메뉴 건너뛰기




Volumn 375, Issue 1-3, 1999, Pages 339-347

Pathophysiological implications of the structural organization of the excitatory synapse

Author keywords

Ca2+ Calmodulin dependent protein kinase II; Diabetes; Glutamate receptor; Methylazoxymethanol; Postsynaptic density; Protein kinase; Synaptic plasticity

Indexed keywords

AMPA RECEPTOR; GLUTAMATE RECEPTOR; IONOTROPIC RECEPTOR; MEMBRANE PROTEIN; METABOTROPIC RECEPTOR; METHYLAZOXYMETHANOL; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHOSPHOTRANSFERASE; POSTSYNAPTIC RECEPTOR; PROTEIN KINASE (CALCIUM,CALMODULIN) II;

EID: 0033057320     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-2999(99)00299-X     Document Type: Review
Times cited : (17)

References (66)
  • 1
    • 0027745596 scopus 로고
    • Modified hippocampal long-term potentiation in protein kinase Cγ-mutant mice
    • Abeliovich A., Chen C., Goda Y., Silva A.J., Stevens C.F., Tonegawa S. Modified hippocampal long-term potentiation in protein kinase Cγ-mutant mice. Cell. 75:1993;1253-1262.
    • (1993) Cell , vol.75 , pp. 1253-1262
    • Abeliovich, A.1    Chen, C.2    Goda, Y.3    Silva, A.J.4    Stevens, C.F.5    Tonegawa, S.6
  • 2
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
    • Barria A., Muller D., Derkach V., Griffith L.C., Soderling T.R. Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation. Science. 276:1997;2042-2045.
    • (1997) Science , vol.276 , pp. 2042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 3
    • 0028841456 scopus 로고
    • High-resolution immunogold localization of AMPA type glutamate receptor subunits at synaptic and non-synaptic sites in rat hippocampus
    • Baude A., Nusser Z., Molnar E., McIlhinney R.A., Somogy P. High-resolution immunogold localization of AMPA type glutamate receptor subunits at synaptic and non-synaptic sites in rat hippocampus. Neuroscience. 69:1995;1031-1055.
    • (1995) Neuroscience , vol.69 , pp. 1031-1055
    • Baude, A.1    Nusser, Z.2    Molnar, E.3    McIlhinney, R.A.4    Somogy, P.5
  • 4
    • 0028897761 scopus 로고
    • N-cadherin is a major glycoprotein component of isolated rat forebrain postsynaptic densities
    • Beesley P.W., Mummery R., Tibaldi J. N-cadherin is a major glycoprotein component of isolated rat forebrain postsynaptic densities. J. Neurochem. 64:1995;2288-2294.
    • (1995) J. Neurochem. , vol.64 , pp. 2288-2294
    • Beesley, P.W.1    Mummery, R.2    Tibaldi, J.3
  • 6
    • 0032572613 scopus 로고    scopus 로고
    • Water maze learning and hippocampal synaptic plasticity in streptozotocin-diabetic rats - Effects of insulin treatment
    • Biessels G.J., Kamal A., Urban I.A., Spruijt B.M., Erkelens D.W., Gispen W.H. Water maze learning and hippocampal synaptic plasticity in streptozotocin-diabetic rats - effects of insulin treatment. Brain Res. 800:1998;125-135.
    • (1998) Brain Res. , vol.800 , pp. 125-135
    • Biessels, G.J.1    Kamal, A.2    Urban, I.A.3    Spruijt, B.M.4    Erkelens, D.W.5    Gispen, W.H.6
  • 8
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domain
    • Brenman J.E., Chao D.S., Gee S.H., McGee A.V., Craven S.E., Sintillano D.R., Wu Z., Xia H., Peters M.F.et al. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domain. Cell. 84:1996;757-767.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.V.4    Craven, S.E.5    Sintillano, D.R.6    Wu, Z.7    Xia, H.8    Peters, M.F.9
  • 9
    • 0030577023 scopus 로고    scopus 로고
    • Differential translocation of protein kinase C isozymes in rats characterized by a chronic lack of long-term potentiation induction and cognitive impairment
    • Caputi A., Rurale S., Pastorino L., Cimino M., Cattabeni F.N., Di Luca M. Differential translocation of protein kinase C isozymes in rats characterized by a chronic lack of long-term potentiation induction and cognitive impairment. FEBS Lett. 393:1996;121-123.
