메뉴 건너뛰기




Volumn 112, Issue 3, 2006, Pages 810-832

Synaptic plasticity and phosphorylation

Author keywords

Homeostatic plasticity; Long term depression; Long term potentiation; Phosphoproteins; Postsynaptic

Indexed keywords

AMPA RECEPTOR; CALCINEURIN; CASEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NEUROGRANIN; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; POSTSYNAPTIC DENSITY PROTEIN 95; PROTEIN; PROTEIN KINASE (CALCIUM,CALMODULIN) II; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; SYNAPSE ASSOCIATED PROTEIN 97; THREONINE; UNCLASSIFIED DRUG;

EID: 33750013411     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2006.06.003     Document Type: Review
Times cited : (169)

References (346)
  • 1
    • 0030952362 scopus 로고    scopus 로고
    • Genetic demonstration of a role for PKA in the late phase of LTP and in hippocampus-based long-term memory
    • Abel T., Nguyen P.V., Barad M., Deuel T.A., Kandel E.R., and Bourtchouladze R. Genetic demonstration of a role for PKA in the late phase of LTP and in hippocampus-based long-term memory. Cell 88 (1997) 615-626
    • (1997) Cell , vol.88 , pp. 615-626
    • Abel, T.1    Nguyen, P.V.2    Barad, M.3    Deuel, T.A.4    Kandel, E.R.5    Bourtchouladze, R.6
  • 2
    • 0027745596 scopus 로고
    • Modified hippocampal long-term potentiation in PKC gamma-mutant mice
    • Abeliovich A., Chen C., Goda Y., Silva A.J., Stevens C.F., and Tonegawa S. Modified hippocampal long-term potentiation in PKC gamma-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
  • 3
    • 0029984320 scopus 로고    scopus 로고
    • Metaplasticity: the plasticity of synaptic plasticity
    • Abraham W.C., and 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
  • 4
    • 23844454133 scopus 로고    scopus 로고
    • Plasticity-specific phosphorylation of CaMKII, MAP-kinases and CREB during late-LTP in rat hippocampal slices in vitro
    • Ahmed T., and Frey J.U. Plasticity-specific phosphorylation of CaMKII, MAP-kinases and CREB during late-LTP in rat hippocampal slices in vitro. Neuropharmacology 49 (2005) 477-492
    • (2005) Neuropharmacology , vol.49 , pp. 477-492
    • Ahmed, T.1    Frey, J.U.2
  • 5
    • 0021954367 scopus 로고
    • Protein kinase C phosphorylates a 47 Mr protein (F1) directly related to synaptic plasticity
    • Akers R.F., and Routtenberg A. Protein kinase C phosphorylates a 47 Mr protein (F1) directly related to synaptic plasticity. Brain Res 334 (1985) 147-151
    • (1985) Brain Res , vol.334 , pp. 147-151
    • Akers, R.F.1    Routtenberg, A.2
  • 6
    • 0023043778 scopus 로고
    • Translocation of protein kinase C activity may mediate hippocampal long-term potentiation
    • Akers R.F., Lovinger D.M., Colley P.A., Linden D.J., and Routtenberg A. Translocation of protein kinase C activity may mediate hippocampal long-term potentiation. Science 231 (1986) 587-589
    • (1986) Science , vol.231 , pp. 587-589
    • Akers, R.F.1    Lovinger, D.M.2    Colley, P.A.3    Linden, D.J.4    Routtenberg, A.5
  • 7
    • 0020827105 scopus 로고
    • Phosphorylation of B-50 protein by calcium-activated, phospholipid-dependent protein kinase and B-50 protein kinase
    • Aloyo V.J., Zwiers H., and Gispen W.H. Phosphorylation of B-50 protein by calcium-activated, phospholipid-dependent protein kinase and B-50 protein kinase. J Neurochem 41 (1983) 649-653
    • (1983) J Neurochem , vol.41 , pp. 649-653
    • Aloyo, V.J.1    Zwiers, H.2    Gispen, W.H.3
  • 8
    • 0025883223 scopus 로고
    • Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin
    • Apel E.D., Litchfield D.W., Clark R.H., Krebs E.G., and Storm D.R. Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin. J Biol Chem 266 (1991) 10544-10551
    • (1991) J Biol Chem , vol.266 , pp. 10544-10551
    • Apel, E.D.1    Litchfield, D.W.2    Clark, R.H.3    Krebs, E.G.4    Storm, D.R.5
  • 10
    • 0037130451 scopus 로고    scopus 로고
    • Subunit-specific NMDA receptor trafficking to synapses
    • Barria A., and Malinow R. Subunit-specific NMDA receptor trafficking to synapses. Neuron 35 (2002) 345-353
    • (2002) Neuron , vol.35 , pp. 345-353
    • Barria, A.1    Malinow, R.2
  • 11
    • 26944487610 scopus 로고    scopus 로고
    • NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII
    • Barria A., and Malinow R. NMDA receptor subunit composition controls synaptic plasticity by regulating binding to CaMKII. Neuron 48 (2005) 289-301
    • (2005) Neuron , vol.48 , pp. 289-301
    • Barria, A.1    Malinow, R.2
  • 12
    • 0031283172 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the alpha-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate-type glutamate receptor
    • 2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the alpha-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate-type glutamate receptor. J Biol Chem 272 (1997) 32727-32730
    • (1997) J Biol Chem , vol.272 , pp. 32727-32730
    • Barria, A.1    Derkach, V.2    Soderling, T.3
  • 13
    • 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., and 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
  • 14
    • 0033047183 scopus 로고    scopus 로고
    • Differential interaction of the tSXV motifs of the NR1 and NR2A NMDA receptor subunits with PSD95 and SAP97
    • Bassand P., Bernard A., Rafiki A., Gayet D., and Khrestchatisky M. Differential interaction of the tSXV motifs of the NR1 and NR2A NMDA receptor subunits with PSD95 and SAP97. Eur J Neurosci 11 (1999) 2031-2043
    • (1999) Eur J Neurosci , vol.11 , pp. 2031-2043
    • Bassand, P.1    Bernard, A.2    Rafiki, A.3    Gayet, D.4    Khrestchatisky, M.5
  • 15
    • 0024546285 scopus 로고
    • Protein kinase C substrates from bovine brain. Purification and characterization of neuromodulin, a neuron-specific calmodulin-binding protein
    • Baudier J., Bronner C., Kligman D., and Cole R.D. Protein kinase C substrates from bovine brain. Purification and characterization of neuromodulin, a neuron-specific calmodulin-binding protein. J Biol Chem 264 (1989) 1824-1828
    • (1989) J Biol Chem , vol.264 , pp. 1824-1828
    • Baudier, J.1    Bronner, C.2    Kligman, D.3    Cole, R.D.4
  • 16
    • 0345465661 scopus 로고    scopus 로고
    • Developmental expression of the CaM kinase II isoforms: ubiquitous gamma- and delta-CaM kinase II are the early isoforms and most abundant in the developing nervous system
    • Bayer K.U., Lohler J., Schulman H., and Harbers K. Developmental expression of the CaM kinase II isoforms: ubiquitous gamma- and delta-CaM kinase II are the early isoforms and most abundant in the developing nervous system. Brain Res Mol Brain Res 70 (1999) 147-154
    • (1999) Brain Res Mol Brain Res , vol.70 , pp. 147-154
    • Bayer, K.U.1    Lohler, J.2    Schulman, H.3    Harbers, K.4
  • 17
    • 0035859082 scopus 로고    scopus 로고
    • Interaction with the NMDA receptor locks CaMKII in an active conformation
    • Bayer K.U., De Koninck P., Leonard A.S., Hell J.W., and Schulman H. Interaction with the NMDA receptor locks CaMKII in an active conformation. Nature 411 (2001) 801-805
    • (2001) Nature , vol.411 , pp. 801-805
    • Bayer, K.U.1    De Koninck, P.2    Leonard, A.S.3    Hell, J.W.4    Schulman, H.5
  • 18
    • 32544447355 scopus 로고    scopus 로고
    • Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B
    • Bayer K.U., LeBel E., McDonald G.L., O'Leary H., Schulman H., and De Koninck P. Transition from reversible to persistent binding of CaMKII to postsynaptic sites and NR2B. J Neurosci 26 (2006) 1164-1174
    • (2006) J Neurosci , vol.26 , pp. 1164-1174
    • Bayer, K.U.1    LeBel, E.2    McDonald, G.L.3    O'Leary, H.4    Schulman, H.5    De Koninck, P.6
  • 19
    • 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
  • 20
    • 0023224483 scopus 로고
    • A physiological basis for a theory of synapse modification
    • Bear M.F., Cooper L.N., and Ebner F.F. A physiological basis for a theory of synapse modification. Science 237 (1987) 42-48
    • (1987) Science , vol.237 , pp. 42-48
    • Bear, M.F.1    Cooper, L.N.2    Ebner, F.F.3
  • 21
    • 0036663023 scopus 로고    scopus 로고
    • Transgenic calmodulin-dependent protein kinase II activation: dose-dependent effects on synaptic plasticity, learning, and memory
