跳到主要內容

臺灣博碩士論文加值系統

(34.204.172.188) 您好!臺灣時間:2023/10/01 19:58
字體大小: 字級放大   字級縮小   預設字形  
回查詢結果 :::

詳目顯示

我願授權國圖
: 
twitterline
研究生:林家豪
研究生(外文):Lin Chia-Hao
論文名稱:吳郭魚AMPA受器次單元GluR1的xT/Sxφ序列與蛋白質SAP97交互作用探討
論文名稱(外文):Studies of interaction between xT/Sxφmotif of a tilapia AMPA receptor subunit GluR1 and SAP97
指導教授:周 姽 嫄
指導教授(外文):Chow Wei-Yuan
學位類別:碩士
校院名稱:國立清華大學
系所名稱:生命科學系
學門:生命科學學門
學類:生物學類
論文種類:學術論文
論文出版年:2002
畢業學年度:90
語文別:中文
論文頁數:67
中文關鍵詞:AMPA受器SAP97麩胺酸受器yeast two hybrid交互作用
相關次數:
  • 被引用被引用:0
  • 點閱點閱:202
  • 評分評分:
  • 下載下載:0
  • 收藏至我的研究室書目清單書目收藏:0
麩氨酸是脊椎動物中樞神經系統主要的興奮性神經衝動傳導物質之一。離子通道型麩氨酸受器依其藥理學及電生理學特性可分為AMPA、 kainate和NMDA受器等三大類。麩胺酸受器次單元的C端區域能與神經後突觸區域內的蛋白質產生交互作用,此作用可能與麩氨酸受器在神經後突觸細胞膜上的固定、聚集有關;或藉此把其他負責細胞內訊息傳遞的蛋白質募集至神經後突觸細胞區,並與麩氨酸受器發生結合,藉以調控麩氨酸受器離子通道的活性。前人研究中以免疫沈澱法及GST蛋白結合技術證明了老鼠GluR1的C端三個氨基酸序列TGL能與SAP97的第一個PDZ domain產生交互作用;而一些文獻中則推論SAP97的PDZ domain能與xS/Txφ(x為任何氨基酸,φ為疏水性氨基酸)序列的C端交互作用。比較老鼠的GluR1 C端序列,TGL,與吳郭魚的GluR1β C端序列,TGM,兩者皆為xS/Txφ,因此我們預測吳郭魚的GluR1β應該能與SAP97產生交互作用。在本實驗中,以吳郭魚GluR1β C端與SAP97第一個PDZ domain進行yeast two hybrid及GST蛋白結合實驗,探討兩者間是否能有交互作用,以及再驗證xS/Txφ型式的C端是否皆能與特定的PDZ domain產生交互作用,結果發現在yeast two hybrid實驗中,老鼠GluR1並未與SAP97有交互作用,在GST蛋白結合實驗中則能觀察到老鼠GluR1與SAP97的交互作用,並且也證明了吳郭魚GluR1β與SAP97的交互作用。由yeast two hybrid實驗結果可以知道yeast two hybrid可能無法偵測到一些蛋白質間交互作用,而在GST蛋白結合技術的實驗中則再一次證明SAP97的PDZ domain能與xS/Txφ序列的C端產生交互作用,而且吳郭魚GluR1β可能能與吳郭魚腦中類似SAP97的蛋白質進行交互作用,而使吳郭魚AMPA受器在突觸膜上的聚集及分佈受到調控。

英文摘要………………………………………………………………..3
中文摘要………………………………………………………………..4
前 言……………………………………………………………….. 5
材料方法………………………………………………………………..14
結 果……………………………………………………………….. 21
討 論……………………………………………………………….. 26
參考文獻……………………………………………………………….. 32
附 表……………………………………………………………….. 43
附 圖……………………………………………………………….. 45
附 件……………………………………………………………….. 63

參考文獻
Armstrong, N., Sun, Y., Chen, G.-Q., and Gouaux, E. (1998). Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 395, 913-917.
Ayer, D. E., Kretzer, L., and Eisenman, R. E. (1993). Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72, 211-222.
Bartel, P., Chien, C., Sternglanz, R., and Fields, S. (1993). Using the two-hybrid system to detect protein-protein interaction in Cellular Interaction in Development:A Practical Approach(Hartley, D. A., ed.). Oxford:Oxford University Press, pp. 153-179.
