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Volumn 2, Issue 8, 2004, Pages 656-668

Oncogenic γ-herpesviruses: Comparison of viral proteins involved in tumorigenesis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA INTERFERON; B LYMPHOCYTE RECEPTOR; BASIC FIBROBLAST GROWTH FACTOR; BETA CATENIN; CYCLINE; CYCLOOXYGENASE 2; CYTOHESIN 1; FLICE INHIBITORY PROTEIN; G PROTEIN COUPLED RECEPTOR; GELATINASE B; GLYCOGEN SYNTHASE KINASE 3BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 10; INTERLEUKIN 17; INTERLEUKIN 2; LATENCY ASSOCIATED NUCLEAR ANTIGEN; LATENT MEMBRANE PROTEIN 1; MACROPHAGE INFLAMMATORY PROTEIN 1ALPHA; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN P85; RANTES; STAT PROTEIN; T LYMPHOCYTE RECEPTOR; TRANSCRIPTION FACTOR NFAT; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; VASCULOTROPIN; VASCULOTROPIN RECEPTOR 2; VIRUS PROTEIN;

EID: 4344714976     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro958     Document Type: Review
Times cited : (120)

References (160)
  • 2
    • 49749222804 scopus 로고
    • Virus particles in culture lymphoblasts from Burkitt's lymphoma
    • Epstein, M. A., Achong, B. & Barr, Y. Virus particles in culture lymphoblasts from Burkitt's lymphoma. Lancet 15, 702-703 (1964).
    • (1964) Lancet , vol.15 , pp. 702-703
    • Epstein, M.A.1    Achong, B.2    Barr, Y.3
  • 3
    • 0014295381 scopus 로고
    • An apparently new herpesvirus from primary kidney cultures of the squirrel monkey (Saimiri sciureus)
    • Melendez, L. V., Daniel, M. D., Hunt, R. D. & Garcia, F. G. An apparently new herpesvirus from primary kidney cultures of the squirrel monkey (Saimiri sciureus). Lab. Anim. Care 18, 374-381 (1968).
    • (1968) Lab. Anim. Care , vol.18 , pp. 374-381
    • Melendez, L.V.1    Daniel, M.D.2    Hunt, R.D.3    Garcia, F.G.4
  • 4
    • 0028588064 scopus 로고
    • Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma
    • Chang, Y. et al. Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma. Science 266, 1865-1869 (1994).
    • (1994) Science , vol.266 , pp. 1865-1869
    • Chang, Y.1
  • 5
    • 0018194335 scopus 로고
    • Tumour induction with DNA of oncogenic primate herpesviruses
    • Fleckenstein, B. et al. Tumour induction with DNA of oncogenic primate herpesviruses. Nature 274, 57-59 (1978).
    • (1978) Nature , vol.274 , pp. 57-59
    • Fleckenstein, B.1
  • 6
    • 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, 831-840 (1985).
    • (1985) Cell , vol.43 , pp. 831-840
    • Wang, D.1    Liebowitz, D.2    Kieff, E.3
  • 7
    • 0025271424 scopus 로고
    • Epstein-Barr virus latent membrane protein inhibits human epithelial cell differentiation
    • Dawson, C. W., Rickinson, A. B. & Young, L. S. Epstein-Barr virus latent membrane protein inhibits human epithelial cell differentiation. Nature 344, 777-780 (1990).
    • (1990) Nature , vol.344 , pp. 777-780
    • Dawson, C.W.1    Rickinson, A.B.2    Young, L.S.3
  • 8
    • 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, 9150-9154 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9150-9154
    • Kaye, K.M.1    Izumi, K.M.2    Kieff, E.3
  • 9
    • 0033536591 scopus 로고    scopus 로고
    • Mimicry of CD40 signals by Epstein-Barr virus LMP1 in B-lymphocyte responses
    • Uchida, J. et al. Mimicry of CD40 signals by Epstein-Barr virus LMP1 in B-lymphocyte responses. Science 286, 300-303 (1999).
    • (1999) Science , vol.286 , pp. 300-303
    • Uchida, J.1
  • 10
    • 0030716307 scopus 로고    scopus 로고
    • Latent membrane protein 1 of Epstein-Barr virus mimics a constitutively active receptor molecule
    • Gires, O. et al. Latent membrane protein 1 of Epstein-Barr virus mimics a constitutively active receptor molecule. EMBO J. 16, 6131-6140 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6131-6140
    • Gires, O.1
  • 11
    • 0031939402 scopus 로고    scopus 로고
    • A fusion of the EBV latent membrane protein-1 (LMP1) transmembrane domains to the CD40 cytoplasmic domain is similar to LMP1 in constitutive activation of epidermal growth factor receptor expression, nuclear factor-κB, and stress-activated protein kinase
    • Hatzivassiliou, E., Miller, W. E., Raab-Traub, N., Kieff, E. & Mosialos, G. A fusion of the EBV latent membrane protein-1 (LMP1) transmembrane domains to the CD40 cytoplasmic domain is similar to LMP1 in constitutive activation of epidermal growth factor receptor expression, nuclear factor-κB, and stress-activated protein kinase. J. Immunol. 160, 1116-1121 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 1116-1121
    • Hatzivassiliou, E.1    Miller W., E.2    Raab-Traub, N.3    Kieff, E.4    Mosialos, G.5
  • 12
    • 0032536860 scopus 로고    scopus 로고
    • Epstein-Barr virus-mediated B-cell proliferation is dependent upon latent membrane protein 1, which simulates an activated CD40 receptor
    • Kilger, E., Kieser, A., Baumann, M. & Hammerschmidth, W. Epstein-Barr virus-mediated B-cell proliferation is dependent upon latent membrane protein 1, which simulates an activated CD40 receptor. EMBO J. 17, 1700-1709 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1700-1709
    • Kilger, E.1    Kieser, A.2    Baumann, M.3    Hammerschmidth, W.4
  • 13
    • 0028853402 scopus 로고
    • The Epstein-Barr virus latent membrane protein-1 (LMP1) mediates activation of NF-κB and cell surface phenotype via two effector regions in its carboxy-terminal cytoplasmic domain
    • Huen, D. S., Henderson, S. A., Croom-Carter, D. & Rowe, M. The Epstein-Barr virus latent membrane protein-1 (LMP1) mediates activation of NF-κB and cell surface phenotype via two effector regions in its carboxy-terminal cytoplasmic domain. Oncogene 10, 549-560 (1995).
    • (1995) Oncogene , vol.10 , pp. 549-560
    • Huen, D.S.1    Henderson, S.A.2    Croom-Carter, D.3    Rowe, M.4
  • 14
    • 0029037660 scopus 로고
    • Expression of LMP1 in epithelial cells leads to the activation of a select subset of NF-κB/Rel family proteins
    • Paine, E., Scheinman, R. I., Baldwin, A. S. Jr & Raab-Traub, N. Expression of LMP1 in epithelial cells leads to the activation of a select subset of NF-κB/Rel family proteins. J. Virol. 69, 4572-4576 (1995).
    • (1995) J. Virol. , vol.69 , pp. 4572-4576
    • Paine, E.1    Scheinman, R.I.2    Baldwin Jr., A.S.3    Raab-Traub, N.4
  • 15
    • 0032750420 scopus 로고    scopus 로고
    • An Epstein-Barr virus that expresses only the first 231 LMP1 amino acids efficiently initiates primary B-lymphocyte growth transformation
    • Kaye, K. M. et al. An Epstein-Barr virus that expresses only the first 231 LMP1 amino acids efficiently initiates primary B-lymphocyte growth transformation. J. Virol. 73, 10525-10530 (1999).
    • (1999) J. Virol. , vol.73 , pp. 10525-10530
    • Kaye, K.M.1
  • 16
    • 0031718910 scopus 로고    scopus 로고
    • Role of the TRAF-binding site and NF-κB activation in Epstein-Barr virus latent membrane protein 1-induced cell gene expression
    • Devergne, O. et al. Role of the TRAF-binding site and NF-κB activation in Epstein-Barr virus latent membrane protein 1-induced cell gene expression. J. Virol. 72, 7900-7908 (1998).
    • (1998) J. Virol. , vol.72 , pp. 7900-7908
    • Devergne, O.1
  • 17
    • 0032901776 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded latent membrane protein 1 activates the JNK pathway through its extreme C terminus via a mechanism involving TRADD and TRAF2
    • Eliopoulos, A. G., Blake, S. M., Floettmann, J. E., Rowe, M. & Young, L. S. Epstein-Barr virus-encoded latent membrane protein 1 activates the JNK pathway through its extreme C terminus via a mechanism involving TRADD and TRAF2. J. Virol. 73, 1023-1035 (1999).
    • (1999) J. Virol. , vol.73 , pp. 1023-1035
    • Eliopoulos, A.G.1    Blake, S.M.2    Floettmann, J.E.3    Rowe, M.4    Young, L.S.5
  • 18
    • 0032788548 scopus 로고    scopus 로고
    • The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-κB activation
    • Izumi, K. M. et al. The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-κB activation. Mol. Cell. Biol. 19, 5759-5767 (1999).
    • (1999) Mol. Cell Biol. , vol.19 , pp. 5759-5767
    • Izumi, K.M.1
  • 19
    • 0030925641 scopus 로고    scopus 로고
    • Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3
    • Sandberg, M., Hammerschmidt, W. & Sugden, B. Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3. J. Virol. 71, 4649-4656 (1997).
    • (1997) J. Virol. , vol.71 , pp. 4649-4656
    • Sandberg, M.1    Hammerschmidt, W.2    Sugden, B.3
  • 20
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe, M., Wong, S. C., Henzel, W. J. & Goeddel, D. V. A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell 78, 681-692 (1994).
