficiency virus type 1 strand transfers
    • Yu H, Jetzt AE, Ron Y, Preston BD, Dougherty JP. 1998. The nature of human immunodeficiency virus type 1 strand transfers. J Biol Chem 273:28384-28391.
    • (1998) J Biol Chem , vol.273 , pp. 28384-28391
    • Yu, H.1    Jetzt, A.E.2    Ron, Y.3    Preston, B.D.4    Dougherty, J.P.5
  • 25
    • 0019381329 scopus 로고
    • Synthesis of plus strands of retroviral DNA in cells infected with avian sarcoma virus and mouse mammary tumor virus
    • Kung HJ, Fung YK, Majors JE, Bishop JM, Varmus HE. 1981. Synthesis of plus strands of retroviral DNA in cells infected with avian sarcoma virus and mouse mammary tumor virus. J Virol 37:127-138.
    • (1981) J Virol , vol.37 , pp. 127-138
    • Kung, H.J.1    Fung, Y.K.2    Majors, J.E.3    Bishop, J.M.4    Varmus, H.E.5
  • 26
    • 0019978297 scopus 로고
    • Single-stranded regions on unintegrated avian retrovirus DNA
    • Hsu TW, Taylor JM. 1982. Single-stranded regions on unintegrated avian retrovirus DNA. J Virol 44:47-53.
    • (1982) J Virol , vol.44 , pp. 47-53
    • Hsu, T.W.1    Taylor, J.M.2
  • 27
    • 0029054119 scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes containing discontinuous plus strands are competent to integrate in vitro
    • Miller MD, Wang B, Bushman FD. 1995. Human immunodeficiency virus type 1 preintegration complexes containing discontinuous plus strands are competent to integrate in vitro. J Virol 69:3938-3944.
    • (1995) J Virol , vol.69 , pp. 3938-3944
    • Miller, M.D.1    Wang, B.2    Bushman, F.D.3
  • 28
    • 0030729201 scopus 로고    scopus 로고
    • Discontinuous plus-strand DNA synthesis in human immunodeficiency virus type 1-infected cells and in a partially reconstituted cell-free system
    • Klarmann GJ, Yu H, Chen X, Dougherty JP, Preston BD. 1997. Discontinuous plus-strand DNA synthesis in human immunodeficiency virus type 1-infected cells and in a partially reconstituted cell-free system. J Virol 71:9259-9269.
    • (1997) J Virol , vol.71 , pp. 9259-9269
    • Klarmann, G.J.1    Yu, H.2    Chen, X.3    Dougherty, J.P.4    Preston, B.D.5
  • 29
    • 34247170928 scopus 로고    scopus 로고
    • Efficiency of human immunodeficiency virus type 1 postentry infection processes: evidence against disproportionate numbers of defective virions
    • Thomas JA, Ott DE, Gorelick RJ. 2007. Efficiency of human immunodeficiency virus type 1 postentry infection processes: evidence against disproportionate numbers of defective virions. J Virol 81:4367-4370.
    • (2007) J Virol , vol.81 , pp. 4367-4370
    • Thomas, J.A.1    Ott, D.E.2    Gorelick, R.J.3
  • 30
    • 85047689363 scopus 로고    scopus 로고
    • Nuclear import of APOBEC3F-labeled HIV-1 preintegration complexes
    • Burdick RC, Hu WS, Pathak VK. 2013. Nuclear import of APOBEC3F-labeled HIV-1 preintegration complexes. Proc Natl Acad Sci U S A 110:E4780-4789.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E4780-4789
    • Burdick, R.C.1    Hu, W.S.2    Pathak, V.K.3
  • 31
    • 1542317624 scopus 로고    scopus 로고
    • Assessment of the role of the central DNA flap in human immunodeficiency virus type 1 replication by using a single-cycle replication system
    • Ao Z, Yao X, Cohen EA. 2004. Assessment of the role of the central DNA flap in human immunodeficiency virus type 1 replication by using a single-cycle replication system. J Virol 78:3170-3177.
    • (2004) J Virol , vol.78 , pp. 3170-3177
    • Ao, Z.1    Yao, X.2    Cohen, E.A.3
  • 32
    • 0037384693 scopus 로고    scopus 로고
    • Impact of the central polypurine tract on the kinetics of human immunodeficiency virus type 1 vector transduction
    • Van Maele B, De Rijck J, De Clercq E, Debyser Z. 2003. Impact of the central polypurine tract on the kinetics of human immunodeficiency virus type 1 vector transduction. J Virol 77:4685-4694.
    • (2003) J Virol , vol.77 , pp. 4685-4694
    • Van Maele, B.1    De Rijck, J.2    De Clercq, E.3    Debyser, Z.4
  • 33
    • 78049501117 scopus 로고    scopus 로고
    • The HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F
    • Hu C, Saenz DT, Fadel HJ, Walker W, Peretz M, Poeschla EM. 2010. The HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F. J Virol 84:11981-11993.
    • (2010) J Virol , vol.84 , pp. 11981-11993
    • Hu, C.1    Saenz, D.T.2    Fadel, H.J.3    Walker, W.4    Peretz, M.5    Poeschla, E.M.6
  • 34
    • 33645221639 scopus 로고    scopus 로고
    • Functional central polypurine tract provides downstream protection of the human immunodeficiency virus type 1 genome from editing by APOBEC3G and APOBEC3B
    • Wurtzer S, Goubard A, Mammano F, Saragosti S, Lecossier D, Hance AJ, Clavel F. 2006. Functional central polypurine tract provides downstream protection of the human immunodeficiency virus type 1 genome from editing by APOBEC3G and APOBEC3B. J Virol 80:3679-3683.
    • (2006) J Virol , vol.80 , pp. 3679-3683
    • Wurtzer, S.1    Goubard, A.2    Mammano, F.3    Saragosti, S.4    Lecossier, D.5    Hance, A.J.6    Clavel, F.7
  • 35
    • 0025185912 scopus 로고
    • Sequence of the circle junction of human immunodeficiency virus type 1: implications for reverse transcription and integration
    • Whitcomb JM, Kumar R, Hughes SH. 1990. Sequence of the circle junction of human immunodeficiency virus type 1: implications for reverse transcription and integration. J Virol 64:4903-4906.
    • (1990) J Virol , vol.64 , pp. 4903-4906
    • Whitcomb, J.M.1    Kumar, R.2    Hughes, S.H.3
  • 36
    • 0026528963 scopus 로고
    • Incomplete removal of the RNA primer for minus-strand DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase
    • Pullen KA, Ishimoto LK, Champoux JJ. 1992. Incomplete removal of the RNA primer for minus-strand DNA synthesis by human immunodeficiency virus type 1 reverse transcriptase. J Virol 66:367-373.
    • (1992) J Virol , vol.66 , pp. 367-373
    • Pullen, K.A.1    Ishimoto, L.K.2    Champoux, J.J.3
  • 37
    • 0026633994 scopus 로고
    • Specificity of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H in removal of the minus-strand primer, tRNA(Lys3)
    • Smith JS, Roth MJ. 1992. Specificity of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H in removal of the minus-strand primer, tRNA(Lys3). J Biol Chem 267:15071-15079.
    • (1992) J Biol Chem , vol.267 , pp. 15071-15079
    • Smith, J.S.1    Roth, M.J.2
  • 38
    • 0027414932 scopus 로고
    • The sequence features important for plus strand priming by human immunodeficiency virus type 1 reverse transcriptase
    • Pullen KA, Rattray AJ, Champoux JJ. 1993. The sequence features important for plus strand priming by human immunodeficiency virus type 1 reverse transcriptase. J Biol Chem 268:6221-6227.
    • (1993) J Biol Chem , vol.268 , pp. 6221-6227
    • Pullen, K.A.1    Rattray, A.J.2    Champoux, J.J.3
  • 39
    • 0037047073 scopus 로고    scopus 로고
    • Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo
    • Julias JG, McWilliams MJ, Sarafianos SG, Arnold E, Hughes SH. 2002. Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo. Proc Natl Acad Sci U S A 99:9515-9520.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9515-9520
    • Julias, J.G.1    McWilliams, M.J.2    Sarafianos, S.G.3    Arnold, E.4    Hughes, S.H.5
  • 40
    • 0037117744 scopus 로고    scopus 로고
    • Altering the RNaseHprimer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity
    • Rausch JW, Lener D, Miller JT, Julias JG, Hughes SH, Le Grice SF. 2002. Altering the RNaseHprimer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity. Biochemistry 41:4856-4865.
    • (2002) Biochemistry , vol.41 , pp. 4856-4865
    • Rausch, J.W.1    Lener, D.2    Miller, J.T.3    Julias, J.G.4    Hughes, S.H.5    Le Grice, S.F.6
  • 41
    • 2542572539 scopus 로고    scopus 로고
    • Using pyrrolo-deoxycytosine to probe RNA/DNA hybrids containing the human immunodeficiency virus type-1 3' polypurine tract
    • Dash C, Rausch JW, Le Grice SF. 2004. Using pyrrolo-deoxycytosine to probe RNA/DNA hybrids containing the human immunodeficiency virus type-1 3' polypurine tract. Nucleic Acids Res 32:1539-1547.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1539-1547
    • Dash, C.1    Rausch, J.W.2    Le Grice, S.F.3
  • 42
    • 21244468276 scopus 로고    scopus 로고
    • Investigating HIV-1 polypurine tract geometry via targeted insertion of abasic lesions in the (-)-DNA template and (+)-RNA primer
    • Yi-Brunozzi HY, Le Grice SF. 2005. Investigating HIV-1 polypurine tract geometry via targeted insertion of abasic lesions in the (-)-DNA template and (+)-RNA primer. J Biol Chem 280:20154-20162.
    • (2005) J Biol Chem , vol.280 , pp. 20154-20162
    • Yi-Brunozzi, H.Y.1    Le Grice, S.F.2
  • 43
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • Coffin JM, Hughes SH, Varmus HE (ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Swanstrom R, Willis JW. 1997. Synthesis, assembly, and processing of viral proteins, p. 263-334. In Coffin JM, Hughes SH, Varmus HE (ed), Retroviruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Willis, J.W.2
  • 44
    • 0033023880 scopus 로고    scopus 로고
    • Foamy viruses are unconventional retroviruses
    • Linial ML. 1999. Foamy viruses are unconventional retroviruses. J Virol 73:1747-1755.
    • (1999) J Virol , vol.73 , pp. 1747-1755
    • Linial, M.L.1
  • 45
    • 0029869049 scopus 로고    scopus 로고
    • Human foamy virus replication: a pathway distinct from that of retroviruses and hepadnaviruses
    • Yu SF, Baldwin DN, Gwynn SR, Yendapalli S, Linial ML. 1996. Human foamy virus replication: a pathway distinct from that of retroviruses and hepadnaviruses. Science 271:1579-1582.
    • (1996) Science , vol.271 , pp. 1579-1582
    • Yu, S.F.1    Baldwin, D.N.2    Gwynn, S.R.3    Yendapalli, S.4    Linial, M.L.5
  • 46
    • 0022413345 scopus 로고
    • Purification and characterization of murine retroviral reverse transcriptase expressed in Escherichia coli
    • Roth MJ, Tanese N, GoffSP. 1985. Purification and characterization of murine retroviral reverse transcriptase expressed in Escherichia coli. J Biol Chem 260:9326-9335.
