메뉴 건너뛰기




Volumn 20, Issue 4, 1998, Pages 693-707

CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; TUBULIN;

EID: 0032055632     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)81009-0     Document Type: Article
Times cited : (257)

References (65)
  • 1
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • in press.
    • Allison, D.W., Gelfand, V.I., Spector, I., and Craig, A.M. (1998). Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J. Neurosci., in press.
    • (1998) J. Neurosci.
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 2
    • 0030113804 scopus 로고    scopus 로고
    • Cell signaling: MAGUK magic
    • Anderson, J.M. (1996). Cell signaling: MAGUK magic. Curr. Biol. 6, 382-384.
    • (1996) Curr. Biol. , vol.6 , pp. 382-384
    • Anderson, J.M.1
  • 3
    • 0017350927 scopus 로고
    • Rat hippocampal neurons in dispersed cell culture
    • Banker, G.A., and Cowan, W.M. (1977). Rat hippocampal neurons in dispersed cell culture. Brain Res. 126, 397-425.
    • (1977) Brain Res. , vol.126 , pp. 397-425
    • Banker, G.A.1    Cowan, W.M.2
  • 5
    • 0025279242 scopus 로고
    • Zinc finger domains: Hypotheses and current knowledge
    • Berg, J.M. (1990). Zinc finger domains: hypotheses and current knowledge. Annu. Rev. Biophys. Biophys. Chem. 19, 405-421.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 405-421
    • Berg, J.M.1
  • 6
  • 7
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and a1-syntrophin mediated by PDZ domains
    • Brenman, J.E., Chao, D.S., Gee, S.H., McGee, A.W., Craven, S.E., Santillano, D.R., Wu, Z., Huang, F., Xia, H., Peters, M.F., et al. (1996a). Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and a1-syntrophin mediated by PDZ domains. Cell 84, 757-767.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.W.4    Craven, S.E.5    Santillano, D.R.6    Wu, Z.7    Huang, F.8    Xia, H.9    Peters, M.F.10
  • 8
    • 0029959179 scopus 로고    scopus 로고
    • Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein
    • Brenman, J.E., Christopherson, K.S., Craven, S.E., McGee, A.W., and Bredt, D.S. (1996b). Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein. J. Neurosci. 16, 7407-7415.
    • (1996) J. Neurosci. , vol.16 , pp. 7407-7415
    • Brenman, J.E.1    Christopherson, K.S.2    Craven, S.E.3    McGee, A.W.4    Bredt, D.S.5
  • 9
    • 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.
    • (1982) J. Neurochem. , vol.38 , pp. 94-100
    • Carlin, R.K.1    Grab, D.J.2    Siekevitz, P.3
  • 10
    • 0010689629 scopus 로고    scopus 로고
    • Novel cystein-rich proteins in the postsynaptic densities
    • Chang, Y.-C., Chiang, S.-F., Lai, S.-L., and Sun, S.H. (1997). Novel cystein-rich proteins in the postsynaptic densities. Soc. Neurosci. 23, 578.13.
    • (1997) Soc. Neurosci. , vol.23 , pp. 57813
    • Chang, Y.-C.1    Chiang, S.-F.2    Lai, S.-L.3    Sun, S.H.4
  • 11
    • 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
  • 12
    • 0030273552 scopus 로고    scopus 로고
    • + channel kir 2.3 to PSD-95 is regulated by protein kinase a phosphorylation
    • + channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation. Neuron 17, 759-767.
    • (1996) Neuron , vol.17 , pp. 759-767
    • Cohen, N.A.1    Brenman, J.E.2    Snyder, S.3    Bredt, D.S.4
  • 13
    • 0031459588 scopus 로고    scopus 로고
    • CLIP-115, a novel brain-specific cytoplasmic linker protein, mediates the localization of dendritic lamellar bodies
    • De Zeeuw, C.I., Hoogenraad, C.C., Goedknegt, E., Hertzberg, E., Neubauer, A., Grosveld, F., and Galjart, N. (1997). CLIP-115, a novel brain-specific cytoplasmic linker protein, mediates the localization of dendritic lamellar bodies. Neuron 19, 1187-1199.