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 21
    • 0032750932 scopus 로고    scopus 로고
    • The residues between the two transformation effector sites of Epstein-Barr virus latent membrane protein 1 are not critical for B-lymphocyte growth transformation
    • Izumi, K. M. et al. The residues between the two transformation effector sites of Epstein-Barr virus latent membrane protein 1 are not critical for B-lymphocyte growth transformation. J. Virol. 73, 9908-9916 (1999).
    • (1999) J. Virol. , vol.73 , pp. 9908-9916
    • Izumi, K.M.1
  • 22
    • 0037423201 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 (LMP1) activates the phosphatidylinositol 3-kinase/Akt pathway to promote cell survival and induce actin filament remodeling
    • Dawson, C. W., Tramountanis, G., Eliopoulos, A. G. & Young, L. S. Epstein-Barr virus latent membrane protein 1 (LMP1) activates the phosphatidylinositol 3-kinase/Akt pathway to promote cell survival and induce actin filament remodeling. J. Biol. Chem. 278, 3694-3704 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 3694-3704
    • Dawson, C.W.1    Tramountanis, G.2    Eliopoulos, A.G.3    Young, L.S.4
  • 23
    • 0032473910 scopus 로고    scopus 로고
    • Activation of the cJun N-terminal kinase (JNK) pathway by the Epstein-Barr virus-encoded latent membrane protein 1 (LMP1)
    • Eliopoulos, A. G. & Young, L. S. Activation of the cJun N-terminal kinase (JNK) pathway by the Epstein-Barr virus-encoded latent membrane protein 1 (LMP1). Oncogene 16, 1731-1742 (1998).
    • (1998) Oncogene , vol.16 , pp. 1731-1742
    • Eliopoulos, A.G.1    Young, L.S.2
  • 24
    • 0035836746 scopus 로고    scopus 로고
    • Epstein-Barr virus latent-infection membrane proteins are palmitoylated and raft-associated: Protein 1 binds to the cytoskeleton through TNF receptor cytoplasmic factors
    • Higuchi, M., Izumi, K. M. & Kieff, E. Epstein-Barr virus latent-infection membrane proteins are palmitoylated and raft-associated: protein 1 binds to the cytoskeleton through TNF receptor cytoplasmic factors. Proc. Natl Acad. Sci. USA 98, 4675-4680 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4675-4680
    • Higuchi, M.1    Izumi, K.M.2    Kieff, E.3
  • 25
    • 0347088997 scopus 로고    scopus 로고
    • Latent infection membrane protein transmembrane FWLY is critical for intermolecular interaction, raft localization, and signaling
    • Yasui, T., Luftig, M., Soni, V. & Kieff, E. Latent infection membrane protein transmembrane FWLY is critical for intermolecular interaction, raft localization, and signaling. Proc. Natl Acad. Sci. USA 101, 278-283 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 278-283
    • Yasui, T.1    Luftig, M.2    Soni, V.3    Kieff, E.4
  • 26
    • 0035811070 scopus 로고    scopus 로고
    • Induction of cyclooxygenase-2 by Epstein-Barr virus latent membrane protein 1 is involved in vascular endothelial growth factor production in nasopharyngeal carcinoma cells
    • Murono, S. et al. Induction of cyclooxygenase-2 by Epstein-Barr virus latent membrane protein 1 is involved in vascular endothelial growth factor production in nasopharyngeal carcinoma cells. Proc. Natl Acad. Sci. USA 98, 6905-6910 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6905-6910
    • Murono, S.1
  • 27
    • 0036829132 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 induces and causes release of fibroblast growth factor-2
    • Wakisaka, N., Murono, S., Yoshizaki, T., Furukawa, M. & Pagano, J. S. Epstein-Barr virus latent membrane protein 1 induces and causes release of fibroblast growth factor-2. Cancer Res. 62, 6337-6344 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 6337-6344
    • Wakisaka, N.1    Murono, S.2    Yoshizaki, T.3    Furukawa, M.4    Pagano, J.S.5
  • 28
    • 0032584221 scopus 로고    scopus 로고
    • The expression of matrix metalloproteinase 9 is enhanced by Epstein-Barr virus latent membrane protein 1
    • Yoshizaki, T., Sato, H., Furukawa, M. & Pagano, J. S. The expression of matrix metalloproteinase 9 is enhanced by Epstein-Barr virus latent membrane protein 1. Proc. Natl Acad. Sci. USA 95, 3621-3626 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3621-3626
    • Yoshizaki, T.1    Sato, H.2    Furukawa, M.3    Pagano, J.S.4
  • 29
    • 0346365370 scopus 로고    scopus 로고
    • Activation of nuclear factor-κB p50 homodimer/Bcl-3 complexes in nasopharyngeal carcinoma
    • Thornburg, N. J., Pathmanathan, R. & Raab-Traub, N. Activation of nuclear factor-κB p50 homodimer/Bcl-3 complexes in nasopharyngeal carcinoma. Cancer Res. 63, 8293-8301 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 8293-8301
    • Thornburg, N.J.1    Pathmanathan, R.2    Raab-Traub, N.3
  • 30
    • 0032499227 scopus 로고    scopus 로고
    • The NPC derived C15 LMP1 protein confers enhanced activation of NF-κB and induction of the EGFR in epithelial cells
    • Miller, W. E., Cheshire, J. L., Baldwin, A. S. Jr & Raab-Traub, N. The NPC derived C15 LMP1 protein confers enhanced activation of NF-κB and induction of the EGFR in epithelial cells. Oncogene 16, 1869-1877 (1998).
    • (1998) Oncogene , vol.16 , pp. 1869-1877
    • Miller, W.E.1    Cheshire, J.L.2    Baldwin Jr., A.S.3    Raab-Traub, N.4
  • 31
    • 17344385795 scopus 로고    scopus 로고
    • Deregulation of cell growth by the K1 gene of Kaposi's sarcoma-associated herpesvirus
    • Lee, H. et al. Deregulation of cell growth by the K1 gene of Kaposi's sarcoma-associated herpesvirus. Nature Med. 4, 435-440 (1998).
    • (1998) Nature Med. , vol.4 , pp. 435-440
    • Lee, H.1
  • 32
    • 0037134705 scopus 로고    scopus 로고
    • Tumorigenesis and aberrant signaling in transgenic mice expressing the human herpesvirus-8 k1 gene
    • Prakash, O. et al. Tumorigenesis and aberrant signaling in transgenic mice expressing the human herpesvirus-8 k1 gene. J. Natl Cancer Inst. 94, 926-935 (2002).
    • (2002) J. Natl. Cancer Inst. , vol.94 , pp. 926-935
    • Prakash, O.1
  • 33
    • 0031572167 scopus 로고    scopus 로고
    • The structure and coding organization of the genomic termini of Kaposi's sarcoma-associated herpesvirus
    • Lagunoff, M. & Ganem, D. The structure and coding organization of the genomic termini of Kaposi's sarcoma-associated herpesvirus. Virology 236, 147-154 (1997).
    • (1997) Virology , vol.236 , pp. 147-154
    • Lagunoff, M.1    Ganem, D.2
  • 34
    • 0033545865 scopus 로고    scopus 로고
    • Deregulated signal transduction by the K1 gene product of Kaposi's sarcoma-associated herpesvirus
    • Lagunoff, M., Majeti, R., Weiss, A. & Ganem, D. Deregulated signal transduction by the K1 gene product of Kaposi's sarcoma-associated herpesvirus. Proc. Natl Acad. Sci. USA 96, 5704-5709 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5704-5709
    • Lagunoff, M.1    Majeti, R.2    Weiss, A.3    Ganem, D.4
  • 35
    • 0031813291 scopus 로고    scopus 로고
    • Identification of an immunoreceptor tyrosine-based activation motif of K1 transforming protein of Kaposi's sarcoma-associated herpesvirus
    • Lee, H. et al. Identification of an immunoreceptor tyrosine-based activation motif of K1 transforming protein of Kaposi's sarcoma-associated herpesvirus. Mol. Cell. Biol. 18, 5219-5228 (1998).
    • (1998) Mol. Cell Biol. , vol.18 , pp. 5219-5228
    • Lee, H.1
  • 36
    • 0842304506 scopus 로고    scopus 로고
    • The K1 protein of Kaposi's sarcoma-associated herpesvirus activates the Akt signaling pathway
    • Tomlinson, C. C. & Damania, B. The K1 protein of Kaposi's sarcoma-associated herpesvirus activates the Akt signaling pathway. J. Virol. 78, 1918-1927 (2004).
    • (2004) J. Virol. , vol.78 , pp. 1918-1927
    • Tomlinson, C.C.1    Damania, B.2
  • 37
    • 0028969818 scopus 로고
    • Inflammatory cytokines induce AIDS-Kaposi's sarcoma-derived spindle cells to produce and release basic fibroblast growth factor and enhance Kaposi's sarcoma-like lesion formation in nude mice
    • Samaniego, F., Markham, P. D., Gallo, R. C. & Ensoli, B. Inflammatory cytokines induce AIDS-Kaposi's sarcoma-derived spindle cells to produce and release basic fibroblast growth factor and enhance Kaposi's sarcoma-like lesion formation in nude mice. J. Immunol. 154, 3582-3592 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 3582-3592
    • Samaniego, F.1    Markham, P.D.2    Gallo, R.C.3    Ensoli, B.4
  • 38
    • 0003064250 scopus 로고    scopus 로고
    • Human herpesvirus 8 K1-associated nuclear factor-κB-dependent promoter activity: Role in Kaposi's sarcoma inflammation?
    • Samaniego, F., Pati, S., Karp, J., Prakash, O. & Bose, D. Human herpesvirus 8 K1-associated nuclear factor-κB-dependent promoter activity: role in Kaposi's sarcoma inflammation? J. Natl Cancer Inst. Monogr. 28, 15-23 (2001).
