메뉴 건너뛰기




Volumn 49, Issue 13, 2010, Pages 2821-2833

Homodimerization of the p51 subunit of HIV-1 reverse transcriptase

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL SELECTION; DIMER CONCENTRATIONS; DIMER FORMATION; DIMER INTERFACE; EXPERIMENTAL CONDITIONS; HETERODIMERS; HIV REVERSE TRANSCRIPTASE; HIV-1 REVERSE TRANSCRIPTASE; HOMODIMERIZATION; HOMODIMERS; MICROMOLAR CONCENTRATION; NON-NUCLEOSIDE REVERSE TRANSCRIPTASE INHIBITORS; SMALL ANGLE X-RAY SCATTERING; SUBDOMAIN;

EID: 77950431002     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi902116z     Document Type: Article
Times cited : (19)

References (56)
  • 1
    • 0030868897 scopus 로고    scopus 로고
    • + T cell homeostasis and function in advanced HIV disease
    • DOI 10.1126/science.277.5322.112
    • Autran, B., Carcelain, G., Li, T. S., Blanc, C., Mathez, D., Tubiana, R., Katlama, C., Debre, P., and Leibowitch, J. (1997) Positive effects of combined antiretroviral therapy on CD4(+) T cell homeostasis and function in advanced HIV disease. Science 277, 112-116. (Pubitemid 27450659)
    • (1997) Science , vol.277 , Issue.5322 , pp. 112-116
    • Autran, B.1    Carcelain, G.2    Li, T.S.3    Blanc, C.4    Mathez, D.5    Tubiana, R.6    Katlama, C.7    Debre, P.8    Leibowitch, J.9
  • 3
    • 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., Arion, D., Abram, M. E., and. Parniak, M. A. (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
  • 5
    • 33644683832 scopus 로고    scopus 로고
    • Effects of efavirenz binding on the subunit equilibria of HIV-1 reverse transcriptase
    • DOI 10.1021/bi051915z
    • Venezia, C. F., Howard, K. J., Ignatov, M. E., Holladay, L. A., and Barkley, M. D. (2006) Effects of efavirenz binding on the subunit equilibria of HIV-1 reverse transcriptase. Biochemistry 45, 2779-2789. (Pubitemid 43334527)
    • (2006) Biochemistry , vol.45 , Issue.9 , pp. 2779-2789
    • Venezia, C.F.1    Howard, K.J.2    Ignatov, M.E.3    Holladay, L.A.4    Barkley, M.D.5
  • 6
    • 33646501535 scopus 로고    scopus 로고
    • Dimerization of human immunodeficiency virus type 1 reverse transcriptase as an antiviral target
    • Srivastava, S., Sluis-Cremer, N., and Tachedjian, G. (2006) Dimerization of human immunodeficiency virus type 1 reverse transcriptase as an antiviral target. Curr. Pharm, Des. 12, 1879-1894.
    • (2006) Curr. Pharm, Des. , vol.12 , pp. 1879-1894
    • Srivastava, S.1    Sluis-Cremer, N.2    Tachedjian, G.3
  • 8
    • 0027191463 scopus 로고
    • Characterization of the dimerization process of HIV-1 reverse transcriptase heterodimer using intrinsic protein fluorescence
    • Divita, G., Restle, T., and. Goody, R. S. (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    Restle, T.2    Goody, R.S.3
  • 9
    • 0028308202 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain
    • Divita, G., Restle, T., Goody, R. S., Chermann, J. C., and. Baillon, J. G. (1994) Inhibition of human immunodeficiency virus type 1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain. J. Biol. Chem. 269, 13080-13083.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13080-13083
    • Divita, G.1    Restle, T.2    Goody, R.S.3    Chermann, J.C.4    Baillon, J.G.5
  • 11
    • 33746948397 scopus 로고    scopus 로고
    • Structure-activity relationships of [2',5'-bis-O-(tert- butyldimethylsilyl)-β-D-ribofuranosyl]-3'spiro-5"-(4"-amino- 1",2"-oxathiole-2",2"-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization
    • Sluis-Cremer, N., Hamamouch, N., San Felix, A., Velazquez, S., Balzarini, J., and Camarasa, M. J. (2006) Structure-activity relationships of [2' ,5'-bis-O-(tert-butyldimethylsilyl)-β-D-ribofuranosyl]-3'spiro-5"- (4"-amino-1",2"-oxathiole-2",2"-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization. J. Med. Chem. 49, 4834-4841.
