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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/82280完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 詹世鵬(Shih-Peng Chan) | |
| dc.contributor.author | Yi-Wen Chen | en |
| dc.contributor.author | 陳怡妏 | zh_TW |
| dc.date.accessioned | 2022-11-25T06:34:55Z | - |
| dc.date.copyright | 2021-11-09 | |
| dc.date.issued | 2021 | |
| dc.date.submitted | 2021-09-28 | |
| dc.identifier.citation | Geuens, T., D. Bouhy, and V. Timmerman, The hnRNP family: insights into their role in health and disease. Hum Genet, 2016. 135(8): p. 851-67. Dreyfuss, G., et al., hnRNP proteins and the biogenesis of mRNA. Annu Rev Biochem, 1993. 62: p. 289-321. Krecic, A.M. and M.S. Swanson, hnRNP complexes: composition, structure, and function. Curr Opin Cell Biol, 1999. 11(3): p. 363-71. Dreyfuss, G., L. Philipson, and I.W. Mattaj, Ribonucleoprotein particles in cellular processes. J Cell Biol, 1988. 106(5): p. 1419-25. Gorlach, M., et al., Interaction of the RNA-binding domain of the hnRNP C proteins with RNA. EMBO J, 1992. 11(9): p. 3289-95. Kiledjian, M. and G. Dreyfuss, Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box. EMBO J, 1992. 11(7): p. 2655-64. Cartegni, L., et al., hnRNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins. J Mol Biol, 1996. 259(3): p. 337-48. Siomi, H., et al., The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res, 1993. 21(5): p. 1193-8. Jensen, K.B., et al., Nova-1 regulates neuron-specific alternative splicing and is essential for neuronal viability. Neuron, 2000. 25(2): p. 359-71. Dreyfuss, G., V.N. Kim, and N. Kataoka, Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol, 2002. 3(3): p. 195-205. Mayeda, A. and A.R. Krainer, Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell, 1992. 68(2): p. 365-75. Gamarnik, A.V. and R. Andino, Two functional complexes formed by KH domain containing proteins with the 5' noncoding region of poliovirus RNA. RNA, 1997. 3(8): p. 882-92. Meng, Q., et al., Signaling-dependent and coordinated regulation of transcription, splicing, and translation resides in a single coregulator, PCBP1. Proc Natl Acad Sci U S A, 2007. 104(14): p. 5866-71. Zhang, T., et al., PCBP-1 regulates alternative splicing of the CD44 gene and inhibits invasion in human hepatoma cell line HepG2 cells. Mol Cancer, 2010. 9: p. 72. Jean-Philippe, J., S. Paz, and M. Caputi, hnRNP A1: the Swiss army knife of gene expression. Int J Mol Sci, 2013. 14(9): p. 18999-9024. Liu, X., et al., Knockdown of HNRNPA1 inhibits lung adenocarcinoma cell proliferation through cell cycle arrest at G0/G1 phase. Gene, 2016. 576(2 Pt 2): p. 791-7. Loh, T.J., et al., CD44 alternative splicing and hnRNP A1 expression are associated with the metastasis of breast cancer. Oncol Rep, 2015. 34(3): p. 1231-8. Anantha, R.W., et al., Requirement of heterogeneous nuclear ribonucleoprotein C for BRCA gene expression and homologous recombination. PLoS One, 2013. 8(4): p. e61368. Waggoner, S.A., G.J. Johannes, and S.A. Liebhaber, Depletion of the poly(C)-binding proteins alphaCP1 and alphaCP2 from K562 cells leads to p53-independent induction of cyclin-dependent kinase inhibitor (CDKN1A) and G1 arrest. J Biol Chem, 2009. 