메뉴 건너뛰기




Volumn 79, Issue 16, 2005, Pages 10247-10257

Mutations that abrogate human immunodeficiency virus type 1 reverse transcriptase dimerization affect maturation of the reverse transcriptase heterodimer

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; GAG PROTEIN; INDINAVIR; POL PROTEIN; PROTEIN P51; PROTEIN P66; PROTEIN SUBUNIT; PROTEINASE; RNA DIRECTED DNA POLYMERASE; TRYPTOPHAN; UNCLASSIFIED DRUG; VIRUS ENZYME; VIRUS PROTEIN;

EID: 23244448649     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.16.10247-10257.2005     Document Type: Article
Times cited : (54)

References (66)
  • 1
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi, A., H. E. Gendelman, S. Koenig, T. Folks, R. Willey, A. Rabson, and M. A. Martin. 1986. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 59:284-291.
    • (1986) J. Virol. , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 2
    • 0032525275 scopus 로고    scopus 로고
    • Chimeric HIV-1 and feline immunodeficiency virus reverse transcriptases: Critical role of the p51 subunit in the structural integrity of heterodimeric lentiviral DNA polymerases
    • Amacker, M., and U. Hubscher. 1998. Chimeric HIV-1 and feline immunodeficiency virus reverse transcriptases: critical role of the p51 subunit in the structural integrity of heterodimeric lentiviral DNA polymerases. J. Mol. Biol. 278:757-765.
    • (1998) J. Mol. Biol. , vol.278 , pp. 757-765
    • Amacker, M.1    Hubscher, U.2
  • 3
    • 0025992146 scopus 로고
    • A leucine zipper-like motif may mediate HIV reverse transcriptase subunit binding
    • Baillon, J. G., N. T. Nashed, A. Kumar, S. H. Wilson, and D. M. Jerina. 1991. A leucine zipper-like motif may mediate HIV reverse transcriptase subunit binding. New Biol. 3:1015-1019.
    • (1991) New Biol. , vol.3 , pp. 1015-1019
    • Baillon, J.G.1    Nashed, N.T.2    Kumar, A.3    Wilson, S.H.4    Jerina, D.M.5
  • 4
    • 0026355738 scopus 로고
    • Protein-protein interactions of HIV-1 reverse transcriptase: Implication of central and C-terminal regions in subunit binding
    • Becerra, S. P., A. Kumar, M. S. Lewis, S. G. Widen, J. Abbotts, E. M. Karawya, S. H. Hughes, J. Shiloach, and S. H. Wilson. 1991. Protein-protein interactions of HIV-1 reverse transcriptase: implication of central and C-terminal regions in subunit binding. Biochemistry 30:11707-11719.
    • (1991) Biochemistry , vol.30 , pp. 11707-11719
    • Becerra, S.P.1    Kumar, A.2    Lewis, M.S.3    Widen, S.G.4    Abbotts, J.5    Karawya, E.M.6    Hughes, S.H.7    Shiloach, J.8    Wilson, S.H.9
  • 6
    • 18144399251 scopus 로고    scopus 로고
    • Analysis of the contribution of reverse transcriptase and integrase proteins to retroviral RNA dimer conformation
    • Buxton, P., G. Tachedjian, and J. Mak. 2005. Analysis of the contribution of reverse transcriptase and integrase proteins to retroviral RNA dimer conformation. J. Virol. 79:6338-6348.
    • (2005) J. Virol. , vol.79 , pp. 6338-6348
    • Buxton, P.1    Tachedjian, G.2    Mak, J.3
  • 7
    • 0026672676 scopus 로고
    • Macrophagetropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: Definition of critical amino acids involved in cell tropism
    • Chesebro, B., K. Wehrly, J. Nishio, and S. Ferryman. 1992. Macrophagetropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: definition of critical amino acids involved in cell tropism. J. Virol. 66:6547-6554.
    • (1992) J. Virol. , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Ferryman, S.4
  • 8
    • 0033856458 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120
    • Derdeyn, C. A., J. M. Decker, J. N. Sfakianos, X. Wu, W. A. O'Brien, L. Ratner, J. C. Kappes, G. M. Shaw, and E. Hunter. 2000. Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120. J. Virol. 74:8358-8367.
