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Volumn 235, Issue 1, 1997, Pages 144-152

Sequence-specific repression of cotranslational translocation of the hepatitis B virus envelope proteins coincides with binding of heat shock protein Hsc70

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; HEAT SHOCK PROTEIN 70;

EID: 0038547688     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8689     Document Type: Article
Times cited : (49)

References (31)
  • 1
    • 85047669331 scopus 로고    scopus 로고
    • Post-translational protein translocation: Not all hsc70s are created equal
    • Brodsky J. L. Post-translational protein translocation: Not all hsc70s are created equal. Trends Biochem. Sci. 21:1996;122-126.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 122-126
    • Brodsky, J.L.1
  • 2
    • 0026034960 scopus 로고
    • The role of envelope proteins in hepatitis B virus assembly
    • Bruss V., Ganem D. The role of envelope proteins in hepatitis B virus assembly. Proc. Natl. Acad. Sci. USA. 88:1991;1059-1063.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1059-1063
    • Bruss, V.1    Ganem, D.2
  • 3
    • 0028236042 scopus 로고
    • Post-translational alterations in transmembrane topology of the hepatitis B large envelope protein
    • Bruss V., Lu X., Thomssen R., Gerlich W. H. Post-translational alterations in transmembrane topology of the hepatitis B large envelope protein. EMBO J. 13:1994;2273-2279.
    • (1994) EMBO J. , vol.13 , pp. 2273-2279
    • Bruss, V.1    Lu, X.2    Thomssen, R.3    Gerlich, W.H.4
  • 4
    • 0028013056 scopus 로고
    • Mapping a region of the large envelope protein required for hepatitis B virion maturation
    • Bruss V., Thomssen R. Mapping a region of the large envelope protein required for hepatitis B virion maturation. J. Virol. 68:1994;1643-1650.
    • (1994) J. Virol. , vol.68 , pp. 1643-1650
    • Bruss, V.1    Thomssen, R.2
  • 5
    • 0028874697 scopus 로고
    • Functions of the internal pre-S domain of the large surface protein in hepatitis B virus particle morphogenesis
    • Bruss V., Vieluf K. Functions of the internal pre-S domain of the large surface protein in hepatitis B virus particle morphogenesis. J. Virol. 69:1995;6652-6657.
    • (1995) J. Virol. , vol.69 , pp. 6652-6657
    • Bruss, V.1    Vieluf, K.2
  • 6
    • 0030457399 scopus 로고    scopus 로고
    • The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation
    • Bush G. L., Meyer D. I. The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J. Cell Biol. 135:1996;1229-1237.
    • (1996) J. Cell Biol. , vol.135 , pp. 1229-1237
    • Bush, G.L.1    Meyer, D.I.2
  • 7
    • 0028849795 scopus 로고
    • In vivo and in vitro association of hsc70 with polyomavirus capsid proteins
    • Cripe T. P., Delos S. E., Estes P. A., Garcea R. L. In vivo and in vitro association of hsc70 with polyomavirus capsid proteins. J. Virol. 69:1995;7807-7813.
    • (1995) J. Virol. , vol.69 , pp. 7807-7813
    • Cripe, T.P.1    Delos, S.E.2    Estes, P.A.3    Garcea, R.L.4
  • 8
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies R. J., Koch B. D., Werner-Washburne M., Craig E. A., Schekman R. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature. 332:1988;800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 9
    • 0028928193 scopus 로고
    • Selection of peptide inhibitors of interaction involved in complex protein assemblies: Association of the core and surface antigens of hepatitis B virus
    • Dyson M. R., Murray K. Selection of peptide inhibitors of interaction involved in complex protein assemblies: Association of the core and surface antigens of hepatitis B virus. Proc. Natl. Acad. Sci. USA. 92:1995;2194-2198.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2194-2198