284(14): p. 9039-49. Chaudhury, A., et al., TGF-beta-mediated phosphorylation of hnRNP E1 induces EMT via transcript-selective translational induction of Dab2 and ILEI. Nat Cell Biol, 2010. 12(3): p. 286-93. Hussey, G.S., et al., Identification of an mRNP complex regulating tumorigenesis at the translational elongation step. Mol Cell, 2011. 41(4): p. 419-31. Gautrey, H., et al., SRSF3 and hnRNP H1 regulate a splicing hotspot of HER2 in breast cancer cells. RNA Biol, 2015. 12(10): p. 1139-51. Bekenstein, U. and H. Soreq, Heterogeneous nuclear ribonucleoprotein A1 in health and neurodegenerative disease: from structural insights to post-transcriptional regulatory roles. Mol Cell Neurosci, 2013. 56: p. 436-46. Mohagheghi, F., et al., TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor. Hum Mol Genet, 2016. 25(3): p. 534-45. Cooper-Knock, J., et al., Antisense RNA foci in the motor neurons of C9ORF72-ALS patients are associated with TDP-43 proteinopathy. Acta Neuropathol, 2015. 130(1): p. 63-75. Kashima, T., et al., hnRNP A1 functions with specificity in repression of SMN2 exon 7 splicing. Hum Mol Genet, 2007. 16(24): p. 3149-59. Chen, H.H., et al., The RNA binding protein hnRNP Q modulates the utilization of exon 7 in the survival motor neuron 2 (SMN2) gene. Mol Cell Biol, 2008. 28(22): p. 6929-38. Cho, S., et al., hnRNP M facilitates exon 7 inclusion of SMN2 pre-mRNA in spinal muscular atrophy by targeting an enhancer on exon 7. Biochim Biophys Acta, 2014. 1839(4): p. 306-15. Dombert, B., et al., Presynaptic localization of Smn and hnRNP R in axon terminals of embryonic and postnatal mouse motoneurons. PLoS One, 2014. 9(10): p. e110846. Moursy, A., F.H. Allain, and A. Clery, Characterization of the RNA recognition mode of hnRNP G extends its role in SMN2 splicing regulation. Nucleic Acids Res, 2014. 42(10): p. 6659-72. Borreca, A., et al., Opposite Dysregulation of Fragile-X Mental Retardation Protein and Heteronuclear Ribonucleoprotein C Protein Associates with Enhanced APP Translation in Alzheimer Disease. Mol Neurobiol, 2016. 53(5): p. 3227-3234. Mizutani, A., et al., SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms. J Biol Chem, 2000. 275(13): p. 9823-31. Mourelatos, Z., et al., SMN interacts with a novel family of hnRNP and spliceosomal proteins. EMBO J, 2001. 20(19): p. 5443-52. Grosset, C., et al., A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell, 2000. 103(1): p. 29-40. Kim, J.H., et al., A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon. Mol Cell Biol, 2004. 24(18): p. 7878-90. Xing, L., et al., Negative regulation of RhoA translation and signaling by hnRNP-Q1 affects cellular morphogenesis. Mol Biol Cell, 2012. 23(8): p. 1500-9. Williams, K.R., et al., hnRNP-Q1 represses nascent axon growth in cortical neurons by inhibiting Gap-43 mRNA translation. Mol Biol Cell, 2016. 27(3): p. 518-34. Lorson, C.L. and E.J. Androphy, An exonic enhancer is required for inclusion of an essential exon in the SMA-determining gene SMN. Hum Mol Genet, 2000. 