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Volumn 84, Issue 19, 2010, Pages 9718-9732

Bub1 and CENP-F can contribute to Kaposi's sarcoma-associated herpesvirus genome persistence by targeting LANA to kinetochores

Author keywords

[No Author keywords available]

Indexed keywords

BUB1 RELATED PROTEIN; CENTROMERE PROTEIN F; LATENCY ASSOCIATED NUCLEAR ANTIGEN; NUCLEAR PROTEIN; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; BUB1 PROTEIN, HUMAN; BUB1 SPINDLE CHECKPOINT PROTEIN; LATENCY-ASSOCIATED NUCLEAR ANTIGEN; NONHISTONE PROTEIN; PROTEIN SERINE THREONINE KINASE; SMALL INTERFERING RNA; VIRUS ANTIGEN;

EID: 77956841815     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00713-10     Document Type: Article
Times cited : (57)

References (78)
  • 2
    • 13544258096 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus modulates cellular gene expression and protects lymphoid cells from p16 INK4A-induced cell cycle arrest
    • An, F. Q., N. Compitello, E. Horwitz, M. Sramkoski, E. S. Knudsen, and R. Renne. 2005. The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus modulates cellular gene expression and protects lymphoid cells from p16 INK4A-induced cell cycle arrest. J. Biol. Chem. 280: 3862-3874.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3862-3874
    • An, F.Q.1    Compitello, N.2    Horwitz, E.3    Sramkoski, M.4    Knudsen, E.S.5    Renne, R.6
  • 3
    • 0033597453 scopus 로고    scopus 로고
    • Efficient persistence of extrachromosomal KSHV DNA mediated by latency-associated nuclear antigen
    • Ballestas, M. E., P. A. Chatis, and K. M. Kaye. 1999. Efficient persistence of extrachromosomal KSHV DNA mediated by latency-associated nuclear antigen. Science 284:641-644.
    • (1999) Science , vol.284 , pp. 641-644
    • Ballestas, M.E.1    Chatis, P.A.2    Kaye, K.M.3
  • 5
    • 0037348197 scopus 로고    scopus 로고
    • Kaposi virus scores cancer coup
    • Boshoff, C. 2003. Kaposi virus scores cancer coup. Nat. Med. 9:261-262.
    • (2003) Nat. Med. , vol.9 , pp. 261-262
    • Boshoff, C.1
  • 7
    • 0027733779 scopus 로고
    • Autoantibodies to a novel cell cycle-regulated protein that accumulates in the nuclear matrix during S phase and is localized in the kinetochores and spindle midzone during mitosis
    • Casiano, C. A., G. Landberg, R. L. Ochs, and E. M. Tan. 1993. Autoantibodies to a novel cell cycle-regulated protein that accumulates in the nuclear matrix during S phase and is localized in the kinetochores and spindle midzone during mitosis. J. Cell Sci. 106:1045-1056.
    • (1993) J. Cell Sci. , vol.106 , pp. 1045-1056
    • Casiano, C.A.1    Landberg, G.2    Ochs, R.L.3    Tan, E.M.4
  • 8
    • 0029069445 scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas
    • Cesarman, E., Y. Chang, P. S. Moore, J. W. Said, and D. M. Knowles. 1995. Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas. N. Engl. J. Med. 332:1186-1191.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 1186-1191
    • Cesarman, E.1    Chang, Y.2    Moore, P.S.3    Said, J.W.4    Knowles, D.M.5
  • 9
    • 0032487444 scopus 로고    scopus 로고
    • Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1
    • Chan, G. K., B. T. Schaar, and T. J. Yen. 1998. Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1. J. Cell Biol. 143:49-63.
    • (1998) J. Cell Biol. , vol.143 , pp. 49-63
    • Chan, G.K.1    Schaar, B.T.2    Yen, T.J.3
  • 10
    • 0028588064 scopus 로고
    • Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma
    • Chang, Y., E. Cesarman, M. S. Pessin, F. Lee, J. Culpepper, D. M. Knowles, and P. S. Moore. 1994. Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma. Science 266:1865-1869.
    • (1994) Science , vol.266 , pp. 1865-1869
    • Chang, Y.1    Cesarman, E.2    Pessin, M.S.3    Lee, F.4    Culpepper, J.5    Knowles, D.M.6    Moore, P.S.7
  • 11
    • 0033604613 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen tethers the Kaposi's sarcoma-associated herpesvirus genome to host chromosomes in body cavity-based lymphoma cells
    • Cotter, M. A., II, and E. S. Robertson. 1999. The latency-associated nuclear antigen tethers the Kaposi's sarcoma-associated herpesvirus genome to host chromosomes in body cavity-based lymphoma cells. Virology 264:254-264.