    • (1996) FEBS Lett. , vol.393 , pp. 121-123
    • Caputi, A.1    Rurale, S.2    Pastorino, L.3    Cimino, M.4    Cattabeni, F.N.5    Di Luca, M.6
  • 10
    • 0032945302 scopus 로고    scopus 로고
    • CaMKII phosphorylation of NR2A and NR2B is decreased in animals constitutively lacking long-term potentiation
    • Caputi A., Gardoni F., Cimino M., Pastorino L., Cattabeni F., DiLuca M. CaMKII phosphorylation of NR2A and NR2B is decreased in animals constitutively lacking long-term potentiation. Eur. J. Neurosci. 11:1999;141-148.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 141-148
    • Caputi, A.1    Gardoni, F.2    Cimino, M.3    Pastorino, L.4    Cattabeni, F.5    Diluca, M.6
  • 11
    • 0019134836 scopus 로고
    • Isolation and characterisation of Post Synaptic Densities from various brain regions: Enrichment of different types of Post Synaptic Densities
    • Carlin R.K., Grab D.J., Cohen R.S., Siekevitz P. Isolation and characterisation of Post Synaptic Densities from various brain regions: enrichment of different types of Post Synaptic Densities. J. Cell Biol. 86:1980;831-843.
    • (1980) J. Cell Biol. , vol.86 , pp. 831-843
    • Carlin, R.K.1    Grab, D.J.2    Cohen, R.S.3    Siekevitz, P.4
  • 12
    • 0026795614 scopus 로고
    • Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins. Characterisation of AKAP 79
    • Carr D.W., Stofko H.R., Fraser I.D., Cone R.D., Scott J.D. Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins. Characterisation of AKAP 79. J. Biol. Chem. 267:1992;16816-16823.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16816-16823
    • Carr, D.W.1    Stofko, H.R.2    Fraser, I.D.3    Cone, R.D.4    Scott, J.D.5
  • 13
    • 0031026537 scopus 로고    scopus 로고
    • Developmental models of brain dysfunctions induced by targeted neuronal ablations with methylazoxymethanol
    • Cattabeni F., Di Luca M. Developmental models of brain dysfunctions induced by targeted neuronal ablations with methylazoxymethanol. Physiol. Rev. 77:1997;199-215.
    • (1997) Physiol. Rev. , vol.77 , pp. 199-215
    • Cattabeni, F.1    Di Luca, M.2
  • 14
    • 0344811293 scopus 로고
    • Selective in vitro blockade of neuroepithelial cells proliferation by methylazoxymethanol, a molecule capable of inducing long lasting functional impairments
    • Cattaneo E., Reinach B., Caputi A., Cattabeni F., Di Luca M. Selective in vitro blockade of neuroepithelial cells proliferation by methylazoxymethanol, a molecule capable of inducing long lasting functional impairments. J. Neurosci. Res. 40:1995;1-8.
    • (1995) J. Neurosci. Res. , vol.40 , pp. 1-8
    • Cattaneo, E.1    Reinach, B.2    Caputi, A.3    Cattabeni, F.4    Di Luca, M.5
  • 15
    • 0032078872 scopus 로고    scopus 로고
    • A synaptic Ras-GTPase activating protein (p153 SynGAP) inhibited by Cam Kinase II
    • Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B. A synaptic Ras-GTPase activating protein (p153 SynGAP) inhibited by Cam Kinase II. Neuron. 20:1998;895-904.
