以微卡計量測細胞膜不同含量膽固醇和神經節苷脂之
PC12細胞與不同型態之類澱粉胜肽作用後的反應熱與其
細胞活性之研究

以作者查詢圖書館館藏

、以作者查詢臺灣博碩士

、以作者查詢全國書目

、勘誤回報

、線上人數：86

、訪客IP：3.21.106.240

姓名

洪士耘(Shih-yun Hung) 查詢紙本館藏

畢業系所

化學工程與材料工程學系

論文名稱

以微卡計量測細胞膜不同含量膽固醇和神經節苷脂之 PC12細胞與不同型態之類澱粉胜肽作用後的反應熱與其細胞活性之研究
(Microcalorimetric and cytotoxic measurements of different cholesterol and ganglioside content plasma membrane PC12 cells exposed to various form of amyloid-beta )

相關論文

★ 類澱粉胜肽聚集行為之電腦模擬	★ 溶解度參數計算及量測於HPLC純化胜肽程序之最佳化研究
★ 利用恆溫滴定微卡計量測蛋白質分子於溶液中之第二維里係數與自我聚集之行為	★ 利用SPRi探討中性DNA探針相較於一般DNA探針在低鹽雜交環境下之優勢
★ 矽奈米線場效電晶體多點之核酸檢測研究	★ 使用不帶電中性核酸探針於矽奈米線場效電晶體檢測去氧核醣核酸與微核醣核酸之研究
★ 運用nDNA 修飾引子於PCR及qPCR平台以提升專一性之研究	★ 設計中性DNA引子及探針以提升PCR與qPCR專一性之研究
★ 使用中性不帶電去氧核醣核酸探針於矽奈米線場效電晶體檢測微核醣核酸之研究	★ 使用不帶電中性核酸探針於原位雜交技術檢測微核醣核酸之研究
★ 設計不帶電中性核酸探針於矽奈米線場效電晶體來改善富含GC鹼基核醣核酸之檢測專一性	★ 合成5’-MeNPOC-2’-deoxynucleoside p-methoxy phosphoramidite以作為應用於原位合成之新穎性中性核苷酸之研究
★ 立體紙基外泌體核酸萃取裝置應用於檢測不同微環境下癌細胞所釋放之外泌體與外泌體微小核醣核酸之表現量	★ 利用抗原結合區段之抗體片段探針於矽奈米線場效電晶體來改善抗原檢測濃度極限之研究
★ 利用表面電漿共振影像儀驗證最適化之抗非專一性吸附場效電晶體表面於血清環境下之免疫測定	★ 使用混合自組裝單層膜於矽奈米線場效電晶體檢測微小核醣核酸之研究

檔案

[Endnote RIS 格式]

[Bibtex 格式]

[相關文章]

[文章引用]

[完整記錄]

[館藏目錄]

[檢視]

[下載]

本電子論文使用權限為同意立即開放。
已達開放權限電子全文僅授權使用者為學術研究之目的，進行個人非營利性質之檢索、閱讀、列印。
請遵守中華民國著作權法之相關規定，切勿任意重製、散佈、改作、轉貼、播送，以免觸法。

摘要(中)

類澱粉蛋白(amyloid-?，A?)被認為是引起阿茲海默症的主因，當A?由單體在細胞膜上聚集成纖維狀結構時就會毒殺細胞，但是A?引起細胞毒性及導致疾病的機制目前還不清楚。近年研究指出，細胞膜上的神經節苷脂?GM1)和膽固醇的含量與A?的貼附和聚集有關。
本研究以恆溫滴定微卡計作為即時熱流量之量測工具，測量細胞膜不同含量膽固醇和神經節苷脂之PC12細胞與不同聚集度之類澱粉蛋白作用後的反應熱，熱流數據計錄從細胞放入恆溫滴定微卡計到注射A?後並反應兩到三天。同時我們也在96孔盤內進行與微卡計內相同條件的實驗，透過這兩個實驗的結合期望能夠了解細胞在類澱粉蛋白的作用下其熱流量與細胞活性的關係。
在96孔盤內的實驗結果顯示在48小時內，降低細胞膜GM1可抑制A?對細胞的毒性；另外降低細胞膜膽固醇也可抑制A?對細胞的毒性，而增加細胞膜膽固醇則會加強A?對細胞的毒性。
將細胞培養在組織培養皿內並改變細胞膜上的膽固醇和GM1的含量後，取下培養皿上細胞放入微卡計內待平衡和細胞貼附後注射入不同聚集度的A??monomer rich, oligomer rich, fiber rich)，結果顯示熱流量與細胞活性及死亡率有高度相關，證明微卡計熱流量可做為細胞狀態的參考，而透過積分注射後之總放熱量並除以死亡細胞數，發現當系統內細胞毒性較強時，單位細胞死亡所放出的熱量會增加。