    • (1985) J Biol Chem , vol.260 , pp. 9326-9335
    • Roth, M.J.1    Tanese, N.2    Goff, S.P.3
  • 47
    • 2642526847 scopus 로고    scopus 로고
    • Characterization of the polymerase and RNase H activities of human foamy virus reverse transcriptase
    • Boyer PL, Stenbak CR, Clark PK, Linial ML, Hughes SH. 2004. Characterization of the polymerase and RNase H activities of human foamy virus reverse transcriptase. J Virol 78:6112-6121.
    • (2004) J Virol , vol.78 , pp. 6112-6121
    • Boyer, P.L.1    Stenbak, C.R.2    Clark, P.K.3    Linial, M.L.4    Hughes, S.H.5
  • 49
    • 0020072467 scopus 로고
    • DNA-processing activities associated with the purified α, β2, and αβ molecular forms of avian sarcoma virus RNA-dependent DNA polymerase
    • Hizi A, Gazit A, Guthmann D, Yaniv A. 1982. DNA-processing activities associated with the purified α, β2, and αβ molecular forms of avian sarcoma virus RNA-dependent DNA polymerase. J Virol 41:974-981.
    • (1982) J Virol , vol.41 , pp. 974-981
    • Hizi, A.1    Gazit, A.2    Guthmann, D.3    Yaniv, A.4
  • 50
    • 0017331645 scopus 로고
    • RNA-dependent DNA polymerase of avian sarcoma virus B77. II. Comparison of the catalytic properties of the α, β2, and αβ enzyme forms
    • Hizi A, Leis JP, Joklik WK. 1977. RNA-dependent DNA polymerase of avian sarcoma virus B77. II. Comparison of the catalytic properties of the α, β2, and αβ enzyme forms. J Biol Chem 252:2290-2295.
    • (1977) J Biol Chem , vol.252 , pp. 2290-2295
    • Hizi, A.1    Leis, J.P.2    Joklik, W.K.3
  • 51
    • 0017653004 scopus 로고
    • The RNA-dependent DNA polymerase of avian sarcoma virus B77. Binding of viral and nonviral ribonucleic acids to the α, β2, and αβ forms of the enzyme
    • Hizi A, Leis JP, Joklik WK. 1977. The RNA-dependent DNA polymerase of avian sarcoma virus B77. Binding of viral and nonviral ribonucleic acids to the α, β2, and αβ forms of the enzyme. J Biol Chem 252: 6878-6884.
    • (1977) J Biol Chem , vol.252 , pp. 6878-6884
    • Hizi, A.1    Leis, J.P.2    Joklik, W.K.3
  • 52
    • 0023019732 scopus 로고
    • Structural characterization of reverse transcriptase and endonuclease polypeptides of the acquired immunodeficiency syndrome retrovirus
    • Lightfoote MM, Coligan JE, Folks TM, Fauci AS, Martin MA, Venkatesan S. 1986. Structural characterization of reverse transcriptase and endonuclease polypeptides of the acquired immunodeficiency syndrome retrovirus. J Virol 60:771-775.
    • (1986) J Virol , vol.60 , pp. 771-775
    • Lightfoote, M.M.1    Coligan, J.E.2    Folks, T.M.3    Fauci, A.S.4    Martin, M.A.5    Venkatesan, S.6
  • 53
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt LA, Wang J, Friedman JM, Rice PA, Steitz TA. 1992. Crystal structure at 3.5 Å 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    Steitz, T.A.5
  • 55
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch O, Sauvaget I, Delarue M, Tordo N. 1989. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J 8:3867-3874.
    • (1989) EMBO J , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 56
    • 0034917751 scopus 로고    scopus 로고
    • Phylogenetic analysis of ribonuclease H domains suggests a late, chimeric origin of LTR retrotransposable elements and retroviruses
    • Malik HS, Eickbush TH. 2001. Phylogenetic analysis of ribonuclease H domains suggests a late, chimeric origin of LTR retrotransposable elements and retroviruses. Genome Res 11:1187-1197.
    • (2001) Genome Res , vol.11 , pp. 1187-1197
    • Malik, H.S.1    Eickbush, T.H.2
  • 57
    • 0031748805 scopus 로고    scopus 로고
    • Replication defect of moloney murine leukemia virus with a mutant reverse transcriptase that can incorporate ribonucleotides and deoxyribonucleotides
    • Gao G, GoffSP. 1998. Replication defect of moloney murine leukemia virus with a mutant reverse transcriptase that can incorporate ribonucleotides and deoxyribonucleotides. J Virol 72:5905-5911.
    • (1998) J Virol , vol.72 , pp. 5905-5911
    • Gao, G.1    Goff, S.P.2
  • 58
    • 0034724175 scopus 로고    scopus 로고
    • Analysis of mutations at positions 115 and 116 in the dNTP binding site of HIV-1 reverse transcriptase
    • Boyer PL, Sarafianos SG, Arnold E, Hughes SH. 2000. Analysis of mutations at positions 115 and 116 in the dNTP binding site of HIV-1 reverse transcriptase. Proc Natl Acad Sci U S A 97:3056-3061.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3056-3061
    • Boyer, P.L.1    Sarafianos, S.G.2    Arnold, E.3    Hughes, S.H.4
  • 59
    • 0028924567 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors
    • Esnouf R, Ren J, Ross C, Jones Y, Stammers D, Stuart D. 1995. Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors. Nat Struct Biol 2:303-308.
    • (1995) Nat Struct Biol , vol.2 , pp. 303-308
    • Esnouf, R.1    Ren, J.2    Ross, C.3    Jones, Y.4    Stammers, D.5    Stuart, D.6
  • 61
    • 0030586090 scopus 로고    scopus 로고
    • Structure of unliganded HIV-1 reverse transcriptase at 2.7 Å resolution: implications of conformational changes for polymerization and inhibition mechanisms
    • Hsiou Y, Ding J, Das K, Clark AD, Jr., Hughes SH, Arnold E. 1996. Structure of unliganded HIV-1 reverse transcriptase at 2.7 Å resolution: implications of conformational changes for polymerization and inhibition mechanisms. Structure 4:853-860.
    • (1996) Structure , vol.4 , pp. 853-860
    • Hsiou, Y.1    Ding, J.2    Das, K.3    Clark, A.D.4    Hughes, S.H.5    Arnold, E.6
  • 64
    • 84873570106 scopus 로고    scopus 로고
    • Complexes of HIV-1 RT, NNRTI and RNA/DNA hybrid reveal a structure compatible with RNA degradation
    • Lapkouski M, Tian L, Miller JT, Le Grice SF, Yang W. 2013. Complexes of HIV-1 RT, NNRTI and RNA/DNA hybrid reveal a structure compatible with RNA degradation. Nat Struct Mol Biol 20: 230-236.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 230-236
    • Lapkouski, M.1    Tian, L.2    Miller, J.T.3    Le Grice, S.F.4    Yang, W.5
  • 65
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance
    • Huang H, Chopra R, Verdine GL, Harrison SC. 1998. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance. Science 282:1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 69
    • 77952724079 scopus 로고    scopus 로고
    • Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design
    • Lansdon EB, Brendza KM, Hung M, Wang R, Mukund S, Jin D, Birkus G, Kutty N, Liu X. 2010. Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design. J Med Chem 53:4295-4299.
    • (2010) J Med Chem , vol.53 , pp. 4295-4299
    • Lansdon, E.B.1    Brendza, K.M.2    Hung, M.3    Wang, R.4    Mukund, S.5    Jin, D.6    Birkus, G.7    Kutty, N.8    Liu, X.9
  • 70
    • 40349091258 scopus 로고    scopus 로고
    • High-resolution structures of HIV-1 reverse transcriptase/TMC278 complexes: strategic flexibility explains potency against resistance mutations
    • Das K, Bauman JD, Clark AD, Jr., Frenkel YV, Lewi PJ, Shatkin AJ, Hughes SH, Arnold E. 2008. High-resolution structures of HIV-1 reverse transcriptase/TMC278 complexes: strategic flexibility explains potency against resistance mutations. Proc Natl Acad Sci U S A 105:1466-1471.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 1466-1471
    • Das, K.1    Bauman, J.D.2    Clark, A.D.3    Frenkel, Y.V.4    Lewi, P.J.5    Shatkin, A.J.6    Hughes, S.H.7    Arnold, E.8
  • 72
    • 0030935265 scopus 로고    scopus 로고
    • Unique features in the structure of the complex between HIV-1 reverse transcriptase and the bis(heteroaryl)piperazine (BHAP) U-90152 explain resistance mutations for this nonnucleoside inhibitor
    • Esnouf RM, Ren J, Hopkins AL, Ross CK, Jones EY, Stammers DK, Stuart DI. 1997. Unique features in the structure of the complex between HIV-1 reverse transcriptase and the bis(heteroaryl)piperazine (BHAP) U-90152 explain resistance mutations for this nonnucleoside inhibitor. Proc Natl Acad Sci U S A 94:3984-3989.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3984-3989
    • Esnouf, R.M.1    Ren, J.2    Hopkins, A.L.3    Ross, C.K.4    Jones, E.Y.5    Stammers, D.K.6    Stuart, D.I.7
  • 73
    • 0029645409 scopus 로고
    • The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design
    • Ren J, Esnouf R, Hopkins A, Ross C, Jones Y, Stammers D, Stuart D. 1995. The structure of HIV-1 reverse transcriptase complexed with 9-chloro-TIBO: lessons for inhibitor design. Structure 3:915-926.
    • (1995) Structure , vol.3 , pp. 915-926
    • Ren, J.1    Esnouf, R.2    Hopkins, A.3    Ross, C.4    Jones, Y.5    Stammers, D.6    Stuart, D.7
  • 74
    • 0034640387 scopus 로고    scopus 로고
    • Binding of the second generation non-nucleoside inhibitor S-1153 to HIV-1 reverse transcriptase involves extensive main chain hydrogen bonding
    • Ren J, Nichols C, Bird LE, Fujiwara T, Sugimoto H, Stuart DI, Stammers DK. 2000. Binding of the second generation non-nucleoside inhibitor S-1153 to HIV-1 reverse transcriptase involves extensive main chain hydrogen bonding. J Biol Chem 275:14316-14320.
    • (2000) J Biol Chem , vol.275 , pp. 14316-14320
    • Ren, J.1    Nichols, C.2    Bird, L.E.3    Fujiwara, T.4    Sugimoto, H.5    Stuart, D.I.6    Stammers, D.K.7
  • 75
    • 0033598368 scopus 로고    scopus 로고
    • Crystallographic analysis of the binding modes of thiazoloisoindolinone non-nucleoside inhibitors to HIV-1 reverse transcriptase and comparison with modeling studies
    • Ren J, Esnouf RM, Hopkins AL, Stuart DI, Stammers DK. 1999. Crystallographic analysis of the binding modes of thiazoloisoindolinone non-nucleoside inhibitors to HIV-1 reverse transcriptase and comparison with modeling studies. J Med Chem 42:3845-3851.
