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Volumn 26, Issue 2-3, 1998, Pages 243-257

Signal transduction molecules at the glutamatergic postsynaptic membrane

Author keywords

Long term potentiation; Postsynaptic density; Protein kinases; Protein phosphorylation; Rac; Ras

Indexed keywords

ANIMAL TISSUE; DENDRITE; INFORMATION PROCESSING; INFORMATION RETRIEVAL; NONHUMAN; POSTSYNAPTIC MEMBRANE; PRIORITY JOURNAL; RAT; REVIEW; SIGNAL TRANSDUCTION;

EID: 0032077680     PISSN: 01650173     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-0173(97)00043-X     Document Type: Review
Times cited : (162)

References (108)
  • 1
    • 0029984320 scopus 로고    scopus 로고
    • Metaplasticity - The plasticity of synaptic plasticity
    • Abraham W.C., Bear M.F. Metaplasticity - the plasticity of synaptic plasticity. Trends Neurosci. 19:1996;126-130.
    • (1996) Trends Neurosci. , vol.19 , pp. 126-130
    • Abraham, W.C.1    Bear, M.F.2
  • 2
    • 0023430927 scopus 로고
    • Internal amino acid sequence analysis of proteins separated by one- or two-dimensional gel electrophoresis after in situ protease digestion on nitrocellulose
    • Aebersold R.H., Leavitt J., Saavedra R.A., Hood L.E., Kent S.B.H. Internal amino acid sequence analysis of proteins separated by one- or two-dimensional gel electrophoresis after in situ protease digestion on nitrocellulose. Proc. Natl. Acad. Sci. USA. 84:1987;6970-6974.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6970-6974
    • Aebersold, R.H.1    Leavitt, J.2    Saavedra, R.A.3    Hood, L.E.4    Kent, S.B.H.5
  • 3
    • 0030018796 scopus 로고    scopus 로고
    • Structural differences in the minimal catalytic domains of the GTPase-activating proteins p120GAP and neurofibromin
    • Ahmadian M.R., Wiesmuller L., Lautwein A., Bischoff F.R., Wittinghofer A. Structural differences in the minimal catalytic domains of the GTPase-activating proteins p120GAP and neurofibromin. J. Biol. Chem. 271:1996;16409-16415.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16409-16415
    • Ahmadian, M.R.1    Wiesmuller, L.2    Lautwein, A.3    Bischoff, F.R.4    Wittinghofer, A.5
  • 4
    • 10244236521 scopus 로고    scopus 로고
    • Characterization of densin-180, a new brain-specific synaptic protein of the O-sialoglycoprotein family
    • Apperson M.L., Moon I.-S., Kennedy M.B. Characterization of densin-180, a new brain-specific synaptic protein of the O-sialoglycoprotein family. J. Neurosci. 16:1996;6839-6852.
    • (1996) J. Neurosci. , vol.16 , pp. 6839-6852
    • Apperson, M.L.1    Moon, I.-S.2    Kennedy, M.B.3
  • 5
    • 0029118793 scopus 로고
    • Tyrosine phosphorylation in a model of ischemia using the rat hippocampal slice: Specific, long-term decrease in the tyrosine phosphorylation of the postsynaptic glycoprotein PSD-GP180
    • Au K.N., Gurd J.W. Tyrosine phosphorylation in a model of ischemia using the rat hippocampal slice: specific, long-term decrease in the tyrosine phosphorylation of the postsynaptic glycoprotein PSD-GP180. J. Neurochem. 65:1995;1834-1841.
    • (1995) J. Neurochem. , vol.65 , pp. 1834-1841
    • Au, K.N.1    Gurd, J.W.2
  • 6
    • 0025813396 scopus 로고
    • Stimulation of protein tyrosine phosphorylation by NMDA receptor activation
    • Bading H., Greenberg M.E. Stimulation of protein tyrosine phosphorylation by NMDA receptor activation. Science. 253:1991;912-914.
    • (1991) Science , vol.253 , pp. 912-914
    • Bading, H.1    Greenberg, M.E.2
  • 7
    • 0029149451 scopus 로고
    • Mechanism for a sliding synaptic modification threshold
    • Bear M.F. Mechanism for a sliding synaptic modification threshold. Neuron. 15:1995;1-4.
    • (1995) Neuron , vol.15 , pp. 1-4
    • Bear, M.F.1
  • 8
    • 0021032297 scopus 로고
    • Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain
    • Bennett M.K., Erondu N.E., Kennedy M.B. Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain. J. Biol. Chem. 258:1983;12735-12744.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12735-12744
    • Bennett, M.K.1    Erondu, N.E.2    Kennedy, M.B.3
  • 9
    • 0026543429 scopus 로고
    • Dendritic localization of type II calcium/calmodulin-dependent protein kinase messenger RNA in normal and re-innervated rat hippocampus
    • Benson D.L., Gall C.M., Isackson P.J. Dendritic localization of type II calcium/calmodulin-dependent protein kinase messenger RNA in normal and re-innervated rat hippocampus. Neurosci. 46:1992;851-857.