    • (1998) Neuron , vol.20 , pp. 895-904
    • Chen, H.-J.1    Rojas-Soto, M.2    Oguni, A.3    Kennedy, M.B.4
  • 17
    • 0014305851 scopus 로고
    • Synaptic patterns on different cell types in the different laminae of the cat visual cortex. An electron microscope study
    • Colonnier M. Synaptic patterns on different cell types in the different laminae of the cat visual cortex. An electron microscope study. Brain Res. 9:1968;268-287.
    • (1968) Brain Res. , vol.9 , pp. 268-287
    • Colonnier, M.1
  • 18
    • 0027512127 scopus 로고
    • Selective alteration in B-50/GAP-43 phosphorylation in brain areas of animals characterized by cognitive impairment
    • Di Luca M., Merazzi F., De Graan P.N.E., Cimino M., Balduini W., Gispen W.H., Cattabeni F. Selective alteration in B-50/GAP-43 phosphorylation in brain areas of animals characterized by cognitive impairment. Brain Res. 607:1993;329-332.
    • (1993) Brain Res. , vol.607 , pp. 329-332
    • Di Luca, M.1    Merazzi, F.2    De Graan, P.N.E.3    Cimino, M.4    Balduini, W.5    Gispen, W.H.6    Cattabeni, F.7
  • 19
    • 0029027790 scopus 로고
    • Changes in protein kinase C and its presynaptic substrate B-50/GAP-43 after intrauterine exposure to methylazoxymethanol, a treatment inducing cortical and hippocampal damage and cognitive deficit in rats
    • Di Luca M., Caputi A., Cinquanta M., Cimino M., Marini P., Princivalle A., De Graan P.N.E., Gispen W.H., Cattabeni F. Changes in protein kinase C and its presynaptic substrate B-50/GAP-43 after intrauterine exposure to methylazoxymethanol, a treatment inducing cortical and hippocampal damage and cognitive deficit in rats. Eur. J. Neurosci. 7:1995;899-906.
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 899-906
    • Di Luca, M.1    Caputi, A.2    Cinquanta, M.3    Cimino, M.4    Marini, P.5    Princivalle, A.6    De Graan, P.N.E.7    Gispen, W.H.8    Cattabeni, F.9
  • 21
    • 0347294707 scopus 로고    scopus 로고
    • NMDA receptor subunits are modified transcriptionally and post-translationally in the brain of streptozotocin-diabetic rats
    • in press
    • Di Luca, M., Ruts, L., Gardoni, F., Cattabeni, F., Biessels, G.J., Gispen, W.H., 1999. NMDA receptor subunits are modified transcriptionally and post-translationally in the brain of streptozotocin-diabetic rats. Diabetologia, in press.
    • (1999) Diabetologia
    • Di Luca, M.1    Ruts, L.2    Gardoni, F.3    Cattabeni, F.4    Biessels, G.J.5    Gispen, W.H.6
  • 22
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong H., O'Brian R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L. GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature. 386:1997;279-284.
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H.1    O'Brian, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 23
    • 0027265754 scopus 로고
    • Inhibition of endogenous phosphatase in a postsynaptic density fraction allows extensive phsphorylation of the major postsynaptic density protein
    • Dosemeci A., Reese T.S. Inhibition of endogenous phosphatase in a postsynaptic density fraction allows extensive phsphorylation of the major postsynaptic density protein. J. Neurochem. 61:1993;550-555.
    • (1993) J. Neurochem. , vol.61 , pp. 550-555
    • Dosemeci, A.1    Reese, T.S.2
  • 24
    • 0029041345 scopus 로고
    • Effect of calpain on the composition and structure of postsynaptic densities
    • Dosemeci A., Reese T.S. Effect of calpain on the composition and structure of postsynaptic densities. Synapse. 20:1995;91-97.
