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Volumn 235, Issue 2, 1997, Pages 241-251

The immunoreceptor tyrosine-based activation motif of Epstein-Barr virus LMP2A is essential for blocking BCR-mediated signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS RECEPTOR;

EID: 0030754766     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8690     Document Type: Article
Times cited : (199)

References (65)
  • 1
    • 0028023367 scopus 로고
    • Detection and characterization of Epstein-Barr virus in clinical specimens
    • Ambinder R. F., Mann R. B. Detection and characterization of Epstein-Barr virus in clinical specimens. Am. J. Pathol. 145:1994;239-252.
    • (1994) Am. J. Pathol. , vol.145 , pp. 239-252
    • Ambinder, R.F.1    Mann, R.B.2
  • 2
    • 0027267532 scopus 로고
    • Nonreceptor tyrosine protein kinases
    • Bolen J. B. Nonreceptor tyrosine protein kinases. Oncogene. 8:1993;2025-2031.
    • (1993) Oncogene , vol.8 , pp. 2025-2031
    • Bolen, J.B.1
  • 3
    • 0026720952 scopus 로고
    • An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinases
    • Burkhardt A. L., Bolen J. B., Kieff E., Longnecker R. An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinases. J. Virol. 66:1992;5161-5167.
    • (1992) J. Virol. , vol.66 , pp. 5161-5167
    • Burkhardt, A.L.1    Bolen, J.B.2    Kieff, E.3    Longnecker, R.4
  • 4
    • 0028890805 scopus 로고
    • Sequence polymorphism in the Epstein-Barr virus latent membrane protein (LMP)-2 gene
    • Busson P., Edwards R. H., Tursz T., Raab-Traub N. Sequence polymorphism in the Epstein-Barr virus latent membrane protein (LMP)-2 gene. J. Gen. Virol. 76:1995;139-145.
    • (1995) J. Gen. Virol. , vol.76 , pp. 139-145
    • Busson, P.1    Edwards, R.H.2    Tursz, T.3    Raab-Traub, N.4
  • 5
    • 0000722327 scopus 로고
    • New nomenclature for the Reth motif (or ARH1/TAM/ARAM/YXXL)
    • Cambier J. C. New nomenclature for the Reth motif (or ARH1/TAM/ARAM/YXXL). Immunol. Today. 16:1995;110.
    • (1995) Immunol. Today , vol.16 , pp. 110
    • Cambier, J.C.1
  • 6
    • 0028346563 scopus 로고
    • Signal transduction by the B cell antigen receptor and its coreceptors
    • Cambier J. C., Pleiman C. M., Clark M. R. Signal transduction by the B cell antigen receptor and its coreceptors. Annu. Rev. Immunol. 12:1994;457-486.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 457-486
    • Cambier, J.C.1    Pleiman, C.M.2    Clark, M.R.3
  • 7
    • 0029067481 scopus 로고
    • A subpopulation of normal B cells latently infected with Epstein-Barr virus resembles Burkitt lymphoma cells in expressing EBNA-1 but not EBNA-2 or LMP1
    • Chen F., Zou J. Z., di Renzo L., Winberg G., Hu L. F., Klein E., Klein G., Ernberg I. A subpopulation of normal B cells latently infected with Epstein-Barr virus resembles Burkitt lymphoma cells in expressing EBNA-1 but not EBNA-2 or LMP1. J. Virol. 69:1995;3752-3758.
    • (1995) J. Virol. , vol.69 , pp. 3752-3758
    • Chen, F.1    Zou, J.Z.2    Di Renzo, L.3    Winberg, G.4    Hu, L.F.5    Klein, E.6    Klein, G.7    Ernberg, I.8
  • 8
    • 0029099161 scopus 로고
    • The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules
    • Chen H. I., Sudol M. The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. Proc. Natl. Acad. Sci. USA. 92:1995;7819-7823.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7819-7823
    • Chen, H.I.1    Sudol, M.2
  • 9
    • 0028783322 scopus 로고
    • Syk tyrosine kinase required for mouse viability and B-cell development
    • Cheng A. M., Rowley B., Pao W., Hayday A., Bolen J. B., Pawson T. Syk tyrosine kinase required for mouse viability and B-cell development. Nature. 378:1995;303-306.