    • (1992) Neurosci. , vol.46 , pp. 851-857
    • Benson, D.L.1    Gall, C.M.2    Isackson, P.J.3
  • 10
    • 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., Bredt D.S. Cloning and characterization of postsynaptic density-93, a nitric oxide synthase interacting protein. J. Neurosci. 16:1996;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
  • 11
    • 0030273505 scopus 로고    scopus 로고
    • Regulation of synapse structure and function by the drosophila tumor-suppressor gene dlg
    • Budnik V., Koh Y.H., Guan B., Hartmann B., Hough C., Woods D., Gorczyca M. Regulation of synapse structure and function by the drosophila tumor-suppressor gene dlg. Neuron. 17:1996;627-640.
    • (1996) Neuron , vol.17 , pp. 627-640
    • Budnik, V.1    Koh, Y.H.2    Guan, B.3    Hartmann, B.4    Hough, C.5    Woods, D.6    Gorczyca, M.7
  • 13
    • 0001715740 scopus 로고
    • Enhanced seizure susceptibility yet impairment of kindling development in α-calcium-calmodulin kinase II mutant mice
    • Butler L., Silva A., Tonegawa S., McNamara J.O. Enhanced seizure susceptibility yet impairment of kindling development in α-calcium-calmodulin kinase II mutant mice. Soc. Neurosci. Abstr. 19:1993;1030.
    • (1993) Soc. Neurosci. Abstr. , vol.19 , pp. 1030
    • Butler, L.1    Silva, A.2    Tonegawa, S.3    McNamara, J.O.4
  • 15
    • 0028114735 scopus 로고
    • Abnormal fear response and aggressive behavior in mutant mice deficient for α-calcium-calmodulin kinase II
    • Chen C., Rainnie D.G., Greene R.W., Tonegawa S. Abnormal fear response and aggressive behavior in mutant mice deficient for α-calcium-calmodulin kinase II. Science. 266:1994;291-294.
    • (1994) Science , vol.266 , pp. 291-294
    • Chen, C.1    Rainnie, D.G.2    Greene, R.W.3    Tonegawa, S.4
  • 16
    • 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., Kennedy M.B. The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron. 9:1992;929-942.
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.-O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 17
    • 0030473999 scopus 로고    scopus 로고
    • Molecular characterization of the dendritic growth cone: Regulated mRNA transport and local protein synthesis
    • Crino P.B., Eberwine J. Molecular characterization of the dendritic growth cone: regulated mRNA transport and local protein synthesis. Neuron. 17:1996;1173-1187.
    • (1996) Neuron , vol.17 , pp. 1173-1187
    • Crino, P.B.1    Eberwine, J.2
  • 18
    • 0025342635 scopus 로고
    • 2-Photon laser scanning fluorescence microscopy
    • Denk W., Strickler J.H., Webb W.W. 2-Photon laser scanning fluorescence microscopy. Science. 248:1990;73-76.
    • (1990) Science , vol.248 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 19
    • 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., MacKinnon R. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell. 85:1996;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
  • 20
    • 0025022491 scopus 로고
    • Homology of a yeast actin binding protein to signal transduction proteins and myosin-I
    • Drubin D.G., Mulholland J., Zhu Z., Botstein D. Homology of a yeast actin binding protein to signal transduction proteins and myosin-I. Nature. 343:1990;288-290.
    • (1990) Nature , vol.343 , pp. 288-290
    • Drubin, D.G.1    Mulholland, J.2    Zhu, Z.3    Botstein, D.4
  • 21
    • 0345579566 scopus 로고    scopus 로고
    • Activation of p42 mitogen-activated protein kinase in hippocampal long term potentiation
    • English J.D., Sweatt J.D. Activation of p42 mitogen-activated protein kinase in hippocampal long term potentiation. J. Biol. Chem. 271:1996;24329-24332.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24329-24332
    • English, J.D.1    Sweatt, J.D.2
  • 22
    • 0022375477 scopus 로고
    • 2+/calmodulin-dependent protein kinase in rat brain
    • 2+/calmodulin-dependent protein kinase in rat brain. J. Neurosci. 5:1985;3270-3277.
    • (1985) J. Neurosci. , vol.5 , pp. 3270-3277
    • Erondu, N.E.1    Kennedy, M.B.2
  • 24
    • 0027512094 scopus 로고
    • Pairing the cholinergic agonist carbachol with patterned Schaffer collateral stimulation initiates protein synthesis in hippocampal CA1 pyramidal cell dendrites via a muscarinic, NMDA-dependent mechanism
    • Feig S., Lipton P. Pairing the cholinergic agonist carbachol with patterned Schaffer collateral stimulation initiates protein synthesis in hippocampal CA1 pyramidal cell dendrites via a muscarinic, NMDA-dependent mechanism. J. Neurosci. 13:1993;1010-1021.