    • Bejar R., Yasuda R., Krugers H., Hood K., and Mayford M. Transgenic calmodulin-dependent protein kinase II activation: dose-dependent effects on synaptic plasticity, learning, and memory. J Neurosci 22 (2002) 5719-5726
    • (2002) J Neurosci , vol.22 , pp. 5719-5726
    • Bejar, R.1    Yasuda, R.2    Krugers, H.3    Hood, K.4    Mayford, M.5
  • 22
    • 0026653052 scopus 로고
    • Protein kinase C modulation of NMDA currents: an important link for LTP induction
    • Ben-Ari Y., Aniksztejn L., and Bregestovski P. Protein kinase C modulation of NMDA currents: an important link for LTP induction. Trends Neurosci 15 (1992) 333-339
    • (1992) Trends Neurosci , vol.15 , pp. 333-339
    • Ben-Ari, Y.1    Aniksztejn, L.2    Bregestovski, P.3
  • 23
    • 0032565873 scopus 로고    scopus 로고
    • Modulation of AMPA receptor unitary conductance by synaptic activity
    • Benke T.A., Luthi A., Isaac J.T., and Collingridge G.L. Modulation of AMPA receptor unitary conductance by synaptic activity. Nature 393 (1998) 793-797
    • (1998) Nature , vol.393 , pp. 793-797
    • Benke, T.A.1    Luthi, A.2    Isaac, J.T.3    Collingridge, G.L.4
  • 24
    • 22544450154 scopus 로고    scopus 로고
    • Lack of NMDA receptor subtype selectivity for hippocampal long-term potentiation
    • Berberich S., Punnakkal P., Jensen V., Pawlak V., Seeburg P.H., Hvalby O., et al. Lack of NMDA receptor subtype selectivity for hippocampal long-term potentiation. J Neurosci 25 (2005) 6907-6910
    • (2005) J Neurosci , vol.25 , pp. 6907-6910
    • Berberich, S.1    Punnakkal, P.2    Jensen, V.3    Pawlak, V.4    Seeburg, P.H.5    Hvalby, O.6
  • 25
    • 0020074887 scopus 로고
    • Theory for the development of neuron selectivity: orientation specificity and binocular interaction in visual cortex
    • Bienenstock E.L., Cooper L.N., and Munro P.W. Theory for the development of neuron selectivity: orientation specificity and binocular interaction in visual cortex. J Neurosci 2 (1982) 32-48
    • (1982) J Neurosci , vol.2 , pp. 32-48
    • Bienenstock, E.L.1    Cooper, L.N.2    Munro, P.W.3
  • 26
    • 0020074887 scopus 로고
    • Theory for the development of neuron selectivity: Orientation specificity and binocular interaction in visual cortex
    • Bienenstock E.L., Cooper L.N., and Munro P.W. Theory for the development of neuron selectivity: Orientation specificity and binocular interaction in visual cortex. J Neurosci 2 (1982) 32-48
    • (1982) J Neurosci , vol.2 , pp. 32-48
    • Bienenstock, E.L.1    Cooper, L.N.2    Munro, P.W.3
  • 27
    • 0028116665 scopus 로고
    • Cyclic AMP and synaptic activity-dependent phosphorylation of AMPA-preferring glutamate receptors
    • Blackstone C., Murphy T.H., Moss S.J., Baraban J.M., and Huganir R.L. Cyclic AMP and synaptic activity-dependent phosphorylation of AMPA-preferring glutamate receptors. J Neurosci 14 (1994) 7585-7593
    • (1994) J Neurosci , vol.14 , pp. 7585-7593
    • Blackstone, C.1    Murphy, T.H.2    Moss, S.J.3    Baraban, J.M.4    Huganir, R.L.5
  • 28
    • 0033991008 scopus 로고    scopus 로고
    • Casein kinase 2 as a potentially important enzyme in the nervous system
    • Blanquet P.R. Casein kinase 2 as a potentially important enzyme in the nervous system. Prog Neurobiol 60 (2000) 211-246
    • (2000) Prog Neurobiol , vol.60 , pp. 211-246
    • Blanquet, P.R.1
  • 29
    • 0015799240 scopus 로고
    • Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path
    • Bliss T.V., and Lomo T. Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path. J Physiol 232 (1973) 331-356
    • (1973) J Physiol , vol.232 , pp. 331-356
    • Bliss, T.V.1    Lomo, T.2
  • 30
    • 0029559465 scopus 로고
    • Postsynaptic cAMP pathway gates early LTP in hippocampal CA1 region
    • Blitzer R.D., Wong T., Nouranifar R., Iyengar R., and Landau E.M. Postsynaptic cAMP pathway gates early LTP in hippocampal CA1 region. Neuron 15 (1995) 1403-1414
    • (1995) Neuron , vol.15 , pp. 1403-1414
    • Blitzer, R.D.1    Wong, T.2    Nouranifar, R.3    Iyengar, R.4    Landau, E.M.5
  • 31
    • 0032546994 scopus 로고    scopus 로고
    • Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP
    • Blitzer R.D., Connor J.H., Brown G.P., Wong T., Shenolikar S., Iyengar R., et al. Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP. Science 280 (1998) 1940-1942
    • (1998) Science , vol.280 , pp. 1940-1942
    • Blitzer, R.D.1    Connor, J.H.2    Brown, G.P.3    Wong, T.4    Shenolikar, S.5    Iyengar, R.6
  • 32
    • 33745927153 scopus 로고    scopus 로고
    • Synaptic incorportation of AMPA receptors during LTP is controlled by a PKC phosphorylation site on GluR1
    • Boehm J., Kang M.G., Johnson R.C., Esteban J., Huganir R.L., and Malinow R. Synaptic incorportation of AMPA receptors during LTP is controlled by a PKC phosphorylation site on GluR1. Neuron 51 (2006) 213-225
    • (2006) Neuron , vol.51 , pp. 213-225
    • Boehm, J.1    Kang, M.G.2    Johnson, R.C.3    Esteban, J.4    Huganir, R.L.5    Malinow, R.6
  • 33
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., and Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72 (2003) 395-447
    • (2003) Annu Rev Biochem , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 35
  • 36
    • 0029082204 scopus 로고
    • Inward rectification of both AMPA and kainate subtype glutamate receptors generated by polyamine-mediated ion channel block
    • Bowie D., and Mayer M.L. Inward rectification of both AMPA and kainate subtype glutamate receptors generated by polyamine-mediated ion channel block. Neuron 15 (1995) 453-462
    • (1995) Neuron , vol.15 , pp. 453-462
    • Bowie, D.1    Mayer, M.L.2
  • 37
    • 0037076287 scopus 로고    scopus 로고
    • Differential roles for NSF and GRIP/ABP in AMPA receptor cycling
    • Braithwaite S.P., Xia H., and Malenka R.C. Differential roles for NSF and GRIP/ABP in AMPA receptor cycling. Proc Natl Acad Sci U S A 99 (2002) 7096-7101
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 7096-7101
    • Braithwaite, S.P.1    Xia, H.2    Malenka, R.C.3
  • 38
    • 0029021176 scopus 로고
    • Hippocampal long-term depression and depotentiation are defective in mice carrying a targeted disruption of the gene encoding the RI beta subunit of cAMP-dependent protein kinase
    • Brandon E.P., Zhuo M., Huang Y.Y., Qi M., Gerhold K.A., Burton K.A., et al. Hippocampal long-term depression and depotentiation are defective in mice carrying a targeted disruption of the gene encoding the RI beta subunit of cAMP-dependent protein kinase. Proc Natl Acad Sci U S A 92 (1995) 8851-8855
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8851-8855
    • Brandon, E.P.1    Zhuo, M.2    Huang, Y.Y.3    Qi, M.4    Gerhold, K.A.5    Burton, K.A.6
  • 39
    • 0030769381 scopus 로고    scopus 로고
    • PKA isoforms, neural pathways, and behaviour: making the connection
    • Brandon E.P., Idzerda R.L., and McKnight G.S. PKA isoforms, neural pathways, and behaviour: making the connection. Curr Opin Neurobiol 7 (1997) 397-403
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 397-403
    • Brandon, E.P.1    Idzerda, R.L.2    McKnight, G.S.3
  • 40
    • 0033529559 scopus 로고    scopus 로고
    • Functional implications of the subunit composition of neuronal CaM kinase II
    • Brocke L., Chiang L.W., Wagner P.D., and Schulman H. Functional implications of the subunit composition of neuronal CaM kinase II. J Biol Chem 274 (1999) 22713-22722
    • (1999) J Biol Chem , vol.274 , pp. 22713-22722
    • Brocke, L.1    Chiang, L.W.2    Wagner, P.D.3    Schulman, H.4
  • 41
    • 0034329255 scopus 로고    scopus 로고
    • Long-term potentiation induced by theta frequency stimulation is regulated by a protein phosphatase-1-operated gate
    • Brown G.P., Blitzer R.D., Connor J.H., Wong T., Shenolikar S., Iyengar R., et al. Long-term potentiation induced by theta frequency stimulation is regulated by a protein phosphatase-1-operated gate. J Neurosci 20 (2000) 7880-7887
    • (2000) J Neurosci , vol.20 , pp. 7880-7887
    • Brown, G.P.1    Blitzer, R.D.2    Connor, J.H.3    Wong, T.4    Shenolikar, S.5    Iyengar, R.6
  • 42
    • 11344290171 scopus 로고    scopus 로고
    • NMDA receptor-dependent activation of the small GTPase Rab5 drives the removal of synaptic AMPA receptors during hippocampal LTD
    • Brown T.C., Tran I.C., Backos D.S., and Esteban J.A. NMDA receptor-dependent activation of the small GTPase Rab5 drives the removal of synaptic AMPA receptors during hippocampal LTD. Neuron 45 (2005) 81-94