    • (1995) Nature , vol.378 , pp. 303-306
    • Cheng, A.M.1    Rowley, B.2    Pao, W.3    Hayday, A.4    Bolen, J.B.5    Pawson, T.6
  • 10
    • 0024317091 scopus 로고
    • Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation
    • Cohen J. I., Wang F., Mannick J., Kieff E. Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation. Proc. Natl. Acad. Sci. USA. 86:1989;9558-9562.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9558-9562
    • Cohen, J.I.1    Wang, F.2    Mannick, J.3    Kieff, E.4
  • 11
    • 0028926070 scopus 로고
    • Transmembrane signaling by antigen receptors of B and T lymphocytes
    • DeFranco A. L. Transmembrane signaling by antigen receptors of B and T lymphocytes. Curr. Opin. Cell Biol. 7:1995;163-175.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 163-175
    • Defranco, A.L.1
  • 12
    • 0028923727 scopus 로고
    • Epstein-Barr virus immortalizing genes
    • Farrell P. J. Epstein-Barr virus immortalizing genes. Trends Microbiol. 3:1995;105-109.
    • (1995) Trends Microbiol. , vol.3 , pp. 105-109
    • Farrell, P.J.1
  • 13
    • 0028125752 scopus 로고
    • Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor
    • Flaswinkel H., Reth M. Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor. EMBO J. 13:1994;83-89.
    • (1994) EMBO J. , vol.13 , pp. 83-89
    • Flaswinkel, H.1    Reth, M.2
  • 14
    • 0028971196 scopus 로고
    • 5′ coding and regulatory region sequence divergence with conserved function of the Epstein-Barr virus LMP2A homolog in herpesvirus papio
    • Franken M., Annis B., Ali A. N., Wang F. 5′ coding and regulatory region sequence divergence with conserved function of the Epstein-Barr virus LMP2A homolog in herpesvirus papio. J. Virol. 69:1995;8011-8019.
    • (1995) J. Virol. , vol.69 , pp. 8011-8019
    • Franken, M.1    Annis, B.2    Ali, A.N.3    Wang, F.4
  • 15
    • 0025316596 scopus 로고
    • Identification of Epstein-Barr virus terminal protein 1 (TP1) in extracts of four lymphoid cell lines, expression in insect cells, and detection of antibodies in human sera
    • Frech B., Zimber-Strobl U., Suentzenich K. O., Pavlish O., Lenoir G. M., Bornkamm G. W., Mueller-Lantzsch N. Identification of Epstein-Barr virus terminal protein 1 (TP1) in extracts of four lymphoid cell lines, expression in insect cells, and detection of antibodies in human sera. J. Virol. 64:1990;2759-2767.
    • (1990) J. Virol. , vol.64 , pp. 2759-2767
    • Frech, B.1    Zimber-Strobl, U.2    Suentzenich, K.O.3    Pavlish, O.4    Lenoir, G.M.5    Bornkamm, G.W.6    Mueller-Lantzsch, N.7
  • 16
    • 9444288215 scopus 로고    scopus 로고
    • Identification of latent membrane protein 2A (LMP2A) domains essential for the LMP2A dominant-negative effect on B-lymphocyte surface immunoglobulin signal transduction
    • Fruehling S., Lee S., Herrold R., Frech B., Laux G., Kremmer E., Grässer F. A., Longnecker R. Identification of latent membrane protein 2A (LMP2A) domains essential for the LMP2A dominant-negative effect on B-lymphocyte surface immunoglobulin signal transduction. J. Virol. 70:1996;6216-6226.
    • (1996) J. Virol. , vol.70 , pp. 6216-6226
    • Fruehling, S.1    Lee, S.2    Herrold, R.3    Frech, B.4    Laux, G.5    Kremmer, E.6    Grässer, F.A.7    Longnecker, R.8
  • 17
    • 0028931028 scopus 로고
    • Signal transduction by the antigen receptors of B and T lymphocytes
    • Gold M. R., Matsuuchi L. Signal transduction by the antigen receptors of B and T lymphocytes. Int. Rev. Cytol. 157:1995;181-276.