    • (1993) J. Neurosci. , vol.13 , pp. 1010-1021
    • Feig, S.1    Lipton, P.2
  • 25
    • 0024443063 scopus 로고
    • 2+/calmodulin-dependent protein kinase II-mutation of threonine-286 to alanine and aspartate
    • 2+/calmodulin-dependent protein kinase II-mutation of threonine-286 to alanine and aspartate. J. Biol. Chem. 264:1989;6759-6763.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6759-6763
    • Fong, Y.L.1    Taylor, W.L.2    Means, A.R.3    Soderling, T.R.4
  • 27
    • 0021089951 scopus 로고
    • Purification and characterization of a calmodulin-dependent kinase from rat brain cytosol able to phosphorylate tubulin and microtubule-associated protein
    • Goldenring J.R., Gonzalez B., McGuire J.S. Jr., DeLorenzo R.J. Purification and characterization of a calmodulin-dependent kinase from rat brain cytosol able to phosphorylate tubulin and microtubule-associated protein. J. Biol. Chem. 258:1983;12632-12640.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12632-12640
    • Goldenring, J.R.1    Gonzalez, B.2    McGuire J.S., Jr.3    DeLorenzo, R.J.4
  • 28
    • 0021331070 scopus 로고
    • Identification of the major postsynaptic density protein as homologous with the major calmodulin-binding subunit of a calmodulin-dependent protein kinase
    • Goldenring J.R., McGuire J.S., DeLorenzo R.J. Identification of the major postsynaptic density protein as homologous with the major calmodulin-binding subunit of a calmodulin-dependent protein kinase. J. Neurochem. 42:1984;1077-1084.
    • (1984) J. Neurochem. , vol.42 , pp. 1077-1084
    • Goldenring, J.R.1    McGuire, J.S.2    DeLorenzo, R.J.3
  • 29
    • 0029978023 scopus 로고    scopus 로고
    • Clustering membrane proteins: It's all coming together with the PSD-95/SAP90 protein family
    • Gomperts S.N. Clustering membrane proteins: it's all coming together with the PSD-95/SAP90 protein family. Cell. 84:1996;659-662.
    • (1996) Cell , vol.84 , pp. 659-662
    • Gomperts, S.N.1
  • 30
    • 0022250242 scopus 로고
    • 2+/calmodulin-dependent protein kinase
    • 2+/calmodulin-dependent protein kinase. J. Neurochem. 45:1985;1128-1135.
    • (1985) J. Neurochem. , vol.45 , pp. 1128-1135
    • Gurd, J.W.1
  • 31
    • 0022001496 scopus 로고
    • Phosphorylation of the postsynaptic density glycoprotein gp180 by endogenous tyrosine kinase
    • Gurd J.W. Phosphorylation of the postsynaptic density glycoprotein gp180 by endogenous tyrosine kinase. Brain Res. 333:1985;385-388.
    • (1985) Brain Res. , vol.333 , pp. 385-388
    • Gurd, J.W.1
  • 33
    • 0030576521 scopus 로고    scopus 로고
    • Peptide-surface association: The case of PDZ and PTB domains
    • Harrison S.C. Peptide-surface association: the case of PDZ and PTB domains. Cell. 86:1996;341-343.
    • (1996) Cell , vol.86 , pp. 341-343
    • Harrison, S.C.1
  • 34
    • 0011793355 scopus 로고
    • Immunoreactivity for a calmodulin-dependent protein kinase is selectively increased in macaque striate cortex after monocular deprivation
    • Hendry S.C., Kennedy M.B. Immunoreactivity for a calmodulin-dependent protein kinase is selectively increased in macaque striate cortex after monocular deprivation. Proc. Natl. Acad. Sci. USA. 83:1986;1536-1540.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1536-1540
    • Hendry, S.C.1    Kennedy, M.B.2
  • 35
    • 0028596211 scopus 로고
    • N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann M., Maron C., Heinemann S. N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron. 13:1994;1331-1343.
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 36
    • 0029962955 scopus 로고    scopus 로고
    • PSD-95 is associated with the postsynaptic density and not with the presynaptic membrane at forebrain synapses
    • Hunt C.A., Schenker L.J., Kennedy M.B. PSD-95 is associated with the postsynaptic density and not with the presynaptic membrane at forebrain synapses. J. Neurosci. 16:1996;1380-1388.
    • (1996) J. Neurosci. , vol.16 , pp. 1380-1388
    • Hunt, C.A.1    Schenker, L.J.2    Kennedy, M.B.3
  • 39
    • 0029794770 scopus 로고    scopus 로고
    • A requirement for local protein synthesis in neurotrophin-induced hippocampal synaptic plasticity
    • Kang H., Schuman E.M. A requirement for local protein synthesis in neurotrophin-induced hippocampal synaptic plasticity. Science. 273:1996;1402-1406.