摘要(英)

?-amyloid(A?) was believed to cause the prime factor of Alzheimer’s disease. The deposition and aggregation of A? on cell membrane led to cytotoxicity. However, the detail mechanism?was still unclear. Recent studies demonstrated that certan components of plasma membrane, ganglioside(GM1) and cholesterol play an influential role in the accumulation of A? on the plasma membranes.
In this study, we applied isothermal titration calorimetry (ITC) as an “on-line” heat probe to identify the living cell systems. We changed the cholesterol and GM1 amount on PC12 cells plasma membrane in vitro and traced the thermodynamic activity of the interaction between A? and different contents plasma membrane PC12 cells by ITC. The heat flux data contained not only metabolic heat of cells but olso other reaction heat between A? and cells. Base on different experiment designs, different forms of A??(monomer rich, oligomer rich and fiber rich) were chosen. All heat flow is recorded by ITC from cell seeding to the end of experiment. We also redo the control experiment in 96 wells as a parallel experiment.
Our results demonstrated that the reduction of cholesterol or GM1 contents on plasma membrane could diminish the A??cytotoxicity?in12, 24 and 48 hours but higher cholesterol content could cause higher cytotoxicity.
The heat flow data from ITC was highly correlated to the MTT reduction and LDH release of parallel experiment. We demonstrated the heat flow from our ITC system could be a good indication of cell viability.
By integrating the total heat dissipation after the injection of A?, the exothermic heat per dead cell enhanced when the system condition was more toxic to cell.

關鍵字(中)

★ 微卡計
★ 細胞膜
★ 細胞毒性
★ 神經節苷脂
★ 膽固醇
★ 類澱粉胜肽
★ 阿茲海默症

關鍵字(英)

★ plasma membrane
★ microcalorimetry
★ cytotoxic
★ ganglioside
★ cholesterol
★ amyloid-beta
★ Alzheimer's disease

