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Volumn 87, Issue 5, 2013, Pages 2563-2576

Protein-primed terminal transferase activity of hepatitis B virus polymerase

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEOTIDE; FOSCARNET; MAGNESIUM; MANGANESE; RNA POLYMERASE; TRANSFERASE;

EID: 84874705088     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02786-12     Document Type: Article
Times cited : (32)

References (81)
  • 1
    • 0030707941 scopus 로고    scopus 로고
    • Hepatitis B virus infection
    • Lee W. 1997. Hepatitis B virus infection. N. Engl. J. Med. 337:1733-1745.
    • (1997) N. Engl. J. Med. , vol.337 , pp. 1733-1745
    • Lee, W.1
  • 3
    • 34547755447 scopus 로고    scopus 로고
    • Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Seeger C, Mason WS, Zoulim F. 2007. Hepadnaviruses, p 2977-3029. In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Hepadnaviruses , pp. 2977-3029
    • Seeger, C.1    Mason, W.S.2    Zoulim, F.3
  • 4
    • 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
  • 5
    • 0025076858 scopus 로고
    • Effects of insertional and point mutations on the functions of the duck hepatitis B virus polymerase
    • Chang LJ, Hirsch RC, Ganem D, Varmus HE. 1990. Effects of insertional and point mutations on the functions of the duck hepatitis B virus polymerase. J. Virol. 64:5553-5558.
    • (1990) J. Virol. , vol.64 , pp. 5553-5558
    • Chang, L.J.1    Hirsch, R.C.2    Ganem, D.3    Varmus, H.E.4
  • 6
    • 0029846357 scopus 로고    scopus 로고
    • Expression and characterization of hepadnavirus reverse transcriptases
    • Hu J, Seeger C. 1996. Expression and characterization of hepadnavirus reverse transcriptases. Methods Enzymol. 275:195-208.
    • (1996) Methods Enzymol. , vol.275 , pp. 195-208
    • Hu, J.1    Seeger, C.2
  • 7
    • 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
  • 8
    • 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
  • 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
    • 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.
    • (1983) Nature , vol.305 , pp. 827-829
    • Toh, H.1    Hayashida, H.2    Miyata, T.3
  • 11
    • 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
  • 12
    • 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
  • 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
    • 0025026431 scopus 로고
    • The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation
    • Bartenschlager R, Junker-Niepmann M, Schaller H. 1990. The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation. J. Virol. 64:5324 -5332.
    • (1990) J. Virol. , vol.64 , pp. 5324-5332
    • Bartenschlager, R.1    Junker-Niepmann, M.2    Schaller, H.3
  • 15
    • 0026706346 scopus 로고
    • Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome
    • Bartenschlager R, Schaller H. 1992. Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome. EMBO J. 11:3413-3420.
    • (1992) EMBO J. , vol.11 , pp. 3413-3420
    • Bartenschlager, R.1    Schaller, H.2
  • 16
    • 0028987482 scopus 로고
    • Mutations in the epsilon sequences of human hepatitis B virus affect both RNA encapsidation and reverse transcription
    • Fallows DA, Goff SP. 1995. Mutations in the epsilon sequences of human hepatitis B virus affect both RNA encapsidation and reverse transcription. J. Virol. 69:3067-3073.
    • (1995) J. Virol. , vol.69 , pp. 3067-3073
    • Fallows, D.A.1    Goff, S.P.2
  • 17
    • 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.
    • (2006) J. Virol. , vol.80 , pp. 2141-2150
    • Hu, J.1    Boyer, M.2
  • 18
    • 63849259055 scopus 로고    scopus 로고
    • RNA-protein interactions in hepadnavirus reverse transcription
    • Hu J, Lin L. 2009. RNA-protein interactions in hepadnavirus reverse transcription. Front. Biosci. 14:1606 -1618.
    • (2009) Front. Biosci. , vol.14 , pp. 1606-1618
    • Hu, J.1    Lin, L.2
  • 19
    • 0029940006 scopus 로고    scopus 로고
    • A bulged region of the hepatitis B virus RNA encapsidation signal contains the replication origin for discontinuous first-strand DNA synthesis
    • Nassal M, Rieger A. 1996. A bulged region of the hepatitis B virus RNA encapsidation signal contains the replication origin for discontinuous first-strand DNA synthesis. J. Virol. 70:2764 -2773.
