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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43906完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 陳佩燁(Rita Pei-Yeh Chen) | |
| dc.contributor.author | Chung-Yu Lee | en |
| dc.contributor.author | 李忠諭 | zh_TW |
| dc.date.accessioned | 2021-06-15T02:32:20Z | - |
| dc.date.available | 2012-08-21 | |
| dc.date.copyright | 2009-08-21 | |
| dc.date.issued | 2009 | |
| dc.date.submitted | 2009-08-14 | |
| dc.identifier.citation | Aguzzi, A., and Polymenidou, M. (2004) Mammalian prion biology: one century of evolving concepts. Cell 116, 313-327.
Alper, T., Cramp, W. A., Haig, D. A., and Clarke, M. C. (1967) Does the agent of scrapie replicate without nucleic acid? Nature 214, 764-766. Anfinsen, C. B. (1973) Principles that govern the folding of protein chains. Science 181, 223-230. Basler, K., Oesch, B., Scott, M., Westaway, D., Walchli, M., Groth, D. F., McKinley, M. P., Prusiner, S. B., and Weissmann, C. (1986) Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46, 417-428. Bocharova, O. V., Breydo, L., Parfenov, A. S., Salnikov, V. V., and Baskakov, I. V. (2005) In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). J Mol Biol 346, 645-659. Bolton, D. C., McKinley, M. P., and Prusiner, S. B. (1982) Identification of a protein that purifies with the scrapie prion. Science 218, 1309-1311. Bruce, M. E., Will, R. G., Ironside, J. W., McConnell, I., Drummond, D., Suttie, A., McCardle, L., Chree, A., Hope, J., Birkett, C., Cousens, S., Fraser, H., and Bostock, C. J. (1997) Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature 389, 498-501. Caughey, B. W., Dong, A., Bhat, K. S., Ernst, D., Hayes, S. F., and Caughey, W. S. (1991) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30, 7672-7680. Chabry, J., Caughey, B., and Chesebro, B. (1998) Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides. J Biol Chem 273, 13203-13207. Chen, P. Y., Lin, C. C., Chang, Y. T., Lin, S. C., and Chan, S. I. (2002) One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide. Proc Natl Acad Sci U S A 99, 12633-12638. Chesebro, B. (2003) Introduction to the transmissible spongiform encephalopathies or prion diseases. Br Med Bull 66, 1-20. Collinge, J. (2001) Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 24, 519-550. DeArmond, S. J., McKinley, M. P., Barry, R. A., Braunfeld, M. B., McColloch, J. R., and Prusiner, S. B. (1985) Identification of prion amyloid filaments in scrapie-infected brain. Cell 41, 221-235. Dobson, C. M. (2004) Principles of protein folding, misfolding and aggregation, Semin Cell Dev Biol 15. 3-16. Donne, D. G., Viles, J. H., Groth, D., Mehlhorn, I., James, T. L., Cohen, F. E., Prusiner, S. B., Wright, P. E., and Dyson, H. J. (1997) Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible, Proc Natl Acad Sci U S A 94, 13452-13457. Ermonval, M., Mouillet-Richard, S., Codogno, P., Kellermann, O., and Botti, J. (2003) Evolving views in prion glycosylation: functional and pathological implications. Biochimie 85, 33-45. Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O., and Tagliavini, F. (1993) Neurotoxicity of a prion protein fragment. Nature 362, 543-546. Gabizon, R., McKinley, M. P., Groth, D., and Prusiner, S. B. (1988) Immunoaffinity purification and neutralization of scrapie prion infectivity. Proc Natl Acad Sci U S A 85, 6617-6621. Griffith, J. S. (1967) Self-replication and scrapie. Nature 215, 1043-1044. Harper, J. D., and Lansbury, P. T., Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66, 385-407. Hill, A. F., Desbruslais, M., Joiner, S., Sidle, K. C., Gowland, I., Collinge, J., Doey, L. J., and Lantos, P. (1997) The same prion strain causes vCJD and BSE. Nature 389, 448-450, 526. Ho, C. C., Lee, L. Y., Huang, K. T., Lin, C. C., Ku, M. Y., Yang, C. C., Chan, S. I., Hsu, R. L., and Chen, R. P. (2009) Tuning the conformational properties of the prion peptide. Proteins 76, 213-225. Huang, Z., Prusiner, S. B., and Cohen, F. E. (1995) Scrapie prions: a three-dimensional model of an infectious fragment. Fold Des 1, 13-19. Jahn, T. R., and Radford, S. E. (2005) The Yin and Yang of protein folding. FEBS J 272, 5962-5970. Kaneko, K., Peretz, D., Pan, K. M., Blochberger, T. C., Wille, H., Gabizon, R., Griffith, O. H., Cohen, F. E., Baldwin, M. A., and Prusiner, S. B. (1995) Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform. Proc Natl Acad Sci U S A 92, 11160-11164. Kitamoto, T., Tateishi, J., Tashima, T., Takeshita, I., Barry, R. A., DeArmond, S. J., and Prusiner, S. B. (1986) Amyloid plaques in Creutzfeldt-Jakob disease stain with prion protein antibodies. Ann Neurol 20, 204-208. Knight, R. (2003) Variant CJD: the present position and future possibilities. Int J Pediatr Otorhinolaryngol 67 Suppl 1, S81-84. Kocisko, D. A., Priola, S. A., Raymond, G. J., Chesebro, B., Lansbury, P. T., Jr., and Caughey, B. (1995) Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. Proc Natl Acad Sci U S A 92, 3923-3927. Krebs, M. R., Bromley, E. H., and Donald, A. M. (2005) The binding of thioflavin-T to amyloid fibrils: localisation and implications. J Struct Biol 149, 30-37. Kretzschmar, H. A., Prusiner, S. B., Stowring, L. E., and DeArmond, S. J. (1986b) Scrapie prion proteins are synthesized in neurons. Am J Pathol 122, 1-5. Kretzschmar, H. A., Stowring, L. E., Westaway, D., Stubblebine, W. H., Prusiner, S. B., and Dearmond, S. J. (1986a) Molecular cloning of a human prion protein cDNA. DNA 5, 315-324. Kundu, B., Maiti, N. R., Jones, E. M., Surewicz, K. A., Vanik, D. L., and Surewicz, W. K. (2003) Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation. Proc Natl Acad Sci U S A 100, 12069-12074. Kyle, R. A. (2001) Amyloidosis: a convoluted story. Br J Haematol 114, 529-538. Langeveld, J. P., Wang, J. J., Van de Wiel, D. F., Shih, G. C., Garssen, G. J., Bossers, A., and Shih, J. C. (2003) Enzymatic degradation of prion protein in brain stem from infected cattle and sheep. J Infect Dis 188, 1782-1789. LeVine, H., 3rd. (1999) Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol 309, 274-284. Liang, F. C., Chen, R. P., Lin, C. C., Huang, K. T., and Chan, S. I. (2006) Tuning the conformation properties of a peptide by glycosylation and phosphorylation. Biochem Biophys Res Commun 342, 482-488. McKintosh, E., Tabrizi, S. J., and Collinge, J. (2003) Prion diseases. J Neurovirol 9, 183-193. Meyer, R. K., McKinley, M. P., Bowman, K. A., Braunfeld, M. B., Barry, R. A., and Prusiner, S. B. (1986) Separation and properties of cellular and scrapie prion proteins. Proc Natl Acad Sci U S A 83, 2310-2314. Muramoto, T., Scott, M., Cohen, F. E., and Prusiner, S. B. (1996) Recombinant scrapie-like prion protein of 106 amino acids is soluble. Proc Natl Acad Sci U S A 93, 15457-15462. Oesch, B., Westaway, D., Walchli, M., McKinley, M. P., Kent, S. B., Aebersold, R., Barry, R. A., Tempst, P., Teplow, D. B., Hood, L. E., and et al. (1985) A