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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 陳美如(Mei-Ru Chen) | |
dc.contributor.author | Chung-Pei Lee | en |
dc.contributor.author | 李重霈 | zh_TW |
dc.date.accessioned | 2021-06-12T18:07:16Z | - |
dc.date.available | 2017-12-27 | |
dc.date.copyright | 2008-02-19 | |
dc.date.issued | 2007 | |
dc.date.submitted | 2007-12-27 | |
dc.identifier.citation | Adachi, Y., M. Luke, and U. K. Laemmli. 1991. Chromosome assembly in vitro: topoisomerase II is required for condensation. Cell 64:137-48.
Advani, S. J., R. R. Weichselbaum, and B. Roizman. 2003. Herpes simplex virus 1 activates cdc2 to recruit topoisomerase II alpha for post-DNA synthesis expression of late genes. Proc Natl Acad Sci U S A 100:4825-30. Aebi, U., J. Cohn, L. Buhle, and L. Gerace. 1986. The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323:560-4. Alber, F., S. Dokudovskaya, L. M. Veenhoff, W. Zhang, J. Kipper, D. Devos, A. Suprapto, O. Karni-Schmidt, R. Williams, B. T. Chait, A. Sali, and M. P. Rout. 2007. The molecular architecture of the nuclear pore complex. Nature 450:695-701. Aleem, E., H. Kiyokawa, and P. Kaldis. 2005. Cdc2-cyclin E complexes regulate the G1/S phase transition. Nat Cell Biol 7:831-6. Andersson, J. 2000. An Overview of Epstein-Barr Virus: from Discovery to Future Directions for Treatment and Prevention. Herpes 7:76-82. Arita, Y., P. Buffolino, and D. L. Coppock. 1998. Regulation of the cell cycle at the G2/M boundary in metastatic melanoma cells by 12-O-tetradecanoyl phorbol-13-acetate (TPA) by blocking p34cdc2 kinase activity. Exp Cell Res 242:381-90. Asai, R., A. Kato, K. Kato, M. Kanamori-Koyama, K. Sugimoto, T. Sairenji, Y. Nishiyama, and Y. Kawaguchi. 2006. Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1. J Virol 80:5125-34. Austin, C. A., and K. L. Marsh. 1998. Eukaryotic DNA topoisomerase II beta. Bioessays 20:215-26. Beaudette, K. N., J. Lew, and J. H. Wang. 1993. Substrate specificity characterization of a cdc2-like protein kinase purified from bovine brain. J Biol Chem 268:20825-30. Beausoleil, S. A., M. Jedrychowski, D. Schwartz, J. E. Elias, J. Villen, J. Li, M. A. Cohn, L. C. Cantley, and S. P. Gygi. 2004. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A 101:12130-5. Berthet, C., E. Aleem, V. Coppola, L. Tessarollo, and P. Kaldis. 2003. Cdk2 knockout mice are viable. Curr Biol 13:1775-85. Bjerke, S. L., and R. J. Roller. 2006. Roles for herpes simplex virus type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress. Virology 347:261-76. Broers, J. L., B. M. Machiels, G. J. van Eys, H. J. Kuijpers, E. M. Manders, R. van Driel, and F. C. Ramaekers. 1999. Dynamics of the nuclear lamina as monitored by GFP-tagged A-type lamins. J Cell Sci 112 ( Pt 20):3463-75. Broers, J. L., F. C. Ramaekers, G. Bonne, R. B. Yaou, and C. J. Hutchison. 2006. Nuclear lamins: laminopathies and their role in premature ageing. Physiol Rev 86:967-1008. Carpenter, A. J., and A. C. Porter. 2004. Construction, characterization, and complementation of a conditional-lethal DNA topoisomerase IIalpha mutant human cell line. Mol Biol Cell 15:5700-11. Chang, Y., C. H. Tung, Y. T. Huang, J. Lu, J. Y. Chen, and C. H. Tsai. 1999. Requirement for cell-to-cell contact in Epstein-Barr virus infection of nasopharyngeal carcinoma cells and keratinocytes. J Virol 73:8857-66. Chang, Y. E., and B. Roizman. 1993. The product of the UL31 gene of herpes simplex virus 1 is a nuclear phosphoprotein which partitions with the nuclear matrix. J Virol 67:6348-56. Chen, M. R., S. J. Chang, H. Huang, and J. Y. Chen. 2000. A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro. J Virol 74:3093-104. Chen, M. R., T. Y. Hsu, J. Y. Chen, and C. S. Yang. 1990. Molecular characterization of a cDNA clone encoding the Epstein-Barr virus (EBV) DNase. J Virol Methods 29:127-41. Chen, M. R., M. Y. Liu, S. M. Hsu, C. C. Fong, C. J. Chen, I. H. Chen, M. M. Hsu, C. S. Yang, and J. Y. Chen. 2001. Use of bacterially expressed EBNA-1 protein cloned from a nasopharyngeal carcinoma (NPC) biopsy as a screening test for NPC patients. J Med Virol 64:51-7. Chien, Y. C., J. Y. Chen, M. Y. Liu, H. I. Yang, M. M. Hsu, C. J. Chen, and C. S. Yang. 2001. Serologic markers of Epstein-Barr virus infection and nasopharyngeal carcinoma in Taiwanese men. N Engl J Med 345:1877-82. Collas, P. 1999. Sequential PKC- and Cdc2-mediated phosphorylation events elicit zebrafish nuclear envelope disassembly. J Cell Sci 112 ( Pt 6):977-87. Cortes, F., N. Pastor, S. Mateos, and I. Dominguez. 2003. Roles of DNA topoisomerases in chromosome segregation and mitosis. Mutat Res 543:59-66. Coulter, L. J., H. W. Moss, J. Lang, and D. J. McGeoch. 1993. A mutant of herpes simplex virus type 1 in which the UL13 protein kinase gene is disrupted. J Gen Virol 74 ( Pt 3):387-95. Cross, T., G. Griffiths, E. Deacon, R. Sallis, M. Gough, D. Watters, and J. M. Lord. 2000. PKC-delta is an apoptotic lamin kinase. Oncogene 19:2331-7. Cuvier, O., and T. Hirano. 