請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/33284
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 翁啟惠(Chi-Huey Wong) | |
dc.contributor.author | Ying-Chih Liu | en |
dc.contributor.author | 劉英志 | zh_TW |
dc.date.accessioned | 2021-06-13T04:32:46Z | - |
dc.date.available | 2012-08-01 | |
dc.date.copyright | 2011-08-01 | |
dc.date.issued | 2011 | |
dc.date.submitted | 2011-07-27 | |
dc.identifier.citation | Becker, D.J., and Lowe, J.B. (2003). Fucose: biosynthesis and biological function in mammals. Glycobiology 13, 41r-53r.
Bitler, B.G., Goverdhan, A., and Schroeder, J.A. (2010). MUC1 regulates nuclear localization and function of the epidermal growth factor receptor. J Cell Sci 123, 1716-1723. Bond, M.R., and Kohler, J.J. (2007). Chemical methods for glycoprotein discovery. Curr Opin Chem Biol 11, 52-58. Bresalier, R.S., Rockwell, R.W., Dahiya, R., Duh, Q.Y., and Kim, Y.S. (1990). Cell surface sialoprotein alterations in metastatic murine colon cancer cell lines selected in an animal model for colon cancer metastasis. Cancer Res 50, 1299-1307. Chang, W.W., Lee, C.H., Lee, P., Lin, J., Hsu, C.W., Hung, J.T., Lin, J.J., Yu, J.C., Shao, L.E., Yu, J., et al. (2008). Expression of Globo H and SSEA3 in breast cancer stem cells and the involvement of fucosyl transferases 1 and 2 in Globo H synthesis. Proc Natl Acad Sci U S A 105, 11667-11672. Cho, H.S., and Leahy, D.J. (2002). Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297, 1330-1333. Chu, Y.W., Yang, P.C., Yang, S.C., Shyu, Y.C., Hendrix, M.J.C., Wu, R., and Wu, C.W. (1997). Selection of invasive and metastatic subpopulations from a human lung adenocarcinoma cell line. Am J Resp Cell Mol 17, 353-360. Citri, A., and Yarden, Y. (2006). EGF-ERBB signalling: towards the systems level. Nat Rev Mol Cell Bio 7, 505-516. Dawson, J.P., Berger, M.B., Lin, C.C., Schlessinger, J., Lemmon, M.A., and Ferguson, K.M. (2005). Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface. Mol Cell Biol 25, 7734-7742. de Freitas Junior, J.C., Silva, B.D., de Souza, W.F., de Araujo, W.M., Abdelhay, E.S., and Morgado-Diaz, J.A. (2010). Inhibition of N-linked glycosylation by tunicamycin induces E-cadherin-mediated cell-cell adhesion and inhibits cell proliferation in undifferentiated human colon cancer cells. Cancer Chemother Pharmacol. De Luca, A., Carotenuto, A., Rachiglio, A., Gallo, M., Maiello, M.R., Aldinucci, D., Pinto, A., and Normanno, N. (2008). The role of the EGFR signaling in tumor microenvironment. J Cell Physiol 214, 559-567. Dell, A., Reason, A.J., Khoo, K.H., Panico, M., McDowell, R.A., and Morris, H.R. (1994). Mass spectrometry of carbohydrate-containing biopolymers. Methods Enzymol 230, 108-132. Dennis, J.W., Laferte, S., Waghorne, C., Breitman, M.L., and Kerbel, R.S. (1987). Beta-1-6 Branching of Asn-Linked Oligosaccharides Is Directly Associated with Metastasis. Science 236, 582-585. Dube, D.H., and Bertozzi, C.R. (2005). Glycans in cancer and inflammation. Potential for therapeutics and diagnostics. Nat Rev Drug Discov 4, 477-488. Dube, D.H., Prescher, J.A., Quang, C.N., and Bertozzi, C.R. (2006). Probing mucin-type O-linked glycosylation in living animals. P Natl Acad Sci USA 103, 4819-4824. Ferguson, K.M., Berger, M.B., Mendrola, J.M., Cho, H.S., Leahy, D.J., and