    • (1999) J Med Chem , vol.42 , pp. 3845-3851
    • Ren, J.1    Esnouf, R.M.2    Hopkins, A.L.3    Stuart, D.I.4    Stammers, D.K.5
  • 76
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie S, Tabor S, Long AM, Richardson CC, Ellenberger T. 1998. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature 391:251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 77
    • 0030966369 scopus 로고    scopus 로고
    • Mutations within the primer grip region of HIV-1 reverse transcriptase result in loss ofRNaseHfunction
    • PalaniappanC, WisniewskiM, Jacques PS, LeGrice SF, Fay PJ, Bambara RA. 1997. Mutations within the primer grip region of HIV-1 reverse transcriptase result in loss ofRNaseHfunction. J BiolChem272:11157-11164.
    • (1997) J BiolChem , vol.272 , pp. 11157-11164
    • Palaniappan, C.1    Wisniewski, M.2    Jacques, P.S.3    LeGrice, S.F.4    Fay, P.J.5    Bambara, R.A.6
  • 78
    • 0032478535 scopus 로고    scopus 로고
    • Effects of mutations in the polymerase domain on the polymerase, RNase H and strand transfer activities of human immunodeficiency virus type 1 reverse transcriptase
    • Gao HQ, Boyer PL, Arnold E, Hughes SH. 1998. Effects of mutations in the polymerase domain on the polymerase, RNase H and strand transfer activities of human immunodeficiency virus type 1 reverse transcriptase. J Mol Biol 277:559-572.
    • (1998) J Mol Biol , vol.277 , pp. 559-572
    • Gao, H.Q.1    Boyer, P.L.2    Arnold, E.3    Hughes, S.H.4
  • 79
    • 0030977397 scopus 로고    scopus 로고
    • Alanine-scanning mutations in the "primer grip" of p66 HIV-1 reverse transcriptase result in selective loss of RNA priming activity
    • Powell MD, Ghosh M, Jacques PS, Howard KJ, Le Grice SF, Levin JG. 1997. Alanine-scanning mutations in the "primer grip" of p66 HIV-1 reverse transcriptase result in selective loss of RNA priming activity. J Biol Chem 272:13262-13269.
    • (1997) J Biol Chem , vol.272 , pp. 13262-13269
    • Powell, M.D.1    Ghosh, M.2    Jacques, P.S.3    Howard, K.J.4    Le Grice, S.F.5    Levin, J.G.6
  • 80
    • 0037338420 scopus 로고    scopus 로고
    • The ribonucleaseHactivity of the reverse transcriptases of human immunodeficiency viruses type 1 and type 2 is modulated by residue 294 of the small subunit
    • Sevilya Z, Loya S, Adir N, Hizi A. 2003. The ribonucleaseHactivity of the reverse transcriptases of human immunodeficiency viruses type 1 and type 2 is modulated by residue 294 of the small subunit. Nucleic Acids Res 31:1481-1487.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1481-1487
    • Sevilya, Z.1    Loya, S.2    Adir, N.3    Hizi, A.4
  • 81
    • 0035979762 scopus 로고    scopus 로고
    • The ribonuclease H activity of the reverse transcriptases of human immunodeficiency viruses type 1 and type 2 is affected by the thumb subdomain of the small protein subunits
    • Sevilya Z, Loya S, Hughes SH, Hizi A. 2001. The ribonuclease H activity of the reverse transcriptases of human immunodeficiency viruses type 1 and type 2 is affected by the thumb subdomain of the small protein subunits. J Mol Biol 311:957-971.
    • (2001) J Mol Biol , vol.311 , pp. 957-971
    • Sevilya, Z.1    Loya, S.2    Hughes, S.H.3    Hizi, A.4
  • 82
    • 0030008999 scopus 로고    scopus 로고
    • Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization
    • Ghosh M, Jacques PS, Rodgers DW, Ottman M, Darlix JL, Le Grice SF. 1996. Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization. Biochemistry 35: 8553-8562.
    • (1996) Biochemistry , vol.35 , pp. 8553-8562
    • Ghosh, M.1    Jacques, P.S.2    Rodgers, D.W.3    Ottman, M.4    Darlix, J.L.5    Le Grice, S.F.6
  • 83
    • 0033538339 scopus 로고    scopus 로고
    • Residues in the aH and aI helices of the HIV-1 reverse transcriptase thumb subdomain required for the specificity of RNase H-catalyzed removal of the polypurine tract primer
    • Powell MD, Beard WA, Bebenek K, Howard KJ, Le Grice SF, Darden TA, Kunkel TA, Wilson SH, Levin JG. 1999. Residues in the aH and aI helices of the HIV-1 reverse transcriptase thumb subdomain required for the specificity of RNase H-catalyzed removal of the polypurine tract primer. J Biol Chem 274:19885-19893.
    • (1999) J Biol Chem , vol.274 , pp. 19885-19893
    • Powell, M.D.1    Beard, W.A.2    Bebenek, K.3    Howard, K.J.4    Le Grice, S.F.5    Darden, T.A.6    Kunkel, T.A.7    Wilson, S.H.8    Levin, J.G.9
  • 84
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • Yang W, Steitz TA. 1995. Recombining the structures of HIV integrase, RuvC and RNase H. Structure 3:131-134.
    • (1995) Structure , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 85
    • 21244451435 scopus 로고    scopus 로고
    • Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis
    • Nowotny M, Gaidamakov SA, Crouch RJ, Yang W. 2005. Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis. Cell 121:1005-1016.
    • (2005) Cell , vol.121 , pp. 1005-1016
    • Nowotny, M.1    Gaidamakov, S.A.2    Crouch, R.J.3    Yang, W.4
  • 86
    • 70450193040 scopus 로고    scopus 로고
    • Mutations in the thumb allow human immunodeficiency virus type 1 reverse transcriptase to be cleaved by protease in virions
    • Dunn LL, McWilliams MJ, Das K, Arnold E, Hughes SH. 2009. Mutations in the thumb allow human immunodeficiency virus type 1 reverse transcriptase to be cleaved by protease in virions. J Virol 83:12336-12344.
    • (2009) J Virol , vol.83 , pp. 12336-12344
    • Dunn, L.L.1    McWilliams, M.J.2    Das, K.3    Arnold, E.4    Hughes, S.H.5
  • 87
    • 84882833684 scopus 로고    scopus 로고
    • Mutations in HIV-1 reverse transcriptase cause misfolding and miscleavage by the viral protease
    • Dunn LL, Boyer PL, Clark PK, Hughes SH. 2013. Mutations in HIV-1 reverse transcriptase cause misfolding and miscleavage by the viral protease. Virology 444:241-249.
    • (2013) Virology , vol.444 , pp. 241-249
    • Dunn, L.L.1    Boyer, P.L.2    Clark, P.K.3    Hughes, S.H.4
  • 88
    • 0037223722 scopus 로고    scopus 로고
    • Amino acid substitutions at position 190 of human immunodeficiency virus type 1 reverse transcriptase increase susceptibility to delavirdine and impair virus replication
    • Huang W, Gamarnik A, Limoli K, Petropoulos CJ, Whitcomb JM. 2003. Amino acid substitutions at position 190 of human immunodeficiency virus type 1 reverse transcriptase increase susceptibility to delavirdine and impair virus replication. J Virol 77:1512-1523.
    • (2003) J Virol , vol.77 , pp. 1512-1523
    • Huang, W.1    Gamarnik, A.2    Limoli, K.3    Petropoulos, C.J.4    Whitcomb, J.M.5
  • 90
    • 0031912656 scopus 로고    scopus 로고
    • Construction and characterization of a temperature-sensitive human immunodeficiency virus type 1 reverse transcriptase mutant
    • Huang M, Zensen R, Cho M, Martin MA. 1998. Construction and characterization of a temperature-sensitive human immunodeficiency virus type 1 reverse transcriptase mutant. J Virol 72:2047-2054.
    • (1998) J Virol , vol.72 , pp. 2047-2054
    • Huang, M.1    Zensen, R.2    Cho, M.3    Martin, M.A.4
  • 91
    • 77956042549 scopus 로고    scopus 로고
    • Reduced fitness in cell culture of HIV-1 with nonnucleoside reverse transcriptase inhibitorresistant mutations correlates with relative levels of reverse transcriptase content and RNase H activity in virions
    • Wang J, Bambara RA, Demeter LM, Dykes C. 2010. Reduced fitness in cell culture of HIV-1 with nonnucleoside reverse transcriptase inhibitorresistant mutations correlates with relative levels of reverse transcriptase content and RNase H activity in virions. J Virol 84:9377-938
    • (2010) J Virol , vol.84 , pp. 9377-9938
    • Wang, J.1    Bambara, R.A.2    Demeter, L.M.3    Dykes, C.4
  • 92
    • 34247565931 scopus 로고    scopus 로고
    • Determination of the ex vivo rates of human immunodeficiency virus type 1 reverse transcription by using novel strand-specific amplification analysis
    • Thomas DC, Voronin YA, Nikolenko GN, Chen J, Hu WS, Pathak VK. 2007. Determination of the ex vivo rates of human immunodeficiency virus type 1 reverse transcription by using novel strand-specific amplification analysis. J Virol 81:4798-4807.
    • (2007) J Virol , vol.81 , pp. 4798-4807
    • Thomas, D.C.1    Voronin, Y.A.2    Nikolenko, G.N.3    Chen, J.4    Hu, W.S.5    Pathak, V.K.6
  • 93
    • 0035078745 scopus 로고    scopus 로고
    • Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1
    • Fassati A, GoffSP. 2001. Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1. J Virol 75:3626-3635.
    • (2001) J Virol , vol.75 , pp. 3626-3635
    • Fassati, A.1    Goff, S.P.2
  • 94
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey BM, von Schwedler U, Sundquist WI, Aiken C. 2002. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J Virol 76:5667-5677.
    • (2002) J Virol , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 95
    • 0038785584 scopus 로고    scopus 로고
    • Structural analyses of purified human immunodeficiency virus type 1 intracellular reverse transcription complexes
    • Nermut MV, Fassati A. 2003. Structural analyses of purified human immunodeficiency virus type 1 intracellular reverse transcription complexes. J Virol 77:8196-8206.
    • (2003) J Virol , vol.77 , pp. 8196-8206
    • Nermut, M.V.1    Fassati, A.2
  • 96
    • 32144445395 scopus 로고    scopus 로고
    • Intracytoplasmic maturation of the human immunodeficiency virus type 1 reverse transcription complexes determines their capacity to integrate into chromatin
    • Iordanskiy S, Berro R, Altieri M, Kashanchi F, Bukrinsky M. 2006. Intracytoplasmic maturation of the human immunodeficiency virus type 1 reverse transcription complexes determines their capacity to integrate into chromatin. Retrovirology 3:4.
    • (2006) Retrovirology , vol.3 , pp. 4
    • Iordanskiy, S.1    Berro, R.2    Altieri, M.3    Kashanchi, F.4    Bukrinsky, M.5
  • 97
    • 33645793789 scopus 로고    scopus 로고
    • Evidence for a functional link between uncoating of the human immunodeficiency virus type 1 core and nuclear import of the viral preintegration complex
    • Dismuke DJ, Aiken C. 2006. Evidence for a functional link between uncoating of the human immunodeficiency virus type 1 core and nuclear import of the viral preintegration complex. J Virol 80:3712-3720.
