메뉴 건너뛰기




Volumn 10, Issue 10, 2011, Pages

A study of the spatial protein organization of the postsynaptic density isolated from porcine cerebral cortex and cerebellum

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ALPHA TUBULIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CROSS LINKING REAGENT; CYTOSKELETON PROTEIN; ELONGATION FACTOR 1ALPHA; GLUTAMATE RECEPTOR; MICROTUBULE ASSOCIATED PROTEIN; POSTSYNAPTIC DENSITY PROTEIN 95; SCAFFOLD PROTEIN; TUBULIN;

EID: 80054047449     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M110.007138     Document Type: Article
Times cited : (9)

References (96)
  • 2
    • 0018190342 scopus 로고
    • Form of the postsynaptic density. A serial section study
    • Cohen, R. S., and Siekevitz, P. (1978) Form of the postsynaptic density. A serial section study. J. Cell Biol. 78, 36-46 (Pubitemid 8369890)
    • (1978) Journal of Cell Biology , vol.78 , Issue.1 , pp. 36-46
    • Cohen, R.S.1    Siekevitz, P.2
  • 4
    • 0023485105 scopus 로고
    • Substructure in the postsynaptic density of Purkinje cell dendritic spines revealed by rapid freezing and etching
    • DOI 10.1002/syn.890010607
    • Landis, D. M., Weinstein, L. A., and Reese, T. S. (1987) Substructure in the postsynaptic density of Purkinje cell dendritic spines revealed by rapid freezing and etching. Synapse 1, 552-558 (Pubitemid 18007835)
    • (1987) Synapse , vol.1 , Issue.6 , pp. 552-558
    • Landis, D.M.D.1    Weinstein, L.A.2    Reese, T.S.3
  • 5
    • 0033604506 scopus 로고    scopus 로고
    • LTP promotes formation of multiple spine synapses between a single axon terminal and a dendrite
    • Toni, N., Buchs, P. A., Nikonenko, I., Bron, C. R., and Muller, D. (1999) LTP promotes formation of multiple spine synapses between a single axon terminal and a dendrite. Nature 402, 421-425 (Pubitemid 129544831)
    • (1999) Nature , vol.402 , Issue.6760 , pp. 421-425
    • Toni, N.1    Buchs, P.-A.2    Nikonenko, I.3    Bron, C.R.4    Muller, D.5
  • 6
    • 0038285449 scopus 로고    scopus 로고
    • Synaptic plasticity and dynamic modulation of the postsynaptic membrane
    • DOI 10.1038/75714
    • Lüscher, C., Nicoll, R. A., Malenka, R. C., and Muller, D. (2000) Synaptic plasticity and dynamic modulation of the postsynaptic membrane. Nat. Neurosci. 3, 545-550 (Pubitemid 30332072)
    • (2000) Nature Neuroscience , vol.3 , Issue.6 , pp. 545-550
    • Luscher, C.1    Nicoll, R.A.2    Malenka, R.C.3    Muller, D.4
  • 9
    • 0034810292 scopus 로고    scopus 로고
    • Rapid formation and remodeling of postsynaptic densities in developing dendrites
    • DOI 10.1038/nn717
    • Marrs, G. S., Green, S. H., and Dailey, M. E. (2001) Rapid formation and remodeling of postsynaptic densities in developing dendrites. Nat. Neurosci. 4, 1006-1013 (Pubitemid 32924140)
    • (2001) Nature Neuroscience , vol.4 , Issue.10 , pp. 1006-1013
    • Marrs, G.S.1    Green, S.H.2    Dailey, M.E.3
  • 10
    • 0035923749 scopus 로고    scopus 로고
    • Inactivity produces increases in neurotransmitter release and synapse size
    • DOI 10.1016/S0896-6273(01)00500-1
    • Murthy, V. N., Schikorski, T., Stevens, C. F., and Zhu, Y. (2001) Inactivity produces increases in neurotransmitter release and synapse size. Neuron 32, 673-682 (Pubitemid 33145200)
    • (2001) Neuron , vol.32 , Issue.4 , pp. 673-682
    • Murthy, V.N.1    Schikorski, T.2    Stevens, C.F.3    Zhu, Y.4
  • 11
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers, M. D. (2003) Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nat. Neurosci. 6, 231-242
    • (2003) Nat. Neurosci. , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 12
    • 3142647940 scopus 로고
    • The postsynaptic density: A possible role in long-lasting effects in the central nervous system