    • (1995) Int. Rev. Cytol. , vol.157 , pp. 181-276
    • Gold, M.R.1    Matsuuchi, L.2
  • 20
    • 0024375760 scopus 로고
    • Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes
    • Hammerschmidt W., Sugden B. Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes. Nature. 340:1989;393-397.
    • (1989) Nature , vol.340 , pp. 393-397
    • Hammerschmidt, W.1    Sugden, B.2
  • 21
    • 0020045179 scopus 로고
    • New Epstein-Barr virus variants from cellular subclones of P3J-HR-1 Burkitt lymphoma
    • Heston L., Rabson M., Brown N., Miller G. New Epstein-Barr virus variants from cellular subclones of P3J-HR-1 Burkitt lymphoma. Nature. 295:1982;160-163.
    • (1982) Nature , vol.295 , pp. 160-163
    • Heston, L.1    Rabson, M.2    Brown, N.3    Miller, G.4
  • 23
    • 0027399703 scopus 로고
    • Functional characterization of a signal transducing motif present in the T cell antigen receptor zeta chain
    • Irving B. A., Chan A. C., Weiss A. Functional characterization of a signal transducing motif present in the T cell antigen receptor zeta chain. J. Exp. Med. 177:1993;1093-1103.
    • (1993) J. Exp. Med. , vol.177 , pp. 1093-1103
    • Irving, B.A.1    Chan, A.C.2    Weiss, A.3
  • 24
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima M., Irving B. A., van O. N., Chan A. C., Weiss A. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science. 263:1994;1136-1139.
    • (1994) Science , vol.263 , pp. 1136-1139
    • Iwashima, M.1    Irving, B.A.2    Van, O.N.3    Chan, A.C.4    Weiss, A.5
  • 25
    • 0027449255 scopus 로고
    • Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation
    • Kaye K. M., Izumi K. M., Kieff E. Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation. Proc. Natl. Acad. Sci. USA. 90:1993;9150-9154.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9150-9154
    • Kaye, K.M.1    Izumi, K.M.2    Kieff, E.3
  • 26
    • 0000942113 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • New York: Raven Press. p. 1109-1162
    • Kieff E. Epstein-Barr virus and its replication. Fundamental Virology. 1996;Raven Press, New York. p. 1109-1162.
    • (1996) Fundamental Virology
    • Kieff, E.1
  • 27
    • 0029864882 scopus 로고    scopus 로고
    • Conformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides
    • Kimura T., Sakamoto H., Appella E., Siraganian R. P. Conformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides. Mol. Cell. Biol. 16:1996;1471-1478.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1471-1478
    • Kimura, T.1    Sakamoto, H.2    Appella, E.3    Siraganian, R.P.4
  • 28
    • 0028239267 scopus 로고
    • Studies on the mechanism of desensitization of the parathyroid hormone-stimulated calcium signal in UMR-106 cells: Reversal of desensitization by alkaline phosphatase but not by protein kinase C downregulation
    • Lee S. K., Stern P. H. Studies on the mechanism of desensitization of the parathyroid hormone-stimulated calcium signal in UMR-106 cells: Reversal of desensitization by alkaline phosphatase but not by protein kinase C downregulation. J. Bone Miner. Res. 9:1994;781-789.
    • (1994) J. Bone Miner. Res. , vol.9 , pp. 781-789
    • Lee, S.K.1    Stern, P.H.2
  • 29
    • 0025915585 scopus 로고
    • An Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinase
    • Longnecker R., Druker B., Roberts T. M., Kieff E. An Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinase. J. Virol. 65:1991;3681-3692.
    • (1991) J. Virol. , vol.65 , pp. 3681-3692
    • Longnecker, R.1    Druker, B.2    Roberts, T.M.3    Kieff, E.4
  • 30
    • 0025305417 scopus 로고
    • A second Epstein-Barr virus membrane protein (LMP2) is expressed in latent infection and colocalizes with LMP1
    • Longnecker R., Kieff E. A second Epstein-Barr virus membrane protein (LMP2) is expressed in latent infection and colocalizes with LMP1. J. Virol. 64:1990;2319-2326.