2003. A role of topoisomerase II in linking DNA replication to chromosome condensation. J Cell Biol 160:645-55. Davis, F. M., T. Y. Tsao, S. K. Fowler, and P. N. Rao. 1983. Monoclonal antibodies to mitotic cells. Proc Natl Acad Sci U S A 80:2926-30. Davison, A. J., and J. E. Scott. 1986. The complete DNA sequence of varicella-zoster virus. J Gen Virol 67 ( Pt 9):1759-816. Dessev, G., C. Iovcheva-Dessev, J. R. Bischoff, D. Beach, and R. Goldman. 1991. A complex containing p34cdc2 and cyclin B phosphorylates the nuclear lamin and disassembles nuclei of clam oocytes in vitro. J Cell Biol 112:523-33. Diffley, J. F. 2004. Regulation of early events in chromosome replication. Curr Biol 14:R778-86. Earnshaw, W. C., B. Halligan, C. A. Cooke, M. M. Heck, and L. F. Liu. 1985. Topoisomerase II is a structural component of mitotic chromosome scaffolds. J Cell Biol 100:1706-15. Eggert, M., N. Radomski, D. Tripier, P. Traub, and E. Jost. 1991. Identification of phosphorylation sites on murine nuclear lamin C by RP-HPLC and microsequencing. FEBS Lett 292:205-9. El Achkar, E., M. Gerbault-Seureau, M. Muleris, B. Dutrillaux, and M. Debatisse. 2005. Premature condensation induces breaks at the interface of early and late replicating chromosome bands bearing common fragile sites. Proc Natl Acad Sci U S A 102:18069-74. Epstein, M. A., B. G. Achong, and Y. M. Barr. 1964. Virus Particles in Cultured Lymphoblasts from Burkitt's Lymphoma. Lancet 1:702-3. Escargueil, A. E., S. Y. Plisov, A. Skladanowski, A. Borgne, L. Meijer, G. J. Gorbsky, and A. K. Larsen. 2001. Recruitment of cdc2 kinase by DNA topoisomerase II is coupled to chromatin remodeling. FASEB J 15:2288-90. Farina, A., R. Feederle, S. Raffa, R. Gonnella, R. Santarelli, L. Frati, A. Angeloni, M. R. Torrisi, A. Faggioni, and H. J. Delecluse. 2005. BFRF1 of Epstein-Barr virus is essential for efficient primary viral envelopment and egress. J Virol 79:3703-12. Fawcett, D. W. 1966. On the occurrence of a fibrous lamina on the inner aspect of the nuclear envelope in certain cells of vertebrates. Am J Anat 119:129-45. Fisher, D. Z., N. Chaudhary, and G. Blobel. 1986. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc Natl Acad Sci U S A 83:6450-4. Frame, M. C., F. C. Purves, D. J. McGeoch, H. S. Marsden, and D. P. Leader. 1987. Identification of the herpes simplex virus protein kinase as the product of viral gene US3. J Gen Virol 68 ( Pt 10):2699-704. Gassmann, R., P. Vagnarelli, D. Hudson, and W. C. Earnshaw. 2004. Mitotic chromosome formation and the condensin paradox. Exp Cell Res 296:35-42. Geiss, B. J., G. L. Cano, J. E. Tavis, and L. A. Morrison. 2004. Herpes simplex virus 2 VP22 phosphorylation induced by cellular and viral kinases does not influence intracellular localization. Virology 330:74-81. Gershburg, E., and J. S. Pagano. 2007. Conserved herpesvirus protein kinases. Biochim Biophys Acta. Gershburg, E., S. Raffa, M. R. Torrisi, and J. S. Pagano. 2007. Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus. J Virol 81:5407-12. Gonnella, R., A. Farina, R. Santarelli, S. Raffa, R. Feederle, R. Bei, M. Granato, A. Modesti, L. Frati, H. J. Delecluse, M. R. Torrisi, A. Angeloni, and A. Faggioni. 2005. Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: interactions with BFRF1 and with the nuclear lamina. J Virol 79:3713-27. Gottesfeld, J. M., and D. J. Forbes. 1997. Mitotic repression of the transcriptional machinery. Trends Biochem Sci 22:197-202. Granzow, H., B. G. Klupp, W. Fuchs, J. Veits, N. Osterrieder, and T. C. Mettenleiter. 2001. Egress of alphaherpesviruses: comparative ultrastructural study. J Virol 75:3675-84. Greber, U. F., and A. Fassati. 2003. Nuclear import of viral DNA genomes. Traffic 4:136-43. Gruenbaum, Y., A. Margalit, R. D. Goldman, D. K. Shumaker, and K. L. Wilson. 2005. The nuclear lamina comes of age. Nat Rev Mol Cell Biol 6:21-31. Gupta, M., D. Trott, and A. C. Porter. 2007. Rescue of a human cell line from endogenous Cdk1 depletion by Cdk1 lacking inhibitory phosphorylation sites. J Biol Chem 282:4301-9. Hagstrom, K. A., and B. J. Meyer. 2003. Condensin and cohesin: more than chromosome compactor and glue. Nat Rev Genet 4:520-34. Heald, R., and F. McKeon. 1990. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 61:579-89. Henle, G., W. Henle, and V. Diehl. 1968. Relation of Burkitt's tumor-associated herpes-ytpe virus to infectious mononucleosis. Proc Natl Acad Sci U S A 59:94-101. Hirano, T. 2005. Condensins: organizing and segregating the genome. Curr Biol 15:R265-75. Hochegger, H., D. Dejsuphong, E. Sonoda, A. Saberi, E. Rajendra, J. Kirk, T. Hunt, and S. Takeda. 2007. An essential role for Cdk1 in S phase control is revealed via chemical genetics in vertebrate cells. J Cell Biol 178:257-68. Hoger, T. H., K. Zatloukal, I. Waizenegger, and G. Krohne. 1990. Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin. Chromosoma 100:67-9. Hong, G. K., M. L. Gulley, W. H. Feng, H. J. Delecluse, E. Holley-Guthrie, and S. C. Kenney. 