Please use this identifier to cite or link to this item:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/51330Full metadata record
| ???org.dspace.app.webui.jsptag.ItemTag.dcfield??? | Value | Language |
|---|---|---|
| dc.contributor.advisor | 張鑫(Shin C. Chang) | |
| dc.contributor.author | Yen-Ju Chen | en |
| dc.contributor.author | 陳彥儒 | zh_TW |
| dc.date.accessioned | 2021-06-15T13:30:44Z | - |
| dc.date.available | 2021-02-26 | |
| dc.date.copyright | 2016-02-26 | |
| dc.date.issued | 2016 | |
| dc.date.submitted | 2016-02-03 | |
| dc.identifier.citation | 1. Feinstone, S.M., et al., Transfusion-associated hepatitis not due to viral
hepatitis type A or B. N Engl J Med, 1975. 292(15): p. 767-70. 2. Choo, Q.L., et al., Isolation of a cDNA clone derived from a blood-borne non- A, non-B viral hepatitis genome. Science, 1989. 244(4902): p. 359-62. 3. Kuo, G., et al., An assay for circulating antibodies to a major etiologic virus of human non-A, non-B hepatitis. Science, 1989. 244(4902): p. 362-4. 4. Moradpour, D., F. Penin, and C.M. Rice, Replication of hepatitis C virus. Nat Rev Microbiol, 2007. 5(6): p. 453-63. 5. Arzumanyan, A., H.M. Reis, and M.A. Feitelson, Pathogenic mechanisms in HBV- and HCV-associated hepatocellular carcinoma. Nat Rev Cancer, 2013. 13(2): p. 123-35. 6. Averhoff, F.M., N. Glass, and D. Holtzman, Global burden of hepatitis C: considerations for healthcare providers in the United States. Clin Infect Dis, 2012. 55 Suppl 1: p. S10-5. 7. Jeong, S.W., J.Y. Jang, and R.T. Chung, Hepatitis C virus and hepatocarcinogenesis. Clin Mol Hepatol, 2012. 18(4): p. 347-56. 8. Fried, M.W., et al., Peginterferon alfa-2a plus ribavirin for chronic hepatitis C virus infection. N Engl J Med, 2002. 347(13): p. 975-82. 9. Afdhal, N., et al., Ledipasvir and sofosbuvir for untreated HCV genotype 1 infection. N Engl J Med, 2014. 370(20): p. 1889-98. 10. Paul, D., V. Madan, and R. Bartenschlager, Hepatitis C virus RNA replication and assembly: living on the fat of the land. Cell Host Microbe, 2014. 16(5): p. 569-79. 11. Tsukiyama-Kohara, K., et al., Internal ribosome entry site within hepatitis C virus RNA. J Virol, 1992. 66(3): p. 1476-83. 12. Wang, C., P. Sarnow, and A. Siddiqui, Translation of human hepatitis C virus RNA in cultured cells is mediated by an internal ribosome-binding mechanism. J Virol, 1993. 67(6): p. 3338-44. 13. Jopling, C.L., et al., Modulation of hepatitis C virus RNA abundance by a liverspecific MicroRNA. Science, 2005. 309(5740): p. 1577-81. 14. Friebe, P. and R. Bartenschlager, Genetic analysis of sequences in the 3' nontranslated region of hepatitis C virus that are important for RNA replication. J Virol, 2002. 76(11): p. 5326-38. 15. Yi, M. and S.M. Lemon, 3' nontranslated RNA signals required for replication of hepatitis C virus RNA. J Virol, 2003. 77(6): p. 3557-68. 16. Gawlik, K. and P.A. Gallay, HCV core protein and virus assembly: what we 57 know without structures. Immunol Res, 2014. 60(1): p. 1-10. 17. Ivanyi-Nagy, R., et al., Analysis of hepatitis C virus RNA dimerization and core- RNA interactions. Nucleic Acids Res, 2006. 34(9): p. 2618-33. 18. Sharma, K., et al., Kinetic analysis of the nucleic acid chaperone activity of the hepatitis C virus core protein. Nucleic Acids Res, 2010. 38(11): p. 3632-42. 19. Syed, G.H., Y. Amako, and A. Siddiqui, Hepatitis C virus hijacks host lipid metabolism. Trends Endocrinol Metab, 2010. 21(1): p. 33-40. 