    • (2001) J. Natl. Cancer Inst. Monogr. , vol.28 , pp. 15-23
    • Samaniego, F.1    Pati, S.2    Karp, J.3    Prakash, O.4    Bose, D.5
  • 39
    • 0037744675 scopus 로고    scopus 로고
    • Structural analysis of the Kaposi's sarcoma-associated herpesvirus K1 protein
    • Lee, B. S., Connole, M., Tang, Z., Harris, N. L. & Jung, J. U. Structural analysis of the Kaposi's sarcoma-associated herpesvirus K1 protein. J. Virol. 77, 8072-8086 (2003).
    • (2003) J. Virol. , vol.77 , pp. 8072-8086
    • Lee, B.S.1    Connole, M.2    Tang, Z.3    Harris, N.L.4    Jung, J.U.5
  • 40
    • 2442692617 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus (KSHV/HHV8) K1 protein induces expression of angiogenic and invasion factors
    • Wang, L. et al. The Kaposi's sarcoma-associated herpesvirus (KSHV/HHV8) K1 protein induces expression of angiogenic and invasion factors. Cancer Res. 64, 2774-2781 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 2774-2781
    • Wang, L.1
  • 41
    • 0019974667 scopus 로고
    • Herpesvirus saimiri strain variability
    • Desrosiers, R. C. & Falk, L. A. Herpesvirus saimiri strain variability. J. Virol. 43, 352-356 (1982).
    • (1982) J. Virol. , vol.43 , pp. 352-356
    • Desrosiers, R.C.1    Falk, L.A.2
  • 42
    • 0031906144 scopus 로고    scopus 로고
    • STP and TIP are essential for herpesvirus saimiri oncogenicity
    • Duboise, S. M., Guo, J., Czajak, S., Desrosiers, R. C. & Jung, J. U. STP and TIP are essential for herpesvirus saimiri oncogenicity. J. Virol. 72, 1308-1313 (1998).
    • (1998) J. Virol. , vol.72 , pp. 1308-1313
    • Duboise, S.M.1    Guo, J.2    Czajak, S.3    Desrosiers, R.C.4    Jung, J.U.5
  • 43
    • 0024353812 scopus 로고
    • Deletion mutants of herpesvirus saimiri define an open reading frame necessary for transformation
    • Murthy, S. C., Trimble, J. J. & Desrosiers, R. C. Deletion mutants of herpesvirus saimiri define an open reading frame necessary for transformation. J. Virol. 63, 3307-3314 (1989).
    • (1989) J. Virol. , vol.63 , pp. 3307-3314
    • Murthy, S.C.1    Trimble, J.J.2    Desrosiers, R.C.3
  • 44
    • 0025785530 scopus 로고
    • Identification of transforming genes of subgroup A and C strains of herpesvirus saimiri
    • Jung, J. U. et al. Identification of transforming genes of subgroup A and C strains of herpesvirus saimiri. Proc. Natl Acad. Sci. USA 88, 7051-7055 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7051-7055
    • Jung, J.U.1
  • 45
    • 0033901337 scopus 로고    scopus 로고
    • The collagen repeat sequence is a determinant of the degree of herpesvirus saimiri STP transforming activity
    • Choi, J. K., Ishido, S. & Jung, J. U. The collagen repeat sequence is a determinant of the degree of herpesvirus saimiri STP transforming activity. J. Virol. 74, 8102-8110 (2000).
    • (2000) J. Virol. , vol.74 , pp. 8102-8110
    • Choi, J.K.1    Ishido, S.2    Jung, J.U.3
  • 46
    • 0028788824 scopus 로고
    • Association of the viral oncoprotein STP-C488 with cellular Ras
    • Jung, J. U. & Desrosiers, R. C. Association of the viral oncoprotein STP-C488 with cellular Ras. Mol. Cell. Biol. 15, 6506-6512 (1995).
    • (1995) Mol. Cell Biol. , vol.15 , pp. 6506-6512
    • Jung, J.U.1    Desrosiers, R.C.2
  • 47
    • 0032898259 scopus 로고    scopus 로고
    • Role of cellular tumor necrosis factor receptor-associated factors in NF-κB activation and lymphocyte transformation by herpesvirus saimiri STP
    • Lee, H. et al. Role of cellular tumor necrosis factor receptor-associated factors in NF-κB activation and lymphocyte transformation by herpesvirus saimiri STP. J. Virol. 73, 3913-3919 (1999).
    • (1999) J. Virol. , vol.73 , pp. 3913-3919
    • Lee, H.1
  • 48
    • 0026582459 scopus 로고
    • Consistent transcription of the Epstein-Barr virus LMP2 gene in nasopharyngeal carcinoma
    • Busson, P. et al. Consistent transcription of the Epstein-Barr virus LMP2 gene in nasopharyngeal carcinoma. J. Virol. 66, 3257-3262 (1992).
    • (1992) J. Virol. , vol.66 , pp. 3257-3262
    • Busson, P.1
  • 49
    • 0024535280 scopus 로고
    • Two related Epstein-Barr virus membrane proteins are encoded by separate genes
    • Sample, J., Liebowitz, D. & Kieff, E. Two related Epstein-Barr virus membrane proteins are encoded by separate genes. J. Virol. 63, 933-937 (1989).
    • (1989) J. Virol. , vol.63 , pp. 933-937
    • Sample, J.1    Liebowitz, D.2    Kieff, E.3
  • 50
    • 0030754766 scopus 로고    scopus 로고
    • The immunoreceptor tyrosine-based activation motif of Epstein-Barr virus LMP2A is essential for blocking BCR-mediated signal transduction
    • Fruehling, S. & Longnecker, R. The immunoreceptor tyrosine-based activation motif of Epstein-Barr virus LMP2A is essential for blocking BCR-mediated signal transduction. Virology 235, 241-251 (1997).
    • (1997) Virology , vol.235 , pp. 241-251
    • Fruehling, S.1    Longnecker, R.2
  • 51
    • 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, 3087-3094 (1993).
    • (1993) J. Virol. , vol.67 , pp. 3087-3094
    • Miller, C.L.1    Longnecker, R.2    Kieff, E.3
  • 52
    • 0035126502 scopus 로고    scopus 로고
    • Epstein-Barr virus co-opts lipid rafts to block the signaling and antigen transport functions of the BCR
    • Dykstra, M. L., Longnecker, R. & Pierce, S. K. Epstein-Barr virus co-opts lipid rafts to block the signaling and antigen transport functions of the BCR. Immunity 14, 57-67 (2001).
    • (2001) Immunity , vol.14 , pp. 57-67
    • Dykstra, M.L.1    Longnecker, R.2    Pierce, S.K.3
  • 53
    • 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, 772-776 (1994).
    • (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
  • 54
    • 0842326032 scopus 로고    scopus 로고
    • Latent membrane protein 2A inhibits transforming growth factor-β1-induced apoptosis through the phosphatidylinositol 3-kinase/Akt pathway
    • Fukuda, M. & Longnecker, R. Latent membrane protein 2A inhibits transforming growth factor-β1-induced apoptosis through the phosphatidylinositol 3-kinase/Akt pathway. J. Virol. 78, 1697-1705 (2004).
    • (2004) J. Virol. , vol.78 , pp. 1697-1705
    • Fukuda, M.1    Longnecker, R.2
  • 55
    • 0032169313 scopus 로고    scopus 로고
    • Epstein-Barr virus LMP2A drives B cell development and survival in the absence of normal B cell receptor signals
    • Caldwell, R. G., Wilson, J. B., Anderson, S. J. & Longnecker, R. Epstein-Barr virus LMP2A drives B cell development and survival in the absence of normal B cell receptor signals. Immunity 9, 405-411 (1998).
    • (1998) Immunity , vol.9 , pp. 405-411
    • Caldwell, R.G.1    Wilson, J.B.2    Anderson, S.J.3    Longnecker, R.4
  • 56
    • 0027537458 scopus 로고
    • The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitro
    • Longnecker, R., Miller, C. L., Miao, X. Q., Tomkinson, B. & Kieff, E. The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitro. J. Virol. 67, 2006-2013 (1993).
    • (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
  • 57
    • 0033756107 scopus 로고    scopus 로고
    • Epstein-Barr virus LMP2A transforms epthelial cells, inhibits cell differentiation, and activates Akt
    • Scholle, F., Bendt, K. M. & Raab-Traub, N. Epstein-Barr virus LMP2A transforms epthelial cells, inhibits cell differentiation, and activates Akt. J. Virol. 74, 10681-10689 (2000).
    • (2000) J. Virol. , vol.74 , pp. 10681-10689
    • Scholle, F.1    Bendt, K.M.2    Raab-Traub, N.3
  • 58
    • 0242363228 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 2A activates β-catenin signaling in epithelial cells
    • Morrison, J. A., Klingelhutz, A. J. & Raab-Traub, N. Epstein-Barr virus latent membrane protein 2A activates β-catenin signaling in epithelial cells. J. Virol. 77, 12276-12284 (2003).
    • (2003) J. Virol. , vol.77 , pp. 12276-12284
    • Morrison, J.A.1    Klingelhutz, A.J.2    Raab-Traub, N.3
  • 59
    • 0032775720 scopus 로고    scopus 로고
    • Identification of a spliced gene from Kaposi's sarcoma-associated herpesvirus encoding a protein with similarities to latent membrane proteins 1 and 2A of Epstein-Barr virus
    • Glenn, M., Rainbow, L., Aurad, F., Davison, A. & Schulz, T. F. Identification of a spliced gene from Kaposi's sarcoma-associated herpesvirus encoding a protein with similarities to latent membrane proteins 1 and 2A of Epstein-Barr virus. J. Virol. 73, 6953-6963 (1999).