    • (2005) Neuron , vol.45 , pp. 81-94
    • Brown, T.C.1    Tran, I.C.2    Backos, D.S.3    Esteban, J.A.4
  • 43
    • 0037191791 scopus 로고    scopus 로고
    • Multiple forms of synaptic plasticity triggered by selective suppression of activity in individual neurons
    • Burrone J., O'Byrne M., and Murthy V.N. Multiple forms of synaptic plasticity triggered by selective suppression of activity in individual neurons. Nature 420 (2002) 414-418
    • (2002) Nature , vol.420 , pp. 414-418
    • Burrone, J.1    O'Byrne, M.2    Murthy, V.N.3
  • 44
    • 0037200059 scopus 로고    scopus 로고
    • Selective binding of synapse-associated protein 97 to GluR-A alpha-amino-5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by a novel sequence motif
    • Cai C., Coleman S.K., Niemi K., and Keinanen K. Selective binding of synapse-associated protein 97 to GluR-A alpha-amino-5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by a novel sequence motif. J Biol Chem 277 (2002) 31484-31490
    • (2002) J Biol Chem , vol.277 , pp. 31484-31490
    • Cai, C.1    Coleman, S.K.2    Niemi, K.3    Keinanen, K.4
  • 45
    • 0033564041 scopus 로고    scopus 로고
    • Characterization of phosphorylation sites on the glutamate receptor 4 subunit of the AMPA receptors
    • Carvalho A.L., Kameyama K., and Huganir R.L. Characterization of phosphorylation sites on the glutamate receptor 4 subunit of the AMPA receptors. J Neurosci 19 (1999) 4748-4754
    • (1999) J Neurosci , vol.19 , pp. 4748-4754
    • Carvalho, A.L.1    Kameyama, K.2    Huganir, R.L.3
  • 46
    • 0032588515 scopus 로고    scopus 로고
    • 2+-calmodulin and protein kinase Cs: a hypothetical synthesis of their conflicting convergences on shared substrate domains
    • 2+-calmodulin and protein kinase Cs: a hypothetical synthesis of their conflicting convergences on shared substrate domains. Trends Neurosci 22 (1999) 12-16
    • (1999) Trends Neurosci , vol.22 , pp. 12-16
    • Chakravarthy, B.1    Morley, P.2    Whitfield, J.3
  • 48
    • 0031049691 scopus 로고    scopus 로고
    • Enhanced phosphorylation of the postsynaptic protein kinase C substrate RC3/neurogranin during long-term potentiation
    • Chen S.J., Sweatt J.D., and Klann E. Enhanced phosphorylation of the postsynaptic protein kinase C substrate RC3/neurogranin during long-term potentiation. Brain Res 749 (1997) 181-187
    • (1997) Brain Res , vol.749 , pp. 181-187
    • Chen, S.J.1    Sweatt, J.D.2    Klann, E.3
  • 49
    • 0034700490 scopus 로고    scopus 로고
    • Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms
    • Chen L., Chetkovich D.M., Petralia R.S., Sweeney N.T., Kawasaki Y., Wenthold R.J., et al. Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms. Nature 408 (2000) 936-943
    • (2000) Nature , vol.408 , pp. 936-943
    • Chen, L.1    Chetkovich, D.M.2    Petralia, R.S.3    Sweeney, N.T.4    Kawasaki, Y.5    Wenthold, R.J.6
  • 50
    • 0037101605 scopus 로고    scopus 로고
    • Phosphorylation of the postsynaptic density-95 (PSD95)/discs large/zona occludens-1 binding site of stargazin regulates binding to PSD95 and synaptic targeting of AMPA receptors
    • Chetkovich D.M., Chen L., Stocker T.J., Nicoll R.A., and Bredt D.S. Phosphorylation of the postsynaptic density-95 (PSD95)/discs large/zona occludens-1 binding site of stargazin regulates binding to PSD95 and synaptic targeting of AMPA receptors. J Neurosci 22 (2002) 5791-5796
    • (2002) J Neurosci , vol.22 , pp. 5791-5796
    • Chetkovich, D.M.1    Chen, L.2    Stocker, T.J.3    Nicoll, R.A.4    Bredt, D.S.5
  • 51
    • 0037023742 scopus 로고    scopus 로고
    • Phosphorylation of stargazin by protein kinase A regulates its interaction with PSD95
    • Choi J., Ko J., Park E., Lee J.R., Yoon J., Lim S., et al. Phosphorylation of stargazin by protein kinase A regulates its interaction with PSD95. J Biol Chem 277 (2002) 12359-12363
    • (2002) J Biol Chem , vol.277 , pp. 12359-12363
    • Choi, J.1    Ko, J.2    Park, E.3    Lee, J.R.4    Yoon, J.5    Lim, S.6
  • 52
    • 8544232133 scopus 로고    scopus 로고
    • Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand
    • Chung H.J., Huang Y.H., Lau L.F., and Huganir R.L. Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand. J Neurosci 24 (2004) 10248-10259
    • (2004) J Neurosci , vol.24 , pp. 10248-10259
    • Chung, H.J.1    Huang, Y.H.2    Lau, L.F.3    Huganir, R.L.4
  • 53
    • 0034307444 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins
    • Chung H.J., Xia J., Scannevin R.H., Zhang X., and Huganir R.L. Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins. J Neurosci 20 (2000) 7258-7267
    • (2000) J Neurosci , vol.20 , pp. 7258-7267
    • Chung, H.J.1    Xia, J.2    Scannevin, R.H.3    Zhang, X.4    Huganir, R.L.5
  • 54
    • 0028874059 scopus 로고
    • Synaptic potentiation of dual-component excitatory postsynaptic currents in the rat hippocampus
    • Clark K.A., and Collingridge G.L. Synaptic potentiation of dual-component excitatory postsynaptic currents in the rat hippocampus. J Physiol 482 Pt 1 (1995) 39-52
    • (1995) J Physiol , vol.482 , Issue.PART 1 , pp. 39-52
    • Clark, K.A.1    Collingridge, G.L.2
  • 55
    • 33344459856 scopus 로고    scopus 로고
    • Pathway-specific trafficking of native AMPARs by in vivo experience
    • Clem R.L., and Barth A. Pathway-specific trafficking of native AMPARs by in vivo experience. Neuron 49 (2006) 663-670
    • (2006) Neuron , vol.49 , pp. 663-670
    • Clem, R.L.1    Barth, A.2
  • 56
    • 0029793743 scopus 로고    scopus 로고
    • Facilitation of long-term potentiation by prior activation of metabotropic glutamate receptors
    • Cohen A.S., and Abraham W.C. Facilitation of long-term potentiation by prior activation of metabotropic glutamate receptors. J Neurophysiol 76 (1996) 953-962
    • (1996) J Neurophysiol , vol.76 , pp. 953-962
    • Cohen, A.S.1    Abraham, W.C.2
  • 57
    • 0031896309 scopus 로고    scopus 로고
    • Priming of long-term potentiation induced by activation of metabotropic glutamate receptors coupled to phospholipase C
    • Cohen A.S., Raymond C.R., and Abraham W.C. Priming of long-term potentiation induced by activation of metabotropic glutamate receptors coupled to phospholipase C. Hippocampus 8 (1998) 160-170
    • (1998) Hippocampus , vol.8 , pp. 160-170
    • Cohen, A.S.1    Raymond, C.R.2    Abraham, W.C.3
  • 58
    • 0027340006 scopus 로고
    • 2+/calmodulin-dependent protein kinase II by basal autophosphorylation
    • 2+/calmodulin-dependent protein kinase II by basal autophosphorylation. J Biol Chem 268 (1993) 7163-7170
    • (1993) J Biol Chem , vol.268 , pp. 7163-7170
    • Colbran, R.J.1
  • 59
    • 2942607447 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II and synaptic plasticity
    • Colbran R.J., and Brown A.M. Calcium/calmodulin-dependent protein kinase II and synaptic plasticity. Curr Opin Neurobiol 14 (2004) 318-327
    • (2004) Curr Opin Neurobiol , vol.14 , pp. 318-327
    • Colbran, R.J.1    Brown, A.M.2
  • 62
    • 0037458663 scopus 로고    scopus 로고
    • Protein kinase C gamma associates directly with the GluR4 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on receptor phosphorylation
    • Correia S.S., Duarte C.B., Faro C.J., Pires E.V., and Carvalho A.L. Protein kinase C gamma associates directly with the GluR4 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on receptor phosphorylation. J Biol Chem 278 (2003) 6307-6313
    • (2003) J Biol Chem , vol.278 , pp. 6307-6313
    • Correia, S.S.1    Duarte, C.B.2    Faro, C.J.3    Pires, E.V.4    Carvalho, A.L.5
  • 63
    • 0033884307 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent inhibition of hippocampal synaptic plasticity
    • Coussens C.M., Williams J.M., Ireland D.R., and Abraham W.C. Tyrosine phosphorylation-dependent inhibition of hippocampal synaptic plasticity. Neuropharmacology 39 (2000) 2267-2277
    • (2000) Neuropharmacology , vol.39 , pp. 2267-2277
    • Coussens, C.M.1    Williams, J.M.2    Ireland, D.R.3    Abraham, W.C.4
  • 64
    • 0035369112 scopus 로고    scopus 로고
    • NMDA receptor subunits: diversity, development and disease
    • Cull-Candy S., Brickley S., and Farrant M. NMDA receptor subunits: diversity, development and disease. Curr Opin Neurobiol 11 (2001) 327-335