    • (1997) Neuron , vol.19 , pp. 1187-1199
    • De Zeeuw, C.I.1    Hoogenraad, C.C.2    Goedknegt, E.3    Hertzberg, E.4    Neubauer, A.5    Grosveld, F.6    Galjart, N.7
  • 14
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M., and MacKinnon, R. (1996). Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85, 1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    Mackinnon, R.6
  • 16
    • 0029589911 scopus 로고
    • Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
    • Feng, S., Kasahara, C., Rickles, R.J., and Schreiber, S.L. (1995). Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proc. Natl. Acad. Sci. USA 92, 12408-12415.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12408-12415
    • Feng, S.1    Kasahara, C.2    Rickles, R.J.3    Schreiber, S.L.4
  • 17
    • 0031974345 scopus 로고    scopus 로고
    • Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated protein
    • Gee, S.H., Madhavan, R., Levinson, S.R., Caldwell, J.H., Sealock, R., and Froehner, S.C. (1998). Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated protein. J. Neurosci. 18, 128-137.
    • (1998) J. Neurosci. , vol.18 , pp. 128-137
    • Gee, S.H.1    Madhavan, R.2    Levinson, S.R.3    Caldwell, J.H.4    Sealock, R.5    Froehner, S.C.6
  • 18
    • 0031974775 scopus 로고    scopus 로고
    • Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase
    • Gitschier, J., Moffat, B., Reilly, D., Wood, W.I., and Fairbrother, W.J. (1998). Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nat. Struct. Biol. 5, 47-54.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 47-54
    • Gitschier, J.1    Moffat, B.2    Reilly, D.3    Wood, W.I.4    Fairbrother, W.J.5
  • 19
    • 0004285740 scopus 로고
    • K. Goslin and G. Banker, eds. (Cambridge, MA: MIT Press).
    • Goslin, K., and Banker, G. (1991). Culturing Nerve Cells, K. Goslin and G. Banker, eds. (Cambridge, MA: MIT Press).
    • (1991) Culturing Nerve Cells
    • Goslin, K.1    Banker, G.2
  • 20
    • 0028330166 scopus 로고
    • Dendritic spines: Cellular specializations imparting both stability and flexibility to synaptic function
    • Harris, K.M., and Kater, S.B. (1994). Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function. Annu. Rev. Neurosci. 17, 341-371.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 341-371
    • Harris, K.M.1    Kater, S.B.2
  • 21
    • 0029018708 scopus 로고
    • Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system
    • Hollenberg, S.M., Sternglanz, R., Cheng, P.F., and Weintraub, H. (1995). Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol. 15, 3813-3822.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3813-3822
    • Hollenberg, S.M.1    Sternglanz, R.2    Cheng, P.F.3    Weintraub, H.4
  • 22
    • 0030473947 scopus 로고    scopus 로고
    • Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain
    • Holmes, T.C., Fadool, D.A., Ren, R., and Levitan, I.B. (1996). Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain. Science 274, 2089-2091.
    • (1996) Science , vol.274 , pp. 2089-2091
    • Holmes, T.C.1    Fadool, D.A.2    Ren, R.3    Levitan, I.B.4
  • 23
    • 17544398829 scopus 로고    scopus 로고
    • Clustering and enhanced activity of an inwardly rectifying potassium channel, Kir4.1, by an anchoring protein, PSD-95/SAP90
    • Horio, Y., Hibino, H., Inanobe, A., Yamada, M., Ishii, M., Tada, Y., Satoh, E., Hata, Y., Takai, Y., and Kurachi, Y. (1997). Clustering and enhanced activity of an inwardly rectifying potassium channel, Kir4.1, by an anchoring protein, PSD-95/SAP90. J. Biol. Chem. 272, 12885-12888.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12885-12888
    • Horio, Y.1    Hibino, H.2    Inanobe, A.3    Yamada, M.4    Ishii, M.5    Tada, Y.6    Satoh, E.7    Hata, Y.8    Takai, Y.9    Kurachi, Y.10
  • 24
    • 0030921919 scopus 로고    scopus 로고
    • Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95
    • Hsueh, Y.-P., Kim, E., and Sheng, M. (1997). Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95. Neuron 18, 803-814.