Bassand, P., Bernard, A., Rafiki, A., Gayet, Dimitri., and Khrestchatisky, M. (1999). Differential interaction of the tSXV motifs of the NR1 and NR2A NMDA receptor subunits with PSD-95 and SAP97. Euro. J. Neurosci. 11, 2031-2043.
Bettler, B., Egebjerg, J., Sharrma, G., Pecht, G., Hermans-Borgmeyer, I., Moll, C., Stevens, C. F., and Heinemann, S. ( 1992 ). Cloning of a putative glutamate receptor a low affinity kainate-binding subunit. Nature 8, 257-265.
Benprozvanny, I., and Maximov, A. (2001). Classification of PDZ domains. FEBS Letters 509, 457-462.
Bliss, T. V. P., and Collingridge, G. L. (1993). A synaptic model of memory-ong term potentiation in the hippocampus. Nature 361, 31-39.
Braithwaite, S. P., Xia, H., and Malenka, R. C. (2002). Differential roles for NSF and GRIP/ABP in AMPA receptor cycling. Proc. Natl. Acad. Sci. USA. 99 (10), 7096-7101.
Cao, Z., Lickey, M. E., Liu, L., Kirk, E., and Gordon, B. (2000a). Postnatal development of NR1, NR2A and NR2B immunoreactivity in the visual cortex of the rat. Brain Res. 859, 26-37.
Cao, Z., Liu, L., Lickey, M., and Gordon B. (2000b). Development of NR1, NR2A and NR2B mRNA in NR1 immunoreactive cells of rat visual cortex. Brain Res. 868, 296-305.
Carroll, R. C., Beattie, E. C., Zastrow, M., and Malenka, R. C. (2001). Role of AMPA receptor endocytosis in synaptic plasticity. Nature Neurosci. 2, 315-324.
Chung, H. J., Xia, J., Scannevin, R. H., Zhang, X., and Huganir, R. L. ( 2000 ). Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with the PDZ domain-containing proteins. J. Neurosci. 20, 7258-7267.
Collingridge, G. L., and Lester, R. A. J. (1989). Excitatory amino acid receptors in the vertebrate central nervous system. Pharmacol. Rev. 41, 143-210.
Das, S., Sasaki, Y. F., Rothe, T., Premkumar, L. S., Takasu, M., Crandall, J. E., Dikkes, P., Conner, D. A., Rayudu, P. V., Cheung, M., Chen, H. S. V., Lipton, S., and Nakanishi, N. ( 1998 ). Increased NMDA current and spine density in mice lacking the NMDA receptor subunit NR3A. Nature 393, 377-381.
Dev, K. K., Nishimune, A., Henley, J. M., and Nakannishi, S. ( 1999 ). The protein kinase C alpha binding protein PICKI interacts with short but not long form alternative splice variants of AMPA receptor subunits. Neuropharmacology 38, 635-644.
Dingledine, R., Borges, K., Bowie, D., and Traynelis, S. F. (1999). The glutamate receptor ion channels. Pharmacol. Rev. 51, 7-61.
Dong, H., Zhang, P., Song, I., Petralia, R. S., Liao, D., and Huganir, R. L. ( 1999 ). Characterization of the glutamate receptor-interacting proteins GRIP1 and GRIP2. J. Neurosci. 19, 6930-6941.
Egebjerg, J., Bettler, B., Hermans-Borgmeyer, I., and Heinemann, S. ( 1990 ). Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA. Nature 351, 745-748.
Ehlers, M. D., Mammen, A. L., Lau, L. F., and Huganir, R. L. ( 1996). Synaptic targeting of glutamate receptors. Curr. Opin. Cell Biol. 8, 484-489.
Fields, S., and Song, O. K. (1989). A novel genetic system to detect protein-protein interaction. Nature 340, 245-246.
Fields, S. (1993). The two-hybrid system to detect protein-protein interactions. Methods 5, 116-124.
Fujita, A., and Kurachi, Y. (2000). Breakthroughs and views SAP family proteins. Biochem. Biophysic. Res. Communi. 269, 1-6.
Gallo, V., Upson, L. M., Hayes, W. P., Vyklicky, L. Jr., Winters, C. A., and Buonanno, A. ( 1992 ). Molecular cloning and developmental analysis of a new glutamate receptor subunit isoform in cerebellum. J. Neurosci. 12, 1010-1023.