    • (1999) J. Virol. , vol.73 , pp. 6953-6963
    • Glenn, M.1    Rainbow, L.2    Aurad, F.3    Davison, A.4    Schulz, T.F.5
  • 60
    • 0033989865 scopus 로고    scopus 로고
    • Identification of the novel K15 gene at the right-most end of Kaposi's sarcoma-associated herpesvirus genome
    • Choi, J., Lee, B. S., Shim, S., Li, M. & Jung, J. U. Identification of the novel K15 gene at the right-most end of Kaposi's sarcoma-associated herpesvirus genome. J. Virol. 74, 436-446 (2000).
    • (2000) J. Virol. , vol.74 , pp. 436-446
    • Choi, J.1    Lee, B.S.2    Shim, S.3    Li, M.4    Jung, J.U.5
  • 61
    • 0032786533 scopus 로고    scopus 로고
    • Comparison of genetic variability at multiple loci across the genomes of the major subtypes of Kaposi's sarcoma-associated herpesvirus reveals evidence for recombination and for two distinct types of open reading frame K15 alleles at the right-hand end
    • Poole, L. J. et al. Comparison of genetic variability at multiple loci across the genomes of the major subtypes of Kaposi's sarcoma-associated herpesvirus reveals evidence for recombination and for two distinct types of open reading frame K15 alleles at the right-hand end. J. Virol. 73, 6646-6660 (1999).
    • (1999) J. Virol. , vol.73 , pp. 6646-6660
    • Poole, L.J.1
  • 62
    • 0041387452 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase and NF-κB pathways by a Kaposi's sarcoma-associated herpesvirus K15 membrane protein
    • Brinkmann, M. M. et al. Activation of mitogen-activated protein kinase and NF-κB pathways by a Kaposi's sarcoma-associated herpesvirus K15 membrane protein. J. Virol. 77, 9346-9358 (2003).
    • (2003) J. Virol. , vol.77 , pp. 9346-9358
    • Brinkmann, M.M.1
  • 63
    • 0028940769 scopus 로고
    • The product of the herpesvirus saimiri open reading frame 1 (TIP) interacts with T-cell-specific kinase p56lck in transformed cells
    • Biesinger, B. et al. The product of the herpesvirus saimiri open reading frame 1 (TIP) interacts with T-cell-specific kinase p56lck in transformed cells. J. Biol. Chem. 270, 4729-4734 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 4729-4734
    • Biesinger, B.1
  • 64
    • 0029098127 scopus 로고
    • Identification of Lck-binding elements in tip of herpesvirus saimiri
    • Jung, J. U. et al. Identification of Lck-binding elements in tip of herpesvirus saimiri. J. Biol. Chem. 270, 20660-20667 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 20660-20667
    • Jung, J.U.1
  • 65
    • 0028800298 scopus 로고
    • Downregulation of Lck-mediated signal transduction by TIP of herpesvirus saimiri
    • Jung, J. U. et al. Downregulation of Lck-mediated signal transduction by TIP of herpesvirus saimiri. J. Virol. 69, 7814-7822 (1995).
    • (1995) J. Virol. , vol.69 , pp. 7814-7822
    • Jung, J.U.1
  • 66
    • 0036308581 scopus 로고    scopus 로고
    • The herpesvirus saimiri TIP484 and TIP488 proteins both stimulate lck tyrosine protein kinase activity in vivo and in vitro
    • Kjellen, P., Amdjadi, K., Lund, T. C., Medveczky, P. G. & Sefton, B. M. The herpesvirus saimiri TIP484 and TIP488 proteins both stimulate lck tyrosine protein kinase activity in vivo and in vitro. Virology 297, 281-288 (2002).
    • (2002) Virology , vol.297 , pp. 281-288
    • Kjellen, P.1    Amdjadi, K.2    Lund, T.C.3    Medveczky, P.G.4    Sefton, B.M.5
  • 67
    • 0031060289 scopus 로고    scopus 로고
    • Herpesvirus saimiri TIP-484 membrane protein markedly increases p56lck activity in T cells
    • Lund, T., Medveczky, M. M. & Medveczky, P. G. Herpesvirus saimiri TIP-484 membrane protein markedly increases p56lck activity in T cells. J. Virol. 71, 378-382 (1997).
    • (1997) J. Virol. , vol.71 , pp. 378-382
    • Lund, T.1    Medveczky, M.M.2    Medveczky, P.G.3
  • 68
    • 0030761720 scopus 로고    scopus 로고
    • Enhanced downregulation of Lck-mediated signal transduction by a Y114 mutation of herpesvirus saimiri TIP
    • Guo, J. et al. Enhanced downregulation of Lck-mediated signal transduction by a Y114 mutation of herpesvirus saimiri TIP. J. Virol. 71, 7092-7096 (1997).
    • (1997) J. Virol. , vol.71 , pp. 7092-7096
    • Guo, J.1
  • 69
    • 0032927057 scopus 로고    scopus 로고
    • The Lck binding domain of herpesvirus saimiri TIP-484 constitutively activates Lck and STAT3 in T cells
    • Lund, T. C., Prator, P. C., Medveczky, M. M. & Medveczky, P. G. The Lck binding domain of herpesvirus saimiri TIP-484 constitutively activates Lck and STAT3 in T cells. J. Virol. 73, 1689-1694 (1999).
    • (1999) J. Virol. , vol.73 , pp. 1689-1694
    • Lund, T.C.1    Prator, P.C.2    Medveczky, M.M.3    Medveczky, P.G.4
  • 70
    • 0035119515 scopus 로고    scopus 로고
    • Herpesvirus saimiri Tip gene causes T-cell lymphomas in transgenic mice
    • Wehner, L. E. et al. Herpesvirus saimiri Tip gene causes T-cell lymphomas in transgenic mice. DNA Cell. Biol. 20, 81-88 (2001).
    • (2001) DNA Cell Biol. , vol.20 , pp. 81-88
    • Wehner, L.E.1
  • 71
    • 0025771410 scopus 로고
    • Epstein-Barr virus nuclear protein 2 transactivates a cis-acting CD23 DNA element
    • Wang, F., Kikutani, H., Tsang, S. F., Kishimoto, T. & Kieff, E. Epstein-Barr virus nuclear protein 2 transactivates a cis-acting CD23 DNA element. J. Virol. 65, 4101-4106 (1991).
    • (1991) J. Virol. , vol.65 , pp. 4101-4106
    • Wang, F.1    Kikutani, H.2    Tsang, S.F.3    Kishimoto, T.4    Kieff, E.5
  • 72
    • 0028124316 scopus 로고
    • The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J κ recombination signal-binding protein
    • Grossman, S. R., Johannsen, E., Tong, X., Yalamanchili, R. & Kieff, E. The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J κ recombination signal-binding protein. Proc. Natl Acad. Sci. USA 91, 7568-7572 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7568-7572
    • Grossman, S.R.1    Johannsen, E.2    Tong, X.3    Yalamanchili, R.4    Kieff, E.5
  • 73
    • 0032923696 scopus 로고    scopus 로고
    • The proto-oncogene c-myc is a direct target gene of Epstein-Barr virus nuclear antigen 2
    • Kaiser, C. et al. The proto-oncogene c-myc is a direct target gene of Epstein-Barr virus nuclear antigen 2. J. Virol. 73, 4481-4484 (1999).
    • (1999) J. Virol. , vol.73 , pp. 4481-4484
    • Kaiser, C.1
  • 74
    • 0028924735 scopus 로고
    • The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein
    • Tong, X., Wang, F., Thut, C. J. & Kieff, E. The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein. J. Virol. 69, 585-588 (1995).
    • (1995) J. Virol. , vol.69 , pp. 585-588
    • Tong, X.1    Wang, F.2    Thut, C.J.3    Kieff, E.4
  • 75
    • 0034602777 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter
    • Wang, L., Grossman, S. R. & Kieff, E. Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter. Proc. Natl Acad. Sci. USA 97, 430-435 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 430-435
    • Wang, L.1    Grossman, S.R.2    Kieff, E.3
  • 76
    • 0020447692 scopus 로고
    • Non-immortalizing P3J-HR-1 Epstein-Barr virus: A deletion mutant of its transforming parent, Jijoye
    • Rabson, M., Gradoville, L., Heston, L. & Miller, G. Non-immortalizing P3J-HR-1 Epstein-Barr virus: a deletion mutant of its transforming parent, Jijoye. J. Virol, 44, 834-844 (1982).
    • (1982) J. Virol. , vol.44 , pp. 834-844
    • Rabson, M.1    Gradoville, L.2    Heston, L.3    Miller, G.4
  • 77
    • 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, 393-397 (1989).
    • (1989) Nature , vol.340 , pp. 393-397
    • Hammerschmidt, W.1    Sugden, B.2
  • 78
    • 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, 9558-9562 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9558-9562
    • Cohen, J.I.1    Wang, F.2    Mannick, J.3    Kieff, E.4
  • 79
    • 0027479649 scopus 로고
    • Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation
    • Tomkinson, B., Robertson, E. & Kieff, E. Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation. J. Virol. 67, 2014-2025 (1993).
    • (1993) J. Virol. , vol.67 , pp. 2014-2025
    • Tomkinson, B.1    Robertson, E.2    Kieff, E.3
  • 80
    • 0027967308 scopus 로고
    • Biochemical characterization of Epstein-Barr virus nuclear antigen 3A and 3C proteins
    • Sample, C. & Parker, B. Biochemical characterization of Epstein-Barr virus nuclear antigen 3A and 3C proteins. Virology 205, 534-539 (1994).