論文目次

摘要 Ⅰ
Abstract Ⅱ
圖目錄 Ⅴ
表目錄 Ⅸ
第一章緒論 1
第二章文獻回顧 2
2.1 阿茲海默症（Alzheimer’s Disease，AD） 2
2.2 類澱粉胜肽（b-Amyloid） 7
2.2.1 類澱粉胜肽的聚集 10
2.3 PC-12細胞株 13
2.4 細胞膜上特定成份對類澱粉胜細胞毒性的影響 13
2.4.1 細胞膜上膽固醇（cholesterol）對類澱粉胜肽細胞毒性的影響 14
2.4.2 細胞膜上神經結苷酯（ganglioside，GM1）對類澱粉胜肽毒性的影響 16
2.4.3 細胞膜上膽固醇和神經結苷脂(GM1)與Ab聚集的機制 18
2.5 恆溫滴定微卡計（Isothermal Titration Calorimetry，ITC） 23
2.6以恆溫微卡計做為細胞放熱的偵測器 25
第三章實驗藥品與儀器設備 30
3.1 實驗藥品 30
3.2 實驗設備 31
3.3 實驗方法 32
3.3.1 PC12細胞的培養 32
3.3.2 玻璃片覆蓋聚離胺酸(poly-D-lysine) 32
3.3.3 微卡計系統內的滅菌 33
3.3.4 A?的製備 33
3.3.5 改變細胞膜上膽固醇和GM1含量 37
3.3.5.1 降低細胞膜膽固醇含量 37
3.3.5.2 增加細胞膜膽固醇含量 37
3.3.5.3減少細胞膜GM1含量 37
3.3.6 細胞活性測試（MTT reduction）與細胞死亡測試（LDH release） 38
3.3.6.1 96孔盤內實驗 38
3.3.6.2 微卡計內細胞的測試 38
3.3.7 微卡計實驗流程 39
3.3.8 細胞死亡熱量之計算 40
第四章結果與討論 41
4.1 不同濃度過氧化氫對PC12細胞的毒性及其熱流量 41
4.2 改變細胞膜組成後對細胞活性的影響以及培養在微卡計內細胞的活性 49
4.3不同聚合度Ab對降低GM1濃度細胞膜之PC12細胞和普通細胞的毒性 53
4.3.1 Fiber rich Ab對降低GM1濃度細胞膜之PC12細胞和普通細胞的毒性 53
及熱流量 53
4.3.2 Monomer rich Ab對降低GM1濃度細胞膜之PC12細胞和普通細胞的 59
毒性及熱流量 59
4.3.3 Oligomer rich Ab對降低GM1濃度細胞膜之PC12細胞和普通細胞的 65
毒性及熱流量 65
4.4 不同聚合度Ab對不同膽固醇含量細胞膜之PC12細胞的毒性及熱流量 71
4.4.1 Fiber rich Ab對不同膽固醇含量細胞膜之PC12細胞的細胞毒性及熱 71
流量 71
4.4.2 Monomer rich Ab對不同膽固醇含量細胞膜之PC12細胞的細胞毒性 77
及其熱流量 77
4.4.3 oligomer rich Ab對不同膽固醇含量細胞膜之PC12細胞的細胞毒性及 82
其熱流量 82
4.5 細胞死亡的放熱 87
4.5.1過氧化氫實驗 87
4.5.2 改變細胞膜GM1含量與不同結構Ab反應實驗 87
4.5.3 改變細胞膜膽固醇含量與不同結構Ab反應實驗 88
第五章結論 89
第六章參考文獻 90