    • Dyson, M.R.1    Murray, K.2
  • 10
    • 0025219320 scopus 로고
    • The N-terminal (preS2) domain of a hepatitis B virus surface glycoprotein is translocated across membranes by downstream signal sequences
    • Eble B. E., Lingappa V. R., Ganem D. The N-terminal (preS2) domain of a hepatitis B virus surface glycoprotein is translocated across membranes by downstream signal sequences. J. Virol. 64:1990;1414-1419.
    • (1990) J. Virol. , vol.64 , pp. 1414-1419
    • Eble, B.E.1    Lingappa, V.R.2    Ganem, D.3
  • 11
    • 0023428332 scopus 로고
    • Multiple topogenic sequences determine the transmembrane orientation of hepatitis B surface antigen
    • Eble B. E., Macrae D. R., Lingappa V. R., Ganem D. Multiple topogenic sequences determine the transmembrane orientation of hepatitis B surface antigen. Mol. Cell. Biol. 7:1987;3591-3601.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3591-3601
    • Eble, B.E.1    Macrae, D.R.2    Lingappa, V.R.3    Ganem, D.4
  • 12
    • 0028788489 scopus 로고
    • A C-terminal preS1 sequence is sufficient to retain hepatitis B virus L protein in 293 Cells
    • Gallina A., Gazina E., Milanesi G. A C-terminal preS1 sequence is sufficient to retain hepatitis B virus L protein in 293 Cells. Virology. 213:1995;57-69.
    • (1995) Virology , vol.213 , pp. 57-69
    • Gallina, A.1    Gazina, E.2    Milanesi, G.3
  • 13
    • 0028037170 scopus 로고
    • The large surface protein of duck hepatitis B virus is phosphorylated in the pre-S domain
    • Grgacic E. V. L., Anderson D. A. The large surface protein of duck hepatitis B virus is phosphorylated in the pre-S domain. J. Virol. 68:1994;7344-7350.
    • (1994) J. Virol. , vol.68 , pp. 7344-7350
    • Grgacic, E.V.L.1    Anderson, D.A.2
  • 15
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick J. P., Hartl F.-U. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62:1993;349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 16
    • 0030296929 scopus 로고    scopus 로고
    • The hepatitis B virus large surface protein (LHBs) is a transcriptional activator
    • Hildt E., Saher G., Bruss V., Hofschneider P. H. The hepatitis B virus large surface protein (LHBs) is a transcriptional activator. Virology. 225:1996;235-239.
    • (1996) Virology , vol.225 , pp. 235-239
    • Hildt, E.1    Saher, G.2    Bruss, V.3    Hofschneider, P.H.4
  • 17
    • 0026658183 scopus 로고
    • Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment
    • Huovila A.-P. J., Eder A. M., Fuller S. D. Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment. J. Cell Biol. 118:1992;1305-1320.
    • (1992) J. Cell Biol. , vol.118 , pp. 1305-1320
    • Huovila A.-P., J.1    Eder, A.M.2    Fuller, S.D.3
  • 18
    • 0022538381 scopus 로고
    • Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus
    • Neurath A. R., Kent S. B. H., Strick N., Parker K. Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell. 46:1986;429-436.
    • (1986) Cell , vol.46 , pp. 429-436
    • Neurath, A.R.1    Kent, S.B.H.2    Strick, N.3    Parker, K.4
  • 19
    • 0028265897 scopus 로고
    • A dramatic shift in the transmembrane topology of a viral envelope glycoprotein accompanies hepatitis B viral morphogenesis
    • Ostapchuk P., Hearing P., Ganem D. A dramatic shift in the transmembrane topology of a viral envelope glycoprotein accompanies hepatitis B viral morphogenesis. EMBO J. 13:1994;1048-1057.
    • (1994) EMBO J. , vol.13 , pp. 1048-1057
    • Ostapchuk, P.1    Hearing, P.2    Ganem, D.3
  • 20
    • 0023094424 scopus 로고
    • Regulation of secretion of the hepatitis B virus major surface antigen by the preS-1 protein