    • (1994) Virology , vol.205 , pp. 534-539
    • Sample, C.1    Parker, B.2
  • 81
    • 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, 2893-2903 (1992).
    • (1992) J. Virol. , vol.66 , pp. 2893-2903
    • Tomkinson, B.1    Kieff, E.2
  • 82
    • 0028076871 scopus 로고
    • The Epstein-Barr virus determined nuclear antigens EBNA-3A, -3B, and -3C repress EBNA-2-mediated transactivation of the viral terminal protein 1 gene promoter
    • Le Roux, A., Kerdiles, B., Walls, D., Dedieu, J. F. & Perricaudet, M. The Epstein-Barr virus determined nuclear antigens EBNA-3A, -3B, and -3C repress EBNA-2-mediated transactivation of the viral terminal protein 1 gene promoter. Virology 205, 596-602 (1994).
    • (1994) Virology , vol.205 , pp. 596-602
    • Le Roux, A.1    Kerdiles, B.2    Walls, D.3    Dedieu, J.F.4    Perricaudet, M.5
  • 83
    • 0029990265 scopus 로고    scopus 로고
    • The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(κ)
    • Robertson, E. S., Lin, J. & Kieff, E. The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(κ). J. Virol. 70, 3068-3074 (1996).
    • (1996) J. Virol. , vol.70 , pp. 3068-3074
    • Robertson, E.S.1    Lin, J.2    Kieff, E.3
  • 84
    • 0029013590 scopus 로고
    • Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator
    • Marshall, D. & Sample, C. Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator. J. Virol. 69, 3624-3630 (1995).
    • (1995) J. Virol. , vol.69 , pp. 3624-3630
    • Marshall, D.1    Sample, C.2
  • 85
    • 0030477260 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen (EBNA)3C is an immortalizing oncoprotein with similar properties to adenovirus E1A and papillomavirus E7
    • Parker, G. A. et al. Epstein-Barr virus nuclear antigen (EBNA)3C is an immortalizing oncoprotein with similar properties to adenovirus E1A and papillomavirus E7. Oncogene 13, 2541-2549 (1996).
    • (1996) Oncogene , vol.13 , pp. 2541-2549
    • Parker, G.A.1
  • 86
    • 0032899921 scopus 로고    scopus 로고
    • Cellular tropism and viral interleukin-6 expression distinguish human herpesvirus 8 involvement in Kaposi's sarcoma, primary effusion lymphoma, and multicentric Castleman's disease
    • Staskus, K. A. et al. Cellular tropism and viral interleukin-6 expression distinguish human herpesvirus 8 involvement in Kaposi's sarcoma, primary effusion lymphoma, and multicentric Castleman's disease. J. Virol. 73, 4181-4187 (1999).
    • (1999) J. Virol. , vol.73 , pp. 4181-4187
    • Staskus, K.A.1
  • 87
    • 0032991715 scopus 로고    scopus 로고
    • A complex translational program generates multiple novel proteins from the latently expressed kaposin (K12) locus of Kaposi's sarcoma-associated herpesvirus
    • Sadler, R. et al. A complex translational program generates multiple novel proteins from the latently expressed kaposin (K12) locus of Kaposi's sarcoma-associated herpesvirus. J. Virol. 73, 5722-5730 (1999).
    • (1999) J. Virol. , vol.73 , pp. 5722-5730
    • Sadler, R.1
  • 88
    • 0035025060 scopus 로고    scopus 로고
    • Signaling by human herpesvirus 8 kaposin A through direct membrane recruitment of cytohesin-1
    • Kliche, S. et al. Signaling by human herpesvirus 8 kaposin A through direct membrane recruitment of cytohesin-1. Mol. Cell 7, 833-843 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 833-843
    • Kliche, S.1
  • 89
    • 0031901339 scopus 로고    scopus 로고
    • Identification of kaposin (open reading frame K12) as a human herpesvirus 8 (Kaposi's sarcoma-associated herpesvirus) transforming gene
    • Muralidhar, S. et al. Identification of kaposin (open reading frame K12) as a human herpesvirus 8 (Kaposi's sarcoma-associated herpesvirus) transforming gene. J. Virol. 72, 4980-4988 (1998).
    • (1998) J. Virol. , vol.72 , pp. 4980-4988
    • Muralidhar, S.1
  • 90
    • 0034061454 scopus 로고    scopus 로고
    • Characterization of the human herpesvirus 8 (Kaposi's sarcoma-associated herpesvirus) oncogene, kaposin (ORF K12)
    • Muralidhar, S. et al. Characterization of the human herpesvirus 8 (Kaposi's sarcoma-associated herpesvirus) oncogene, kaposin (ORF K12). J. Clin. Virol. 16, 203-213 (2000).
    • (2000) J. Clin. Virol. , vol.16 , pp. 203-213
    • Muralidhar, S.1
  • 91
    • 0029798249 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus contains G protein-coupled receptor and cyclin D homologs which are expressed in Kaposi's sarcoma and malignant lymphoma
    • Cesarman, E. et al. Kaposi's sarcoma-associated herpesvirus contains G protein-coupled receptor and cyclin D homologs which are expressed in Kaposi's sarcoma and malignant lymphoma. J. Virol. 70, 8218-8223 (1996).
    • (1996) J. Virol. , vol.70 , pp. 8218-8223
    • Cesarman, E.1
  • 92
    • 17044448294 scopus 로고    scopus 로고
    • Characterization of a chemokine receptor-related gene in human herpesvirus 8 and its expression in Kaposi's sarcoma
    • Guo, H. G. et al. Characterization of a chemokine receptor-related gene in human herpesvirus 8 and its expression in Kaposi's sarcoma. Virology 228, 371-378 (1997).
    • (1997) Virology , vol.228 , pp. 371-378
    • Guo, H.G.1
  • 93
    • 0036118279 scopus 로고    scopus 로고
    • Patterns of gene expression and a transactivation function exhibited by the vGCR (ORF74) chemokine receptor protein of Kaposi's sarcoma-associated herpesvirus
    • Chiou, C. J. et al. Patterns of gene expression and a transactivation function exhibited by the vGCR (ORF74) chemokine receptor protein of Kaposi's sarcoma-associated herpesvirus. J. Virol. 76, 3421-3439 (2002).
    • (2002) J. Virol. , vol.76 , pp. 3421-3439
    • Chiou, C.J.1
  • 94
    • 0031032769 scopus 로고    scopus 로고
    • Human herpesvirus KSHV encodes a constitutively active G-protein-coupled receptor linked to cell proliferation
    • Arvanitakis, L., Geras-Raaka, E., Varma, A., Gershengorn, M. C. & Cesarman, E. Human herpesvirus KSHV encodes a constitutively active G-protein-coupled receptor linked to cell proliferation. Nature 385, 347-350 (1997).
    • (1997) Nature , vol.385 , pp. 347-350
    • Arvanitakis, L.1    Geras-Raaka, E.2    Varma, A.3    Gershengorn, M.C.4    Cesarman, E.5
  • 95
    • 0032532063 scopus 로고    scopus 로고
    • Chemokines activate Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor in mammalian cells in culture
    • Gershengorn, M. C., Geras-Raaka, E., Varma, A. & Clark-Lewis, I. Chemokines activate Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor in mammalian cells in culture. J. Clin. Invest. 102, 1469-1472 (1998).
    • (1998) J. Clin. Invest. , vol.102 , pp. 1469-1472
    • Gershengorn, M.C.1    Geras-Raaka, E.2    Varma, A.3    Clark-Lewis, I.4
  • 96
    • 0032583452 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus (KSHV) chemokine vMIP-II and human SDF-1α inhibit signaling by KSHV G protein-coupled receptor
    • Geras-Raaka, E., Varma, A., Clark-Lewis, I. & Gershengorn, M. C. Kaposi's sarcoma-associated herpesvirus (KSHV) chemokine vMIP-II and human SDF-1α inhibit signaling by KSHV G protein-coupled receptor. Biochem. Biophys. Res. Commun. 253, 725-727 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 725-727
    • Geras-Raaka, E.1    Varma, A.2    Clark-Lewis, I.3    Gershengorn, M.C.4
  • 97
    • 0031823574 scopus 로고    scopus 로고
    • Human interferon-γ-inducible protein 10 (IP-10) inhibits constitutive signaling of Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor
    • Geras-Raaka, E., Varma, A., Ho, H., Clark-Lewis, I. & Gershengorn, M. C. Human interferon-γ-inducible protein 10 (IP-10) inhibits constitutive signaling of Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor. J. Exp. Med. 188, 405-408 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 405-408
    • Geras-Raaka, E.1    Varma, A.2    Ho, H.3    Clark-Lewis, I.4    Gershengorn, M.C.5
  • 98
    • 0034282553 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpes virus G protein-coupled receptor upregulates vascular endothelial growth factor expression and secretion through mitogen-activated protein kinase and p38 pathways acting on hypoxia-inducible factor 1α
    • Sodhi, A. et al. The Kaposi's sarcoma-associated herpes virus G protein-coupled receptor upregulates vascular endothelial growth factor expression and secretion through mitogen-activated protein kinase and p38 pathways acting on hypoxia-inducible factor 1α. Cancer Res. 60, 4873-4880 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 4873-4880
    • Sodhi, A.1
  • 99
    • 0035866812 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor promotes endothelial cell survival through the activation of Akt/protein kinase B
    • Montaner, S., Sodhi, A., Pece, S., Mesri, E. A. & Gutkind, J. S. The Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor promotes endothelial cell survival through the activation of Akt/protein kinase B. Cancer Res. 61, 2641-2648 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 2641-2648
    • Montaner, S.1    Sodhi, A.2    Pece, S.3    Mesri, E.A.4    Gutkind, J.S.5
  • 100
    • 0037213288 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor has broad signaling effects in primary effusion lymphoma cells
    • Cannon, M., Philpott, N. J. & Cesarman, E. The Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor has broad signaling effects in primary effusion lymphoma cells. J. Virol. 77, 57-67 (2003).