2005a. Epstein-Barr virus lytic infection contributes to lymphoproliferative disease in a SCID mouse model. J Virol 79:13993-4003. Hong, G. K., P. Kumar, L. Wang, B. Damania, M. L. Gulley, H. J. Delecluse, P. J. Polverini, and S. C. Kenney. 2005b. Epstein-Barr virus lytic infection is required for efficient production of the angiogenesis factor vascular endothelial growth factor in lymphoblastoid cell lines. J Virol 79:13984-92. Hutchison, C. J., M. Alvarez-Reyes, and O. A. Vaughan. 2001. Lamins in disease: why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes? J Cell Sci 114:9-19. Izumi, M., O. A. Vaughan, C. J. Hutchison, and D. M. Gilbert. 2000. Head and/or CaaX domain deletions of lamin proteins disrupt preformed lamin A and C but not lamin B structure in mammalian cells. Mol Biol Cell 11:4323-37. Jin, P., S. Hardy, and D. O. Morgan. 1998. Nuclear localization of cyclin B1 controls mitotic entry after DNA damage. J Cell Biol 141:875-85. Kato, A., M. Yamamoto, T. Ohno, H. Kodaira, Y. Nishiyama, and Y. Kawaguchi. 2005. Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1. J Virol 79:9325-31. Kato, A., M. Yamamoto, T. Ohno, M. Tanaka, T. Sata, Y. Nishiyama, and Y. Kawaguchi. 2006. Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral Us3 protein kinase and regulates nuclear localization of viral envelopment factors UL34 and UL31. J Virol 80:1476-86. Kato, K., A. Yokoyama, Y. Tohya, H. Akashi, Y. Nishiyama, and Y. Kawaguchi. 2003. Identification of protein kinases responsible for phosphorylation of Epstein-Barr virus nuclear antigen leader protein at serine-35, which regulates its coactivator function. J Gen Virol 84:3381-92. Kawaguchi, Y., K. Kato, M. Tanaka, M. Kanamori, Y. Nishiyama, and Y. Yamanashi. 2003. Conserved protein kinases encoded by herpesviruses and cellular protein kinase cdc2 target the same phosphorylation site in eukaryotic elongation factor 1delta. J Virol 77:2359-68. Kawanishi, M. 1993. Topoisomerase I and II activities are required for Epstein-Barr virus replication. J Gen Virol 74:2263-8. Kieff, E. a. R., A.B. 2007. Epstein-Barr Virus and Its Replication, p. 2603-2667. In D. M. K. a. P. M. Howley (ed.), Fields Virology, 5 ed. Lippincott Williams & Wilkins. Kimura, K., O. Cuvier, and T. Hirano. 2001. Chromosome condensation by a human condensin complex in Xenopus egg extracts. J Biol Chem 276:5417-20. Kimura, K., M. Hirano, R. Kobayashi, and T. Hirano. 1998. Phosphorylation and activation of 13S condensin by Cdc2 in vitro. Science 282:487-90. Klein, E., L. L. Kis, and G. Klein. 2007. Epstein-Barr virus infection in humans: from harmless to life endangering virus-lymphocyte interactions. Oncogene 26:1297-305. Klupp, B. G., H. Granzow, and T. C. Mettenleiter. 2000. Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product. J Virol 74:10063-73. Kudoh, A., T. Daikoku, Y. Ishimi, Y. Kawaguchi, N. Shirata, S. Iwahori, H. Isomura, and T. Tsurumi. 2006. Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication. J Virol 80:10064-72. Kudoh, A., T. Daikoku, Y. Sugaya, H. Isomura, M. Fujita, T. Kiyono, Y. Nishiyama, and T. Tsurumi. 2004. Inhibition of S-phase cyclin-dependent kinase activity blocks expression of Epstein-Barr virus immediate-early and early genes, preventing viral lytic replication. J Virol 78:104-15. Kudoh, A., M. Fujita, T. Kiyono, K. Kuzushima, Y. Sugaya, S. Izuta, Y. Nishiyama, and T. Tsurumi. 2003. Reactivation of lytic replication from B cells latently infected with Epstein-Barr virus occurs with high S-phase cyclin-dependent kinase activity while inhibiting cellular DNA replication. J Virol 77:851-61. Kudoh, A., M. Fujita, L. Zhang, N. Shirata, T. Daikoku, Y. Sugaya, H. Isomura, Y. Nishiyama, and T. Tsurumi. 2005. Epstein-Barr virus lytic replication elicits ATM checkpoint signal transduction while providing an S-phase-like cellular environment. J Biol Chem 280:8156-63. Labrecque, L. G., D. M. Barnes, I. S. Fentiman, and B. E. Griffin. 1995. Epstein-Barr virus in epithelial cell tumors: a breast cancer study. Cancer Res 55:39-45. Laronne, A., S. Rotkopf, A. Hellman, Y. Gruenbaum, A. C. Porter, and M. Brandeis. 2003. Synchronization of interphase events depends neither on mitosis nor on cdk1. Mol Biol Cell 14:3730-40. Lawrence, G. L., M. Chee, M. A. Craxton, U. A. Gompels, R. W. Honess, and B. G. Barrell. 1990. Human herpesvirus 6 is closely related to human cytomegalovirus. J Virol 64:287-99. Leach, N., S. L. Bjerke, D. K. Christensen, J. M. Bouchard, F. Mou, R. Park, J. Baines, T. Haraguchi, and R. J. Roller. 2007. Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3. J Virol 81:10792-803. Lew, D. J., and S. Kornbluth. 1996. Regulatory roles of cyclin dependent kinase phosphorylation in cell cycle control. Curr Opin Cell Biol 8:795-804. Lin, C. T., C. I. Wong, W. Y. Chan, K. W. Tzung, J. K. Ho, M. M. Hsu, and S. M. Chuang. 1990. Establishment and characterization of two nasopharyngeal carcinoma cell lines. Lab Invest 62:713-24. Lin, J. C., W. Y. Wang, K. Y. Chen, Y. H. Wei, W. M. Liang, J. S. Jan, and R. S. Jiang. 