20. Boulant, S., et al., Structural determinants that target the hepatitis C virus core protein to lipid droplets. J Biol Chem, 2006. 281(31): p. 22236-47. 21. Chang, S.C., et al., Nuclear localization signals in the core protein of hepatitis C virus. Biochem Biophys Res Commun, 1994. 205(2): p. 1284-90. 22. Ravaggi, A., et al., Intracellular localization of full-length and truncated hepatitis C virus core protein expressed in mammalian cells. J Hepatol, 1994. 20(6): p. 833-6. 23. Suzuki, R., et al., Nuclear localization of the truncated hepatitis C virus core protein with its hydrophobic C terminus deleted. J Gen Virol, 1995. 76 ( Pt 1): p. 53-61. 24. Ray, R.B., et al., Transcriptional repression of p53 promoter by hepatitis C virus core protein. J Biol Chem, 1997. 272(17): p. 10983-6. 25. Masaki, T., et al., Interaction of hepatitis C virus nonstructural protein 5A with core protein is critical for the production of infectious virus particles. J Virol, 2008. 82(16): p. 7964-76. 26. Herker, E., et al., Efficient hepatitis C virus particle formation requires diacylglycerol acyltransferase-1. Nat Med, 2010. 16(11): p. 1295-8. 27. Menzel, N., et al., MAP-kinase regulated cytosolic phospholipase A2 activity is essential for production of infectious hepatitis C virus particles. PLoS Pathog, 2012. 8(7): p. e1002829. 28. Neveu, G., et al., Identification and targeting of an interaction between a tyrosine motif within hepatitis C virus core protein and AP2M1 essential for viral assembly. PLoS Pathog, 2012. 8(8): p. e1002845. 29. Ikeda, M., et al., Selectable subgenomic and genome-length dicistronic RNAs derived from an infectious molecular clone of the HCV-N strain of hepatitis C virus replicate efficiently in cultured Huh7 cells. J Virol, 2002. 76(6): p. 2997- 3006. 30. Kang, S.M., et al., Regulation of hepatitis C virus replication by the core protein through its interaction with viral RNA polymerase. Biochem Biophys Res Commun, 2009. 386(1): p. 55-9. 31. Horner, S.M. and M. Gale, Jr., Regulation of hepatic innate immunity by 58 hepatitis C virus. Nat Med, 2013. 19(7): p. 879-88. 32. Melen, K., et al., Expression of hepatitis C virus core protein inhibits interferoninduced nuclear import of STATs. J Med Virol, 2004. 73(4): p. 536-47. 33. Lin, W., et al., Hepatitis C virus core protein blocks interferon signaling by interaction with the STAT1 SH2 domain. J Virol, 2006. 80(18): p. 9226-35. 34. Kao, C.F., et al., Modulation of p53 transcription regulatory activity and posttranslational modification by hepatitis C virus core protein. Oncogene, 2004. 23(14): p. 2472-83. 35. Herzer, K., et al., Hepatitis C virus core protein inhibits tumor suppressor protein promyelocytic leukemia function in human hepatoma cells. Cancer Res, 2005. 65(23): p. 10830-7. 36. Cho, J., et al., HCV core protein modulates Rb pathway through pRb downregulation and E2F-1 up-regulation. Biochim Biophys Acta, 2001. 1538(1): p. 59-66. 37. Piodi, A., et al., Morphological changes in intracellular lipid droplets induced by different hepatitis C virus genotype core sequences and relationship with steatosis. Hepatology, 2008. 48(1): p. 16-27. 38. Moriishi, K., et al., Critical role of PA28gamma in hepatitis C virus-associated steatogenesis and hepatocarcinogenesis. Proc Natl Acad Sci U S A, 2007. 104(5): p. 1661-6. 39. Dharancy, S., et al., Impaired expression of the peroxisome proliferatoractivated receptor alpha during hepatitis C virus infection. Gastroenterology, 2005. 