    • (2006) J Virol , vol.80 , pp. 3712-3720
    • Dismuke, D.J.1    Aiken, C.2
  • 98
    • 79959988674 scopus 로고    scopus 로고
    • Complementary assays reveal a relationship between HIV-1 uncoating and reverse transcription
    • Hulme AE, Perez O, Hope TJ. 2011. Complementary assays reveal a relationship between HIV-1 uncoating and reverse transcription. Proc Natl Acad Sci U S A 108:9975-9980.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9975-9980
    • Hulme, A.E.1    Perez, O.2    Hope, T.J.3
  • 99
    • 0019949367 scopus 로고
    • Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate
    • Summers J, Mason WS. 1982. Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate. Cell 29:403-415.
    • (1982) Cell , vol.29 , pp. 403-415
    • Summers, J.1    Mason, W.S.2
  • 100
    • 0032932713 scopus 로고    scopus 로고
    • Evidence that the human foamy virus genome is DNA
    • Yu SF, Sullivan MD, Linial ML. 1999. Evidence that the human foamy virus genome is DNA. J Virol 73:1565-1572.
    • (1999) J Virol , vol.73 , pp. 1565-1572
    • Yu, S.F.1    Sullivan, M.D.2    Linial, M.L.3
  • 103
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S, Hill CP, Sundquist WI, Finch JT. 2000. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407:409-413.
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 104
    • 0034855639 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells
    • Tang S, Murakami T, Agresta BE, Campbell S, Freed EO, Levin JG. 2001. Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells. J Virol 75:9357-9366.
    • (2001) J Virol , vol.75 , pp. 9357-9366
    • Tang, S.1    Murakami, T.2    Agresta, B.E.3    Campbell, S.4    Freed, E.O.5    Levin, J.G.6
  • 106
  • 107
    • 0040896601 scopus 로고
    • Retroviral integration: structure of the initial covalent product and its precursor, and a role for the viral IN protein
    • Brown PO, Bowerman B, Varmus HE, Bishop JM. 1989. Retroviral integration: structure of the initial covalent product and its precursor, and a role for the viral IN protein. Proc Natl Acad Sci U S A 86:2525-2529.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 2525-2529
    • Brown, P.O.1    Bowerman, B.2    Varmus, H.E.3    Bishop, J.M.4
  • 108
    • 0021033226 scopus 로고
    • Discontinuities in the DNA synthesized by an avian retrovirus
    • Taylor JM, Cywinski A, Smith JK. 1983. Discontinuities in the DNA synthesized by an avian retrovirus. J Virol 48:654-659.
    • (1983) J Virol , vol.48 , pp. 654-659
    • Taylor, J.M.1    Cywinski, A.2    Smith, J.K.3
  • 109
    • 0030053661 scopus 로고    scopus 로고
    • The human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein
    • Lochelt M, Flugel RM. 1996. The human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein. J Virol 70:1033-1040.
    • (1996) J Virol , vol.70 , pp. 1033-1040
    • Lochelt, M.1    Flugel, R.M.2
  • 110
    • 0028839595 scopus 로고
    • Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein
    • Konvalinka J, Lochelt M, Zentgraf H, Flugel RM, Krausslich HG. 1995. Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein. J Virol 69:7264-7268.
    • (1995) J Virol , vol.69 , pp. 7264-7268
    • Konvalinka, J.1    Lochelt, M.2    Zentgraf, H.3    Flugel, R.M.4    Krausslich, H.G.5
  • 112
    • 0036314441 scopus 로고    scopus 로고
    • Zinc finger domain of murine leukemia virus nucleocapsid protein enhances the rate of viral DNA synthesis in vivo
    • Zhang WH, Hwang CK, Hu WS, Gorelick RJ, Pathak VK. 2002. Zinc finger domain of murine leukemia virus nucleocapsid protein enhances the rate of viral DNA synthesis in vivo. J Virol 76:7473-7484.
    • (2002) J Virol , vol.76 , pp. 7473-7484
    • Zhang, W.H.1    Hwang, C.K.2    Hu, W.S.3    Gorelick, R.J.4    Pathak, V.K.5
  • 113
    • 0033799017 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid protein can prevent self-priming of minus-strand strong stop DNA by promoting the annealing of short oligonucleotides to hairpin sequences
    • Driscoll MD, Hughes SH. 2000. Human immunodeficiency virus type 1 nucleocapsid protein can prevent self-priming of minus-strand strong stop DNA by promoting the annealing of short oligonucleotides to hairpin sequences. J Virol 74:8785-8792.
    • (2000) J Virol , vol.74 , pp. 8785-8792
    • Driscoll, M.D.1    Hughes, S.H.2
  • 114
    • 0037223701 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid Zn2+ fingers are required for efficient reverse transcription, initial integration processes, and protection of newly synthesized viral DNA
    • Buckman JS, Bosche WJ, Gorelick RJ. 2003. Human immunodeficiency virus type 1 nucleocapsid Zn2+ fingers are required for efficient reverse transcription, initial integration processes, and protection of newly synthesized viral DNA. J Virol 77:1469-1480.
    • (2003) J Virol , vol.77 , pp. 1469-1480
    • Buckman, J.S.1    Bosche, W.J.2    Gorelick, R.J.3
  • 115
    • 33747875746 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid zinc-finger mutations cause defects in reverse transcription and integration
    • Thomas JA, Gagliardi TD, Alvord WG, Lubomirski M, Bosche WJ, Gorelick RJ. 2006. Human immunodeficiency virus type 1 nucleocapsid zinc-finger mutations cause defects in reverse transcription and integration. Virology 353:41-51.
    • (2006) Virology , vol.353 , pp. 41-51
    • Thomas, J.A.1    Gagliardi, T.D.2    Alvord, W.G.3    Lubomirski, M.4    Bosche, W.J.5    Gorelick, R.J.6
  • 116
    • 52649129852 scopus 로고    scopus 로고
    • Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription
    • Thomas JA, Bosche WJ, Shatzer TL, Johnson DG, Gorelick RJ. 2008. Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription. J Virol 82: 9318-9328.
    • (2008) J Virol , vol.82 , pp. 9318-9328
    • Thomas, J.A.1    Bosche, W.J.2    Shatzer, T.L.3    Johnson, D.G.4    Gorelick, R.J.5
  • 117
    • 43049089699 scopus 로고    scopus 로고
    • Nucleocapsid protein function in early infection processes
    • Thomas JA, Gorelick RJ. 2008. Nucleocapsid protein function in early infection processes. Virus Res 134:39-63.
    • (2008) Virus Res , vol.134 , pp. 39-63
    • Thomas, J.A.1    Gorelick, R.J.2
  • 118
    • 0033803461 scopus 로고    scopus 로고
    • Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minusand plus-strand transfer
    • Guo J, Wu T, Anderson J, Kane BF, Johnson DG, Gorelick RJ, Henderson LE, Levin JG. 2000. Zinc finger structures in the human immunodeficiency virus type 1 nucleocapsid protein facilitate efficient minusand plus-strand transfer. J Virol 74:8980-8988.
    • (2000) J Virol , vol.74 , pp. 8980-8988
    • Guo, J.1    Wu, T.2    Anderson, J.3    Kane, B.F.4    Johnson, D.G.5    Gorelick, R.J.6    Henderson, L.E.7    Levin, J.G.8
  • 119
    • 0028915128 scopus 로고
    • Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication
    • Engelman A, Englund G, Orenstein JM, Martin MA, Craigie R. 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
  • 120
    • 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, Planelles V, Krogstad P, Chen IS. 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
  • 121
    • 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 AD, Robles G, Alesandro N, Varmus HE. 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
  • 122
    • 0033019033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 integrase protein promotes reverse transcription through specific interactions with the nucleoprotein reverse transcription complex
    • Wu X, Liu H, Xiao H, Conway JA, Hehl E, Kalpana GV, Prasad V, Kappes JC. 1999. Human immunodeficiency virus type 1 integrase protein promotes reverse transcription through specific interactions with the nucleoprotein reverse transcription complex. J Virol 73:2126-2135.
    • (1999) J Virol , vol.73 , pp. 2126-2135
    • Wu, X.1    Liu, H.2    Xiao, H.3    Conway, J.A.4    Hehl, E.5    Kalpana, G.V.6    Prasad, V.7    Kappes, J.C.8
  • 123
    • 0029938476 scopus 로고    scopus 로고
    • Ty3 integrase mutants defective in reverse transcription or 3'-end processing of extrachromosomal Ty3 DNA
    • Kirchner J, Sandmeyer SB. 1996. Ty3 integrase mutants defective in reverse transcription or 3'-end processing of extrachromosomal Ty3 DNA. J Virol 70:4737-4747.
    • (1996) J Virol , vol.70 , pp. 4737-4747
    • Kirchner, J.1    Sandmeyer, S.B.2
  • 125
    • 0032888949 scopus 로고    scopus 로고
    • Mutations in nonconserved domains of Ty3 integrase affect multiple stages of the Ty3 life cycle
    • Nymark-McMahon MH, Sandmeyer SB. 1999. Mutations in nonconserved domains of Ty3 integrase affect multiple stages of the Ty3 life cycle. J Virol 73:453-465.
    • (1999) J Virol , vol.73 , pp. 453-465
    • Nymark-McMahon, M.H.1    Sandmeyer, S.B.2
  • 126
    • 0030957531 scopus 로고    scopus 로고
    • Tat is required for efficient HIV-1 reverse transcription
    • Harrich D, Ulich C, Garcia-Martinez LF, Gaynor RB. 1997. Tat is required for efficient HIV-1 reverse transcription. EMBO J 16:1224-1235.
    • (1997) EMBO J , vol.16 , pp. 1224-1235
    • Harrich, D.1    Ulich, C.2    Garcia-Martinez, L.F.3    Gaynor, R.B.4
  • 127
    • 0036200154 scopus 로고    scopus 로고
    • The Tat protein of human immunodeficiency virus type 1 (HIV-1) can promote placement of tRNA primer onto viral RNA and suppress later DNA polymerization in HIV-1 reverse transcription
    • Kameoka M, Morgan M, Binette M, Russell RS, Rong L, Guo X, Mouland A, Kleiman L, Liang C, Wainberg MA. 2002. The Tat protein of human immunodeficiency virus type 1 (HIV-1) can promote placement of tRNA primer onto viral RNA and suppress later DNA polymerization in HIV-1 reverse transcription. J Virol 76:3637-3645.
    • (2002) J Virol , vol.76 , pp. 3637-3645
    • Kameoka, M.1    Morgan, M.2    Binette, M.3    Russell, R.S.4    Rong, L.5    Guo, X.6    Mouland, A.7    Kleiman, L.8    Liang, C.9    Wainberg, M.A.10
  • 128
    • 0036233757 scopus 로고    scopus 로고
    • The role of Tat in HIV-1 replication: an activator and/or a suppressor?