    • (1996) Science , vol.273 , pp. 1402-1406
    • Kang, H.1    Schuman, E.M.2
  • 41
  • 42
    • 0031172429 scopus 로고    scopus 로고
    • The postsynaptic density at glutamatergic synapses
    • Kennedy M.B. The postsynaptic density at glutamatergic synapses. Trends Neurosci. 20:1997;264-268.
    • (1997) Trends Neurosci. , vol.20 , pp. 264-268
    • Kennedy, M.B.1
  • 43
    • 0024805897 scopus 로고
    • Regulation of synaptic transmission in the central nervous system: Long-term potentiation
    • Kennedy M.B. Regulation of synaptic transmission in the central nervous system: long-term potentiation. Cell. 59:1989;777-787.
    • (1989) Cell , vol.59 , pp. 777-787
    • Kennedy, M.B.1
  • 45
    • 0038823489 scopus 로고
    • Biochemical and immunochemical evidence that the 'major postsynaptic density protein' is a subunit of a calmodulin-dependent protein kinase
    • Kennedy M.B., Bennett M.K., Erondu N.E. Biochemical and immunochemical evidence that the 'major postsynaptic density protein' is a subunit of a calmodulin-dependent protein kinase. Proc. Natl. Acad. Sci. USA. 80:1983;7357-7361.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7357-7361
    • Kennedy, M.B.1    Bennett, M.K.2    Erondu, N.E.3
  • 46
    • 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., Sheng M. Heteromultimerization and NMDA receptor-clustering activity of chapsyn-110, a member of the PSD-95 family of proteins. Neuron. 17:1996;103-113.
    • (1996) Neuron , vol.17 , pp. 103-113
    • Kim, E.1    Cho, K.O.2    Rothschild, A.3    Sheng, M.4
  • 48
    • 85047677350 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II in hippocampal slices
    • 2+/calmodulin-dependent protein kinase II in hippocampal slices. J. Neurosci. Meth. 68:1996;61-70.
    • (1996) J. Neurosci. Meth. , vol.68 , pp. 61-70
    • Kindler, S.1    Kennedy, M.B.2
  • 49
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe B., Deisenhofer J. The leucine-rich repeat: a versatile binding motif. TIBS. 19:1994;415-421.
    • (1994) TIBS , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 51
    • 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., Seeburg P.H. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science. 269:1995;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
  • 52
    • 0030744829 scopus 로고    scopus 로고
    • Interaction of ion channels and receptors with PDZ domain proteins
    • Kornau H.-C., Seeburg P.H., Kennedy M.B. Interaction of ion channels and receptors with PDZ domain proteins. Curr. Opin. Neurobiol. 7:1997;368-373.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 368-373
    • Kornau, H.-C.1    Seeburg, P.H.2    Kennedy, M.B.3
  • 53
    • 0030248099 scopus 로고    scopus 로고
    • LTP of AMPA and NMDA receptor-mediated signals: Evidence for presynaptic expression and extrasynaptic glutamate spill-over
    • Kullmann D.M., Erdemli G., Asztly F. LTP of AMPA and NMDA receptor-mediated signals: evidence for presynaptic expression and extrasynaptic glutamate spill-over. Neuron. 17:1996;461-474.
    • (1996) Neuron , vol.17 , pp. 461-474
    • Kullmann, D.M.1    Erdemli, G.2    Asztly, F.3
  • 54
    • 0016136465 scopus 로고
    • Differences in membrane structure between excitatory and inhibitory components of the reciprocal synapse in the olfactory bulb
    • Landis D.M.D., Reese T.S., Raviola S. Differences in membrane structure between excitatory and inhibitory components of the reciprocal synapse in the olfactory bulb. J. Comp. Neurol. 155:1974;67-92.
    • (1974) J. Comp. Neurol. , vol.155 , pp. 67-92
    • Landis, D.M.D.1    Reese, T.S.2    Raviola, S.3
  • 55
    • 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.D., Kindler S., Chung W.J., Garner C.C., Huganir R.L. Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, sap102. J. Biol. Chem. 271:1996;21622-21628.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21622-21628
    • Lau, L.F.1    Mammen, A.2    Ehlers, M.D.3    Kindler, S.4    Chung, W.J.5    Garner, C.C.6    Huganir, R.L.7
  • 56
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the ras-related rhoA GTPase which translocates the kinase to peripheral membranes
    • Leung T., Manser E., Tank L., Lim L. A novel serine/threonine kinase binding the ras-related rhoA GTPase which translocates the kinase to peripheral membranes. J. Biol. Chem. 270:1995;27-34.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27-34
    • Leung, T.1    Manser, E.2    Tank, L.3    Lim, L.4
  • 57
    • 0029018512 scopus 로고
    • Activation of postsynaptically silent synapses during pairing-induced LTP in CA1 region of hippocampal slice
    • Liao D.Z., Hessler N.A., Malinow R. Activation of postsynaptically silent synapses during pairing-induced LTP in CA1 region of hippocampal slice. Nature. 375:1995;400-404.