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 327-335
    • Cull-Candy, S.1    Brickley, S.2    Farrant, M.3
  • 66
    • 0011628863 scopus 로고
    • Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I
    • Czernik A.J., Pang D.T., and Greengard P. Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I. Proc Natl Acad Sci U S A 84 (1987) 7518-7522
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7518-7522
    • Czernik, A.J.1    Pang, D.T.2    Greengard, P.3
  • 67
    • 5344240347 scopus 로고    scopus 로고
    • Spike timing-dependent plasticity of neural circuits
    • Dan Y., and Poo M.M. Spike timing-dependent plasticity of neural circuits. Neuron 44 (2004) 23-30
    • (2004) Neuron , vol.44 , pp. 23-30
    • Dan, Y.1    Poo, M.M.2
  • 68
    • 0034523581 scopus 로고    scopus 로고
    • PDZ proteins interacting with C-terminal GluR2/3 are involved in a PKC-dependent regulation of AMPA receptors at hippocampal synapses
    • Daw M.I., Chittajallu R., Bortolotto Z.A., Dev K.K., Duprat F., Henley J.M., et al. PDZ proteins interacting with C-terminal GluR2/3 are involved in a PKC-dependent regulation of AMPA receptors at hippocampal synapses. Neuron 28 (2000) 873-886
    • (2000) Neuron , vol.28 , pp. 873-886
    • Daw, M.I.1    Chittajallu, R.2    Bortolotto, Z.A.3    Dev, K.K.4    Duprat, F.5    Henley, J.M.6
  • 70
    • 0025857757 scopus 로고
    • A rapid purification method for neurogranin, a brain specific calmodulin-binding protein kinase C substrate
    • Deloulme J.C., Sensenbrenner M., and Baudier J. A rapid purification method for neurogranin, a brain specific calmodulin-binding protein kinase C substrate. FEBS Lett 282 (1991) 183-188
    • (1991) FEBS Lett , vol.282 , pp. 183-188
    • Deloulme, J.C.1    Sensenbrenner, M.2    Baudier, J.3
  • 71
    • 0032588030 scopus 로고    scopus 로고
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors. Proc Natl Acad Sci U S A 96 (1999) 3269-3274
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3269-3274
    • Derkach, V.1    Barria, A.2    Soderling, T.R.3
  • 72
    • 0029056120 scopus 로고
    • 2+)-permeable alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors
    • 2+)-permeable alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors. Proc Natl Acad Sci U S A 92 (1995) 9298-9302
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9298-9302
    • Donevan, S.D.1    Rogawski, M.A.2
  • 73
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., and 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'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 74
    • 0026579349 scopus 로고
    • Homosynaptic long-term depression in area CA1 of hippocampus and effects of N-methyl-d-aspartate receptor blockade
    • Dudek S.M., and Bear M.F. Homosynaptic long-term depression in area CA1 of hippocampus and effects of N-methyl-d-aspartate receptor blockade. Proc Natl Acad Sci U S A 89 (1992) 4363-4367
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4363-4367
    • Dudek, S.M.1    Bear, M.F.2
  • 75
    • 0033639083 scopus 로고    scopus 로고
    • Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting
    • Ehlers M.D. Reinsertion or degradation of AMPA receptors determined by activity-dependent endocytic sorting. Neuron 28 (2000) 511-525
    • (2000) Neuron , vol.28 , pp. 511-525
    • Ehlers, M.D.1
  • 76
    • 0029147928 scopus 로고
    • Regulated subcellular distribution of the NR1 subunit of the NMDA receptor
    • Ehlers M.D., Tingley W.G., and Huganir R.L. Regulated subcellular distribution of the NR1 subunit of the NMDA receptor. Science 269 (1995) 1734-1737
    • (1995) Science , vol.269 , pp. 1734-1737
    • Ehlers, M.D.1    Tingley, W.G.2    Huganir, R.L.3
  • 77
    • 0037168124 scopus 로고    scopus 로고
    • Inhibitory autophosphorylation of CaMKII controls PSD association, plasticity, and learning
    • Elgersma Y., Fedorov N.B., Ikonen S., Choi E.S., Elgersma M., Carvalho O.M., et al. Inhibitory autophosphorylation of CaMKII controls PSD association, plasticity, and learning. Neuron 36 (2002) 493-505
    • (2002) Neuron , vol.36 , pp. 493-505
    • Elgersma, Y.1    Fedorov, N.B.2    Ikonen, S.3    Choi, E.S.4    Elgersma, M.5    Carvalho, O.M.6
  • 78
    • 0345579566 scopus 로고    scopus 로고
    • Activation of p42 mitogen-activated protein kinase in hippocampal long term potentiation
    • English J.D., and 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
  • 79
    • 0030749510 scopus 로고    scopus 로고
    • A requirement for the mitogen-activated protein kinase cascade in hippocampal long term potentiation
    • English J.D., and Sweatt J.D. A requirement for the mitogen-activated protein kinase cascade in hippocampal long term potentiation. J Biol Chem 272 (1997) 19103-19106
    • (1997) J Biol Chem , vol.272 , pp. 19103-19106
    • English, J.D.1    Sweatt, J.D.2
  • 80
    • 0037312605 scopus 로고    scopus 로고
    • PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity
    • Esteban J.A., Shi S.H., Wilson C., Nuriya M., Huganir R.L., and Malinow R. PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity. Nat Neurosci 6 (2003) 136-143
    • (2003) Nat Neurosci , vol.6 , pp. 136-143
    • Esteban, J.A.1    Shi, S.H.2    Wilson, C.3    Nuriya, M.4    Huganir, R.L.5    Malinow, R.6
  • 81
    • 15944381871 scopus 로고    scopus 로고
    • Function of cGMP-dependent protein kinases in the nervous system
    • Feil R., Hofmann F., and Kleppisch T. Function of cGMP-dependent protein kinases in the nervous system. Rev Neurosci 16 (2005) 23-41
    • (2005) Rev Neurosci , vol.16 , pp. 23-41
    • Feil, R.1    Hofmann, F.2    Kleppisch, T.3
  • 82
    • 0036606735 scopus 로고    scopus 로고
    • Molecular mechanisms of CaMKII activation in neuronal plasticity
    • Fink C.C., and Meyer T. Molecular mechanisms of CaMKII activation in neuronal plasticity. Curr Opin Neurobiol 12 (2002) 293-299
    • (2002) Curr Opin Neurobiol , vol.12 , pp. 293-299
    • Fink, C.C.1    Meyer, T.2
  • 83
    • 0042347897 scopus 로고    scopus 로고
    • Selective regulation of neurite extension and synapse formation by the beta but not the alpha isoform of CaMKII
    • Fink C.C., Bayer K.U., Myers J.W., Ferrell Jr. J.E., Schulman H., and Meyer T. Selective regulation of neurite extension and synapse formation by the beta but not the alpha isoform of CaMKII. Neuron 39 (2003) 283-297
    • (2003) Neuron , vol.39 , pp. 283-297
    • Fink, C.C.1    Bayer, K.U.2    Myers, J.W.3    Ferrell Jr., J.E.4    Schulman, H.5    Meyer, T.6
  • 84
    • 0037088921 scopus 로고    scopus 로고
    • Rapid synaptic remodeling by protein kinase C: reciprocal translocation of NMDA receptors and calcium/calmodulin-dependent kinase II
    • Fong D.K., Rao A., Crump F.T., and Craig A.M. Rapid synaptic remodeling by protein kinase C: reciprocal translocation of NMDA receptors and calcium/calmodulin-dependent kinase II. J Neurosci 22 (2002) 2153-2164
    • (2002) J Neurosci , vol.22 , pp. 2153-2164
    • Fong, D.K.1    Rao, A.2    Crump, F.T.3    Craig, A.M.4
  • 85
    • 0035902010 scopus 로고    scopus 로고
    • Alpha-CaMKII-dependent plasticity in the cortex is required for permanent memory
    • Frankland P.W., O'Brien C., Ohno M., Kirkwood A., and Silva A.J. Alpha-CaMKII-dependent plasticity in the cortex is required for permanent memory. Nature 411 (2001) 309-313
    • (2001) Nature , vol.411 , pp. 309-313
    • Frankland, P.W.1    O'Brien, C.2    Ohno, M.3    Kirkwood, A.4    Silva, A.J.5
  • 86
    • 15044340596 scopus 로고    scopus 로고
    • Spike-timing-dependent synaptic plasticity depends on dendritic location
    • Froemke R.C., Poo M.M., and Dan Y. Spike-timing-dependent synaptic plasticity depends on dendritic location. Nature 434 (2005) 221-225
    • (2005) Nature , vol.434 , pp. 221-225
    • Froemke, R.C.1    Poo, M.M.2    Dan, Y.3
  • 87
    • 0025779446 scopus 로고
    • Reversal of long-term potentiation (depotentiation) induced by tetanus stimulation of the input to CA1 neurons of guinea pig hippocampal slices
    • Fujii S., Saito K., Miyakawa H., Ito K., and Kato H. Reversal of long-term potentiation (depotentiation) induced by tetanus stimulation of the input to CA1 neurons of guinea pig hippocampal slices. Brain Res 555 (1991) 112-122
    • (1991) Brain Res , vol.555 , pp. 112-122