    • (1997) Neuron , vol.18 , pp. 803-814
    • Hsueh, Y.-P.1    Kim, E.2    Sheng, M.3
  • 26
    • 0018186208 scopus 로고
    • Characterization of tubulin and actin and identification of a distinct postsynaptic density polypeptide
    • Kelly, P.T., and Cotman, C.W. (1978). Characterization of tubulin and actin and identification of a distinct postsynaptic density polypeptide. J. Cell Biol. 79, 173-183.
    • (1978) J. Cell Biol. , vol.79 , pp. 173-183
    • Kelly, P.T.1    Cotman, C.W.2
  • 27
    • 0031172429 scopus 로고    scopus 로고
    • The postsynaptic density at glutamatergic synapses
    • Kennedy, M.B. (1997). The postsynaptic density at glutamatergic synapses. Trends Neurosci. 20, 264-268.
    • (1997) Trends Neurosci. , vol.20 , pp. 264-268
    • Kennedy, M.B.1
  • 28
    • 0030002705 scopus 로고    scopus 로고
    • + channel clustering activity of PSD-95 and SAP97, two related membrane-associated putative guanylate kinases
    • + channel clustering activity of PSD-95 and SAP97, two related membrane-associated putative guanylate kinases. Neuropharmacology 35, 993-1000.
    • (1996) Neuropharmacology , vol.35 , pp. 993-1000
    • Kim, E.1    Sheng, M.2
  • 30
    • 0030200438 scopus 로고    scopus 로고
    • Heteromultimerization and NMDA receptor-clustering activity of chapsyn-110, a member of the PSD-95 family of proteins
    • 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.
    • (1996) Neuron , vol.17 , pp. 103-113
    • Kim, E.1    Cho, K.-O.2    Rothschild, A.3    Sheng, M.4
  • 31
    • 0031052970 scopus 로고    scopus 로고
    • GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/ SAP90 family of channel clustering molecules
    • Kim, E., Naisbitt, S., Hsueh, Y.-P., Rao, A., Rothschild, A., Craig, A.M., and Sheng, M. (1997). GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/ SAP90 family of channel clustering molecules. J. Cell Biol. 136, 669-678.
    • (1997) J. Cell Biol. , vol.136 , pp. 669-678
    • Kim, E.1    Naisbitt, S.2    Hsueh, Y.-P.3    Rao, A.4    Rothschild, A.5    Craig, A.M.6    Sheng, M.7
  • 35
    • 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
  • 36
    • 0030744829 scopus 로고    scopus 로고
    • Interaction of ion channels and receptors with PDZ domain proteins
    • Kornau, H., Seeburg, P., and Kennedy, M. (1997). Interaction of ion channels and receptors with PDZ domain proteins. Curr. Opin. Neurobiol. 7, 368-373.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 368-373
    • Kornau, H.1    Seeburg, P.2    Kennedy, M.3
  • 37
    • 0029788216 scopus 로고    scopus 로고
    • Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102
    • Lau, L.-F., Mammen, A., Ehlers, M.E., Kindler, S., Chung, W.J., Garner, C.C., and Huganir, R.L. (1996). Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102. J. Biol. Chem. 271, 21622-21628.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21622-21628
    • Lau, L.-F.1    Mammen, A.2    Ehlers, M.E.3    Kindler, S.4    Chung, W.J.5    Garner, C.C.6    Huganir, R.L.7
  • 38
    • 0026794064 scopus 로고
    • Specification of subunit assembly by the hydrophilic amino-terminal domain of the shaker potassium channel
    • Li, M., Jan, Y.N., and Jan, L.Y. (1992). Specification of subunit assembly by the hydrophilic amino-terminal domain of the shaker potassium channel. Science 257, 1225-1230.
    • (1992) Science , vol.257 , pp. 1225-1230
    • Li, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 39
    • 0028096801 scopus 로고
    • Cloning and characterization of hdlg: The human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1
    • Lue, R.A., Marfatia, S.M., Branton, D., and Chishti, A.H. (1994). Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1. Proc. Natl. Acad. Sci. USA 91, 9818-9822.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9818-9822
    • Lue, R.A.1    Marfatia, S.M.2    Branton, D.3    Chishti, A.H.4
  • 40
    • 0029851093 scopus 로고    scopus 로고
    • Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton
    • Marfatia, S.M., Cabral, J.H.M., Lin, L., Hough, C., Bryant, P.J., Stolz, L., and Chishti, A.H. (1996). Modular organization of the PDZ domains in the human discs-large protein suggests a mechanism for coupling PDZ domain-binding proteins to ATP and the membrane cytoskeleton. J. Cell Biol. 135, 753-766.