    • Liang C, Wainberg MA. 2002. The role of Tat in HIV-1 replication: an activator and/or a suppressor? AIDS Rev 4:41-49.
    • (2002) AIDS Rev , vol.4 , pp. 41-49
    • Liang, C.1    Wainberg, M.A.2
  • 130
    • 34548585250 scopus 로고    scopus 로고
    • Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription
    • Henriet S, Sinck L, Bec G, Gorelick RJ, Marquet R, Paillart JC. 2007. Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription. Nucleic Acids Res 35:5141-5153.
    • (2007) Nucleic Acids Res , vol.35 , pp. 5141-5153
    • Henriet, S.1    Sinck, L.2    Bec, G.3    Gorelick, R.J.4    Marquet, R.5    Paillart, J.C.6
  • 131
    • 38949093228 scopus 로고    scopus 로고
    • Human immunodeficiency virus 1 (HIV-1) virion infectivity factor (Vif) is part of reverse transcription complexes and acts as an accessory factor for reverse transcription
    • Carr JM, Coolen C, Davis AJ, Burrell CJ, Li P. 2008. Human immunodeficiency virus 1 (HIV-1) virion infectivity factor (Vif) is part of reverse transcription complexes and acts as an accessory factor for reverse transcription. Virology 372:147-156.
    • (2008) Virology , vol.372 , pp. 147-156
    • Carr, J.M.1    Coolen, C.2    Davis, A.J.3    Burrell, C.J.4    Li, P.5
  • 133
    • 0027420358 scopus 로고
    • Molecular cloning and characterization of deoxyuridine triphosphatase from feline immunodeficiency virus (FIV)
    • Wagaman PC, Hasselkus-Light CS, Henson M, Lerner DL, Phillips TR, Elder JH. 1993. Molecular cloning and characterization of deoxyuridine triphosphatase from feline immunodeficiency virus (FIV). Virology 196:451-457.
    • (1993) Virology , vol.196 , pp. 451-457
    • Wagaman, P.C.1    Hasselkus-Light, C.S.2    Henson, M.3    Lerner, D.L.4    Phillips, T.R.5    Elder, J.H.6
  • 135
    • 0030958826 scopus 로고    scopus 로고
    • Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest
    • Selig L, Benichou S, Rogel ME, Wu LI, Vodicka MA, Sire J, Benarous R, Emerman M. 1997. Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest. J Virol 71:4842-4846.
    • (1997) J Virol , vol.71 , pp. 4842-4846
    • Selig, L.1    Benichou, S.2    Rogel, M.E.3    Wu, L.I.4    Vodicka, M.A.5    Sire, J.6    Benarous, R.7    Emerman, M.8
  • 136
    • 0033925801 scopus 로고    scopus 로고
    • The interaction of vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 In vivo mutation rate
    • Mansky LM, Preveral S, Selig L, Benarous R, Benichou S. 2000. The interaction of vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 In vivo mutation rate. J Virol 74:7039-7047.
    • (2000) J Virol , vol.74 , pp. 7039-7047
    • Mansky, L.M.1    Preveral, S.2    Selig, L.3    Benarous, R.4    Benichou, S.5
  • 137
    • 3142651460 scopus 로고    scopus 로고
    • Vpr-mediated incorporation of UNG2 into HIV-1 particles is required to modulate the virus mutation rate and for replication in macrophages
    • Chen R, Le Rouzic E, Kearney JA, Mansky LM, Benichou S. 2004. Vpr-mediated incorporation of UNG2 into HIV-1 particles is required to modulate the virus mutation rate and for replication in macrophages. J Biol Chem 279:28419-28425.
    • (2004) J Biol Chem , vol.279 , pp. 28419-28425
    • Chen, R.1    Le Rouzic, E.2    Kearney, J.A.3    Mansky, L.M.4    Benichou, S.5
  • 138
    • 23844471513 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases
    • Schrofelbauer B, Yu Q, Zeitlin SG, Landau NR. 2005. Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. J Virol 79:10978-10987.
    • (2005) J Virol , vol.79 , pp. 10978-10987
    • Schrofelbauer, B.1    Yu, Q.2    Zeitlin, S.G.3    Landau, N.R.4
  • 140
    • 0037123436 scopus 로고    scopus 로고
    • Correlation between tRNALys3 aminoacylation and its incorporation into HIV-1
    • Javanbakht H, Cen S, Musier-Forsyth K, Kleiman L. 2002. Correlation between tRNALys3 aminoacylation and its incorporation into HIV-1. J Biol Chem 277:17389-17396.
    • (2002) J Biol Chem , vol.277 , pp. 17389-17396
    • Javanbakht, H.1    Cen, S.2    Musier-Forsyth, K.3    Kleiman, L.4
  • 141
    • 34548556416 scopus 로고    scopus 로고
    • Forced selection of tRNA (Glu) reveals the importance of two adenosine-rich RNA loops within the U5-PBS for SIV(smmPBj) replication
    • Kelly MC, KosloffBR, Morrow CD. 2007. Forced selection of tRNA (Glu) reveals the importance of two adenosine-rich RNA loops within the U5-PBS for SIV(smmPBj) replication. Virology 366:330-339.
    • (2007) Virology , vol.366 , pp. 330-339
    • Kelly, M.C.1    Kosloff, B.R.2    Morrow, C.D.3
  • 142
    • 33847196756 scopus 로고    scopus 로고
    • Analysis of the replication of HIV-1 forced to use tRNAMet(i) supports a link between primer selection, translation and encapsidation
    • Djekic UV, Morrow CD. 2007. Analysis of the replication of HIV-1 forced to use tRNAMet(i) supports a link between primer selection, translation and encapsidation. Retrovirology 4:10.
    • (2007) Retrovirology , vol.4 , pp. 10
    • Djekic, U.V.1    Morrow, C.D.2
  • 143
    • 33749531066 scopus 로고    scopus 로고
    • HIV-1 designed to use different tRNAGln isoacceptors prefers to select tRNAThr for replication
    • Li M, Eipers PG, Ni N, Morrow CD. 2006. HIV-1 designed to use different tRNAGln isoacceptors prefers to select tRNAThr for replication. Virol J 3:80.
    • (2006) Virol J , vol.3 , pp. 80
    • Li, M.1    Eipers, P.G.2    Ni, N.3    Morrow, C.D.4
  • 144
  • 146
    • 0024602652 scopus 로고
    • Genetic analysis of endogenous xenotropic murine leukemia viruses: association with two common mouse mutations and the viral restriction locus Fv-1
    • Frankel WN, Stoye JP, Taylor BA, Coffin JM. 1989. Genetic analysis of endogenous xenotropic murine leukemia viruses: association with two common mouse mutations and the viral restriction locus Fv-1. J Virol 63: 1763-1774.
    • (1989) J Virol , vol.63 , pp. 1763-1774
    • Frankel, W.N.1    Stoye, J.P.2    Taylor, B.A.3    Coffin, J.M.4
  • 147
    • 0029763293 scopus 로고    scopus 로고
    • Positional cloning of the mouse retrovirus restriction gene Fv1
    • Best S, Le Tissier P, Towers G, Stoye JP. 1996. Positional cloning of the mouse retrovirus restriction gene Fv1. Nature 382:826-829.
    • (1996) Nature , vol.382 , pp. 826-829
    • Best, S.1    Le Tissier, P.2    Towers, G.3    Stoye, J.P.4
  • 148
    • 4444241947 scopus 로고    scopus 로고
    • A Trim5-cyclophilin A fusion protein found in owl monkey kidney cells can restrict HIV-1
    • Nisole S, Lynch C, Stoye JP, Yap MW. 2004. A Trim5-cyclophilin A fusion protein found in owl monkey kidney cells can restrict HIV-1. Proc Natl Acad Sci U S A 101:13324-13328.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13324-13328
    • Nisole, S.1    Lynch, C.2    Stoye, J.P.3    Yap, M.W.4
  • 149
    • 3242876747 scopus 로고    scopus 로고
    • Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1
    • Sayah DM, Sokolskaja E, Berthoux L, Luban J. 2004. Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1. Nature 430:569-573.
    • (2004) Nature , vol.430 , pp. 569-573
    • Sayah, D.M.1    Sokolskaja, E.2    Berthoux, L.3    Luban, J.4
  • 150
  • 152
    • 33646595636 scopus 로고    scopus 로고
    • Proteasome inhibitors uncouple rhesus TRIM5a restriction of HIV-1 reverse transcription and infection
    • Wu X, Anderson JL, Campbell EM, Joseph AM, Hope TJ. 2006. Proteasome inhibitors uncouple rhesus TRIM5a restriction of HIV-1 reverse transcription and infection. Proc Natl Acad Sci U S A 103:7465-7470.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7465-7470
    • Wu, X.1    Anderson, J.L.2    Campbell, E.M.3    Joseph, A.M.4    Hope, T.J.5
  • 153
    • 69249214157 scopus 로고    scopus 로고
    • Analysis of human immunodeficiency virus type 1 viremia and provirus in resting CD4+ T cells reveals a novel source of residual viremia in patients on antiretroviral therapy
    • Brennan TP, Woods JO, Sedaghat AR, Siliciano JD, Siliciano RF, Wilke CO. 2009. Analysis of human immunodeficiency virus type 1 viremia and provirus in resting CD4+ T cells reveals a novel source of residual viremia in patients on antiretroviral therapy. J Virol 83:8470-8481.
    • (2009) J Virol , vol.83 , pp. 8470-8481
    • Brennan, T.P.1    Woods, J.O.2    Sedaghat, A.R.3    Siliciano, J.D.4    Siliciano, R.F.5    Wilke, C.O.6
  • 155
  • 157
    • 84859482628 scopus 로고    scopus 로고
    • HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1
    • Ahn J, Hao C, Yan J, DeLucia M, Mehrens J, Wang C, Gronenborn AM, Skowronski J. 2012. HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1. J Biol Chem 287:12550-12558.
    • (2012) J Biol Chem , vol.287 , pp. 12550-12558
    • Ahn, J.1    Hao, C.2    Yan, J.3    DeLucia, M.4    Mehrens, J.5    Wang, C.6    Gronenborn, A.M.7    Skowronski, J.8
  • 159
    • 79959933961 scopus 로고    scopus 로고
    • SAMHD1: a new insight into HIV-1 restriction in myeloid cells
    • St Gelais C, Wu L. 2011. SAMHD1: a new insight into HIV-1 restriction in myeloid cells. Retrovirology 8:55.
    • (2011) Retrovirology , vol.8 , pp. 55
    • St Gelais, C.1    Wu, L.2
  • 160
    • 84871412468 scopus 로고    scopus 로고
    • SAMHD1 restricts HIV-1 infection in dendritic cells (DCs) by dNTP depletion, but its expression in DCs and primary CD4+ T-lymphocytes cannot be upregulated by interferons
    • St Gelais C, de Silva S, Amie SM, Coleman CM, Hoy H, Hollenbaugh JA, Kim B, Wu L. 2012. SAMHD1 restricts HIV-1 infection in dendritic cells (DCs) by dNTP depletion, but its expression in DCs and primary CD4+ T-lymphocytes cannot be upregulated by interferons. Retrovirology 9:105.