    • (1996) J. Virol. , vol.70 , pp. 2764-2773
    • Nassal, M.1    Rieger, A.2
  • 20
    • 0028308495 scopus 로고
    • Hepadnavirus reverse transcription initiates within the stem-loop of the RNA packaging signal and employs a novel strand transfer
    • Tavis JE, Perri S, Ganem D. 1994. Hepadnavirus reverse transcription initiates within the stem-loop of the RNA packaging signal and employs a novel strand transfer. J. Virol. 68:3536 -3543.
    • (1994) J. Virol. , vol.68 , pp. 3536-3543
    • Tavis, J.E.1    Perri, S.2    Ganem, D.3
  • 21
    • 0027494086 scopus 로고
    • Novel mechanism for reverse transcription in hepatitis B viruses
    • Wang GH, 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
  • 22
    • 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
  • 23
    • 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
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0031427926 scopus 로고    scopus 로고
    • RNA signals that control DNA replication in hepadnaviruses
    • Hu J, Seeger C. 1997. RNA signals that control DNA replication in hepadnaviruses. Semin. Virol. 8:205-211.
    • (1997) Semin. Virol. , vol.8 , pp. 205-211
    • Hu, J.1    Seeger, C.2
  • 27
    • 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.
    • (2012) J. Virol. , vol.86 , pp. 5134-5150
    • Jones, S.A.1    Boregowda, R.2    Spratt, T.E.3    Hu, J.4
  • 28
    • 0029655242 scopus 로고    scopus 로고
    • Specific hepatitis B virus minus-strand DNA synthesis requires only the 5' encapsidation signal and the 3'-proximal direct repeat DR1
    • Rieger A, Nassal M. 1996. Specific hepatitis B virus minus-strand DNA synthesis requires only the 5' encapsidation signal and the 3'-proximal direct repeat DR1. J. Virol. 70:585-589.
    • (1996) J. Virol. , vol.70 , pp. 585-589
    • Rieger, A.1    Nassal, M.2
  • 29
    • 0025045477 scopus 로고
    • A short cisacting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA
    • Junker-Niepmann M, Bartenschlager R, Schaller H. 1990. A short cisacting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA. EMBO J. 9:3389 -3396.
    • (1990) EMBO J. , vol.9 , pp. 3389-3396
    • Junker-Niepmann, M.1    Bartenschlager, R.2    Schaller, H.3
  • 30
    • 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.
    • (2004) J. Virol. , vol.78 , pp. 13122-13131
    • Hu, J.1    Flores, D.2    Toft, D.3    Wang, X.4    Nguyen, D.5
  • 31
    • 0026493753 scopus 로고
    • The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis
    • Wang GH, Seeger C. 1992. The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis. Cell 71:663- 670.
    • (1992) Cell , vol.71 , pp. 663-670
    • Wang, G.H.1    Seeger, C.2
  • 32
    • 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
  • 33
    • 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
  • 34
    • 84864023867 scopus 로고    scopus 로고
    • TP-RT domain interactions of duck hepatitis B virus reverse transcriptase in cis and in trans during proteinprimed initiation of DNA synthesis in vitro
    • Boregowda R, Adams C, Hu J. 2012. TP-RT domain interactions of duck hepatitis B virus reverse transcriptase in cis and in trans during proteinprimed initiation of DNA synthesis in vitro. J. Virol. 86:6522- 6536.
    • (2012) J. Virol. , vol.86 , pp. 6522-6536
    • Boregowda, R.1    Adams, C.2    Hu, J.3
  • 35
    • 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.
    • (2000) J. Virol. , vol.74 , pp. 11447-11455
    • Hu, J.1    Anselmo, D.2
  • 36
    • 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
  • 37
    • 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.
    • (2002) J. Virol. , vol.76 , pp. 269-279
    • Hu, J.1    Toft, D.2    Anselmo, D.3    Wang, X.4
  • 38
    • 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. EMBO J. 16:59-68.
    • (1997) EMBO J. , vol.16 , pp. 59-68
    • Hu, J.1    Toft, D.O.2    Seeger, C.3
  • 39
    • 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.
    • (2007) J. Virol. , vol.81 , pp. 13354-13364
    • Stahl, M.1    Beck, J.2    Nassal, M.3
  • 40
    • 0036111150 scopus 로고    scopus 로고
    • Distinct requirement for two stages of proteinprimed initiation of reverse transcription in hepadnaviruses
    • Wang X, Hu J. 2002. Distinct requirement for two stages of proteinprimed initiation of reverse transcription in hepadnaviruses. J. Virol. 76: 5857-5865.
