메뉴 건너뛰기




Volumn 88, Issue 5, 2014, Pages 2584-2599

Large-scale production and structural and biophysical characterizations of the human hepatitis B virus polymerase

Author keywords

[No Author keywords available]

Indexed keywords

HEPATITIS B VIRUS POLYMERASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; VIRUS ENZYME;

EID: 84896739556     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02575-13     Document Type: Article
Times cited : (28)

References (88)
  • 1
    • 84857358267 scopus 로고    scopus 로고
    • Global epidemiology of hepatitis B virus infection: new estimates of age-specific HBsAg seroprevalence and endemicity
    • Ott JJ, Stevens GA, Groeger J, Wiersma ST. 2012. Global epidemiology of hepatitis B virus infection: new estimates of age-specific HBsAg seroprevalence and endemicity. Vaccine 30:2212-2219. http://dx.doi.org/10 .1016/j.vaccine.2011.12.116.
    • (2012) Vaccine , vol.30 , pp. 2212-2219
    • Ott, J.J.1    Stevens, G.A.2    Groeger, J.3    Wiersma, S.T.4
  • 3
    • 78650807161 scopus 로고    scopus 로고
    • Hepatitis B virus resistance to antiviral drugs: where are we going
    • Zoulim F. 2011. Hepatitis B virus resistance to antiviral drugs: where are we going? Liver Int. 31(Suppl 1):111-116. http://dx.doi.org/10.1111/j .1478-3231.2010.02399.x.
    • (2011) Liver Int , vol.31 , Issue.SUPPL. 1 , pp. 111-116
    • Zoulim, F.1
  • 4
    • 78349236621 scopus 로고    scopus 로고
    • Review of hepatitis B therapeutics
    • Bhattacharya D, Thio CL. 2010. Review of hepatitis B therapeutics. Clin. Infect. Dis. 51:1201-1208. http://dx.doi.org/10.1086/656624.
    • (2010) Clin. Infect. Dis. , vol.51 , pp. 1201-1208
    • Bhattacharya, D.1    Thio, C.L.2
  • 5
    • 33646186755 scopus 로고    scopus 로고
    • Entecavir for the treatment of chronic hepatitis B virus infection
    • Matthews SJ. 2006. Entecavir for the treatment of chronic hepatitis B virus infection. Clin. Ther. 28:184-203. http://dx.doi.org/10.1016/j .clinthera.2006.02.012.
    • (2006) Clin. Ther. , vol.28 , pp. 184-203
    • Matthews, S.J.1
  • 6
    • 33846514081 scopus 로고    scopus 로고
    • Hepatitis B virus replication
    • Beck J, Nassal M. 2007. Hepatitis B virus replication. World J. Gastroenterol. 13:48-64. http://www.wjgnet.com/1007-9327/13/48.asp.
    • (2007) World J. Gastroenterol. , vol.13 , pp. 48-64
    • Beck, J.1    Nassal, M.2
  • 7
    • 0032845490 scopus 로고    scopus 로고
    • Hepatitis B virus replication: novel roles for virus-host interactions
    • Nassal M. 1999. Hepatitis B virus replication: novel roles for virus-host interactions. Intervirology 42:100-116. http://dx.doi.org/10.1159 /000024970.
    • (1999) Intervirology , vol.42 , pp. 100-116
    • Nassal, M.1
  • 8
    • 43049117085 scopus 로고    scopus 로고
    • Hepatitis B viruses: reverse transcription a different way
    • Nassal M. 2008. Hepatitis B viruses: reverse transcription a different way. Virus Res. 134:235-249. http://dx.doi.org/10.1016/j.virusres.2007.12.024.
    • (2008) Virus Res. , vol.134 , pp. 235-249
    • Nassal, M.1
  • 9
    • 0028241493 scopus 로고
    • Selected mutations of the duck hepatitis B virus P gene RNase H domain affect both RNA packaging and priming of minus-strand DNA synthesis
    • Chen Y, Robinson WS, Marion PL. 1994. Selected mutations of the duck hepatitis B virus P gene RNase H domain affect both RNA packaging and priming of minus-strand DNA synthesis. J. Virol. 68:5232-5238.
    • (1994) J. Virol. , vol.68 , pp. 5232-5238
    • Chen, Y.1    Robinson, W.S.2    Marion, P.L.3
  • 10
    • 0025061039 scopus 로고
    • Mutational analysis of the hepatitis B virus P gene product: domain structure and RNase H activity
    • Radziwill G, Tucker W, Schaller H. 1990. Mutational analysis of the hepatitis B virus P gene product: domain structure and RNase H activity. J. Virol. 64:613-620.