2004. Quantification of plasma Epstein-Barr virus DNA in patients with advanced nasopharyngeal carcinoma. N Engl J Med 350:2461-70. Long, M. C., V. Leong, P. A. Schaffer, C. A. Spencer, and S. A. Rice. 1999. ICP22 and the UL13 protein kinase are both required for herpes simplex virus-induced modification of the large subunit of RNA polymerase II. J Virol 73:5593-604. Lou, Z., K. Minter-Dykhouse, and J. Chen. 2005. BRCA1 participates in DNA decatenation. Nat Struct Mol Biol 12:589-93. Lu, C. C., and M. R. Chen. 2006. Lytic replication of Epstein-Barr virus. Future Virology 1:435-46. Lu, C. C., Y. C. Chen, J. T. Wang, P. W. Yang, and M. R. Chen. 2007. Xeroderma pigmentosum C is involved in Epstein Barr virus DNA replication. J Gen Virol 88:3234-43. Lu, C. C., Y. Y. Jeng, C. H. Tsai, M. Y. Liu, S. W. Yeh, T. Y. Hsu, and M. R. Chen. 2006. Genome-wide transcription program and expression of the Rta responsive gene of Epstein-Barr virus. Virology 345:358-72. Machiels, B. M., A. H. Zorenc, J. M. Endert, H. J. Kuijpers, G. J. van Eys, F. C. Ramaekers, and J. L. Broers. 1996. An alternative splicing product of the lamin A/C gene lacks exon 10. J Biol Chem 271:9249-53. Makarova, O., E. Kamberov, and B. Margolis. 2000. Generation of deletion and point mutations with one primer in a single cloning step. Biotechniques 29:970-2. Malumbres, M. 2005. Revisiting the 'Cdk-centric' view of the mammalian cell cycle. Cell Cycle 4:206-10. Marechal, V., A. Dehee, R. Chikhi-Brachet, T. Piolot, M. Coppey-Moisan, and J. C. Nicolas. 1999. Mapping EBNA-1 domains involved in binding to metaphase chromosomes. J Virol 73:4385-92. Maresca, T. J., and R. Heald. 2006. The long and the short of it: linker histone H1 is required for metaphase chromosome compaction. Cell Cycle 5:589-91. Marin, O., F. Meggio, G. Draetta, and L. A. Pinna. 1992. The consensus sequences for cdc2 kinase and for casein kinase-2 are mutually incompatible. A study with peptides derived from the beta-subunit of casein kinase-2. FEBS Lett 301:111-4. Marschall, M., A. Marzi, P. aus dem Siepen, R. Jochmann, M. Kalmer, S. Auerochs, P. Lischka, M. Leis, and T. Stamminger. 2005. Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina. J Biol Chem 280:33357-67. Mauser, A., E. Holley-Guthrie, A. Zanation, W. Yarborough, W. Kaufmann, A. Klingelhutz, W. T. Seaman, and S. Kenney. 2002. The Epstein-Barr virus immediate-early protein BZLF1 induces expression of E2F-1 and other proteins involved in cell cycle progression in primary keratinocytes and gastric carcinoma cells. J Virol 76:12543-52. McGeoch, D. J., and A. J. Davison. 1986. Alphaherpesviruses possess a gene homologous to the protein kinase gene family of eukaryotes and retroviruses. Nucleic Acids Res 14:1765-77. McKeon, F. D., M. W. Kirschner, and D. Caput. 1986. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319:463-8. Mettenleiter, T. C., B. G. Klupp, and H. Granzow. 2006. Herpesvirus assembly: a tale of two membranes. Curr Opin Microbiol 9:423-9. Milbradt, J., S. Auerochs, and M. Marschall. 2007. Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C. J Gen Virol 88:2642-50. Moir, R. D., T. P. Spann, and R. D. Goldman. 1995. The dynamic properties and possible functions of nuclear lamins. Int Rev Cytol 162B:141-82. Monier, K., J. C. Armas, S. Etteldorf, P. Ghazal, and K. F. Sullivan. 2000. Annexation of the interchromosomal space during viral infection. Nat Cell Biol 2:661-5. Morgan, D. O. 1997. Cyclin-dependent kinases: engines, clocks, and microprocessors. Annu Rev Cell Dev Biol 13:261-91. Morris, J. B., H. Hofemeister, and P. O'Hare. 2007. Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein. J Virol 81:4429-37. Morrison, E. E., Y. F. Wang, and D. M. Meredith. 1998. Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument. J Virol 72:7108-14. Mou, F., T. Forest, and J. D. Baines. 2007. US3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells. J Virol 81:6459-70. Muranyi, W., J. Haas, M. Wagner, G. Krohne, and U. H. Koszinowski. 2002. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 297:854-7. Nishiyama, Y., Y. Yamada, R. Kurachi, and T. Daikoku. 1992. Construction of a US3 lacZ insertion mutant of herpes simplex virus type 2 and characterization of its phenotype in vitro and in vivo. Virology 190:256-68. Nowak, S. J., and V. G. Corces. 2004. Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet 20:214-20. Nurse, P. 1990. Universal control mechanism regulating onset of M-phase. Nature 344:503-8. Ogle, W. O., and B. Roizman. 1999. Functional anatomy of herpes simplex virus 1 overlapping genes encoding infected-cell protein 22 and US1.5 protein. J Virol 73:4305-15. Ono, T., Y. Fang, D. L. Spector, and T. Hirano. 2004. Spatial and temporal regulation of Condensins I and II in mitotic chromosome assembly in human cells. Mol Biol Cell 15:3296-308. Ortega, S., I. Prieto, J. Odajima, A. Martin, P. Dubus, R. Sotillo, J. L. Barbero, M. Malumbres, and M. Barbacid. 