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Volumn 390, Issue 1, 2009, Pages 130-138

An interdomain RNA binding site on the hepadnaviral polymerase that is essential for reverse transcription

Author keywords

Hepadnavirus; Hepatitis B virus; Reverse transcriptase; Reverse transcription; RNA binding

Indexed keywords

RNA DIRECTED DNA POLYMERASE; VIRUS DNA; VIRUS RNA;

EID: 67649479264     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.04.023     Document Type: Article
Times cited : (26)

References (50)
  • 1
    • 33749541260 scopus 로고    scopus 로고
    • Combining genetic and biochemical approaches to identify functional molecular contact points
    • Badtke M.P., Cao F., and Tavis J.E. Combining genetic and biochemical approaches to identify functional molecular contact points. Biol. Proced. Online 8 (2006) 77-86
    • (2006) Biol. Proced. Online , vol.8 , pp. 77-86
    • Badtke, M.P.1    Cao, F.2    Tavis, J.E.3
  • 2
    • 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., and Schaller H. The P gene product of hepatitis B virus is required as a structural component for genomic RNA encapsidation. J. Virol. 64 (1990) 5324-5332
    • (1990) J. Virol. , vol.64 , pp. 5324-5332
    • Bartenschlager, R.1    Junker-Niepmann, M.2    Schaller, H.3
  • 3
    • 33646369149 scopus 로고    scopus 로고
    • Antiviral drug resistance: clinical consequences and molecular aspects
    • Bartholomeusz A., and Locarnini S.A. Antiviral drug resistance: clinical consequences and molecular aspects. Semin. Liver Dis. 26 (2006) 162-170
    • (2006) Semin. Liver Dis. , vol.26 , pp. 162-170
    • Bartholomeusz, A.1    Locarnini, S.A.2
  • 4
    • 2342433984 scopus 로고    scopus 로고
    • Comparisons of the HBV and HIV polymerase, and antiviral resistance mutations
    • Bartholomeusz A., Tehan B.G., and Chalmers D.K. Comparisons of the HBV and HIV polymerase, and antiviral resistance mutations. Antivir. Ther. 9 (2004) 149-160
    • (2004) Antivir. Ther. , vol.9 , pp. 149-160
    • Bartholomeusz, A.1    Tehan, B.G.2    Chalmers, D.K.3
  • 5
    • 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., and Nassal M. Sequence- and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B viruses. J. Virol. 71 (1997) 4971-4980
    • (1997) J. Virol. , vol.71 , pp. 4971-4980
    • Beck, J.1    Nassal, M.2
  • 6
    • 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., and Nassal M. Formation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template. Mol. Cell Biol. 18 (1998) 6265-6272
    • (1998) Mol. Cell Biol. , vol.18 , pp. 6265-6272
    • Beck, J.1    Nassal, M.2
  • 7
    • 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., and Nassal M. 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 (2003) 36128-36138
    • (2003) J. Biol. Chem. , vol.278 , pp. 36128-36138
    • Beck, J.1    Nassal, M.2
  • 8
    • 23244462337 scopus 로고    scopus 로고
    • Identification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptase
    • Cao F., Badtke M.P., Metzger L.M., Yao E., Adeyemo B., Gong Y.H., and Tavis J.E. Identification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptase. J. Virol. 79 (2005) 10164-10170
    • (2005) J. Virol. , vol.79 , pp. 10164-10170
    • Cao, F.1    Badtke, M.P.2    Metzger, L.M.3    Yao, E.4    Adeyemo, B.5    Gong, Y.H.6    Tavis, J.E.7
  • 9
    • 0025076858 scopus 로고
    • Effects of insertional and point mutations on the functions of the duck hepatitis B virus polymerase