    • (2000) J. Virol. , vol.74 , pp. 8358-8367
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Wu, X.4    O'Brien, W.A.5    Ratner, L.6    Kappes, J.C.7    Shaw, G.M.8    Hunter, E.9
  • 10
    • 0027191463 scopus 로고
    • Characterization of the dimerization process of HIV-1 reverse transcriptase heterodimer using intrinsic protein fluorescence
    • Divita, G., T. Resile, and R. S. Goody. 1993. Characterization of the dimerization process of HIV-1 reverse transcriptase heterodimer using intrinsic protein fluorescence. FEBS Lett. 324:153-158.
    • (1993) FEBS Lett. , vol.324 , pp. 153-158
    • Divita, G.1    Resile, T.2    Goody, R.S.3
  • 11
    • 0029561990 scopus 로고
    • Conformational stability of dimeric HIV-1 and HIV-2 reverse transcriptases
    • Divita, G., K. Rittinger, T. Restle, U. Immendorfer, and R. S. Goody. 1995. Conformational stability of dimeric HIV-1 and HIV-2 reverse transcriptases. Biochemistry 34:16337-16346.
    • (1995) Biochemistry , vol.34 , pp. 16337-16346
    • Divita, G.1    Rittinger, K.2    Restle, T.3    Immendorfer, U.4    Goody, R.S.5
  • 13
    • 0010472999 scopus 로고
    • Tumor necrosis factor alpha induces expression of human immunodeficiency virus in a chronically infected T-cell clone
    • Folks, T. M., K. A. Clouse, J. Justement, A. Rabson, E. Duh, J. H. Kehrl, and A. S. Fauci. 1989. Tumor necrosis factor alpha induces expression of human immunodeficiency virus in a chronically infected T-cell clone. Proc. Natl. Acad. Sci. USA 86:2365-2368.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2365-2368
    • Folks, T.M.1    Clouse, K.A.2    Justement, J.3    Rabson, A.4    Duh, E.5    Kehrl, J.H.6    Fauci, A.S.7
  • 14
    • 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., P. S. Jacques, D. W. Rodgers, M. Ottman, J. L. Darlix, and S. F. Le Grice. 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
  • 16
    • 0022404296 scopus 로고
    • Infection of HTLV-III/LAV in HTLV-I-carrying cells MT-2 and MT-4 and application in a plaque assay
    • Harada, S., Y. Koyanagi, and N. Yamamoto. 1985. Infection of HTLV-III/LAV in HTLV-I-carrying cells MT-2 and MT-4 and application in a plaque assay. Science 229:563-566.
    • (1985) Science , vol.229 , pp. 563-566
    • Harada, S.1    Koyanagi, Y.2    Yamamoto, N.3
  • 17
    • 0036150082 scopus 로고    scopus 로고
    • Mechanistic aspects of HIV-1 reverse transcription initiation
    • Harrich, D., and B. Hooker. 2002. Mechanistic aspects of HIV-1 reverse transcription initiation. Rev. Med. Virol. 12:31-45.
    • (2002) Rev. Med. Virol. , vol.12 , pp. 31-45
    • Harrich, D.1    Hooker, B.2
  • 18
    • 0002958859 scopus 로고
    • General principles underlying laboratory diagnosis in viral infections
    • American Public Health Association, Washington, D.C.
    • Hawkes, R. 1979. General principles underlying laboratory diagnosis in viral infections, p. 34-35. In Diagnostic procedures for viral, rickettsial and chla-mydial infection, 5th ed. American Public Health Association, Washington, D.C.
    • (1979) Diagnostic Procedures for Viral, Rickettsial and Chla-mydial Infection, 5th Ed. , pp. 34-35
    • Hawkes, R.1
  • 19
    • 2342648913 scopus 로고    scopus 로고
    • Interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase proteins
    • Hehl, E. A., P. Joshi, G. V. Kalpana, and V. R. Prasad. 2004. Interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase proteins. J. Virol. 78:5056-5067.