    • Fujii, S.1    Saito, K.2    Miyakawa, H.3    Ito, K.4    Kato, H.5
  • 90
    • 0028988308 scopus 로고
    • 2+/calmodulin-dependent protein kinase II and its endogenous substrates in the induction of long-term potentiation
    • 2+/calmodulin-dependent protein kinase II and its endogenous substrates in the induction of long-term potentiation. J Biol Chem 270 (1995) 6119-6124
    • (1995) J Biol Chem , vol.270 , pp. 6119-6124
    • Fukunaga, K.1    Muller, D.2    Miyamoto, E.3
  • 92
    • 0028921368 scopus 로고
    • 2+/calmodulin- and cAMP-dependent protein kinases in vitro
    • 2+/calmodulin- and cAMP-dependent protein kinases in vitro. J Neurosci 15 (1995) 2385-2395
    • (1995) J Neurosci , vol.15 , pp. 2385-2395
    • Fykse, E.M.1    Li, C.2    Sudhof, T.C.3
  • 93
    • 15444362199 scopus 로고    scopus 로고
    • Calcium-permeable AMPA receptor plasticity is mediated by subunit-specific interactions with PICK1 and NSF
    • Gardner S.M., Takamiya K., Xia J., Suh J.G., Johnson R., Yu S., et al. Calcium-permeable AMPA receptor plasticity is mediated by subunit-specific interactions with PICK1 and NSF. Neuron 45 (2005) 903-915
    • (2005) Neuron , vol.45 , pp. 903-915
    • Gardner, S.M.1    Takamiya, K.2    Xia, J.3    Suh, J.G.4    Johnson, R.5    Yu, S.6
  • 94
    • 0032588758 scopus 로고    scopus 로고
    • AlphaCaMKII binding to the C-terminal tail of NMDA receptor subunit NR2A and its modulation by autophosphorylation
    • Gardoni F., Schrama L.H., van Dalen J.J., Gispen W.H., Cattabeni F., and Di Luca M. AlphaCaMKII binding to the C-terminal tail of NMDA receptor subunit NR2A and its modulation by autophosphorylation. FEBS Lett 456 (1999) 394-398
    • (1999) FEBS Lett , vol.456 , pp. 394-398
    • Gardoni, F.1    Schrama, L.H.2    van Dalen, J.J.3    Gispen, W.H.4    Cattabeni, F.5    Di Luca, M.6
  • 95
    • 0035831431 scopus 로고    scopus 로고
    • Protein kinase C activation modulates alpha-calmodulin kinase II binding to NR2A subunit of N-methyl-d-aspartate receptor complex
    • Gardoni F., Bellone C., Cattabeni F., and Di Luca M. Protein kinase C activation modulates alpha-calmodulin kinase II binding to NR2A subunit of N-methyl-d-aspartate receptor complex. J Biol Chem 276 (2001) 7609-7613
    • (2001) J Biol Chem , vol.276 , pp. 7609-7613
    • Gardoni, F.1    Bellone, C.2    Cattabeni, F.3    Di Luca, M.4
  • 98
    • 0032488659 scopus 로고    scopus 로고
    • Autophosphorylation at Thr286 of the alpha calcium-calmodulin kinase II in LTP and learning
    • Giese K.P., Fedorov N.B., Filipkowski R.K., and Silva A.J. Autophosphorylation at Thr286 of the alpha calcium-calmodulin kinase II in LTP and learning. Science 279 (1998) 870-873
    • (1998) Science , vol.279 , pp. 870-873
    • Giese, K.P.1    Fedorov, N.B.2    Filipkowski, R.K.3    Silva, A.J.4
  • 99
    • 0141756280 scopus 로고    scopus 로고
    • Mechanisms underlying the inhibition of long-term potentiation by preconditioning stimulation in the hippocampus in vitro
    • Gisabella B., Rowan M.J., and Anwyl R. Mechanisms underlying the inhibition of long-term potentiation by preconditioning stimulation in the hippocampus in vitro. Neuroscience 121 (2003) 297-305
    • (2003) Neuroscience , vol.121 , pp. 297-305
    • Gisabella, B.1    Rowan, M.J.2    Anwyl, R.3
  • 100
    • 33747598065 scopus 로고    scopus 로고
    • Cross-modal regulation of synaptic AMPA receptors in primary sensory cortices by visual experience
    • Goel A., Jiang B., Xu L.W., Song L., Kirkwood A., and Lee H.-K. Cross-modal regulation of synaptic AMPA receptors in primary sensory cortices by visual experience. Nat Neurosci 9 (2006) 1001-1003
    • (2006) Nat Neurosci , vol.9 , pp. 1001-1003
    • Goel, A.1    Jiang, B.2    Xu, L.W.3    Song, L.4    Kirkwood, A.5    Lee, H.-K.6
  • 101
    • 0027092647 scopus 로고
    • Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice
    • Grant S.G., O'Dell T.J., Karl K.A., Stein P.L., Soriano P., and 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.1    O'Dell, T.J.2    Karl, K.A.3    Stein, P.L.4    Soriano, P.5    Kandel, E.R.6
  • 102
    • 0036139881 scopus 로고    scopus 로고
    • LTP leads to rapid surface expression of NMDA but not AMPA receptors in adult rat CA1
    • Grosshans D.R., Clayton D.A., Coultrap S.J., and Browning M.D. LTP leads to rapid surface expression of NMDA but not AMPA receptors in adult rat CA1. Nat Neurosci 5 (2002) 27-33
    • (2002) Nat Neurosci , vol.5 , pp. 27-33
    • Grosshans, D.R.1    Clayton, D.A.2    Coultrap, S.J.3    Browning, M.D.4
  • 103
    • 0038457551 scopus 로고    scopus 로고
    • Neocortical long-term potentiation and experience-dependent synaptic plasticity require alpha-calcium/calmodulin-dependent protein kinase II autophosphorylation
    • Hardingham N., Glazewski S., Pakhotin P., Mizuno K., Chapman P.F., Giese K.P., et al. Neocortical long-term potentiation and experience-dependent synaptic plasticity require alpha-calcium/calmodulin-dependent protein kinase II autophosphorylation. J Neurosci 23 (2003) 4428-4436
    • (2003) J Neurosci , vol.23 , pp. 4428-4436
    • Hardingham, N.1    Glazewski, S.2    Pakhotin, P.3    Mizuno, K.4    Chapman, P.F.5    Giese, K.P.6
  • 105
    • 0033565945 scopus 로고    scopus 로고
    • Impairment of AMPA receptor function in cerebellar granule cells of ataxic mutant mouse stargazer
    • Hashimoto K., Fukaya M., Qiao X., Sakimura K., Watanabe M., and Kano M. Impairment of AMPA receptor function in cerebellar granule cells of ataxic mutant mouse stargazer. J Neurosci 19 (1999) 6027-6036
    • (1999) J Neurosci , vol.19 , pp. 6027-6036
    • Hashimoto, K.1    Fukaya, M.2    Qiao, X.3    Sakimura, K.4    Watanabe, M.5    Kano, M.6
  • 106
    • 3042794099 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases
    • Hayashi T., and Huganir R.L. Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases. J Neurosci 24 (2004) 6152-6160
    • (2004) J Neurosci , vol.24 , pp. 6152-6160
    • Hayashi, T.1    Huganir, R.L.2
  • 107
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction
    • Hayashi Y., Shi S.H., Esteban J.A., Piccini A., Poncer J.C., and Malinow R. Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science 287 (2000) 2262-2267
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1    Shi, S.H.2    Esteban, J.A.3    Piccini, A.4    Poncer, J.C.5    Malinow, R.6
  • 109
  • 110
    • 0022499320 scopus 로고
    • Frequency-dependent involvement of NMDA receptors in the hippocampus: a novel synaptic mechanism
    • Herron C.E., Lester R.A., Coan E.J., and Collingridge G.L. Frequency-dependent involvement of NMDA receptors in the hippocampus: a novel synaptic mechanism. Nature 322 (1986) 265-268
    • (1986) Nature , vol.322 , pp. 265-268
    • Herron, C.E.1    Lester, R.A.2    Coan, E.J.3    Collingridge, G.L.4
  • 111
    • 0033635615 scopus 로고    scopus 로고
    • Bidirectional, activity-dependent regulation of glutamate receptors in the adult hippocampus in vivo
    • Heynen A.J., Quinlan E.M., Bae D.C., and Bear M.F. Bidirectional, activity-dependent regulation of glutamate receptors in the adult hippocampus in vivo. Neuron 28 (2000) 527-536
    • (2000) Neuron , vol.28 , pp. 527-536
    • Heynen, A.J.1    Quinlan, E.M.2    Bae, D.C.3    Bear, M.F.4
  • 112
    • 0032456783 scopus 로고    scopus 로고
    • CA1 long-term potentiation is diminished but present in hippocampal slices from alpha-CaMKII mutant mice
    • Hinds H.L., Tonegawa S., and Malinow R. CA1 long-term potentiation is diminished but present in hippocampal slices from alpha-CaMKII mutant mice. Learn Mem 5 (1998) 344-354
    • (1998) Learn Mem , vol.5 , pp. 344-354
    • Hinds, H.L.1    Tonegawa, S.2    Malinow, R.3
  • 113
    • 0025923461 scopus 로고
    • 2+ permeability of KA-AMPA-gated glutamate receptor channels depends on subunit composition
    • 2+ permeability of KA-AMPA-gated glutamate receptor channels depends on subunit composition. Science 252 (1991) 851-853
    • (1991) Science , vol.252 , pp. 851-853
    • Hollmann, M.1    Hartley, M.2    Heinemann, S.3
  • 114
    • 0029799241 scopus 로고    scopus 로고
    • Bidirectional regulation of protein kinase M zeta in the maintenance of long-term potentiation and long-term depression
    • Hrabetova S., and Sacktor T.C. Bidirectional regulation of protein kinase M zeta in the maintenance of long-term potentiation and long-term depression. J Neurosci 16 (1996) 5324-5333