    • (2006) J. Med. Chem. , vol.49 , pp. 4834-4841
    • Sluis-Cremer, N.1    Hamamouch, N.2    San Felix, A.3    Velazquez, S.4    Balzarini, J.5    Camarasa, M.J.6
  • 12
    • 13544274130 scopus 로고    scopus 로고
    • Insight into the mechanism of a peptide inhibitor of HIV reverse transcriptase dimerization
    • DOI 10.1021/bi0484264
    • Depollier, J., Hourdou, M. L., Aldrian-Herrada, G., Rothwell, P., Restle, T., and Divita, G. (2005) Insight into the mechanism of a peptide inhibitor of HIV reverse transcriptase dimerization. Biochemistry. 44, 1909-1918. (Pubitemid 40223620)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 1909-1918
    • Depollier, J.1    Hourdou, M.-L.2    Aldrian-Herrada, G.3    Rothwell, P.4    Restle, T.5    Divita, G.6
  • 14
    • 58649097300 scopus 로고    scopus 로고
    • A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility
    • Agopian, A., Gros, E., Aldrian-Herrada, G., Bosquet, N., Clayette, P., and. Divita, G. (2009) A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility. J. Biol. Chem. 284, 254-264.
    • (2009) J. Biol. Chem. , vol.284 , pp. 254-264
    • Agopian, A.1    Gros, E.2    Aldrian-Herrada, G.3    Bosquet, N.4    Clayette, P.5    Divita, G.6
  • 16
    • 0030008999 scopus 로고    scopus 로고
    • Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization
    • DOI 10.1021/bi952773j
    • Ghosh, M., Jacques, P. S., Rodgers, D. W., Ottman, M., Darlix, J. L., and Le Grice, S. F. (1996) Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization. Biochemistry 35, 8553-8562. (Pubitemid 26240189)
    • (1996) Biochemistry , vol.35 , Issue.26 , 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.J.6
  • 17
    • 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
    • DOI 10.1074/jbc.272.28.17581
    • Wohrl, B. M., Krebs, R., Thrall, S. H., Le Grice, S. F., Scheidig, A. J., and Goody, R. S. (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. (Pubitemid 27311192)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.28 , pp. 17581-17587
    • Wohrl, B.M.1    Krebs, R.2    Thrall, S.H.3    Le Grice, S.F.J.4    Scheidig, A.J.5    Goody, R.S.6
  • 19
    • 0036428535 scopus 로고    scopus 로고
    • Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules
    • DOI 10.1046/j.1432-1033.2002.03216.x
    • Sluis-Cremer, N., and Tachedjian, G. (2002) Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules. Eur. J. Biochem, 269, 5103-5111. (Pubitemid 35340819)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.21 , pp. 5103-5111
    • Sluis-Cremer, N.1    Tachedjian, G.2
  • 20
    • 20244372866 scopus 로고    scopus 로고
    • The N137 and P140 amino acids in the p51 and the P95 amino acid in the p66 subunit of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase are instrumental to maintain catalytic activity and to design new classes of anti-HIV-1 drugs
    • Auwerx, J., Van Nieuwenhove, J., Rodriguez-Barrios, F., de Castro, S., Velazquez, S., Ceccherini-Silberstein, F., De Clercq, E., Camarasa, M. J., Perno, C. F., Gago, F., and. Baizarini, J. (2005) The N137 and P140 amino acids in the p51 and the P95 amino acid in the p66 subunit of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase are instrumental to maintain catalytic activity and to design new classes of anti-HIV-1 drugs. FERS Lett. 579, 2294-2300.