    • (2004) J. Virol. , vol.78 , pp. 5056-5067
    • Hehl, E.A.1    Joshi, P.2    Kalpana, G.V.3    Prasad, V.R.4
  • 20
    • 0026515142 scopus 로고
    • Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: Posttranslational modifications, proteolytic processing, and complete amino acid sequences
    • Henderson, L. E., M. A. Bowers, R. C. Sowder II, S. A. Serabyn, D. G. Johnson, J. W. Bess, Jr., L. O. Arthur, D. K. Bryant, and C. Fenselau. 1992. Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processing, and complete amino acid sequences. J. Virol. 66:1856-1865.
    • (1992) J. Virol. , vol.66 , pp. 1856-1865
    • Henderson, L.E.1    Bowers, M.A.2    Sowder II, R.C.3    Serabyn, S.A.4    Johnson, D.G.5    Bess Jr., J.W.6    Arthur, L.O.7    Bryant, D.K.8    Fenselau, C.9
  • 21
    • 11444267329 scopus 로고    scopus 로고
    • The packaging and maturation of the HIV-1 Pol proteins
    • Hill, M., G. Tachedjian, and J. Mak. 2005. The packaging and maturation of the HIV-1 Pol proteins. Curr. HIV Res. 3:73-85.
    • (2005) Curr. HIV Res. , vol.3 , pp. 73-85
    • Hill, M.1    Tachedjian, G.2    Mak, J.3
  • 22
    • 0036828175 scopus 로고    scopus 로고
    • Proline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability
    • Hill, M. K., M. Shehu-Xhilaga, S. M. Crowe, and J. Mak. 2002. Proline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability. J. Virol. 76:11245-11253.
    • (2002) J. Virol. , vol.76 , pp. 11245-11253
    • Hill, M.K.1    Shehu-Xhilaga, M.2    Crowe, S.M.3    Mak, J.4
  • 23
    • 0026519216 scopus 로고
    • Reverse transcriptase of human immunodeficiency virus type 1: Functionality of subunits of the heterodimer in DNA synthesis
    • Hostomsky, Z., Z. Hostomska, T. B. Fu, and J. Taylor. 1992. Reverse transcriptase of human immunodeficiency virus type 1: functionality of subunits of the heterodimer in DNA synthesis. J. Virol. 66:3179-3182.
    • (1992) J. Virol. , vol.66 , pp. 3179-3182
    • Hostomsky, Z.1    Hostomska, Z.2    Fu, T.B.3    Taylor, J.4
  • 25
    • 0028096227 scopus 로고
    • Modulation of HIV-1 reverse transcriptase function in "selectively deleted" p66/p51 heterodimers
    • Jacques, P. S., B. M. Wohrl, K. J. Howard, and S. F. Le Grice. 1994. Modulation of HIV-1 reverse transcriptase function in "selectively deleted" p66/p51 heterodimers. J. Biol. Chem. 269:1388-1393.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1388-1393
    • Jacques, P.S.1    Wohrl, B.M.2    Howard, K.J.3    Le Grice, S.F.4
  • 26
    • 0028172953 scopus 로고
    • Mutating the "primer grip" of p66 HIV-1 reverse transcriptase implicates tryptophan-229 in template-primer utilization
    • Jacques, P. S., B. M. Wohrl, M. Ottmann, J. L. Darlix, and S. F. Le Grice. 1994. Mutating the "primer grip" of p66 HIV-1 reverse transcriptase implicates tryptophan-229 in template-primer utilization. J. Biol. Chem. 269:26472-26478.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26472-26478
    • Jacques, P.S.1    Wohrl, B.M.2    Ottmann, M.3    Darlix, J.L.4    Le Grice, S.F.5
  • 27
    • 0027932364 scopus 로고
    • The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency
    • Kaplan, A. H., M. Manchester, and R. Swanstrom. 1994. The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency. J. Virol. 68:6782-6786.