    • (1990) J. Virol. , vol.64 , pp. 613-620
    • Radziwill, G.1    Tucker, W.2    Schaller, H.3
  • 11
    • 0020557417 scopus 로고
    • Sequence homology between retroviral reverse transcriptase and putative polymerases of hepatitis B virus and cauliflower mosaic virus
    • Toh H, Hayashida H, Miyata T. 1983. Sequence homology between retroviral reverse transcriptase and putative polymerases of hepatitis B virus and cauliflower mosaic virus. Nature 305:827-829. http://dx.doi.org /10.1038/305827a0.
    • (1983) Nature , vol.305 , pp. 827-829
    • Toh, H.1    Hayashida, H.2    Miyata, T.3
  • 12
    • 0025006614 scopus 로고
    • Origin and evolution of retroelements based upon their reverse transcriptase sequences
    • Xiong Y, Eickbush TH. 1990. Origin and evolution of retroelements based upon their reverse transcriptase sequences. EMBO J. 9:3353-3362.
    • (1990) EMBO J. , vol.9 , pp. 3353-3362
    • Xiong, Y.1    Eickbush, T.H.2
  • 13
    • 0030896812 scopus 로고    scopus 로고
    • Transcomplementation of nucleotide priming and reverse transcription between independently expressed TP and RT domains of the hepatitis B virus reverse transcriptase
    • Lanford RE, Notvall L, Lee H, Beames B. 1997. Transcomplementation of nucleotide priming and reverse transcription between independently expressed TP and RT domains of the hepatitis B virus reverse transcriptase. J. Virol. 71:2996-3004.
    • (1997) J. Virol. , vol.71 , pp. 2996-3004
    • Lanford, R.E.1    Notvall, L.2    Lee, H.3    Beames, B.4
  • 14
    • 0028300388 scopus 로고
    • Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription
    • Weber M, Bronsema V, Bartos H, Bosserhoff A, Bartenschlager R, Schaller H. 1994. Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription. J. Virol. 68:2994-2999.
    • (1994) J. Virol. , vol.68 , pp. 2994-2999
    • Weber, M.1    Bronsema, V.2    Bartos, H.3    Bosserhoff, A.4    Bartenschlager, R.5    Schaller, H.6
  • 15
    • 0028091053 scopus 로고
    • Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase
    • Zoulim F, Seeger C. 1994. Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase. J. Virol. 68:6-13.
    • (1994) J. Virol. , vol.68 , pp. 6-13
    • Zoulim, F.1    Seeger, C.2
  • 16
    • 8644249753 scopus 로고    scopus 로고
    • Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function
    • Hu J, Flores D, Toft D, Wang X, Nguyen D. 2004. Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J. Virol. 78:13122-13131. http://dx.doi.org/10.1128/JVI.78.23.13122 -13131.2004.
    • (2004) J. Virol. , vol.78 , pp. 13122-13131
    • Hu, J.1    Flores, D.2    Toft, D.3    Wang, X.4    Nguyen, D.5
  • 17
    • 84861321768 scopus 로고    scopus 로고
    • In vitro epsilon RNAdependent protein priming activity of human hepatitis B virus polymerase
    • Jones SA, Boregowda R, Spratt TE, Hu J. 2012. In vitro epsilon RNAdependent protein priming activity of human hepatitis B virus polymerase. J. Virol. 86:5134-5150. http://dx.doi.org/10.1128/JVI.07137-11.
    • (2012) J. Virol. , vol.86 , pp. 5134-5150
    • Jones, S.A.1    Boregowda, R.2    Spratt, T.E.3    Hu, J.4
  • 18
    • 0034468897 scopus 로고    scopus 로고
    • Interaction between hepatitis B virus core protein and reverse transcriptase
    • Lott L, Beames B, Notvall L, Lanford RE. 2000. Interaction between hepatitis B virus core protein and reverse transcriptase. J. Virol. 74:11479-11489. http://dx.doi.org/10.1128/JVI.74.24.11479-11489.2000.
    • (2000) J. Virol. , vol.74 , pp. 11479-11489
    • Lott, L.1    Beames, B.2    Notvall, L.3    Lanford, R.E.4
  • 19
    • 0027494086 scopus 로고
    • Novel mechanism for reverse transcription in hepatitis B viruses
    • Wang G-H, Seeger C. 1993. Novel mechanism for reverse transcription in hepatitis B viruses. J. Virol. 67:6507-6512.