    • Siekevitz, P. (1985) The postsynaptic density: a possible role in long-lasting effects in the central nervous system. Proc. Natl. Acad. Sci. U.S.A. 82, 3494-3498
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 3494-3498
    • Siekevitz, P.1
  • 13
    • 0031442806 scopus 로고    scopus 로고
    • Enlightening the postsynaptic density
    • Ziff, E. B. (1997) Enlightening the postsynaptic density. Neuron 19, 1163-1174
    • (1997) Neuron , vol.19 , pp. 1163-1174
    • Ziff, E.B.1
  • 14
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy, M. B. (2000) Signal-processing machines at the postsynaptic density. Science 290, 750-754
    • (2000) Science , vol.290 , pp. 750-754
    • Kennedy, M.B.1
  • 15
    • 0017396421 scopus 로고
    • The structure of postsynaptic densities isolated from dog cerebral cortex. I. Overall morphology and protein composition
    • Cohen, R. S., Blomberg, F., Berzins, K., and Siekevitz, P. (1977) The structure of postsynaptic densities isolated from dog cerebral cortex. I. Overall morphology and protein composition. J. Cell Biol. 74, 181-203 (Pubitemid 8141493)
    • (1977) Journal of Cell Biology , vol.74 , Issue.1 , pp. 181-203
    • Cohen, R.S.1    Blomberg, F.2    Berzins, K.3    Siekevitz, P.4
  • 16
    • 0017408222 scopus 로고
    • The structure of postsynaptic densities isolated from dog cerebral cortex. II. Characterization and arrangement of some of the major proteins within the structure
    • Blomberg, F., Cohen, R. S., and Siekevitz, P. (1977) The structure of postsynaptic densities isolated from dog cerebral cortex. II. Characterization and arrangement of some of the major proteins within the structure. J. Cell Biol. 74, 204-225 (Pubitemid 8141494)
    • (1977) Journal of Cell Biology , vol.74 , Issue.1 , pp. 204-225
    • Blomberg, F.1    Cohen, R.C.2    Siekevitz, P.3
  • 17
    • 0019134836 scopus 로고
    • Isolation and characterization of postsynaptic densities from various brain regions: Enrichment of different types of postsynaptic densities
    • Carlin, R. K., Grab, D. J., Cohen, R. S., and Siekevitz, P. (1980) Isolation and characterization of postsynaptic densities from various brain regions: enrichment of different types of postsynaptic densities. J. Cell Biol. 86, 831-845
    • (1980) J. Cell Biol. , vol.86 , pp. 831-845
    • Carlin, R.K.1    Grab, D.J.2    Cohen, R.S.3    Siekevitz, P.4
  • 18
    • 0032692291 scopus 로고    scopus 로고
    • Interprotein disulfide bonds formed during isolation process tighten the structure of the postsynaptic density
    • Lai, S. L., Chiang, S. F., Chen, I. T., Chow, W. Y., and Chang, Y. C. (1999) Interprotein disulfide bonds formed during isolation process tighten the structure of the postsynaptic density. J. Neurochem. 73, 2130-2138
    • (1999) J. Neurochem. , vol.73 , pp. 2130-2138
    • Lai, S.L.1    Chiang, S.F.2    Chen, I.T.3    Chow, W.Y.4    Chang, Y.C.5
  • 19
    • 0026651939 scopus 로고
    • The postsynaptic density: Constituent and associated proteins characterized by electrophoresis, immunoblotting, and peptide sequencing
    • Walsh, M. J., and Kuruc, N. (1992) The postsynaptic density: constituent and associated proteins characterized by electrophoresis, immunoblotting, and peptide sequencing. J. Neurochem. 59, 667-678
    • (1992) J. Neurochem. , vol.59 , pp. 667-678
    • Walsh, M.J.1    Kuruc, N.2
  • 21
    • 0036195888 scopus 로고    scopus 로고
    • Identification of activity-regulated proteins in the postsynaptic density fraction
    • DOI 10.1046/j.1356-9597.2001.00505.x
    • Satoh, K., Takeuchi, M., Oda, Y., Deguchi-Tawarada, M., Sakamoto, Y., Matsubara, K., Nagasu, T., and Takai, Y. (2002) Identification of activityregulated proteins in the postsynaptic density fraction. Genes Cells 7, 187-197 (Pubitemid 34213363)