    • (1994) J. Virol. , vol.68 , pp. 6782-6786
    • Kaplan, A.H.1    Manchester, M.2    Swanstrom, R.3
  • 28
    • 0035145330 scopus 로고    scopus 로고
    • Salmonella pathogenicity island 2-encoded proteins SseC and SseD are essential for virulence and are substrates of the type III secretion system
    • Klein, J. R., and B. D. Jones. 2001. Salmonella pathogenicity island 2-encoded proteins SseC and SseD are essential for virulence and are substrates of the type III secretion system. Infect. Immun. 69:737-743.
    • (2001) Infect. Immun. , vol.69 , pp. 737-743
    • Klein, J.R.1    Jones, B.D.2
  • 29
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 a resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt, L. A., J. Wang, J. M. Friedman, P. A. Rice, and T. A. Steitz. 1992. Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256:1783-1790.
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 30
    • 0025729443 scopus 로고
    • Quantitative assessment of HIV-1 DNA load by coamplification of HIV-1 gag and HLA-DQ-alpha genes
    • Lee, T. H., F. J. Sunzeri, L. H. Totaler, B. G. Williams, and M. P. Busch. 1991. Quantitative assessment of HIV-1 DNA load by coamplification of HIV-1 gag and HLA-DQ-alpha genes. AIDS 5:683-691.
    • (1991) AIDS , vol.5 , pp. 683-691
    • Lee, T.H.1    Sunzeri, F.J.2    Totaler, L.H.3    Williams, B.G.4    Busch, M.P.5
  • 31
    • 0028789990 scopus 로고
    • Purification and characterization of human immunodeficiency virus type 1 reverse transcriptase
    • Le Grice, S. F., C. E. Cameron, and S. J. Benkovic. 1995. Purification and characterization of human immunodeficiency virus type 1 reverse transcriptase. Methods Enzymol. 262:130-144.
    • (1995) Methods Enzymol. , vol.262 , pp. 130-144
    • Le Grice, S.F.1    Cameron, C.E.2    Benkovic, S.J.3
  • 32
    • 0026070438 scopus 로고
    • Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase
    • Le Grice, S. F., T. Naas, B. Wohlgensinger, and O. Schatz. 1991. Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase. EMBO J. 10:3905-3911.
    • (1991) EMBO J. , vol.10 , pp. 3905-3911
    • Le Grice, S.F.1    Naas, T.2    Wohlgensinger, B.3    Schatz, O.4
  • 33
    • 0029417217 scopus 로고
    • In vivo processing of Pr160gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes
    • Lindhofer, H., K. von der Helm, and H. Nitschko. 1995. In vivo processing of Pr160gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes. Virology 214:624-627.
    • (1995) Virology , vol.214 , pp. 624-627
    • Lindhofer, H.1    Von Der Helm, K.2    Nitschko, H.3
  • 35
    • 2942654608 scopus 로고    scopus 로고
    • Subunit-specific analysis of the human immunodeficiency virus type 1 reverse transcriptase in vivo
    • Mulky, A., S. G. Sarafianos, E. Arnold, X. Wu, and J. C. Kappes. 2004. Subunit-specific analysis of the human immunodeficiency virus type 1 reverse transcriptase in vivo. J. Virol. 78:7089-7096.
    • (2004) J. Virol. , vol.78 , pp. 7089-7096
    • Mulky, A.1    Sarafianos, S.G.2    Arnold, E.3    Wu, X.4    Kappes, J.C.5
  • 36
    • 0029670765 scopus 로고    scopus 로고
    • Monoclonal antibodies against human immunodeficiency virus type 1 integrase: Epitope mapping and differential effects on integrase activities in vitro
    • Nilsen, B. M., I. R. Haugan, K. Berg, L. Olsen, P. O. Brown, and D. E. Helland. 1996. Monoclonal antibodies against human immunodeficiency virus type 1 integrase: epitope mapping and differential effects on integrase activities in vitro. J. Virol. 70:1580-1587.