cellular gene encodes scrapie PrP 27-30 protein. Cell 40, 735-746. Pan, K. M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., Cohen, F. E., and et al. (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci U S A 90, 10962-10966. Paravastu, A. K., Leapman, R. D., Yau, W. M., and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci U S A 105, 18349-18354. Peretz, D., Williamson, R. A., Kaneko, K., Vergara, J., Leclerc, E., Schmitt-Ulms, G., Mehlhorn, I. R., Legname, G., Wormald, M. R., Rudd, P. M., Dwek, R. A., Burton, D. R., and Prusiner, S. B. (2001) Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412, 739-743. Priola, S. A., Caughey, B., Wehrly, K., and Chesebro, B. (1995) A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP. J Biol Chem 270, 3299-3305. Priola, S. A., and Chesebro, B. (1995) A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. J Virol 69, 7754-7758. Prusiner, S. B. (1991) Molecular biology of prion diseases. Science 252, 1515-1522. Prusiner, S. B. (1998) Prions. Proc Natl Acad Sci U S A 95, 13363-13383. Prusiner, S. B., Bolton, D. C., Groth, D. F., Bowman, K. A., Cochran, S. P., and McKinley, M. P. (1982) Further purification and characterization of scrapie prions. Biochemistry 21, 6942-6950. Prusiner, S. B., and DeArmond, S. J. (1990) Prion diseases of the central nervous system. Monogr Pathol, 86-122. Prusiner, S. B., Groth, D. F., Bolton, D. C., Kent, S. B., and Hood, L. E. (1984) Purification and structural studies of a major scrapie prion protein. Cell 38, 127-134. Prusiner, S. B., McKinley, M. P., Bowman, K. A., Bolton, D. C., Bendheim, P. E., Groth, D. F., and Glenner, G. G. (1983) Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35, 349-358. Prusiner, S. B., Scott, M., Foster, D., Pan, K. M., Groth, D., Mirenda, C., Torchia, M., Yang, S. L., Serban, D., Carlson, G. A., and et al. (1990) Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63, 673-686. Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., and Wuthrich, K. (1996) NMR structure of the mouse prion protein domain PrP(121-321). Nature 382, 180-182. Riek, R., Hornemann, S., Wider, G., Glockshuber, R., and Wuthrich, K. (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 413, 282-288. Rogers, M., Yehiely, F., Scott, M., and Prusiner, S. B. (1993) Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc Natl Acad Sci U S A 90, 3182-3186. Saborio, G. P., Permanne, B., and Soto, C. (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding, Nature 411, 810-813. Salemme, F. R. (1983) Structural properties of protein beta-sheets. Prog Biophys Mol Biol 42, 95-133. Schatzl, H. M., Da Costa, M., Taylor, L., Cohen, F. E., and Prusiner, S. B. (1995) Prion protein gene variation among primates. J Mol Biol 245, 362-374. Scott, M., Foster, D., Mirenda, C., Serban, D., Coufal, F., Walchli, M., Torchia, M., Groth, D., Carlson, G., DeArmond, S. J., and et al. (1989) Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 59, 847-857. Scott, M. R., Will, R., Ironside, J., Nguyen, H. O., Tremblay, P., DeArmond, S. J., and Prusiner, S. B. (1999) Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans. Proc Natl Acad Sci U S A 96, 15137-15142. Sipe, J. D., and Cohen, A. S. (2000) Review: history of the amyloid fibril. J Struct Biol 130, 88-98. Sreerama, N., and Woody, R. W. (2004) Computation and analysis of protein circular dichroism spectra. Methods Enzymol 383, 318-351. Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., and Prusiner, S. B. (1993) Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32, 1991-2002. Stahl, N., Borchelt, D. R., Hsiao, K., and Prusiner, S. B. (1987) Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229-240. Stefani, M., and Dobson, C. M. (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81, 678-699. Tagliavini, F., Prelli, F., Verga, L., Giaccone, G., Sarma, R., Gorevic, P., Ghetti, B., Passerini, F., Ghibaudi, E., Forloni, G., and et al. (1993) Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro. Proc Natl Acad Sci U S A 90, 9678-9682. Trevitt, C. R., and Singh, P. N. (2003) Variant Creutzfeldt-Jakob disease: pathology, epidemiology, and public health implications. Am J Clin Nutr 78, 651S-656S. Weissmann, C. (2004) The state of the prion. Nat Rev Microbiol 2, 861-871. White, A. R., Enever, P., Tayebi, M., Mushens, R., Linehan, J., Brandner, S., Anstee, D., Collinge, J., and Hawke, S. (2003) Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422, 80-83. Will, R. G., Ironside, J. W., Zeidler, M., Cousens, S. N., Estibeiro, K., Alperovitch, A., Poser, S., Pocchiari, M., Hofman, A., and Smith, P. G. (1996) A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347, 921-925. Wille, H., Michelitsch, M. D., Guenebaut, V., Supattapone, S., Serban, A., Cohen, F. E., Agard, D. A., and Prusiner, S. B. (2002) Structural studies of the scrapie prion protein by electron crystallography. Proc Natl Acad Sci U S A 99, 3563-3568. Zahn, R., Liu, A., Luhrs, T., Riek, R., von Schroetter, C., Lopez Garcia, F., Billeter, M., Calzolai, L., Wider, G., and Wuthrich, K. (2000) NMR solution structure of the human prion protein. Proc Natl Acad Sci U S A 97, 145-150. Zhang, H., Kaneko, K., Nguyen, J. T., Livshits, T. L., Baldwin, M. A., Cohen, F. E., James, T. L., and Prusiner, S. B. (1995) Conformational transitions in peptides containing two putative alpha-helices of the prion protein. J Mol Biol 250, 514-526. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43906 | - |
| dc.description.abstract | 類澱粉纖維為蛋白質發生錯誤摺疊後並堆疊所產生；當類澱粉纖維於生物個體內形成並累積時，則可能會造成疾病的產生，而這些疾病則被泛稱為類澱粉病變，普昂疾病便屬於其中之一。普昂疾病又稱為傳播性海綿樣腦病變，係因哺乳動物體內之普昂蛋白發生構形變化，由富含 α-螺旋之結構轉為富含 β-摺板之結構後，堆疊累積成類澱粉纖維之結構所致。
為了解普昂蛋白發生構形變化而形成類澱粉纖維的過程以及能夠影響此過程進行之因子，本研究團隊利用大腸桿菌表現出全長小鼠普昂蛋白（簡稱作 mPrP(23-231)）並進行純化以作為研究主角；純化後的 mPrP(23-231) 於試管內進行類澱粉纖維形成之試驗，並以螢光分子 thioflavin T（ThT）與類澱粉纖維結合後之螢光放射行為觀察其類澱粉纖維之形成動力學。在輕度變性及劇烈震盪環境下，mPrP(23-231) 在經過約一天的遲滯期後，能夠自發地形成類澱粉纖維；若於培養環境中加入已形成的普昂類澱粉纖維作為晶種，則類澱粉纖維形成過程中之遲滯期時間有縮短之現象。此外，本研究團隊亦使用化學合成之小鼠普昂胜肽片段 108-144（簡稱作 mPrP(108-144)），配合 mPrP(23-231) 進行交叉引晶之試驗，結果發現由 mPrP(23-231) 所形成之類澱粉纖維可作為晶種加速 mPrP(108-144) 單體之類澱粉纖維形成，而當二者角色對調時，亦可得到相同的結果，隱含著二者在形成類澱粉纖維時，皆是以序列 108-144 堆疊成為纖維主體之資訊。 而為了探討 mPrP(23-231) 與 mPrP(108-144) 所形成之類澱粉纖維在於其核心結構以及外在形態上之異同，則分別使用到 ThT 進行其與類澱粉纖維複合物之螢光壽命測定以及穿透式電子顯微鏡觀察；二者皆在以上試驗中具有相似之結果，顯示出 mPrP(23-231) 與 mPrP(108-144) 在形成類澱粉之纖維過程具有相同之核心結構，且形成之序列即在 108-144 之中。 | zh_TW |
| dc.description.abstract | Amyloids are aggregates of misfolded proteins. Many diseases are caused by amyloids accumulation. The prion disease, also called transmissible spongiform encephalopathy (TSE), is caused by conformational change of host-encoded prion protein to a β-sheet-rich conformer. When prion protein changes its conformation, it will aggregate and form fibril-like structure.