    • (2002) Genes to Cells , vol.7 , Issue.2 , pp. 187-197
    • Satoh, K.1    Takeuchi, M.2    Oda, Y.3    Deguchi-Tawarada, M.4    Sakamoto, Y.5    Matsubara, K.6    Nagasu, T.7    Takai, Y.8
  • 23
    • 0942287657 scopus 로고    scopus 로고
    • Molecular constituents of the postsynaptic density fraction revealed by proteomic analysis using multidimensional liquid chromatography-tandem mass spectrometry
    • DOI 10.1046/j.1471-4159.2003.02136.x
    • Yoshimura, Y., Yamauchi, Y., Shinkawa, T., Taoka, M., Donai, H., Takahashi, N., Isobe, T., and Yamauchi, T. (2004) Molecular constituents of the postsynaptic density fraction revealed by proteomic analysis using multidimensional liquid chromatography-tandem mass spectrometry. J. Neurochem. 88, 759-768 (Pubitemid 38140219)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.3 , pp. 759-768
    • Yoshimura, Y.1    Yamauchi, Y.2    Shinkawa, T.3    Taoka, M.4    Donai, H.5    Takahashi, N.6    Isobe, T.7    Yamauchi, T.8
  • 24
    • 2442683994 scopus 로고    scopus 로고
    • Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry
    • DOI 10.1074/jbc.M400103200
    • Peng, J., Kim, M. J., Cheng, D., Duong, D. M., Gygi, S. P., and Sheng, M. (2004) Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry. J. Biol. Chem. 279, 21003-21011 (Pubitemid 38656501)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 21003-21011
    • Peng, J.1    Kim, M.J.2    Cheng, D.3    Duong, D.M.4    Gygi, S.P.5    Sheng, M.6
  • 28
    • 24044487619 scopus 로고    scopus 로고
    • Determination of absolute protein numbers in single synapses by a GFP-based calibration technique
    • DOI 10.1038/nmeth783
    • Sugiyama, Y., Kawabata, I., Sobue, K., and Okabe, S. (2005) Determination of absolute protein numbers in single synapses by a GFP-based calibration technique. Nat. Methods 2, 677-684 (Pubitemid 41223094)
    • (2005) Nature Methods , vol.2 , Issue.9 , pp. 677-684
    • Sugiyama, Y.1    Kawabata, I.2    Sobue, K.3    Okabe, S.4
  • 30
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: A more quantitative view
    • Sheng, M., and Hoogenraad, C. C. (2007) The postsynaptic architecture of excitatory synapses: a more quantitative view. Annu. Rev. Biochem. 76, 823-847
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 31
    • 33646937404 scopus 로고    scopus 로고
    • Comprehensive identification of phosphorylation sites in postsynaptic density preparations
    • DOI 10.1074/mcp.T500041-MCP200
    • Trinidad, J. C., Specht, C. G., Thalhammer, A., Schoepfer, R., and Burlingame, A. L. (2006) Comprehensive identification of phosphorylation sites in postsynaptic density preparations. Mol. Cell. Proteomics 5, 914-922 (Pubitemid 43792800)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.5 , pp. 914-922
    • Trinidad, J.C.1    Specht, C.G.2    Thalhammer, A.3    Schoepfer, R.4    Burlingame, A.L.5
  • 34
    • 62649083636 scopus 로고    scopus 로고
    • Densin-180: Revised membrane topology, domain structure and phosphorylation status
    • Thalhammer, A., Trinidad, J. C., Burlingame, A. L., and Schoepfer, R. (2009) Densin-180: revised membrane topology, domain structure and phosphorylation status. J. Neurochem. 109, 297-302
    • (2009) J. Neurochem. , vol.109 , pp. 297-302
    • Thalhammer, A.1    Trinidad, J.C.2    Burlingame, A.L.3    Schoepfer, R.4
  • 35
    • 0033946468 scopus 로고    scopus 로고
    • Proteomic analysis of NMDA receptor-adhesion protein signaling complexes
    • DOI 10.1038/76615
    • Husi, H., Ward, M. A., Choudhary, J. S., Blackstock, W. P., and Grant, S. G. (2000) Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat. Neurosci. 3, 661-669 (Pubitemid 30437200)
    • (2000) Nature Neuroscience , vol.3 , Issue.7 , pp. 661-669
    • Husi, H.1    Ward, M.A.2    Choudhary, J.S.3    Blackstock, W.P.4    Grant, S.G.N.5