    • (2012) Retrovirology , vol.9 , pp. 105
    • St Gelais, C.1    de Silva, S.2    Amie, S.M.3    Coleman, C.M.4    Hoy, H.5    Hollenbaugh, J.A.6    Kim, B.7    Wu, L.8
  • 167
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng YH, Irwin D, Kurosu T, Tokunaga K, Sata T, Peterlin BM. 2004. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J Virol 78:6073-6076.
    • (2004) J Virol , vol.78 , pp. 6073-6076
    • Zheng, Y.H.1    Irwin, D.2    Kurosu, T.3    Tokunaga, K.4    Sata, T.5    Peterlin, B.M.6
  • 169
    • 0038825009 scopus 로고    scopus 로고
    • DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses
    • Harris RS, SheehyAM, CraigHM, MalimMH, Neuberger MS. 2003. DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses. Nat Immunol 4:641-643.
    • (2003) Nat Immunol , vol.4 , pp. 641-643
    • Harris, R.S.1    Sheehy, A.M.2    Craig, H.M.3    Malim, M.H.4    Neuberger, M.S.5
  • 170
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D. 2003. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424:99-103.
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 171
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • Bishop KN, Holmes RK, Malim MH. 2006. Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J Virol 80:8450-8458.
    • (2006) J Virol , vol.80 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 173
    • 33847636341 scopus 로고    scopus 로고
    • APOBEC-mediated viral restriction: not simply editing?
    • Holmes RK, Malim MH, Bishop KN. 2007. APOBEC-mediated viral restriction: not simply editing? Trends Biochem Sci 32:118-128.
    • (2007) Trends Biochem Sci , vol.32 , pp. 118-128
    • Holmes, R.K.1    Malim, M.H.2    Bishop, K.N.3
  • 176
    • 0028952146 scopus 로고
    • HIV population dynamics in vivo: implications for genetic variation, pathogenesis, and therapy
    • Coffin JM. 1995. HIV population dynamics in vivo: implications for genetic variation, pathogenesis, and therapy. Science 267:483-489.
    • (1995) Science , vol.267 , pp. 483-489
    • Coffin, J.M.1
  • 177
    • 0033165851 scopus 로고    scopus 로고
    • A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase
    • Meyer PR, Matsuura SE, Mian AM, So AG, Scott WA. 1999. A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase. Mol Cell 4:35-43.
    • (1999) Mol Cell , vol.4 , pp. 35-43
    • Meyer, P.R.1    Matsuura, S.E.2    Mian, A.M.3    So, A.G.4    Scott, W.A.5
  • 178
    • 0035031936 scopus 로고    scopus 로고
    • Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase
    • Boyer PL, Sarafianos SG, Arnold E, Hughes SH. 2001. Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase. J Virol 75:4832-4842.
    • (2001) J Virol , vol.75 , pp. 4832-4842
    • Boyer, P.L.1    Sarafianos, S.G.2    Arnold, E.3    Hughes, S.H.4
  • 179
    • 0033819409 scopus 로고    scopus 로고
    • 3'-Azido-3'-deoxythymidine (AZT) and AZT-resistant reverse transcriptase can increase the in vivo mutation rate of human immunodeficiency virus type 1
    • Mansky LM, Bernard LC. 2000. 3'-Azido-3'-deoxythymidine (AZT) and AZT-resistant reverse transcriptase can increase the in vivo mutation rate of human immunodeficiency virus type 1. J Virol 74:9532-9539.
    • (2000) J Virol , vol.74 , pp. 9532-9539
    • Mansky, L.M.1    Bernard, L.C.2
  • 180
    • 34249726498 scopus 로고    scopus 로고
    • Stimulation of RNA polymerase II transcript cleavage activity contributes to maintain transcriptional fidelity in yeast
    • Koyama H, Ito T, Nakanishi T, Sekimizu K. 2007. Stimulation of RNA polymerase II transcript cleavage activity contributes to maintain transcriptional fidelity in yeast. Genes Cells 12:547-559.
    • (2007) Genes Cells , vol.12 , pp. 547-559
    • Koyama, H.1    Ito, T.2    Nakanishi, T.3    Sekimizu, K.4
  • 181
    • 0037064085 scopus 로고    scopus 로고
    • Mutational analysis of HIV-1 long terminal repeats to explore the relative contribution of reverse transcriptase and RNA polymerase II to viral mutagenesis
    • O'Neil PK, Sun G, Yu H, Ron Y, Dougherty JP, Preston BD. 2002. Mutational analysis of HIV-1 long terminal repeats to explore the relative contribution of reverse transcriptase and RNA polymerase II to viral mutagenesis. J Biol Chem 277:38053-38061.
    • (2002) J Biol Chem , vol.277 , pp. 38053-38061
    • O'Neil, P.K.1    Sun, G.2    Yu, H.3    Ron, Y.4    Dougherty, J.P.5    Preston, B.D.6
  • 182
    • 0029075130 scopus 로고
    • Lower in vivo mutation rate of human immunodeficiency virus type 1 than that predicted from the fidelity of purified reverse transcriptase
    • Mansky LM, Temin HM. 1995. Lower in vivo mutation rate of human immunodeficiency virus type 1 than that predicted from the fidelity of purified reverse transcriptase. J Virol 69:5087-5094.
    • (1995) J Virol , vol.69 , pp. 5087-5094
    • Mansky, L.M.1    Temin, H.M.2
  • 183
    • 0030060447 scopus 로고    scopus 로고
    • Forward mutation rate of human immunodeficiency virus type 1 in a T lymphoid cell line
    • Mansky LM. 1996. Forward mutation rate of human immunodeficiency virus type 1 in a T lymphoid cell line. AIDS Res Hum Retroviruses 12:307-314.
    • (1996) AIDS Res Hum Retroviruses , vol.12 , pp. 307-314
    • Mansky, L.M.1
  • 184
    • 77956820495 scopus 로고    scopus 로고
    • The nature, position and frequency of mutations made in a single-cycle of HIV-1 replication
    • Abram ME, Ferris AL, Shao W, Alvord WG, Hughes SH. 2010. The nature, position and frequency of mutations made in a single-cycle of HIV-1 replication. J Virol 84:9864-9878.
    • (2010) J Virol , vol.84 , pp. 9864-9878
    • Abram, M.E.1    Ferris, A.L.2    Shao, W.3    Alvord, W.G.4    Hughes, S.H.5
  • 186
    • 0024273119 scopus 로고
    • The accuracy of reverse transcriptase from HIV-1
    • Roberts JD, Bebenek K, Kunkel TA. 1988. The accuracy of reverse transcriptase from HIV-1. Science 242:1171-1173.
    • (1988) Science , vol.242 , pp. 1171-1173
    • Roberts, J.D.1    Bebenek, K.2    Kunkel, T.A.3
  • 187
    • 0024438889 scopus 로고
    • Specificity and mechanism of error-prone replication by human immunodeficiency virus-1 reverse transcriptase
    • Bebenek K, Abbotts J, Roberts JD, Wilson SH, Kunkel TA. 1989. Specificity and mechanism of error-prone replication by human immunodeficiency virus-1 reverse transcriptase. J Biol Chem 264:16948-16956.
    • (1989) J Biol Chem , vol.264 , pp. 16948-16956
    • Bebenek, K.1    Abbotts, J.2    Roberts, J.D.3    Wilson, S.H.4    Kunkel, T.A.5
  • 188
    • 0031897968 scopus 로고    scopus 로고
    • The impact of multidideoxynucleoside resistance-conferring mutations in human immunodeficiency virus type 1 reverse transcriptase on polymerase fidelity and error specificity
    • Rezende LF, Curr K, Ueno T, Mitsuya H, Prasad VR. 1998. The impact of multidideoxynucleoside resistance-conferring mutations in human immunodeficiency virus type 1 reverse transcriptase on polymerase fidelity and error specificity. J Virol 72:2890-2895.
    • (1998) J Virol , vol.72 , pp. 2890-2895
    • Rezende, L.F.1    Curr, K.2    Ueno, T.3    Mitsuya, H.4    Prasad, V.R.5
  • 189
    • 0033934724 scopus 로고    scopus 로고
    • Effects of amino acid substitutions at position 115 on the fidelity of human immunodeficiency virus type 1 reverse transcriptase
    • Boyer PL, Hughes SH. 2000. Effects of amino acid substitutions at position 115 on the fidelity of human immunodeficiency virus type 1 reverse transcriptase. J Virol 74:6494-6500.
    • (2000) J Virol , vol.74 , pp. 6494-6500
    • Boyer, P.L.1    Hughes, S.H.2
  • 190
    • 0036721138 scopus 로고    scopus 로고
    • Combination of drugs and drug-resistant reverse transcriptase results in a multiplicative increase of human immunodeficiency virus type 1 mutant frequencies
    • Mansky LM, Pearl DK, Gajary LC. 2002. Combination of drugs and drug-resistant reverse transcriptase results in a multiplicative increase of human immunodeficiency virus type 1 mutant frequencies. J Virol 76: 9253-9259.
    • (2002) J Virol , vol.76 , pp. 9253-9259
    • Mansky, L.M.1    Pearl, D.K.2    Gajary, L.C.3
  • 191
    • 0041145086 scopus 로고    scopus 로고
    • Mispair extension fidelity of human immunodeficiency virus type 1 reverse transcriptases with amino acid substitutions affecting Tyr115
    • Martin-Hernandez AM, Gutierrez-Rivas M, Domingo E, Menendez-Arias L. 1997. Mispair extension fidelity of human immunodeficiency virus type 1 reverse transcriptases with amino acid substitutions affecting Tyr115. Nucleic Acids Res 25:1383-1389.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1383-1389
    • Martin-Hernandez, A.M.1    Gutierrez-Rivas, M.2    Domingo, E.3    Menendez-Arias, L.4
  • 192
    • 0000937442 scopus 로고    scopus 로고
    • Fidelity analysis of HIV-1 reverse transcriptase mutants with an altered amino-acid sequence at residues Leu74, Glu89, Tyr115, Tyr183 and Met184
    • Jonckheere H, De Clercq E, Anne J. 2000. Fidelity analysis of HIV-1 reverse transcriptase mutants with an altered amino-acid sequence at residues Leu74, Glu89, Tyr115, Tyr183 and Met184. Eur J Biochem 267: 2658-2665.
    • (2000) Eur J Biochem , vol.267 , pp. 2658-2665
    • Jonckheere, H.1    De Clercq, E.2    Anne, J.3
  • 194
    • 0030060362 scopus 로고    scopus 로고
    • Role of methionine 184 of human immunodeficiency virus type-1 reverse transcriptase in the polymerase function and fidelity of DNA synthesis
    • Pandey VN, Kaushik N, Rege N, Sarafianos SG, Yadav PN, Modak MJ. 1996. Role of methionine 184 of human immunodeficiency virus type-1 reverse transcriptase in the polymerase function and fidelity of DNA synthesis. Biochemistry 35:2168-2179.