    • (1995) Nature , vol.375 , pp. 400-404
    • Liao, D.Z.1    Hessler, N.A.2    Malinow, R.3
  • 58
    • 0028031221 scopus 로고
    • The CaM kinase II hypothesis for the storage of synaptic memory
    • Lisman J. The CaM kinase II hypothesis for the storage of synaptic memory. Trends Neurosci. 17:1994;406-412.
    • (1994) Trends Neurosci. , vol.17 , pp. 406-412
    • Lisman, J.1
  • 59
    • 0024043858 scopus 로고
    • 2+/calmodulin-dependent protein kinase molecules of the postsynaptic density
    • 2+/calmodulin-dependent protein kinase molecules of the postsynaptic density. Proc. Natl. Acad. Sci. USA. 85:1988;5320-5324.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5320-5324
    • Lisman, J.E.1    Goldring, M.A.2
  • 60
    • 0029957043 scopus 로고    scopus 로고
    • Localization of alpha Type II calcium /calmodulin-dependent protein kinase at glutamatergic but not gamma-aminobutyric acid (GABAergic) synapses in thalamus and cerebral cortex
    • Liu X.B., Jones E.G. Localization of alpha Type II calcium /calmodulin-dependent protein kinase at glutamatergic but not gamma-aminobutyric acid (GABAergic) synapses in thalamus and cerebral cortex. Proc. Natl. Acad. Sci. USA. 93:1996;7332-7336.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7332-7336
    • Liu, X.B.1    Jones, E.G.2
  • 61
    • 0028880861 scopus 로고
    • Calcium calmodulin-dependent kinase-II and long-term potentiation enhance synaptic transmission by the same mechanism
    • Lledo P.M., Hjelmstad G.O., Mukherji S., Soderling T.R., Malenka R.C., Nicoll R.A. Calcium calmodulin-dependent kinase-II and long-term potentiation enhance synaptic transmission by the same mechanism. Proc. Natl. Acad. Sci. USA. 92:1995;11175-11179.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11175-11179
    • Lledo, P.M.1    Hjelmstad, G.O.2    Mukherji, S.3    Soderling, T.R.4    Malenka, R.C.5    Nicoll, R.A.6
  • 62
    • 0009486537 scopus 로고
    • Cloning of the α-chain of human platelet glycoprotein-IB - A transmembrane protein with homology to leucine-rich α-2-glycoprotein
    • Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Papayannopoulou T., Roth G.J. Cloning of the α-chain of human platelet glycoprotein-IB - a transmembrane protein with homology to leucine-rich α-2-glycoprotein. Proc. Natl. Acad. Sci. USA. 84:1987;5615-5619.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5615-5619
    • Lopez, J.A.1    Chung, D.W.2    Fujikawa, K.3    Hagen, F.S.4    Papayannopoulou, T.5    Roth, G.J.6
  • 63
    • 0030026182 scopus 로고    scopus 로고
    • Differential effects of the rac GTPase on Purkinje cell axons and dendritic trunks and spines
    • Luo L.Q., Hensch T.K., Ackerman L., Barbel S., Jan L.Y., Jan Y.N. Differential effects of the rac GTPase on Purkinje cell axons and dendritic trunks and spines. Nature. 379:1996;837-840.
    • (1996) Nature , vol.379 , pp. 837-840
    • Luo, L.Q.1    Hensch, T.K.2    Ackerman, L.3    Barbel, S.4    Jan, L.Y.5    Jan, Y.N.6
  • 64
    • 0026793775 scopus 로고
    • Stimulus-induced cooordinate changes in mRNA abundance in single postsynaptic hippocampal CA1 neurons
    • Mackler S.A., Brooks B.P., Eberwine J.H. Stimulus-induced cooordinate changes in mRNA abundance in single postsynaptic hippocampal CA1 neurons. Neuron. 9:1992;539-548.
    • (1992) Neuron , vol.9 , pp. 539-548
    • Mackler, S.A.1    Brooks, B.P.2    Eberwine, J.H.3
  • 66
    • 0028969322 scopus 로고
    • Synaptic activation of voltage-gated channels in the dendrites of hippocampal pyramidal neurons
    • Magee J.C., Johnston D. Synaptic activation of voltage-gated channels in the dendrites of hippocampal pyramidal neurons. Science. 268:1995;301-304.
    • (1995) Science , vol.268 , pp. 301-304
    • Magee, J.C.1    Johnston, D.2
  • 67
    • 0031012390 scopus 로고    scopus 로고
    • A synaptically controlled, associative signal for Hebbian plasticity in hippocampal neurons
    • Magee J.C., Johnston D. A synaptically controlled, associative signal for Hebbian plasticity in hippocampal neurons. Science. 275:1997;209-213.
    • (1997) Science , vol.275 , pp. 209-213
    • Magee, J.C.1    Johnston, D.2
  • 68
    • 0031012615 scopus 로고    scopus 로고
    • Regulation of synaptic efficacy by coincidence of postsynaptic APs and EPSPs
    • Markram H., Lbke J., Frotscher M., Sakmann B. Regulation of synaptic efficacy by coincidence of postsynaptic APs and EPSPs. Science. 275:1997;213-215.