    • (1993) J. Virol. , vol.67 , pp. 6507-6512
    • Wang, G.-H.1    Seeger, C.2
  • 20
    • 78651384693 scopus 로고    scopus 로고
    • The arginine clusters of the carboxyterminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication
    • Lewellyn EB, Loeb DD. 2011. The arginine clusters of the carboxyterminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication. J. Virol. 85:1298-1309. http://dx.doi .org/10.1128/JVI.01957-10.
    • (2011) J. Virol. , vol.85 , pp. 1298-1309
    • Lewellyn, E.B.1    Loeb, D.D.2
  • 21
    • 84873648615 scopus 로고    scopus 로고
    • The helicase-primase complex as a target for effective herpesvirus antivirals
    • Field HJ, Mickleburgh I. 2013. The helicase-primase complex as a target for effective herpesvirus antivirals. Adv. Exp. Med. Biol. 767:145-159. http://dx.doi.org/10.1007/978-1-4614-5037-5_7.
    • (2013) Adv. Exp. Med. Biol. , vol.767 , pp. 145-159
    • Field, H.J.1    Mickleburgh, I.2
  • 24
    • 7944233573 scopus 로고    scopus 로고
    • The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061, from the NMR tube to the clinic
    • Tsantrizos YS. 2004. The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061, from the NMR tube to the clinic. Biopolymers 76:309-323. http://dx.doi.org/10.1002/bip.20127.
    • (2004) Biopolymers , vol.76 , pp. 309-323
    • Tsantrizos, Y.S.1
  • 26
    • 0036289220 scopus 로고    scopus 로고
    • Expression of the active human and duck hepatitis B virus polymerases in heterologous system of Pichia methanolica
    • Choi J, Kim EE, Park YI, Han YS. 2002. Expression of the active human and duck hepatitis B virus polymerases in heterologous system of Pichia methanolica. Antiviral Res. 55:279-290. http://dx.doi.org/10.1016/S0166 -3542(02)00023-2.
    • (2002) Antiviral Res. , vol.55 , pp. 279-290
    • Choi, J.1    Kim, E.E.2    Park, Y.I.3    Han, Y.S.4
  • 27
    • 0033656213 scopus 로고    scopus 로고
    • Expression of stable hepatitis B viral polymerase associated with GRP94 in E
    • Kim SS, Shin HJ, Cho YH, Rho HM. 2000. Expression of stable hepatitis B viral polymerase associated with GRP94 in E. coli. Arch. Virol. 145: 1305-1320. http://dx.doi.org/10.1007/s007050070092.
    • (2000) coli. Arch. Virol. , vol.145 , pp. 1305-1320
    • Kim, S.S.1    Shin, H.J.2    Cho, Y.H.3    Rho, H.M.4
  • 28
    • 78649811910 scopus 로고    scopus 로고
    • Expression and purification of a functional human hepatitis B virus polymerase
    • Yu Y, Pandeya DR, Liu M-L, Liu M-J, Hong S-T. 2010. Expression and purification of a functional human hepatitis B virus polymerase. World J. Gastroenterol. 16:5752-5758. http://dx.doi.org/10.3748/wjg.v16.i45.5752.
    • (2010) World J. Gastroenterol. , vol.16 , pp. 5752-5758
    • Yu, Y.1    Pandeya, D.R.2    Liu, M.-L.3    Liu, M.-J.4    Hong, S.-T.5
  • 29
    • 0027275624 scopus 로고
    • High level expression and phosphorylation of hepatitis B virus polymerase in insect cells with recombinant baculoviruses
    • Ayola B, Kanda P, Lanford RE. 1993. High level expression and phosphorylation of hepatitis B virus polymerase in insect cells with recombinant baculoviruses. Virology 194:370-373. http://dx.doi.org/10.1006 /viro.1993.1270.
    • (1993) Virology , vol.194 , pp. 370-373
    • Ayola, B.1    Kanda, P.2    Lanford, R.E.3
  • 30
    • 0034356011 scopus 로고    scopus 로고
    • Expression of recombinant HBV Pol proteins in HepG2 cells
    • Cho G, Na S, Suh SW, Jung G. 2000. Expression of recombinant HBV Pol proteins in HepG2 cells. J. Biochem. Mol. Biol. 33:440-447. http://www.jbmb.or.kr/view_article.php3?cont=jbmb&kid=7&mid=2&pid=2.