Garcia, E. P., Mehta, S., Blair, L. A. C., Wells, D. G., Shang, J., Fukushima, T., Fallon, J. R., Garner, C. C., and Marshall, J. ( 1998 ). SAP90 binds and clusters kainate receptors causing incomplete desensitization. Neuron 21, 727-739.
Hanley, J. G.., Khatri, L., Hanson, P., and Ziff, E. B. (2002). NSF ATPase and α-/β-SNAPs disassemble the AMPA receptor-PICK1 complex. Neuron 34, 53-67.
Harper, J. W., Adami, G. R., Wei, N., Keyomarsi, K., and Elledge, S. J. (1993). The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinase. Cell 75, 805-816.
Hayashi, Y., Shi, S. H., Esteban, J. A., Piccini, A., Poncer, J. —C., and Malinow, R. ( 2000 ). Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science 287, 2262-2267.
Herv’e, D., Levenes, C., and Cr’epel, F. (1998). Cellular mechanism of cerebellar LTD. Trends Neurosci. 21, 401-407.
Hirai H., Kirsch J., Laube B., Betz H., and Kuhse J. (1996). The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region. Proc. Natl. Acad. Sci. USA. 93, 6031-6036
Hollmann, M., Boulter, J., Maron, C., Beasley, L., Sullivan, J., Pecht, G.., and Heinemann, S. ( 1993 ). Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor. Neuron 10, 943-954.
Hollmann, M., and Heinemann, S. (1994). Cloned glutamate receptors. Annu. Rev. Neurosci. 17, 31-108.
Hughes, T. E. (1994). Transmembrane topology of the glutamate receptors. A tale of novel twists and turns. J. Mol. Neurosci. 95, 211-217.
Hung, A. Y., and Sheng, M. (2002). PDZ domain:structural modules for protein complex assembly. J. Biol. Chem. 277, 5699-5702.
Irie, M., Hata, Y., Takeuchi, M., Ichtchenko, K., Toyoda, A., Hirao, K., Takai, Y., Rosahl, T. W., and Südhof, T. C. (1997). Binding of neuroligin to PSD-95. Science 277, 1511-1515.
Jay, E. B., Karen, S., Christopherson, Sarah, E. C., Aaron, W. M., and David, S. B. (1996). Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein. J. Neurosci. 16, 7407-7415.
Joanne, E., Roger, B., and Erica, A. G. (1995). Correlation of two-hybrid affinity data with in vitro measurements. Mol. Cell. Biol. 15, 5820-5829.
Jonas, P., and Burnashev, N. (1995). Molecular mechanisms controlling calcium entry through AMPA-type glutamate receptor channels. Neuron. 15, 987-990.
Kim, E., Cho, K. O., Rothschild, A., and Sheng, M. ( 1996 ). Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins. Neuron 17, 103-113.
Kirson, E. D., and Yaari, Y. (1996). Synaptic NMDA receptors in developing mouse hippocampal neurones: functional properties and sensitivity to ifenprodil. J. Physiol. (Lond.). 497, 437-455.
Köhler, M., Kornau, H. C., and Seeburg, P. H. ( 1994 ). The organization of the gene for the functionally domain α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunit GluR-B. J. Biol. Chem. 269, 17367-17370.
Kornau, H. C., Schenker, L. T., Kennedy, M. B., and Seeburg, P. H. ( 1995 ). Domain interaction between NMDA receptor subunits and postsynaptic density protein
PSD-95. Science 269, 1737-1740.
Kung, S. S., Wu, Y. M., and Chow, W. Y. (1996). Characterization of two fish gutamate receptor cDNA molecules:absence of RNA editing at Q/R site. Mol. Brain. Res. 35, 119-130.
Kutsuwada, T., Kashiwabuchi, N., Mori, H., Sakimura, K., Kushuya, E., Araki, K., Meguro, H., Mashki, H., Kumanishi, T., Arakawa, M., and Mishina, M. ( 1992 ). Molecular diversity of the NMDA receptor channel. Nature 358, 36-41.
Kuryatov A., Laube B., Betz H. and Kuhse J. (1994). Mutational analysis of the glycine-binding site of the NMDA receptor: structural similarity with bacterial amino acid-binding proteins. Neuron. 12, 1291-1300.
Kuusinen, A., Arvola, M., and Keinanen, K. (1995). Molecular dissection of the agonist binding site of an AMPA receptor. EMBO J. 14, 6327-6332.