    • (1996) Biochemistry , vol.35 , pp. 2168-2179
    • Pandey, V.N.1    Kaushik, N.2    Rege, N.3    Sarafianos, S.G.4    Yadav, P.N.5    Modak, M.J.6
  • 195
    • 0033587620 scopus 로고    scopus 로고
    • Mechanistic studies examining the efficiency and fidelity of DNA synthesis by the 3TC-resistant mutant (184V) of HIV-1 reverse transcriptase
    • Feng JY, Anderson KS. 1999. Mechanistic studies examining the efficiency and fidelity of DNA synthesis by the 3TC-resistant mutant (184V) of HIV-1 reverse transcriptase. Biochemistry 38:9440-9448.
    • (1999) Biochemistry , vol.38 , pp. 9440-9448
    • Feng, J.Y.1    Anderson, K.S.2
  • 196
    • 0032526623 scopus 로고    scopus 로고
    • The influence of 3TC resistance mutation M184I on the fidelity and error specificity of human immunodeficiency virus type 1 reverse transcriptase
    • Rezende LF, Drosopoulos WC, Prasad VR. 1998. The influence of 3TC resistance mutation M184I on the fidelity and error specificity of human immunodeficiency virus type 1 reverse transcriptase. Nucleic Acids Res 26:3066-3072.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3066-3072
    • Rezende, L.F.1    Drosopoulos, W.C.2    Prasad, V.R.3
  • 197
    • 0344521323 scopus 로고    scopus 로고
    • The fidelity of reverse transcription differs in reactions primed with RNA versus DNA primers
    • Oude Essink BB, Berkhout B. 1999. The fidelity of reverse transcription differs in reactions primed with RNA versus DNA primers. J Biomed Sci 6:121-132.
    • (1999) J Biomed Sci , vol.6 , pp. 121-132
    • Oude Essink, B.B.1    Berkhout, B.2
  • 198
    • 0030772853 scopus 로고    scopus 로고
    • Higher fidelity of RNA-dependent DNA mispair extension by M184V drug-resistant than wild-type reverse transcriptase of human immunodeficiency virus type 1
    • Hsu M, Inouye P, Rezende L, Richard N, Li Z, Prasad VR, Wainberg MA. 1997. Higher fidelity of RNA-dependent DNA mispair extension by M184V drug-resistant than wild-type reverse transcriptase of human immunodeficiency virus type 1. Nucleic Acids Res 25:4532-4536.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4532-4536
    • Hsu, M.1    Inouye, P.2    Rezende, L.3    Richard, N.4    Li, Z.5    Prasad, V.R.6    Wainberg, M.A.7
  • 199
    • 0031980213 scopus 로고    scopus 로고
    • Increased misincorporation fidelity observed for nucleoside analog resistance mutations M184V and E89G in human immunodeficiency virus type 1 reverse transcriptase does not correlate with the overall error rate measured in vitro
    • Drosopoulos WC, Prasad VR. 1998. Increased misincorporation fidelity observed for nucleoside analog resistance mutations M184V and E89G in human immunodeficiency virus type 1 reverse transcriptase does not correlate with the overall error rate measured in vitro. J Virol 72:4224-4230.
    • (1998) J Virol , vol.72 , pp. 4224-4230
    • Drosopoulos, W.C.1    Prasad, V.R.2
  • 200
    • 0028289584 scopus 로고
    • Fidelity of HIV-1 reverse transcriptase copying a hypervariable region of the HIV-1 env gene
    • Ji J, Loeb LA. 1994. Fidelity of HIV-1 reverse transcriptase copying a hypervariable region of the HIV-1 env gene. Virology 199:323-330.
    • (1994) Virology , vol.199 , pp. 323-330
    • Ji, J.1    Loeb, L.A.2
  • 201
    • 0026536430 scopus 로고
    • Fidelity of HIV-1 reverse transcriptase copying RNA in vitro
    • Ji JP, Loeb LA. 1992. Fidelity of HIV-1 reverse transcriptase copying RNA in vitro. Biochemistry 31:954-958.
    • (1992) Biochemistry , vol.31 , pp. 954-958
    • Ji, J.P.1    Loeb, L.A.2
  • 202
    • 0030966487 scopus 로고    scopus 로고
    • Mutations in the SIVenv and theM13 lacZa gene generated in vitro by reverse transcriptases and DNA polymerases
    • Stuke AW, Ahmad-Omar O, Hoefer K, Hunsmann G, Jentsch KD. 1997. Mutations in the SIVenv and theM13 lacZa gene generated in vitro by reverse transcriptases and DNA polymerases. Arch Virol 142:1139-1154.
    • (1997) Arch Virol , vol.142 , pp. 1139-1154
    • Stuke, A.W.1    Ahmad-Omar, O.2    Hoefer, K.3    Hunsmann, G.4    Jentsch, K.D.5
  • 203
    • 0025095253 scopus 로고
    • Genetic consequences of packaging two RNA genomes in one retroviral particle: pseudodiploidy and high rate of genetic recombination
    • Hu WS, Temin HM. 1990. Genetic consequences of packaging two RNA genomes in one retroviral particle: pseudodiploidy and high rate of genetic recombination. Proc Natl Acad Sci U S A 87:1556-1560.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 1556-1560
    • Hu, W.S.1    Temin, H.M.2
  • 205
    • 0031594585 scopus 로고    scopus 로고
    • Retroviral recombination rates do not increase linearly with marker distance and are limited by the size of the recombining subpopulation
    • Anderson JA, Bowman EH, Hu WS. 1998. Retroviral recombination rates do not increase linearly with marker distance and are limited by the size of the recombining subpopulation. J Virol 72:1195-1202.
    • (1998) J Virol , vol.72 , pp. 1195-1202
    • Anderson, J.A.1    Bowman, E.H.2    Hu, W.S.3
  • 206
    • 0033977268 scopus 로고    scopus 로고
    • High rate of recombination throughout the human immunodeficiency virus type 1 genome
    • Jetzt AE, Yu H, Klarmann GJ, Ron Y, Preston BD, Dougherty JP. 2000. High rate of recombination throughout the human immunodeficiency virus type 1 genome. J Virol 74:1234-1240.
    • (2000) J Virol , vol.74 , pp. 1234-1240
    • Jetzt, A.E.1    Yu, H.2    Klarmann, G.J.3    Ron, Y.4    Preston, B.D.5    Dougherty, J.P.6
  • 210
    • 0141676563 scopus 로고    scopus 로고
    • High rates of human immunodeficiency virus type 1 recombination: near-random segregation of markers one kilobase apart in one round of viral replication
    • Rhodes T, Wargo H, Hu WS. 2003. High rates of human immunodeficiency virus type 1 recombination: near-random segregation of markers one kilobase apart in one round of viral replication. J Virol 77: 11193-11200.
    • (2003) J Virol , vol.77 , pp. 11193-11200
    • Rhodes, T.1    Wargo, H.2    Hu, W.S.3
  • 211
    • 13744254540 scopus 로고    scopus 로고
    • Genetic recombination of human immunodeficiency virus type 1 in one round of viral replication: effects of genetic distance, target cells, accessory genes, and lack of high negative interference in crossover events
    • Rhodes TD, Nikolaitchik O, Chen J, Powell D, Hu WS. 2005. Genetic recombination of human immunodeficiency virus type 1 in one round of viral replication: effects of genetic distance, target cells, accessory genes, and lack of high negative interference in crossover events. J Virol 79:1666-1677.
    • (2005) J Virol , vol.79 , pp. 1666-1677
    • Rhodes, T.D.1    Nikolaitchik, O.2    Chen, J.3    Powell, D.4    Hu, W.S.5
  • 212
    • 77954518935 scopus 로고    scopus 로고
    • Patterns of Human Immunodeficiency Virus type 1 recombination ex vivo provide evidence for coadaptation of distant sites, resulting in purifying selection for intersubtype recombinants during replication
    • Galli A, Kearney M, Nikolaitchik OA, Yu S, Chin MP, Maldarelli F, Coffin JM, Pathak VK, Hu WS. 2010. Patterns of Human Immunodeficiency Virus type 1 recombination ex vivo provide evidence for coadaptation of distant sites, resulting in purifying selection for intersubtype recombinants during replication. J Virol 84:7651-7661.
    • (2010) J Virol , vol.84 , pp. 7651-7661
    • Galli, A.1    Kearney, M.2    Nikolaitchik, O.A.3    Yu, S.4    Chin, M.P.5    Maldarelli, F.6    Coffin, J.M.7    Pathak, V.K.8    Hu, W.S.9
  • 213
    • 0018304892 scopus 로고
    • Structure, replication, and recombination of retrovirus genomes: some unifying hypotheses
    • Coffin JM. 1979. Structure, replication, and recombination of retrovirus genomes: some unifying hypotheses. J Gen Virol 42:1-26.
    • (1979) J Gen Virol , vol.42 , pp. 1-26
    • Coffin, J.M.1
  • 215
    • 0027176378 scopus 로고
    • Maturation of dimeric viral RNA of Moloney murine leukemia virus
    • Fu W, Rein A. 1993. Maturation of dimeric viral RNA of Moloney murine leukemia virus. J Virol 67:5443-5449.
    • (1993) J Virol , vol.67 , pp. 5443-5449
    • Fu, W.1    Rein, A.2
  • 216
    • 21144446779 scopus 로고    scopus 로고
    • Identification of a major restriction in HIV-1 intersubtype recombination
    • Chin MP, Rhodes TD, Chen J, Fu W, Hu WS. 2005. Identification of a major restriction in HIV-1 intersubtype recombination. Proc Natl Acad Sci U S A 102:9002-9007.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9002-9007
    • Chin, M.P.1    Rhodes, T.D.2    Chen, J.3    Fu, W.4    Hu, W.S.5
  • 217
    • 65549100184 scopus 로고    scopus 로고
    • Fluorescence fluctuation spectroscopy on viral-like particles reveals variable gag stoichiometry
    • Chen Y, Wu B, Musier-Forsyth K, Mansky LM, Mueller JD. 2009. Fluorescence fluctuation spectroscopy on viral-like particles reveals variable gag stoichiometry. Biophys J 96:1961-1969.
    • (2009) Biophys J , vol.96 , pp. 1961-1969
    • Chen, Y.1    Wu, B.2    Musier-Forsyth, K.3    Mansky, L.M.4    Mueller, J.D.5
  • 218
    • 34247095230 scopus 로고    scopus 로고
    • Dimer initiation signal of human immunodeficiency virus type 1: its role in partner selection during RNA copackaging and its effects on recombination
    • Moore MD, Fu W, Nikolaitchik O, Chen J, Ptak RG, Hu WS. 2007. Dimer initiation signal of human immunodeficiency virus type 1: its role in partner selection during RNA copackaging and its effects on recombination. J Virol 81:4002-4011.
    • (2007) J Virol , vol.81 , pp. 4002-4011
    • Moore, M.D.1    Fu, W.2    Nikolaitchik, O.3    Chen, J.4    Ptak, R.G.5    Hu, W.S.6
  • 219
    • 77953297008 scopus 로고    scopus 로고
    • Delineation of the preferences and requirements of the human immunodeficiency virus type 1 dimerization initiation signal by using an in vivo cell-based selection approach
    • Hussein IT, Ni N, Galli A, Chen J, Moore MD, Hu WS. 2010. Delineation of the preferences and requirements of the human immunodeficiency virus type 1 dimerization initiation signal by using an in vivo cell-based selection approach. J Virol 84:6866-6875.