    • (2000) J. Biochem. Mol. Biol. , vol.33 , pp. 440-447
    • Cho, G.1    Na, S.2    Suh, S.W.3    Jung, G.4
  • 31
    • 0031922339 scopus 로고    scopus 로고
    • In vitro activity of hepatitis B virus polymerase: requirement for distinct metal ions and the viral epsilon stem-loop
    • Urban M, McMillan DJ, Canning G, Newell A, Brown E, Mills JS, Jupp R. 1998. In vitro activity of hepatitis B virus polymerase: requirement for distinct metal ions and the viral epsilon stem-loop. J. Gen. Virol. 79:1121-1131.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1121-1131
    • Urban, M.1    McMillan, D.J.2    Canning, G.3    Newell, A.4    Brown, E.5    Mills, J.S.6    Jupp, R.7
  • 32
    • 0030908648 scopus 로고    scopus 로고
    • Sequence-and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B viruses
    • Beck J, Nassal M. 1997. Sequence-and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B viruses. J. Virol. 71:4971-4980.
    • (1997) J. Virol. , vol.71 , pp. 4971-4980
    • Beck, J.1    Nassal, M.2
  • 33
    • 0031774329 scopus 로고    scopus 로고
    • Formation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template
    • Beck J, Nassal M. 1998. Formation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template. Mol. Cell. Biol. 18:6265-6272.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6265-6272
    • Beck, J.1    Nassal, M.2
  • 34
    • 0032978330 scopus 로고    scopus 로고
    • Mapping of the hepatitis B virus reverse transcriptase TP and RT domains by transcomplementation for nucleotide priming and by protein-protein interaction
    • Lanford RE, Kim Y-H, Lee H, Notvall L, Beames B. 1999. Mapping of the hepatitis B virus reverse transcriptase TP and RT domains by transcomplementation for nucleotide priming and by protein-protein interaction. J. Virol. 73:1885-1893.
    • (1999) J. Virol. , vol.73 , pp. 1885-1893
    • Lanford, R.E.1    Kim, Y.-H.2    Lee, H.3    Notvall, L.4    Beames, B.5
  • 35
    • 37049026247 scopus 로고    scopus 로고
    • Chaperones activate hepadnavirus reverse transcriptase by transiently exposing a C-proximal region in the terminal protein domain that contributes to epsilon RNA binding
    • Stahl M, Beck J, Nassal M. 2007. Chaperones activate hepadnavirus reverse transcriptase by transiently exposing a C-proximal region in the terminal protein domain that contributes to epsilon RNA binding. J. Virol. 81:13354-13364. http://dx.doi.org/10.1128/JVI.01196-07.
    • (2007) J. Virol. , vol.81 , pp. 13354-13364
    • Stahl, M.1    Beck, J.2    Nassal, M.3
  • 36
    • 0034909748 scopus 로고    scopus 로고
    • Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli
    • Beck J, Nassal M. 2001. Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli. J. Virol. 75:7410-7419. http://dx .doi.org/10.1128/JVI.75.16.7410-7419.2001.
    • (2001) J. Virol. , vol.75 , pp. 7410-7419
    • Beck, J.1    Nassal, M.2
  • 37
    • 0034468780 scopus 로고    scopus 로고
    • In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90
    • Hu J, Anselmo D. 2000. In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90. J. Virol. 74:11447-11455. http://dx.doi.org/10.1128/JVI.74.24 .11447-11455.2000.
    • (2000) J. Virol. , vol.74 , pp. 11447-11455
    • Hu, J.1    Anselmo, D.2
  • 38
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu J, Seeger C. 1996. Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc. Natl. Acad. Sci. U. S. A. 93:1060-1064.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 39
    • 0141815723 scopus 로고    scopus 로고
    • Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein
    • Beck J, Nassal M. 2003. Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein. J. Biol. Chem. 278:36128-36138. http://dx .doi.org/10.1074/jbc.M301069200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36128-36138
    • Beck, J.1    Nassal, M.2
  • 40
    • 0036133258 scopus 로고    scopus 로고
    • In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins
    • Hu J, Toft D, Anselmo D, Wang X. 2002. In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins. J. Virol. 76:269-279. http://dx.doi.org/10.1128/JVI.76.1.269 -279.2002.
    • (2002) J. Virol. , vol.76 , pp. 269-279
    • Hu, J.1    Toft, D.2    Anselmo, D.3    Wang, X.4
  • 41
    • 35548994976 scopus 로고    scopus 로고
    • Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system
    • Stahl M, Retzlaff M, Nassal M, Beck J. 2007. Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system. Nucleic Acids Res. 35:6124-6136. http://dx.doi.org/10.1093/nar/gkm628.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6124-6136
    • Stahl, M.1    Retzlaff, M.2    Nassal, M.3    Beck, J.4
  • 42
    • 79960400918 scopus 로고    scopus 로고
    • A Tyr residue in the reverse transcriptase domain can mimic the protein-priming Tyr residue in the terminal protein domain of a hepadnavirus P protein
    • Beck J, Nassal M. 2011. A Tyr residue in the reverse transcriptase domain can mimic the protein-priming Tyr residue in the terminal protein domain of a hepadnavirus P protein. J. Virol. 85:7742-7753. http://dx.doi .org/10.1128/JVI.00482-11.