    • (2005) FERS Lett. , vol.579 , pp. 2294-2300
    • Auwerx, J.1    Van Nieuwenhove, J.2    Rodriguez-Barrios, F.3    De Castro, S.4    Velazquez, S.5    Ceccherini-Silberstein, F.6    De Clercq, E.7    Camarasa, M.J.8    Perno, C.F.9    Gago, F.10    Baizarini, J.11
  • 22
    • 19444375120 scopus 로고    scopus 로고
    • Identification of amino acid residues in the human immunodeficiency virus type-1 reverse transcriptase tryptophan-repeat motif that are required for subunit interaction using infectious virions
    • DOI 10.1016/j.jmb.2005.03.057, PII S0022283605003487
    • Mulky, A., Sarafianos, S. G., Jia, Y., Arnold, E., and Kappes, J. C. (2005) Identification of amino acid residues in the human immunodeficiency virus type-1 reverse transcriptase tryptophan-repeat motif that are required for subunit interaction using infectious virions. J. Mol. Biol. 349, 673-684. (Pubitemid 40725947)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.4 , pp. 673-684
    • Mulky, A.1    Sarafianos, S.G.2    Jia, Y.3    Arnold, E.4    Kappes, J.C.5
  • 23
    • 33846069355 scopus 로고    scopus 로고
    • Analysis of Amino Acids in the β7-β8 Loop of Human Immunodeficiency Virus Type 1 Reverse Transcriptase for their Role in Virus Replication
    • DOI 10.1016/j.jmb.2006.10.089, PII S0022283606015178
    • Mulky, A., Vu, B. C., Conway, J. A., Hughes, S. H., and Kappes, J. C. (2007) Analysis of amino acids in the β7-β8 loop of human immunodeficiency virus type 1 reverse transcriptase for their role in virus replication. J. Mol. Biol. 365, 1368-1378. (Pubitemid 46061425)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1368-1378
    • Mulky, A.1    Vu, B.C.2    Conway, J.A.3    Hughes, S.H.4    Kappes, J.C.5
  • 24
    • 23244448649 scopus 로고    scopus 로고
    • Mutations that abrogate human immunodeficiency virus type 1 reverse transcriptase dimerization affect maturation of the reverse transcriptase heterodimer
    • DOI 10.1128/JVI.79.16.10247-10257.2005
    • Wapling, J., Moore, K. L., Sonza, S., Mak, J., and Tachedjian, G. (2005) Mutations that abrogate human immunodeficiency virus type 1 reverse transcriptase dimerization affect maturation of the reverse transcriptase heterodimer. J. Virol. 79, 10247-10257. (Pubitemid 41098566)
    • (2005) Journal of Virology , vol.79 , Issue.16 , pp. 10247-10257
    • Wapling, J.1    Moore, K.L.2    Sonza, S.3    Mak, J.4    Tachedjian, G.5
  • 25
    • 41249088246 scopus 로고    scopus 로고
    • Impact of residues in the nonnucleoside reverse transcriptase inhibitor binding pocket on HIV-1 reverse transcriptase heterodimer stability
    • Figueiredo, A., Zelina, S., Sluis-Cremer, N., and Tachedjian, G. (2008) Impact of residues in the nonnucleoside reverse transcriptase inhibitor binding pocket on HIV-1 reverse transcriptase heterodimer stability. Curr. HIV Res. 130-137.
    • (2008) Curr. HIV Res. , pp. 130-137
    • Figueiredo, A.1    Zelina, S.2    Sluis-Cremer, N.3    Tachedjian, G.4
  • 26
    • 0035080919 scopus 로고    scopus 로고
    • Factors affecting the dimerization of the p66 form of HIV-1 reverse transcriptase
    • Cabodevilla, J. F., Odriozola, L., Santiago, E., and. Martinez-Irujo, J. J. (2001) Factors affecting the dimerization of the p66 form of HIV-1 reverse transcriptase. Eur. J. Biochem. 268, 1163-1172.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1163-1172
    • Cabodevilla, J.F.1    Odriozola, L.2    Santiago, E.3    Martinez-Irujo, J.J.4
  • 27
    • 0025297454 scopus 로고
    • Dimerization of human immunodeficiency virus type 1 reverse transcriptase. A target for chemotherapeutic intervention
    • Restle, T., Muller, B., and. Goody, R. S. (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
  • 28
    • 0028964233 scopus 로고
    • Dimerization kinetics of HIV-1 and HIV-2 reverse transcriptase: A two step process
    • Divita, G., Rittinger, K., Geourjon, C., Deleage, G., and Goody, R. S. (1995) Dimerization kinetics of HIV-1 and HIV-2 reverse transcriptase: A two step process. J. Mol. Biol. 245, 508-521.