Lemmon, M.A. (2003). EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell 11, 507-517. Gullick, W.J., Downward, J., Parker, P.J., Whittle, N., Kris, R., Schlessinger, J., Ullrich, A., and Waterfield, M.D. (1985). The structure and function of the epidermal growth factor receptor studied by using antisynthetic peptide antibodies. Proc R Soc Lond B Biol Sci 226, 127-134. Guo, H.B., Johnson, H., Randolph, M., Lee, I., and Pierce, M. (2009). Knockdown of GnT-Va expression inhibits ligand-induced downregulation of the epidermal growth factor receptor and intracellular signaling by inhibiting receptor endocytosis. Glycobiology 19, 547-559. Hanash, S.M., Pitteri, S.J., and Faca, V.M. (2008). Mining the plasma proteome for cancer biomarkers. Nature 452, 571-579. Hang, H.C., Yu, C., Kato, D.L., and Bertozzi, C.R. (2003). A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation. P Natl Acad Sci USA 100, 14846-14851. Hanson, S.R., Hsu, T.L., Weerapana, E., Kishikawa, K., Simon, G.M., Cravatt, B.F., and Wong, C.H. (2007). Tailored glycoproteomics and glycan site mapping using saccharide-selective bioorthogonal probes. J Am Chem Soc 129, 7266-7267. Harduin-Lepers, A., Vallejo-Ruiz, V., Krzewinski-Recchi, M.A., Samyn-Petit, B., Julien, S., and Delannoy, P. (2001). The human sialyltransferase family. Biochimie 83, 727-737. Hsu, T.L., Hanson, S.R., Kishikawa, K., Wang, S.K., Sawa, M., and Wong, C.H. (2007). Alkynyl sugar analogs for the labeling and visualization of glycoconjugates in cells. P Natl Acad Sci USA 104, 2614-2619. Javaud, C., Dupuy, F., Maftah, A., Julien, R., and Petit, J.M. (2003). The fucosyltransferase gene family: an amazing summary of the underlying mechanisms of gene evolution. Genetica 118, 157-170. Kannagi, R., Izawa, M., Koike, T., Miyazaki, K., and Kimura, N. (2004). Carbohydrate-mediated cell adhesion in cancer metastasis and angiogenesis. Cancer Sci 95, 377-384. Keppler, O.T., Horstkorte, R., Pawlita, M., Schmidt, C., and Reutter, W. (2001). Biochemical engineering of the N-acyl side chain of sialic acid: biological implications. Glycobiology 11, 11R-18R. Kroes, R.A., He, H., Emmett, M.R., Nilsson, C.L., Leach, F.E., 3rd, Amster, I.J., Marshall, A.G., and Moskal, J.R. (2010). Overexpression of ST6GalNAcV, a ganglioside-specific alpha2,6-sialyltransferase, inhibits glioma growth in vivo. Proc Natl Acad Sci U S A 107, 12646-12651. Kuster, B., Wheeler, S.F., Hunter, A.P., Dwek, R.A., and Harvey, D.J. (1997). Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography. Anal Biochem 250, 82-101. Lau, K.S., Partridge, E.A., Grigorian, A., Silvescu, C.I., Reinhold, V.N., Demetriou, M., and Dennis, J.W. (2007). Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129, 123-134. Lax, I., Bellot, F., Howk, R., Ullrich, A., Givol, D., and Schlessinger, J. (1989). Functional-Analysis of the Ligand-Binding Site of Egf-Receptor Utilizing Chimeric Chicken Human Receptor Molecules. Embo J 8, 421-427. Le Pendu, J., Marionneau, S., Cailleau-Thomas, A., Rocher, J., Le Moullac-Vaidye, B., and Clement, M. (2001). ABH and Lewis histo-blood group antigens in cancer. APMIS 109, 9-31. Lemmon, M.A. (2009). Ligand-induced ErbB receptor dimerization. Exp Cell Res 315, 638-648. Li, J., Cheng, L., Wang, L.J., Liu, H.C., Li, L., Wang, X.L., and