    • (2003) J. Virol. , vol.77 , pp. 57-67
    • Cannon, M.1    Philpott, N.J.2    Cesarman, E.3
  • 101
    • 0142213135 scopus 로고    scopus 로고
    • Kaposi's sarcoma associated herpesvirus G protein-coupled receptor immortalizes human endothelial cells by activation of the VEGF receptor-2/ KDR
    • Bais, C. et al. Kaposi's sarcoma associated herpesvirus G protein-coupled receptor immortalizes human endothelial cells by activation of the VEGF receptor-2/ KDR. Cancer Cell 3, 131-143 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 131-143
    • Bais, C.1
  • 102
    • 0031937076 scopus 로고    scopus 로고
    • G-protein-coupled receptor of Kaposi's sarcoma-associated herpesvirus is a viral oncogene and angiogenesis activator
    • Bais, C. et al. G-protein-coupled receptor of Kaposi's sarcoma-associated herpesvirus is a viral oncogene and angiogenesis activator. Nature 391, 86-89 (1998).
    • (1998) Nature , vol.391 , pp. 86-89
    • Bais, C.1
  • 103
    • 0034742155 scopus 로고    scopus 로고
    • Activation of NF-κB by the human herpesvirus 8 chemokine receptor ORF74: Evidence for a paracrine model of Kaposi's sarcoma pathogenesis
    • Pati, S. et al. Activation of NF-κB by the human herpesvirus 8 chemokine receptor ORF74: evidence for a paracrine model of Kaposi's sarcoma pathogenesis. J. Virol. 75, 8660-8673 (2001).
    • (2001) J. Virol. , vol.75 , pp. 8660-8673
    • Pati, S.1
  • 104
    • 0037772150 scopus 로고    scopus 로고
    • Endothelial infection with KSHV genes in vivo reveals that vGPCR initiates Kaposi's sarcomagenesis and can promote the tumorigenic potential of viral latent genes
    • Montaner, S. et al. Endothelial infection with KSHV genes in vivo reveals that vGPCR initiates Kaposi's sarcomagenesis and can promote the tumorigenic potential of viral latent genes. Cancer Cell 3, 23-36 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 23-36
    • Montaner, S.1
  • 105
    • 0034614888 scopus 로고    scopus 로고
    • Transgenic expression of the chemokine receptor encoded by human herpesvirus 8 induces an angioproliferative disease resembling Kaposi's sarcoma
    • Yang, T. Y. et al. Transgenic expression of the chemokine receptor encoded by human herpesvirus 8 induces an angioproliferative disease resembling Kaposi's sarcoma. J. Exp. Med. 191, 445-454 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 445-454
    • Yang, T.Y.1
  • 106
    • 0037320031 scopus 로고    scopus 로고
    • Kaposi's sarcoma-like tumors in a human herpesvirus 8 ORF74 transgenic mouse
    • Guo, H. G. et al. Kaposi's sarcoma-like tumors in a human herpesvirus 8 ORF74 transgenic mouse. J. Virol. 77, 2631-2639 (2003).
    • (2003) J. Virol. , vol.77 , pp. 2631-2639
    • Guo, H.G.1
  • 107
    • 0030014205 scopus 로고    scopus 로고
    • Expression of Epstein-Barr virus nuclear antigen-1 induces B cell neoplasia in transgenic mice
    • Wilson, J. B., Bell, J. L. & Levine, A. J. Expression of Epstein-Barr virus nuclear antigen-1 induces B cell neoplasia in transgenic mice. EMBO J. 15, 3117-3126 (1996).
    • (1996) EMBO J. , vol.15 , pp. 3117-3126
    • Wilson, J.B.1    Bell, J.L.2    Levine, A.J.3
  • 108
    • 0141479972 scopus 로고    scopus 로고
    • The EBV nuclear antigen 1 (EBNA1) enhances B-cell immortalization several thousandfold
    • Humme, S. et al. The EBV nuclear antigen 1 (EBNA1) enhances B-cell immortalization several thousandfold. Proc. Natl Acad. Sci. USA 100, 10989-10994 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10989-10994
    • Humme, S.1
  • 109
    • 10544223747 scopus 로고    scopus 로고
    • Enhanced malignant progression of nasopharyngeal carcinoma cells mediated by the expression of Epstein-Barr nuclear antigen 1 in vivo
    • Sheu, L. F. et al. Enhanced malignant progression of nasopharyngeal carcinoma cells mediated by the expression of Epstein-Barr nuclear antigen 1 in vivo. J. Pathol. 180, 243-248 (1996).
    • (1996) J. Pathol. , vol.180 , pp. 243-248
    • Sheu, L.F.1
  • 110
    • 0036667330 scopus 로고    scopus 로고
    • bcl-xL and RAG genes are induced and the response to IL-2 enhanced in EmuEBNA-1 transgenic mouse lymphocytes
    • Tsimbouri, P., Drotar, M. E., Coy, J. L. & Wilson, J. B. bcl-xL and RAG genes are induced and the response to IL-2 enhanced in EmuEBNA-1 transgenic mouse lymphocytes. Oncogene 21, 5182-5187 (2002).
    • (2002) Oncogene , vol.21 , pp. 5182-5187
    • Tsimbouri, P.1    Drotar, M.E.2    Coy, J.L.3    Wilson, J.B.4
  • 111
    • 0042887514 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 1 (EBNA1) induced cytotoxicity in epithelial cells is associated with EBNA1 degradation and processing
    • Jones, R. J. et al. Epstein-Barr virus nuclear antigen 1 (EBNA1) induced cytotoxicity in epithelial cells is associated with EBNA1 degradation and processing. Virology 313, 663-676 (2003).
    • (2003) Virology , vol.313 , pp. 663-676
    • Jones, R.J.1
  • 112
    • 0029003999 scopus 로고
    • Inhibition of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1
    • Levitskaya, J. et al. Inhibition of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1. Nature 375, 685-688 (1995).
    • (1995) Nature , vol.375 , pp. 685-688
    • Levitskaya, J.1
  • 113
    • 0030775380 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1
    • Levitskaya, J., Sharipo, A., Leonchiks, A., Ciechanover, A. & Masucci, M. G. Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc. Natl Acad. Sci. USA 94, 12616-12621 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12616-12621
    • Levitskaya, J.1    Sharipo, A.2    Leonchiks, A.3    Ciechanover, A.4    Masucci, M.G.5
  • 114
    • 0031714795 scopus 로고    scopus 로고
    • A cluster of latently expressed genes in Kaposi's sarcoma-associated herpesvirus
    • Dittmer, D. et al. A cluster of latently expressed genes in Kaposi's sarcoma-associated herpesvirus. J. Virol. 72, 8309-8315 (1998).
    • (1998) J. Virol. , vol.72 , pp. 8309-8315
    • Dittmer, D.1
  • 115
    • 0036100266 scopus 로고    scopus 로고
    • Charting latency transcripts in Kaposi's sarcoma-associated herpesvirus by whole-genome real-time quantitative reverse transcription-PCR
    • Fakhari, F. D. & Dittmer, D. P. Charting latency transcripts in Kaposi's sarcoma-associated herpesvirus by whole-genome real-time quantitative reverse transcription-PCR. J. Virol. 76 6213-6223 (2002).
    • (2002) J. Virol. , vol.76 , pp. 6213-6223
    • Fakhari, F.D.1    Dittmer, D.P.2
  • 116
    • 0038405070 scopus 로고    scopus 로고
    • Transcription profile of Kaposi's sarcoma-associated herpesvirus in primary Kaposi's sarcoma lesions as determined by real-time PCR arrays
    • Dittmer, D. P. Transcription profile of Kaposi's sarcoma-associated herpesvirus in primary Kaposi's sarcoma lesions as determined by real-time PCR arrays. Cancer Res. 63, 2010-2015 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 2010-2015
    • Dittmer, D.P.1
  • 117
    • 0033597453 scopus 로고    scopus 로고
    • Efficient persistence of extrachromosomal KSHV DNA mediated by latency-associated nuclear antigen
    • Ballestas, M. E., Chatis, P. A. & Kaye, K. M. Efficient persistence of extrachromosomal KSHV DNA mediated by latency-associated nuclear antigen. Science 284, 641-644 (1999).
    • (1999) Science , vol.284 , pp. 641-644
    • Ballestas, M.E.1    Chatis, P.A.2    Kaye, K.M.3
  • 118
    • 0035697261 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen binds to specific sequences at the left end of the viral genome through its carboxy-terminus
    • Cotter, M. A., Subramanian, C. & Robertson, E. S. The Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen binds to specific sequences at the left end of the viral genome through its carboxy-terminus. Virology 291, 241-259 (2001).
    • (2001) Virology , vol.291 , pp. 241-259
    • Cotter, M.A.1    Subramanian, C.2    Robertson, E.S.3
  • 119
    • 0037321704 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus permits replication of terminal repeat-containing plasmids
    • Grundhoff, A. & Ganem, D. The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus permits replication of terminal repeat-containing plasmids. J. Virol. 77, 2779-2783 (2003).