    • (1996) J. Virol. , vol.70 , pp. 1580-1587
    • Nilsen, B.M.1    Haugan, I.R.2    Berg, K.3    Olsen, L.4    Brown, P.O.5    Helland, D.E.6
  • 38
    • 0027236954 scopus 로고
    • Production of high-liter helper-free retroviruses by transient transfection
    • Pear, W. S., G. P. Nolan, M. L. Scott, and D. Baltimore. 1993. Production of high-liter helper-free retroviruses by transient transfection. Proc. Natl. Acad. Sci. USA 90:8392-8396.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 39
    • 3543142335 scopus 로고    scopus 로고
    • Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism
    • Pettit, S. C., L. E. Everitt, S. Choudhury, B. M. Dunn, and A. H. Kaplan. 2004. Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism. J. Virol. 78:8477-8485.
    • (2004) J. Virol. , vol.78 , pp. 8477-8485
    • Pettit, S.C.1    Everitt, L.E.2    Choudhury, S.3    Dunn, B.M.4    Kaplan, A.H.5
  • 40
    • 0037213627 scopus 로고    scopus 로고
    • The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage
    • Pettit, S. C., S. Gulnik, L. Everitt, and A. H. Kaplan. 2003. The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage. J. Virol. 77:366-374.
    • (2003) J. Virol. , vol.77 , pp. 366-374
    • Pettit, S.C.1    Gulnik, S.2    Everitt, L.3    Kaplan, A.H.4
  • 41
    • 0025297454 scopus 로고
    • Dimerization of human immunodeficiency virus type 1 reverse transcriptase. A target for chemotherapeutic intervention
    • Restle, T., B. Muller, and R. S. Goody. 1990. Dimerization of human immunodeficiency virus type 1 reverse transcriptase. A target for chemotherapeutic intervention. J. Biol. Chem. 265:8986-8988.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8986-8988
    • Restle, T.1    Muller, B.2    Goody, R.S.3
  • 42
    • 11144220847 scopus 로고    scopus 로고
    • Basic statistical considerations in virological experiments
    • Richardson, B. A., and J. Overbaugh. 2005. Basic statistical considerations in virological experiments. J. Virol. 79:669-676.
    • (2005) J. Virol. , vol.79 , pp. 669-676
    • Richardson, B.A.1    Overbaugh, J.2
  • 44
    • 0028006533 scopus 로고
    • Genetic analysis of the human immunodeficiency virus type 1 integrase protein
    • Shin, C. G., B. Taddeo, W. A. Haseltine, and C. M. Farnet. 1994. Genetic analysis of the human immunodeficiency virus type 1 integrase protein. J. Virol. 68:1633-1642.
    • (1994) J. Virol. , vol.68 , pp. 1633-1642
    • Shin, C.G.1    Taddeo, B.2    Haseltine, W.A.3    Farnet, C.M.4
  • 45
    • 2942620594 scopus 로고    scopus 로고
    • Proteolytic processing of an HIV-1 Pol polyprotein precursor: Insights into the mechanism of reverse transcriptase p66/p51 heterodimer formation
    • Sluis-Cremer, N., D. Arion, M. E. Abram, and M. A. Parniak. 2004. Proteolytic processing of an HIV-1 Pol polyprotein precursor: insights into the mechanism of reverse transcriptase p66/p51 heterodimer formation. Int. J. Biochem. Cell Biol. 36:1836-1847.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1836-1847
    • Sluis-Cremer, N.1    Arion, D.2    Abram, M.E.3    Parniak, M.A.4
  • 46
    • 0036076157 scopus 로고    scopus 로고
    • Destabilization of the HIV-1 reverse transcriptase dimer upon interaction with N-acyl hydrazone inhibitors
    • Sluis-Cremer, N., D. Arion, and M. A. Parniak. 2002. Destabilization of the HIV-1 reverse transcriptase dimer upon interaction with N-acyl hydrazone inhibitors. Mol. Pharmacol. 62:398-405.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 398-405
    • Sluis-Cremer, N.1    Arion, D.2    Parniak, M.A.3
  • 47
    • 0034673154 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 reverse transcriptase dimer destabilization by 1-[spiro[4"-amino-2",2"-dioxo-1",- 2"-oxathiole-5",3′-[2′,5′-bis-O-(tert- butyldimethylsilyl)-beta-D-ribofuranosyl]]]-3-ethylthymine
    • Sluis-Cremer, N., G. I. Dmitrienko, J. Balzarini, M. J. Camarasa, and M. A. Parniak. 2000. Human immunodeficiency virus type 1 reverse transcriptase dimer destabilization by 1-[spiro[4"-amino-2",2"-dioxo-1",- 2"-oxathiole-5",3′-[2′,5′-bis-O-(tert- butyldimethylsilyl)-beta-D-ribofuranosyl]]]-3-ethylthymine. Biochemistry 39:1427-1433.