To know how prion protein forms amyloid fibrils and the factors affecting its formation, we expressed full-length mouse prion protein [mPrP(23-231)] in Escherichia coli and purified it. We studied the amyloid fibril formation in vitro by thioflavin T (ThT) fluorescence spectroscopy. In mild denaturing condition with vigorous shaking, mPrP(23-231) forms amyloid fibrils after one-day incubation. Adding pre-formed amyloid fibrils as seeds may shorten the lag time of amyloid fibril formation. In addition, we synthesized mouse prion peptide (mPrP(108-144)) to do cross seeding experiment. Full-length mPrP(23-231) can function as seeds to accelerate the fibril formation of chemically synthetic mPrP(108-144), and vice versa. Amyloid fibrils formed from mPrP(23-231) and mPrP(108-144) with share very similar morphology in TEM and fluorescence lifetime assay using ThT as dye, suggesting that mPrP(23-231) and mPrP(108-144) has the same amyloid core. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T02:32:20Z (GMT). No. of bitstreams: 1 ntu-98-R96B46023-1.pdf: 4845934 bytes, checksum: a762cb75f086a5cf0bf12fcada51dc3d (MD5) Previous issue date: 2009 | en |
| dc.description.tableofcontents | 第一章 緒論
1.1 類澱粉纖維 1 1.2 普昂疾病 3 1.3 普昂蛋白之結構 6 1.4 普昂蛋白之類澱粉纖維形成 9 1.5 普昂蛋白之構型轉變 12 1.6 其他與普昂蛋白及普昂疾病相關之研究 13 1.7 本論文之研究動機 14 第二章 材料與方法 2.1 材料 15 2.1.1 水 15 2.1.2 化學藥品 15 2.1.3 載體 16 2.1.4 菌株 16 2.1.5 培養基 17 2.1.6 酵素 17 2.2 儀器 17 2.2.1 純化、分析用管柱 17 2.2.2 大型儀器 18 2.3 方法 19 2.3.1 全長小鼠普昂蛋白的表現 19 2.3.2 全長小鼠普昂蛋白的純化 19 2.3.2.1 全長小鼠普昂蛋白的粗萃取 19 2.3.2.2 以親和層析對全長小鼠普昂蛋白進行純化 21 2.3.2.3 全長小鼠普昂蛋白雙硫鍵之形成 22 2.3.2.4 以逆相－高效液相層析對全長小鼠普昂蛋白進行純化 22 2.3.3 全長小鼠普昂蛋白的鑑定 23 2.3.3.1 蛋白質電泳 23 2.3.3.2 西方墨點法 25 2.3.3.3 基質輔助雷射脫附游離－時間式飛行質譜分析 26 2.3.4 以胺基酸分析進行全長小鼠普昂蛋白的定量 26 2.3.4.1 樣本蛋白的酸水解 26 2.3.4.2 以胺基酸分析管柱進行樣本蛋白之定量 27 2.3.5 普昂蛋白之類澱粉纖維形成與觀測 28 2.3.5.1 全長小鼠普昂蛋白之類澱粉纖維形成 28 2.3.5.2 以 thioflavin T 之螢光光譜紀錄普昂蛋白類澱粉纖維形成 28 2.3.5.3 以圓二色光譜紀錄普昂蛋白之類澱粉纖維形成 29 2.3.5.4 化學合成小鼠普昂胜肽的類澱粉纖維形成 29 2.3.5.5 普昂類澱粉纖維之晶種製備 30 2.3.5.6 普昂蛋白/普昂胜肽之引晶實驗 30 2.3.5.7 以穿透式電子顯微鏡觀測普昂蛋白類澱粉纖維之形態 30 2.3.5.8 以時間相依單光子探測螢光光譜探討普昂類澱粉纖維之結構 31 第三章 結果與討論（一） 3.1 全長小鼠普昂蛋白之表現 32 3.2 全長小鼠普昂蛋白的純化 32 3.2.1 全長小鼠普昂蛋白的粗萃取 32 3.2.2 以親和層析對全長小鼠普昂蛋白進行純化 34 3.2.3 全長小鼠普昂蛋白雙硫鍵之形成 38 3.2.4 以逆相－高效液相層析對全長小鼠普昂蛋白進行純化 38 3.2.5 全長小鼠普昂蛋白純化之縱觀 39 3.3 全長小鼠普昂蛋白的鑑定 39 3.3.1 西方墨點法 39 3.3.2 基質輔助雷射脫附游離－時間式飛行質譜分析 40 3.4 以胺基酸分析進行全長小鼠普昂蛋白的定量 41 第四章 結果與討論（二） 4.1 全長小鼠普昂蛋白之類澱粉纖維形成 45 4.2 化學合成小鼠普昂胜肽之類澱粉纖維形成 47 4.3 引晶對新類澱粉纖維形成的影響 51 4.4 以 mPrP(23-231) 形成之類澱粉纖維作為晶種對 mPrP(108-144) 之類澱粉纖維形成動力學曲線之影響 53 4.5 以mPrP(108-144) 形成之類澱粉纖維作為晶種對mPrP(23-231) 之類澱粉纖維形成動力學曲線之影響 55 第五章 結果與討論（三） 5.1 以普昂蛋白/胜肽與 thioflavin T 之複合物之螢光壽命探討並比較 類澱粉纖維之構造 57 5.2 以穿透式電子顯微鏡觀測小鼠普昂類澱粉纖維之形態 65 第六章 結論與未來展望 69 參考文獻 72 | |
| dc.language.iso | zh-TW | |
| dc.subject | 類澱粉纖維 | zh_TW |
| dc.subject | 普昂胜肽 | zh_TW |
| dc.subject | 普昂蛋白 | zh_TW |
| dc.subject | prion peptide | en |
| dc.subject | prion protein | en |
| dc.subject | amyloid fibril | en |
| dc.title | 全長小鼠普昂蛋白與短片段小鼠普昂胜肽類澱粉纖維形成之研究 | zh_TW |
| dc.title | The Study of Amyloid Fibril Formation of Full-length Mouse Prion Protein and Short Mouse Prion Peptide | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 97-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 楊健志(Chien-Chih Yang),王勝仕(Sheng-Shih Wang),楊定一(Ding-I Yang),金之彥(Chih-Yen King) | |
| dc.subject.keyword | 普昂蛋白,普昂胜肽,類澱粉纖維, | zh_TW |
| dc.subject.keyword | prion protein,prion peptide,amyloid fibril, | en |
| dc.relation.page | 77 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2009-08-14 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科學研究所 | zh_TW |
| 顯示於系所單位： | 生化科學研究所 | |
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