Geng, M.Y. (2010). Cell surface sialic acid inhibits Cx43 gap junction functions in constructed Hela cancer cells involving in sialylated N-cadherin. Mol Cell Biochem 344, 241-251. Li, W.Z., Nakagawa, T., Koyama, N., Wang, X.C., Jin, J.H., Mizuno-Horikawa, Y., Gu, J.G., Miyoshi, E., Kato, I., Honke, K., et al. (2006). Down-regulation of trypsinogen expression is associated with growth retardation in alpha 1,6-fucosyltransferase-deficient mice: attenuation of proteinase-activated receptor 2 activity. Glycobiology 16, 1007-1019. Lo, H.W., Hsu, S.C., Xia, W., Cao, X., Shih, J.Y., Wei, Y., Abbruzzese, J.L., Hortobagyi, G.N., and Hung, M.C. (2007). Epidermal growth factor receptor cooperates with signal transducer and activator of transcription 3 to induce epithelial-mesenchymal transition in cancer cells via up-regulation of TWIST gene expression. Cancer Res 67, 9066-9076. Mahal, L.K., Yarema, K.J., and Bertozzi, C.R. (1997). Engineering chemical reactivity on cell surfaces through oligosaccharide biosynthesis. Science 276, 1125-1128. Matsumoto, K., Yokote, H., Arao, T., Maegawa, M., Tanaka, K., Fujita, Y., Shimizu, C., Hanafusa, T., Fujiwara, Y., and Nishio, K. (2008). N-Glycan fucosylation of epidermal growth factor receptor modulates receptor activity and sensitivity to epidermal growth factor receptor tyrosine kinase inhibitor. Cancer Sci 99, 1611-1617. Merlin, J., Stechly, L., de Beauce, S., Monte, D., Leteurtre, E., van Seuningen, I., Huet, G., and Pigny, P. (2011). Galectin-3 regulates MUC1 and EGFR cellular distribution and EGFR downstream pathways in pancreatic cancer cells. Oncogene 30, 2514-2525. Meuillet, E.J., Kroes, R., Yamamoto, H., Warner, T.G., Ferrari, J., Mania-Farnell, B., George, D., Rebbaa, A., Moskal, J.R., and Bremer, E.G. (1999). Sialidase gene transfection enhances epidermal growth factor receptor activity in an epidermoid carcinoma cell line, A431. Cancer Res 59, 234-240. Nyati, M.K., Morgan, M.A., Feng, F.Y., and Lawrence, T.S. (2006). Integration of EGFR inhibitors with radiochemotherapy. Nat Rev Cancer 6, 876-885. Ogiso, H., Ishitani, R., Nureki, O., Fukai, S., Yamanaka, M., Kim, J.H., Saito, K., Sakamoto, A., Inoue, M., Shirouzu, M., et al. (2002). Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell 110, 775-787. Partridge, E.A., Le Roy, C., Di Guglielmo, G.M., Pawling, J., Cheung, P., Granovsky, M., Nabi, I.R., Wrana, J.L., and Dennis, J.W. (2004). Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Science 306, 120-124. Ramasamy, S., Duraisamy, S., Barbashov, S., Kawano, T., Kharbanda, S., and Kufe, D. (2007). The MUC1 and galectin-3 oncoproteins function in a microRNA-dependent regulatory loop. Mol Cell 27, 992-1004. Sagi, D., Kienz, P., Denecke, J., Marquardt, T., and Peter-Katalinic, J. (2005). Glycoproteomics of N-glycosylation by in-gel deglycosylation and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry mapping: application to congenital disorders of glycosylation. Proteomics 5, 2689-2701. Sampathkumar, S.G., Li, A.V., Jones, M.B., Sun, Z.H., and Yarema, K.J. (2006). Metabolic installation of thiols into sialic acid modulates adhesion and stem cell biology. Nat Chem Biol 2, 149-152. Sato, Y., Takahashi, M., Shibukawa, Y., Jain, S.K., Hamaoka, R., Miyagawa, J., Yaginuma, Y., Honke, K., Ishikawa, M., and