128(2): p. 334-42. 40. Deleersnyder, V., et al., Formation of native hepatitis C virus glycoprotein complexes. J Virol, 1997. 71(1): p. 697-704. 41. Bartosch, B., et al., Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor. J Biol Chem, 2003. 278(43): p. 41624-30. 42. Pileri, P., et al., Binding of hepatitis C virus to CD81. Science, 1998. 282(5390): p. 938-41. 43. Griffin, S.D., et al., The p7 protein of hepatitis C virus forms an ion channel that is blocked by the antiviral drug, Amantadine. FEBS Lett, 2003. 535(1-3): p. 34-8. 44. Steinmann, E., et al., Hepatitis C virus p7 protein is crucial for assembly and release of infectious virions. PLoS Pathog, 2007. 3(7): p. e103. 45. Reed, K.E., A. Grakoui, and C.M. Rice, Hepatitis C virus-encoded NS2-3 protease: cleavage-site mutagenesis and requirements for bimolecular cleavage. J Virol, 1995. 69(7): p. 4127-36. 59 46. Stempniak, M., et al., The NS3 proteinase domain of hepatitis C virus is a zinccontaining enzyme. J Virol, 1997. 71(4): p. 2881-6. 47. Grakoui, A., et al., Expression and identification of hepatitis C virus polyprotein cleavage products. J Virol, 1993. 67(3): p. 1385-95. 48. Kim, D.W., et al., C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity. Biochem Biophys Res Commun, 1995. 215(1): p. 160-6. 49. Tanji, Y., et al., Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing. J Virol, 1995. 69(3): p. 1575-81. 50. Pang, P.S., et al., The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. EMBO J, 2002. 21(5): p. 1168-76. 51. Egger, D., et al., Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J Virol, 2002. 76(12): p. 5974-84. 52. Evans, M.J., C.M. Rice, and S.P. Goff, Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication. Proc Natl Acad Sci U S A, 2004. 101(35): p. 13038-43. 53. Behrens, S.E., L. Tomei, and R. De Francesco, Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus. EMBO J, 1996. 15(1): p. 12-22. 54. Lohmann, V., et al., Biochemical properties of hepatitis C virus NS5B RNAdependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity. J Virol, 1997. 71(11): p. 8416-28. 55. Zhong, W., et al., De novo initiation of RNA synthesis by hepatitis C virus nonstructural protein 5B polymerase. J Virol, 2000. 74(4): p. 2017-22. 56. Cheng, J.C., M.F. Chang, and S.C. Chang, Specific interaction between the hepatitis C virus NS5B RNA polymerase and the 3' end of the viral RNA. J Virol, 1999. 73(8): p. 7044-9. 57. You, S., et al., A cis-acting replication element in the sequence encoding the NS5B RNA-dependent RNA polymerase is required for hepatitis C virus RNA replication. J Virol, 2004. 78(3): p. 1352-66. 58. Kumon, I., In situ characterization of mononuclear cell phenotype in intrahepatic lymphoid follicles in patients with chronic viral hepatitis. Gastroenterol Jpn, 1992. 27(5): p. 638-45. 59. Lindenbach, B.D. and C.M. Rice, The ins and outs of hepatitis C virus entry and assembly. Nat Rev Microbiol, 2013. 11(10): p. 688-700. 60. Pereira, A.A. and I.M. Jacobson, New and experimental therapies for HCV. Nat Rev Gastroenterol Hepatol, 2009. 6(7): p. 403-11. 60 61. Kong, L., et al., Hepatitis C virus E2 envelope glycoprotein core structure. Science, 2013. 342(6162): p. 1090-4. 62. Evans, M.J., et al., Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry. Nature, 2007. 446(7137): p. 801-5. 63. Ploss, A., et al., Human occludin is a hepatitis C virus entry factor required for infection of mouse cells. Nature, 2009. 