    • (1999) Virology , vol.264 , pp. 254-264
    • Cotter II, M.A.1    Robertson, E.S.2
  • 12
    • 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 carboxyterminus
    • Cotter, M. A., II, C. Subramanian, and E. S. Robertson. 2001. The Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen binds to specific sequences at the left end of the viral genome through its carboxyterminus. Virology 291:241-259.
    • (2001) Virology , vol.291 , pp. 241-259
    • Cotter, M.A.1    Subramanian, I.I.C.2    Robertson, E.S.3
  • 13
    • 0030037520 scopus 로고    scopus 로고
    • The Kaposi sarcoma-associated herpesvirus (KSHV) is present as an intact latent genome in KS tissue but replicates in the peripheral blood mononuclear cells of KS patients
    • Decker, L. L., P. Shankar, G. Khan, R. B. Freeman, B. J. Dezube, J. Lieberman, and D. A. Thorley-Lawson. 1996. The Kaposi sarcoma-associated herpesvirus (KSHV) is present as an intact latent genome in KS tissue but replicates in the peripheral blood mononuclear cells of KS patients. J. Exp. Med. 184:283-288.
    • (1996) J. Exp. Med. , vol.184 , pp. 283-288
    • Decker, L.L.1    Shankar, P.2    Khan, G.3    Freeman, R.B.4    Dezube, B.J.5    Lieberman, J.6    Thorley-Lawson, D.A.7
  • 14
    • 44649172694 scopus 로고    scopus 로고
    • KSHV LANA inhibits TGF-beta signaling through epigenetic silencing of the TGF-beta type II receptor
    • Di Bartolo, D. L., M. Cannon, Y. F. Liu, R. Renne, A. Chadburn, C. Boshoff, and E. Cesarman. 2008. KSHV LANA inhibits TGF-beta signaling through epigenetic silencing of the TGF-beta type II receptor. Blood 111:4731-4740.
    • (2008) Blood , vol.111 , pp. 4731-4740
    • Di Bartolo, D.L.1    Cannon, M.2    Liu, Y.F.3    Renne, R.4    Chadburn, A.5    Boshoff, C.6    Cesarman, E.7
  • 16
    • 0034651687 scopus 로고    scopus 로고
    • HHV-8 is associated with a plasmablastic variant of Castleman disease that is linked to HHV-8-positive plasmablastic lymphoma
    • Dupin, N., T. L. Diss, P. Kellam, M. Tulliez, M. Q. Du, D. Sicard, R. A. Weiss, P. G. Isaacson, and C. Boshoff. 2000. HHV-8 is associated with a plasmablastic variant of Castleman disease that is linked to HHV-8-positive plasmablastic lymphoma. Blood 95:1406-1412.
    • (2000) Blood , vol.95 , pp. 1406-1412
    • Dupin, N.1    Diss, T.L.2    Kellam, P.3    Tulliez, M.4    Du, M.Q.5    Sicard, D.6    Weiss, R.A.7    Isaacson, P.G.8    Boshoff, C.9
  • 18
    • 66349129914 scopus 로고    scopus 로고
    • Targeting mitotic chromosomes: A conserved mechanism to ensure viral genome persistence
    • Feeney, K. M., and J. L. Parish. 2009. Targeting mitotic chromosomes: a conserved mechanism to ensure viral genome persistence. Proc. Biol. Sci. 276:1535-1544.
    • (2009) Proc. Biol. Sci. , vol.276 , pp. 1535-1544
    • Feeney, K.M.1    Parish, J.L.2
  • 19
    • 0033599006 scopus 로고    scopus 로고
    • p53 inhibition by the LANA protein of KSHV protects against cell death
    • Friborg, J., Jr., W. Kong, M. O. Hottiger, and G. J. Nabel. 1999. p53 inhibition by the LANA protein of KSHV protects against cell death. Nature 402:889-894.
    • (1999) Nature , vol.402 , pp. 889-894
    • Friborg Jr., J.1    Kong, W.2    Hottiger, M.O.3    Nabel, G.J.4
  • 20
    • 0037348372 scopus 로고    scopus 로고
    • A novel viral mechanism for dysregulation of beta-catenin in Kaposi's sarcoma-associated herpesvirus latency
    • Fujimuro, M., F. Y. Wu, C. ApRhys, H. Kajumbula, D. B. Young, G. S. Hayward, and S. D. Hayward. 2003. A novel viral mechanism for dysregulation of beta-catenin in Kaposi's sarcoma-associated herpesvirus latency. Nat. Med. 9:300-306.