    • (2000) Biochemistry , vol.39 , pp. 1427-1433
    • Sluis-Cremer, N.1    Dmitrienko, G.I.2    Balzarini, J.3    Camarasa, M.J.4    Parniak, M.A.5
  • 48
    • 0036428535 scopus 로고    scopus 로고
    • Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules
    • Sluis-Cremer, N., and G. Tachedjian. 2002. Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules. Eur. J. Biochem. 269:5103-5111.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5103-5111
    • Sluis-Cremer, N.1    Tachedjian, G.2
  • 49
    • 0029888991 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 replication is blocked prior to reverse transcription and integration in freshly isolated peripheral blood monocytes
    • Sonza, S., A. Maerz, N. Deacon, J. Meanger, J. Mills, and S. Crowe. 1996. Human immunodeficiency virus type 1 replication is blocked prior to reverse transcription and integration in freshly isolated peripheral blood monocytes. J. Virol. 70:3863-3869.
    • (1996) J. Virol. , vol.70 , pp. 3863-3869
    • Sonza, S.1    Maerz, A.2    Deacon, N.3    Meanger, J.4    Mills, J.5    Crowe, S.6
  • 51
    • 0037436335 scopus 로고    scopus 로고
    • Role of residues in the tryptophan repeat motif for HIV-1 reverse transcriptase dimerization
    • Tachedjian, G., H. E. Aronson, M. de los Santos, J. Seehra, J. M. McCoy, and S. P. Goff. 2003. Role of residues in the tryptophan repeat motif for HIV-1 reverse transcriptase dimerization. J. Mol. Biol. 326:381-396.
    • (2003) J. Mol. Biol. , vol.326 , pp. 381-396
    • Tachedjian, G.1    Aronson, H.E.2    De Los Santos, M.3    Seehra, J.4    McCoy, J.M.5    Goff, S.P.6
  • 52
    • 0034612275 scopus 로고    scopus 로고
    • Analysis of mutations and suppressors affecting interactions between the subunits of the HIV type 1 reverse transcriptase
    • Tachedjian, G., H. E. Aronson, and S. P. Goff. 2000. Analysis of mutations and suppressors affecting interactions between the subunits of the HIV type 1 reverse transcriptase. Proc. Natl. Acad. Sci. USA 97:6334-6339.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6334-6339
    • Tachedjian, G.1    Aronson, H.E.2    Goff, S.P.3
  • 53
    • 19544363941 scopus 로고    scopus 로고
    • Relationship between enzyme activity and dimeric structure of recombinant HIV-1 reverse transcriptase
    • Tachedjian, G., J. Radzio, and N. Sluis-Cremer. 2005. Relationship between enzyme activity and dimeric structure of recombinant HIV-1 reverse transcriptase. Proteins 60:5-13.
    • (2005) Proteins , vol.60 , pp. 5-13
    • Tachedjian, G.1    Radzio, J.2    Sluis-Cremer, N.3
  • 54
    • 0034873489 scopus 로고    scopus 로고
    • Functional genomics in HIV-1 virus replication: Protein-protein interactions as a basis for recruiting the host cell machinery for viral propagation
    • Tasara, T., M. O. Hottiger, and U. Hubscher. 2001. Functional genomics in HIV-1 virus replication: protein-protein interactions as a basis for recruiting the host cell machinery for viral propagation. Biol. Chem. 382:993-999.
    • (2001) Biol. Chem. , vol.382 , pp. 993-999
    • Tasara, T.1    Hottiger, M.O.2    Hubscher, U.3
  • 55
    • 0035914054 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase and integrase enzymes physically interact and inhibit each other
    • Tasara, T., G. Maga, M. O. Hottiger, and U, Hubscher. 2001. HIV-1 reverse transcriptase and integrase enzymes physically interact and inhibit each other. FEBS Lett. 507:39-44.