    • (2011) J. Virol. , vol.85 , pp. 7742-7753
    • Beck, J.1    Nassal, M.2
  • 43
    • 79960404258 scopus 로고    scopus 로고
    • Cryptic protein priming sites in two different domains of duck hepatitis B virus reverse transcriptase for initiating DNA synthesis in vitro
    • Boregowda RK, Lin L, Zhu Q, Tian F, Hu J. 2011. Cryptic protein priming sites in two different domains of duck hepatitis B virus reverse transcriptase for initiating DNA synthesis in vitro. J. Virol. 85:7754-7765. http://dx.doi.org/10.1128/JVI.00483-11.
    • (2011) J. Virol. , vol.85 , pp. 7754-7765
    • Boregowda, R.K.1    Lin, L.2    Zhu, Q.3    Tian, F.4    Hu, J.5
  • 44
    • 0345701495 scopus 로고    scopus 로고
    • Heat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase
    • Wang X, Qian X, Guo H-C, Hu J. 2003. Heat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase. J. Virol. 77:4471-4480. http://dx.doi.org/10.1128/JVI.77.8.4471-4480.2003.
    • (2003) J. Virol. , vol.77 , pp. 4471-4480
    • Wang, X.1    Qian, X.2    Guo, H.-C.3    Hu, J.4
  • 45
    • 33144476637 scopus 로고    scopus 로고
    • Hepatitis B virus reverse transcriptase and epsilon RNAsequences required for specific interaction in vitro
    • Hu J, Boyer M. 2006. Hepatitis B virus reverse transcriptase and epsilon RNAsequences required for specific interaction in vitro. J. Virol. 80:2141-2150. http://dx.doi.org/10.1128/JVI.80.5.2141-2150.2006.
    • (2006) J. Virol. , vol.80 , pp. 2141-2150
    • Hu, J.1    Boyer, M.2
  • 46
    • 84874705088 scopus 로고    scopus 로고
    • Protein-primed terminal transferase activity of hepatitis B virus polymerase
    • Jones SA, Hu J. 2013. Protein-primed terminal transferase activity of hepatitis B virus polymerase. J. Virol. 87:2563-2576. http://dx.doi.org/10 .1128/JVI.02786-12.
    • (2013) J. Virol. , vol.87 , pp. 2563-2576
    • Jones, S.A.1    Hu, J.2
  • 47
    • 35348829315 scopus 로고    scopus 로고
    • Darunavir, a conceptually new HIV-1 protease inhibitor for the treatment of drug-resistant HIV
    • Ghosh AK, Dawson ZL, Mitsuya H. 2007. Darunavir, a conceptually new HIV-1 protease inhibitor for the treatment of drug-resistant HIV. Bioorg. Med. Chem. 15:7576-7580. http://dx.doi.org/10.1016.j.bmc.2007.09.010.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 7576-7580
    • Ghosh, A.K.1    Dawson, Z.L.2    Mitsuya, H.3
  • 48
    • 33747099931 scopus 로고    scopus 로고
    • Overcoming HIV drug resistance through rational drug design based on molecular, biochemical, and structural profiles of HIV resistance
    • Yin PD, Das D, Mitsuya H. 2006. Overcoming HIV drug resistance through rational drug design based on molecular, biochemical, and structural profiles of HIV resistance. Cell. Mol. Life Sci. 63:1706-1724. http: //dx.doi.org/10.1007/s00018-006-6009-7.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 1706-1724
    • Yin, P.D.1    Das, D.2    Mitsuya, H.3
  • 49
    • 15544387770 scopus 로고    scopus 로고
    • Agents and strategies in development for improved management of herpes simplex virus infection and disease
    • Kleymann G. 2005. Agents and strategies in development for improved management of herpes simplex virus infection and disease. Expert Opin. Invest. Drugs 14:135-161. http://dx.doi.org/10.1517/13543784.14.2.135.