參考文獻

1. Hardy, J.; Selkoe, D. J., Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 2002, 297 (5580), 353-356.
2. Lambert, M. P.; Barlow, A. K.; Chromy, B. A.; Edwards, C.; Freed, R.; Liosatos, M.; Morgan, T. E.; Rozovsky, I.; Trommer, B.; Viola, K. L.; Wals, P.; Zhang, C.; Finch, C. E.; Krafft, G. A.; Klein, W. L., Diffusible, nonfibrillar ligands derived from A beta(1-42) are potent central nervous system neurotoxins. P Natl Acad Sci USA 1998, 95 (11), 6448-6453.
3. Esteban, J. A., Living with the enemy: a physiological role for the beta-amyloid peptide. Trends Neurosci 2004, 27 (1), 1-3.
4. Wood, W. G.; Eckert, G. P.; Igbavboa, U.; Muller, W. E., Amyloid beta-protein interactions with membranes and cholesterol: causes or casualties of Alzheimer's disease. Bba-Biomembranes 2003, 1610 (2), 281-290.
5. Sultana, R.; Perluigi, M.; Butterfield, D. A., Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around A beta(1-42). J Chromatogr B 2006, 833 (1), 3-11.
6. Blennow, K.; de Leon, M. J.; Zetterberg, H., Alzheimer's disease. Lancet 2006, 368 (9533), 387-403.
7. Selkoe, D. J., Cell Biology of the Amyloid Beta-Protein Precursor and the Mechanism of Alzheimers-Disease. Annu Rev Cell Biol 1994, 10, 373-403.
8. Cappai, R.; White, A. R., Amyloid beta. Int J Biochem Cell B 1999, 31 (9), 885-889.
9. Kakio, A.; Nishimoto, S.; Yanagisawa, K.; Kozutsumi, Y.; Matsuzaki, K., Cholesterol-dependent formation of GM1 ganglioside-bound amyloid beta-protein, an endogenous seed for Alzheimer amyloid. Journal of Biological Chemistry 2001, 276 (27), 24985-24990.
10. Bieschke, J.; Zhang, Q. H.; Powers, E. T.; Lerner, R. A.; Kelly, J. W., Oxidative metabolites accelerate Alzheimer's amyloidogenesis by a two-step mechanism, eliminating the requirement for nucleation. Biochemistry 2005, 44 (13), 4977-4983.
11. Shoghi-Jadid, K.; Barrio, J. R.; Kepe, V.; Wu, H. M.; Small, G. W.; Phelps, M. E.; Huang, S. C., Imaging beta-amyloid fibrils in Alzheimer's disease: a critical analysis through simulation of amyloid fibril polymerization. Nucl Med Biol 2005, 32 (4), 337-351.
12. Xing, Y. M.; Higuchi, K., Amyloid fibril proteins. Mech Ageing Dev 2002, 123 (12), 1625-1636.
13. Serpell, L. C., Alzheimer's amyloid fibrils: structure and assembly. Biochimica Et Biophysica Acta-Molecular Basis of Disease 2000, 1502 (1), 16-30.
14. Lin, M. S.; Chen, L. Y.; Tsai, H. T.; Wang, S. S. S.; Chang, Y.; Higuchi, A.; Chen, W. Y., Investigation of the mechanism of beta-amyloid fibril formation by kinetic and thermodynamic analyses. Langmuir 2008, 24 (11), 5802-5808.
15. Burdick, D.; Soreghan, B.; Kwon, M.; Kosmoski, J.; Knauer, M.; Henschen, A.; Yates, J.; Cotman, C.; Glabe, C., Assembly and Aggregation Properties of Synthetic Alzheimers A4/Beta Amyloid Peptide Analogs. Journal of Biological Chemistry 1992, 267 (1), 546-554.
16. Stine, W. B.; Dahlgren, K. N.; Krafft, G. A.; LaDu, M. J., In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. Journal of Biological Chemistry 2003, 278 (13), 11612-11622.
17. Jarrett, J. T.; Berger, E. P.; Lansbury, P. T., The Carboxy Terminus of the Beta-Amyloid Protein Is Critical for the Seeding of Amyloid Formation - Implications for the Pathogenesis of Alzheimers-Disease. Biochemistry 1993, 32 (18), 4693-4697.
18. Terzi, E.; Holzemann, G.; Seelig, J., Self-Association of Beta-Amyloid Peptide(1-40) in Solution and Binding to Lipid-Membranes. Journal of Molecular Biology 1995, 252 (5), 633-642.
19. Gursky, O.; Aleshkov, S., Temperature-dependent beta-sheet formation in beta-amyloid A beta(1-40) peptide in water: uncoupling beta-structure folding from aggregation. Bba-Protein Struct M 2000, 1476 (1), 93-102.
20. ChooSmith, L. P.; GarzonRodriguez, W.; Glabe, C. G.; Surewicz, W. K., Acceleration of amyloid fibril formation by specific binding of A beta-(1-40) peptide to ganglioside-containing membrane vesicles. Journal of Biological Chemistry 1997, 272 (37), 22987-22990.
