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Volumn 79, Issue 11, 1998, Pages 2673-2677

A new cysteine in rotavirus VP4 participates in the formation of an alternate disulfide bond

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; VIRUS PROTEIN;

EID: 0031767619     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/0022-1317-79-11-2673     Document Type: Article
Times cited : (4)

References (22)
  • 1
  • 2
    • 0030998380 scopus 로고    scopus 로고
    • Rotavirus contains integrin ligand sequences and a disintegrin-like domain implicated in virus entry into cells
    • Coulson, B. S., Londrigan, S. H. & Lee, D. J. (1997). Rotavirus contains integrin ligand sequences and a disintegrin-like domain implicated in virus entry into cells. Proceedings of the National Academy of Sciences, USA 94, 5389-5394.
    • (1997) Proceedings of the National Academy of Sciences, USA , vol.94 , pp. 5389-5394
    • Coulson, B.S.1    Londrigan, S.H.2    Lee, D.J.3
  • 3
    • 0026546746 scopus 로고
    • Conserved cysteine residues in the human immunodeficiency virus type 1 transmembrane envelope protein are essential for precursor envelope cleavage
    • Dedera, D., Ruili, G. & Ratner, L. (1992). Conserved cysteine residues in the human immunodeficiency virus type 1 transmembrane envelope protein are essential for precursor envelope cleavage. Journal of Virology 66, 1207-1209.
    • (1992) Journal of Virology , vol.66 , pp. 1207-1209
    • Dedera, D.1    Ruili, G.2    Ratner, L.3
  • 4
    • 0022385153 scopus 로고
    • Interventions for the control of diarrhoeal diseases among young children: Rotavirus and cholera immunization
    • De Zoysa, I. & Feachem, R. G. (1985). Interventions for the control of diarrhoeal diseases among young children: rotavirus and cholera immunization. Bulletin of the World Health Organization 63, 569-583.
    • (1985) Bulletin of the World Health Organization , vol.63 , pp. 569-583
    • De Zoysa, I.1    Feachem, R.G.2
  • 5
    • 0018856932 scopus 로고
    • Different polypeptide composition of two human rotavirus types
    • Espejo, R., Martinez, E., López, S. & Munoz, O. (1980). Different polypeptide composition of two human rotavirus types. Infection and Immunity 28, 230-237.
    • (1980) Infection and Immunity , vol.28 , pp. 230-237
    • Espejo, R.1    Martinez, E.2    López, S.3    Munoz, O.4
  • 6
    • 0024408580 scopus 로고
    • Rotavirus gene structure and function
    • Estes, M. K. & Cohen, J. (1989). Rotavirus gene structure and function. Microbiological Reviews 53, 410-449.
    • (1989) Microbiological Reviews , vol.53 , pp. 410-449
    • Estes, M.K.1    Cohen, J.2
  • 7
    • 0028969720 scopus 로고
    • Disulfide bonds between two enveloped proteins of lactate dehydrogenase-elevating virus are essential for viral infectivity
    • Faaberg, K. S., Even, C., Palmer, G. A. & Plagemann, P. G. (1995). Disulfide bonds between two enveloped proteins of lactate dehydrogenase-elevating virus are essential for viral infectivity. Journal of Virology 69, 613-617.
    • (1995) Journal of Virology , vol.69 , pp. 613-617
    • Faaberg, K.S.1    Even, C.2    Palmer, G.A.3    Plagemann, P.G.4
  • 8
    • 0025756384 scopus 로고
    • The VP8 fragment of VP4 is the rhesus rotavirus hemagglutinin
    • Fiore, L., Greenberg, H. B. & Mackow, E. R. (1991). The VP8 fragment of VP4 is the rhesus rotavirus hemagglutinin. Virology 181, 553-563.
    • (1991) Virology , vol.181 , pp. 553-563
    • Fiore, L.1    Greenberg, H.B.2    Mackow, E.R.3
  • 9
    • 0024426261 scopus 로고
    • Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell absorption
    • Fukudome, K., Yoshie, O. & Konno, T. (1989). Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell absorption. Virology 172, 196-205.
    • (1989) Virology , vol.172 , pp. 196-205
    • Fukudome, K.1    Yoshie, O.2    Konno, T.3
  • 10
    • 1842291025 scopus 로고    scopus 로고
    • Functional and structural analysis of the sialic acid-binding domain of rotaviruses
    • Isa, P., López, S., Segovia, L. & Arias, C. F. (1997). Functional and structural analysis of the sialic acid-binding domain of rotaviruses. Journal of Virology 71, 6749-6756.
    • (1997) Journal of Virology , vol.71 , pp. 6749-6756
    • Isa, P.1    López, S.2    Segovia, L.3    Arias, C.F.4
  • 11
    • 0023973434 scopus 로고
    • Characterization of binding of simian rotavirus SA-11 to cultured epithelial cells