    • Ou J.-H., Rutter W. J. Regulation of secretion of the hepatitis B virus major surface antigen by the preS-1 protein. J. Virol. 61:1987;782-786.
    • (1987) J. Virol. , vol.61 , pp. 782-786
    • Ou, J.-H.1    Rutter, W.J.2
  • 21
    • 0025864197 scopus 로고
    • Myristylation is involved in intracellular retention of hepatitis B virus envelope proteins
    • Prange R., Clemen A., Streeck R. E. Myristylation is involved in intracellular retention of hepatitis B virus envelope proteins. J. Virol. 65:1991;3919-3923.
    • (1991) J. Virol. , vol.65 , pp. 3919-3923
    • Prange, R.1    Clemen, A.2    Streeck, R.E.3
  • 22
    • 0028859149 scopus 로고
    • Novel transmembrane topology of the hepatitis B virus envelope proteins
    • Prange R., Streeck R. E. Novel transmembrane topology of the hepatitis B virus envelope proteins. EMBO J. 14:1995;247-256.
    • (1995) EMBO J. , vol.14 , pp. 247-256
    • Prange, R.1    Streeck, R.E.2
  • 23
    • 0029085840 scopus 로고
    • Properties of modified hepatitis B virus surface antigen particles carrying preS epitopes
    • Prange R., Werr M., Birkner M., Hilfrich R., Streeck R. E. Properties of modified hepatitis B virus surface antigen particles carrying preS epitopes. J. Gen. Virol. 76:1995;2131-2140.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2131-2140
    • Prange, R.1    Werr, M.2    Birkner, M.3    Hilfrich, R.4    Streeck, R.E.5
  • 24
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • Rothman J. E. Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells. Cell. 59:1989;591-601.
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothman, J.E.1
  • 25
    • 0026675014 scopus 로고
    • Identification of heat shock protein 70 in rabies virion
    • Sagara J., Kawai A. Identification of heat shock protein 70 in rabies virion. Virology. 190:1992;845-848.
    • (1992) Virology , vol.190 , pp. 845-848
    • Sagara, J.1    Kawai, A.2
  • 26
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon S. M., Blobel G. A protein-conducting channel in the endoplasmic reticulum. Cell. 65:1991;371-380.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 27
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed inEscherichia coliS
    • Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed inEscherichia coliS. Gene. 67:1988;31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 28
    • 0025334855 scopus 로고
    • Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification
    • Summers J., Smith P. M., Horwich A. L. Hepadnavirus envelope proteins regulate covalently closed circular DNA amplification. J. Virol. 64:1990;2819-2824.
    • (1990) J. Virol. , vol.64 , pp. 2819-2824
    • Summers, J.1    Smith, P.M.2    Horwich, A.L.3
  • 29
    • 85030295111 scopus 로고    scopus 로고
    • I. Swameye, C. Kuhn, M. Hild, U. Klingmüller, H. Schaller
    • I. Swameye, C. Kuhn, M. Hild, U. Klingmüller, H. Schaller.
  • 30
    • 0025879364 scopus 로고
    • Three envelope proteins of hepatitis B virus: Large S, middle S, and major S proteins needed for the formation of Dane particles
    • Ueda K. L., Tsurimoto T., Matsubara K. Three envelope proteins of hepatitis B virus: Large S, middle S, and major S proteins needed for the formation of Dane particles. J. Virol. 65:1991;3521-3529.
    • (1991) J. Virol. , vol.65 , pp. 3521-3529
    • Ueda, K.L.1    Tsurimoto, T.2    Matsubara, K.3
  • 31
    • 0024077833 scopus 로고
    • Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes
    • Zimmermann R., Sagstetter M., Lewis M. J., Pelham H. R. B. Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes. EMBO J. 7:1988;2875-2880.
    • (1988) EMBO J. , vol.7 , pp. 2875-2880
    • Zimmermann, R.1    Sagstetter, M.2    Lewis, M.J.3    Pelham, H.R.B.4


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