2003. Cyclin-dependent kinase 2 is essential for meiosis but not for mitotic cell division in mice. Nat Genet 35:25-31. Overton, H. A., D. J. McMillan, L. S. Klavinskis, L. Hope, A. J. Ritchie, and P. Wong-kai-in. 1992. Herpes simplex virus type 1 gene UL13 encodes a phosphoprotein that is a component of the virion. Virology 190:184-92. Park, R., and J. D. Baines. 2006. Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B. J Virol 80:494-504. Peter, M., J. Nakagawa, M. Doree, J. C. Labbe, and E. A. Nigg. 1990. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61:591-602. Purves, F. C., R. M. Longnecker, D. P. Leader, and B. Roizman. 1987. Herpes simplex virus 1 protein kinase is encoded by open reading frame US3 which is not essential for virus growth in cell culture. J Virol 61:2896-901. Purves, F. C., W. O. Ogle, and B. Roizman. 1993. Processing of the herpes simplex virus regulatory protein alpha 22 mediated by the UL13 protein kinase determines the accumulation of a subset of alpha and gamma mRNAs and proteins in infected cells. Proc Natl Acad Sci U S A 90:6701-5. Purves, F. C., and B. Roizman. 1992. The UL13 gene of herpes simplex virus 1 encodes the functions for posttranslational processing associated with phosphorylation of the regulatory protein alpha 22. Proc Natl Acad Sci U S A 89:7310-4. Purves, F. C., D. Spector, and B. Roizman. 1992. UL34, the target of the herpes simplex virus U(S)3 protein kinase, is a membrane protein which in its unphosphorylated state associates with novel phosphoproteins. J Virol 66:4295-303. Reynolds, A. E., L. Liang, and J. D. Baines. 2004. Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34. J Virol 78:5564-75. Reynolds, A. E., B. J. Ryckman, J. D. Baines, Y. Zhou, L. Liang, and R. J. Roller. 2001. U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids. J Virol 75:8803-17. Reynolds, A. E., E. G. Wills, R. J. Roller, B. J. Ryckman, and J. D. Baines. 2002. Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids. J Virol 76:8939-52. Rickinson, A. B. a. K., E. 2007. Epstein-Barr virus-associated malignancies of the immunocompromised host, p. 2668-2700. In D. M. K. a. P. M. Howley (ed.), Fields Virology, 5 ed, vol. 2. Lippincott Williams & Wilkins. Robison, J. G., J. Elliott, K. Dixon, and G. G. Oakley. 2004. Replication protein A and the Mre11.Rad50.Nbs1 complex co-localize and interact at sites of stalled replication forks. J Biol Chem 279:34802-10. Russo, J. J., R. A. Bohenzky, M. C. Chien, J. Chen, M. Yan, D. Maddalena, J. P. Parry, D. Peruzzi, I. S. Edelman, Y. Chang, and P. S. Moore. 1996. Nucleotide sequence of the Kaposi sarcoma-associated herpesvirus (HHV8). Proc Natl Acad Sci U S A 93:14862-7. Ryckman, B. J., and R. J. Roller. 2004. Herpes simplex virus type 1 primary envelopment: UL34 protein modification and the US3-UL34 catalytic relationship. J Virol 78:399-412. Sarisky, R. T., Z. Gao, P. M. Lieberman, E. D. Fixman, G. S. Hayward, and S. D. Hayward. 1996. A replication function associated with the activation domain of the Epstein-Barr virus Zta transactivator. J Virol 70:8340-7. Schroter, H., G. Maier, H. Ponstingl, and A. Nordheim. 1985. DNA intercalators induce specific release of HMG 14, HMG 17 and other DNA-binding proteins from chicken erythrocyte chromatin. Embo J 4:3867-72. Scott, E. S., and P. O'Hare. 2001. Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection. J Virol 75:8818-30. Shapiro, P. S., A. M. Whalen, N. S. Tolwinski, J. Wilsbacher, S. J. Froelich-Ammon, M. Garcia, N. Osheroff, and N. G. Ahn. 1999. Extracellular signal-regulated kinase activates topoisomerase IIalpha through a mechanism independent of phosphorylation. Mol Cell Biol 19:3551-60. Shumaker, D. K., E. R. Kuczmarski, and R. D. Goldman. 2003. The nucleoskeleton: lamins and actin are major players in essential nuclear functions. Curr Opin Cell Biol 15:358-66. Spann, T. P., A. E. Goldman, C. Wang, S. Huang, and R. D. Goldman. 2002. Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription. J Cell Biol 156:603-8. Spann, T. P., R. D. Moir, A. E. Goldman, R. Stick, and R. D. Goldman. 1997. Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis. J Cell Biol 136:1201-12. Stern, B., and P. Nurse. 1996. A quantitative model for the cdc2 control of S phase and mitosis in fission yeast. Trends Genet 12:345-50. Su, I. J., Y. H. Hsu, M. T. Lin, A. L. Cheng, C. H. Wang, and L. M. Weiss. 1993. Epstein-Barr virus-containing T-cell lymphoma presents with hemophagocytic syndrome mimicking malignant histiocytosis. Cancer 72:2019-27. Sumner, A. T. 1995. Inhibitors of topoisomerase II delay progress through mitosis and induce a doubling of the DNA content in CHO cells. Exp Cell Res 217:440-7. Swenson, J. J., A. E. Mauser, W. K. Kaufmann, and S. C. Kenney. 1999. The Epstein-Barr virus protein BRLF1 activates S phase entry through E2F1 induction. J Virol 73:6540-50. Takada, K., K. Horinouchi, Y. Ono, T. Aya, T. Osato, M. Takahashi, and S. Hayasaka. 