    • (2003) Nat. Med. , vol.9 , pp. 300-306
    • Fujimuro, M.1    Wu, F.Y.2    ApRhys, C.3    Kajumbula, H.4    Young, D.B.5    Hayward, G.S.6    Hayward, S.D.7
  • 21
    • 0037178856 scopus 로고    scopus 로고
    • Latency-associated nuclear antigen (LANA) cooperatively binds to two sites within the terminal repeat, and both sites contribute to the ability of LANA to suppress transcription and to facilitate DNA replication
    • Garber, A. C., J. Hu, and R. Renne. 2002. Latency-associated nuclear antigen (LANA) cooperatively binds to two sites within the terminal repeat, and both sites contribute to the ability of LANA to suppress transcription and to facilitate DNA replication. J. Biol. Chem. 277:27401-27411.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27401-27411
    • Garber, A.C.1    Hu, J.2    Renne, R.3
  • 22
    • 0034870212 scopus 로고    scopus 로고
    • DNA binding and modulation of gene expression by the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus
    • DOI 10.1128/JVI.75.17.7882-7892.2001
    • Garber, A. C., M. A. Shu, J. Hu, and R. Renne. 2001. DNA binding and modulation of gene expression by the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus. J. Virol. 75:7882-7892. (Pubitemid 32743660)
    • (2001) Journal of Virology , vol.75 , Issue.17 , pp. 7882-7892
    • Garber, A.C.1    Shu, M.A.2    Hu, J.3    Renne, R.4
  • 23
    • 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., and D. Ganem. 2003. The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus permits replication of terminal repeat-containing plasmids. J. Virol. 77:2779-2783.
    • (2003) J. Virol. , vol.77 , pp. 2779-2783
    • Grundhoff, A.1    Ganem, D.2
  • 24
    • 0036827642 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus supports latent DNA replication in dividing cells
    • Hu, J., A. C. Garber, and R. Renne. 2002. The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus supports latent DNA replication in dividing cells. J. Virol. 76:11677-11687.
    • (2002) J. Virol. , vol.76 , pp. 11677-11687
    • Hu, J.1    Garber, A.C.2    Renne, R.3
  • 25
    • 0032415592 scopus 로고    scopus 로고
    • The hBUB1 and hBUBR1 kinases sequentially assemble onto kinetochores during prophase with hBUBR1 concentrating at the kinetochore plates in mitosis
    • Jablonski, S. A., G. K. Chan, C. A. Cooke, W. C. Earnshaw, and T. J. Yen. 1998. The hBUB1 and hBUBR1 kinases sequentially assemble onto kinetochores during prophase with hBUBR1 concentrating at the kinetochore plates in mitosis. Chromosoma 107:386-396.
    • (1998) Chromosoma , vol.107 , pp. 386-396
    • Jablonski, S.A.1    Chan, G.K.2    Cooke, C.A.3    Earnshaw, W.C.4    Yen, T.J.5
  • 26
    • 35548957419 scopus 로고    scopus 로고
    • Bub1 mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis
    • DOI 10.1083/jcb.200706015
    • Jeganathan, K., L. Malureanu, D. J. Baker, S. C. Abraham, and J. M. van Deursen. 2007. Bub1 mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. J. Cell Biol. 179:255-267. (Pubitemid 350004890)
    • (2007) Journal of Cell Biology , vol.179 , Issue.2 , pp. 255-267
    • Jeganathan, K.1    Malureanu, L.2    Baker, D.J.3    Abraham, S.C.4    Van Deursen, J.M.5
  • 27
    • 2342439525 scopus 로고    scopus 로고
    • Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression
    • Johnson, V. L., M. I. Scott, S. V. Holt, D. Hussein, and S. S. Taylor. 2004. Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression. J. Cell Sci. 117:1577-1589.
    • (2004) J. Cell Sci. , vol.117 , pp. 1577-1589
    • Johnson, V.L.1    Scott, M.I.2    Holt, S.V.3    Hussein, D.4    Taylor, S.S.5
  • 28
    • 34249950934 scopus 로고    scopus 로고
    • Protein complexes associated with the Kaposi's sarcoma-associated herpesvirus-encoded LANA
    • Kaul, R., S. C. Verma, and E. S. Robertson. 2007. Protein complexes associated with the Kaposi's sarcoma-associated herpesvirus-encoded LANA. Virology 364:317-329.
