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Volumn 149, Issue 2, 2010, Pages 241-244

Structural comparisons of hepatitis B core antigen particles with different C-terminal lengths

Author keywords

HBcAg particle; Nuclease sensitivity; RNA encapsidation; Structural comparison

Indexed keywords

HEPATITIS B CORE ANTIGEN; VIRUS RNA;

EID: 77950628777     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2010.01.020     Document Type: Article
Times cited : (14)

References (24)
  • 1
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S.A., Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 1997, 386(6620):88-91.
    • (1997) Nature , vol.386 , Issue.6620 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 2
    • 0027216173 scopus 로고
    • Carboxy-terminal truncations of the HBV core protein affect capsid formation and the apparent size of encapsidated HBV RNA
    • Beames B., Lanford R.E. Carboxy-terminal truncations of the HBV core protein affect capsid formation and the apparent size of encapsidated HBV RNA. Virology 1993, 194(2):597-607.
    • (1993) Virology , vol.194 , Issue.2 , pp. 597-607
    • Beames, B.1    Lanford, R.E.2
  • 3
    • 33846514081 scopus 로고    scopus 로고
    • Hepatitis B virus replication
    • Beck J., Nassal M. Hepatitis B virus replication. World J. Gastroenterol. 2007, 13(1):48-64.
    • (2007) World J. Gastroenterol. , vol.13 , Issue.1 , pp. 48-64
    • Beck, J.1    Nassal, M.2
  • 4
    • 0025316017 scopus 로고
    • Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein
    • Birnbaum F., Nassal M. Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein. J. Virol. 1990, 64(7):3319-3330.
    • (1990) J. Virol. , vol.64 , Issue.7 , pp. 3319-3330
    • Birnbaum, F.1    Nassal, M.2
  • 6
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J.F., Cheng N., Zlotnick A., Wingfield P.T., Stahl S.J., Steven A.C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 1997, 386(6620):91-94.
    • (1997) Nature , vol.386 , Issue.6620 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 7
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis-B virus core particels determined by electron cryomicroscopy
    • Crowther R.A., Kiselev N.A., Bottcher B., Berriman J.A., Borisova G.P., Ose V., Pumpens P. Three-dimensional structure of hepatitis-B virus core particels determined by electron cryomicroscopy. Cell 1994, 77(6):943-950.
    • (1994) Cell , vol.77 , Issue.6 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Bottcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 9
    • 0024474088 scopus 로고
    • A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids
    • Gallina A., Bonelli F., Zentilin L., Rindi G., Muttini M., Milanesi G. A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids. J. Virol. 1989, 63:4645-4652.
    • (1989) J. Virol. , vol.63 , pp. 4645-4652
    • Gallina, A.1    Bonelli, F.2    Zentilin, L.3    Rindi, G.4    Muttini, M.5    Milanesi, G.6
  • 10
    • 0001435504 scopus 로고    scopus 로고
    • Hepadnaviridae and their replication
    • Raven Press, Philadelphia, B.N. Fields, D.M. Knipe, P.M. Howley (Eds.)
    • Ganem D. Hepadnaviridae and their replication. Fields Virology 1996, 2703-2737. Raven Press, Philadelphia. 3rd ed. B.N. Fields, D.M. Knipe, P.M. Howley (Eds.).
    • (1996) Fields Virology , pp. 2703-2737
    • Ganem, D.1
  • 11
    • 0026795429 scopus 로고
    • RNA- and DNA-binding activities in hepatitis B virus capsid protein: a model for their roles in viral replication
    • Hatton T., Zhou S., Standring D.N. RNA- and DNA-binding activities in hepatitis B virus capsid protein: a model for their roles in viral replication. J. Virol. 1992, 66:5232-5241.
    • (1992) J. Virol. , vol.66 , pp. 5232-5241
    • Hatton, T.1    Zhou, S.2    Standring, D.N.3
  • 12
    • 13744260482 scopus 로고    scopus 로고