    • (1996) J. Cell Biol. , vol.135 , pp. 753-766
    • Marfatia, S.M.1    Cabral, J.H.M.2    Lin, L.3    Hough, C.4    Bryant, P.J.5    Stolz, L.6    Chishti, A.H.7
  • 42
    • 0029124881 scopus 로고
    • Identification of a gephyrin binding motif on the glycine receptor β subunit
    • Meyer, G., Kirsch, J., Betz, H., and Langosch, D. (1995). Identification of a gephyrin binding motif on the glycine receptor β subunit. Neuron 15, 563-572.
    • (1995) Neuron , vol.15 , pp. 563-572
    • Meyer, G.1    Kirsch, J.2    Betz, H.3    Langosch, D.4
  • 43
    • 0028906288 scopus 로고
    • Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein
    • Müller, B.M., Kistner, U., Veh, R.W., Cases-Langhoff, C., Becker, B., Gundelfinger, E.D., and Garner, C.C. (1995). Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein. J. Neurosci. 15, 2354-2366.
    • (1995) J. Neurosci. , vol.15 , pp. 2354-2366
    • Müller, B.M.1    Kistner, U.2    Veh, R.W.3    Cases-Langhoff, C.4    Becker, B.5    Gundelfinger, E.D.6    Garner, C.C.7
  • 45
    • 0030858386 scopus 로고    scopus 로고
    • Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with posysynaptic density-95/synapse-associated protein 90
    • Naisbitt, S., Kim, E., Weinberg, R.J., Rao, A., Yang, F.-C., Craig, A.M., and Sheng, M. (1997). Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with posysynaptic density-95/synapse-associated protein 90. J. Neurosci. 17, 5687-5696.
    • (1997) J. Neurosci. , vol.17 , pp. 5687-5696
    • Naisbitt, S.1    Kim, E.2    Weinberg, R.J.3    Rao, A.4    Yang, F.-C.5    Craig, A.M.6    Sheng, M.7
  • 46
    • 0032313490 scopus 로고    scopus 로고
    • Identification of ion channel-associated proteins using the yeast two-hybrid system
    • in press.
    • Niethammer, M., and Sheng, M. (1998). Identification of ion channel-associated proteins using the yeast two-hybrid system. Methods Enzymol., in press.
    • (1998) Methods Enzymol.
    • Niethammer, M.1    Sheng, M.2
  • 47
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • 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 kinases. J. Neurosci. 16, 2157-2163.
    • (1996) J. Neurosci. , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 48
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T., and Scott, J.D. (1997). Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 49
    • 0028987110 scopus 로고
    • An osmium-free method of epon embedment that preserves both ultrastructure and antigenicity for postembedding immunocytochemistry
    • Phend, K.D., Rustioni, A., and Weinberg, R.J. (1995). An osmium-free method of Epon embedment that preserves both ultrastructure and antigenicity for postembedding immunocytochemistry. J. Histochem. Cytochem. 43, 283-292.
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 283-292
    • Phend, K.D.1    Rustioni, A.2    Weinberg, R.J.3
  • 50
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: Targeting signaling molecules to sub-membranous sites
    • Ponting, C.P., Phillips, C., Davies, K.E., and Blake, D.J. (1997). PDZ domains: targeting signaling molecules to sub-membranous sites. BioEssays 19, 469-479.
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 51
    • 0032520191 scopus 로고    scopus 로고
    • Heterogeneity in the molecular composition of excitatory postsynaptic sites during development of hippocampal neurons in culture
    • Rao, A., Kim, E., Sheng, M., and Craig, A.M. (1998) Heterogeneity in the molecular composition of excitatory postsynaptic sites during development of hippocampal neurons in culture. J. Neurosci. 18, 1217-1229.