    • (2007) Virology , vol.364 , pp. 317-329
    • Kaul, R.1    Verma, S.C.2    Robertson, E.S.3
  • 29
    • 0030734037 scopus 로고    scopus 로고
    • Identification of the gene encoding the major latency-associated nuclear antigen of the Kaposi's sarcoma-associated herpesvirus
    • Kedes, D. H., M. Lagunoff, R. Renne, and D. Ganem. 1997. Identification of the gene encoding the major latency-associated nuclear antigen of the Kaposi's sarcoma-associated herpesvirus. J. Clin. Invest. 100:2606-2610.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2606-2610
    • Kedes, D.H.1    Lagunoff, M.2    Renne, R.3    Ganem, D.4
  • 30
    • 0031261173 scopus 로고    scopus 로고
    • Identification of a major latent nuclear antigen, LNA-1, in the human herpesvirus 8 genome
    • Kellam, P., C. Boshoff, D. Whitby, S. Matthews, R. A. Weiss, and S. J. Talbot. 1997. Identification of a major latent nuclear antigen, LNA-1, in the human herpesvirus 8 genome. J. Hum. Virol. 1:19-29.
    • (1997) J. Hum. Virol. , vol.1 , pp. 19-29
    • Kellam, P.1    Boshoff, C.2    Whitby, D.3    Matthews, S.4    Weiss, R.A.5    Talbot, S.J.6
  • 31
    • 13944261954 scopus 로고    scopus 로고
    • Human Bub1 defines the persistent cohesion site along the mitotic chromosome by affecting Shugoshin localization
    • Kitajima, T. S., S. Hauf, M. Ohsugi, T. Yamamoto, and Y. Watanabe. 2005. Human Bub1 defines the persistent cohesion site along the mitotic chromosome by affecting Shugoshin localization. Curr. Biol. 15:353-359.
    • (2005) Curr. Biol. , vol.15 , pp. 353-359
    • Kitajima, T.S.1    Hauf, S.2    Ohsugi, M.3    Yamamoto, T.4    Watanabe, Y.5
  • 32
    • 12344289259 scopus 로고    scopus 로고
    • Kinetochore-spindle microtubule interactions during mitosis
    • Kline-Smith, S. L., S. Sandall, and A. Desai. 2005. Kinetochore-spindle microtubule interactions during mitosis. Curr. Opin. Cell Biol. 17:35-46.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 35-46
    • Kline-Smith, S.L.1    Sandall, S.2    Desai, A.3
  • 33
    • 0035933745 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus transactivates the telomerase reverse transcriptase promoter
    • Knight, J. S., M. A. Cotter II, and E. S. Robertson. 2001. The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus transactivates the telomerase reverse transcriptase promoter. J. Biol. Chem. 276: 22971-22978.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22971-22978
    • Knight, J.S.1    Cotter II, M.A.2    Robertson, E.S.3
  • 34
    • 1342321886 scopus 로고    scopus 로고
    • KSHV LANA1 binds DNA as an oligomer and residues N-terminal to the oligomerization domain are essential for DNA binding, replication, and episome persistence
    • Komatsu, T., M. E. Ballestas, A. J. Barbera, B. Kelley-Clarke, and K. M. Kaye. 2004. KSHV LANA1 binds DNA as an oligomer and residues N-terminal to the oligomerization domain are essential for DNA binding, replication, and episome persistence. Virology 319:225-236.
    • (2004) Virology , vol.319 , pp. 225-236
    • Komatsu, T.1    Ballestas, M.E.2    Barbera, A.J.3    Kelley-Clarke, B.4    Kaye, K.M.5
  • 35
    • 25844475838 scopus 로고    scopus 로고
    • On the road to cancer: Aneuploidy and the mitotic checkpoint
    • Kops, G. J., B. A. Weaver, and D. W. Cleveland. 2005. On the road to cancer: aneuploidy and the mitotic checkpoint. Nat. Rev. Cancer 5:773-785.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 773-785
    • Kops, G.J.1    Weaver, B.A.2    Cleveland, D.W.3
  • 36
    • 0036828167 scopus 로고    scopus 로고
    • Protein interactions targeting the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus to cell chromosomes
    • Krithivas, A., M. Fujimuro, M. Weidner, D. B. Young, and S. D. Hayward. 2002. Protein interactions targeting the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus to cell chromosomes. J. Virol. 76: 11596-11604.
    • (2002) J. Virol. , vol.76 , pp. 11596-11604
    • Krithivas, A.1    Fujimuro, M.2    Weidner, M.3    Young, D.B.4    Hayward, S.D.5
  • 37
    • 0033809462 scopus 로고    scopus 로고
    • Human herpesvirus 8 LANA interacts with proteins of the mSin3 corepressor complex and negatively regulates Epstein-Barr virus gene expression in dually infected PEL cells
    • Krithivas, A., D. B. Young, G. Liao, D. Greene, and S. D. Hayward. 2000. Human herpesvirus 8 LANA interacts with proteins of the mSin3 corepres- sor complex and negatively regulates Epstein-Barr virus gene expression in dually infected PEL cells. J. Virol. 74:9637-9645.
