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Volumn 220, Issue 1, 1996, Pages 91-99

Protein-protein interactions between Epstein-Barr virus nuclear antigen-LP and cellular gene products: Binding of 70-kilodalton heat shock proteins

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS ANTIGEN; HEAT SHOCK PROTEIN;

EID: 0029894601     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.0289     Document Type: Article
Times cited : (40)

References (43)
  • 2
    • 0024345877 scopus 로고
    • Epstein-Barr Virus latent gene expression during the initiation of B cell immortalization
    • Allday, M. J., Crawford, D. H., and Griffin, B. (1989). Epstein-Barr Virus latent gene expression during the initiation of B cell immortalization. J. Gen. Virol. 70, 1755-1764.
    • (1989) J. Gen. Virol. , vol.70 , pp. 1755-1764
    • Allday, M.J.1    Crawford, D.H.2    Griffin, B.3
  • 3
    • 0028951944 scopus 로고
    • Epstein-Barr virus efficiently immortalizes human B cells without neutralizing the function of p53
    • Allday, M. J., Sinclair, A., Parker, G., Crawford, D. H., and Farrell, P. J. (1995). Epstein-Barr virus efficiently immortalizes human B cells without neutralizing the function of p53. EMBO J. 14, 1382-1391.
    • (1995) EMBO J. , vol.14 , pp. 1382-1391
    • Allday, M.J.1    Sinclair, A.2    Parker, G.3    Crawford, D.H.4    Farrell, P.J.5
  • 4
    • 0028145079 scopus 로고
    • The bovine papillomavirus E1 protein alters the host cell cycle and growth properties
    • Belyavskyi, M., Miller, J., and Wilson, V. (1994). The bovine papillomavirus E1 protein alters the host cell cycle and growth properties. Virology 204, 132-143.
    • (1994) Virology , vol.204 , pp. 132-143
    • Belyavskyi, M.1    Miller, J.2    Wilson, V.3
  • 6
    • 0024429019 scopus 로고
    • Phosphorylation of the retinoblastoma gene product is modulated during the cell cycle and cellular differentiation
    • Chen, P. L., Scully, P., Shew, J. Y., Wang, Y. J., and Lee, W. H. (1989). Phosphorylation of the retinoblastoma gene product is modulated during the cell cycle and cellular differentiation. Cell 58, 193-1198.
    • (1989) Cell , vol.58 , pp. 193-1198
    • Chen, P.L.1    Scully, P.2    Shew, J.Y.3    Wang, Y.J.4    Lee, W.H.5
  • 7
    • 0027397206 scopus 로고
    • Epstein-Barr virus (EBV) nuclear-antigen-2-induced up-regulation of CD21 and CD23 molecules is dependent on a permissive cellular context
    • Cordier-Bussat, M., Billaud, M., Calender, A., and Lenoir, G. M. (1993). Epstein-Barr virus (EBV) nuclear-antigen-2-induced up-regulation of CD21 and CD23 molecules is dependent on a permissive cellular context. Int. J. Cancer 53, 153-160.
    • (1993) Int. J. Cancer , vol.53 , pp. 153-160
    • Cordier-Bussat, M.1    Billaud, M.2    Calender, A.3    Lenoir, G.M.4
  • 8
    • 0023499869 scopus 로고
    • Monoclonal and polyclonal antibodies against Epstein-Barr virus nuclear antigen 5 (EBNA5) detect multiple protein species in Burkitt's lymphoma and lymphoblastoid cell lines
    • Finke, J., Rowe, M., Kallin, B., Ernberg, I., Rosen, A., Dillner, J., and Klein, G. (1987). Monoclonal and polyclonal antibodies against Epstein-Barr virus nuclear antigen 5 (EBNA5) detect multiple protein species in Burkitt's lymphoma and lymphoblastoid cell lines. J. Virol. 61, 3870-3878.
    • (1987) J. Virol. , vol.61 , pp. 3870-3878
    • Finke, J.1    Rowe, M.2    Kallin, B.3    Ernberg, I.4    Rosen, A.5    Dillner, J.6    Klein, G.7
  • 9
    • 0023959795 scopus 로고
    • Mutations which activate p53 transformation with ras produce an altered p53 protein that preferentially binds to a heat shock protein hsc70
    • Finlay, C., Hinds, P., Frey, A. B., and Levine, A. J. (1988). Mutations which activate p53 transformation with ras produce an altered p53 protein that preferentially binds to a heat shock protein hsc70. Mol. Cell. Biol. 8, 531-539.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 531-539
    • Finlay, C.1    Hinds, P.2    Frey, A.B.3    Levine, A.J.4
  • 10
    • 0026059137 scopus 로고
    • Peptide binding specificity of the molecular chaperone BiP
    • Flynn, G. C., Pohl, J., Flocco, M. T., and Rothman, J. E. (1991). Peptide binding specificity of the molecular chaperone BiP. Nature (London) 353, 726-730.