    • (2003) J. Virol. , vol.77 , pp. 2779-2783
    • Grundhoff, A.1    Ganem, D.2
  • 120
    • 0037178856 scopus 로고    scopus 로고
    • LANA cooperatively binds to two sites within the terminal repeat, both sites contribute to LANA's ability to suppress transcription and facilitate DNA replication
    • Garber, A. C., Hu, J. & Renne, R. LANA cooperatively binds to two sites within the terminal repeat, both sites contribute to LANA's ability to suppress transcription and facilitate DNA replication. J. Biol. Chem. 277, 27401-27411 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 27401-27411
    • Garber, A.C.1    Hu, J.2    Renne, R.3
  • 121
    • 0033599006 scopus 로고    scopus 로고
    • p53 inhibition by the LANA protein of KSHV protects against cell death
    • Friborg, J. Jr, Kong, W., Hottiger, M. O. & Nabel, G. J. p53 inhibition by the LANA protein of KSHV protects against cell death. Nature 402, 889-894 (1999).
    • (1999) Nature , vol.402 , pp. 889-894
    • Friborg Jr., J.1    Kong, W.2    Hottiger, M.O.3    Nabel, G.J.4
  • 122
    • 0033782793 scopus 로고    scopus 로고
    • The latent nuclear antigen of Kaposi sarcoma-associated herpesvirus targets the retinoblastoma-E2F pathway and with the oncogene Hras transforms primary rat cells
    • Radkov, S. A., Kellam, P. & Boshoff, C. The latent nuclear antigen of Kaposi sarcoma-associated herpesvirus targets the retinoblastoma-E2F pathway and with the oncogene Hras transforms primary rat cells. Nature Med. 6, 1121-1127 (2000).
    • (2000) Nature Med. , vol.6 , pp. 1121-1127
    • Radkov, S.A.1    Kellam, P.2    Boshoff, C.3
  • 123
    • 0037348372 scopus 로고    scopus 로고
    • A novel viral mechanism for dysregulation of β-catenin in Kaposi's sarcoma-associated herpesvirus latency
    • Fujimuro, M. et al. A novel viral mechanism for dysregulation of β-catenin in Kaposi's sarcoma-associated herpesvirus latency. Nature Med. 9, 300-306 (2003).
    • (2003) Nature Med. , vol.9 , pp. 300-306
    • Fujimuro, M.1
  • 124
    • 0033761708 scopus 로고    scopus 로고
    • Characterization of the herpesvirus saimiri ORF73 gene product
    • Hall, K. T. et al. Characterization of the herpesvirus saimiri ORF73 gene product. J. Gen. Virol. 81, 2653-2658 (2000).
    • (2000) J. Gen. Virol. , vol.81 , pp. 2653-2658
    • Hall, K.T.1
  • 125
    • 0038709489 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen homolog of herpesvirus saimiri inhibits lytic virus replication
    • Schafer, A. et al. The latency-associated nuclear antigen homolog of herpesvirus saimiri inhibits lytic virus replication. J. Virol. 77, 5911-5925 (2003).
    • (2003) J. Virol. , vol.77 , pp. 5911-5925
    • Schafer, A.1
  • 126
    • 1642462852 scopus 로고    scopus 로고
    • The herpesvirus saimiri ORF73 gene product interacts with host-cell mitotic chromosomes and self-associates via its C terminus
    • Calderwood, M. A., Hall, K. T., Matthews, D. A. & Whitehouse, A. The herpesvirus saimiri ORF73 gene product interacts with host-cell mitotic chromosomes and self-associates via its C terminus. J. Gen. Virol. 85, 147-153 (2004).
    • (2004) J. Gen. Virol. , vol.85 , pp. 147-153
    • Calderwood, M.A.1    Hall, K.T.2    Matthews, D.A.3    Whitehouse, A.4
  • 127
    • 0242409493 scopus 로고    scopus 로고
    • ORF73 of herpesvirus Saimiri strain C488 tethers the viral genome to metaphase chromosomes and binds to cis-acting DNA sequences in the terminal repeats
    • Verma, S. C. & Robertson, E. S. ORF73 of herpesvirus Saimiri strain C488 tethers the viral genome to metaphase chromosomes and binds to cis-acting DNA sequences in the terminal repeats. J. Virol. 77, 12494-12506 (2003).
    • (2003) J. Virol. , vol.77 , pp. 12494-12506
    • Verma, S.C.1    Robertson, E.S.2
  • 128
    • 0036827655 scopus 로고    scopus 로고
    • The herpesvirus saimiri open reading frame 73 gene product interacts with the cellular protein p32
    • Hall, K. T. et al. The herpesvirus saimiri open reading frame 73 gene product interacts with the cellular protein p32. J. Virol. 76, 11612-11622 (2002).
    • (2002) J. Virol. , vol.76 , pp. 11612-11622
    • Hall, K.T.1
  • 129
    • 2642586357 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-encoded latency-associated nuclear antigen inhibits lytic replication by targeting Rta: A potential mechanism for virus-mediated control of latency
    • Lan, K., Kuppers, D. A., Verma, S. C. & Robertson, E. S. Kaposi's sarcoma-associated herpesvirus-encoded latency-associated nuclear antigen inhibits lytic replication by targeting Rta: a potential mechanism for virus-mediated control of latency. J. Virol. 78, 6585-6594 (2004).
    • (2004) J. Virol. , vol.78 , pp. 6585-6594
    • Lan, K.1    Kuppers, D.A.2    Verma, S.C.3    Robertson, E.S.4
  • 130
    • 0027201577 scopus 로고
    • Viral interleukin 10 is critical for the induction of B cell growth transformation by Epstein-Barr virus
    • Miyazaki, I., Cheung, R. K. & Dosch, H. M. Viral interleukin 10 is critical for the induction of B cell growth transformation by Epstein-Barr virus. J. Exp. Med. 178, 439-447 (1993).
    • (1993) J. Exp. Med. , vol.178 , pp. 439-447
    • Miyazaki, I.1    Cheung, R.K.2    Dosch, H.M.3
  • 131
    • 0030881322 scopus 로고    scopus 로고
    • Downregulation of TAP1 in B lymphocytes by cellular and Epstein-Barr virus-encoded interleukin-10
    • Zeidler, R. et al. Downregulation of TAP1 in B lymphocytes by cellular and Epstein-Barr virus-encoded interleukin-10. Blood 90, 2390-2397 (1997).
    • (1997) Blood , vol.90 , pp. 2390-2397
    • Zeidler, R.1
  • 132
    • 0026000892 scopus 로고
    • Interleukin 10 (IL-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via downregulation of class II major histocompatibility complex expression
    • de Waal Malefyt, R. et al. Interleukin 10 (IL-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via downregulation of class II major histocompatibility complex expression. J. Exp. Med. 174, 915-924 (1991).
    • (1991) J. Exp. Med. , vol.174 , pp. 915-924
    • de Waal Malefyt, R.1
  • 133
    • 0036058131 scopus 로고    scopus 로고
    • High level expression and purification of the Epstein-Barr virus encoded cytokine viral interleukin 10: Efficient removal of endotoxin
    • Salek-Ardakani, S. et al. High level expression and purification of the Epstein-Barr virus encoded cytokine viral interleukin 10: efficient removal of endotoxin. Cytokine 17, 1-13 (2002).
    • (2002) Cytokine , vol.17 , pp. 1-13
    • Salek-Ardakani, S.1
  • 134
    • 0028824268 scopus 로고
    • The Epstein-Barr virus encoded cytokine viral interleukin-10 enhances transformation of human B lymphocytes
    • Stuart, A. D., Stewart, J. P., Arrand, J. R. & Mackett, M. The Epstein-Barr virus encoded cytokine viral interleukin-10 enhances transformation of human B lymphocytes. Oncogene 11, 1711-1719 (1995).
    • (1995) Oncogene , vol.11 , pp. 1711-1719
    • Stuart, A.D.1    Stewart, J.P.2    Arrand, J.R.3    Mackett, M.4
  • 135
    • 0032400864 scopus 로고    scopus 로고
    • Intereukin-10 abrogates the inhibition of Epstein-Barr virus-induced B-cell transformation by memory T-cell responses
    • Bejarano, M. T. & Masucci, M. G. Intereukin-10 abrogates the inhibition of Epstein-Barr virus-induced B-cell transformation by memory T-cell responses. Blood 92, 4256-4262 (1998).
    • (1998) Blood , vol.92 , pp. 4256-4262
    • Bejarano, M.T.1    Masucci, M.G.2
  • 136
    • 0029100824 scopus 로고
    • Viral interleukin 10 (IL-10), the human herpes virus 4 cellular IL-10 homologue, induces local energy to allogeneic and syngeneic tumors
    • Suzuki, T. et al. Viral interleukin 10 (IL-10), the human herpes virus 4 cellular IL-10 homologue, induces local energy to allogeneic and syngeneic tumors. J. Exp. Med. 182, 477-486 (1995).
    • (1995) J. Exp. Med. , vol.182 , pp. 477-486
    • Suzuki, T.1
  • 137
    • 0027358464 scopus 로고
    • Epstein-Barr virus recombinants with specifically mutated BCRF1 genes
    • Swaminathan, S., Hesselton, R., Sullivan, J. & Kieff, E. Epstein-Barr virus recombinants with specifically mutated BCRF1 genes. J. Virol. 67, 7406-7413 (1993).
    • (1993) J. Virol. , vol.67 , pp. 7406-7413
    • Swaminathan, S.1    Hesselton, R.2    Sullivan, J.3    Kieff, E.4
  • 138
    • 0029837991 scopus 로고    scopus 로고
    • Molecular mimicry of human cytokine and cytokine response pathway genes by KSHV
    • Moore, P. S., Boshoff, C., Weiss, R. A. & Chang, Y. Molecular mimicry of human cytokine and cytokine response pathway genes by KSHV. Science 274, 1739-1744 (1996).