9(2): p. 259-65. Lorson, C.L., et al., SMN oligomerization defect correlates with spinal muscular atrophy severity. Nat Genet, 1998. 19(1): p. 63-6. Wirth, B., et al., Mildly affected patients with spinal muscular atrophy are partially protected by an increased SMN2 copy number. Hum Genet, 2006. 119(4): p. 422-8. Vu, L.P., et al., Functional screen of MSI2 interactors identifies an essential role for SYNCRIP in myeloid leukemia stem cells. Nat Genet, 2017. 49(6): p. 866-875. Santangelo, L., et al., The RNA-Binding Protein SYNCRIP Is a Component of the Hepatocyte Exosomal Machinery Controlling MicroRNA Sorting. Cell Rep, 2016. 17(3): p. 799-808. Hobor, F., et al., A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets. Nat Commun, 2018. 9(1): p. 831. Chen, Y., et al., SYNCRIP, a new player in pri-let-7a processing. RNA, 2020. 26(3): p. 290-305. Ha, M. and V.N. Kim, Regulation of microRNA biogenesis. Nat Rev Mol Cell Biol, 2014. 15(8): p. 509-24. Denli, A.M., et al., Processing of primary microRNAs by the Microprocessor complex. Nature, 2004. 432(7014): p. 231-5. Okada, C., et al., A high-resolution structure of the pre-microRNA nuclear export machinery. Science, 2009. 326(5957): p. 1275-9. Zhang, H., et al., Single processing center models for human Dicer and bacterial RNase III. Cell, 2004. 118(1): p. 57-68. Yoda, M., et al., ATP-dependent human RISC assembly pathways. Nat Struct Mol Biol, 2010. 17(1): p. 17-23. Huntzinger, E. and E. Izaurralde, Gene silencing by microRNAs: contributions of translational repression and mRNA decay. Nat Rev Genet, 2011. 12(2): p. 99-110. Ipsaro, J.J. and L. Joshua-Tor, From guide to target: molecular insights into eukaryotic RNA-interference machinery. Nat Struct Mol Biol, 2015. 22(1): p. 20-8. Reinhart, B.J., et al., The 21-nucleotide let-7 RNA regulates developmental timing in Caenorhabditis elegans. Nature, 2000. 403(6772): p. 901-6. Pasquinelli, A.E., et al., Conservation of the sequence and temporal expression of let-7 heterochronic regulatory RNA. Nature, 2000. 408(6808): p. 86-9. Lee, H., et al., Biogenesis and regulation of the let-7 miRNAs and their functional implications. Protein Cell, 2016. 7(2): p. 100-13. Grosshans, H., et al., The temporal patterning microRNA let-7 regulates several transcription factors at the larval to adult transition in C. elegans. Dev Cell, 2005. 8(3): p. 321-30. Takamizawa, J., et al., Reduced expression of the let-7 microRNAs in human lung cancers in association with shortened postoperative survival. Cancer Res, 2004. 64(11): p. 3753-6. Boyerinas, B., et al., The role of let-7 in cell differentiation and cancer. Endocr Relat Cancer, 2010. 17(1): p. F19-36. Johnson, S.M., et al., RAS is regulated by the let-7 microRNA family. Cell, 2005. 120(5): p. 635-47. Kumar, M.S., et al., Suppression of non-small cell lung tumor development by the let-7 microRNA family. Proc Natl Acad Sci U S A, 2008. 105(10): p. 3903-8. Wulczyn, F.G., et al., Post-transcriptional regulation of the let-7 microRNA during neural cell specification. FASEB J, 2007. 21(2): p. 415-26. Schulman, B.R., A. Esquela-Kerscher, and F.J. Slack, Reciprocal expression of lin-41 and the microRNAs let-7 and mir-125 during mouse embryogenesis. Dev Dyn, 2005. 