    • (1997) Science , vol.275 , pp. 213-215
    • Markram, H.1    Lbke, J.2    Frotscher, M.3    Sakmann, B.4
  • 70
    • 0019209573 scopus 로고
    • Brain postsynaptic densities: Their relationship to glial and neuronal filaments
    • Matus A., Pehling G., Ackermann M., Maeder J. Brain postsynaptic densities: their relationship to glial and neuronal filaments. J. Cell Biol. 87:1980;346-359.
    • (1980) J. Cell Biol. , vol.87 , pp. 346-359
    • Matus, A.1    Pehling, G.2    Ackermann, M.3    Maeder, J.4
  • 71
    • 0029066116 scopus 로고
    • CaMKII regulates the frequency-response function of hippocampal synapses for the production of both LTD and LTP
    • Mayford M., Wang J., Kandel E.R., O'Dell T.J. CaMKII regulates the frequency-response function of hippocampal synapses for the production of both LTD and LTP. Cell. 81:1995;891-904.
    • (1995) Cell , vol.81 , pp. 891-904
    • Mayford, M.1    Wang, J.2    Kandel, E.R.3    O'Dell, T.J.4
  • 72
    • 0027480086 scopus 로고
    • Phosphorylation and regulation of glutamate receptors by calcium/calmodulin-dependent protein kinase II
    • McGlade-McCulloh E., Yamamoto H., Tan S.-E., Brickey D.A., Soderling T.R. Phosphorylation and regulation of glutamate receptors by calcium/calmodulin-dependent protein kinase II. Nature. 362:1993;640-642.
    • (1993) Nature , vol.362 , pp. 640-642
    • McGlade-McCulloh, E.1    Yamamoto, H.2    Tan, S.-E.3    Brickey, D.A.4    Soderling, T.R.5
  • 73
    • 0022258786 scopus 로고
    • 2+/calmodulin-dependent protein kinase associate differently with the postsynaptic density fraction
    • 2+/calmodulin-dependent protein kinase associate differently with the postsynaptic density fraction. J. Biol. Chem. 260:1985;9039-9046.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9039-9046
    • Miller, S.G.1    Kennedy, M.B.2
  • 74
    • 0022519298 scopus 로고
    • 2+-triggered molecular switch
    • 2+-triggered molecular switch. Cell. 44:1986;861-870.
    • (1986) Cell , vol.44 , pp. 861-870
    • Miller, S.G.1    Kennedy, M.B.2
  • 76
    • 0025758890 scopus 로고
    • 2+/calmodulin-dependent protein kinase in cultures of postnatal rat hippocampal slices
    • 2+/calmodulin-dependent protein kinase in cultures of postnatal rat hippocampal slices. Proc. Natl. Acad. Sci. USA. 88:1991;4756-4760.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4756-4760
    • Molloy, S.S.1    Kennedy, M.B.2
  • 78
    • 0000927212 scopus 로고
    • The major tyrosine-phosphorylated protein in the postsynaptic density fraction is N-methyl-D-aspartate receptor subunit 2B
    • Moon I.S., Apperson M.L., Kennedy M.B. The major tyrosine-phosphorylated protein in the postsynaptic density fraction is N-methyl-D-aspartate receptor subunit 2B. Proc. Natl. Acad. Sci. USA. 91:1994;3954-3958.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3954-3958
    • Moon, I.S.1    Apperson, M.L.2    Kennedy, M.B.3
  • 80
    • 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., Sheng M. Interaction between the C-terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J. Neurosci. 16:1996;2157-2163.
    • (1996) J. Neurosci. , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 81
    • 0025923695 scopus 로고
    • 2+ calmodulin-dependent kinase in intact hippocampal slices
    • 2+ calmodulin-dependent kinase in intact hippocampal slices. Neuron. 6:1991;907-914.
    • (1991) Neuron , vol.6 , pp. 907-914
    • Ocorr, K.A.1    Schulman, H.2
  • 82
    • 0029905992 scopus 로고    scopus 로고
    • Identification of a phosphorylation site for calcium/calmodulin-dependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor
    • in press.
    • R.V. Omkumar, M.J. Kiely, A.J. Rosenstein, K.-T. Min, M.B. Kennedy, 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 (1996) in press.
    • (1996) J. Biol. Chem. , vol.271
    • Omkumar, R.V.1    Kiely, M.J.2    Rosenstein, A.J.3    Min, K.-T.4    Kennedy, M.B.5
  • 83
    • 0021127817 scopus 로고
    • Immunocytochemical localization of calcium/calmodulin-dependent protein kinase II in rat brain
    • Ouimet C.C., McGuinness T.L., Greengard P. Immunocytochemical localization of calcium/calmodulin-dependent protein kinase II in rat brain. Proc. Natl. Acad. Sci. USA. 81:1984;5604-5608.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5604-5608
    • Ouimet, C.C.1    McGuinness, T.L.2    Greengard, P.3
  • 84
    • 16944366067 scopus 로고    scopus 로고
    • Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus
    • Ouyang Y., Kantor D., Harris K.M., Schuman E.M., Kennedy M.B. Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus. J. Neurosci. 17:1997;5416-5427.