    • (2005) Expert Opin. Invest. Drugs , vol.14 , pp. 135-161
    • Kleymann, G.1
  • 50
    • 44949179578 scopus 로고    scopus 로고
    • Functional and structural dynamics of hepadnavirus reverse transcriptase during protein-primed initiation of reverse transcription: effects of metal ions
    • Lin L, Wan F, Hu J. 2008. Functional and structural dynamics of hepadnavirus reverse transcriptase during protein-primed initiation of reverse transcription: effects of metal ions. J. Virol. 82:5703-5714. http://dx.doi .org/10.1128/JVI.02760-07.
    • (2008) J. Virol. , vol.82 , pp. 5703-5714
    • Lin, L.1    Wan, F.2    Hu, J.3
  • 51
    • 0029833252 scopus 로고    scopus 로고
    • Evidence for activation of the hepatitis B virus polymerase by binding of its RNA template
    • Tavis JE, Ganem D. 1996. Evidence for activation of the hepatitis B virus polymerase by binding of its RNA template. J. Virol. 70:5741-5750.
    • (1996) J. Virol. , vol.70 , pp. 5741-5750
    • Tavis, J.E.1    Ganem, D.2
  • 52
    • 0031777692 scopus 로고    scopus 로고
    • The duck hepatitis B virus polymerase is activated by its RNA packaging signal, epsilon
    • Tavis JE, Massey B, Gong Y. 1998. The duck hepatitis B virus polymerase is activated by its RNA packaging signal, epsilon. J. Virol. 72:5789-5796.
    • (1998) J. Virol. , vol.72 , pp. 5789-5796
    • Tavis, J.E.1    Massey, B.2    Gong, Y.3
  • 53
    • 0242664703 scopus 로고    scopus 로고
    • Purification of recombinant and endogenous HSP70s
    • Ménoret A. 2004. Purification of recombinant and endogenous HSP70s. Methods 32:7-12. http://dx.doi.org/10.1016/S1046-2023(03)00180-4.
    • (2004) Methods , vol.32 , pp. 7-12
    • Ménoret, A.1
  • 54
    • 0031897370 scopus 로고    scopus 로고
    • Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52
    • Buchner J, Weikl T, Bugl H, Pirkl F, Bose S. 1998. Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52. Methods Enzymol. 290: 418-429.
    • (1998) Methods Enzymol. , vol.290 , pp. 418-429
    • Buchner, J.1    Weikl, T.2    Bugl, H.3    Pirkl, F.4    Bose, S.5
  • 55
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human hsp90 by a client protein
    • McLaughlin SH, Smith HW, Jackson SE. 2002. Stimulation of the weak ATPase activity of human hsp90 by a client protein. J. Mol. Biol. 315:787-798. http://dx.doi.org/10.1006.jmbi.2001.5245.
    • (2002) J. Mol. Biol. , vol.315 , pp. 787-798
    • McLaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 58
    • 33846630895 scopus 로고    scopus 로고
    • A generalized analysis of hydrophobic and loop clusters within globular protein sequences
    • Eudes R, Le Tuan K, Delettré J, Mornon J-P, Callebaut I. 2007. A generalized analysis of hydrophobic and loop clusters within globular protein sequences. BMC Struct. Biol. 7:2. http://dx.doi.org/10.1186/1472 -6807-7-2.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 2
    • Eudes, R.1    Le Tuan, K.2    Delettré, J.3    Mornon, J.-P.4    Callebaut, I.5
  • 60
    • 0024293490 scopus 로고
    • The amino-terminal domain of the hepadnaviral P-gene encodes the terminal protein (genome-linked protein) believed to prime reverse transcription
    • Bartenschlager R, Schaller H. 1988. The amino-terminal domain of the hepadnaviral P-gene encodes the terminal protein (genome-linked protein) believed to prime reverse transcription. EMBO J. 7:4185-4192.
    • (1988) EMBO J. , vol.7 , pp. 4185-4192
    • Bartenschlager, R.1    Schaller, H.2
  • 61
    • 84864023867 scopus 로고    scopus 로고
    • TP-RT domain interactions of duck hepatitis B virus reverse transcriptase in cis and in trans during protein-primed initiation of DNA synthesis in vitro
    • Boregowda RK, Adams C, Hu J. 2012. TP-RT domain interactions of duck hepatitis B virus reverse transcriptase in cis and in trans during protein-primed initiation of DNA synthesis in vitro. J. Virol. 86:6522-6536. http://dx.doi.org/10.1128/JVI.00086-12.
    • (2012) J. Virol. , vol.86 , pp. 6522-6536
    • Boregowda, R.K.1    Adams, C.2    Hu, J.3
  • 63
    • 34347374452 scopus 로고    scopus 로고
    • Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E
    • de Marco A, Deuerling E, Mogk A, Tomoyasu T, Bukau B. 2007. Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli. BMC Biotechnol. 7:32. http://dx.doi.org/10 .1186/1472-6750-7-32.