Taniguchi, N. (2001). Overexpression of N-acetylglucosaminyltransferase III enhances the epidermal growth factor-induced phosphorylation of ERK in HeLaS3 cells by up-regulation of the internalization rate of the receptors. J Biol Chem 276, 11956-11962. Sawa, M., Hsu, T.L., Itoh, T., Sugiyama, M., Hanson, S.R., Vogt, P.K., and Wong, C.H. (2006). Glycoproteomic probes for fluorescent imaging of fucosylated glycans in vivo. P Natl Acad Sci USA 103, 12371-12376. Saxon, E., and Bertozzi, C.R. (2000). Cell surface engineering by a modified Staudinger reaction. Science 287, 2007-2010. Schlessinger, J. (2000). Cell signaling by receptor tyrosine kinases. Cell 103, 211-225. Schroeder, J.A., Pochampalli, M.R., and el Bejjani, R.M. (2007). MUC1 is a novel regulator of erbB1 receptor trafficking. Oncogene 26, 1693-1701. Stowell, S.R., Arthur, C.M., Mehta, P., Slanina, K.A., Blixt, O., Leffler, H., Smith, D.F., and Cummings, R.D. (2008). Galectin-1, -2, and -3 exhibit differential recognition of sialylated glycans and blood group antigens. J Biol Chem 283, 10109-10123. Tai, H.C., Khidekel, N., Ficarro, S.B., Peters, E.C., and Hsieh-Wilson, L.C. (2004). Parallel identification of O-GlcNAc-modified proteins from cell lysates. J Am Chem Soc 126, 10500-10501. Takahashi, M., Yokoe, S., Asahi, M., Lee, S.H., Li, W., Osumi, D., Miyoshi, E., and Taniguchi, N. (2008). N-glycan of ErbB family plays a crucial role in dimer formation and tumor promotion. Bba-Gen Subjects 1780, 520-524. Taniguchi, N., Gu, J.G., Takahashi, M., and Miyoshi, E. (2004). Functional glycomics and evidence for gain- and loss-of-functions of target proteins for glycosyltransferases involved in N-glycan biosynthesis: their pivotal roles in growth and development, cancer metastasis and antibody therapy against cancer. P Jpn Acad B-Phys 80, 82-91. Taniguchi, N., Miyoshi, E., Gu, J.G., Honke, K., and Matsumoto, A. (2006). Decoding sugar functions by identifying target glycoproteins. Curr Opin Struc Biol 16, 561-566. Tsuda, T., Ikeda, Y., and Taniguchi, N. (2000). The Asn-420-linked sugar chain in human epidermal growth factor receptor suppresses ligand-independent spontaneous oligomerization - Possible role of a specific chain in controllable receptor activation. J Biol Chem 275, 21988-21994. Vercoutter-Edouart, A.S., Slomianny, M.C., Dekeyzer-Beseme, O., Haeuw, J.F., and Michalski, J.C. (2008). Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells. Proteomics 8, 3236-3256. Wang, C.C., Chen, J.R., Tseng, Y.C., Hsu, C.H., Hung, Y.F., Chen, S.W., Chen, C.M., Khoo, K.H., Cheng, T.J., Cheng, Y.S., et al. (2009). Glycans on influenza hemagglutinin affect receptor binding and immune response. Proc Natl Acad Sci U S A 106, 18137-18142. Wang, X., Gu, J., Ihara, H., Miyoshi, E., Honke, K., and Taniguchi, N. (2006). Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling. J Biol Chem 281, 2572-2577. Whitson, K.B., Whitson, S.R., Red-Brewer, M.L., McCoy, A.J., Vitali, A.A., Walker, F., Johns, T.G., Beth, A.H., and Staros, J.V. (2005). Functional effects of glycosylation at asn-579 of the epidermal growth factor receptor. Biochemistry-Us 44, 14920-14931. Yamamoto, H., Kaneko, Y., Rebbaa, A., Bremer, E.G., and Moskal, J.R. (1997). alpha2,6-Sialyltransferase gene transfection into a human glioma cell line (U373 MG) results in decreased invasivity. J Neurochem 68, 2566-2576. Yamamoto, H., Oviedo, A., Sweeley, C., Saito, T., and Moskal, J.R. (2001). alpha 2,6-Sialylation of cell-surface N-glycans inhibits glioma formation in vivo. Cancer Res 61, 6822-6829. Yamamoto, H., Swoger, J., Greene, S., Saito, T., Hurh, J., Sweeley, C., Leestma, J., Mkrdichian, E., Cerullo, L., Nishikawa, A., et al. (2000). Beta1,6-N-acetylglucosamine-bearing N-glycans in human gliomas: implications for a role in regulating invasivity. Cancer Res 60, 134-142. Yang, X.S., Liu, S., Liu, Y.J., Liu, J.W., Liu, T.J., Wang, X.Q., and Yan, Q. (2010). Overexpression of fucosyltransferase IV promotes A431 cell proliferation through activating MAPK and PI3K/Akt signaling pathways. J Cell Physiol 225, 612-619. Yokoe, S. (2008). The role of ErbB3 N-glycan in dimer formation: Implications for transforming activity. Trends Glycosci Glyc 20, 219-225. Zhen, Y.J., Caprioli, R.M., and Staros, J.V. (2003). Characterization of glycosylation sites of the epidermal growth factor receptor. Biochemistry-Us 42, 5478-5492. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/33284 | - |
dc.description.abstract | 蛋白質醣化是一項重要的轉譯後修飾,可調節蛋白質的摺疊與功能表現。過去研究顯示,癌細胞中異常的醣化作用可能影響癌症的發生與惡化。在目前的研究中,我們試著藉由炔化類醣(alkynyl sugars)比較兩株源自同細胞但具有不同侵襲力的肺癌細胞株CL1-0與CL1-5之中受唾液酸化與岩藻醣化的蛋白質。最初的結果發現,在較具侵襲力的CL1-5細胞中可觀察到比起CL1-0更高量之唾液酸化與岩藻醣化蛋白質的表現。接下來,我們定出CL1-5中受高量唾液酸化的蛋白質,並從中選定上皮細胞生長激素受器(EGFR)更深入探討唾液酸化對其功能之影響。我們定出EGFR在兩種細胞株中醣鍊的序列結構,並且確認了EGFR的確在CL1-5中較CL1-0受到更高程度的唾液酸化。有趣的是,我們也從醣鍊定序的結果中觀察到CL1-5中的EGFR有較CL1-0高量的岩藻醣化現象,與先前利用炔化類岩藻醣比較兩細胞中蛋白質醣化的結果相符合。進一步的實驗中,我們發現表現高量唾液酸轉移酶的CL1-5以及過量表現岩藻醣轉移酶4/6的A549細胞,其EGFR在受質EGF處理下,發生聚合、磷酸化,以及下游訊息活化的程度都會受到抑制。然而,若在CL1-5中抑制岩藻醣轉移酶8的表現,則減弱了EGFR的聚合與磷酸化,顯示核心岩藻醣化(core-fucosylation)具有強化EGFR活性的效果。此影響聚合與醣化的關聯已經由唾液酸水解酶與岩藻醣水解酶的處理而得到證實,並且發現唾液酸化與岩藻醣化程度的高低的確會影響肺癌細胞受EGF刺激所引發的侵襲現象。本研究成果提供了一個新的觀點,唾液酸化與岩藻醣化程度的上升,特別是在某些EGFR過量表現的癌細胞中,可能具有拮抗癌細胞發育的作用。 | zh_TW |
dc.description.abstract | Glycosylation is an important post-translational modification, which regulates proteins folding and functional expression. Previous studies have shown that, abnormal glycosylation in tumor cells can participate in cancer progression and malignancy. In the current study, we compared the sialylated and fucosylated proteins with alkynyl sugars in different lung cancer cell lines, CL1-0 and CL1-5, two subpopulations derived from the same parental cell line but with distinct invasiveness. Our initial experiments demonstrated that CL1-5, the highly aggressive cells, expressed more sialylated and fucosylated proteins than CL1-0. At next step, we identified the unique sialylated proteins in CL1-5. Among them, we chose epidermal growth factor receptor (EGFR) to further study the role of sialylation on its function. Based on glycan analysis, we validated the distinct sialylation level of EGFR in both cells. Interestingly, we also observed higher fucosylation of EGFR in CL1-5 than in CL1-0, corresponding to the comparison of whole proteins glycosylation in both cells using alkynyl fucose. Further study suggested that overexpression of sialyltranssferases in CL1-5 and | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T04:32:46Z (GMT). No. of bitstreams: 1 ntu-100-D94b46002-1.pdf: 6465845 bytes, checksum: 4029d149ddba73ac12b471323b32705c (MD5) Previous issue date: 2011 | en |