    • (1991) Nature (London) , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 11
    • 0017710978 scopus 로고
    • Characteristics of a human cell line transformed by DNA from human adenovirus type 5
    • Graham, F. L., Smiley, J., Russell, W. C., and Nairn, R. (1977). Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J. Gen. Virol. 36, 33-42.
    • (1977) J. Gen. Virol. , vol.36 , pp. 33-42
    • Graham, F.L.1    Smiley, J.2    Russell, W.C.3    Nairn, R.4
  • 12
    • 0024375760 scopus 로고
    • Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes
    • Hammerschmidt, W., and Sugden, B. (1989). Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes. Nature 340, 393-397.
    • (1989) Nature , vol.340 , pp. 393-397
    • Hammerschmidt, W.1    Sugden, B.2
  • 14
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones, and proteotoxicity
    • Hightower, L. E. (1991). Heat shock, stress proteins, chaperones, and proteotoxicity. Cell 66, 191-197.
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 15
    • 0023394825 scopus 로고
    • Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p-53-plus-ras transformed cell lines
    • Hinds, P. W., Finlay, C. A., Frey, A. B., and Levine, A. J. (1987). Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p-53-plus-ras transformed cell lines. Mol. Cell. Biol. 7, 2863-2869.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2863-2869
    • Hinds, P.W.1    Finlay, C.A.2    Frey, A.B.3    Levine, A.J.4
  • 16
    • 0026346116 scopus 로고
    • Co-localization of the retinoblastoma protein and the Epstein-Barr virus-encloded nuclear antigen EBNA5
    • Jang, W.-Q., Szekely, L., Wendel-Hansen, V., Ringertz, N., Klein, G., and Rosen, A. (1991). Co-localization of the retinoblastoma protein and the Epstein-Barr virus-encloded nuclear antigen EBNA5. Exp. Cell Res. 197, 314-318.
    • (1991) Exp. Cell Res. , vol.197 , pp. 314-318
    • Jang, W.-Q.1    Szekely, L.2    Wendel-Hansen, V.3    Ringertz, N.4    Klein, G.5    Rosen, A.6
  • 17
    • 0026021882 scopus 로고
    • Identification of cellular proteins that can interact with the T/E1a-binding region of the retinoblastoma gene product
    • Kaelin, W. G., Pallas, D. C., DeCaprio, J. A., Kaye, F. J., and Livingston, D. M. (1991). Identification of cellular proteins that can interact with the T/E1a-binding region of the retinoblastoma gene product. Cell 64, 521-432.
    • (1991) Cell , vol.64 , pp. 521-1432
    • Kaelin, W.G.1    Pallas, D.C.2    Decaprio, J.A.3    Kaye, F.J.4    Livingston, D.M.5
  • 18
    • 0028209073 scopus 로고
    • Interaction of the E6 protein of human papillomavirus with cellular proteins
    • Keen, N., Elston, R., and Crawford, L. (1994). Interaction of the E6 protein of human papillomavirus with cellular proteins. Oncogene 9, 1493-1499.
    • (1994) Oncogene , vol.9 , pp. 1493-1499
    • Keen, N.1    Elston, R.2    Crawford, L.3
  • 19
    • 0029095056 scopus 로고
    • Immune regulation in Epstein-Barr virus-associated diseases
    • Khanna, R., Burrows, S. R., and Moss, D. J. (1995). Immune regulation in Epstein-Barr virus-associated diseases. Microbiol. Rev. 59, 387-405.
    • (1995) Microbiol. Rev. , vol.59 , pp. 387-405
    • Khanna, R.1    Burrows, S.R.2    Moss, D.J.3
  • 20
    • 0020618207 scopus 로고
    • Chromosomal translocations and the genesis of B cell derived tumors in mice and men
    • Klein, G. (1983). Chromosomal translocations and the genesis of B cell derived tumors in mice and men. Cell 32, 311-315.
    • (1983) Cell , vol.32 , pp. 311-315
    • Klein, G.1
  • 21
    • 0028340056 scopus 로고
    • Epstein-Barr virus strategy in normal and neoplastic B cells
    • Klein, G. (1994). Epstein-Barr virus strategy in normal and neoplastic B cells. Cell 77, 791-793.
    • (1994) Cell , vol.77 , pp. 791-793
    • Klein, G.1
  • 23
    • 0000462866 scopus 로고
    • Epstein-Barr virus and its replication
    • B. N. Fields, D. M. Knipe et al., Eds. Raven Press, New York
    • Leibowitz, D., and Kieff, E. (1990). Epstein-Barr virus and its replication. In "Fields Virology" (B. N. Fields, D. M. Knipe et al., Eds.), pp. 1889-1920. Raven Press, New York.