Lau, L. F., and Huganir, R. L. ( 1995 ). Differential tyrosine phosphorylation of N-methyl-D-aspartate receptor subunit. J. Biol. Chem. 270, 20036-20041.
Laube, B., Kuhse, J., and Betz, H. (1998). Evidence for a tetrameric structure of recombinant NMDA receptors. J. Neurosci. 18, 2954-2961.
Leonard, A. S., and Hell, J. W. ( 1997 ). Cyclic AMP-dependent protein kinase and protein kinase C phosphorylate N-methyl-D-aspartate receptors at different sites. J. Biol. Chem. 272, 12107-12115.
Leonard, A. S., Davare, M. A., Horne, M. C., Garner, C. C., and Hell, J. W. (1998). SAP97 is associated with the -amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit. J. Biol. Chem. 273, 19518-19524.
Leronard, A. S., Lim, I. A., Hemsworth, D. E., Horne, M. C., and Hell, J. W. (1999). Calcium/calmodulin-dependent protein kinase II is associated with the N-methyl-D-aspartate receptor. Proc. Natl. Acad. Sci. USA. 96, 3239-3244.
Li, B., and Fields, S. (1993). Identification of mutation in p53 that affect its binding to SV40 T antigen by using the yeast two-hybrid system. FASEB J. 7, 957-963.
Lynch D. R., Anegawa N. J., Verdoorn T., and Pritchett, D. B. (1994). N-methyl-D-aspartate receptors: different subunit requirements for binding of glutamate antagonists, glycine antagonists, and channel-blocking agents. Mol. Pharmacol. 45, 540-545.
Mano, I., and Teichberg, V. I. (1998). A tetrameric subunit stoichiometry for a glutamate receptor-channel complex. NeuroReport 9, 327-331.
Meguro, H., Mori, H., Araki, K., Kushiya, E., Kutsuwada, T., Yamazaki, M., Kumanishi, T., Arakawa, M., Sakimura, K., and Mishina, M. ( 1992 ). Functional characterization of a heteromeric NMDA receptor channel expressed from cloned cDNAs. Nature 357, 70-74.
Mehta, S., Wu, H., Garner, C. C., and Marshall, J. (2001). Molecular mechanism regulating differential association of Kainate receptor subunit with SAP90/PSD-95 and SAP97. J. Biol. Chem. 276, 16092-16099.
Monyer, H., Sprengel, R., Schoepfer, R., Herb, A., Higuchi, M., Lomeli, H., Burnashev, N., Sakamann, B., and Seeburg, P. H. ( 1992 ). Heteromeric NMDA receptor: molecular and functional distinction of subtypes. Science 256, 1217-1221.
Monyer, H., Burnashev, N., Laurie, D. J., Sakmann, B., and Seeburg, P. H. (1994). Developmental and regional expression in the rat brain and functional properties of four NMDA receptors. Neuron 12, 529-540.
Moon, I. S., Apperson, M. L., and Kennedy, M. B. ( 1994 ). The major tyrosine phosphorylated protein in the postsynaptic density fraction is N-methyl-D-aspartate receptor subunit 2B. Proc. Natl. Acad. Sci. USA 91, 3954-3958.
Mori, H., Manabe, T., Watanabe, M., Sath, Y., and Suzuki, N. (1998). Role of the carboxy-terminal region of the GluR epsilon2 subunit in synaptic localization of the NMDA receptor channel. Neuron 21, 571-580.
Moriyoshi, K., Masayuki, M., Ishii, T., Shigemoto, R., Mizuno, N., and Nakanish, S. ( 1991 ). Molecular cloning and characterization of the rat NMDA receptor. Nature 354, 31-37.
Müller, B. M., Kistner, U., Kindler, S., Chung, W. J., Kuhlendahl, S., Fenster, S. D., Lau, L. F., Veh, R. W., Huganir, R. L., Gundelfinger, E. D., and Garner, C. C. ( 1996 ). SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo. Neuron 17, 255-265.
Munk, M. D., Garcia, K. S., Medina, J. F., and Steele, P. M. (1998). Dose cerebellar LTD mediate motor learning?Toeard a resolation without a smorking gun. Neuron 20, 359-362.
Niethammer, M., Kim, E., and Sheng, M. ( 1996 ). Interaction between the C-terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinase. J. Neurosci. 16, 2157-2163.