  • 36
    • 5444257565 scopus 로고    scopus 로고
    • Proteomic analysis of native metabotropic glutamate receptor 5 protein complexes reveals novel molecular constituents
    • DOI 10.1111/j.1471-4159.2004.02735.x
    • Farr, C. D., Gafken, P. R., Norbeck, A. D., Doneanu, C. E., Stapels, M. D., Barofsky, D. F., Minami, M., and Saugstad, J. A. (2004) Proteomic analysis of native metabotropic glutamate receptor 5 protein complexes reveals novel molecular constituents. J. Neurochem. 91, 438-450 (Pubitemid 39363443)
    • (2004) Journal of Neurochemistry , vol.91 , Issue.2 , pp. 438-450
    • Farr, C.D.1    Gafken, P.R.2    Norbeck, A.D.3    Doneanu, C.E.4    Stapels, M.D.5    Barofsky, D.F.6    Minami, M.7    Saugstad, J.A.8
  • 37
  • 39
    • 0348010289 scopus 로고    scopus 로고
    • 2+/ Calmodulin-Dependent Protein Kinase II at the PSD
    • Petersen, J. D., Chen, X., Vinade, L., Dosemeci, A., Lisman, J. E., and Reese, T. S. (2003) Distribution of postsynaptic density (PSD)-95 and Ca2+/calmodulin-dependent protein kinase II at the PSD. J. Neurosci. 23, 11270-11278 (Pubitemid 37548963)
    • (2003) Journal of Neuroscience , vol.23 , Issue.35 , pp. 11270-11278
    • Petersen, J.D.1    Chen, X.2    Vinade, L.3    Dosemeci, A.4    Lisman, J.E.5    Reese, T.S.6
  • 40
    • 0035865546 scopus 로고    scopus 로고
    • Laminar organization of the NMDA receptor complex within the postsynaptic density
    • Valtschanoff, J. G., and Weinberg, R. J. (2001) Laminar Organization of the NMDA Receptor Complex within the Postsynaptic Density. J. Neurosci. 21, 1211-1217 (Pubitemid 32140480)
    • (2001) Journal of Neuroscience , vol.21 , Issue.4 , pp. 1211-1217
    • Valtschanoff, J.G.1    Weinberg, R.J.2
  • 43
    • 0021099455 scopus 로고
    • Structural organization of filamentous proteins in postsynaptic density
    • Ratner, N., and Mahler, H. R. (1983) Structural organization of filamentous proteins in postsynaptic density. Biochemistry 22, 2446-2453
    • (1983) Biochemistry , vol.22 , pp. 2446-2453
    • Ratner, N.1    Mahler, H.R.2
  • 44
    • 33745617861 scopus 로고    scopus 로고
    • Studying the Protein Organization of the Postsynaptic Density by a Novel Solid Phase- and Chemical Cross-linking-based Technology
    • Liu, S. H., Cheng, H. H., Huang, S. Y., Yiu, P. C., and Chang, Y. C. (2006) Studying the Protein Organization of the Postsynaptic Density by a Novel Solid Phase- and Chemical Cross-linking-based Technology. Mol. Cell. Proteomics 5, 1019-1032
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1019-1032
    • Liu, S.H.1    Cheng, H.H.2    Huang, S.Y.3    Yiu, P.C.4    Chang, Y.C.5
  • 45
    • 0026553732 scopus 로고
    • A novel photoactivatable crosslinker for the functionally-directed region-specific fluorescent labeling of proteins
    • Thevenin, B. J., Shahrokh, Z., Williard, R. L., Fujimoto, E. K., Kang, J. J., Ikemoto, N., and Shohet, S. B. (1992) A novel photoactivatable crosslinker for the functionally-directed region-specific fluorescent labeling of proteins. Eur. J. Biochem. 206, 471-477
    • (1992) Eur. J. Biochem. , vol.206 , pp. 471-477
    • Thevenin, B.J.1    Shahrokh, Z.2    Williard, R.L.3    Fujimoto, E.K.4    Kang, J.J.5    Ikemoto, N.6    Shohet, S.B.7
  • 46
    • 55849128881 scopus 로고    scopus 로고
    • A novel solid phase- and chemical crosslinking-based technology for determining protein localization in biological supramolecules
    • Horng, W. C., Yen, Y. H., and Chang, Y. C. (2008) A novel solid phase- and chemical crosslinking-based technology for determining protein localization in biological supramolecules. Proteomics 8, 4642-4646
    • (2008) Proteomics , vol.8 , pp. 4642-4646
    • Horng, W.C.1    Yen, Y.H.2    Chang, Y.C.3
  • 47
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range