    • (1996) J Neurosci , vol.16 , pp. 5324-5333
    • Hrabetova, S.1    Sacktor, T.C.2
  • 115
    • 0242571496 scopus 로고    scopus 로고
    • Protein tyrosine kinase is required for the induction of long-term potentiation in the rat hippocampus
    • Huang C.C., and Hsu K.S. Protein tyrosine kinase is required for the induction of long-term potentiation in the rat hippocampus. J Physiol 520 Pt 3 (1999) 783-796
    • (1999) J Physiol , vol.520 , Issue.PART 3 , pp. 783-796
    • Huang, C.C.1    Hsu, K.S.2
  • 116
    • 0028429943 scopus 로고
    • Recruitment of long-lasting and protein kinase A-dependent long-term potentiation in the CA1 region of hippocampus requires repeated tetanization
    • Huang Y.Y., and Kandel E.R. Recruitment of long-lasting and protein kinase A-dependent long-term potentiation in the CA1 region of hippocampus requires repeated tetanization. Learn Mem 1 (1994) 74-82
    • (1994) Learn Mem , vol.1 , pp. 74-82
    • Huang, Y.Y.1    Kandel, E.R.2
  • 117
    • 0026696192 scopus 로고
    • Postsynaptic then presynaptic protein kinase C activity may be necessary for long-term potentiation
    • Huang Y.Y., Colley P.A., and Routtenberg A. Postsynaptic then presynaptic protein kinase C activity may be necessary for long-term potentiation. Neuroscience 49 (1992) 819-827
    • (1992) Neuroscience , vol.49 , pp. 819-827
    • Huang, Y.Y.1    Colley, P.A.2    Routtenberg, A.3
  • 118
    • 17744380787 scopus 로고    scopus 로고
    • CAKbeta/Pyk2 kinase is a signaling link for induction of long-term potentiation in CA1 hippocampus
    • Huang Y., Lu W., Ali D.W., Pelkey K.A., Pitcher G.M., Lu Y.M., et al. CAKbeta/Pyk2 kinase is a signaling link for induction of long-term potentiation in CA1 hippocampus. Neuron 29 (2001) 485-496
    • (2001) Neuron , vol.29 , pp. 485-496
    • Huang, Y.1    Lu, W.2    Ali, D.W.3    Pelkey, K.A.4    Pitcher, G.M.5    Lu, Y.M.6
  • 119
    • 9344271526 scopus 로고    scopus 로고
    • Neurogranin/RC3 enhances long-term potentiation and learning by promoting calcium-mediated signaling
    • Huang K.P., Huang F.L., Jager T., Li J., Reymann K.G., and Balschun D. Neurogranin/RC3 enhances long-term potentiation and learning by promoting calcium-mediated signaling. J Neurosci 24 (2004) 10660-10669
    • (2004) J Neurosci , vol.24 , pp. 10660-10669
    • Huang, K.P.1    Huang, F.L.2    Jager, T.3    Li, J.4    Reymann, K.G.5    Balschun, D.6
  • 120
    • 0035341239 scopus 로고    scopus 로고
    • Proteomics of the nervous system
    • Husi H., and Grant S.G. Proteomics of the nervous system. Trends Neurosci 24 (2001) 259-266
    • (2001) Trends Neurosci , vol.24 , pp. 259-266
    • Husi, H.1    Grant, S.G.2
  • 121
    • 0033946468 scopus 로고    scopus 로고
    • Proteomic analysis of NMDA receptor-adhesion protein signaling complexes
    • Husi H., Ward M.A., Choudhary J.S., Blackstock W.P., and Grant S.G. Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat Neurosci 3 (2000) 661-669
    • (2000) Nat Neurosci , vol.3 , pp. 661-669
    • Husi, H.1    Ward, M.A.2    Choudhary, J.S.3    Blackstock, W.P.4    Grant, S.G.5
  • 122
    • 0019876587 scopus 로고
    • Differential phosphorylation of multiple sites in purified protein I by cyclic AMP-dependent and calcium-dependent protein kinases
    • Huttner W.B., DeGennaro L.J., and Greengard P. Differential phosphorylation of multiple sites in purified protein I by cyclic AMP-dependent and calcium-dependent protein kinases. J Biol Chem 256 (1981) 1482-1488
    • (1981) J Biol Chem , vol.256 , pp. 1482-1488
    • Huttner, W.B.1    DeGennaro, L.J.2    Greengard, P.3
  • 123
    • 0035955626 scopus 로고    scopus 로고
    • N-methyl-d-aspartate-induced alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid (AMPA) receptor down-regulation involves interaction of the carboxyl terminus of GluR2/3 with Pick1. Ligand-binding studies using Sindbis vectors carrying AMPA receptor decoys
    • Iwakura Y., Nagano T., Kawamura M., Horikawa H., Ibaraki K., Takei N., et al. N-methyl-d-aspartate-induced alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid (AMPA) receptor down-regulation involves interaction of the carboxyl terminus of GluR2/3 with Pick1. Ligand-binding studies using Sindbis vectors carrying AMPA receptor decoys. J Biol Chem 276 (2001) 40025-40032
    • (2001) J Biol Chem , vol.276 , pp. 40025-40032
    • Iwakura, Y.1    Nagano, T.2    Kawamura, M.3    Horikawa, H.4    Ibaraki, K.5    Takei, N.6
  • 124
    • 1842510043 scopus 로고    scopus 로고
    • Differential modulation of NR1-NR2A and NR1-NR2B subtypes of NMDA receptor by PDZ domain-containing proteins
    • Iwamoto T., Yamada Y., Hori K., Watanabe Y., Sobue K., and Inui M. Differential modulation of NR1-NR2A and NR1-NR2B subtypes of NMDA receptor by PDZ domain-containing proteins. J Neurochem 89 (2004) 100-108
    • (2004) J Neurochem , vol.89 , pp. 100-108
    • Iwamoto, T.1    Yamada, Y.2    Hori, K.3    Watanabe, Y.4    Sobue, K.5    Inui, M.6
  • 125
    • 0347182889 scopus 로고    scopus 로고
    • A juvenile form of postsynaptic hippocampal long-term potentiation in mice deficient for the AMPA receptor subunit GluR-A
    • Jensen V., Kaiser K.M., Borchardt T., Adelmann G., Rozov A., Burnashev N., et al. A juvenile form of postsynaptic hippocampal long-term potentiation in mice deficient for the AMPA receptor subunit GluR-A. J Physiol 553 (2003) 843-856
    • (2003) J Physiol , vol.553 , pp. 843-856
    • Jensen, V.1    Kaiser, K.M.2    Borchardt, T.3    Adelmann, G.4    Rozov, A.5    Burnashev, N.6
  • 126
    • 10744232737 scopus 로고    scopus 로고
    • Activity-dependent regulation of dendritic synthesis and trafficking of AMPA receptors
    • Ju W., Morishita W., Tsui J., Gaietta G., Deerinck T.J., Adams S.R., et al. Activity-dependent regulation of dendritic synthesis and trafficking of AMPA receptors. Nat Neurosci 7 (2004) 244-253
    • (2004) Nat Neurosci , vol.7 , pp. 244-253
    • Ju, W.1    Morishita, W.2    Tsui, J.3    Gaietta, G.4    Deerinck, T.J.5    Adams, S.R.6
  • 127
    • 7944234850 scopus 로고    scopus 로고
    • Src in synaptic transmission and plasticity
    • Kalia L.V., Gingrich J.R., and Salter M.W. Src in synaptic transmission and plasticity. Oncogene 23 (2004) 8007-8016
    • (2004) Oncogene , vol.23 , pp. 8007-8016
    • Kalia, L.V.1    Gingrich, J.R.2    Salter, M.W.3
  • 128
    • 0032215153 scopus 로고    scopus 로고
    • Involvement of a postsynaptic protein kinase A substrate in the expression of homosynaptic long-term depression
    • Kameyama K., Lee H.K., Bear M.F., and Huganir R.L. Involvement of a postsynaptic protein kinase A substrate in the expression of homosynaptic long-term depression. Neuron 21 (1998) 1163-1175
    • (1998) Neuron , vol.21 , pp. 1163-1175
    • Kameyama, K.1    Lee, H.K.2    Bear, M.F.3    Huganir, R.L.4
  • 129
    • 0024151163 scopus 로고
    • A persistent postsynaptic modification mediates long-term potentiation in the hippocampus
    • Kauer J.A., Malenka R.C., and Nicoll R.A. A persistent postsynaptic modification mediates long-term potentiation in the hippocampus. Neuron 1 (1988) 911-917
    • (1988) Neuron , vol.1 , pp. 911-917
    • Kauer, J.A.1    Malenka, R.C.2    Nicoll, R.A.3
  • 130
    • 0026525444 scopus 로고
    • Calcium influx through subunits GluR1/GluR3 of kainate/AMPA receptor channels is regulated by cAMP dependent protein kinase
    • Keller B.U., Hollmann M., Heinemann S., and Konnerth A. Calcium influx through subunits GluR1/GluR3 of kainate/AMPA receptor channels is regulated by cAMP dependent protein kinase. EMBO J 11 (1992) 891-896
    • (1992) EMBO J , vol.11 , pp. 891-896
    • Keller, B.U.1    Hollmann, M.2    Heinemann, S.3    Konnerth, A.4
  • 131
    • 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., and 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 U S A 80 (1983) 7357-7361
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 7357-7361
    • Kennedy, M.B.1    Bennett, M.K.2    Erondu, N.E.3
  • 132
    • 0035949629 scopus 로고    scopus 로고
    • Interaction of the AMPA receptor subunit GluR2/3 with PDZ domains regulates hippocampal long-term depression
    • Kim C.H., Chung H.J., Lee H.K., and Huganir R.L. Interaction of the AMPA receptor subunit GluR2/3 with PDZ domains regulates hippocampal long-term depression. Proc Natl Acad Sci U S A 98 (2001) 11725-11730