    • Exposure of RNA templates and encapsidation of spliced viral RNA are influenced by the arginine-rich domain of human hepatitis B virus core antigen (HBcAg 165-173)
    • Le Pogam S., Chua P.K., Newman M., Shih C. Exposure of RNA templates and encapsidation of spliced viral RNA are influenced by the arginine-rich domain of human hepatitis B virus core antigen (HBcAg 165-173). J. Virol. 2005, 79(3):1871-1887.
    • (2005) J. Virol. , vol.79 , Issue.3 , pp. 1871-1887
    • Le Pogam, S.1    Chua, P.K.2    Newman, M.3    Shih, C.4
  • 13
    • 0036420061 scopus 로고    scopus 로고
    • IMIRS: a high-resolution 3D reconstruction package integrated with a relational image database
    • Liang Y., Ke E.Y., Zhou Z.H. IMIRS: a high-resolution 3D reconstruction package integrated with a relational image database. J. Struct. Biol. 2002, 137(3):292-304.
    • (2002) J. Struct. Biol. , vol.137 , Issue.3 , pp. 292-304
    • Liang, Y.1    Ke, E.Y.2    Zhou, Z.H.3
  • 14
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semi-automated software for high resolution single particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semi-automated software for high resolution single particle reconstructions. J. Struct. Biol. 1999, 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 15
    • 0026695732 scopus 로고
    • The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly
    • Nassal M. The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly. J. Virol. 1992, 66(7):4107-4116.
    • (1992) J. Virol. , vol.66 , Issue.7 , pp. 4107-4116
    • Nassal, M.1
  • 16
    • 0344304690 scopus 로고    scopus 로고
    • Stability and morphology comparisons of self-assembled virus-like particles from wild-type and mutant human hepatitis B virus capsid proteins
    • Newman M., Suk F.M., Cajimat M., Chua P.M., Shih C. Stability and morphology comparisons of self-assembled virus-like particles from wild-type and mutant human hepatitis B virus capsid proteins. J. Virol. 2003, 77(24):12950-12960.
    • (2003) J. Virol. , vol.77 , Issue.24 , pp. 12950-12960
    • Newman, M.1    Suk, F.M.2    Cajimat, M.3    Chua, P.M.4    Shih, C.5
  • 20
    • 0028136709 scopus 로고
    • A protease-sensitive hinge linking the two domains of the hepatitis B virus core protein is exposed on the viral capsid surface
    • Seifer M., Standring D.N. A protease-sensitive hinge linking the two domains of the hepatitis B virus core protein is exposed on the viral capsid surface. J. Virol. 1994, 68(9):5548-5555.
    • (1994) J. Virol. , vol.68 , Issue.9 , pp. 5548-5555
    • Seifer, M.1    Standring, D.N.2
  • 21
    • 67649393359 scopus 로고    scopus 로고
    • Electrostatic regulation of genome packaging in human hepatitis B virus
    • Tao J., Zhen-Gang W., Jianzhong W. Electrostatic regulation of genome packaging in human hepatitis B virus. Biophys. J. 2009, 3065-3073.
    • (2009) Biophys. J. , pp. 3065-3073
    • Tao, J.1    Zhen-Gang, W.2    Jianzhong, W.3
  • 22
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly
    • Wingfield P.T., Stahl S.J., Williams R.W., Steven A.C. Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry 1995, 34(15). 4949-4932.
    • (1995) Biochemistry , vol.34 , Issue.15 , pp. 4949-4932
    • Wingfield, P.T.1    Stahl, S.J.2    Williams, R.W.3    Steven, A.C.4
  • 23
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne S.A., Crowther R.A., Leslie A.G. The crystal structure of the human hepatitis B virus capsid. Mol. Cell. 1999, 3(6):771-780.
    • (1999) Mol. Cell. , vol.3 , Issue.6 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 24
    • 0042827239 scopus 로고    scopus 로고
    • Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution
    • Zhou Z.H., Chiu W. Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution. Adv. Protein Chem. 2003, 64:93-124.
    • (2003) Adv. Protein Chem. , vol.64 , pp. 93-124
    • Zhou, Z.H.1    Chiu, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.