21. Nichols, M. R.; Moss, M. A.; Reed, D. K.; Cratic-McDaniei, S.; Hoh, J. H.; Rosenberry, T. L., Amyloid-beta protofibrils differ from Amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology. Journal of Biological Chemistry 2005, 280 (4), 2471-2480.
22. Roher, A. E.; Chaney, M. O.; Kuo, Y. M.; Webster, S. D.; Stine, W. B.; Haverkamp, L. J.; Woods, A. S.; Cotter, R. J.; Tuohy, J. M.; Krafft, G. A.; Bonnell, B. S.; Emmerling, M. R., Morphology and toxicity of A beta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. Journal of Biological Chemistry 1996, 271 (34), 20631-20635.
23. kayed, R., common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003, 300.
24. Koo, E. H.; Lansbury, P. T.; Kelly, J. W. In Amyloid diseases: Abnormal protein aggregation in neurodegeneration, Natl Acad Sciences: 1999; pp 9989-9990.
25. Wang, S. S. S.; Rymer, D. L.; Good, T. A., Reduction in cholesterol and sialic acid content protects cells from the toxic effects of beta-amyloid peptides. Journal of Biological Chemistry 2001, 276 (45), 42027-42034.
26. Wakabayashi, M.; Matsuzaki, K., Formation of amyloids by a beta-(1-42) on NGF-differentiated PC12 cells: roles of Gangliosides and cholesterol. Journal of Molecular Biology 2007, 371 (4), 924-933.
27. Arispe, N.; Doh, M., Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease A beta P (1-40) and (1-42) peptides. Faseb Journal 2002, 16 (12), 1526-1536.
28. Lin, M. S.; Chen, L. Y.; Wang, S. S. S.; Chang, Y.; Chen, W. Y., Examining the levels of ganglioside and cholesterol in cell membrane on attenuation the cytotoxicity of beta-amyloid peptide. Colloids and Surfaces B-Biointerfaces 2008, 65 (2), 172-177.
29. Schneider, A.; Schulz-Schaeffer, W.; Hartmann, T.; Schulz, J. B.; Simons, M., Cholesterol depletion reduces aggregation of amyloid-beta peptide in hippocampal neurons. Neurobiol Dis 2006, 23 (3), 573-577.
30. Yanagisawa, K.; Odaka, A.; Suzuki, N.; Ihara, Y., GM1 GANGLOSIDE-BOUND AMYLOID BETA-PROTEIN (AB) - A POSSIBLE FORM OF PREAMYLOID IN ALZHEIMERS-DISEASE. Nature Medicine 1995, 1 (10), 1062-1066.
31. Hayashi, H.; Kimura, N.; Yamaguchi, H.; Hasegawa, K.; Yokoseki, T.; Shibata, M.; Yamamoto, N.; Michikawa, M.; Yoshikawa, Y.; Terao, K.; Matsuzaki, K.; Lemere, C. A.; Selkoe, D. J.; Naiki, H.; Yanagisawa, K., A seed for Alzheimer amyloid in the brain. Journal of Neuroscience 2004, 24 (20), 4894-4902.
32. Wakabayashi, M.; Okada, T.; Kozutsumi, Y.; Matsuzaki, K., GM1 ganglioside-mediated accumulation of amyloid beta-protein on cell membranes. Biochemical and Biophysical Research Communications 2005, 328 (4), 1019-1023.
33. Okada, T.; Wakabayashi, M.; Ikeda, K.; Matsuzaki, K., Formation of toxic fibrils of Alzheimer's amyloid beta-protein-(1-40) by monosialoganglioside GM1, a neuronal membrane component. Journal of Molecular Biology 2007, 371 (2), 481-489.
34. Kakio, A.; Nishimoto, S.; Yanagisawa, K.; Kozutsumi, Y.; Matsuzaki, K., Interactions of amyloid beta-protein with various gangliosides in raft-like membranes: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry 2002, 41 (23), 7385-7390.
35. 方瓊儀, 利用微卡計對於蛋白質與離子交換樹脂觸手間親疏水作用力的研究. 2002.
36. Ladbury, J. E., Application of isothermal titration calorirnetry in the biological sciences: Things are heating up! BioTechniques 2004, 37 (6), 885-887.
37. Boyer, R., Concepts i biochemistry. 2001.
38. Bottcher, H.; Furst, P., Microcalorimetric and biochemical investigations of thermogenesis and metabolic pathways in human white adipocytes. International Journal of Obesity 1996, 20 (9), 874-881.
39. levin K, F. P., Harris R Heat production from human erythrocyte in relation to their metabolism of glucose and amino acid. Scandinavian journal of clinical and laboratory investigation 1974, 34, 141-148.
40. Bottcher, H.; Furst, P., A new microcatheter enables microcalorimetric assessment of thermogenesis after stimulation in cell cultures. Journal of Biochemical and Biophysical Methods 1996, 32 (3), 191-194.