    • (1995) J. Mol. Biol. , vol.245 , pp. 508-521
    • Divita, G.1    Rittinger, K.2    Geourjon, C.3    Deleage, G.4    Goody, R.S.5
  • 29
    • 0029561990 scopus 로고
    • Conformational stability of dimeric HIV-1 and HIV-2 reverse transcriptases
    • DOI 10.1021/bi00050a014
    • Divita, G., Rittinger, K., Restle, T., Immendorfer, U., and Goody, R. S. (1995) Conformational stability of dimeric HIV-1 and HIV-2 reverse transcriptases. Biochemistry 34, 16337-16346. (Pubitemid 26006477)
    • (1995) Biochemistry , vol.34 , Issue.50 , pp. 16337-16346
    • Divita, G.1    Rittinger, K.2    Restle, T.3    Immendorfer, U.4    Goody, R.S.5
  • 30
    • 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)-β-D-ribofuranosyl]]}-3-ethylthymine
    • DOI 10.1021/bi991682+
    • Sluis-Cremer, N., Dmitrienko, G. I., Balzarini, J., Camarasa, M. J., and Parniak, M. A. (2000) Human immunodeficiency virus type 1 reverse transcriptase dimer destabilization by 1-[spiro[4″-amino2″,2″-dioxo- 1″,2″-oxathiole-5″,3′-[2″,5″'-bis-O-(tert- butyldimethylsilyl)β-D-ribofuranosyl]]]-3-ethvlthvmine. Biochemistrey 39, 1427-1433. (Pubitemid 30090712)
    • (2000) Biochemistry , vol.39 , Issue.6 , pp. 1427-1433
    • Sluis-Cremer, N.1    Dmitrienko, G.I.2    Balzarini, J.3    Camarasa, M.-J.4    Parniak, M.A.5
  • 31
    • 11844282799 scopus 로고    scopus 로고
    • Efavirenz enhances the proteolytic processing of an HIV-1 pol polyprotein precursor and reverse transcriptase homodimer formation
    • DOI 10.1016/j.febslet.2004.11.099, PII S001457930401511X
    • Tachedjian, G., Moore, K. L., Goff, S. P., and Sluis-Cremer, N. (2005) Efavirenz enhances the proteolytic processing of an HIV-1 pol polyprotein precursor and reverse transcriptase homodimer formation. FEBS Lett. 579, 379-384. (Pubitemid 40092415)
    • (2005) FEBS Letters , vol.579 , Issue.2 , pp. 379-384
    • Tachedjian, G.1    Moore, K.L.2    Goff, S.P.3    Sluis-Cremer, N.4
  • 32
    • 0027441816 scopus 로고
    • HIV-1 reverse transcriptase: Polymerization properties of the p51 homodimer compared to the p66/p51 heterodimer
    • Bavand, M. R., Wagner, R., and Richmond, T. J. (1993) HIV-1 reverse transcriptase: Polymerization properties of the p51 homodimer compared to the p66/p51 heterodimer. Biochemistry 32, 10543-10552.
    • (1993) Biochemistry , vol.32 , pp. 10543-10552
    • Bavand, M.R.1    Wagner, R.2    Richmond, T.J.3
  • 33
    • 0043011942 scopus 로고    scopus 로고
    • Structure-activity relationships in HIV-1 reverse transcriptase revealed by radiation target analysis
    • DOI 10.1110/ps.03130503
    • Sluis-Cremer, N., Kempner, E., and Parniak, M. A. (2003) Structureactivity relationships in HIV-1 reverse transcriptase revealed by radiation target analysis. Protein Sci., 12, 2081-2086. (Pubitemid 37022829)
    • (2003) Protein Science , vol.12 , Issue.9 , pp. 2081-2086
    • Sluis-Cremer, N.1    Kempner, E.2    Parniak, M.A.3
  • 34
    • 0034714106 scopus 로고    scopus 로고
    • Temperature-dependent equilibrium between the open and closed conformation of the p66 subunit of HIV-1 reverse transcriptase revealed by site-directed spin labelling
    • Kensch, O., Restle, T., Wohrl, B. M., Goody, R. S., and Steinhoff, H. J. (2000) Temperature-dependent equilibrium between the open and closed conformation of the p66 subunit of HIV-1 reverse transcriptase revealed by site-directed spin labelling. J. Mol. Biol. 301, 1029-1039.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1029-1039
    • Kensch, O.1    Restle, T.2    Wohrl, B.M.3    Goody, R.S.4    Steinhoff, H.J.5
  • 35
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expression Purif. 41, 207-234.