    • (1990) J. Virol. , vol.64 , pp. 2319-2326
    • Longnecker, R.1    Kieff, E.2
  • 31
    • 0026739517 scopus 로고
    • The only domain which distinguishes Epstein-Barr virus latent membrane 2A (LMP2A) from LMP2B is dispensible for lymphocyte infection and growth transformation in vitro, and LMP2A is therefore nonessential
    • Longnecker R., Miller C. L., Miao X.-Q., Marchini A., Kieff E. The only domain which distinguishes Epstein-Barr virus latent membrane 2A (LMP2A) from LMP2B is dispensible for lymphocyte infection and growth transformation in vitro, and LMP2A is therefore nonessential. J. Virol. 66:1992;6461-6469.
    • (1992) J. Virol. , vol.66 , pp. 6461-6469
    • Longnecker, R.1    Miller, C.L.2    Miao, X.-Q.3    Marchini, A.4    Kieff, E.5
  • 32
    • 0027537458 scopus 로고
    • The last seven transmembrane and carboxy terminal tail of Epstein-Barr virus latent membrane 2 (LMP2) are dispensible for lymphocyte infection and growth transformation
    • Longnecker R., Miller C. L., Miao X.-Q., Tomkinson B., Kieff E. The last seven transmembrane and carboxy terminal tail of Epstein-Barr virus latent membrane 2 (LMP2) are dispensible for lymphocyte infection and growth transformation. J. Virol. 67:1993a;2006-2013.
    • (1993) J. Virol. , vol.67 , pp. 2006-2013
    • Longnecker, R.1    Miller, C.L.2    Miao, X.-Q.3    Tomkinson, B.4    Kieff, E.5
  • 33
    • 0027236266 scopus 로고
    • Deletion of DNA encoding the first five transmembrane domains of Epstein-Barr virus latent membrane proteins 2A and 2B
    • Longnecker R., Miller C. L., Tomkinson B., Miao X. Q., Kieff E. Deletion of DNA encoding the first five transmembrane domains of Epstein-Barr virus latent membrane proteins 2A and 2B. J. Virol. 67:1993b;5068-5074.
    • (1993) J. Virol. , vol.67 , pp. 5068-5074
    • Longnecker, R.1    Miller, C.L.2    Tomkinson, B.3    Miao, X.Q.4    Kieff, E.5
  • 34
    • 0342556457 scopus 로고
    • An Epstein-Barr virus-encoded protein found in plasma membranes of transformed cells
    • Mann K., Staunton D., Thorley-Lawson D. A. An Epstein-Barr virus-encoded protein found in plasma membranes of transformed cells. J. Virol. 55:1985;233-237.
    • (1985) J. Virol. , vol.55 , pp. 233-237
    • Mann, K.1    Staunton, D.2    Thorley-Lawson, D.A.3
  • 35
    • 0025932085 scopus 로고
    • BHRF1, the Epstein-Barr virus gene with homology to Bcl2, is dispensible for B-lymphocyte transformation and virus replication
    • Marchini A., Tomkinson B., Cohen J. I., Kieff E. BHRF1, the Epstein-Barr virus gene with homology to Bcl2, is dispensible for B-lymphocyte transformation and virus replication. J. Virol. 65:1991;5991-6000.
    • (1991) J. Virol. , vol.65 , pp. 5991-6000
    • Marchini, A.1    Tomkinson, B.2    Cohen, J.I.3    Kieff, E.4
  • 36
    • 0016835245 scopus 로고
    • Establishment and characterization of an Epstein-Barr virus (EBV)- negative lymphoblastoid B cell line (BJA-B) from an exceptional, EBV-genome-negative African Burkitt's lymphoma
    • Menezes J., Leibold W., Klein G., Clements G. Establishment and characterization of an Epstein-Barr virus (EBV)- negative lymphoblastoid B cell line (BJA-B) from an exceptional, EBV-genome-negative African Burkitt's lymphoma. Biomedicine. 22:1975;276-284.
    • (1975) Biomedicine , vol.22 , pp. 276-284
    • Menezes, J.1    Leibold, W.2    Klein, G.3    Clements, G.4
  • 38
    • 0028970289 scopus 로고
    • Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases
    • Miller C. L., Burkhardt A. L., Lee J. H., Stealey B., Longnecker R., Bolen J. B., Kieff E. Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases. Immunity. 2:1995;155-166.