41. Kemp, R. B.; Guan, Y., Heat flux and the calorimetric-respirometric ratio as measures of catabolic flux in mammalian cells. Thermochim Acta 1997, 300 (1-2), 199-211.
42. Jordi Bermudez, P. B., and Arne Schon, Microcalorimetric evaluation of the effect of methotrexate and 6-thioguanine on sensitive T-lymphoma cells and on a methotrxate-resistant subline. cell biophysics 1992, 20, 111-123.
43. Charlebois, S. J.; Daniels, A. U.; Smith, R. A., Metabolic heat production as a measure of macrophage response to particles from orthopedic implant materials. J Biomed Mater Res 2002, 59 (1), 166-175.
44. Liu, W.; Chaspoul, F.; Lefranc, D. B.; Decome, L.; Gallice, P. In Microcalorimetry as a tool for Cr(VI) toxicity evaluation of human dermal fibroblasts, Springer: 2007; pp 21-24.
45. Lin, M. S.; Chiu, H. M.; Fan, F. J.; Tsai, H. T.; Wang, S. S. S.; Chang, Y.; Chen, W. Y., Kinetics and enthalpy measurements of interaction between P-amyloid and liposomes by surface plasmon resonance and isothermal titration microcalorimetry. Colloids and Surfaces B-Biointerfaces 2007, 58 (2), 231-236.
46. Terzi, E.; Holzemann, G.; Seelig, J., Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes. Biochemistry 1997, 36 (48), 14845-14852.
47. Sponne, I.; Fifre, A.; Kriem, B.; Koziel, V.; Bihain, B.; Oster, T.; Olivier, J. L.; Pillot, T., Membrane cholesterol interferes with neuronal apoptosis induced by soluble oligomers but not fibrils of the amyloid-beta peptide. Faseb Journal 2004, 18 (3), 836-+.
48. Sun, Z. X.; Zhou, Q. H.; Sui, S. F., Cholesterol depletion inhibits the degradation of amyloid beta-peptide in rat pheochromocytoma (PC12) cells. Neuroscience Letters 2005, 391 (1-2), 71-75.
49. Kemp, R. B.; Guan, Y. H., The application of heat flux measurements to improve the growth of mammalian cells in culture. Thermochim Acta 2000, 349 (1-2), 23-30.
50. Sultana, R.; Perluigi, M.; Butterfield, D. A., Oxidatively modified proteins in Alzheimer's disease (AD), mild cognitive impairment and animal models of AD: role of Abeta in pathogenesis. Acta Neuropathol 2009, 118 (1), 131-150.
51. Everse, J.; Coates, P. W., Neurodegeneration and peroxidases. Neurobiology of Aging 2009, 30 (7), 1011-1025.
52. Butterfield, D. A., Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: Implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radical Research 2002, 36 (12), 1307-1313.
53. Rauk, A., Why is the amyloid beta peptide of Alzheimer's disease neurotoxic? Dalton Trans. 2008, (10), 1273-1282.
54. Calderon, F. H.; Bonnefont, A.; Munoz, F. J.; Fernandez, V.; Videla, L. A.; Inestrosa, N. C., PC12 and neuro 2a cells have different susceptibilities to acetylcholinesterase-amyloid complexes, amyloid(25-35) fragment, glutamate, and hydrogen peroxide. J Neurosci Res 1999, 56 (6), 620-631.
55. Hwang, S. L.; Yen, G. C., Neuroprotective effects of the citrus flavanones against H2O2-induced cytotoxicity in PC12 cells. J Agr Food Chem 2008, 56 (3), 859-864.
56. Guan, S.; Bao, Y. M.; Jiang, B.; An, L. J., Protective effect of protocatechuic acid from Alpinia oxyphylla on hydrogen peroxide-induced oxidative PC12 cell death. European Journal of Pharmacology 2006, 538 (1-3), 73-79.
57. Jacob, R. A., The Integrated Antioxidant System. Nutr Res 1995, 15 (5), 755-766.
58. Feng, Y.; Luo, S. F.; Qu, S. S.; Zeng, C. Y.; Xu, H., Study on the thermosensitivity of a tumor cell by microcalorimetry. Thermochim Acta 1997, 303 (2), 203-207.
59. Bottcher, H.; Furst, P., Direct microcalorimetry as a technique in cell cultures. Bailliere Clin Endoc 1997, 11 (4), 739-752.
60. Okada, T.; Ikeda, K.; Wakabayashi, M.; Ogawa, M.; Matsuzaki, K., Formation of toxic A beta(1-40) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: Polymorphisms in A beta(1-40) fibrils. Journal of Molecular Biology 2008, 382 (4), 1066-1074.
61. Ariga, T.; McDonald, M. P.; Yu, R. K., Role of ganglioside metabolism in the pathogenesis of Alzheimer's disease - a review. J Lipid Res 2008, 49 (6), 1157-1175.

指導教授

陳文逸(Wen-yih Chen)

審核日期

2009-11-1

推文