234(4): p. 1046-54. Hammell, C.M., X. Karp, and V. Ambros, A feedback circuit involving let-7-family miRNAs and DAF-12 integrates environmental signals and developmental timing in Caenorhabditis elegans. Proc Natl Acad Sci U S A, 2009. 106(44): p. 18668-73. Sampson, V.B., et al., MicroRNA let-7a down-regulates MYC and reverts MYC-induced growth in Burkitt lymphoma cells. Cancer Res, 2007. 67(20): p. 9762-70. Thornton, J.E., et al., Lin28-mediated control of let-7 microRNA expression by alternative TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7). RNA, 2012. 18(10): p. 1875-85. Nam, Y., et al., Molecular basis for interaction of let-7 microRNAs with Lin28. Cell, 2011. 147(5): p. 1080-91. Rybak, A., et al., A feedback loop comprising lin-28 and let-7 controls pre-let-7 maturation during neural stem-cell commitment. Nat Cell Biol, 2008. 10(8): p. 987-93. Newman, M.A., J.M. Thomson, and S.M. Hammond, Lin-28 interaction with the Let-7 precursor loop mediates regulated microRNA processing. RNA, 2008. 14(8): p. 1539-49. Viswanathan, S.R., G.Q. Daley, and R.I. Gregory, Selective blockade of microRNA processing by Lin28. Science, 2008. 320(5872): p. 97-100. Piskounova, E., et al., Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct mechanisms. Cell, 2011. 147(5): p. 1066-79. Michlewski, G. and J.F. Caceres, Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis. Nat Struct Mol Biol, 2010. 17(8): p. 1011-8. Kaletta, T. and M.O. Hengartner, Finding function in novel targets: C. elegans as a model organism. Nat Rev Drug Discov, 2006. 5(5): p. 387-98. Ambros, V. and H.R. Horvitz, Heterochronic mutants of the nematode Caenorhabditis elegans. Science, 1984. 226(4673): p. 409-16. Sulston, J.E. and H.R. Horvitz, Post-embryonic cell lineages of the nematode, Caenorhabditis elegans. Dev Biol, 1977. 56(1): p. 110-56. Moss, E.G., Heterochronic genes and the nature of developmental time. Curr Biol, 2007. 17(11): p. R425-34. Nimmo, R.A. and F.J. Slack, An elegant miRror: microRNAs in stem cells, developmental timing and cancer. Chromosoma, 2009. 118(4): p. 405-18. Thomson, J.M., et al., Extensive post-transcriptional regulation of microRNAs and its implications for cancer. Genes Dev, 2006. 20(16): p. 2202-7. Kinnaird, J.H., et al., HRP-2, a heterogeneous nuclear ribonucleoprotein, is essential for embryogenesis and oogenesis in Caenorhabditis elegans. Exp Cell Res, 2004. 298(2): p. 418-30. Kabat, J.L., S. Barberan-Soler, and A.M. Zahler, HRP-2, the Caenorhabditis elegans homolog of mammalian heterogeneous nuclear ribonucleoproteins Q and R, is an alternative splicing factor that binds to UCUAUC splicing regulatory elements. J Biol Chem, 2009. 284(42): p. 28490-7. Stefani, G., et al., A novel mechanism of LIN-28 regulation of let-7 microRNA expression revealed by in vivo HITS-CLIP in C. elegans. RNA, 2015. 21(5): p. 985-96. Ecsedi, M., M. Rausch, and H. Grosshans, The let-7 microRNA directs vulval development through a single target. Dev Cell, 2015. 