    • Keljo, D. J. & Smith, A. K. (1988). Characterization of binding of simian rotavirus SA-11 to cultured epithelial cells. Journal of Pediatric Gastroenterology and Nutrition 7, 249-256.
    • (1988) Journal of Pediatric Gastroenterology and Nutrition , vol.7 , pp. 249-256
    • Keljo, D.J.1    Smith, A.K.2
  • 12
    • 0022006581 scopus 로고
    • Primary structure of the cleavage site associated with trypsin enhancement of rotavirus SA11 infectivity
    • López, S., Arias, C. F., Bell, J. R., Strauss, J. H. & Espejo, R. T. (1985). Primary structure of the cleavage site associated with trypsin enhancement of rotavirus SA11 infectivity. Virology 144, 11-19.
    • (1985) Virology , vol.144 , pp. 11-19
    • López, S.1    Arias, C.F.2    Bell, J.R.3    Strauss, J.H.4    Espejo, R.T.5
  • 13
    • 0028145081 scopus 로고
    • Mapping the subgroup epitopes of rotavirus protein VP6
    • López, S., Espinosa, R., Greenberg, H. B. & Arias, C. F. (1994). Mapping the subgroup epitopes of rotavirus protein VP6. Virology 204, 153-162.
    • (1994) Virology , vol.204 , pp. 153-162
    • López, S.1    Espinosa, R.2    Greenberg, H.B.3    Arias, C.F.4
  • 14
    • 0023838918 scopus 로고
    • The rhesus rotavirus gene encoding protein VP3: Location of amino acids involved in homologous and heterologous rotavirus neutralization and identification of a putative fusion region
    • Mackow, E. R., Shaw, R. D., Matsui, S. M., Vo, P. T., Dang, M. N. & Greenberg, H. B. (1988). The rhesus rotavirus gene encoding protein VP3: location of amino acids involved in homologous and heterologous rotavirus neutralization and identification of a putative fusion region. Proceedings of the National Academy of Sciences, USA 85, 645-649.
    • (1988) Proceedings of the National Academy of Sciences, USA , vol.85 , pp. 645-649
    • Mackow, E.R.1    Shaw, R.D.2    Matsui, S.M.3    Vo, P.T.4    Dang, M.N.5    Greenberg, H.B.6
  • 15
    • 0027257854 scopus 로고
    • Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture
    • Méndez, E., Arias, C. F. & López, S. (1993). Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture. Journal of Virology 67, 5253-5259.
    • (1993) Journal of Virology , vol.67 , pp. 5253-5259
    • Méndez, E.1    Arias, C.F.2    López, S.3
  • 16
    • 0030045766 scopus 로고    scopus 로고
    • Interactions between the two surface proteins of rotavirus may alter the receptor-binding specificity of the virus
    • Méndez, E., Arias, C. F. & López, S. (1996). Interactions between the two surface proteins of rotavirus may alter the receptor-binding specificity of the virus. Journal of Virology 70, 1218-1222.
    • (1996) Journal of Virology , vol.70 , pp. 1218-1222
    • Méndez, E.1    Arias, C.F.2    López, S.3
  • 18
    • 0027301674 scopus 로고
    • Location of intrachain disulfide bonds in the VP5* and VP8* trypsin cleavage fragments of the rhesus rotavirus spike protein VP4
    • Patton, J. T., Hua, J. & Mansell, E. A. (1993). Location of intrachain disulfide bonds in the VP5* and VP8* trypsin cleavage fragments of the rhesus rotavirus spike protein VP4. Journal of Virology 67, 4848-4855.
    • (1993) Journal of Virology , vol.67 , pp. 4848-4855
    • Patton, J.T.1    Hua, J.2    Mansell, E.A.3
  • 19
    • 0025900084 scopus 로고
    • Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture
    • Ruggieri, F. M. & Greenberg, H. B. (1991). Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture. Journal of Virology 65, 2211-2219.
    • (1991) Journal of Virology , vol.65 , pp. 2211-2219
    • Ruggieri, F.M.1    Greenberg, H.B.2
  • 20
    • 0029133206 scopus 로고
    • Analysis of cysteine mutations on the transmembrane protein of Moloney murine leukemia virus
    • Thomas, A. & Roth, M. J. (1995). Analysis of cysteine mutations on the transmembrane protein of Moloney murine leukemia virus. Virology 211, 285-289.
    • (1995) Virology , vol.211 , pp. 285-289
    • Thomas, A.1    Roth, M.J.2
  • 21
    • 0025271056 scopus 로고
    • Functional contribution of cysteine residues to the human immuno-deficiency virus type 1 envelope
    • Tschachler, E., Buchow, H., Gallo, R. G. & Reitz, M. S., Jr (1990). Functional contribution of cysteine residues to the human immuno-deficiency virus type 1 envelope. Journal of Virology 64, 2250-2259.
    • (1990) Journal of Virology , vol.64 , pp. 2250-2259
    • Tschachler, E.1    Buchow, H.2    Gallo, R.G.3    Reitz Jr., M.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.