    • Udenfriend, S., Stein, S., Böhlen, P., Dairman, W., Leimgruber, W., and Weigele, M. (1972) Fluorescamine: A reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science 178, 871-872
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Böhlen, P.3    Dairman, W.4    Leimgruber, W.5    Weigele, M.6
  • 48
    • 0034622296 scopus 로고    scopus 로고
    • A convenient and scaleable procedure for removing the Fmoc group in solution
    • PII S0040403900008534
    • Sheppeck, J. E., Kar, H., and Hong, H. (2000) A convenient and scaleable procedure for removing the Fmoc group in solution. Tetrahedron Letters 41, 5329-5333 (Pubitemid 30450788)
    • (2000) Tetrahedron Letters , vol.41 , Issue.28 , pp. 5329-5333
    • Sheppeck II, J.E.1    Kar, H.2    Hong, H.3
  • 49
    • 76549252207 scopus 로고
    • The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling, L., Corey, R. B., and Branson, H. R. (1951) The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl. Acad. Sci. U.S.A. 37, 205-211
    • (1951) Proc. Natl. Acad. Sci. U.S.A. , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 50
    • 0030298538 scopus 로고    scopus 로고
    • Chemically modifying glass surfaces to study substratum-guided neurite outgrowth in culture
    • DOI 10.1016/S0165-0270(96)00052-0, PII S0165027096000520
    • Matsuzawa, M., Liesi, P., and Knoll, W. (1996) Chemically modifying glass surfaces to study substratum-guided neurite outgrowth in culture. J. Neurosci. Methods 69, 189-196 (Pubitemid 26377777)
    • (1996) Journal of Neuroscience Methods , vol.69 , Issue.2 , pp. 189-196
    • Matsuzawa, M.1    Liesi, P.2    Knoll, W.3
  • 51
    • 0020021878 scopus 로고
    • [18] Purification of muscle actin
    • Dixie W. Frederiksen, L. W. C., ed. Academic Press
    • Pardee, J. D., and Aspudich, J. (1982) [18] Purification of muscle actin. In: Dixie W. Frederiksen, L. W. C., ed. Methods in Enzymology, pp. 164-181, Academic Press
    • (1982) Methods in Enzymology , pp. 164-181
    • Pardee, J.D.1    Aspudich, J.2
  • 52
    • 0020445435 scopus 로고
    • A one-step purification of membrane proteins using a high efficiency immunomatrix
    • Schneider, C., Newman, R. A., Sutherland, D. R., Asser, U., and Greaves, M. F. (1982) A one-step purification of membrane proteins using a high efficiency immunomatrix. J. Biol. Chem. 257, 10766-10769 (Pubitemid 13210653)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.18 , pp. 10766-10769
    • Schneider, C.1    Newman, R.A.2    Sutherland, D.R.3
  • 53
    • 0942287183 scopus 로고    scopus 로고
    • Use of Immunomatrix Methods to Improve Protein-Protein Interaction Detection
    • DOI 10.1155/S1110724303209256
    • Qoronfleh, M. W., Ren, L., Emery, D., Perr, M., and Kaboord, B. (2003) Use of immunomatrix methods to improve protein-protein interaction detection. J. Biomed. Biotechnol. 2003 (5), 291-298 (Pubitemid 38140637)
    • (2003) Journal of Biomedicine and Biotechnology , vol.2003 , Issue.5 , pp. 291-298
    • Qoronfleh, M.W.1    Ren, L.2    Emery, D.3    Perr, M.4    Kaboord, B.5
  • 54
    • 38449094436 scopus 로고    scopus 로고
    • Studying the protein-protein interactions in the postsynaptic density by means of immunoabsorption and chemical crosslinking
    • Chang, C. W., Peng, S. C., Cheng, W. Y., Liu, S. H., Cheng, H. H., Huang, S. Y., and Chang, Y. C. (2007) Studying the protein-protein interactions in the postsynaptic density by means of immunoabsorption and chemical crosslinking. Proteomics 1, 1499-1512
    • (2007) Proteomics , vol.1 , pp. 1499-1512
    • Chang, C.W.1    Peng, S.C.2    Cheng, W.Y.3    Liu, S.H.4    Cheng, H.H.5    Huang, S.Y.6    Chang, Y.C.7
  • 55
    • 0014949207 scopus 로고
    • Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 56
    • 0029989334 scopus 로고    scopus 로고