    • (1997) J. Neurosci. , vol.17 , pp. 5416-5427
    • Ouyang, Y.1    Kantor, D.2    Harris, K.M.3    Schuman, E.M.4    Kennedy, M.B.5
  • 85
    • 0000639902 scopus 로고
    • Identification of functionally significant phosphorylation sites on neuronal proteins and preparation of antibodies that recognize them
    • Patton B.L., Miller S.G., Kennedy M.B. Identification of functionally significant phosphorylation sites on neuronal proteins and preparation of antibodies that recognize them. Methods in Neurosci. 6:1991;158-176.
    • (1991) Methods in Neurosci. , vol.6 , pp. 158-176
    • Patton, B.L.1    Miller, S.G.2    Kennedy, M.B.3
  • 86
    • 0027395059 scopus 로고
    • Autophosphorylation of type II CaM kinase in hippocampal neurons: Localization of phospho- and dephosphokinase with complementary phosphorylation site-specific antibodies
    • Patton B.L., Molloy S.S., Kennedy M.B. Autophosphorylation of type II CaM kinase in hippocampal neurons: localization of phospho- and dephosphokinase with complementary phosphorylation site-specific antibodies. Mol. Biol. Cell. 4:1993;159-172.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 159-172
    • Patton, B.L.1    Molloy, S.S.2    Kennedy, M.B.3
  • 87
    • 0028144080 scopus 로고
    • SH2 and SH3 domains in signal-transduction
    • Pawson T. SH2 and SH3 domains in signal-transduction. Adv. Cancer Res. 64:1994;87-110.
    • (1994) Adv. Cancer Res. , vol.64 , pp. 87-110
    • Pawson, T.1
  • 88
    • 0028579743 scopus 로고
    • Potentiated transmission and prevention of further LTP by increased CaM KII activity in postsynaptic hippocampal slice neurons
    • Pettit D.L., Perlman S., Malinow R. Potentiated transmission and prevention of further LTP by increased CaM KII activity in postsynaptic hippocampal slice neurons. Science. 266:1994;1881-1885.
    • (1994) Science , vol.266 , pp. 1881-1885
    • Pettit, D.L.1    Perlman, S.2    Malinow, R.3
  • 89
    • 0030297781 scopus 로고    scopus 로고
    • Changes in hippocampal gene expression associated with the induction of long-term potentiation
    • Roberts L.A., Higgins M.J., O'Shaughnessy C.T., Stone T.W., Morris B.J. Changes in hippocampal gene expression associated with the induction of long-term potentiation. Mol. Brain Res. 42:1996;123-127.
    • (1996) Mol. Brain Res. , vol.42 , pp. 123-127
    • Roberts, L.A.1    Higgins, M.J.2    O'Shaughnessy, C.T.3    Stone, T.W.4    Morris, B.J.5
  • 90
    • 0029829561 scopus 로고    scopus 로고
    • Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras
    • Scheffzek K., Lautwein A., Kabsch W., Ahmadian M.R., Wittinghofer A. Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras. Nature. 384:1996;591-596.
    • (1996) Nature , vol.384 , pp. 591-596
    • Scheffzek, K.1    Lautwein, A.2    Kabsch, W.3    Ahmadian, M.R.4    Wittinghofer, A.5
  • 91
    • 0023819289 scopus 로고
    • 2+/calmodulin-dependent protein kinase II. Identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains
    • 2+/calmodulin-dependent protein kinase II. Identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains. J. Biol. Chem. 263:1988;13486-13489.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13486-13489
    • Schworer, C.M.1    Colbran, R.J.2    Keefer, J.R.3    Soderling, T.R.4
  • 92
    • 0030273003 scopus 로고    scopus 로고
    • PDZs and receptor/channel clustering: Rounding up the latest suspects
    • Sheng M. PDZs and receptor/channel clustering: rounding up the latest suspects. Neuron. 17:1996;575-578.
    • (1996) Neuron , vol.17 , pp. 575-578
    • Sheng, M.1
  • 93
    • 0026742451 scopus 로고
    • Impaired spatial learning in α-calcium-calmodulin kinase II mutant mice
    • Silva A.J., Paylor R., Wehner J.M., Tonegawa S. Impaired spatial learning in α-calcium-calmodulin kinase II mutant mice. Science. 257:1992;206-211.
    • (1992) Science , vol.257 , pp. 206-211
    • Silva, A.J.1    Paylor, R.2    Wehner, J.M.3    Tonegawa, S.4
  • 94
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in α-calcium-calmodulin kinase II mutant mice
    • Silva A.J., Stevens C.F., Tonegawa S., Wang Y. Deficient hippocampal long-term potentiation in α-calcium-calmodulin kinase II mutant mice. Science. 257:1992;201-206.