    • (2005) Protein Expression Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 36
    • 0024836418 scopus 로고
    • Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
    • Muchmore, D. C., Mcintosh, L. P., Russell, C. B., Anderson, D. E., and Dahlquist, F. W. (1989) Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177, 44-73.
    • (1989) Methods Enzymol. , vol.177 , pp. 44-73
    • Muchmore, D.C.1    Mcintosh, L.P.2    Russell, C.B.3    Anderson, D.E.4    Dahlquist, F.W.5
  • 37
    • 1442338399 scopus 로고    scopus 로고
    • High-level expression and purification of untagged and histidine-tagged HIV-1 reverse transcriptase
    • DOI 10.1016/j.pep.2003.10.018
    • Hou, E. W., Prasad, R., Beard, W. A., and Wilson, S. H. (2004) High-level expression and purification of untagged and histidinetagged HIV-1 reverse transcriptase. Protein Expression Purif. 34, 75-86. (Pubitemid 38272315)
    • (2004) Protein Expression and Purification , vol.34 , Issue.1 , pp. 75-86
    • Hou, E.W.1    Prasad, R.2    Beard, W.A.3    Wilson, S.H.4
  • 39
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 40
    • 34249765651 scopus 로고
    • Nmr view: A computer program for the visualization and analysis of Nmr data
    • Johnson, B. A., and. Blevins, R. A. (1994) Nmr View: A Computer Program for the Visualization and Analysis of Nmr Data. J. Biomol. NMR 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 42
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D., Barberato, C., and Koch, M. H. J. (1995) CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773. (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 43
    • 36849047420 scopus 로고    scopus 로고
    • Crystal structures of HIV-1 reverse transcriptase complexes with thiocarbamate non-nucleoside inhibitors
    • DOI 10.1016/j.bbrc.2007.11.036, PII S0006291X07024461
    • Spallarossa, A., Cesarini, S., Ranise, A., Ponassi, M., Unge, T., and Bolognesi, M. (2008) Crystal structures of HIV-1 reverse transcriptase complexes with thiocarbamate non-nucleoside inhibitors. Biochem. Biophys. Res. Commun. 365, 764-770. (Pubitemid 350234856)
    • (2008) Biochemical and Biophysical Research Communications , vol.365 , Issue.4 , pp. 764-770
    • Spallarossa, A.1    Cesarini, S.2    Ranise, A.3    Ponassi, M.4    Unge, T.5    Bolognesi, M.6
  • 48
    • 0025344721 scopus 로고
    • Stabilization and activation of recombinant human immunodeficiency virus-1 reverse transcriptase-P66
    • Rowley, G. L., Ma, Q. F., Bathurst, I. C., Barr, P. J., and Kenyon, G. L. (1990) Stabilization and activation of recombinant human immunodeficiency virus-1 reverse transcriptase-P66. Biochem, Bio- phys. Res. Commun. 167, 673-679.
    • (1990) Biochem, Bio- Phys. Res. Commun. , vol.167 , pp. 673-679
    • Rowley, G.L.1    Ma, Q.F.2    Bathurst, I.C.3    Barr, P.J.4    Kenyon, G.L.5
  • 49
    • 69249097475 scopus 로고    scopus 로고
    • Therapeutic potential of peptide motifs against HIV-1 reverse transcriptase and integrase
    • Andreola, M. L. (2009) Therapeutic potential of peptide motifs against HIV-1 reverse transcriptase and integrase. Curr. Pharm, Des. 15, 2508-2519.