    • (1995) Synapse , vol.20 , pp. 91-97
    • Dosemeci, A.1    Reese, T.S.2
  • 25
    • 0024443063 scopus 로고
    • Studies of the regulatory mechanisms of calcium/calmodulin-dependent protein kinase II mutation of threonine-286 to alanine and aspartate
    • Fong Y.R., Taylor W.R., Means A.R., Soderling T.R. Studies of the regulatory mechanisms of calcium/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.R.1    Taylor, W.R.2    Means, A.R.3    Soderling, T.R.4
  • 27
    • 0031667493 scopus 로고    scopus 로고
    • Calcium/Calmodulin-dependent protein kinase II is associated with NR2A/B subunits of NMDA receptor in postsynaptic densities
    • Gardoni F., Caputi A., Cimino M., Pastorino L., Cattabeni F., DiLuca M. Calcium/Calmodulin-dependent protein kinase II is associated with NR2A/B subunits of NMDA receptor in postsynaptic densities. J. Neurochem. 71:1998;1733-1741.
    • (1998) J. Neurochem. , vol.71 , pp. 1733-1741
    • Gardoni, F.1    Caputi, A.2    Cimino, M.3    Pastorino, L.4    Cattabeni, F.5    Diluca, M.6
  • 28
    • 0027092647 scopus 로고
    • Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice
    • Grant S.G.N., O'Dell T.J., Karl K.A., Stein P.L., Soriano P., Kandel E.R. Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice. Science. 258:1992;1903-1910.
    • (1992) Science , vol.258 , pp. 1903-1910
    • Grant, S.G.N.1    O'Dell, T.J.2    Karl, K.A.3    Stein, P.L.4    Soriano, P.5    Kandel, E.R.6
  • 31
  • 32
    • 0032077680 scopus 로고    scopus 로고
    • Signal transduction molecules at the glutamatergic postsynaptic membrane
    • Kennedy M.B. Signal transduction molecules at the glutamatergic postsynaptic membrane. Brain Res. Rev. 26:1998;243-257.
    • (1998) Brain Res. Rev. , vol.26 , pp. 243-257
    • Kennedy, M.B.1
  • 33
    • 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
  • 34
    • 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., Rotschild A., Craig A.M., Sheng M. 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. 136:1997;669-678.
    • (1997) J. Cell. Biol. , vol.136 , pp. 669-678
    • Kim, E.1    Naisbitt, S.2    Hsueh, Y.P.3    Rao, A.4    Rotschild, A.5    Craig, A.M.6    Sheng, M.7
  • 35
    • 0032055396 scopus 로고    scopus 로고
    • SynGAP: A synaptic RasGAP that associates with the PSD-95/SAP90 protein family
    • Kim J.H., Liao D., Lau L.-F. SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family. Neuron. 20:1998;683-691.
    • (1998) Neuron , vol.20 , pp. 683-691
    • Kim, J.H.1    Liao, D.2    Lau, L.-F.3
  • 36
    • 0029887701 scopus 로고    scopus 로고
    • Coordination of three signalling enzymes bu AKAP79, a methylazoxy-methanolmalian scaffold protein
    • Klauch T.M., Faux M.C., Labudda K., Langeberg L.K., Jaken S., Scott J.D. Coordination of three signalling enzymes bu AKAP79, a methylazoxy-methanolmalian scaffold protein. Science. 271:1996;1589-1592.
    • (1996) Science , vol.271 , pp. 1589-1592
    • Klauch, T.M.1    Faux, M.C.2    Labudda, K.3    Langeberg, L.K.4    Jaken, S.5    Scott, J.D.6
  • 37
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau T.M., Scott J.D. 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, T.M.1    Scott, J.D.2
  • 38
    • 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
  • 39
    • 0030704241 scopus 로고    scopus 로고
    • Differential plasma membrane distribution of metabotropic glutamate receptors mGluR1 alpha, mGluR2 and mGluR5, relative to neurotrasnmitter release sites
    • Lujan R., Roberts J.D., Shigemoto R., Ohishi H., Somogyi P. Differential plasma membrane distribution of metabotropic glutamate receptors mGluR1 alpha, mGluR2 and mGluR5, relative to neurotrasnmitter release sites. J. Chem. Neuroanat. 13:1997;219-241.