    • (2007) coli. BMC Biotechnol. , vol.7 , pp. 32
    • de Marco, A.1    Deuerling, E.2    Mogk, A.3    Tomoyasu, T.4    Bukau, B.5
  • 65
    • 12644320243 scopus 로고    scopus 로고
    • Expression, purification, and characterization of an active RNase H domain of the hepatitis B viral polymerase
    • Wei X, Peterson DL. 1996. Expression, purification, and characterization of an active RNase H domain of the hepatitis B viral polymerase. J. Biol. Chem. 271:32617-32622.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32617-32622
    • Wei, X.1    Peterson, D.L.2
  • 66
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, Woody RW. 2000. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287:252-260. http://dx.doi.org/10.1006/abio.2000.4880.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 67
  • 68
    • 0032736844 scopus 로고    scopus 로고
    • Conformation and stability of barley chymotryp-sin inhibitor-2 (CI-2) mutants containing multiple lysine substitutions
    • Roesler KR, Rao AG. 1999. Conformation and stability of barley chymotryp-sin inhibitor-2 (CI-2) mutants containing multiple lysine substitutions. Protein Eng. 12:967-973. http://dx.doi.org/10.1093/protein/12.11.967.
    • (1999) Protein Eng. , vol.12 , pp. 967-973
    • Roesler, K.R.1    Rao, A.G.2
  • 70
    • 55649088213 scopus 로고    scopus 로고
    • Static light scattering to characterize membrane proteins in detergent solution
    • Slotboom DJ, Duurkens RH, Olieman K, Erkens GB. 2008. Static light scattering to characterize membrane proteins in detergent solution. Methods 46:73-82. http://dx.doi.org/10.1016/j.ymeth.2008.06.012.
    • (2008) Methods , vol.46 , pp. 73-82
    • Slotboom, D.J.1    Duurkens, R.H.2    Olieman, K.3    Erkens, G.B.4
  • 71
    • 0003607955 scopus 로고    scopus 로고
    • Refractive increment data book for polymer and biomolecular scientists
    • Nottingham University Press, Nottingham, United Kingdom.
    • Theisen A. 2000. Refractive increment data book for polymer and biomolecular scientists. Nottingham University Press, Nottingham, United Kingdom.
    • (2000)
    • Theisen, A.1
  • 72
    • 33748572634 scopus 로고    scopus 로고
    • Aspects of native proteins are retained in vacuum
    • Ruotolo BT, Robinson CV. 2006. Aspects of native proteins are retained in vacuum. Curr. Opin. Chem. Biol. 10:402-408. http://dx.doi.org/10.10 16/j.cbpa.2006.08.020.
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 402-408
    • Ruotolo, B.T.1    Robinson, C.V.2
  • 73
    • 36348991325 scopus 로고    scopus 로고
    • Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry
    • Smith DP, Giles K, Bateman RH, Radford SE, Ashcroft AE. 2007. Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry. J. Am. Soc. Mass Spectrom. 18:2180-2190. http://dx.doi .org/10.1016/j.jasms.2007.09.017.
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 2180-2190
    • Smith, D.P.1    Giles, K.2    Bateman, R.H.3    Radford, S.E.4    Ashcroft, A.E.5
  • 75
    • 32344431772 scopus 로고    scopus 로고
    • Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35
    • Gohon Y, Giusti F, Prata C, Charvolin D, Timmins P, Ebel C, Tribet C, Popot JL. 2006. Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35. Langmuir 22:1281-1290. http://dx.doi.org/10.1021/la052243g.
    • (2006) Langmuir , vol.22 , pp. 1281-1290
    • Gohon, Y.1    Giusti, F.2    Prata, C.3    Charvolin, D.4    Timmins, P.5    Ebel, C.6    Tribet, C.7    Popot, J.L.8
  • 77
    • 0032720338 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of protein-protein interactions
    • Pierce MM, Raman CS, Nall BT. 1999. Isothermal titration calorimetry of protein-protein interactions. Methods 19:213-221. http://dx.doi.org /10.1006/meth.1999.0852.
    • (1999) Methods , vol.19 , pp. 213-221
    • Pierce, M.M.1    Raman, C.S.2    Nall, B.T.3
  • 78
    • 67649479264 scopus 로고    scopus 로고
    • An interdomain RNA binding site on the hepadnaviral polymerase that is essential for reverse transcription
    • Badtke MP, Khan I, Cao F, Hu J, Tavis JE. 2009. An interdomain RNA binding site on the hepadnaviral polymerase that is essential for reverse transcription. Virology 390:130-138. http://dx.doi.org/10.1016/j.virol .2009.04.023.