457(7231): p. 882-6. 64. Meertens, L., C. Bertaux, and T. Dragic, Hepatitis C virus entry requires a critical postinternalization step and delivery to early endosomes via clathrincoated vesicles. J Virol, 2006. 80(23): p. 11571-8. 65. Blanchard, E., et al., Hepatitis C virus entry depends on clathrin-mediated endocytosis. J Virol, 2006. 80(14): p. 6964-72. 66. McMahon, H.T. and E. Boucrot, Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat Rev Mol Cell Biol, 2011. 12(8): p. 517-33. 67. Tosoni, D., et al., TTP specifically regulates the internalization of the transferrin receptor. Cell, 2005. 123(5): p. 875-88. 68. Paul, D., et al., Morphological and biochemical characterization of the membranous hepatitis C virus replication compartment. J Virol, 2013. 87(19): p. 10612-27. 69. Elazar, M., et al., An N-terminal amphipathic helix in hepatitis C virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication. J Virol, 2004. 78(20): p. 11393- 400. 70. Reiss, S., et al., Recruitment and activation of a lipid kinase by hepatitis C virus NS5A is essential for integrity of the membranous replication compartment. Cell Host Microbe, 2011. 9(1): p. 32-45. 71. Boulant, S., et al., Hepatitis C virus core protein induces lipid droplet redistribution in a microtubule- and dynein-dependent manner. Traffic, 2008. 9(8): p. 1268-82. 72. Masaki, T., et al., Involvement of hepatitis C virus NS5A hyperphosphorylation mediated by casein kinase I-alpha in infectious virus production. J Virol, 2014. 88(13): p. 7541-55. 73. Farci, P., et al., Lack of protective immunity against reinfection with hepatitis C virus. Science, 1992. 258(5079): p. 135-40. 74. Choo, Q.L., et al., Vaccination of chimpanzees against infection by the hepatitis C virus. Proc Natl Acad Sci U S A, 1994. 91(4): p. 1294-8. 75. Dorner, M., et al., A genetically humanized mouse model for hepatitis C virus infection. Nature, 2011. 474(7350): p. 208-11. 61 76. Dorner, M., et al., Completion of the entire hepatitis C virus life cycle in genetically humanized mice. Nature, 2013. 501(7466): p. 237-41. 77. Shimizu, Y.K., et al., Evidence for in vitro replication of hepatitis C virus genome in a human T-cell line. Proc Natl Acad Sci U S A, 1992. 89(12): p. 5477-81. 78. Yoo, B.J., et al., Transfection of a differentiated human hepatoma cell line (Huh7) with in vitro-transcribed hepatitis C virus (HCV) RNA and establishment of a long-term culture persistently infected with HCV. J Virol, 1995. 69(1): p. 32-8. 79. Lohmann, V., et al., Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science, 1999. 285(5424): p. 110-3. 80. Blight, K.J., J.A. McKeating, and C.M. Rice, Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication. J Virol, 2002. 76(24): p. 13001-14. 81. Kato, T., et al., Efficient replication of the genotype 2a hepatitis C virus subgenomic replicon. Gastroenterology, 2003. 125(6): p. 1808-17. 82. Wakita, T., et al., Production of infectious hepatitis C virus in tissue culture from a cloned viral genome. Nat Med, 2005. 11(7): p. 791-6. 83. Lindenbach, B.D., et al., Complete replication of hepatitis C virus in cell culture. Science, 2005. 309(5734): p. 623-6. 84. Zhong, J., et al., Robust hepatitis C virus infection in vitro. Proc Natl Acad Sci U S A, 2005. 102(26): p. 9294-9. 85. Gailus, S., et al., Insights into lysosomal cobalamin trafficking: lessons learned from cblF disease. J Mol Med (Berl), 2010. 88(5): p. 459-66. 