    • Chang L.J., Hirsch R.C., Ganem D., and Varmus H.E. Effects of insertional and point mutations on the functions of the duck hepatitis B virus polymerase. J. Virol. 64 (1990) 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
  • 10
    • 0035041976 scopus 로고    scopus 로고
    • Molecular modeling and biochemical characterization reveal the mechanism of hepatitis B virus polymerase resistance to lamivudine (3TC) and emtricitabine (FTC)
    • Das K., Xiong X., Yang H., Westland C.E., Gibbs C.S., Sarafianos S.G., and Arnold E. Molecular modeling and biochemical characterization reveal the mechanism of hepatitis B virus polymerase resistance to lamivudine (3TC) and emtricitabine (FTC). J. Virol. 75 (2001) 4771-4779
    • (2001) J. Virol. , vol.75 , pp. 4771-4779
    • Das, K.1    Xiong, X.2    Yang, H.3    Westland, C.E.4    Gibbs, C.S.5    Sarafianos, S.G.6    Arnold, E.7
  • 12
    • 0032902564 scopus 로고    scopus 로고
    • Characterization of soluble hepatitis C virus RNA dependent RNA polymerase expressed in Escherichia coli
    • Ferrari E., Wright-Minogue J., Fang J.W.S., Baroudy B.M., Lau J.Y.N., and Hong Z. Characterization of soluble hepatitis C virus RNA dependent RNA polymerase expressed in Escherichia coli. J. Virol. 73 (1999) 1649-1654
    • (1999) J. Virol. , vol.73 , pp. 1649-1654
    • Ferrari, E.1    Wright-Minogue, J.2    Fang, J.W.S.3    Baroudy, B.M.4    Lau, J.Y.N.5    Hong, Z.6
  • 13
    • 34247222010 scopus 로고    scopus 로고
    • Drug targets and molecular mechanisms of drug resistance in chronic hepatitis B
    • Ghany M., and Liang T.J. Drug targets and molecular mechanisms of drug resistance in chronic hepatitis B. Gastroenterology 132 (2007) 1574-1585
    • (2007) Gastroenterology , vol.132 , pp. 1574-1585
    • Ghany, M.1    Liang, T.J.2
  • 14
    • 13944282885 scopus 로고    scopus 로고
    • Identification and characterization of avihepadnaviruses isolated from exotic anseriformes maintained in captivity
    • Guo H., Mason W.S., Aldrich C.E., Saputelli J.R., Miller D.S., Jilbert A.R., and Newbold J.E. Identification and characterization of avihepadnaviruses isolated from exotic anseriformes maintained in captivity. J. Virol. 79 (2005) 2729-2742
    • (2005) J. Virol. , vol.79 , pp. 2729-2742
    • Guo, H.1    Mason, W.S.2    Aldrich, C.E.3    Saputelli, J.R.4    Miller, D.S.5    Jilbert, A.R.6    Newbold, J.E.7
  • 15
    • 0025238448 scopus 로고
    • Polymerase gene products of hepatitis B viruses are required for genomic RNA packaging as well as for reverse transcription
    • Hirsch R.C., Lavine J.E., Chang L.J., Varmus H.E., and Ganem D. Polymerase gene products of hepatitis B viruses are required for genomic RNA packaging as well as for reverse transcription. Nature (London) 344 (1990) 552-555
    • (1990) Nature (London) , vol.344 , pp. 552-555
    • Hirsch, R.C.1    Lavine, J.E.2    Chang, L.J.3    Varmus, H.E.4    Ganem, D.5
  • 16
    • 0034468780 scopus 로고    scopus 로고
    • In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by HSP90
    • Hu J., and Anselmo D. In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by HSP90. J. Virol. 74 (2000) 11447-11455
    • (2000) J. Virol. , vol.74 , pp. 11447-11455
    • Hu, J.1    Anselmo, D.2
  • 17
    • 33144476637 scopus 로고    scopus 로고
    • Hepatitis B virus reverse transcriptase and epsilon RNA sequences required for specific interaction in vitro
    • Hu J., and Boyer M. Hepatitis B virus reverse transcriptase and epsilon RNA sequences required for specific interaction in vitro. J. Virol. 80 (2006) 2141-2150
    • (2006) J. Virol. , vol.80 , pp. 2141-2150