    • (1990) Fields Virology , pp. 1889-1920
    • Leibowitz, D.1    Kieff, E.2
  • 24
    • 0022311860 scopus 로고
    • Use of lymphomatous and lymphoblastoid cell lines in the study of Burkitt's lymphoma
    • (G. M. Lenoir, G. O'Connor, and C. L. M. Olweny, Eds.), Scientific Publication No. 60, International Agency for Research on Cancer, Lyon, France
    • Lenoir, G. M., Vuillaume, M., and Bonnardel, C. (1985). Use of lymphomatous and lymphoblastoid cell lines in the study of Burkitt's lymphoma. In "Burkitt's Lymphoma: A Human Cancer Model" (G. M. Lenoir, G. O'Connor, and C. L. M. Olweny, Eds.), Scientific Publication No. 60, pp. 309-318. International Agency for Research on Cancer, Lyon, France.
    • (1985) Burkitt's Lymphoma: A Human Cancer Model , pp. 309-318
    • Lenoir, G.M.1    Vuillaume, M.2    Bonnardel, C.3
  • 25
    • 0027358873 scopus 로고
    • The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein
    • Ling, P. D., Rawlins, D. R., and Hayward, S. D. (1993). The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein. Proc. Natl. Acad. Sci. USA 90, 9237-9241.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9237-9241
    • Ling, P.D.1    Rawlins, D.R.2    Hayward, S.D.3
  • 26
    • 0025750139 scopus 로고
    • The Epstein-Barr virus nuclear protein encoded by the leader of the EBNA RNAs is important in B-lymphocyte transformation
    • Mannick, J. B., Cohen, J. I., Birkenbach, M., Marchini, A., and Kieff, E. (1991). The Epstein-Barr virus nuclear protein encoded by the leader of the EBNA RNAs is important in B-lymphocyte transformation. J. Virol. 65, 6826-6837.
    • (1991) J. Virol. , vol.65 , pp. 6826-6837
    • Mannick, J.B.1    Cohen, J.I.2    Birkenbach, M.3    Marchini, A.4    Kieff, E.5
  • 27
    • 0029013590 scopus 로고
    • Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator
    • Marshall, D., and Sample, C. (1995). Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator. J. Virol. 69, 3624-3630.
    • (1995) J. Virol. , vol.69 , pp. 3624-3630
    • Marshall, D.1    Sample, C.2
  • 28
    • 0024804191 scopus 로고
    • A protein binding to the J kappa recombination sequence of immunoglobulin genes contains a sequence related to the integrase motif
    • Matsunami, N., Hamaguchi, Y., Yamamoto, Y., Kuze, K., Kangawa, K., Matsuo, H., Kawaichi, M., and Honjo, T. (1989). A protein binding to the J kappa recombination sequence of immunoglobulin genes contains a sequence related to the integrase motif. Nature 342, 934-937.
    • (1989) Nature , vol.342 , pp. 934-937
    • Matsunami, N.1    Hamaguchi, Y.2    Yamamoto, Y.3    Kuze, K.4    Kangawa, K.5    Matsuo, H.6    Kawaichi, M.7    Honjo, T.8
  • 29
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos, R., Birkenbach, M., Yalamanchili, R., Van Arsdale, T., Ware, C., and Kieff, E. (1995). The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell 80, 389-400.
    • (1995) Cell , vol.80 , pp. 389-400
    • Mosialos, R.1    Birkenbach, M.2    Yalamanchili, R.3    Van Arsdale, T.4    Ware, C.5    Kieff, E.6
  • 31
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros, D. P., Welch, W. J., and Fink, A. L. (1991). Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding. Proc. Natl. Acad. Sci. USA 88, 5719-5723.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5719-5723
    • Palleros, D.P.1    Welch, W.J.2    Fink, A.L.3
  • 33
    • 0022134525 scopus 로고
    • Sequence specific DNA binding of the Epstein-Barr virus nuclear antigen (EBNA-1) to clustered sites in the plasmid maintenance region
    • Rawlins, D. R., Milman, G., Hayward, S. D., and Hayward, G. S. (1985). Sequence specific DNA binding of the Epstein-Barr virus nuclear antigen (EBNA-1) to clustered sites in the plasmid maintenance region. Cell 42, 859-868.
    • (1985) Cell , vol.42 , pp. 859-868
    • Rawlins, D.R.1    Milman, G.2    Hayward, S.D.3    Hayward, G.S.4
  • 34
    • 0028833924 scopus 로고
    • Reducing the complexity of the transforming Epstein-Barr virus genome to 64 kilobase pairs
    • Robertson, E., and Kieff, E. (1995). Reducing the complexity of the transforming Epstein-Barr virus genome to 64 kilobase pairs. J. Virol. 691, 983-993.