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11725-11730
    • Kim, C.H.1    Chung, H.J.2    Lee, H.K.3    Huganir, R.L.4
  • 133
    • 0032906585 scopus 로고    scopus 로고
    • Long-term potentiation in the hippocampal CA1 region of mice lacking cGMP-dependent kinases is normal and susceptible to inhibition of nitric oxide synthase
    • Kleppisch T., Pfeifer A., Klatt P., Ruth P., Montkowski A., Fassler R., et al. Long-term potentiation in the hippocampal CA1 region of mice lacking cGMP-dependent kinases is normal and susceptible to inhibition of nitric oxide synthase. J Neurosci 19 (1999) 48-55
    • (1999) J Neurosci , vol.19 , pp. 48-55
    • Kleppisch, T.1    Pfeifer, A.2    Klatt, P.3    Ruth, P.4    Montkowski, A.5    Fassler, R.6
  • 134
    • 0029887725 scopus 로고    scopus 로고
    • Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family
    • Kohr G., and Seeburg P.H. Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family. J Physiol 492 Pt 2 (1996) 445-452
    • (1996) J Physiol , vol.492 , Issue.PART 2 , pp. 445-452
    • Kohr, G.1    Seeburg, P.H.2
  • 135
    • 9144250426 scopus 로고    scopus 로고
    • Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors
    • Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., et al. Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors. Neuron 40 (2003) 1199-1212
    • (2003) Neuron , vol.40 , pp. 1199-1212
    • Kolleker, A.1    Zhu, J.J.2    Schupp, B.J.3    Qin, Y.4    Mack, V.5    Borchardt, T.6
  • 136
    • 0034640259 scopus 로고    scopus 로고
    • Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIalpha and truncated CaM kinase IIalpha reveal a unique organization for its structural core and functional domains
    • Kolodziej S.J., Hudmon A., Waxham M.N., and Stoops J.K. Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIalpha and truncated CaM kinase IIalpha reveal a unique organization for its structural core and functional domains. J Biol Chem 275 (2000) 14354-14359
    • (2000) J Biol Chem , vol.275 , pp. 14354-14359
    • Kolodziej, S.J.1    Hudmon, A.2    Waxham, M.N.3    Stoops, J.K.4
  • 137
    • 0036662781 scopus 로고    scopus 로고
    • Targeted disruption of RC3 reveals a calmodulin-based mechanism for regulating metaplasticity in the hippocampus
    • Krucker T., Siggins G.R., McNamara R.K., Lindsley K.A., Dao A., Allison D.W., et al. Targeted disruption of RC3 reveals a calmodulin-based mechanism for regulating metaplasticity in the hippocampus. J Neurosci 22 (2002) 5525-5535
    • (2002) J Neurosci , vol.22 , pp. 5525-5535
    • Krucker, T.1    Siggins, G.R.2    McNamara, R.K.3    Lindsley, K.A.4    Dao, A.5    Allison, D.W.6
  • 138
    • 0036236357 scopus 로고    scopus 로고
    • Calcineurin acts via the C-terminus of NR2A to modulate desensitization of NMDA receptors
    • Krupp J.J., Vissel B., Thomas C.G., Heinemann S.F., and Westbrook G.L. Calcineurin acts via the C-terminus of NR2A to modulate desensitization of NMDA receptors. Neuropharmacology 42 (2002) 593-602
    • (2002) Neuropharmacology , vol.42 , pp. 593-602
    • Krupp, J.J.1    Vissel, B.2    Thomas, C.G.3    Heinemann, S.F.4    Westbrook, G.L.5
  • 141
    • 0029093990 scopus 로고
    • Differential tyrosine phosphorylation of N-methyl-d-aspartate receptor subunits
    • Lau L.F., and Huganir R.L. Differential tyrosine phosphorylation of N-methyl-d-aspartate receptor subunits. J Biol Chem 270 (1995) 20036-20041
    • (1995) J Biol Chem , vol.270 , pp. 20036-20041
    • Lau, L.F.1    Huganir, R.L.2
  • 142
    • 3242706790 scopus 로고    scopus 로고
    • Subunit-specific regulation of NMDA receptor endocytosis
    • Lavezzari G., McCallum J., Dewey C.M., and Roche K.W. Subunit-specific regulation of NMDA receptor endocytosis. J Neurosci 24 (2004) 6383-6391
    • (2004) J Neurosci , vol.24 , pp. 6383-6391
    • Lavezzari, G.1    McCallum, J.2    Dewey, C.M.3    Roche, K.W.4
  • 143
    • 80053560691 scopus 로고    scopus 로고
    • AMPA receptor phosphorylation in synaptic plasticity: insights from knockin mice
    • Kittler J., and Moss S.J. (Eds), CRC Press, Boca Raton, FL
    • Lee H.K. AMPA receptor phosphorylation in synaptic plasticity: insights from knockin mice. In: Kittler J., and Moss S.J. (Eds). The Dynamic Synapse: Molecular Methods in Ionotropic Receptor Biology (2006), CRC Press, Boca Raton, FL
    • (2006) The Dynamic Synapse: Molecular Methods in Ionotropic Receptor Biology
    • Lee, H.K.1
  • 144
    • 0032214513 scopus 로고    scopus 로고
    • NMDA induces long-term synaptic depression and dephosphorylation of the GluR1 subunit of AMPA receptors in hippocampus
    • Lee H.K., Kameyama K., Huganir R.L., and Bear M.F. NMDA induces long-term synaptic depression and dephosphorylation of the GluR1 subunit of AMPA receptors in hippocampus. Neuron 21 (1998) 1151-1162
    • (1998) Neuron , vol.21 , pp. 1151-1162
    • Lee, H.K.1    Kameyama, K.2    Huganir, R.L.3    Bear, M.F.4
  • 145
    • 0034702259 scopus 로고    scopus 로고
    • Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity
    • Lee H.K., Barbarosie M., Kameyama K., Bear M.F., and Huganir R.L. Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature 405 (2000) 955-959
    • (2000) Nature , vol.405 , pp. 955-959
    • Lee, H.K.1    Barbarosie, M.2    Kameyama, K.3    Bear, M.F.4    Huganir, R.L.5
  • 146
    • 33750032600 scopus 로고    scopus 로고
    • Identification and characterization of a novel phosphorylation site on the GluR1 subunit of AMPA receptors
    • Lee H.K., Takamiya K., Kameyama K., Yu S., Rossetti L., He C., et al. Identification and characterization of a novel phosphorylation site on the GluR1 subunit of AMPA receptors. Soc Neurosci (2002) 747.14
    • (2002) Soc Neurosci
    • Lee, H.K.1    Takamiya, K.2    Kameyama, K.3    Yu, S.4    Rossetti, L.5    He, C.6
  • 147
    • 0037423916 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor GluR1 subunit is required for synaptic plasticity and retention of spatial memory
    • Lee H.K., Takamiya K., Han J.S., Man H., Kim C.H., Rumbaugh G., et al. Phosphorylation of the AMPA receptor GluR1 subunit is required for synaptic plasticity and retention of spatial memory. Cell 112 (2003) 631-643
    • (2003) Cell , vol.112 , pp. 631-643
    • Lee, H.K.1    Takamiya, K.2    Han, J.S.3    Man, H.4    Kim, C.H.5    Rumbaugh, G.6
  • 148
    • 33749988516 scopus 로고    scopus 로고
    • Dissecting out the role of specific AMPA receptor GluR1 phosphorylation sites in long-term potentiation and long-term depression
    • Lee H.K., Takamiya K., Yu S., and Huganir R.L. Dissecting out the role of specific AMPA receptor GluR1 phosphorylation sites in long-term potentiation and long-term depression. Soc Neurosci (2004) 971.8
    • (2004) Soc Neurosci
    • Lee, H.K.1    Takamiya, K.2    Yu, S.3    Huganir, R.L.4
  • 149
    • 0030911620 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase and protein kinase C phosphorylate N-methyl-d-aspartate receptors at different sites
    • Leonard A.S., and Hell J.W. Cyclic AMP-dependent protein kinase and protein kinase C phosphorylate N-methyl-d-aspartate receptors at different sites. J Biol Chem 272 (1997) 12107-12115
    • (1997) J Biol Chem , vol.272 , pp. 12107-12115
    • Leonard, A.S.1    Hell, J.W.2
  • 150
    • 0032584656 scopus 로고    scopus 로고
    • SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit
    • Leonard A.S., Davare M.A., Horne M.C., Garner C.C., and Hell J.W. SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit. J Biol Chem 273 (1998) 19518-19524
    • (1998) J Biol Chem , vol.273 , pp. 19518-19524
    • Leonard, A.S.1    Davare, M.A.2    Horne, M.C.3    Garner, C.C.4    Hell, J.W.5
  • 151
    • 0033026832 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II is associated with the N-methyl-d-aspartate receptor
    • Leonard A.S., Lim I.A., Hemsworth D.E., Horne M.C., and Hell J.W. Calcium/calmodulin-dependent protein kinase II is associated with the N-methyl-d-aspartate receptor. Proc Natl Acad Sci U S A 96 (1999) 3239-3244
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3239-3244
    • Leonard, A.S.1    Lim, I.A.2    Hemsworth, D.E.3    Horne, M.C.4    Hell, J.W.5
  • 152
    • 33747724678 scopus 로고    scopus 로고
    • Stargazer-a mouse to seize!