    • (2002) J. Virol. , vol.76 , pp. 5857-5865
    • Wang, X.1    Hu, J.2
  • 41
    • 0345701495 scopus 로고    scopus 로고
    • Heat shock protein 90- independent activation of truncated hepadnavirus reverse transcriptase
    • Wang X, Qian X, Guo HC, Hu J. 2003. Heat shock protein 90- independent activation of truncated hepadnavirus reverse transcriptase. J. Virol. 77:4471- 4480.
    • (2003) J. Virol. , vol.77 , pp. 4471-4480
    • Wang, X.1    Qian, X.2    Guo, H.C.3    Hu, J.4
  • 42
    • 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.
    • (2008) J. Virol. , vol.82 , pp. 5703-5714
    • Lin, L.1    Wan, F.2    Hu, J.3
  • 43
    • 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.
    • (2011) J. Virol. , vol.85 , pp. 7742-7753
    • Beck, J.1    Nassal, M.2
  • 44
    • 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.
    • (2011) J. Virol. , vol.85 , pp. 7754-7765
    • Boregowda, R.K.1    Lin, L.2    Zhu, Q.3    Tian, F.4    Hu, J.5
  • 45
    • 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
  • 46
    • 1942453741 scopus 로고    scopus 로고
    • Oligomer synthesis by priming deficient polymerase in hepatitis B virus core particle
    • Kim HY, Park GS, Kim EG, Kang SH, Shin HJ, Park S, Kim KH. 2004. Oligomer synthesis by priming deficient polymerase in hepatitis B virus core particle. Virology 322:22-30.
    • (2004) Virology , vol.322 , pp. 22-30
    • Kim, H.Y.1    Park, G.S.2    Kim, E.G.3    Kang, S.H.4    Shin, H.J.5    Park, S.6    Kim, K.H.7
  • 47
    • 34247635482 scopus 로고    scopus 로고
    • Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G
    • Nguyen DH, Gummuluru S, Hu J. 2007. Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G. J. Virol. 81:4465- 4472.
    • (2007) J. Virol. , vol.81 , pp. 4465-4472
    • Nguyen, D.H.1    Gummuluru, S.2    Hu, J.3
  • 48
    • 39749175026 scopus 로고    scopus 로고
    • Inhibition of hepadnavirus reverse transcriptaseepsilon RNA interaction by porphyrin compounds
    • Lin L, Hu J. 2008. Inhibition of hepadnavirus reverse transcriptaseepsilon RNA interaction by porphyrin compounds. J. Virol. 82:2305- 2312.
    • (2008) J. Virol. , vol.82 , pp. 2305-2312
    • Lin, L.1    Hu, J.2
  • 49
    • 70349673605 scopus 로고    scopus 로고
    • A human 5'-tyrosyl DNA phosphodiesterase that repairs topoisomerase- mediated DNA damage
    • Cortes Ledesma F, El Khamisy SF, Zuma MC, Osborn K, Caldecott KW. 2009. A human 5'-tyrosyl DNA phosphodiesterase that repairs topoisomerase- mediated DNA damage. Nature 461:674-678.
    • (2009) Nature , vol.461 , pp. 674-678
    • Cortes Ledesma, F.1    El Khamisy, S.F.2    Zuma, M.C.3    Osborn, K.4    Caldecott, K.W.5
  • 50
    • 78650964114 scopus 로고    scopus 로고
    • TDP2/ TTRAP is the major 5'-tyrosyl DNA phosphodiesterase activity in vertebrate cells and is critical for cellular resistance to topoisomerase IIinduced DNA damage
    • Zeng Z, Cortes-Ledesma F, El Khamisy SF, Caldecott KW. 2011. TDP2/ TTRAP is the major 5'-tyrosyl DNA phosphodiesterase activity in vertebrate cells and is critical for cellular resistance to topoisomerase IIinduced DNA damage. J. Biol. Chem. 286:403- 409.