    • Hu, J.1    Boyer, M.2
  • 18
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu J., and Seeger C. Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 1060-1064
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 19
    • 0031018112 scopus 로고    scopus 로고
    • Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
    • Hu J., Toft D.O., and Seeger C. Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO J. 16 (1997) 59-68
    • (1997) EMBO J. , vol.16 , pp. 59-68
    • Hu, J.1    Toft, D.O.2    Seeger, C.3
  • 20
    • 0036133258 scopus 로고    scopus 로고
    • In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins
    • Hu J., Toft D., Anselmo D., and Wang X. In vitro reconstitution of functional hepadnavirus reverse transcriptase with cellular chaperone proteins. J. Virol. 76 (2002) 269-279
    • (2002) J. Virol. , vol.76 , pp. 269-279
    • Hu, J.1    Toft, D.2    Anselmo, D.3    Wang, X.4
  • 21
    • 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., and Nguyen D. Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J. Virol. 78 (2004) 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
  • 22
    • 0025045477 scopus 로고
    • A short cis-acting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA
    • Junker-Niepmann M., Bartenschlager R., and Schaller H. A short cis-acting sequence is required for hepatitis B virus pregenome encapsidation and sufficient for packaging of foreign RNA. EMBO J. 9 (1990) 3389-3396
    • (1990) EMBO J. , vol.9 , pp. 3389-3396
    • Junker-Niepmann, M.1    Bartenschlager, R.2    Schaller, H.3
  • 23
    • 0026031446 scopus 로고
    • Epitope Tagging and Protein Surveillance
    • Kolodziej P.A., and Young R.A. Epitope Tagging and Protein Surveillance. Methods Enzymol. 194 (1991) 508-519
    • (1991) Methods Enzymol. , vol.194 , pp. 508-519
    • Kolodziej, P.A.1    Young, R.A.2
  • 24
    • 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 R.E., Notvall L., Lee H., and Beams B. Transcomplementation of nucleotide priming and reverse transcription between independently expressed TP and RT domains of the hepatitis B virus reverse transcriptase. J. Virol. 71 (1997) 2996-3004
    • (1997) J. Virol. , vol.71 , pp. 2996-3004
    • Lanford, R.E.1    Notvall, L.2    Lee, H.3    Beams, B.4
  • 25
    • 0032510691 scopus 로고    scopus 로고
    • Isolation of a hepadnavirus from the woolly monkey, a New World primate
    • Lanford R.E., Chavez D., Brasky K.M., Burns III R.B., and Rico-Hesse R. Isolation of a hepadnavirus from the woolly monkey, a New World primate. PNAS 95 (1998) 5757-5761
    • (1998) PNAS , vol.95 , pp. 5757-5761
    • Lanford, R.E.1    Chavez, D.2    Brasky, K.M.3    Burns III, R.B.4    Rico-Hesse, R.5
  • 26
    • 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 R.E., Kim Y.H., Lee H., Notvall L., and Beames B. 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 (1999) 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
  • 28
    • 39749175026 scopus 로고    scopus 로고
    • Inhibition of hepadnavirus reverse transcriptase-epsilon RNA interaction by porphyrin compounds
    • Lin L., and Hu J. Inhibition of hepadnavirus reverse transcriptase-epsilon RNA interaction by porphyrin compounds. J. Virol. 82 (2008) 2305-2312
    • (2008) J. Virol. , vol.82 , pp. 2305-2312
    • Lin, L.1    Hu, J.2
  • 29
    • 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., and Hu J. Functional and structural dynamics of hepadnavirus reverse transcriptase during protein-primed initiation of reverse transcription: effects of metal ions. J. Virol. 82 (2008) 5703-5714