    • (2000) J. Virol. , vol.74 , pp. 9637-9645
    • Krithivas, A.1    Young, D.B.2    Liao, G.3    Greene, D.4    Hayward, S.D.5
  • 38
    • 0031572167 scopus 로고    scopus 로고
    • The structure and coding organization of the genomic termini of Kaposi's sarcoma-associated herpesvirus
    • Lagunoff, M., and D. Ganem. 1997. The structure and coding organization of the genomic termini of Kaposi's sarcoma-associated herpesvirus. Virology 236:147-154.
    • (1997) Virology , vol.236 , pp. 147-154
    • Lagunoff, M.1    Ganem, D.2
  • 39
    • 0032516030 scopus 로고    scopus 로고
    • Segregation of viral plasmids depends on tethering to chromosomes and is regulated by phosphorylation
    • Lehman, C. W., and M. R. Botchan. 1998. Segregation of viral plasmids depends on tethering to chromosomes and is regulated by phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 95:4338-4343.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4338-4343
    • Lehman, C.W.1    Botchan, M.R.2
  • 40
    • 0034103269 scopus 로고    scopus 로고
    • EBNA-1: A protein pivotal to latent infection by Epstein-Barr virus
    • Leight, E. R., and B. Sugden. 2000. EBNA-1: a protein pivotal to latent infection by Epstein-Barr virus. Rev. Med. Virol. 10:83-100.
    • (2000) Rev. Med. Virol. , vol.10 , pp. 83-100
    • Leight, E.R.1    Sugden, B.2
  • 41
    • 0029096822 scopus 로고
    • CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis
    • Liao, H., R. J. Winkfein, G. Mack, J. B. Rattner, and T. J. Yen. 1995. CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 130:507-518.
    • (1995) J. Cell Biol. , vol.130 , pp. 507-518
    • Liao, H.1    Winkfein, R.J.2    Mack, G.3    Rattner, J.B.4    Yen, T.J.5
  • 42
    • 0033767391 scopus 로고    scopus 로고
    • Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus (human herpesvirus-8) binds ATF4/CREB2 and inhibits its transcriptional activation activity
    • Lim, C., H. Sohn, Y. Gwack, and J. Choe. 2000. Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus (human herpesvirus-8) binds ATF4/CREB2 and inhibits its transcriptional activation activity. J. Gen. Virol. 81:2645-2652.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2645-2652
    • Lim, C.1    Sohn, H.2    Gwack, Y.3    Choe, J.4
  • 43
    • 33646723291 scopus 로고    scopus 로고
    • Acetylation of the latency-associated nuclear antigen regulates repression of Kaposi's sarcoma-associated herpesvirus lytic transcription
    • Lu, F., L. Day, S. J. Gao, and P. M. Lieberman. 2006. Acetylation of the latency-associated nuclear antigen regulates repression of Kaposi's sarcoma-associated herpesvirus lytic transcription. J. Virol. 80:5273-5282.
    • (2006) J. Virol. , vol.80 , pp. 5273-5282
    • Lu, F.1    Day, L.2    Gao, S.J.3    Lieberman, P.M.4
  • 44
    • 0036161468 scopus 로고    scopus 로고
    • The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20
    • Luo, X., Z. Tang, J. Rizo, and H. Yu. 2002. The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20. Mol. Cell 9:59-71.
    • (2002) Mol. Cell , vol.9 , pp. 59-71
    • Luo, X.1    Tang, Z.2    Rizo, J.3    Yu, H.4
  • 46
  • 47
    • 18444378391 scopus 로고    scopus 로고
    • A dual role for Bub1 in the spindle checkpoint and chromosome congression
    • Meraldi, P., and P. K. Sorger. 2005. A dual role for Bub1 in the spindle checkpoint and chromosome congression. EMBO J. 24:1621-1633.