    • (2001) FEBS Lett. , vol.507 , pp. 39-44
    • Tasara, T.1    Maga, G.2    Hottiger, M.O.3    Hubscher, U.4
  • 56
    • 0027382852 scopus 로고
    • Two defective forms of reverse transcriptase can complement to restore retroviral infectivity
    • Telesnitsky, A., and S. P. Goff. 1993. Two defective forms of reverse transcriptase can complement to restore retroviral infectivity. EMBO J. 12:4433-4438.
    • (1993) EMBO J. , vol.12 , pp. 4433-4438
    • Telesnitsky, A.1    Goff, S.P.2
  • 61
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites
    • Wiegers, K., G. Rutter, H. Kottler, U. Tessmer, H. Hohenberg, and H. G. Krausslich. 1998. Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J. Virol. 72:2846-2854.
    • (1998) J. Virol. , vol.72 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3    Tessmer, U.4    Hohenberg, H.5    Krausslich, H.G.6
  • 62
    • 0030859022 scopus 로고    scopus 로고
    • Kinetic analysis of four HIV-1 reverse transcriptase enzymes mutated in the primer grip region of p66. Implications for DNA synthesis and dimerization
    • Wohrl, B. M., R. Krebs, S. H. Thrall, S. F. Le Grice, A. J. Scheidig, and R. S. Goody. 1997. Kinetic analysis of four HIV-1 reverse transcriptase enzymes mutated in the primer grip region of p66. Implications for DNA synthesis and dimerization. J. Biol. Chem. 272:17581-17587.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17581-17587
    • Wohrl, B.M.1    Krebs, R.2    Thrall, S.H.3    Le Grice, S.F.4    Scheidig, A.J.5    Goody, R.S.6
  • 63
    • 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., H. Liu, H. Xiao, J. A. Conway, E. Hehl, G. V. Kalpana, V. Prasad, and J. C. Kappes. 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
  • 64
    • 0030851908 scopus 로고    scopus 로고
    • Functional RT and in incorporated into HIV-1 particles independently of the Gag/Pol precursor protein
    • Wu, X., H. Liu, H. Xiao, J. A. Conway, E. Hunter, and J. C. Kappes. 1997. Functional RT and IN incorporated into HIV-1 particles independently of the Gag/Pol precursor protein. EMBO J. 16:5113-5122.
    • (1997) EMBO J. , vol.16 , pp. 5113-5122
    • Wu, X.1    Liu, H.2    Xiao, H.3    Conway, J.A.4    Hunter, E.5    Kappes, J.C.6
  • 65
    • 0031820968 scopus 로고    scopus 로고
    • Mutations in the primer grip of human immunodeficiency virus type 1 reverse transcriptase impair proviral DNA synthesis and virion maturation
    • Yu, Q., M. Ottmann, C. Pechoux, S. Le Grice, and J. L. Darlix. 1998. Mutations in the primer grip of human immunodeficiency virus type 1 reverse transcriptase impair proviral DNA synthesis and virion maturation. J. Virol. 72:7676-7680.
    • (1998) J. Virol. , vol.72 , pp. 7676-7680
    • Yu, Q.1    Ottmann, M.2    Pechoux, C.3    Le Grice, S.4    Darlix, J.L.5
  • 66
    • 0025342694 scopus 로고
    • HIV-1 entry into quiescent primary lymphocytes: Molecular analysis reveals a labile, latent viral structure
    • Zack, J. A., S. J. Arrigo, S. R. Weitsman, A. S. Go, A. Haislip, and I. S. Chen. 1990. HIV-1 entry into quiescent primary lymphocytes: molecular analysis reveals a labile, latent viral structure. Cell 61:213-222.
    • (1990) Cell , vol.61 , pp. 213-222
    • Zack, J.A.1    Arrigo, S.J.2    Weitsman, S.R.3    Go, A.S.4    Haislip, A.5    Chen, I.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.