    • A study of the oligomeric state of the alpha-amino-3-hydroxy-5-methyl-4- isoxazolepropionic acid-preferring glutamate receptors in the synaptic junctions of porcine brain
    • Wu, T. Y., Liu, C. I., and Chang, Y. C. (1996) A study of the oligomeric state of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-preferring glutamate receptors in the synaptic junctions of porcine brain. Biochem. J. 319, 731-739
    • (1996) Biochem. J. , vol.319 , pp. 731-739
    • Wu, T.Y.1    Liu, C.I.2    Chang, Y.C.3
  • 57
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., Boulikas, T., Wray, V. P., and Hancock, R. (1981) Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118, 197-203
    • (1981) Anal. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 62
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • DOI 10.1146/annurev.neuro.24.1.1
    • Sheng, M., and Sala, C. (2001) PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29 (Pubitemid 32695221)
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 63
    • 0032219588 scopus 로고    scopus 로고
    • Elongation factor-1alpha stabilizes microtubules in a calcium/calmodulin- dependent manner
    • DOI 10.1002/(SICI)1097-0169(1998)41:2<168::AID-CM7>3.0.CO;2-A
    • Moore, R. C., Durso, N. A., and Cyr, R. J. (1998) Elongation factor-1αstabilizes microtubules in a calcium/calmodulin-dependent manner. Cell Motility Cytoskeleton 41, 168-180 (Pubitemid 29071297)
    • (1998) Cell Motility and the Cytoskeleton , vol.41 , Issue.2 , pp. 168-180
    • Moore, R.C.1    Durso, N.A.2    Cyr, R.J.3
  • 64
    • 26944487335 scopus 로고    scopus 로고
    • Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology
    • DOI 10.1038/nsmb979, PII NSMB979
    • Gross, S. R., and Kinzy, T. G. (2005) Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nat. Struct. Mol. Biol. 12, 772-778 (Pubitemid 43086251)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.9 , pp. 772-778
    • Gross, S.R.1    Kinzy, T.G.2
  • 65
    • 3242657356 scopus 로고    scopus 로고
    • Presence of translation elongation factor-1A (eEF1A) in the excitatory postsynaptic density of rat cerebral cortex
    • DOI 10.1016/j.neulet.2004.05.036, PII S0304394004005658
    • Cho, S. J., Jung, J. S., Ko, B. H., Jin, I., and Moon, I. S. (2004) Presence of translation elongation factor-1A (eEF1A) in the excitatory postsynaptic density of rat cerebral cortex. Neurosci. Lett. 366, 29-33 (Pubitemid 38953142)
    • (2004) Neuroscience Letters , vol.366 , Issue.1 , pp. 29-33
    • Cho, S.-J.1    Jung, J.-S.2    Ko, B.H.3    Jin, I.4    Moon, I.S.5
  • 66
    • 0035139220 scopus 로고    scopus 로고
    • The neuronal Rho-GEF Kalirin-7 interacts with PDZ domain-containing proteins and regulates dendritic morphogenesis
    • DOI 10.1016/S0896-6273(01)00193-3
    • Penzes, P., Johnson, R. C., Sattler, R., Zhang, X., Huganir, R. L., Kambampati, V., Mains, R. E., and Eipper, B. A. (2001) The neuronal Rho-GEF Kalirin-7 interacts with PDZ domain-containing proteins and regulates dendritic morphogenesis. Neuron 29, 229-242 (Pubitemid 32108735)
    • (2001) Neuron , vol.29 , Issue.1 , pp. 229-242
    • Penzes, P.1    Johnson, R.C.2    Sattler, R.3    Zhang, X.4    Huganir, R.L.5    Kambampati, V.6    Mains, R.E.7    Eipper, B.A.8
  • 67
    • 0033566873 scopus 로고    scopus 로고
    • Nitric oxide acts as a postsynaptic signaling molecule in calcium/calmodulin-induced synaptic potentiation in hippocampal CA1 pyramidal neurons
    • Ko, G. Y., and Kelly, P. T. (1999) Nitric Oxide Acts as a Postsynaptic Signaling Molecule in Calcium/Calmodulin-Induced Synaptic Potentiation in Hippocampal CA1 Pyramidal Neurons. J. Neurosci. 19, 6784-6794 (Pubitemid 29380107)
    • (1999) Journal of Neuroscience , vol.19 , Issue.16 , pp. 6784-6794
    • Ko, G.Y.1    Kelly, P.T.2