    • (2011) J. Biol. Chem. , vol.286 , pp. 403-409
    • Zeng, Z.1    Cortes-Ledesma, F.2    El Khamisy, S.F.3    Caldecott, K.W.4
  • 51
    • 0020452229 scopus 로고
    • Determination of free and bound manganese( II) in hepatocytes from fed and fasted rats
    • Ash DE, Schramm VL. 1982. Determination of free and bound manganese( II) in hepatocytes from fed and fasted rats. J. Biol. Chem. 257:9261- 9264.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9261-9264
    • Ash, D.E.1    Schramm, V.L.2
  • 52
    • 0036240008 scopus 로고    scopus 로고
    • Inhibition of reverse transcription in vivo by elevated manganese ion concentration
    • Bolton EC, Mildvan AS, Boeke JD. 2002. Inhibition of reverse transcription in vivo by elevated manganese ion concentration. Mol. Cell 9:879- 889.
    • (2002) Mol. Cell , vol.9 , pp. 879-889
    • Bolton, E.C.1    Mildvan, A.S.2    Boeke, J.D.3
  • 55
    • 0026699945 scopus 로고
    • Regulation of cell magnesium
    • Romani A, Scarpa A. 1992. Regulation of cell magnesium. Arch. Biochem. Biophys. 298:1-12. 56. Berdis AJ, McCutcheon D. 2007. The use of non-natural nucleotides to probe template-independent DNA synthesis. Chembiochem 8:1399-1408.
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 1-12
    • Romani, A.1    Scarpa, A.2
  • 56
    • 34548118299 scopus 로고    scopus 로고
    • The use of non-natural nucleotides to probe template-independent DNA synthesis
    • Berdis AJ, McCutcheon D. 2007. The use of non-natural nucleotides to probe template-independent DNA synthesis. Chembiochem 8:1399-1408.
    • (2007) Chembiochem , vol.8 , pp. 1399-1408
    • Berdis, A.J.1    McCutcheon, D.2
  • 57
    • 77949569085 scopus 로고    scopus 로고
    • Terminal deoxynucleotidyl transferase: the story of a misguided DNA polymerase
    • Motea EA, Berdis AJ. 2010. Terminal deoxynucleotidyl transferase: the story of a misguided DNA polymerase. Biochim. Biophys. Acta 1804: 1151-1166.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1151-1166
    • Motea, E.A.1    Berdis, A.J.2
  • 59
    • 0023734473 scopus 로고
    • Novel non-templated nucleotide addition reactions catalyzed by procaryotic and eucaryotic DNA polymerases
    • Clark JM. 1988. Novel non-templated nucleotide addition reactions catalyzed by procaryotic and eucaryotic DNA polymerases. Nucleic Acids Res. 16:9677-9686.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9677-9686
    • Clark, J.M.1
  • 60
    • 0028088986 scopus 로고
    • Marked infidelity of human immunodeficiency virus type 1 reverse transcriptase at RNA and DNA template ends
    • Patel PH, Preston BD. 1994. Marked infidelity of human immunodeficiency virus type 1 reverse transcriptase at RNA and DNA template ends. Proc. Natl. Acad. Sci. U. S. A. 91:549-553.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 549-553
    • Patel, P.H.1    Preston, B.D.2
  • 61
    • 50949083564 scopus 로고    scopus 로고
    • Nontemplated terminal nucleotidyltransferase activity of double-stranded RNA bacteriophage phi6 RNA-dependent RNA polymerase
    • Poranen MM, Koivunen MR, Bamford DH. 2008. Nontemplated terminal nucleotidyltransferase activity of double-stranded RNA bacteriophage phi6 RNA-dependent RNA polymerase. J. Virol. 82:9254-9264.
    • (2008) J. Virol. , vol.82 , pp. 9254-9264
    • Poranen, M.M.1    Koivunen, M.R.2    Bamford, D.H.3
  • 62
    • 0034881065 scopus 로고    scopus 로고
    • Terminal nucleotidyl transferase activity of recombinant Flaviviridae RNA-dependentRNApolymerases: implication for viralRNAsynthesis
    • Ranjith-Kumar CT, Gajewski J, Gutshall L, Maley D, Sarisky RT, Kao CC. 2001. Terminal nucleotidyl transferase activity of recombinant Flaviviridae RNA-dependentRNApolymerases: implication for viralRNAsynthesis. J. Virol. 75:8615- 8623.
    • (2001) J. Virol. , vol.75 , pp. 8615-8623
    • Ranjith-Kumar, C.T.1    Gajewski, J.2    Gutshall, L.3    Maley, D.4    Sarisky, R.T.5    Kao, C.C.6
  • 63
    • 0017840927 scopus 로고
    • Biochemistry of terminal deoxynucleotidyltransferase: mechanism of inhibition by adenosine 5'-triphosphate
    • Modak MJ. 1978. Biochemistry of terminal deoxynucleotidyltransferase: mechanism of inhibition by adenosine 5'-triphosphate. Biochemistry 17: 3116-3120.