    • (1995) Immunity , vol.2 , pp. 155-166
    • Miller, C.L.1    Burkhardt, A.L.2    Lee, J.H.3    Stealey, B.4    Longnecker, R.5    Bolen, J.B.6    Kieff, E.7
  • 39
    • 0028088994 scopus 로고
    • An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking
    • Miller C. L., Lee J. H., Kieff E., Longnecker R. An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking. Proc. Natl. Acad. Sci. USA. 91:1994;772-776.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 772-776
    • Miller, C.L.1    Lee, J.H.2    Kieff, E.3    Longnecker, R.4
  • 40
    • 0027211796 scopus 로고
    • Epstein-Barr virus latent membrane protein 2A blocks calcium mobilization in B lymphocytes
    • Miller C. L., Longnecker R., Kieff E. Epstein-Barr virus latent membrane protein 2A blocks calcium mobilization in B lymphocytes. J. Virol. 67:1993;3087-3094.
    • (1993) J. Virol. , vol.67 , pp. 3087-3094
    • Miller, C.L.1    Longnecker, R.2    Kieff, E.3
  • 41
    • 0000157121 scopus 로고
    • The Epstein-Barr virus
    • B.N. Fields, & D.M. Knipe. New York: Raven Press
    • Miller G. The Epstein-Barr virus. Fields B. N., Knipe D. M. Virology. 1990;563-589 Raven Press, New York.
    • (1990) Virology , pp. 563-589
    • Miller, G.1
  • 44
    • 0026484261 scopus 로고
    • SH2 and SH3 domains: From structure to function
    • Pawson T., Gish G. D. SH2 and SH3 domains: From structure to function. Cell. 71:1992;359-362.
    • (1992) Cell , vol.71 , pp. 359-362
    • Pawson, T.1    Gish, G.D.2
  • 45
    • 0026764617 scopus 로고
    • Epstein-Barr virus latent gene expression in uncultured peripheral blood lymphocytes
    • Qu L., Rowe D. Epstein-Barr virus latent gene expression in uncultured peripheral blood lymphocytes. J. Virol. 66:1992;3715-3724.
    • (1992) J. Virol. , vol.66 , pp. 3715-3724
    • Qu, L.1    Rowe, D.2
  • 46
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth M. Antigen receptor tail clue. Nature. 338:1989;383-384.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 47
    • 0026537801 scopus 로고
    • Sequence requirements for induction of cytolysis by the T cell antigen/Fc receptor zeta chain
    • Romeo C., Amiot M., Seed B. Sequence requirements for induction of cytolysis by the T cell antigen/Fc receptor zeta chain. Cell. 68:1992;889-897.
    • (1992) Cell , vol.68 , pp. 889-897
    • Romeo, C.1    Amiot, M.2    Seed, B.3
  • 48
    • 0025302972 scopus 로고
    • Identification of the Epstein-Barr virus terminal protein gene products in latently infected lymphocytes
    • Rowe D. T., Hall L., Joab I., Laux G. Identification of the Epstein-Barr virus terminal protein gene products in latently infected lymphocytes. J. Virol. 64:1990;2866-2875.
    • (1990) J. Virol. , vol.64 , pp. 2866-2875
    • Rowe, D.T.1    Hall, L.2    Joab, I.3    Laux, G.4
  • 49
    • 0029081101 scopus 로고
    • SH2 domain structure and function
    • Schaffhausen B. SH2 domain structure and function. Biochim. Biophys. Acta. 1242:1995;61-75.
    • (1995) Biochim. Biophys. Acta , vol.1242 , pp. 61-75
    • Schaffhausen, B.1
  • 52
    • 0027506845 scopus 로고
    • NIH conference. Epstein-Barr virus infections: Biology, pathogenesis, and management
    • Straus S. E., Cohen J. I., Tosato G., Meier J. NIH conference. Epstein-Barr virus infections: Biology, pathogenesis, and management. Ann. Int. Med. 118:1993;45-58.