    • (1997) J. Chem. Neuroanat. , vol.13 , pp. 219-241
    • Lujan, R.1    Roberts, J.D.2    Shigemoto, R.3    Ohishi, H.4    Somogyi, P.5
  • 40
    • 0029066116 scopus 로고
    • CaMKII regulates the frequency-response function of hippocampal synapses for the production of both long-term depression and long-term potentiation
    • Mayford M., Wang J., Kandell E.R., O'Dell D.J. CaMKII regulates the frequency-response function of hippocampal synapses for the production of both long-term depression and long-term potentiation. Cell. 81:1995;891-904.
    • (1995) Cell , vol.81 , pp. 891-904
    • Mayford, M.1    Wang, J.2    Kandell, E.R.3    O'Dell, D.J.4
  • 41
    • 0026683654 scopus 로고
    • The impact of diabetes on the CNS
    • McCall A.I. The impact of diabetes on the CNS. Diabetes. 41:1992;557-570.
    • (1992) Diabetes , vol.41 , pp. 557-570
    • McCall, A.I.1
  • 43
    • 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
  • 44
    • 0027937531 scopus 로고
    • Subsynaptic segregation of metabotropic and inonotropic glutamate receptors by immunoglod localization
    • Nusser Z., Mulvihil E., Streit P., Somogy P. Subsynaptic segregation of metabotropic and inonotropic glutamate receptors by immunoglod localization. Neuroscience. 61:1994;421-427.
    • (1994) Neuroscience , vol.61 , pp. 421-427
    • Nusser, Z.1    Mulvihil, E.2    Streit, P.3    Somogy, P.4
  • 45
    • 0032102070 scopus 로고    scopus 로고
    • Molecular mechanisms of glutamate receptor clustering at excitatory synapses
    • O'Brien R.J., Lau L.-F., Huganir R.L. Molecular mechanisms of glutamate receptor clustering at excitatory synapses. Curr. Opin. Neurobiol. 8:1998;364-369.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 364-369
    • O'Brien, R.J.1    Lau, L.-F.2    Huganir, R.L.3
  • 46
    • 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
    • Omkumar R.V., Kiely M.J., Rosenstein A.J., Min K.-T., Kennedy M.B. 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;31670-31678.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31670-31678
    • Omkumar, R.V.1    Kiely, M.J.2    Rosenstein, A.J.3    Min, K.-T.4    Kennedy, M.B.5
  • 47
    • 77049268148 scopus 로고
    • Synapses in the central nervous system
    • Palay S.L. Synapses in the central nervous system. Biophys. Biochem. Cytol. 2:1956;193-202.
    • (1956) Biophys. Biochem. Cytol. , vol.2 , pp. 193-202
    • Palay, S.L.1
  • 48
    • 0027278867 scopus 로고
    • The impairment of long-term potentiation in the CA1 field of the hippocampus of cognitive deficient microencephalic rats is restored by D-serine
    • Ramakers G.M.J., Urban I.J.A., De Graan P.N.E., Di Luca M., Cattabeni F., Gispen W.H. The impairment of long-term potentiation in the CA1 field of the hippocampus of cognitive deficient microencephalic rats is restored by D-serine. Neuroscience. 54:1993;49-60.
    • (1993) Neuroscience , vol.54 , pp. 49-60
    • Ramakers, G.M.J.1    Urban, I.J.A.2    De Graan, P.N.E.3    Di Luca, M.4    Cattabeni, F.5    Gispen, W.H.6
  • 49
    • 0033515884 scopus 로고    scopus 로고
    • Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
    • Shen K., Meyer T. Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation. Science. 284:1999;162-166.