    • (1998) J. Neurosci. , vol.18 , pp. 1217-1229
    • Rao, A.1    Kim, E.2    Sheng, M.3    Craig, A.M.4
  • 53
    • 0030273284 scopus 로고    scopus 로고
    • Ion channel associated proteins
    • Sheng, M., and Kim, E. (1996). Ion channel associated proteins. Curr. Opin. Neurobiol. 6, 602-608.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 602-608
    • Sheng, M.1    Kim, E.2
  • 54
    • 0031260047 scopus 로고    scopus 로고
    • Ion channel targeting in neurons
    • Sheng, M., and Wyszynski, M. (1997). Ion channel targeting in neurons. BioEssays 19, 847-853.
    • (1997) BioEssays , vol.19 , pp. 847-853
    • Sheng, M.1    Wyszynski, M.2
  • 56
    • 0028219211 scopus 로고
    • Changing subunit composition of heteromeric NMDA receptors during development of rat cortex
    • 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.
    • (1994) Nature , vol.368 , pp. 144-147
    • Sheng, M.1    Cummings, J.2    Roldan, L.A.3    Jan, Y.N.4    Jan, L.Y.5
  • 59
    • 0030777701 scopus 로고    scopus 로고
    • Synaptic clustering of the cell adhesion molecule fasciclin II by discs-large and its role in the regulation of presynaptic structure
    • Thomas, U., Kim, E., Kuhlendahl, S., Ho Koh, Y., Gundelfinger, E.D., Sheng, M., Garner, C.C., and Budnik, V. (1997). Synaptic clustering of the cell adhesion molecule fasciclin II by discs-large and its role in the regulation of presynaptic structure. Neuron 19, 787-799.
    • (1997) Neuron , vol.19 , pp. 787-799
    • Thomas, U.1    Kim, E.2    Kuhlendahl, S.3    Ho Koh, Y.4    Gundelfinger, E.D.5    Sheng, M.6    Garner, C.C.7    Budnik, V.8
  • 60
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZ-domain protein assembles signaling complexes in a G-protein-coupled cascade
    • Tsunoda, S., Sierralta, J., Sun, Y., Bodner, R., Suzuki, E., Becker, A., Socolich, M., and Zuker, C.S. (1997). A multivalent PDZ-domain protein assembles signaling complexes in a G-protein-coupled cascade. Nature 388, 243-249.
    • (1997) Nature , vol.388 , pp. 243-249
    • Tsunoda, S.1    Sierralta, J.2    Sun, Y.3    Bodner, R.4    Suzuki, E.5    Becker, A.6    Socolich, M.7    Zuker, C.S.8
  • 61
    • 0016594329 scopus 로고
    • Tubulin in postsynaptic junctional lattice
    • Walters, B.B., and Matus, A.I. (1975). Tubulin in postsynaptic junctional lattice. Nature 257, 496-498.
    • (1975) Nature , vol.257 , pp. 496-498
    • Walters, B.B.1    Matus, A.I.2
  • 62
    • 0025941465 scopus 로고
    • The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods, D.F., and Bryant, P.J. (1991). The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell 66, 451-464.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.F.1    Bryant, P.J.2
  • 63
    • 0031053363 scopus 로고    scopus 로고
    • NMDA channel regulation by channel-associated protein tyrosine kinase Src
    • Yu, X.M., Askalan, R., Keil, G.J., and Salter, M.W. (1997). NMDA channel regulation by channel-associated protein tyrosine kinase Src. Science 275, 674-678.
    • (1997) Science , vol.275 , pp. 674-678
    • Yu, X.M.1    Askalan, R.2    Keil, G.J.3    Salter, M.W.4
  • 64
    • 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
  • 65
    • 0030612949 scopus 로고    scopus 로고
    • Synaptic clustering of fasciclin II and shaker: Essential targeting sequences and role of dlg
    • Zito, K., Fetter, R.D., Goodman, C.S., and Isacoff, E.Y. (1997). Synaptic clustering of fasciclin II and shaker: essential targeting sequences and role of dlg. Neuron 19, 1007-1016.
    • (1997) Neuron , vol.19 , pp. 1007-1016
    • Zito, K.1    Fetter, R.D.2    Goodman, C.S.3    Isacoff, E.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.