    • (2010) J Virol , vol.84 , pp. 6866-6875
    • Hussein, I.T.1    Ni, N.2    Galli, A.3    Chen, J.4    Moore, M.D.5    Hu, W.S.6
  • 220
    • 0031977440 scopus 로고    scopus 로고
    • Infectious molecular clones with the nonhomologous dimer initiation sequences found in different subtypes of human immunodeficiency virus type 1 can recombine and initiate a spreading infection in vitro
    • St Louis DC, Gotte D, Sanders-Buell E, Ritchey DW, Salminen MO, Carr JK, McCutchan FE. 1998. Infectious molecular clones with the nonhomologous dimer initiation sequences found in different subtypes of human immunodeficiency virus type 1 can recombine and initiate a spreading infection in vitro. J Virol 72:3991-3998.
    • (1998) J Virol , vol.72 , pp. 3991-3998
    • St Louis, D.C.1    Gotte, D.2    Sanders-Buell, E.3    Ritchey, D.W.4    Salminen, M.O.5    Carr, J.K.6    McCutchan, F.E.7
  • 221
    • 34249072310 scopus 로고    scopus 로고
    • Molecular determinants of HIV-1 intersubtype recombination potential
    • Chin MP, Chen J, Nikolaitchik OA, Hu WS. 2007. Molecular determinants of HIV-1 intersubtype recombination potential. Virology 363: 437-446.
    • (2007) Virology , vol.363 , pp. 437-446
    • Chin, M.P.1    Chen, J.2    Nikolaitchik, O.A.3    Hu, W.S.4
  • 222
    • 0032880103 scopus 로고    scopus 로고
    • Effect of distance between homologous sequences and 3' homology on the frequency of retroviral reverse transcriptase template switching
    • Delviks KA, Pathak VK. 1999. Effect of distance between homologous sequences and 3' homology on the frequency of retroviral reverse transcriptase template switching. J Virol 73:7923-7932.
    • (1999) J Virol , vol.73 , pp. 7923-7932
    • Delviks, K.A.1    Pathak, V.K.2
  • 223
    • 0032845116 scopus 로고    scopus 로고
    • Development of murine leukemia virus-based self-activating vectors that efficiently delete the selectable drug resistance gene during reverse transcription
    • Delviks KA, Pathak VK. 1999. Development of murine leukemia virus-based self-activating vectors that efficiently delete the selectable drug resistance gene during reverse transcription. J Virol 73:8837-8842.
    • (1999) J Virol , vol.73 , pp. 8837-8842
    • Delviks, K.A.1    Pathak, V.K.2
  • 224
    • 0029150042 scopus 로고
    • Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors
    • Rittinger K, Divita G, Goody RS. 1995. Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors. Proc Natl Acad Sci U S A 92:8046-8049.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8046-8049
    • Rittinger, K.1    Divita, G.2    Goody, R.S.3
  • 225
    • 0028925773 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors
    • Spence RA, Kati WM, Anderson KS, Johnson KA. 1995. Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors. Science 267:988-993.
    • (1995) Science , vol.267 , pp. 988-993
    • Spence, R.A.1    Kati, W.M.2    Anderson, K.S.3    Johnson, K.A.4
  • 226
    • 78650647927 scopus 로고    scopus 로고
    • Pre-steady-state kinetic analysis of the incorporation of anti-HIV nucleotide analogs catalyzed by human X-and Y-familyDNApolymerases
    • Brown JA, Pack LR, Fowler JD, Suo Z. 2011. Pre-steady-state kinetic analysis of the incorporation of anti-HIV nucleotide analogs catalyzed by human X-and Y-familyDNApolymerases. Antimicrob Agents Chemother 55:276-283.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 276-283
    • Brown, J.A.1    Pack, L.R.2    Fowler, J.D.3    Suo, Z.4
  • 227
    • 0038215451 scopus 로고    scopus 로고
    • Structural determinants in human DNA polymerase gamma account for mitochondrial toxicity from nucleoside analogs
    • Lim SE, Ponamarev MV, Longley MJ, Copeland WC. 2003. Structural determinants in human DNA polymerase gamma account for mitochondrial toxicity from nucleoside analogs. J Mol Biol 329:45-57.
    • (2003) J Mol Biol , vol.329 , pp. 45-57
    • Lim, S.E.1    Ponamarev, M.V.2    Longley, M.J.3    Copeland, W.C.4
  • 228
    • 84856711380 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase complex with DNA and nevirapine reveals non-nucleoside inhibition mechanism
    • Das K, Martinez SE, Bauman JD, Arnold E. 2012. HIV-1 reverse transcriptase complex with DNA and nevirapine reveals non-nucleoside inhibition mechanism. Nat Struct Mol Biol 19:253-259.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 253-259
    • Das, K.1    Martinez, S.E.2    Bauman, J.D.3    Arnold, E.4
  • 230
    • 20844451906 scopus 로고    scopus 로고
    • Emergence of drug-resistant HIV-1 after intrapartum administration of single-dose nevirapine is substantially underestimated
    • Johnson JA, Li JF, Morris L, Martinson N, Gray G, McIntyre J, Heneine W. 2005. Emergence of drug-resistant HIV-1 after intrapartum administration of single-dose nevirapine is substantially underestimated. J Infect Dis 192:16-23.
    • (2005) J Infect Dis , vol.192 , pp. 16-23
    • Johnson, J.A.1    Li, J.F.2    Morris, L.3    Martinson, N.4    Gray, G.5    McIntyre, J.6    Heneine, W.7
  • 231
    • 33646474114 scopus 로고    scopus 로고
    • Persistence of nevirapine-resistant HIV-1 in women after single-dose nevirapine therapy for prevention of maternal-to-fetal HIV-1 transmission
    • Palmer S, Boltz V, Martinson N, Maldarelli F, Gray G, McIntyre J, Mellors J, Morris L, Coffin J. 2006. Persistence of nevirapine-resistant HIV-1 in women after single-dose nevirapine therapy for prevention of maternal-to-fetal HIV-1 transmission. Proc Natl Acad Sci U S A 103: 7094-7099.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7094-7099
    • Palmer, S.1    Boltz, V.2    Martinson, N.3    Maldarelli, F.4    Gray, G.5    McIntyre, J.6    Mellors, J.7    Morris, L.8    Coffin, J.9
  • 232
    • 9744258219 scopus 로고    scopus 로고
    • Crystallography and the design of anti-AIDS drugs: conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors
    • Das K, Lewi PJ, Hughes SH, Arnold E. 2005. Crystallography and the design of anti-AIDS drugs: conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors. Prog Biophys Mol Biol 88:209-231.
    • (2005) Prog Biophys Mol Biol , vol.88 , pp. 209-231
    • Das, K.1    Lewi, P.J.2    Hughes, S.H.3    Arnold, E.4
  • 234
    • 0033621167 scopus 로고    scopus 로고
    • Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with β-branched amino acids
    • Sarafianos SG, Das K, Clark AD, Jr, Ding J, Boyer PL, Hughes SH, Arnold E. 1999. Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with β-branched amino acids. Proc Natl Acad Sci U S A 96:10027-10032.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 10027-10032
    • Sarafianos, S.G.1    Das, K.2    Clark, A.D.3    Ding, J.4    Boyer, P.L.5    Hughes, S.H.6    Arnold, E.7
  • 235
    • 0034616958 scopus 로고    scopus 로고
    • The role of steric hindrance in 3TC resistance of human immunodeficiency virus type-1 reverse transcriptase
    • Gao HQ, Boyer PL, Sarafianos SG, Arnold E, Hughes SH. 2000. The role of steric hindrance in 3TC resistance of human immunodeficiency virus type-1 reverse transcriptase. J Mol Biol 300:403-418.
    • (2000) J Mol Biol , vol.300 , pp. 403-418
    • Gao, H.Q.1    Boyer, P.L.2    Sarafianos, S.G.3    Arnold, E.4    Hughes, S.H.5
  • 236
    • 0036233261 scopus 로고    scopus 로고
    • Effects of specific zidovudine resistance mutations and substrate structure on nucleotide-dependent primer unblocking by human immunodeficiency virus type 1 reverse transcriptase
    • Meyer PR, Matsuura SE, Tolun AA, Pfeifer I, So AG, Mellors JW, Scott WA. 2002. Effects of specific zidovudine resistance mutations and substrate structure on nucleotide-dependent primer unblocking by human immunodeficiency virus type 1 reverse transcriptase. Antimicrob Agents Chemother 46:1540-1545.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1540-1545
    • Meyer, P.R.1    Matsuura, S.E.2    Tolun, A.A.3    Pfeifer, I.4    So, A.G.5    Mellors, J.W.6    Scott, W.A.7
  • 237
    • 0035965124 scopus 로고    scopus 로고
    • Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors
    • Ren J, Nichols C, Bird L, Chamberlain P, Weaver K, Short S, Stuart DI, Stammers DK. 2001. Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors. J Mol Biol 312:795-805.
    • (2001) J Mol Biol , vol.312 , pp. 795-805
    • Ren, J.1    Nichols, C.2    Bird, L.3    Chamberlain, P.4    Weaver, K.5    Short, S.6    Stuart, D.I.7    Stammers, D.K.8
  • 238
    • 33751529192 scopus 로고    scopus 로고
    • Crystal structures of clinically relevant Lys103Asn/Tyr181Cys double mutant HIV-1 reverse transcriptase in complexes with ATP and non-nucleoside inhibitor HBY 097
    • Das K, Sarafianos SG, Clark AD, Jr., Boyer PL, Hughes SH, Arnold E. 2007. Crystal structures of clinically relevant Lys103Asn/Tyr181Cys double mutant HIV-1 reverse transcriptase in complexes with ATP and non-nucleoside inhibitor HBY 097. J Mol Biol 365:77-89.
    • (2007) J Mol Biol , vol.365 , pp. 77-89
    • Das, K.1    Sarafianos, S.G.2    Clark, A.D.3    Boyer, P.L.4    Hughes, S.H.5    Arnold, E.6
  • 239
    • 13144282707 scopus 로고    scopus 로고
    • Structures of Tyr188Leu mutant and wild-type HIV-1 reverse transcriptase complexed with the non-nucleoside inhibitor HBY 097: inhibitor flexibility is a useful design feature for reducing drug resistance
    • Hsiou Y, Das K, Ding J, Clark AD, Jr., Kleim JP, Rosner M, Winkler I, Riess G, Hughes SH, Arnold E. 1998. Structures of Tyr188Leu mutant and wild-type HIV-1 reverse transcriptase complexed with the non-nucleoside inhibitor HBY 097: inhibitor flexibility is a useful design feature for reducing drug resistance. J Mol Biol 284:313-323.
    • (1998) J Mol Biol , vol.284 , pp. 313-323
    • Hsiou, Y.1    Das, K.2    Ding, J.3    Clark, A.D.4    Kleim, J.P.5    Rosner, M.6    Winkler, I.7    Riess, G.8    Hughes, S.H.9    Arnold, E.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.