32(3): p. 335-44. Bettinger, J.C., K. Lee, and A.E. Rougvie, Stage-specific accumulation of the terminal differentiation factor LIN-29 during Caenorhabditis elegans development. Development, 1996. 122(8): p. 2517-27. Aeschimann, F., et al., LIN41 Post-transcriptionally Silences mRNAs by Two Distinct and Position-Dependent Mechanisms. Mol Cell, 2017. 65(3): p. 476-489 e4. Bird, D.M. and D.L. Riddle, Molecular cloning and sequencing of ama-1, the gene encoding the largest subunit of Caenorhabditis elegans RNA polymerase II. Mol Cell Biol, 1989. 9(10): p. 4119-30. Yang, F.-J., et al., phiC31 integrase for recombination mediated single copy insertion and genome manipulation in C. elegans. 2020, Cold Spring Harbor Laboratory. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/82280 | - |
| dc.description.abstract | 異質性核醣核酸家族是一群參與在許多核醣核酸生合成步驟中的核醣核酸結合蛋白。錯誤調控的異質性核醣核酸已經被證實和癌症及神經退化性疾病相關。其中異質性核醣核酸 Q (hnRNP Q)又被稱為SYNCRIP,而它的突變會參與在脊髓性肌肉萎縮症及急性骨髓性白血病的發生。除此之外,它也會調控微小核醣核酸(microRNA) let-7的成熟。let-7最早是被發現在線蟲中調控發育時間點的異時性基因(heterochronic gene)。它屬於非編碼核醣核酸(non-coding RNA)且在各物種間具有高度的保留性。在人類中,低表現的let-7和癌症的發生息息相關。而在線蟲中let-7 (n2853)的突變也會造成let-7表現量下降,並且會造成線蟲的外陰爆裂(vulva bursting)以及接縫細胞(seam cell)無法在成蟲時完成最終分化而持續分裂,這也類似於癌細胞的分裂。let-7會被許多不同的蛋白調控,像是LIN-28以及異質性核醣核酸。在先前的實驗中發現在人類細胞株中,LIN-28和hnRNP Q有交互作用且降低hnRNP Q的表現能夠使let-7的表現量提升。由於let-7和LIN-28在物種間都具有高度的保留性,而且hnRNP Q在線蟲中也有同源蛋白HRPR-1,因此我們實驗室以線蟲作為模式生物來探討HRPR-1可能參與let-7和LIN-28的調節機制。我們實驗室先前觀察到,利用核醣核酸干擾(RNAi)的方式降低線蟲HRPR-1表現量可以抑制let-7(n2853)突變所造成的接縫細胞意外分裂的情形。因此我們想要觀察降低線蟲HRPR-1表現量是否可以抑制其他let-7(n2853)突變所造成的表現,並且探討HRPR-1在異時性路徑中所扮演的角色。 在本篇研究中我們觀察到降低線蟲HRPR-1表現可以抑制let-7(n2853)突變的線蟲外陰爆裂的現象進而轉變為外陰突出的現象,然而接縫細胞意外分裂的情形並不會受到影響。取而代之的是我們發現降低線蟲HRPR-1表現會使線蟲在第四幼蟲期(L4)發育到成蟲的過程發生遲滯,並且會使線蟲的性腺發育受到抑制。除此之外我們觀察到HRPR-1的降低並不會影響到let-7在異時性路徑的下游蛋白LIN-29。我們也發現在線蟲中HRPR-1並不會直接和LIN-28有交互作用,而這也顯示LIN-28和hnRNP Q的交互作用可能沒有在物種間被保留。然而有趣的是我們發現基於HRPR-1在胚胎及第一期幼蟲(L1)的表現量特別高,他可能是一個異時性基因且他表現的時間比LIN-28早一個階段。然而他在異時性路徑中所扮演的角色仍然是未知的且需要更多的研究來探討。 | zh_TW |
| dc.description.provenance | Made available in DSpace on 2022-11-25T06:34:55Z (GMT). No. of bitstreams: 1 U0001-2709202121021800.pdf: 11159176 bytes, checksum: 9f37eadacef01e818b1814d36936cc3e (MD5) Previous issue date: 2021 | en |
| dc.description.tableofcontents | "口試委員會審定書 I 誌謝 II 中文摘要 III ABSTRACT V CONTENTS VII Chapter 1 Introduction 1 1.1 Heterogeneous nuclear protein (hnRNP) 1 1.1.1 The heterogeneous nuclear protein (hnRNP) family 1 1.1.2 The functions and related diseases of hnRNPs 2 1.2 hnRNP Q 3 1.3 microRNA (miRNA) 4 1.3.1 The biogenesis and functions of miRNAs 4 1.3.2 let-7 miRNA 5 1.3.3 Regulation of let-7 biogenesis 6 1.4 The model organism – Caenorhabditis elegans 7 1.4.1 The advantages of using C. elegans as an animal model 7 1.4.2 The heterochronic pathway in C. elegans 8 1.5 HRPR-1 in C. elegans 9 1.5.1 The relationship between HRPR-1 and let-7 9 1.5.2 The structure and function of HRPR-1 10 1.6 Project aim 10 Chapter2 Materials and Methods 11 2.1 Nematode strains and culture condition 11 2.2 Solid medium culture method 12 2.2.1 Synchronization 12 2.2.2 Collect L1, L2, L3, L4, young adult, adult worms 12 2.3 RNA Interference (RNAi) 13 2.3.1 RNAi clone preparation 13 2.3.2 Feeding RNAi 14 2.4 Bursting assay 