1991. An Epstein-Barr virus-producer line Akata: establishment of the cell line and analysis of viral DNA. Virus Genes 5:147-56. Takemoto, A., K. Kimura, S. Yokoyama, and F. Hanaoka. 2004. Cell cycle-dependent phosphorylation, nuclear localization, and activation of human condensin. J Biol Chem 279:4551-9. Tarakanova, V., V. Leung-Pineda, S. Hwang, C. Yang, K. Matatall, M. Basson, R. Sun, H. Piwnica-Worms, B. Sleckman, and H. Virgin IV. 2007. gamma-Herpesvirus kinase actively initiates a DNA damage response by inducing phosphorylation of H2AX to foster viral replication. Cell Host and Microbe 1:275?86. Tsurumi, T., M. Fujita, and A. Kudoh. 2005. Latent and lytic Epstein-Barr virus replication strategies. Rev Med Virol 15:3-15. Ubersax, J. A., E. L. Woodbury, P. N. Quang, M. Paraz, J. D. Blethrow, K. Shah, K. M. Shokat, and D. O. Morgan. 2003. Targets of the cyclin-dependent kinase Cdk1. Nature 425:859-64. Uemura, T., H. Ohkura, Y. Adachi, K. Morino, K. Shiozaki, and M. Yanagida. 1987. DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe. Cell 50:917-25. Vaughan, A., M. Alvarez-Reyes, J. M. Bridger, J. L. Broers, F. C. Ramaekers, M. Wehnert, G. E. Morris, W. G. F. Whitfield, and C. J. Hutchison. 2001. Both emerin and lamin C depend on lamin A for localization at the nuclear envelope. J Cell Sci 114:2577-90. Vermeulen, W., S. Rademakers, N. G. Jaspers, E. Appeldoorn, A. Raams, B. Klein, W. J. Kleijer, L. K. Hansen, and J. H. Hoeijmakers. 2001. A temperature-sensitive disorder in basal transcription and DNA repair in humans. Nat Genet 27:299-303. Vlcek, S., and R. Foisner. 2007. Lamins and lamin-associated proteins in aging and disease. Curr Opin Cell Biol 19:298-304. Wang, J. T., P. W. Yang, C. P. Lee, C. H. Han, C. H. Tsai, and M. R. Chen. 2005. Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles. J Gen Virol 86:3215-25. Ward, G. E., and M. W. Kirschner. 1990. Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C. Cell 61:561-77. Wasserman, R. A., C. A. Austin, L. M. Fisher, and J. C. Wang. 1993. Use of yeast in the study of anticancer drugs targeting DNA topoisomerases: expression of a functional recombinant human DNA topoisomerase II alpha in yeast. Cancer Res 53:3591-6. Wells, N. J., and I. D. Hickson. 1995. Human topoisomerase II alpha is phosphorylated in a cell-cycle phase-dependent manner by a proline-directed kinase. Eur J Biochem 231:491-7. Yamashiro, S., and F. Matsumura. 1991. Mitosis-specific phosphorylation of caldesmon: possible molecular mechanism of cell rounding during mitosis. Bioessays 13:563-8. Young, L. S., and A. B. Rickinson. 2004. Epstein-Barr virus: 40 years on. Nat Rev Cancer 4:757-68. Yue, W., E. Gershburg, and J. S. Pagano. 2005. Hyperphosphorylation of EBNA2 by Epstein-Barr virus protein kinase suppresses transactivation of the LMP1 promoter. J Virol 79:5880-5. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/27497 | - |
dc.description.abstract | 泡疹病毒科的病毒在順利感染宿主細胞後,在細胞中面臨複製資源、細胞核內空間及核膜障壁等不同的限制;因此病毒必須演化出一套相應的策略,以進行有效率的病毒基因體複製及病毒顆粒成熟。過去對於EB病毒(Epstein-Barr Virus)複製的研究主要著重於探討參與病毒基因體複製、組裝或細胞週期調控相關病毒及細胞因子;但對EB病毒複製時對於宿主細胞核結構或核中染色質分佈的影響仍無明確及深入的研究。
我的研究首先利用觀察帶有EB病毒的鼻咽癌上皮細胞株NA或B細胞株Akata,發現在病毒再活化(reactivation)的同時,宿主細胞染色質有高度濃縮,而核模呈現不規則外型等現象。進一步探討病毒導致染色質高度濃縮及不規則核模形成的機制,發現EB病毒唯一的Ser/Thr蛋白質激酶BGLF4扮演了重要的角色。當BGLF4激酶單獨表現於細胞時,可在無需細胞DNA複製及細胞分裂蛋白質激酶Cdc2的參與下,造成未成熟染色體濃縮(premature chromosome condensation)、 核板蛋白層溶解(nuclear lamina disassemly)、細胞骨架重組(cytoskeleton rearrangement)等似未成熟細胞分裂現象(premature mitotic events)。在分子機制的探討中發現BGLF4和染色質濃縮主要調控因子濃縮素(condensin)有交互作用。於細胞或試管內實驗發現BGLF4可造成濃縮素於蛋白質激酶Cdc2調控次單元hCAP-G的磷酸化。另一方面,BGLF4可透過和調控細胞DNA結構的第二型拓樸酶 (topoisomerase II)交互作用和磷酸化,進而造成拓樸酶第二型蛋白磷酸化和解DNA環套作用能力(decatenation activity)的增進;顯示BGLF4激酶可能透過活化濃縮素和拓樸酶第二型蛋白造成未成熟染色體濃縮,進而提供更多的染色體外空間(extrachromosomal space)以利病毒複製。此外也發現這個造成宿主細胞未成熟染色體濃縮的能力是存在於其他丙型泡疹病毒激酶(gamma herpesviral kinases)中,如 卡波西氏肉瘤相關性病毒ORF36激酶(KSHV ORF36)及鼠泡疹病毒68型ORF36激酶(murine herpesvirus 68 ORF36)。 由於EB病毒於複製後必須克服來自宿主細胞的核膜障壁,以進行隨後的病毒顆粒成熟。因此在研究EB病毒對於宿主細胞核結構的影響上,發現BGLF4在造成未成熟染色體濃縮的同時也會造成細胞核板蛋白層溶解及細胞骨架重組。BGLF4可以和A和C型板蛋白(lamin A/C)交互作用(interaction)並於試管中造成 A型板蛋白(lamin A)磷酸化;這暗示EBV可透過BGLF4在無須其他病毒蛋白質的協助下直接調節核板蛋白層的完整性,可能進而有助於病毒核心顆粒(nucleocapsid)於細胞核膜的穿透。透過板蛋白點突變試驗,也發現人類泡疹病毒激酶(human herpesviral UL kinases)皆可透過板蛋白上相似的絲胺酸殘基(serine residues),造成宿主細胞核板蛋白層溶解。綜合本論文的研究發現了一個新的機制,顯示EB病毒BGLF4激酶可透過類似於細胞中Cdc2激酶的作用方式影響不同的細胞受質(substrates),進而造成多重似未成熟細胞分裂現象,於核內提供更多的染色體外空間及不完整的核板蛋白層。如此可有效解決來自細胞中對於細胞核內空間及核膜障壁的限制,有助於病毒基因體複製及病毒核心顆粒有效率的穿透細胞核膜。推測病毒複製時BGLF4激酶影響造成的宿主細胞核和染色質結構改變,也可能在 EB病毒的致病機轉上扮演角色。 | zh_TW |
dc.description.abstract | For efficient virus replication and virion production, herpesviruses must defeat several cellular limitations in replication resources, intranuclear space and nuclear architecture barrier. Previous studies of Epstein-Barr virus (EBV) replication focused mainly on the viral and cellular factors involved in replication compartment and cell cycle control. However, little is known about how EBV reorganizes nuclear architecture, the chromatin territories, nuclear envelope architecture and cell morphology.