    • (1999) Science , vol.284 , pp. 162-166
    • Shen, K.1    Meyer, T.2
  • 50
    • 0026742451 scopus 로고
    • Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice
    • Silva A.J., Paylor R., Wehner J.M., Tonegawa S. Impaired spatial learning in alpha-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
  • 51
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in a-calcium-calmodulin kinase II mutant mice
    • Silva A.J., Stevens C.F., Tonegawa S., Wang Y. Deficient hippocampal long-term potentiation in a-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
  • 53
    • 0030759412 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor rapidly enhances phsophorylation of the postsynaptic N-methyl-D-aspartate receptor subunit 1
    • Suen P.C., Wu K., Levine E.S., Mount H.T., Xu J.L., Lin S.Y., Black I.B. Brain-derived neurotrophic factor rapidly enhances phsophorylation of the postsynaptic N-methyl-D-aspartate receptor subunit 1. Proc. Natl. Acad. Sci. USA. 94:1997;8191-8195.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8191-8195
    • Suen, P.C.1    Wu, K.2    Levine, E.S.3    Mount, H.T.4    Xu, J.L.5    Lin, S.Y.6    Black, I.B.7
  • 54
    • 0028889715 scopus 로고
    • NMDA receptor subunits epsilon 1 (NR2A) and epsilon 2 (NR2B) are substrates for Fyn in the postsynaptic density fraction isolated from rat brain
    • Suzuki T., Okumura N.K. NMDA receptor subunits epsilon 1 (NR2A) and epsilon 2 (NR2B) are substrates for Fyn in the postsynaptic density fraction isolated from rat brain. Biochem. Biophys. Res. Commun. 216:1995;582-588.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 582-588
    • Suzuki, T.1    Okumura, N.K.2
  • 55
    • 0027293091 scopus 로고
    • Characterisation of protein kinase C activities in postsynaptic density fractions prepared from cerebral cortex, hippocampus and cerebellum
    • Suzuki T., Okumura N.K., Tanaka R., Ogura A., Nakamura K., Kudo Y., Tada T. Characterisation of protein kinase C activities in postsynaptic density fractions prepared from cerebral cortex, hippocampus and cerebellum. Brain Res. 619:1993;69-75.
    • (1993) Brain Res. , vol.619 , pp. 69-75
    • Suzuki, T.1    Okumura, N.K.2    Tanaka, R.3    Ogura, A.4    Nakamura, K.5    Kudo, Y.6    Tada, T.7
  • 56
    • 0029030786 scopus 로고
    • ERK2-type mitogen-activated protein kinase (MAPK) and its substrates in postsynaptic density fractions from rat brain
    • Suzuki T., Okumura N.K., Nishida E. ERK2-type mitogen-activated protein kinase (MAPK) and its substrates in postsynaptic density fractions from rat brain. Neurosci. Res. 22:1995;277-285.
    • (1995) Neurosci. Res. , vol.22 , pp. 277-285
    • Suzuki, T.1    Okumura, N.K.2    Nishida, E.3
  • 57
    • 0033582266 scopus 로고    scopus 로고
    • PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A
    • Tezuka T., Umemori H., Akiyama T., Nakanishi S., Yaoto T. PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A. Proc. Natl. Acad. Sci. USA. 96:1999;435-440.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 435-440
    • Tezuka, T.1    Umemori, H.2    Akiyama, T.3    Nakanishi, S.4    Yaoto, T.5
  • 58
    • 0025006846 scopus 로고
    • Modulation of N-methyl-D-aspartate receptor desensitization by glycine in mouse hippocampal neurones
    • Vyklicky L., Benveniste M., Mayer M.L. Modulation of N-methyl-D-aspartate receptor desensitization by glycine in mouse hippocampal neurones. J. Physiol. 428:1990;313-331.