Nishimune, A., Isaac, J. T. R., Molnar, E., Noel, J., Nash, S. R., Tagaya, M.,
Collingridge, G. L., Nakanishi, S., and Henley, J. M. ( 1998 ). NSF binding to GluR2 regulates synaptic transmission. Neuron 21, 87-97.
Omkumar, R. V., Kiely, M. J., Rosenstein, A. J., Min, K. T., and Kennedy M. B. ( 1996 ). Identification of a phosphorylation site for calcium/ calmodulin dependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor. J. Biol. Chem. 271, 31670-31678.
Osten, P., Srivastava, S., Inman, G. J., Vilim, F. S., Khatri, L., Lee, L. M., States, B. A., Einheber, S., Milner, T. A., Hanson, P. I., and Ziff, E. B. ( 1998 ). The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and a- and b-SNAPs. Neuron 21, 99-110.
Osten, P., Khatri, L., Köhr, G., Giese, G., Daly, C., Schulz, T. W., Wensky, A., Lee, L. M., and Ziff, E. B. ( 2000 ). Mutagenesis reveals a role for ABP/ GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor. Neuron 27, 313-325.
Prasher, D. C., Echenrode, V. K., Ward, W. W., Prendergast, F. G., and Cormier, M. J. (1992). Primary structure of the Aequorea victoria green fluorescent protein. Gene 111, 229-233.
Rosenmund, C., Stern-Bach, Y., and Stevens, C. F. (1998). The tetrameric structure of a glutamate receptor channel. Science 280, 1596-1599.
Sambrook, J., Fristsch, E. F., and Maniatis, T. (1989). Molecular cloning:a laboratory manual.(Colding Spring Harbor. New York. Cold Spring Harbor Laboratory).
Schiffer, H. H., Swanson, G. T., and Heinemann, S. F. ( 1997 ). Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional kainate receptor subunits with a low sensitivity to glutamate. Neuron 19, 1141-1146.
Seeburg, P. H. (1993). The TINS/TiPS Lecture. The molecular biology of mammalian glutamate receptor channels. Trends Neurosci. 16, 359-365.
Shen, L., Liang, F., Walensky, L. D., and Huganir, R. L. (2000). Regulation of AMPA receptor GluR1 subunit surface expression by a 4.1N-linked actin cytoskeletal association. J. Neurosci. 20, 7932-7940.
Sheng, M., Cummings, J., Roldan, L. A., Jan, Y. N., and Jan, L. Y. (1994). Changing subunit composition of heteromeric NMDA receptors during development of rat cortex. Nature 368, 144-147.
Sheng, M., and Pak, D. T. S. (2000). Ligand-gated ion channel interactions with cytoskeletal and signaling proteins. Annu. Rev. Physiol. 62, 755-778
Sheng, M., and Lee, S. H. (2001). AMPA receptor trafficking and the control of synaptic transmission. Cell 105, 825-828.
Sheng, M., and Sala, C. (2001). PDZ domain and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29.
Smith, D. B., and Johnson, K. S. (1988). Single-step purification of polypeptides expressed in Eshcherichia coli. As fusion with glutathione-S-transferase. Gene 67, 31-40.
Sommer, B., and Seeburg, P. H. ( 1992 ). Glutamate receptor channels-novel properties and new clones. Trend Pharmacol. Sci. 13, 291-296.
Song, I., Kamboj, S., Xia, J., Dong, H., Liao, D., and Huganir, R. L. ( 1998 ). Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors. Neuron 21, 393-400.
Sprengel, R., Suchanek, B., Amico, C., Brusa, R., and Burnasheve, N. (1998). Importance of the intracellular domain NR2 subunit for NMDA receptor function in vivo. Cell 92, 279-289
Srivastava, S., Osten, P., Vilim, F. S., Khatri, L., Inman, G. J., States, B., Daly, C., DeSouza, S., Abagyan, R., and Valtschanoff, J. G.. ( 1998 ). Novel anchorage of GluR2/ GluR3 to the postsynaptic density by the AMPA receptor binding protein ABP. Neuron 21, 581-591.
Sucher, N. J., Akbarian, S., Chi, C. L., Leclerc, C. L., Awobuluyi, M., Deitcher, D. L., Wu, M. K., Yuan, J. P., Jones, E. G.., and Lipton, S. A. ( 1995 ). Developmental and regional expression pattern of a novel NMDA receptor-like subunit ( NMDAR-L ) in the rodent brain. J. Neurosci. 15, 6509-6520.