In EBV-positive nasopharyngeal carcinoma NA cells or Burkitt’s lymphoma Akata cells, we noticed that cellular chromatin becomes highly condensed and nuclear envelope structure becomes irregular upon EBV reactivation. In searching for the possible mechanisms involved, we found that transient expression of EBV BGLF4 kinase induces unscheduled chromosome condensation and multiple premature mitotic events, such as nuclear lamina disassembly and stress fiber rearrangements, independent of cellular DNA replication and Cdc2 activity. To the mechanism, BGLF4 interacts with condensin complexes and phosphorylates condensin hCAP-G subunit at region similar to Cdc2-targeted. Additionally, BGLF4 phosphorylates and stimulates the decatenation activity of topoisomerase II, suggesting that BGLF4 may induce chromosome condensation through condensin and topoisomerase II activation. This unscheduled chromosome condensation may provide more extrachromosomal space for virus replication. The ability to induce chromosome condensation is conserved in gamma herpesviral kinase, such as KSHV ORF36 and murine herpesvirus 68 ORF36. For virion maturation, EBV must overcome the structural barrier of nuclear envelope of host cells. In the study of how EBV regulates nuclear architecture, we found BGLF4 induces the disruption of nuclear lamina and cytoskeleton rearrangement. BGLF4 interacts with lamin A/C and phosphorylates lamin A protein at sites more than Cdc2 targeted, suggesting BGLF4 is able to directly regulate the nuclear lamina independent of other viral proteins. BGLF4 mediated nuclear lamina disassembly may facilitate viral nucleocapsid egress through nuclear envelope. In addition, amino acid Ser-22, Ser-390 and Ser-392 residues of lamin A are important for BGLF4-induced nuclear lamina disassembly. The ability to induce nuclear lamin disassembly is conserved through human herpesviral UL protein kinases. Together, these findings suggest a novel mechanism by which human gamma-herpesviral kinases may induce multiple premature mitotic events to provide more extrachromosomal space and nuclear lamina disassembly for viral DNA replication and successful egress of nucleocapsids. Whether BGLF4 induced architecture changes in cellular chromatin and nuclear lamina may be involved in EBV pathogenesis will need further investigation. | en |
dc.description.provenance | Made available in DSpace on 2021-06-12T18:07:16Z (GMT). No. of bitstreams: 1 ntu-96-F91445121-1.pdf: 5984411 bytes, checksum: aef72898a2c10ab6c04a34e12fbe583b (MD5) Previous issue date: 2007 | en |
dc.description.tableofcontents | 中文摘要..................................................................................................................... I
Abstract................................................................................................................. ..... III Abbreviations............................................................................................................. V Contents...................................................................................................................... VII Chapter 1: Epstein-Barr virus and its BGLF4 kinase...................................... ..... 1 1.1 Epstein-Barr virus (EBV).............................................................................. 1 1.2 EBV replication strategies............................................................................. 4 1.3 EBV BGLF4 protein kinase........................................................................... 5 1.4 Herpesviral homologues of BGLF4 kinase.................................................... 6 1.5 Cellular homologues of BGLF4 kinase, cyclin-dependent kinases............... 8 1.6 The regulation of mitotic cyclin-dependent kinase, Cdc2 kinase.................. 9 1.7 Specific aims.................................................................................................. 10 Chapter 2: EBV BGLF4 kinase induces chromosome condensation.................... 11 2.1 Introduction.................................................................................................. 11 2.2 Results 2.2.1 EBV reactivation induces cellular chromatin condensation and interchromosomal space enlargement.................................................. 12 2.2.2 EBV BGLF4 kinase induces cellular chromosome condensation.............. 14 2.2.3 BGLF4 induces premature chromosome condensation independent of G2/M accumulation and Cdc2 signaling........................... 15 2.2.4 BGLF4 associates with cellular chromatin, interacts with condensin, and induces condensin phosphorylation................................... 16 2.2.5 BGLF4 phosphorylates topoisomerase II and stimulates its activity.................................................................................................... 19 2.2.6 Gamma-herpesviral kinases can induce chromosome condensation.......... 21 2.3 Conclusions 2.3.1 EBV replication induces changes in cellular chromatin architecture......... 22 2.3.2 BGLF4 induces cellular chromatin architecture change............................. 23 2.3.3 EBV BGLF4 kinase induces chromosome condensation through condensin and topoisomerase II phosphorylation and activation................ 24 Chapter 3: EBV BGLF4 kinase induces nuclear lamina disassembly................... 25 3.1 Introduction 2.2.1 The architecture and dynamics of nuclear lamina....................................... 25 2.2.2 Nuclear lamina alteration during herpesvirus infection............................... 26 3.2 Results 3.2.1 BGLF4 induces nuclear lamina disassembly............................................... 28 3.2.2 BGLF4 interacts with lamin A/C and induces lamin A phosphorylation........................................................................................... 29 3.2.3 Ser-22, Ser-390 and Ser-392 of lamin A are important for BGLF4-induces nuclear lamina disassembly.............................................. 31 3.2.4 BGLF4 target sites are important for EBV reactivation-mediated nuclear lamin redistribution......................................................................... 33 3.2.5 BGLF4 induces reorganization of the cytoskeleton, but not centrosome polarization............................................................................... 34 3.2.6 Human herpesviral UL protein kinases induce nuclear lamina redistribution through similar mechanism................................................... 35 3.3 Conclusion..................................................................................................... 37 Chapter 4: Discussions............................................................................................... 