    • (2005) EMBO J. , vol.24 , pp. 1621-1633
    • Meraldi, P.1    Sorger, P.K.2
  • 48
    • 0029005449 scopus 로고
    • Detection of herpesvirus-like DNA sequences in Kaposi's sarcoma in patients with and without HIV infection
    • Moore, P. S., and Y. Chang. 1995. Detection of herpesvirus-like DNA sequences in Kaposi's sarcoma in patients with and without HIV infection. N. Engl. J. Med. 332:1181-1185.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 1181-1185
    • Moore, P.S.1    Chang, Y.2
  • 49
    • 34247333444 scopus 로고    scopus 로고
    • The spindle-assembly checkpoint in space and time
    • Musacchio, A., and E. D. Salmon. 2007. The spindle-assembly checkpoint in space and time. Nat. Rev. Mol. Cell Biol. 8:379-393.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 379-393
    • Musacchio, A.1    Salmon, E.D.2
  • 50
    • 0029974841 scopus 로고    scopus 로고
    • Primary effusion lymphoma: A distinct clinicopathologic entity associated with the Kaposi's sarcoma-associated herpes virus
    • Nador, R. G., E. Cesarman, A. Chadburn, D. B. Dawson, M. Q. Ansari, J. Sald, and D. M. Knowles. 1996. Primary effusion lymphoma: a distinct clinicopathologic entity associated with the Kaposi's sarcoma-associated herpes virus. Blood 88:645-656.
    • (1996) Blood , vol.88 , pp. 645-656
    • Nador, R.G.1    Cesarman, E.2    Chadburn, A.3    Dawson, D.B.4    Ansari, M.Q.5    Sald, J.6    Knowles, D.M.7
  • 53
    • 0035078957 scopus 로고    scopus 로고
    • Close but distinct regions of human herpesvirus 8 latency-associated nuclear antigen 1 are responsible for nuclear targeting and binding to human mitotic chromosomes
    • Piolot, T., M. Tramier, M. Coppey, J. C. Nicolas, and V. Marechal. 2001. Close but distinct regions of human herpesvirus 8 latency-associated nuclear antigen 1 are responsible for nuclear targeting and binding to human mitotic chromosomes. J. Virol. 75:3948-3959.
    • (2001) J. Virol. , vol.75 , pp. 3948-3959
    • Piolot, T.1    Tramier, M.2    Coppey, M.3    Nicolas, J.C.4    Marechal, V.5
  • 54
    • 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., P. Kellam, and C. Boshoff. 2000. The latent nuclear antigen of Kaposi sarcoma-associated herpesvirus targets the retinoblastoma-E2F pathway and with the oncogene Hras transforms primary rat cells. Nat. Med. 6:1121-1127.
    • (2000) Nat. Med. , vol.6 , pp. 1121-1127
    • Radkov, S.A.1    Kellam, P.2    Boshoff, C.3
  • 55
    • 0030834122 scopus 로고    scopus 로고
    • The 222- to 234-kilodalton latent nuclear protein (LNA) of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) is encoded by orf73 and is a component of the latency-associated nuclear antigen
    • Rainbow, L., G. M. Platt, G. R. Simpson, R. Sarid, S. J. Gao, H. Stoiber, C. S. Herrington, P. S. Moore, and T. F. Schulz. 1997. The 222- to 234-kilodalton latent nuclear protein (LNA) of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) is encoded by orf73 and is a component of the latency-associated nuclear antigen. J. Virol. 71:5915-5921.
    • (1997) J. Virol. , vol.71 , pp. 5915-5921
    • Rainbow, L.1    Platt, G.M.2    Simpson, G.R.3    Sarid, R.4    Gao, S.J.5    Stoiber, H.6    Herrington, C.S.7    Moore, P.S.8    Schulz, T.F.9
  • 56
    • 0027436345 scopus 로고
    • CENP-F is a ca. 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization
    • Rattner, J. B., A. Rao, M. J. Fritzler, D. W. Valencia, and T. J. Yen. 1993. CENP-F is a ca. 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization. Cell Motil. Cytoskeleton 26:214-226.
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 214-226
    • Rattner, J.B.1    Rao, A.2    Fritzler, M.J.3    Valencia, D.W.4    Yen, T.J.5
  • 57
    • 0032146974 scopus 로고    scopus 로고
    • The vertebrate cell kinetochore and its roles during mitosis
    • Rieder, C. L., and E. D. Salmon. 1998. The vertebrate cell kinetochore and its roles during mitosis. Trends Cell Biol. 8:310-318.
    • (1998) Trends Cell Biol. , vol.8 , pp. 310-318
    • Rieder, C.L.1    Salmon, E.D.2
  • 58
    • 0028089758 scopus 로고
    • The Saccharomyces cerevisiae checkpoint gene BUB1 encodes a novel protein kinase
    • Roberts, B. T., K. A. Farr, and M. A. Hoyt. 1994. The Saccharomyces cerevisiae checkpoint gene BUB1 encodes a novel protein kinase. Mol. Cell. Biol. 14:8282-8291.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8282-8291
    • Roberts, B.T.1    Farr, K.A.2    Hoyt, M.A.3
  • 60
    • 0029015381 scopus 로고
    • A role for a new herpes virus (KSHV) in different forms of Kaposi's sarcoma
    • Schalling, M., M. Ekman, E. E. Kaaya, A. Linde, and P. Biberfeld. 1995. A role for a new herpes virus (KSHV) in different forms of Kaposi's sarcoma. Nat. Med. 1:707-708.