  • 68
    • 0028307255 scopus 로고
    • Hydrodynamic and pharmacological characterization of putative alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/kainate-sensitive L-glutamate receptors solubilized from pig brain
    • Wu, T. Y., and Chang, Y. C. (1994) Hydrodynamic and pharmacological characterization of putative alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid/kainate-sensitive L-glutamate receptors solubilized from pig brain. Biochem. J. 300, 365-371
    • (1994) Biochem. J. , vol.300 , pp. 365-371
    • Wu, T.Y.1    Chang, Y.C.2
  • 69
    • 0032523002 scopus 로고    scopus 로고
    • Evidence for a tetrameric structure of recombinant NMDA receptors
    • Laube, B., Kuhse, J., and Betz, H. (1998) Evidence for a tetrameric structure of recombinant NMDA receptors. J. Neurosci. 18, 2954-2961 (Pubitemid 28163225)
    • (1998) Journal of Neuroscience , vol.18 , Issue.8 , pp. 2954-2961
    • Laube, B.1    Kuhse, J.2    Betz, H.3
  • 70
    • 0032486422 scopus 로고    scopus 로고
    • The tetrameric structure of a glutamate receptor channel
    • DOI 10.1126/science.280.5369.1596
    • Rosenmund, C., Stern-Bach, Y., and Stevens, C. F. (1998) The tetrameric structure of a glutamate receptor channel. Science 280, 1596-1599 (Pubitemid 28277703)
    • (1998) Science , vol.280 , Issue.5369 , pp. 1596-1599
    • Rosenmund, C.1    Stern-Bach, Y.2    Stevens, C.F.3
  • 71
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky, A. I., Rosconi, M. P., and Gouaux, E. (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 75
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H. C., Schenker, L. T., Kennedy, M. B., and Seeburg, P. H. (1995) Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269, 1737-1740
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 76
    • 0020394540 scopus 로고
    • Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity
    • DOI 10.1083/jcb.95.1.345
    • Fifková, E., and Delay, R. J. (1982) Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity. J. Cell Biol. 95, 345-350 (Pubitemid 13197106)
    • (1982) Journal of Cell Biology , vol.95 , Issue.1 , pp. 345-350
    • Fifkova, E.1    Delay, R.I.2
  • 77
    • 0020550407 scopus 로고
    • Cytoplasmic organization in cerebellar dendritic spines
    • Landis, D. M., and Reese, T. S. (1983) Cytoplasmic organization in cerebellar dendritic spines. J. Cell Biol. 97, 1169-1178 (Pubitemid 13017113)
    • (1983) Journal of Cell Biology , vol.97 , Issue.4 , pp. 1169-1178
    • Landis, D.M.D.1    Reese, T.S.2
  • 78
    • 27444434998 scopus 로고    scopus 로고
    • Multivalent interactions of calcium/calmodulin-dependent protein kinase II with the postsynaptic density proteins NR2B, densin-180, and alpha-actinin-2
    • DOI 10.1074/jbc.M502191200
    • Robison, A. J., Bass, M. A., Jiao, Y., MacMillan, L. B., Carmody, L. C., Bartlett, R. K., and Colbran, R. J. (2005) Multivalent interactions of calcium/calmodulin-dependent protein kinase II with the postsynaptic density proteins NR2B, densin-180, and alpha-actinin-2. J. Biol. Chem. 280, 35329-35336 (Pubitemid 41532721)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35329-35336
    • Robison, A.J.1    Bass, M.A.2    Jiao, Y.3    MacMillan, L.B.4    Carmody, L.C.5    Bartlett, R.K.6    Colbran, R.J.7
  • 79
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher, A. (1991) Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol. 7, 337-374
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 80
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • Bennett, V., and Baines, A. J. (2001) Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev. 81, 1353-1392 (Pubitemid 32606672)
    • (2001) Physiological Reviews , vol.81 , Issue.3 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 81