    • (1993) Ann. Int. Med. , vol.118 , pp. 45-58
    • Straus, S.E.1    Cohen, J.I.2    Tosato, G.3    Meier, J.4
  • 53
    • 0028997651 scopus 로고
    • Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain
    • Sudol M., Bork P., Einbond A., Kastury K., Druck T., Negrini M., Hueber K., Lehman D. Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain. J. Biol. Chem. 270:1995;14733-14741.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14733-14741
    • Sudol, M.1    Bork, P.2    Einbond, A.3    Kastury, K.4    Druck, T.5    Negrini, M.6    Hueber, K.7    Lehman, D.8
  • 54
    • 0026022320 scopus 로고
    • Recombinant Epstein-Barr virus with small RNA (EBER) genes deleted transforms lymphocytes and replicates in vitro
    • Swaminathan S., Tomkinson B., Kieff E. Recombinant Epstein-Barr virus with small RNA (EBER) genes deleted transforms lymphocytes and replicates in vitro. Proc. Natl. Acad. Sci. USA. 88:1991;1546-1550.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1546-1550
    • Swaminathan, S.1    Tomkinson, B.2    Kieff, E.3
  • 57
    • 0028130271 scopus 로고
    • Epstein-Barr virus latency in blood mononuclear cells: Analysis of viral gene transcription during primary infection and in the carrier state
    • Tierney R. J., Steven N., Young L. S., Rickinson A. B. Epstein-Barr virus latency in blood mononuclear cells: Analysis of viral gene transcription during primary infection and in the carrier state. J. Virol. 68:1994;7374-7385.
    • (1994) J. Virol. , vol.68 , pp. 7374-7385
    • Tierney, R.J.1    Steven, N.2    Young, L.S.3    Rickinson, A.B.4
  • 58
    • 0026549160 scopus 로고
    • Use of second-site homologous recombination to demonstrate that Epstein-Barr virus nuclear protein 3B is not important for lymphocyte infection or growth transformation in vitro
    • Tomkinson B., Kieff E. Use of second-site homologous recombination to demonstrate that Epstein-Barr virus nuclear protein 3B is not important for lymphocyte infection or growth transformation in vitro. J. Virol. 66:1992;2893-2903.
    • (1992) J. Virol. , vol.66 , pp. 2893-2903
    • Tomkinson, B.1    Kieff, E.2
  • 59
    • 0027479649 scopus 로고
    • Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3B are essential for B lymphocyte growth transformation
    • Tomkinson B., Robertson E., Kieff E. Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3B are essential for B lymphocyte growth transformation. J. Virol. 67:1993;2014-2025.
    • (1993) J. Virol. , vol.67 , pp. 2014-2025
    • Tomkinson, B.1    Robertson, E.2    Kieff, E.3
  • 61
    • 0022309824 scopus 로고
    • An EBV membrane protein expressed in immortalized lymphocytes transforms established rodent cells
    • Wang D., Liebowitz D., Kieff E. An EBV membrane protein expressed in immortalized lymphocytes transforms established rodent cells. Cell. 43:1985;831-840.
    • (1985) Cell , vol.43 , pp. 831-840
    • Wang, D.1    Liebowitz, D.2    Kieff, E.3
  • 62
    • 0027328526 scopus 로고
    • Tandem SH2 domains of ZAP-70 bind to T cell antigen receptor zeta and CD3 epsilon from activated Jurkat T cells
    • Wange R. L., Malek S. N., Desiderio S., Samelson L. E. Tandem SH2 domains of ZAP-70 bind to T cell antigen receptor zeta and CD3 epsilon from activated Jurkat T cells. J. Biol. Chem. 268:1993;19797-19801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19797-19801
    • Wange, R.L.1    Malek, S.N.2    Desiderio, S.3    Samelson, L.E.4
  • 63
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss A., Littman D. R. Signal transduction by lymphocyte antigen receptors. Cell. 76:1994;263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 64
    • 0021988550 scopus 로고
    • Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells
    • Yates J. L., Warren N., Sugden B. Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells. Nature. 313:1985;812-815.
    • (1985) Nature , vol.313 , pp. 812-815
    • Yates, J.L.1    Warren, N.2    Sugden, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.