    • (1978) Biochemistry , vol.17 , pp. 3116-3120
    • Modak, M.J.1
  • 64
    • 80053182210 scopus 로고    scopus 로고
    • A reverse transcriptase-related protein mediates phage resistance and polymerizes untemplated DNA in vitro
    • Wang C, Villion M, Semper C, Coros C, Moineau S, Zimmerly S. 2011. A reverse transcriptase-related protein mediates phage resistance and polymerizes untemplated DNA in vitro. Nucleic Acids Res. 39: 7620-7629.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 7620-7629
    • Wang, C.1    Villion, M.2    Semper, C.3    Coros, C.4    Moineau, S.5    Zimmerly, S.6
  • 65
    • 0027167557 scopus 로고
    • An RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation
    • Pollack JR, Ganem D. 1993. An RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation. J. Virol. 67:3254-3263.
    • (1993) J. Virol. , vol.67 , pp. 3254-3263
    • Pollack, J.R.1    Ganem, D.2
  • 66
    • 0028095240 scopus 로고
    • Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis
    • Pollack JR, Ganem D. 1994. Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis. J. Virol. 68:5579-5587.
    • (1994) J. Virol. , vol.68 , pp. 5579-5587
    • Pollack, J.R.1    Ganem, D.2
  • 67
    • 33646205969 scopus 로고    scopus 로고
    • Base pairing between the 5' half of epsilon and a cis-acting sequence, phi, makes a contribution to the synthesis of minus-strand DNA for human hepatitis B virus
    • Abraham TM, Loeb DD. 2006. Base pairing between the 5' half of epsilon and a cis-acting sequence, phi, makes a contribution to the synthesis of minus-strand DNA for human hepatitis B virus. J. Virol. 80:4380- 4387.
    • (2006) J. Virol. , vol.80 , pp. 4380-4387
    • Abraham, T.M.1    Loeb, D.D.2
  • 68
    • 66149123741 scopus 로고    scopus 로고
    • Direct detection of abortive RNA transcripts in vivo
    • Goldman SR, Ebright RH, Nickels BE. 2009. Direct detection of abortive RNA transcripts in vivo. Science 324:927-928.
    • (2009) Science , vol.324 , pp. 927-928
    • Goldman, S.R.1    Ebright, R.H.2    Nickels, B.E.3
  • 69
    • 33746303519 scopus 로고    scopus 로고
    • An 8 nt RNA triggers a rate-limiting shift of RNA polymerase II complexes into elongation
    • Hieb AR, Baran S, Goodrich JA, Kugel JF. 2006. An 8 nt RNA triggers a rate-limiting shift of RNA polymerase II complexes into elongation. EMBO J. 25:3100-3109.
    • (2006) EMBO J. , vol.25 , pp. 3100-3109
    • Hieb, A.R.1    Baran, S.2    Goodrich, J.A.3    Kugel, J.F.4
  • 70
    • 33645303495 scopus 로고    scopus 로고
    • The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition
    • Kamtekar S, Berman AJ, Wang J, Lazaro JM, de Vega M, Blanco L, Salas M, Steitz TA. 2006. The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition. EMBO J. 25: 1335-1343.
    • (2006) EMBO J. , vol.25 , pp. 1335-1343
    • Kamtekar, S.1    Berman, A.J.2    Wang, J.3    Lazaro, J.M.4    de Vega, M.5    Blanco, L.6    Salas, M.7    Steitz, T.A.8
  • 71
    • 78650566210 scopus 로고    scopus 로고
    • Pol II waiting in the starting gates: regulating the transition from transcription initiation into productive elongation
    • Nechaev S, Adelman K. 2011. Pol II waiting in the starting gates: regulating the transition from transcription initiation into productive elongation. Biochim. Biophys. Acta 1809:34-45.
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 34-45
    • Nechaev, S.1    Adelman, K.2
  • 72
    • 33747621427 scopus 로고    scopus 로고
    • Visualizing polynucleotide polymerase machines at work
    • Steitz TA. 2006. Visualizing polynucleotide polymerase machines at work. EMBO J. 25:3458-3468.