    • (1995) J. Virol. , vol.691 , pp. 983-993
    • Robertson, E.1    Kieff, E.2
  • 35
    • 0028233417 scopus 로고
    • 1 transition during immortalization of resting human B lymphocytes by Epstein-Barr virus
    • 1 transition during immortalization of resting human B lymphocytes by Epstein-Barr virus. EMBO J. 13, 3321-3328.
    • (1994) EMBO J. , vol.13 , pp. 3321-3328
    • Sinclair, A.J.1    Palermo, I.2    Peters, G.3    Farrell, P.J.4
  • 36
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B., and Johnson, K. S. (1988). Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 37
    • 0027222646 scopus 로고
    • EBNA-5, an Epstein-Barr virus-encoded nuclear antigen, binds to the retinoblastoma and p53 proteins
    • Szekely, L., Selivanova, G., Magnusson, K. P., Klein, G., and Wiman, K. G. (1993). EBNA-5, an Epstein-Barr virus-encoded nuclear antigen, binds to the retinoblastoma and p53 proteins. Proc. Natl. Acad. Sci. USA 90, 5455-5459.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5455-5459
    • Szekely, L.1    Selivanova, G.2    Magnusson, K.P.3    Klein, G.4    Wiman, K.G.5
  • 38
    • 0021812445 scopus 로고
    • Early events in EBV infection provide a model for B cell activation
    • Thorley-Lawson, D. A., and Mann, K. P. (1985). Early events in EBV infection provide a model for B cell activation. J. Exp. Med. 162, 45-47.
    • (1985) J. Exp. Med. , vol.162 , pp. 45-47
    • Thorley-Lawson, D.A.1    Mann, K.P.2
  • 39
    • 0028232496 scopus 로고
    • Epstein-Barr virus nuclear protein 2A forms oligomers in vitro and in vivo through a region required for B-cell transformation
    • Tsui, S., and Schubach, W. H. (1994). Epstein-Barr virus nuclear protein 2A forms oligomers in vitro and in vivo through a region required for B-cell transformation. J. Virol. 68, 4287-4294.
    • (1994) J. Virol. , vol.68 , pp. 4287-4294
    • Tsui, S.1    Schubach, W.H.2
  • 40
    • 0028171081 scopus 로고
    • The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements
    • Waltzer, L., Logeat, F., Brou, C., Israel, A., Sergeant, A., and Manet, E. (1994). The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements. EMBO J. 13, 5633-5638.
    • (1994) EMBO J. , vol.13 , pp. 5633-5638
    • Waltzer, L.1    Logeat, F.2    Brou, C.3    Israel, A.4    Sergeant, A.5    Manet, E.6
  • 41
    • 0023914010 scopus 로고
    • Association between an oncogene and an anti-oncogene: The adenovirus E1A proteins bind to the retinoblastoma gene product
    • Whyte, P., Buckovich, K. J., Howitz, J. M., Friend, S. H., Raybuck, M., Weinberg, R. A., and Harlow, E. (1988). Association between an oncogene and an anti-oncogene: The adenovirus E1A proteins bind to the retinoblastoma gene product. Nature 334, 124-129.
    • (1988) Nature , vol.334 , pp. 124-129
    • Whyte, P.1    Buckovich, K.J.2    Howitz, J.M.3    Friend, S.H.4    Raybuck, M.5    Weinberg, R.A.6    Harlow, E.7
  • 42
    • 0018777485 scopus 로고
    • Recovery of Epstein-Barr virus from non-producer neonatal human lymphoid cell transformants
    • Wilson, G., and Miller, G. (1979). Recovery of Epstein-Barr virus from non-producer neonatal human lymphoid cell transformants. Virology 95, 351-358.
    • (1979) Virology , vol.95 , pp. 351-358
    • Wilson, G.1    Miller, G.2
  • 43
    • 0028063483 scopus 로고
    • The Epstein-Barr virus nuclear antigen 2 exerts its function through interaction with recombination signal binding protein RBP-J Kappa, the homologue of Drosophila suppressor of hairless
    • Zimber-Strobl, U., Strobl, L. J., Meitinger, C., Hinrichs, R., Sakai, T., Furukawa, T., Honjo, T., and Bornkamm, G. W. (1994). The Epstein-Barr virus nuclear antigen 2 exerts its function through interaction with recombination signal binding protein RBP-J Kappa, the homologue of Drosophila suppressor of hairless. EMBO J. 13, 4973-4982.
    • (1994) EMBO J. , vol.13 , pp. 4973-4982
    • Zimber-Strobl, U.1    Strobl, L.J.2    Meitinger, C.3    Hinrichs, R.4    Sakai, T.5    Furukawa, T.6    Honjo, T.7    Bornkamm, G.W.8


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