    • (1996) Science , vol.274 , pp. 1739-1744
    • Moore, P.S.1    Boshoff, C.2    Weiss, R.A.3    Chang, Y.4
  • 139
    • 0031060368 scopus 로고    scopus 로고
    • Human herpesvirus 8 encodes a homolog of interleukin-6
    • Neipel, F. et al. Human herpesvirus 8 encodes a homolog of interleukin-6. J. Virol. 71, 839-842 (1997).
    • (1997) J. Virol. , vol.71 , pp. 839-842
    • Neipel, F.1
  • 140
    • 16944362511 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated human herpesvirus-8 encodes homologues of macrophage inflammatory protein-1 and interleukin-6
    • Nicholas, J. et al. Kaposi's sarcoma-associated human herpesvirus-8 encodes homologues of macrophage inflammatory protein-1 and interleukin-6. Nature Med. 3, 287-292 (1997).
    • (1997) Nature Med. , vol.3 , pp. 287-292
    • Nicholas, J.1
  • 141
    • 0034080072 scopus 로고    scopus 로고
    • Human herpesvirus 8-encoded interleukin-6 homologue (viral IL-6) induces endogenous human IL-6 secretion
    • Mori, Y. et al. Human herpesvirus 8-encoded interleukin-6 homologue (viral IL-6) induces endogenous human IL-6 secretion. J. Med. Virol. 61, 332-335 (2000).
    • (2000) J. Med. Virol. , vol.61 , pp. 332-335
    • Mori, Y.1
  • 142
    • 0032735983 scopus 로고    scopus 로고
    • Human interleukin-6 is in vivo an autocrine growth factor for human herpesvirus-8-infected malignant B lymphocytes
    • Foussat, A. et al. Human interleukin-6 is in vivo an autocrine growth factor for human herpesvirus-8-infected malignant B lymphocytes. Eur. Cytokine Netw. 10, 501-508 (1999).
    • (1999) Eur. Cytokine Netw. , vol.10 , pp. 501-508
    • Foussat, A.1
  • 143
    • 0037112208 scopus 로고    scopus 로고
    • Viral IL-6-induced cell proliferation and immune evasion of interferon activity
    • Chatterjee, M., Osborne, J., Bestetti, G., Chang, Y. & Moore, P. S. Viral IL-6-induced cell proliferation and immune evasion of interferon activity. Science 298, 1432-1435 (2002).
    • (2002) Science , vol.298 , pp. 1432-1435
    • Chatterjee, M.1    Osborne, J.2    Bestetti, G.3    Chang, Y.4    Moore, P.S.5
  • 144
    • 0030852894 scopus 로고    scopus 로고
    • A Kaposi's sarcoma-associated herpesvirus-encoded cytokine homolog (vIL-6) activates signaling through the shared gp130 receptor subunit
    • Molden, J., Chang, Y., You, Y., Moore, P. S. & Goldsmith, M. A. A Kaposi's sarcoma-associated herpesvirus-encoded cytokine homolog (vIL-6) activates signaling through the shared gp130 receptor subunit. J. Biol. Chem. 272, 19625-19631 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 19625-19631
    • Molden, J.1    Chang, Y.2    You, Y.3    Moore, P.S.4    Goldsmith, M.A.5
  • 145
    • 0030680299 scopus 로고    scopus 로고
    • Expression of a virus-derived cytokine, KSHV vIL-6, in HIV-seronegative Castleman's disease
    • Parravinci, C. et al. Expression of a virus-derived cytokine, KSHV vIL-6, in HIV-seronegative Castleman's disease. Am. J. Pathol. 151, 1517-1522 (1997).
    • (1997) Am. J. Pathol. , vol.151 , pp. 1517-1522
    • Parravinci, C.1
  • 146
    • 0032857038 scopus 로고    scopus 로고
    • Involvement of interleukin-10 (IL-10) and viral IL-6 in the spontaneous growth of Kaposi's sarcoma herpesvirus-associated infected primary effusion lymphoma cells
    • Jones, K. D. et al. Involvement of interleukin-10 (IL-10) and viral IL-6 in the spontaneous growth of Kaposi's sarcoma herpesvirus-associated infected primary effusion lymphoma cells. Blood 94, 2871-2879 (1999).
    • (1999) Blood , vol.94 , pp. 2871-2879
    • Jones, K.D.1
  • 147
    • 0033901248 scopus 로고    scopus 로고
    • Differential viral protein expression in Kaposi's sarcoma-associated herpesvirus-infected diseases: Kaposi's sarcoma, primary effusion lymphoma, and multicentric Castleman's disease
    • Parravicini, C. et al. Differential viral protein expression in Kaposi's sarcoma-associated herpesvirus-infected diseases: Kaposi's sarcoma, primary effusion lymphoma, and multicentric Castleman's disease. Am. J. Pathol. 156, 743-749 (2000).
    • (2000) Am. J. Pathol. , vol.156 , pp. 743-749
    • Parravicini, C.1
  • 148
    • 0030771974 scopus 로고    scopus 로고
    • Angiogenic and HIV-inhibitory functions of KSHV-encoded chemokines
    • Boshoff, C. et al. Angiogenic and HIV-inhibitory functions of KSHV-encoded chemokines. Science 278, 290-294 (1997).
    • (1997) Science , vol.278 , pp. 290-294
    • Boshoff, C.1
  • 149
    • 0032217050 scopus 로고    scopus 로고
    • H2 chemoattractant
    • H2 chemoattractant. Blood 92, 4036-4039 (1998).
    • (1998) Blood , vol.92 , pp. 4036-4039
    • Sozzani, S.1
  • 150
    • 18344398654 scopus 로고    scopus 로고
    • H2 cells
    • H2 cells. Blood 95, 1151-1157 (2000).
    • (2000) Blood , vol.95 , pp. 1151-1157
    • Stine, J.T.1
  • 151
    • 0038732559 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus (KSHV)-encoded vMIP-I and vMIP-II induce signal transduction and chemotaxis in monocytic cells
    • Nakano, K. et al. Kaposi's sarcoma-associated herpesvirus (KSHV)-encoded vMIP-I and vMIP-II induce signal transduction and chemotaxis in monocytic cells. Arch. Virol. 148, 871-890 (2003).
    • (2003) Arch. Virol. , vol.148 , pp. 871-890
    • Nakano, K.1
  • 152
    • 0034857404 scopus 로고    scopus 로고
    • H2-type cells and evasion from a cytotoxic immune response mediated by viral macrophage inhibitory protein-II
    • H2-type cells and evasion from a cytotoxic immune response mediated by viral macrophage inhibitory protein-II. Eur. J. Immunol. 31, 2458-2466 (2001).
    • (2001) Eur. J. Immunol. , vol.31 , pp. 2458-2466
    • Weber, K.S.1
  • 153
    • 0029555301 scopus 로고
    • Herpesvirus Saimiri encodes a new cytokine, IL-17, which binds to a novel cytokine receptor
    • Yao, Z. et al. Herpesvirus Saimiri encodes a new cytokine, IL-17, which binds to a novel cytokine receptor. Immunity 3, 811-821 (1995).
    • (1995) Immunity , vol.3 , pp. 811-821
    • Yao, Z.1
  • 154
    • 0028858556 scopus 로고
    • Human IL-17: A novel cytokine derived from T cells
    • Yao, Z. et al. Human IL-17: a novel cytokine derived from T cells. J. Immunol. 155, 5483-5486 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 5483-5486
    • Yao, Z.1
  • 155
    • 0028819981 scopus 로고
    • The normal cell cycle activation program is exploited during the infection of quiescent B lymphocytes by Epstein-Barr virus
    • Hollyoake, M., Stuhler, A., Farrell, P., Gordon, J. & Sinclair, A. The normal cell cycle activation program is exploited during the infection of quiescent B lymphocytes by Epstein-Barr virus. Cancer Res. 55, 4784-4787 (1995).
    • (1995) Cancer Res. , vol.55 , pp. 4784-4787
    • Hollyoake, M.1    Stuhler, A.2    Farrell, P.3    Gordon, J.4    Sinclair, A.5
  • 156
    • 0026541641 scopus 로고
    • Herpesvirus saimiri encodes homologues of G protein-coupled receptors and cyclins
    • Nicholas, J., Cameron, K. R. & Honess, R. W. Herpesvirus saimiri encodes homologues of G protein-coupled receptors and cyclins. Nature 355, 362-365 (1992).
    • (1992) Nature , vol.355 , pp. 362-365
    • Nicholas, J.1    Cameron, K.R.2    Honess, R.W.3
  • 157
    • 0033774291 scopus 로고    scopus 로고
    • The apoptotic v-cyclin-CDK6 complex phosphorylates and inactivates Bcl-2
    • Ojala, P. M. et al. The apoptotic v-cyclin-CDK6 complex phosphorylates and inactivates Bcl-2. Nature Cell Biol. 2, 819-825 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 819-825
    • Ojala, P.M.1
  • 158
    • 0036730664 scopus 로고    scopus 로고
    • The oncogenic potential of Kaposi's sarcoma-associated herpesvirus cyclin is exposed by p53 loss in vitro and in vivo
    • Verschuren, E. W., Klefstrom, J., Evan, G. I. & Jones, N. The oncogenic potential of Kaposi's sarcoma-associated herpesvirus cyclin is exposed by p53 loss in vitro and in vivo. Cancer Cell 2, 229-241 (2002).
    • (2002) Cancer Cell , vol.2 , pp. 229-241
    • Verschuren, E.W.1    Klefstrom, J.2    Evan, G.I.3    Jones, N.4
  • 160
    • 0035809313 scopus 로고    scopus 로고
    • Independence of herpesvirus-induced T cell lymphoma from viral cyclin D homologue
    • Ensser, A. et al. Independence of herpesvirus-induced T cell lymphoma from viral cyclin D homologue. J. Exp. Med. 193, 637-642 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 637-642
    • Ensser, A.1


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