86. Clark, R.M., P.C. Marker, and D.M. Kingsley, A novel candidate gene for mouse and human preaxial polydactyly with altered expression in limbs of Hemimelic extra-toes mutant mice. Genomics, 2000. 67(1): p. 19-27. 87. Lettice, L.A., et al., Disruption of a long-range cis-acting regulator for Shh causes preaxial polydactyly. Proc Natl Acad Sci U S A, 2002. 99(11): p. 7548- 53. 88. Rutsch, F., et al., Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism. Nat Genet, 2009. 41(2): p. 234-9. 89. Tseng, L.T., et al., LMBD1 protein serves as a specific adaptor for insulin receptor internalization. J Biol Chem, 2013. 288(45): p. 32424-32. 90. Wang, Y.H., et al., Novel nuclear export signal-interacting protein, NESI, critical for the assembly of hepatitis delta virus. J Virol, 2005. 79(13): p. 8113- 20. 62 91. Huang, C., et al., Nuclear export signal-interacting protein forms complexes with lamin A/C-Nups to mediate the CRM1-independent nuclear export of large hepatitis delta antigen. J Virol, 2013. 87(3): p. 1596-604. 92. Wu, S.C., et al., Hepatitis C virus NS5A protein down-regulates the expression of spindle gene Aspm through PKR-p38 signaling pathway. J Biol Chem, 2008. 283(43): p. 29396-404. 93. 高志賢,2008,利用新建立之C 型肝炎病毒感染細胞株篩選可調節病毒複 製之宿主細胞因子及化合物,碩士論文 94. 蔡雅莉,2002,建立以重組腺病毒誘導C 型肝炎病毒核心蛋白質表現之系 統,碩士論文 95. Hinson, E.R. and P. Cresswell, The antiviral protein, viperin, localizes to lipid droplets via its N-terminal amphipathic alpha-helix. Proc Natl Acad Sci U S A, 2009. 106(48): p. 20452-7. 96. Cheng, J.C., et al., 293 cells over-expressing human ADI1 and CD81 are permissive for serum-derived hepatitis C virus infection. J Med Virol, 2009. 81(9): p. 1560-8. 97. Kato, T., et al., Cell culture and infection system for hepatitis C virus. Nat Protoc, 2006. 1(5): p. 2334-9. 98. Sumpter, R., Jr., et al., Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I. J Virol, 2005. 79(5): p. 2689-99. 99. Ceresa, B.P., et al., Inhibition of clathrin-mediated endocytosis selectively attenuates specific insulin receptor signal transduction pathways. Mol Cell Biol, 1998. 18(7): p. 3862-70. 100. Wen, Y. and C. Cheng Kao, The hepatitis C virus core protein can modulate RNA-dependent RNA synthesis by the 2a polymerase. Virus Res, 2014. 189: p. 165-76. 101. 張均薇,2012,LMBD1 蛋白質參與C 型肝炎病毒的增殖,碩士論文 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/51330 | - |
| dc.description.abstract | C 型肝炎病毒(Hepatitis C virus,HCV)主要經由血液和體液傳染,此病毒感
染會造成C 型肝炎,屬於全球性的感染疾病。目前全球大約有一億五千萬人是慢 性C 型肝炎患者。HCV 在感染宿主細胞後,會在內質網的周邊形成適合病毒複 製的特殊網狀結構,並且在細胞中的油滴(lipid droplet)上進行病毒顆粒的組裝。 本實驗室先前的研究發現,在細胞中過量表現LMBD1 重組蛋白質時,此蛋白質 與細胞中的油滴有明顯共位(co-localization)的現象,此外,在細胞中同時送入 LMBD1 與HCV 之core 蛋白質的表現質體後也可以觀察到LMBD1 與core 蛋白 質的共位現象。更進一步以shRNA 將lmbrd1 基因踢弱(knockdown)後,再過量 表現HCV 的core 蛋白質時,發現在踢弱lmbrd1 基因的細胞中,core 蛋白質的 分布會散開在細胞質中,無法保持在細胞核附近聚集的狀態。為了瞭解LMBD1 蛋白質與HCV 的相關性,本研究首先以免疫共沉澱的方式證實LMBD1 蛋白質 與core 蛋白質具有交互作用,接著以Huh7.5 細胞建立的感染性HCV 細胞培養 系統(infectious HCV cell culture system,infectious HCVcc system)探討LMBD1 蛋 白質在HCV 的生活史中所扮演的角色。以HCVcc conditional medium 感染lmbrd1 基因受到踢弱的Huh7.5 細胞,RT-qPCR 的結果發現在細胞內病毒的負向基因體 有明顯升高的情況。進一步研究顯示,LMBD1 蛋白質並不參與HCV 貼附與進 入宿主細胞的過程,而是參與在HCV 之病毒基因體的複製過程。然而在帶有病 毒次基因體(subgenome replicon)的細胞株中踢弱lmbrd1 基因時卻發現subgenome replicon 之負向基因體的複製受到抑制。另一方面,當過量表現LMBD1 重組蛋 白質在lmbrd1 基因受到踢弱的細胞中時,不論是在HCV 細胞培養系統或在HCV subgenome replicon 系統中,都具有增強HCV RNA 複製的現象。LMBD1 蛋白質 對HCV 基因體的調控是否和core 蛋白質與LMBD1 蛋白質的交互作用有關,有 待更進一步的探討。 | zh_TW |
| dc.description.abstract | Hepatitis C virus infection is mainly transmitted through blood and body fluids.