    • (2009) Curr. Pharm, Des. , vol.15 , pp. 2508-2519
    • Andreola, M.L.1
  • 50
    • 0032518621 scopus 로고    scopus 로고
    • P66/p51 and p51/p51 recombinant forms of reverse transcriptase from human immunodeficiency virus type 1 - Interactions with primer tRNA(Lys3), initiation of cDNA synthesis, and effect of inhibitors
    • DOI 10.1046/j.1432-1327.1998.2510487.x
    • Dufour, E., El Dirani-Diab, R., Boulme, F., Fournier, M., Nevinsky, G., Tarrago-Litvak, L., Litvak, S., and Andreola, M. L. (1998) p66/ p51 and p51/p51 recombinant forms of reverse transcriptase from human immunodeficiency virus type 1: Interactions with primer tRNA(Lys3), initiation of cDNA synthesis, and effect of inhibitors. Eur. J. Biochem, 251, 487-495. (Pubitemid 28080951)
    • (1998) European Journal of Biochemistry , vol.251 , Issue.1-2 , pp. 487-495
    • Dufour, E.1    El Dirani-Diab, R.2    Boulme, F.3    Fournier, M.4    Nevinsky, G.5    Tarrago-Litvak, L.6    Litvak, S.7    Andreola, M.-L.8
  • 51
    • 0026693137 scopus 로고
    • Crystal-Structure at 3.5 Angstrom Resolution of HIV-1 Reverse-Transcriptase Complexed with an Inhibitor
    • Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A., and Steitz, T. A. (1992) Crystal-Structure at 3.5 Angstrom 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
  • 52
    • 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
    • DOI 10.1006/jmbi.2001.4988
    • Ren, J., Nichols, C., Bird, L., Chamberlain, P., Weaver, K., Short, S., Stuart, D. I., and Stammers, D. K. (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 nonnucleoside inhibitors. J. Mol. Biol. 312, 795-805. (Pubitemid 33116741)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.4 , 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
  • 53
    • 0036776359 scopus 로고    scopus 로고
    • Crystal structures of zidovudine- Or lamivudine-resistant human immunodeficiency virus type 1 reverse transcriptases containing mutations at codons 41, 184, and 215
    • Chamberlain, P. P., Ren, J., Nichols, C. E., Douglas, L., Lennerstrand, J., Larder, B. A., Stuart, D. I., and. Stammers, D. K. (2002) Crystal structures of zidovudine- or lamivudine-resistant human immunodeficiency virus type 1 reverse transcriptases containing mutations at codons 41, 184, and 215. J. Virol. 76, 10015-10019.
    • (2002) J. Virol. , vol.76 , pp. 10015-10019
    • Chamberlain, P.P.1    Ren, J.2    Nichols, C.E.3    Douglas, L.4    Lennerstrand, J.5    Larder, B.A.6    Stuart, D.I.7    Stammers, D.K.8
  • 54
    • 70349776272 scopus 로고    scopus 로고
    • Kinetics of association and dissociation of HIV-1 reverse transcriptase subunits
    • Veneria, C. F., Meany, B. J., Braz, V. A., and Barkley, M. D. (2009) Kinetics of association and dissociation of HIV-1 reverse transcriptase subunits. Biochemistry. 48, 9084-9093.
    • (2009) Biochemistry. , vol.48 , pp. 9084-9093
    • Veneria, C.F.1    Meany, B.J.2    Braz, V.A.3    Barkley, M.D.4
  • 55
    • 0037469137 scopus 로고    scopus 로고
    • Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium
    • DOI 10.1021/bi0204894
    • Pari, K., Mueller, G. A., DeRose, E. F., Kirby, T. W., and London, R. E. (2003) Solution structure of the RN'ase H domain of the HIV-1 reverse transcriptase in the presence of magnesium. Biochemistry. 42, 639-650. (Pubitemid 36133288)
    • (2003) Biochemistry , vol.42 , Issue.3 , pp. 639-650
    • Pari, K.1    Mueller, G.A.2    Derose, E.F.3    Kirby, T.W.4    London, R.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.