    • (2006) EMBO J. , vol.25 , pp. 3458-3468
    • Steitz, T.A.1
  • 73
    • 79960134404 scopus 로고    scopus 로고
    • Phosphonoformic acid inhibits viral replication by trapping the closed form of the DNA polymerase
    • Zahn KE, Tchesnokov EP, Gotte M, Doublie S. 2011. Phosphonoformic acid inhibits viral replication by trapping the closed form of the DNA polymerase. J. Biol. Chem. 286:25246-25255.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25246-25255
    • Zahn, K.E.1    Tchesnokov, E.P.2    Gotte, M.3    Doublie, S.4
  • 74
    • 0037732696 scopus 로고    scopus 로고
    • Human DNA polymerase lambda diverged in evolution from DNA polymerase beta toward specific Mn(++) dependence: a kinetic and thermodynamic study
    • Blanca G, Shevelev I, Ramadan K, Villani G, Spadari S, Hubscher U, Maga G. 2003. Human DNA polymerase lambda diverged in evolution from DNA polymerase beta toward specific Mn(++) dependence: a kinetic and thermodynamic study. Biochemistry 42:7467-7476.
    • (2003) Biochemistry , vol.42 , pp. 7467-7476
    • Blanca, G.1    Shevelev, I.2    Ramadan, K.3    Villani, G.4    Spadari, S.5    Hubscher, U.6    Maga, G.7
  • 75
    • 0027164918 scopus 로고
    • Recombinant human hepatitis B virus reverse transcriptase is active in the absence of the nucleocapsid or the viral replication origin, DR1
    • Seifer M, Standring DN. 1993. Recombinant human hepatitis B virus reverse transcriptase is active in the absence of the nucleocapsid or the viral replication origin, DR1. J. Virol. 67:4513- 4520.
    • (1993) J. Virol. , vol.67 , pp. 4513-4520
    • Seifer, M.1    Standring, D.N.2
  • 76
    • 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.
    • (2007) Virus Res. , vol.127 , pp. 164-176
    • Kay, A.1    Zoulim, F.2
  • 77
    • 0028946153 scopus 로고
    • A unique insertion in the S gene of surface antigen-negative hepatitis B virus Chinese carriers
    • Hou J, Karayiannis P, Waters J, Luo K, Liang C, Thomas HC. 1995. A unique insertion in the S gene of surface antigen-negative hepatitis B virus Chinese carriers. Hepatology 21:273-278.
    • (1995) Hepatology , vol.21 , pp. 273-278
    • Hou, J.1    Karayiannis, P.2    Waters, J.3    Luo, K.4    Liang, C.5    Thomas, H.C.6
  • 78
    • 7444263584 scopus 로고    scopus 로고
    • Detection and characterization of cytoplasmic hepatitis B virus reverse transcriptase
    • Cao F, Tavis JE. 2004. Detection and characterization of cytoplasmic hepatitis B virus reverse transcriptase. J. Gen. Virol. 85:3353-3360.
    • (2004) J. Gen. Virol. , vol.85 , pp. 3353-3360
    • Cao, F.1    Tavis, J.E.2
  • 79
    • 0033851105 scopus 로고    scopus 로고
    • The majority of duck hepatitis B virus reverse transcriptase in cells is nonencapsidated and is bound to a cytoplasmic structure
    • Yao E, Gong Y, Chen N, Tavis JE. 2000. The majority of duck hepatitis B virus reverse transcriptase in cells is nonencapsidated and is bound to a cytoplasmic structure. J. Virol. 74:8648-8657.
    • (2000) J. Virol. , vol.74 , pp. 8648-8657
    • Yao, E.1    Gong, Y.2    Chen, N.3    Tavis, J.E.4
  • 80
    • 2642561273 scopus 로고    scopus 로고
    • Localization of duck hepatitis B virus polymerase within cells
    • Yao E, Tavis JE. 2004. Localization of duck hepatitis B virus polymerase within cells. Methods Mol. Med. 95:281-293.
    • (2004) Methods Mol. Med. , vol.95 , pp. 281-293
    • Yao, E.1    Tavis, J.E.2
  • 81
    • 79954423286 scopus 로고    scopus 로고
    • Adenylylation: renaissance of a forgotten post-translational modification
    • Itzen A, Blankenfeldt W, Goody RS. 2011. Adenylylation: renaissance of a forgotten post-translational modification. Trends Biochem. Sci. 36:221- 228.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 221-228
    • Itzen, A.1    Blankenfeldt, W.2    Goody, R.S.3


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