The viral infection can cause the occurrence of hepatitis C which belongs to the global infection disease. There are 150 million people suffered from chronic hepatitis C infection in the world. HCV infection induces formation of membranous web around the endoplasmic reticulum where the replication of genome takes place. In our previous studies, ectopically expressed LMBD1 recombinant protein was found to localize on the surface of lipid droplets. In addition, colocalization of LMBD1 and HCV core protein was observed. Furthermore, distribution of the core protein became scattering when lmbrd1 was knocked down. Towards understanding the association of LMBD1 with HCV in this study, the interaction between LMBD1 and HCV core protein was confirmed by co-immunoprecipitation assay. The infectious HCV cell culture system (HCVcc system) was established to elucidate the roles of LMBD1 in HCV life cycle. Results from RT-qPCR demonstrated an enhancement of HCV anti-genomic RNAlevel in lmbrd1 knockdown cells. This is mainly due to an effect on the viral genome replication rather than the viral attachment and entry. However, the replication of viral RNA was reduced in lmbrd1 knockdown HCVR subgenome replicon cells. On the other hand, HCV RNA replication was enhanced in both lmbrd1 knockdown HCVcc and HCVR system when overexpressing LMBD1 protein. Whether the involvement of LMBD1 in HCV RNA replication is regulated through the interaction between LMBD1 and core protein needs to be further investigated. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T13:30:44Z (GMT). No. of bitstreams: 1 ntu-105-R02445112-1.pdf: 5997558 bytes, checksum: 954644b273bfa4427be4eb2d883ae40e (MD5) Previous issue date: 2016 | en |
| dc.description.tableofcontents | 摘要................................................................................................................................i
Abstract ..........................................................................................................................ii 中英對照表.................................................................................................................. iii 目錄...............................................................................................................................iv 壹、緒論........................................................................................................................1 一、C 型肝炎病毒(Hepatitis C virus,HCV)......................................................1 二、lmbrd1 基因與LMBD1 蛋白質研究探討..................................................13 三、研究目的......................................................................................................15 貳、實驗材料與方法..................................................................................................17 一、實驗材料......................................................................................................17 二、實驗方法......................................................................................................24 參、實驗結果..............................................................................................................36 一、Core 蛋白質與LMBD1 蛋白質具有交互作用.........................................36 二、建立 HCV 細胞培養系統...........................................................................36 三、建立慢病毒轉導之 lmbrd1 基因踢弱系統與過量表現系統....................37 四、細胞中 lmbrd1 基因的踢弱會增強JFH1 病毒基因體RNA 的複製.......38 五、細胞中 lmbrd1 基因的踢弱不影響JFH1 病毒進入細胞的能力.............39 六、細胞中 lmbrd1 基因的踢弱會減弱HCVR 病毒次基因體RNA 的複製.40 七、外送 LMBD1 蛋白質表現質體可增強細胞中HCV 基因體的複製........40 肆、討論......................................................................................................................41 伍、圖表......................................................................................................................45 陸、參考文獻..............................................................................................................56 附錄..............................................................................................................................63 | |
| dc.language.iso | zh-TW | |
| dc.subject | core 蛋白質 | zh_TW |
| dc.subject | C 型肝炎病毒 | zh_TW |
| dc.subject | LMBD1 蛋白質 | zh_TW |
| dc.subject | 病毒基因體複製 | zh_TW |
| dc.subject | C 型肝炎病毒 | zh_TW |
| dc.subject | core 蛋白質 | zh_TW |
| dc.subject | LMBD1 蛋白質 | zh_TW |
| dc.subject | 病毒基因體複製 | zh_TW |
| dc.subject | core protein | en |
| dc.subject | Hepatitis C virus | en |
| dc.subject | viral genome replication | en |
| dc.subject | LMBD1 protein | en |
| dc.subject | Hepatitis C virus | en |
| dc.subject | core protein | en |
| dc.subject | LMBD1 protein | en |
| dc.subject | viral genome replication | en |
| dc.title | LMBD1蛋白質對C型肝炎病毒RNA複製的調節作用 | zh_TW |
| dc.title | Cellular Protein LMBD1 Regulates RNA Replication of Hepatitis C Virus | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 104-1 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 陳美如(Mei-Ru Chen),楊宏志(Hung-Chih Yang),史有伶(Yu-Ling Shih) | |
| dc.subject.keyword | C 型肝炎病毒,core 蛋白質,LMBD1 蛋白質,病毒基因體複製, | zh_TW |
| dc.subject.keyword | Hepatitis C virus,core protein,LMBD1 protein,viral genome replication, | en |
| dc.relation.page | 69 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2016-02-03 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 微生物學研究所 | zh_TW |
| Appears in Collections: | 微生物學科所 | |
Files in This Item:
| File | Size | Format | |
|---|---|---|---|
| ntu-105-1.pdf Restricted Access | 5.86 MB | Adobe PDF |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