    • (1992) Science , vol.257 , pp. 201-206
    • Silva, A.J.1    Stevens, C.F.2    Tonegawa, S.3    Wang, Y.4
  • 96
    • 0028903712 scopus 로고
    • Activity-dependent action potential invasion and calcium influx into hippocampal CA1 dendrites
    • Spruston N., Schiller Y., Stuart G., Sakmann B. Activity-dependent action potential invasion and calcium influx into hippocampal CA1 dendrites. Science. 268:1995;297-300.
    • (1995) Science , vol.268 , pp. 297-300
    • Spruston, N.1    Schiller, Y.2    Stuart, G.3    Sakmann, B.4
  • 97
    • 0028486257 scopus 로고
    • The role of calcium-calmodulin kinase II in 3 forms of synaptic plasticity
    • Stevens C.F., Tonegawa S., Wang Y. The role of calcium-calmodulin kinase II in 3 forms of synaptic plasticity. Curr. Biol. 4:1994;687-693.
    • (1994) Curr. Biol. , vol.4 , pp. 687-693
    • Stevens, C.F.1    Tonegawa, S.2    Wang, Y.3
  • 98
    • 0028111814 scopus 로고
    • 2+/calmodulin-dependent protein kinase II into postsynaptic density after decapitation
    • 2+/calmodulin-dependent protein kinase II into postsynaptic density after decapitation. J. Neurochem. 63:1994;1529-1537.
    • (1994) J. Neurochem. , vol.63 , pp. 1529-1537
    • Suzuki, T.1    Okumuranoji, K.2    Tanaka, R.3    Tada, T.4
  • 101
    • 0028033340 scopus 로고
    • Spatial and temporal changes in signal transduction pathways during LTP
    • Thomas K.L., Laroche S., Errington M.L., Bliss T.V.P., Hunt S.P. Spatial and temporal changes in signal transduction pathways during LTP. Neuron. 13:1994;737-745.
    • (1994) Neuron , vol.13 , pp. 737-745
    • Thomas, K.L.1    Laroche, S.2    Errington, M.L.3    Bliss, T.V.P.4    Hunt, S.P.5
  • 102
    • 0028360327 scopus 로고
    • Regulation of NMDA receptors by tyrosine kinases and phosphatases
    • Wang Y.T., Salter M.W. Regulation of NMDA receptors by tyrosine kinases and phosphatases. Nature. 369:1994;233-235.
    • (1994) Nature , vol.369 , pp. 233-235
    • Wang, Y.T.1    Salter, M.W.2
  • 104
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Wo Z.G., Oswald R.E. Unraveling the modular design of glutamate-gated ion channels. Trends Neurosci. 18:1995;161-168.
    • (1995) Trends Neurosci. , vol.18 , pp. 161-168
    • Wo, Z.G.1    Oswald, R.E.2
  • 105
    • 0025941465 scopus 로고
    • The discs-large tumor suppressor gene of drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods D.F., Bryant P.J. The discs-large tumor suppressor gene of drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell. 66:1991;451-464.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.F.1    Bryant, P.J.2
  • 106
    • 0029819449 scopus 로고    scopus 로고
    • Dlg protein is required for junction structure, cell polarity, and proliferation control in drosophila epithelia
    • Woods D.F., Hough C., Peel D., Callaini G., Bryant P.J. Dlg protein is required for junction structure, cell polarity, and proliferation control in drosophila epithelia. J. Cell Biol. 134:1996;1469-1482.
    • (1996) J. Cell Biol. , vol.134 , pp. 1469-1482
    • Woods, D.F.1    Hough, C.2    Peel, D.3    Callaini, G.4    Bryant, P.J.5
  • 107
    • 0010489587 scopus 로고    scopus 로고
    • Citron, a rho-interacting protein is a component of the rat forebrain postsynaptic density fraction
    • in press.
    • W. Zhang, M.L. Apperson, M.B. Kennedy, Citron, a rho-interacting protein is a component of the rat forebrain postsynaptic density fraction, Abstr. Soc. Neurosci. 23 (1997) in press.
    • (1997) Abstr. Soc. Neurosci. , vol.23
    • Zhang, W.1    Apperson, M.L.2    Kennedy, M.B.3
  • 108
    • 0010489772 scopus 로고    scopus 로고
    • Identification and cloning of a novel 130 kd protein containing a ras GTPase-activating domain from the rat forebrain postsynaptic density fraction
    • in press.
    • H.-J. Chen, M.B. Kennedy, Identification and cloning of a novel 130 kd protein containing a ras GTPase-activating domain from the rat forebrain postsynaptic density fraction, Abstr. Soc. Neurosci. 23 (1997) in press.
    • (1997) Abstr. Soc. Neurosci. , vol.23
    • Chen, H.-J.1    Kennedy, M.B.2


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