38 4.1 BGLF4 kinase induces multiple mitosis-like events through Cdc2 mimicry................................................................................. 38 4.2 The contribution of BGLF4-induced premature mitotic events to EBV replication 4.2.1 BGLF4-induced mitosis-like events may facilitate virus replication and maturation........................................................................... 41 4.2.2 BGLF4 kinase may regulate cellular environment through nuclear lamina modification.......................................................... 45 4.2.3 Possible effects of BGLF4 on EBV pathogenesis....................................... 46 4.3 The role of herpesviral kinases in nuclear changes 4.3.1 Gammaherpesviral kinases-induced chromosome condensation................ 46 4.3.2 Human herpesviral UL kinases-induced nuclear lamin redistribution........ 47 Chapter 5: Materials and methods........................................................................... 49 5.1 Cell culture...................................................................................................... 49 5.2 Virus induction and transfection..................................................................... 49 5.3 Plasmid construction....................................................................................... 50 5.4 Antibodies and indirect immunofluorescence assay....................................... 51 5.5 Chromosome spreads...................................................................................... 52 5.6 DNA content analysis..................................................................................... 52 5.7 Co-immunoprecipitation assay....................................................................... 53 5.8 Immunoblot analysis....................................................................................... 53 5.9 Expression of BGLF4 and K102I proteins in recombinant baculoviruses system................................................................. 54 5.10 Immunoprecipitation kinase assays.............................................................. 55 5.11 Subcellular fractionation of chromatin-associated proteins.......................... 56 5.12 Expression and purification of bacterially expressed GST fusion proteins...................................................................................... 56 5.13 Pulsed-field gel electrophoresis.................................................................... 57 5.14 DNA decatenation assay................................................................................ 58 5.15 BrdU incorporation assay.............................................................................. 58 5.16 Thymidine incorporation assay..................................................................... 59 5.17 Overall transcription assay............................................................................ 59 Tables........................................................................................................................... 60 Table 1. Oligonucleotides primers and plasmid DNA templates used in this study..................................................................................... 60 Table 2. Immunofluorescence assay conditions used in this study....................... 61 Table 3. Summary of newly identified EBV BGLF4 kinase targeting proteins and putative target sequence...................................... 62 Table 4. The ability of herpesviral kinases to induce chromosome condensation and lamina disassembly..................................................... 63 Figures......................................................................................................................... 64 Fig. 1. EBV reactivation induces morphological changes in cellular chromosome................................................................................. 64 Fig. 2. EBV reactivation induces cell morphological changes............................. 65 Fig. 3. Expression profiles of cellular Cdc2, cyclin B and viral proteins in EBV-replicating NA and EBV-negative TW01 cells............................ 66 Fig. 4. BGLF4 kinase induces cellular DNA condensation.................................. 67 Fig. 5. BGLF4 expression levels in EBV-replicating Akata, NA or transiently transfected HeLa cells......................................................... 68 Fig. 6. BGLF4 induces chromosome condensation independent of G2/M accumulation and DNA replication............................................ 69 Fig. 7. BGLF4 induces chromosome condensation independent of Cdc2 signaling...................................................................................... 70 Fig. 8. BGLF4 induces multiple protein phosphorylations on MPM-2 epitope.................................................................................... 71 Fig. 9. BGLF4 associates with cellular chromatin............................................... 72 Fig. 10. BGLF4 interacts with human condensin complexes............................... 73 Fig. 11. BGLF4 interacts with condensin independent of the presence of DNA............................................................................... 74 Fig. 12. BGLF4 induces condensin phosphorylation in vivo............................... 75 Fig. 13. BGLF4 induced autophosphorylation and histone H1 phosphorylation.................................................................... 76 Fig. 14. Purification of bacterially expressed GST-fusion human condensin hCAP-G protein fragments........................................ 77 Fig. 15. BGLF4 phosphorylates condensin hCAP-G subunit in vitro........................................................................................ 78 Fig. 16. BGLF4 interacts with topoisomerase II | |
dc.language.iso | en | |
dc.title | EB病毒BGLF4 蛋白質酶引發未成熟染色體濃縮及核板蛋白層溶解之研究 | zh_TW |
dc.title | Study on Epstein-Barr virus BGLF4 kinase-induced premature chromosome condensation and nuclear lamina disassembly | en |
dc.type | Thesis | |
dc.date.schoolyear | 96-1 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 陳振陽(Jen-Yang Chen),蔡錦華(Ching-Hwa Tsai),李財坤(Tsai-Kun Li),羅婉升(Wan-Sheng Lo),張智芬(Zee-Fen Chang) | |
dc.subject.keyword | BGLF4 激酶,Cdc2 激酶,聚合素,EB 病毒,板蛋白A/C,未成熟染色體濃縮,核板蛋白層溶解,拓,樸酶,第二型, | zh_TW |
dc.subject.keyword | BGLF4 kinase,Cdc2,condensin,Epstein-Barr virus,lamin A/C,premature chromosome condensation,nuclear lamina disassembly,topoisomerase IIα, | en |
dc.relation.page | 125 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2007-12-27 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 微生物學研究所 | zh_TW |
顯示於系所單位: | 微生物學科所 |
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