    • (1995) Nat. Med. , vol.1 , pp. 707-708
    • Schalling, M.1    Ekman, M.2    Kaaya, E.E.3    Linde, A.4    Biberfeld, P.5
  • 61
    • 58249094849 scopus 로고    scopus 로고
    • Impaired Bub1 function in vivo compromises tension-dependent checkpoint function leading to aneuploidy and tumorigenesis
    • Schliekelman, M., D. O. Cowley, R. O'Quinn, T. G. Oliver, L. Lu, E. D. Salmon, and T. Van Dyke. 2009. Impaired Bub1 function in vivo compromises tension-dependent checkpoint function leading to aneuploidy and tumorigenesis. Cancer Res. 69:45-54.
    • (2009) Cancer Res. , vol.69 , pp. 45-54
    • Schliekelman, M.1    Cowley, D.O.2    O'Quinn, R.3    Oliver, T.G.4    Lu, L.5    Salmon, E.D.6    Van Dyke, T.7
  • 62
    • 0033857732 scopus 로고    scopus 로고
    • Carboxy terminus of human herpesvirus 8 latency-associated nuclear antigen mediates dimerization, transcriptional repression, and targeting to nuclear bodies
    • Schwam, D. R., R. L. Luciano, S. S. Mahajan, L. Wong, and A. C. Wilson. 2000. Carboxy terminus of human herpesvirus 8 latency-associated nuclear antigen mediates dimerization, transcriptional repression, and targeting to nuclear bodies. J. Virol. 74:8532-8540.
    • (2000) J. Virol. , vol.74 , pp. 8532-8540
    • Schwam, D.R.1    Luciano, R.L.2    Mahajan, S.S.3    Wong, L.4    Wilson, A.C.5
  • 63
    • 33749243937 scopus 로고    scopus 로고
    • Recruitment of the de novo DNA methyltransferase Dnmt3a by Kaposi's sarcoma-associated herpesvirus LANA
    • Shamay, M., A. Krithivas, J. Zhang, and S. D. Hayward. 2006. Recruitment of the de novo DNA methyltransferase Dnmt3a by Kaposi's sarcoma-associated herpesvirus LANA. Proc. Natl. Acad. Sci. U. S. A. 103:14554-14559.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14554-14559
    • Shamay, M.1    Krithivas, A.2    Zhang, J.3    Hayward, S.D.4
  • 64
    • 0035844878 scopus 로고    scopus 로고
    • Spindle checkpoint protein Bub1 is required for kinetochore localization of Mad1, Mad2, Bub3, and CENP-E, independently of its kinase activity
    • Sharp-Baker, H., and R. H. Chen. 2001. Spindle checkpoint protein Bub1 is required for kinetochore localization of Mad1, Mad2, Bub3, and CENP-E, independently of its kinase activity. J. Cell Biol. 153:1239-1250.
    • (2001) J. Cell Biol. , vol.153 , pp. 1239-1250
    • Sharp-Baker, H.1    Chen, R.H.2
  • 65
    • 45749151740 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-encoded LANA can interact with the nuclear mitotic apparatus protein to regulate genome maintenance and segregation
    • Si, H., S. C. Verma, M. A. Lampson, Q. Cai, and E. S. Robertson. 2008. Kaposi's sarcoma-associated herpesvirus-encoded LANA can interact with the nuclear mitotic apparatus protein to regulate genome maintenance and segregation. J. Virol. 82:6734-6746.
    • (2008) J. Virol. , vol.82 , pp. 6734-6746
    • Si, H.1    Verma, S.C.2    Lampson, M.A.3    Cai, Q.4    Robertson, E.S.5
  • 66
    • 0037093326 scopus 로고    scopus 로고
    • Crystal structure of the tetrameric Mad1-Mad2 core complex: Implications of a 'safety belt' binding mechanism for the spindle checkpoint
    • Sironi, L., M. Mapelli, S. Knapp, A. De Antoni, K. T. Jeang, and A. Musacchio. 2002. Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint. EMBO J. 21:2496-2506.
    • (2002) EMBO J. , vol.21 , pp. 2496-2506
    • Sironi, L.1    Mapelli, M.2    Knapp, S.3    De Antoni, A.4    Jeang, K.T.5    Musacchio, A.6
  • 69
    • 0038305578 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen induces expression of the helix-loop-helix protein Id-1 in human endothelial cells
    • Tang, J., G. M. Gordon, M. G. Muller, M. Dahiya, and K. E. Foreman. 2003. Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen induces expression of the helix-loop-helix protein Id-1 in human endothelial cells. J. Virol. 77:5975-5984.