    • (2008) J. Virol. , vol.82 , pp. 5703-5714
    • Lin, L.1    Wan, F.2    Hu, J.3
  • 30
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch O., Sauvaget I., Delarue M., and Tordo N. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J. 8 (1989) 3867-3874
    • (1989) EMBO J. , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 31
    • 0028095240 scopus 로고
    • Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis
    • Pollack J.R., and Ganem D. Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis. J. Virol. 68 (1994) 5579-5587
    • (1994) J. Virol. , vol.68 , pp. 5579-5587
    • Pollack, J.R.1    Ganem, D.2
  • 32
    • 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 D.L., and Russo A. 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 (2007) 93-99
    • (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
  • 33
    • 0023972489 scopus 로고
    • The duck hepatitis B virus DNA polymerase is tightly associated with the viral core structure and unable to switch to an exogenous template
    • Radziwill G., Zentgraf H., Schaller H., and Bosch V. The duck hepatitis B virus DNA polymerase is tightly associated with the viral core structure and unable to switch to an exogenous template. Virology 163 (1988) 123-132
    • (1988) Virology , vol.163 , pp. 123-132
    • Radziwill, G.1    Zentgraf, H.2    Schaller, H.3    Bosch, V.4
  • 34
    • 0025061039 scopus 로고
    • Mutational analysis of the hepatitis B virus P gene product: domain structure and RNase H activity
    • Radziwill G., Tucker W., and Schaller H. Mutational analysis of the hepatitis B virus P gene product: domain structure and RNase H activity. J. Virol. 64 (1990) 613-620
    • (1990) J. Virol. , vol.64 , pp. 613-620
    • Radziwill, G.1    Tucker, W.2    Schaller, H.3
  • 36
    • 0030586781 scopus 로고    scopus 로고
    • Mutagenesis of a hepatitis B virus reverse transcriptase yields temperature-sensitive virus
    • Seeger C., Leber E.H., Wiens L.K., and Hu J. Mutagenesis of a hepatitis B virus reverse transcriptase yields temperature-sensitive virus. Virology 222 (1996) 430-439
    • (1996) Virology , vol.222 , pp. 430-439
    • Seeger, C.1    Leber, E.H.2    Wiens, L.K.3    Hu, J.4
  • 37
    • 34547755447 scopus 로고    scopus 로고
    • Hepadnaviruses
    • Knipe D.M., Howley P., Griffin D.E., Lamb R.A., Martin A., Roizman B., and Straus S.E. (Eds), Lippincott Williams and Wilkins, Philadelphia
    • Seeger C., Zoulim F., and Mason W.S. Hepadnaviruses. In: Knipe D.M., Howley P., Griffin D.E., Lamb R.A., Martin A., Roizman B., and Straus S.E. (Eds). Fields Virology (2007), Lippincott Williams and Wilkins, Philadelphia 2977-3029
    • (2007) Fields Virology , pp. 2977-3029
    • Seeger, C.1    Zoulim, F.2    Mason, W.S.3
  • 39
    • 0021924489 scopus 로고
    • Comparative sequence analysis of duck and human hepatitis B virus genomes
    • Sprengel R., Kuhn C., Will H., and Schaller H. Comparative sequence analysis of duck and human hepatitis B virus genomes. J. Med. Virol. 15 (1985) 323-333
    • (1985) J. Med. Virol. , vol.15 , pp. 323-333
    • Sprengel, R.1    Kuhn, C.2    Will, H.3    Schaller, H.4
  • 40
    • 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., and Nassal M. 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 (2007) 13354-13364
    • (2007) J. Virol. , vol.81 , pp. 13354-13364
    • Stahl, M.1    Beck, J.2    Nassal, M.3
  • 41
    • 0019949367 scopus 로고
    • Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate
    • Summers J., and Mason W.S. Replication of the genome of a hepatitis B-like virus by reverse transcription of an RNA intermediate. Cell 29 (1982) 403-415
    • (1982) Cell , vol.29 , pp. 403-415
    • Summers, J.1    Mason, W.S.2
  • 42
    • 0029833252 scopus 로고    scopus 로고
    • Evidence for the activation of the hepatitis B virus polymerase by binding of its RNA template
    • Tavis J.E., and Ganem D. Evidence for the activation of the hepatitis B virus polymerase by binding of its RNA template. J. Virol. 70 (1996) 5741-5750
    • (1996) J. Virol. , vol.70 , pp. 5741-5750
    • Tavis, J.E.1    Ganem, D.2
  • 43
    • 0028308495 scopus 로고
    • Hepadnavirus reverse transcription initiates within the stem-loop of the RNA packaging signal and employs a novel strand transfer
    • Tavis J.E., Perri S., and Ganem D. Hepadnavirus reverse transcription initiates within the stem-loop of the RNA packaging signal and employs a novel strand transfer. J. Virol. 68 (1994) 3536-3543
    • (1994) J. Virol. , vol.68 , pp. 3536-3543
    • Tavis, J.E.1    Perri, S.2    Ganem, D.3
  • 44
    • 0031777692 scopus 로고    scopus 로고
    • The duck hepatitis B virus polymerase is activated by its RNA packaging signal, Epsilon
    • Tavis J.E., Massey B., and Gong Y. The duck hepatitis B virus polymerase is activated by its RNA packaging signal, Epsilon. J. Virol. 72 (1998) 5789-5796
    • (1998) J. Virol. , vol.72 , pp. 5789-5796
    • Tavis, J.E.1    Massey, B.2    Gong, Y.3
  • 45
    • 0027494086 scopus 로고
    • Novel mechanism for reverse transcription in hepatitis B viruses
    • Wang G.H., and Seeger C. Novel mechanism for reverse transcription in hepatitis B viruses. J. Virol. 67 (1993) 6507-6512
    • (1993) J. Virol. , vol.67 , pp. 6507-6512
    • Wang, G.H.1    Seeger, C.2
  • 46
    • 0028004062 scopus 로고
    • Role of RNA in enzymatic activity of the reverse transcriptase of hepatitis B viruses
    • Wang G.H., Zoulim F., Leber E.H., Kitson J., and Seeger C. Role of RNA in enzymatic activity of the reverse transcriptase of hepatitis B viruses. J. Virol. 68 (1994) 8437-8442
    • (1994) J. Virol. , vol.68 , pp. 8437-8442
    • Wang, G.H.1    Zoulim, F.2    Leber, E.H.3    Kitson, J.4    Seeger, C.5
  • 47
    • 0345701495 scopus 로고    scopus 로고
    • Heat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase
    • Wang X., Qian X., Guo H.C., and Hu J. Heat shock protein 90-independent activation of truncated hepadnavirus reverse transcriptase. J. Virol. 77 (2003) 4471-4480
    • (2003) J. Virol. , vol.77 , pp. 4471-4480
    • Wang, X.1    Qian, X.2    Guo, H.C.3    Hu, J.4
  • 48
    • 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., and Schaller H. Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription. J. Virol. 68 (1994) 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
  • 49
    • 0025006614 scopus 로고
    • Origin and evolution of retroelements based upon their reverse transcriptase sequences
    • Xiong Y., and Eickbush T.H. Origin and evolution of retroelements based upon their reverse transcriptase sequences. EMBO J. 9 (1990) 3353-3362
    • (1990) EMBO J. , vol.9 , pp. 3353-3362
    • Xiong, Y.1    Eickbush, T.H.2
  • 50
    • 0028091053 scopus 로고
    • Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase
    • Zoulim F., and Seeger C. Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase. J. Virol. 68 (1994) 6-13
    • (1994) J. Virol. , vol.68 , pp. 6-13
    • Zoulim, F.1    Seeger, C.2


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