    • 0034332508 scopus 로고    scopus 로고
    • Regulation of AMPA receptor GluR1 subunit surface expression by a 4. 1N-linked actin cytoskeletal association
    • 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
    • (2000) J. Neurosci. , vol.20 , pp. 7932-7940
    • Shen, L.1    Liang, F.2    Walensky, L.D.3    Huganir, R.L.4
  • 83
    • 0035055799 scopus 로고    scopus 로고
    • Protein 4.1 in forebrain postsynaptic density preparations: Enrichment of 4.1 gene products and detection of 4.1R binding proteins
    • DOI 10.1046/j.1432-1327.2001.01968.x
    • Scott, C., Keating, L., Bellamy, M., and Baines, A. J. (2001) Protein 4.1 in forebrain postsynaptic density preparations: enrichment of 4.1 gene products and detection of 4.1R binding proteins. Eur. J. Biochem. 268, 1084-1094 (Pubitemid 32328353)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.4 , pp. 1084-1094
    • Scott, C.1    Keating, L.2    Bellamy, M.3    Baines, A.J.4
  • 88
    • 0020059402 scopus 로고
    • Postmortem accumulation of tubulin in postsynaptic density preparations
    • Carlin, R. K., Grab, D. J., and Siekevitz, P. (1982) Postmortem accumulation of tubulin in postsynaptic density preparations. J. Neurochem. 38, 94-100 (Pubitemid 12189199)
    • (1982) Journal of Neurochemistry , vol.38 , Issue.1 , pp. 94-100
    • Carlin, R.K.1    Grab, D.J.2    Siekevitz, P.3
  • 89
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho, K. O., Hunt, C. A., and Kennedy, M. B. (1992) The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 9, 929-942
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 90
    • 0033756376 scopus 로고    scopus 로고
    • Overview on the structure, composition, function, development, and plasticity of hippocampal dendritic spines
    • Sorra, K. E., and Harris, K. M. (2000) Overview on the structure, composition, function, development, and plasticity of hippocampal dendritic spines. Hippocampus 10, 501-511
    • (2000) Hippocampus , vol.10 , pp. 501-511
    • Sorra, K.E.1    Harris, K.M.2
  • 91
    • 58149225472 scopus 로고    scopus 로고
    • Microtubules in dendritic spine development
    • Gu, J., Firestein, B. L., and Zheng, J. Q. (2008) Microtubules in dendritic spine development. J. Neurosci. 28, 12120-12124
    • (2008) J. Neurosci. , vol.28 , pp. 12120-12124
    • Gu, J.1    Firestein, B.L.2    Zheng, J.Q.3
  • 93
    • 1042284932 scopus 로고    scopus 로고
    • Protein Profiling with Cleavable Isotope-coded Affinity Tag (cICAT) Reagents
    • Li, J., Steen, H., and Gygi, S. P. (2003) Protein Profiling with Cleavable Isotope-coded Affinity Tag (cICAT) Reagents. Mol. Cell. Proteomics 2, 1198-1204
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1198-1204
    • Li, J.1    Steen, H.2    Gygi, S.P.3
  • 94
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • DOI 10.1038/nbt1001-946
    • Han, D. K., Eng, J., Zhou, H., and Aebersold, R. (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotech. 19, 946-951 (Pubitemid 32947573)
    • (2001) Nature Biotechnology , vol.19 , Issue.10 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 95
    • 0347334566 scopus 로고    scopus 로고
    • Mass Spectrometric Analysis of Protein Mixtures at Low Levels Using Cleavable 13C-Isotope-coded Affinity Tag and Multidimensional Chromatography
    • Hansen, K. C., Schmitt-Ulms, G., Chalkley, R. J., Hirsch, J., Baldwin, M. A., and Burlingame, A. L. (2003) Mass Spectrometric Analysis of Protein Mixtures at Low Levels Using Cleavable 13C-Isotope-coded Affinity Tag and Multidimensional Chromatography. Mol. Cell. Proteomics 2, 299-314
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 299-314
    • Hansen, K.C.1    Schmitt-Ulms, G.2    Chalkley, R.J.3    Hirsch, J.4    Baldwin, M.A.5    Burlingame, A.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.