    • (1990) J. Physiol. , vol.428 , pp. 313-331
    • Vyklicky, L.1    Benveniste, M.2    Mayer, M.L.3
  • 59
    • 0026651939 scopus 로고
    • The postsynaptic density: Constituent and associated proteins characterized by electrophoresis, immunoblotting and peptide sequencing
    • Walsh M.J., Kuruc N. The postsynaptic density: constituent and associated proteins characterized by electrophoresis, immunoblotting and peptide sequencing. J. Neurochem. 59:1992;667-678.
    • (1992) J. Neurochem. , vol.59 , pp. 667-678
    • Walsh, M.J.1    Kuruc, N.2
  • 60
    • 0032527719 scopus 로고    scopus 로고
    • Brain spectrin binding to the NMDA receptor is regulated by phosphorylation, calcium and calmodulin
    • Wechsler A., Teichberg V.I. Brain spectrin binding to the NMDA receptor is regulated by phosphorylation, calcium and calmodulin. EMBO J. 17:1998;3931-3939.
    • (1998) EMBO J. , vol.17 , pp. 3931-3939
    • Wechsler, A.1    Teichberg, V.I.2
  • 61
    • 0026674924 scopus 로고
    • Occurrence of the alpha subunits of G proteins in cerebral cortex synaptic membrane and postsynaptic density fractions: Modulation of ADP-ribosylation by Calcium/Calmodulin
    • Wu K., Nigam S.K., LeDoux M., Huang Y.-Y., Aoki C., Siekevitz P. Occurrence of the alpha subunits of G proteins in cerebral cortex synaptic membrane and postsynaptic density fractions: modulation of ADP-ribosylation by Calcium/Calmodulin. Proc. Natl. Acad. Sci. USA. 89:1992;8686-8690.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8686-8690
    • Wu, K.1    Nigam, S.K.2    Ledoux, M.3    Huang, Y.-Y.4    Aoki, C.5    Siekevitz, P.6
  • 62
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of alpha-actinin and calmodulin to the NMDA receptor
    • Wyszynski M., Lin J., Rao A., Nigh E., Beggs A.H., Craig A.M., Sheng M. Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature. 385:1997;439-442.
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 63
    • 0031053363 scopus 로고    scopus 로고
    • NMDA channel regulation by channel-associated protein tyrosine kinase Src
    • Yu X.M., Askalan R., Keil G.J., Salter M.W. NMDA channel regulation by channel-associated protein tyrosine kinase Src. Science. 275:1997;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
    • 0032142987 scopus 로고    scopus 로고
    • Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors
    • Zhang S., Ehelrs M.D., Bernhardt J.P., Su C.T., Huganir R.L. Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors. Neuron. 21:1998;443-453.
    • (1998) Neuron , vol.21 , pp. 443-453
    • Zhang, S.1    Ehelrs, M.D.2    Bernhardt, J.P.3    Su, C.T.4    Huganir, R.L.5
  • 65
    • 0032946267 scopus 로고    scopus 로고
    • Citron binds to PSD-95 at glutamatergic synapses on inhibitory neurons in the hippocampus
    • Zhang W., Vazquez L., Apperson M., Kennedy M.B. Citron binds to PSD-95 at glutamatergic synapses on inhibitory neurons in the hippocampus. J. Neurosci. 19:1999;96-108.
    • (1999) J. Neurosci. , vol.19 , pp. 96-108
    • Zhang, W.1    Vazquez, L.2    Apperson, M.3    Kennedy, M.B.4
  • 66
    • 0031442806 scopus 로고    scopus 로고
    • Enlightening the postsynaptic density
    • Ziff E.B. Enlightening the postsynaptic density. Neuron. 19:1997;1163-1174.
    • (1997) Neuron , vol.19 , pp. 1163-1174
    • Ziff, E.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.