    • (2003) J. Virol. , vol.77 , pp. 5975-5984
    • Tang, J.1    Gordon, G.M.2    Muller, M.G.3    Dahiya, M.4    Foreman, K.E.5
  • 70
    • 33646098667 scopus 로고    scopus 로고
    • PP2A is required for centromeric localization of SgoI and proper chromosome segregation
    • Tang, Z., H. Shu, W. Qi, N. A. Mahmood, M. C. Mumby, and H. Yu. 2006. PP2A is required for centromeric localization of SgoI and proper chromosome segregation. Dev. Cell 10:575-585.
    • (2006) Dev. Cell , vol.10 , pp. 575-585
    • Tang, Z.1    Shu, H.2    Qi, W.3    Mahmood, N.A.4    Mumby, M.C.5    Yu, H.6
  • 71
    • 11144235699 scopus 로고    scopus 로고
    • Human Bub1 protects centromeric sister-chromatid cohesion through Shugoshin during mitosis
    • Tang, Z., Y. Sun, S. E. Harley, H. Zou, and H. Yu. 2004. Human Bub1 protects centromeric sister-chromatid cohesion through Shugoshin during mitosis. Proc. Natl. Acad. Sci. U. S. A. 101:18012-18017.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 18012-18017
    • Tang, Z.1    Sun, Y.2    Harley, S.E.3    Zou, H.4    Yu, H.5
  • 72
    • 0030687987 scopus 로고    scopus 로고
    • Kinetochore localization of murine Bub1 is required for normal mitotic timing and checkpoint response to spindle damage
    • Taylor, S. S., and F. McKeon. 1997. Kinetochore localization of murine Bub1 is required for normal mitotic timing and checkpoint response to spindle damage. Cell 89:727-735.
    • (1997) Cell , vol.89 , pp. 727-735
    • Taylor, S.S.1    McKeon, F.2
  • 73
    • 4544290097 scopus 로고    scopus 로고
    • Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus up-regulates transcription of human telomerase reverse transcriptase promoter through interaction with transcription factor Sp1
    • Verma, S. C., S. Borah, and E. S. Robertson. 2004. Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus up-regulates transcription of human telomerase reverse transcriptase promoter through interaction with transcription factor Sp1. J. Virol. 78:10348-10359.
    • (2004) J. Virol. , vol.78 , pp. 10348-10359
    • Verma, S.C.1    Borah, S.2    Robertson, E.S.3
  • 75
    • 33748484257 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen interacts with bromodomain protein Brd4 on host mitotic chromosomes
    • You, J., V. Srinivasan, G. V. Denis, W. J. Harrington, Jr., M. E. Ballestas, K. M. Kaye, and P. M. Howley. 2006. Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen interacts with bromodomain protein Brd4 on host mitotic chromosomes. J. Virol. 80:8909-8919.
    • (2006) J. Virol. , vol.80 , pp. 8909-8919
    • You, J.1    Srinivasan, V.2    Denis, G.V.3    Harrington Jr., W.J.4    Ballestas, M.E.5    Kaye, K.M.6    Howley, P.M.7
  • 76
    • 21544443242 scopus 로고    scopus 로고
    • Bub1 multitasking in mitosis
    • Yu, H., and Z. Tang. 2005. Bub1 multitasking in mitosis. Cell Cycle 4:262-265.
    • (2005) Cell Cycle , vol.4 , pp. 262-265
    • Yu, H.1    Tang, Z.2
  • 77
    • 0029101199 scopus 로고
    • The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization
    • Zhu, X., K. H. Chang, D. He, M. A. Mancini, W. R. Brinkley, and W. H. Lee. 1995. The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization. J. Biol. Chem. 270: 19545-19550.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19545-19550
    • Zhu, X.1    Chang, K.H.2    He, D.3    Mancini, M.A.4    Brinkley, W.R.5    Lee, W.H.6
  • 78
    • 0029098787 scopus 로고
    • Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression
    • Zhu, X., M. A. Mancini, K. H. Chang, C. Y. Liu, C. F. Chen, B. Shan, D. Jones, T. L. Yang-Feng, and W. H. Lee. 1995. Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression. Mol. Cell. Biol. 15:5017-5029.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5017-5029
    • Zhu, X.1    Mancini, M.A.2    Chang, K.H.3    Liu, C.Y.4    Chen, C.F.5    Shan, B.6    Jones, D.7    Yang-Feng, T.L.8    Lee, W.H.9


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