    • (2009) Virology , vol.390 , pp. 130-138
    • Badtke, M.P.1    Khan, I.2    Cao, F.3    Hu, J.4    Tavis, J.E.5
  • 79
    • 84866177939 scopus 로고    scopus 로고
    • Carbonyl J acid derivatives block protein priming of hepadnaviral P protein and DNA-dependent DNA synthesis activity of hepadnaviral nucleocapsids
    • Wang Y-X, Wen Y-M, Nassal M. 2012. Carbonyl J acid derivatives block protein priming of hepadnaviral P protein and DNA-dependent DNA synthesis activity of hepadnaviral nucleocapsids. J. Virol. 86:10079 -10092. http://dx.doi.org/10.1128/JVI.00816-12.
    • (2012) J. Virol. , vol.86 , pp. 10079-10092
    • Wang, Y.-X.1    Wen, Y.-M.2    Nassal, M.3
  • 80
    • 34547916087 scopus 로고    scopus 로고
    • Optimized expression from a synthetic gene of an untagged RNase H domain of human hepatitis B virus polymerase which is enzymatically active
    • Potenza N, Salvatore V, Raimondo D, Falanga D, Nobile V, Peterson DL, Russo A. 2007. Optimized expression from a synthetic gene of an untagged RNase H domain of human hepatitis B virus polymerase which is enzymatically active. Protein Expr. Purif. 55:93-99. http://dx.doi.org/10 .1016/j.pep.2007.04.005.
    • (2007) Protein Expr. Purif. , vol.55 , pp. 93-99
    • Potenza, N.1    Salvatore, V.2    Raimondo, D.3    Falanga, D.4    Nobile, V.5    Peterson, D.L.6    Russo, A.7
  • 81
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan C-Y, Lee S, Cyr DM. 2003. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 8:309-316. http://dx.doi.org /10.1379/1466-1268(2003)0080309:MFROHF2.0.CO;2.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.-Y.1    Lee, S.2    Cyr, D.M.3
  • 82
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer MP, Bukau B. 2005. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62:670-684. http://dx.doi.org /10.1007/s00018-004-4464-6.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 83
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C. 2006. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75:271-294. http: //dx.doi.org/10.1146/annurev.biochem.75.103004.142738.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 84
    • 34447500303 scopus 로고    scopus 로고
    • Hepatitis B virus genetic variability and evolution
    • Kay A, Zoulim F. 2007. Hepatitis B virus genetic variability and evolution. Virus Res. 127:164-176. http://dx.doi.org/10.1016/j.virusres.2007.02.021.
    • (2007) Virus Res. , vol.127 , pp. 164-176
    • Kay, A.1    Zoulim, F.2
  • 85
    • 17744375593 scopus 로고    scopus 로고
    • Nomenclature for antiviral-resistant human hepatitis B virus mutations in the polymerase region
    • Stuyver LJ, Locarnini SA, Lok A, Richman DD, Carman WF, Dienstag JL, Schinazi RF. 2001. Nomenclature for antiviral-resistant human hepatitis B virus mutations in the polymerase region. Hepatology 33:751-757. http://dx.doi.org/10.1053/jhep.2001.22166.
    • (2001) Hepatology , vol.33 , pp. 751-757
    • Stuyver, L.J.1    Locarnini, S.A.2    Lok, A.3    Richman, D.D.4    Carman, W.F.5    Dienstag, J.L.6    Schinazi, R.F.7
  • 86
    • 0031018112 scopus 로고    scopus 로고
    • Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
    • Hu J, Toft DO, Seeger C. 1997. Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids.EMBOJ. 16:59-68. http://dx.doi.org/10 .1093/emboj/16.1.59.
    • (1997) EMBOJ. , vol.16 , pp. 59-68
    • Hu, J.1    Toft, D.O.2    Seeger, C.3
  • 87
    • 0028978938 scopus 로고
    • Nucleotide priming and reverse transcriptase activity of hepatitis B virus polymerase expressed in insect cells
    • Lanford RE, Notvall L, Beames B. 1995. Nucleotide priming and reverse transcriptase activity of hepatitis B virus polymerase expressed in insect cells. J. Virol. 69:4431-4439.
    • (1995) J. Virol. , vol.69 , pp. 4431-4439
    • Lanford, R.E.1    Notvall, L.2    Beames, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.