15 2.5 Nematode total protein extraction 15 2.5.1 For western blot 15 2.5.2 For immunoprecipitation 16 2.6 Immunoprecipitation 17 2.7 Protein gel electrophoresis 17 2.8 Western blotting 18 2.9 microinjection 19 2.9.1 phiC31 lin-41 promotor series worms 19 Chapter 3 Results 21 3.1 Knockdown HRPR-1 rescues the vulva bursting of let-7 mutant worms but causes vulva protruding 21 3.2 The seam cell lineage of let-7(n2853) worms is not rescued by knocking down HRPR-1 21 3.3 Knockdown HRPR-1 doesn’t affect LIN-29 expression 23 3.4 HRPR-1 does not interact directly with LIN-28 24 3.5 Relationship between HRPR-1 and let-7/LIN-41 pathway 26 Chapter 4 Discussion 28 4.1 HRPR-1 affects the morphology of the vulva and gonad rather than seam cell lineage 28 4.2 HRPR-1 might be critical for juvenile-to-adult switch 29 4.3 Investigate the relationship between LIN-41 and let-7/LIN-41 pathway through dual color reporter worms 29 4.4 The relationship between HRPR-1 and LIN-28 30 4.5 Prospective directions of HRPR-1 research 31 Chapter 5 Figures 33 Figure 1. The vulva bursting rate of hrpr-1 RNAi 33 Figure 2. The seam cell development of hrpr-1 RNAi in let-7(n2853) worms 37 Figure 3. The LIN-29A expression of HW1826 worms’ seam cells 39 Figure 4. The LIN-29B expression of HW1835 worms’ seam cells 42 Figure 5. The expression of LIN-29A in let-7(n2853) worms’ seam cells 44 Figure 6. The expression of LIN-28 in SPN054 worms 47 Figure 7. The correlation between LIN-28 and HRPR-1 49 Figure 8. The PhiC31 dual color reporter system 52 Figure 9. The images of 7LW/7LWA/8LW plasmid integrated worms 55 Chapter 6 References 56 Chapter 7 Appendix 62 Appendix Figure 1. The heterogeneous nuclear protein (hnRNP) family 62 Appendix Figure 2. The let-7 pathway and let-7(n2853) mutation 63 Appendix Figure 3. The construct of hrpr-1 CDS RNAi clone 65 Appendix Figure 4. The let-7/LIN-41 pathway in seam cells 67 Table 1 68 Table 2 68 Table 3 69 Table 4 69 Table 5 69 Table 6 69" | |
| dc.language.iso | en | |
| dc.subject | 異質性核醣核酸蛋白 | zh_TW |
| dc.subject | SYNCRIP | zh_TW |
| dc.subject | HRPR-1 | zh_TW |
| dc.subject | LIN-28 | zh_TW |
| dc.subject | let-7 微小核醣核酸 | zh_TW |
| dc.subject | Heterogeneous nuclear protein | en |
| dc.subject | HRPR-1 | en |
| dc.subject | LIN-28 | en |
| dc.subject | let-7 miRNA | en |
| dc.subject | SYNCRIP | en |
| dc.title | 探討人類hnRNP Q/R同源蛋白HRPR-1對於線蟲發育的影響 | zh_TW |
| dc.title | "Investigate the influence of human hnRNP Q/R homolog, HRPR-1, in C. elegans development" | en |
| dc.date.schoolyear | 109-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 顏伯勳(Hsin-Tsai Liu),歐展言(Chih-Yang Tseng) | |
| dc.subject.keyword | 異質性核醣核酸蛋白,SYNCRIP,let-7 微小核醣核酸,LIN-28,HRPR-1, | zh_TW |
| dc.subject.keyword | Heterogeneous nuclear protein,SYNCRIP,let-7 miRNA,LIN-28,HRPR-1, | en |
| dc.relation.page | 71 | |
| dc.identifier.doi | 10.6342/NTU202103415 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2021-09-29 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 微生物學研究所 | zh_TW |
| dc.date.embargo-lift | 2026-09-28 | - |
| 顯示於系所單位: | 微生物學科所 | |
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