dc.description.tableofcontents | 1. Introduction 1
1.1 The importance of glycosylation 1 1.2 Tumor-associated glycans 2 1.3 Sialyltransferases (STs) and Fucosyltransferases (FUTs) 3 1.4 The specific glycan tagging systems 4 1.5 Importance of epidermal growth factor receptor (EGFR) 7 1.6 Effect of glycosylation on EGFR 8 1.7 Purpose 9 2. Materials and methods 14 2.1 Materials 14 2.2 Methods 19 2.2.1 Cell culture 19 2.2.2 Microspcopic analysis of fluorescent labeling in cells 19 2.2.3 On-membrane click reaction 20 2.2.4 Identification of glycoproteomes 20 2.2.5 Pull-down of EGFR with antibody and lectin 22 2.2.6 Plasmid construction and stable lines establishment 23 2.2.7 Purification of FLAG-tagged full length EGFR and soluble EGFR (sEGFR) 25 2.2.8 In solution tryptic digestion, N-glycosite determination and assigning glycopeptides 25 2.2.9 Nano-LC-MS/MS 26 2.2.10 Analysis of N-glycans 27 2.2.11 In-Gel PNGase F Digestion 28 2.2.12 Permethylation of glycans and MALDI-MS analysis 28 2.2.13 Deconvolution of MALDI-MS data 29 2.2.14 ELISA 29 2.2.15 SPR/Biacore-binding assay 30 2.2.16 EGFR dimerization assay 31 2.2.17 Detection of EGFR tyrosine phsophorylation 31 2.2.18 Glycosidase treatment 32 2.2.19 Western blot blotting 33 2.2.20 Flow cytometric analysis 33 2.2.21 EGF-mediated invasion assay 34 3. Results 35 3.1 Fluorescent labeling of fucosylated and sialylated glycoconjugates on cell surface 35 3.2 Labeling of fucosylated or sialylated glycoproteins in cell lysate 36 3.3 Identification of sialyl glycoproteins in CL1-0 and CL1-5 lung cancer cells 38 3.4 Validation of EGFR sialylation level in CL1-0 and CL1-5 cells 39 3.5 Overexpression and purification of EGFR in CL1-0 and CL1-5 cells 40 3.6 Glycan sequencing of EGFR in CL1-0 and CL1-5 cells 41 3.7 Ligand binding ability of the sEGFR from CL1-0 and CL1-5 44 3.8 Comparison of EGFR dimerization, phosphorylation, and its downstream signaling in CL1-0 and CL1-5 45 3.9 Validation of the role of sialylation on EGFR dimerization and phsophorylation 46 3.10 In vitro dimerization of sialidase-modified EGFR 47 3.11 Role of fucosylation on EGFR dimerization and phosphorylation 48 3.12 Role of sialylation and fucosylation in EGF-mediated cell invasion 50 3.13 Summary 51 4. Discussion 52 5. Figures 57 6. Tables 96 7. References 103 | |
dc.language.iso | en | |
dc.title | 唾液酸化與岩藻醣化對肺癌細胞中上皮生長激素受器的聚合作用及活性調控之探討 | zh_TW |
dc.title | Sialylation and Fucosylation of Epidermal Growth Factor Receptor Suppress its Dimerization and Activation in Lung Cancer Cells | en |
dc.type | Thesis | |
dc.date.schoolyear | 99-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 楊泮池(Pan-Chyr Yang),陳鈴津(Lin-Tsing Chen),劉扶東(Fu-Tong Liu),邱繼輝(Kay-Hooi Khoo),吳宗益(Chung-Yi Wu) | |
dc.subject.keyword | 唾液酸,岩藻醣,上皮細胞生長激素受器,醣蛋白質體學,醣定序, | zh_TW |
dc.subject.keyword | Sialic acid,Fucose,EGFR,Glycoproteomics,glycan sequencing, | en |
dc.relation.page | 113 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2011-07-27 | |
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 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-100-1.pdf 目前未授權公開取用 | 6.31 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。