Sun, L., Shipley, M. T., and Lidow, M. S. (2000). Expression of NR1, NR2AD, and NR3 Subunits of the NMDA receptor in the cerebral cortex and olfactory bulb of adult rat. Synapse 35, 212-221.
Tavalin , S. J., Marcie, C., Johannes, W. H., Lorene, K. L., Richard, L. H., and
John, D. S. (2002). Regulation of GluR1 by the A-Kinase Anchoring Protein 79
(AKAP79) signaling complex shares properties with Long-Term
Depression. J. Neurosci. 22, 3041-3051.
Tingley, W. G., Roche, K. W., Thompson, A. K., and Huganir, R. L. ( 1993 ). Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. Nature 364, 70-73.
Wafford, K., Kathoria, M., Bain, C. J., Marshall, G., LeBourdelles, B., Kemp, J. A., and Whiting, P. J. (1995). Indentification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site. Mol. Pharmacol. 47, 374-380.
Wang, Y. H., Bosy, T. Z., Yasuda, R. P., Grayson, D. R., Vicini, S., Pizzorusso, T., and Wolfe, B. B. (1995). Characterization of NMDA receptor subunit specific antibodies: distribution of NR2A and NR2B receptor subunits in rat brain and ontogenic profile in the cerebellum. J. Neurochem. 65, 176-183.
Watkins, J. C., and Evans, R. H. (1981). Excitatory amino acid transmitters. Annu. Rev. Pharmacol. Toxicol. 21, 165-204.
Wenthold, R. J., Petralia, R. S., Blahos, J. II., and Niedzielski, A. S. (1996). Evidence for multiple AMPA receptor complexes in hippocampal CA1/CA2 neurons. J. Neurosci. 16, 1982-1989.
Wu, Y. M., Kung, S. S., Chen, J. C., and Chow, W. Y. (1996). Molecular analysis of cDNA molecules encoding glutamate receptors of Oreochromis mossambicus. DNA cell. Biol. 9, 717-725.
Wu, H., Nash, J. E., Zamorano, P., and Garner, P. P. (2002). Interaction of SAP97 with minus-end directed actin motor myosin VI: implications for AMPA receptor trafficking. J. Biol. Chem. In press.
Wyszynski, M., Kharazia, V., Shanghvi, R., Rao, A., and Beggs, A. H. (1998). Differential regional expression and ultra-structure localization of alpha-actinin-2, a putative NMDA receptor-anchoring protein, in rat brain. J. Neurosci. 18, 1383-1392.
Wyszynski, M., Kim, E., Dunah, A. W., Passafrao, M., Valtschanoff, J. G., Serra-Page`s, C., Streuli, M., and Weinberg, R. J. (2002). Interaction between GRIP and Liprin-α /SYD2 is required for AMPA receptor targeting. Neuron 34, 39-52.
Xia, J., Zhang, X., Staudinger, J., and Huganir, R. L. ( 1999 ). Clustering of AMPA receptors by the synaptic PDZ-containing protein PICKI. Neuron 22, 179-187.
Ye, B., Liao, D., Zhang, P., Dong, H., and Huganir, R. L. ( 2000 ). GRASPI: a neuronal rasGEF associated with the AMPA receptor/ GRIP complex. Neuron 26, 603-617.
Zhong, J., Carrozza, D. P., Williams, K., Pritchett, D. B., and Molinoff, P. B. (1995). Expression of mRNAs encoding subunits of the NMDA receptor in developing rat brain. J. Neurochem. 64, 531-539.
Zervous, A. S., Gyuris, J., and Brent, R. (1993). Mxil, a protein that specifically interact with Max to bind Myc-Max recognition sites. Cell 72, 223-232.
Zukin, R. S., and Bennett, M. V. L. (1995). Alternatively spliced isoforms of the NMDARI receptor subunit. Trends Neurosci. 18, 306-313.
吳怡宓 ( 1998 ) 吳郭魚麩氨酸受器cDNA之選殖及受器基因於發育不同時期表現之研究。清華大學輻射生物研究所博士論文。
徐玉君(1995)吳郭魚魚腦麩胺酸受器cDNA(fGluR3α)的選殖與分析。清華大學輻射生物研究所碩士論文。

QRCODE
 
 
 
 
 
                                                                                                                                                                                                                                                                                                                                                                                                               
第一頁 上一頁 下一頁 最後一頁 top