    • Letts V.A. Stargazer-a mouse to seize!. Epilepsy Curr 5 (2005) 161-165
    • (2005) Epilepsy Curr , vol.5 , pp. 161-165
    • Letts, V.A.1
  • 153
    • 0034120051 scopus 로고    scopus 로고
    • The postsynaptic density protein PSD95 differentially regulates insulin- and Src-mediated current modulation of mouse NMDA receptors expressed in Xenopus oocytes
    • Liao G.Y., Kreitzer M.A., Sweetman B.J., and Leonard J.P. The postsynaptic density protein PSD95 differentially regulates insulin- and Src-mediated current modulation of mouse NMDA receptors expressed in Xenopus oocytes. J Neurochem 75 (2000) 282-287
    • (2000) J Neurochem , vol.75 , pp. 282-287
    • Liao, G.Y.1    Kreitzer, M.A.2    Sweetman, B.J.3    Leonard, J.P.4
  • 154
    • 0035040079 scopus 로고    scopus 로고
    • Evidence for direct protein kinase-C mediated modulation of N-methyl-d-aspartate receptor current
    • Liao G.Y., Wagner D.A., Hsu M.H., and Leonard J.P. Evidence for direct protein kinase-C mediated modulation of N-methyl-d-aspartate receptor current. Mol Pharmacol 59 (2001) 960-964
    • (2001) Mol Pharmacol , vol.59 , pp. 960-964
    • Liao, G.Y.1    Wagner, D.A.2    Hsu, M.H.3    Leonard, J.P.4
  • 157
    • 0010424768 scopus 로고
    • A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase
    • Lisman J.E. A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase. Proc Natl Acad Sci U S A 82 (1985) 3055-3057
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 3055-3057
    • Lisman, J.E.1
  • 158
    • 0024341227 scopus 로고
    • A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory
    • Lisman J. A mechanism for the Hebb and the anti-Hebb processes underlying learning and memory. Proc Natl Acad Sci U S A 86 (1989) 9574-9578
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 9574-9578
    • Lisman, J.1
  • 159
    • 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
  • 160
    • 0035797491 scopus 로고    scopus 로고
    • A model of synaptic memory: a CaMKII/PP1 switch that potentiates transmission by organizing an AMPA receptor anchoring assembly
    • Lisman J.E., and Zhabotinsky A.M. A model of synaptic memory: a CaMKII/PP1 switch that potentiates transmission by organizing an AMPA receptor anchoring assembly. Neuron 31 (2001) 191-201
    • (2001) Neuron , vol.31 , pp. 191-201
    • Lisman, J.E.1    Zhabotinsky, A.M.2
  • 161
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • Lisman J., Schulman H., and Cline H. The molecular basis of CaMKII function in synaptic and behavioural memory. Nat Rev Neurosci 3 (2002) 175-190
    • (2002) Nat Rev Neurosci , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 163
    • 2342637165 scopus 로고    scopus 로고
    • Role of NMDA receptor subtypes in governing the direction of hippocampal synaptic plasticity
    • Liu L., Wong T.P., Pozza M.F., Lingenhoehl K., Wang Y., Sheng M., et al. Role of NMDA receptor subtypes in governing the direction of hippocampal synaptic plasticity. Science 304 (2004) 1021-1024
    • (2004) Science , vol.304 , pp. 1021-1024
    • Liu, L.1    Wong, T.P.2    Pozza, M.F.3    Lingenhoehl, K.4    Wang, Y.5    Sheng, M.6
  • 164
    • 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., and Nicoll R.A. Calcium/calmodulin-dependent kinase II and long-term potentiation enhance synaptic transmission by the same mechanism. Proc Natl Acad Sci U S A 92 (1995) 11175-11179
    • (1995) Proc Natl Acad Sci U S A , 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
  • 165
    • 0024348039 scopus 로고
    • 2+/calmodulin-dependent protein kinase
    • 2+/calmodulin-dependent protein kinase. J Neurosci 9 (1989) 2020-2032
    • (1989) J Neurosci , vol.9 , pp. 2020-2032
    • Lou, L.L.1    Schulman, H.2
  • 166
    • 0023633194 scopus 로고
    • Protein kinase C inhibitors eliminate hippocampal long-term potentiation
    • Lovinger D.M., Wong K.L., Murakami K., and Routtenberg A. Protein kinase C inhibitors eliminate hippocampal long-term potentiation. Brain Res 436 (1987) 177-183
    • (1987) Brain Res , vol.436 , pp. 177-183
    • Lovinger, D.M.1    Wong, K.L.2    Murakami, K.3    Routtenberg, A.4
  • 167
    • 23044457365 scopus 로고    scopus 로고
    • PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking
    • Lu W., and Ziff E.B. PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking. Neuron 47 (2005) 407-421
    • (2005) Neuron , vol.47 , pp. 407-421
    • Lu, W.1    Ziff, E.B.2
  • 168
    • 0001048711 scopus 로고    scopus 로고
    • Src activation in the induction of long-term potentiation in CA1 hippocampal neurons
    • Lu Y.M., Roder J.C., Davidow J., and Salter M.W. Src activation in the induction of long-term potentiation in CA1 hippocampal neurons. Science 279 (1998) 1363-1367
    • (1998) Science , vol.279 , pp. 1363-1367
    • Lu, Y.M.1    Roder, J.C.2    Davidow, J.3    Salter, M.W.4
  • 169
    • 0033493229 scopus 로고    scopus 로고
    • Nitric oxide signaling contributes to late-phase LTP and CREB phosphorylation in the hippocampus
    • Lu Y.F., Kandel E.R., and Hawkins R.D. Nitric oxide signaling contributes to late-phase LTP and CREB phosphorylation in the hippocampus. J Neurosci 19 (1999) 10250-10261
    • (1999) J Neurosci , vol.19 , pp. 10250-10261
    • Lu, Y.F.1    Kandel, E.R.2    Hawkins, R.D.3
  • 170
    • 0033711436 scopus 로고    scopus 로고
    • Calcineurin-mediated LTD of GABAergic inhibition underlies the increased excitability of CA1 neurons associated with LTP
    • Lu Y.M., Mansuy I.M., Kandel E.R., and Roder J. Calcineurin-mediated LTD of GABAergic inhibition underlies the increased excitability of CA1 neurons associated with LTP. Neuron 26 (2000) 197-205
    • (2000) Neuron , vol.26 , pp. 197-205
    • Lu, Y.M.1    Mansuy, I.M.2    Kandel, E.R.3    Roder, J.4
  • 172
    • 0035967952 scopus 로고    scopus 로고
    • Conditional restoration of hippocampal synaptic potentiation in Glur-A-deficient mice
    • Mack V., Burnashev N., Kaiser K.M., Rozov A., Jensen V., Hvalby O., et al. Conditional restoration of hippocampal synaptic potentiation in Glur-A-deficient mice. Science 292 (2001) 2501-2504
    • (2001) Science , vol.292 , pp. 2501-2504
    • Mack, V.1    Burnashev, N.2    Kaiser, K.M.3    Rozov, A.4    Jensen, V.5    Hvalby, O.6
  • 173
    • 0036483593 scopus 로고    scopus 로고
    • The structure and function of glutamate receptor ion channels
    • Madden D.R. The structure and function of glutamate receptor ion channels. Nat Rev Neurosci 3 (2002) 91-101
    • (2002) Nat Rev Neurosci , vol.3 , pp. 91-101
    • Madden, D.R.1
  • 174
    • 13744257897 scopus 로고    scopus 로고
    • Selective reconfiguration of layer 4 visual cortical circuitry by visual deprivation
    • Maffei A., Nelson S.B., and Turrigiano G.G. Selective reconfiguration of layer 4 visual cortical circuitry by visual deprivation. Nat Neurosci 7 (2004) 1353-1359
    • (2004) Nat Neurosci , vol.7 , pp. 1353-1359
    • Maffei, A.1    Nelson, S.B.2    Turrigiano, G.G.3
  • 175
    • 5344241223 scopus 로고    scopus 로고
    • LTP and LTD: an embarrassment of riches
    • Malenka R.C., and Bear M.F. LTP and LTD: an embarrassment of riches. Neuron 44 (2004) 5-21
    • (2004) Neuron , vol.44 , pp. 5-21
    • Malenka, R.C.1    Bear, M.F.2
  • 176
    • 0024393433 scopus 로고
    • An essential role for postsynaptic calmodulin and protein kinase activity in long-term potentiation
    • Malenka R.C., Kauer J.A., Perkel D.J., Mauk M.D., Kelly P.T., Nicoll R.A., et al. An essential role for postsynaptic calmodulin and protein kinase activity in long-term potentiation. Nature 340 (1989) 554-557
    • (1989) Nature , vol.340 , pp. 554-557
    • Malenka, R.C.1    Kauer, J.A.2    Perkel, D.J.3    Mauk, M.D.4    Kelly, P.T.5    Nicoll, R.A.6
  • 177
    • 0024461379 scopus 로고
    • Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP
    • Malinow R., Schulman H., and Tsien R.W. Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP. Science 245 (1989) 862-866
    • (1989) Science , vol.245 , pp. 862-866
    • Malinow, R.1    Schulman, H.2    Tsien, R.W.3
  • 178
    • 0035831033 scopus 로고    scopus 로고
    • Inducible and reversible enhancement of learning, memory, and long-term potentiation by genetic inhibition of calcineurin
    • Malleret G., Haditsch U., Genoux D., Jones M.W., Bliss T.V., Vanhoose A.M., et al. Inducible and reversible enhancement of learning, memory, and long-term potentiation by genetic inhibition of calcineurin. Cell 104 (2001) 675-686
    • (2001) Cell , vol.104 , pp. 675-686
    • Malleret, G.1    Haditsch, U.2    Genoux, D.3    Jones, M.W.4    Bliss, T.V.5    Vanhoose, A.M.6
  • 179
    • 0031435496 scopus 로고    scopus 로고
    • Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II
    • Mammen A.L., Kameyama K., Roche K.W., and Huganir R.L. Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II. J Biol Chem 272 (1997) 32528-32533
    • (1997) J Biol Chem , vol.272 , pp. 32528-32533
    • Mammen, A.L.1    Kameyama, K.2    Roche, K.W.3    Huganir, R.L.4
  • 180
    • 0027480426 scopus 로고
    • AMPA glutamate receptor subunits are differentially distributed in rat brain
    • Martin L.J., Blackstone C.D., Levey A.I., Huganir R.L., and Price D.L. AMPA glutamate receptor subunits are differentially distributed in rat brain. Neuroscience 53 (1993) 327-358
    • (1993) Neuroscience , vol.53 , pp. 327-358
    • Martin, L.J.1    Blackstone, C.D.2    Levey, A.I.3    Huganir, R.L.4    Price, D.L.5
  • 181
    • 4544373236 scopus 로고    scopus 로고
    • Differential roles of NR2A and NR2B-containing NMDA receptors in cortical long-term potentiation and long-term depression
    • Massey P.V., Johnson B.E., Moult P.R., Auberson Y.P., Brown M.W., Molnar E., et al. Differential roles of NR2A and NR2B-containing NMDA receptors in cortical long-term potentiation and long-term depression. J Neurosci 24 (2004) 7821-7828
    • (2004) J Neurosci , vol.24 , pp. 7821-7828
    • Massey, P.V.1    Johnson, B.E.2    Moult, P.R.3    Auberson, Y.P.4    Brown, M.W.5    Molnar, E.6
  • 182
    • 0029829890 scopus 로고    scopus 로고
    • Site-specific phosphorylation of synapsin I by mitogen-activated protein kinase and Cdk5 and its effects on physiological functions
    • Matsubara M., Kusubata M., Ishiguro K., Uchida T., Titani K., and Taniguchi H. Site-specific phosphorylation of synapsin I by mitogen-activated protein kinase and Cdk5 and its effects on physiological functions. J Biol Chem 271 (1996) 21108-21113
    • (1996) J Biol Chem , vol.271 , pp. 21108-21113
    • Matsubara, M.1    Kusubata, M.2    Ishiguro, K.3    Uchida, T.4    Titani, K.5    Taniguchi, H.6
  • 183
    • 0032823580 scopus 로고    scopus 로고
    • Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein
    • Matsuda S., Mikawa S., and Hirai H. Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein. J Neurochem 73 (1999) 1765-1768
    • (1999) J Neurochem , vol.73 , pp. 1765-1768
    • Matsuda, S.1    Mikawa, S.2    Hirai, H.3
  • 184
    • 0027160056 scopus 로고
    • Protein kinase A inhibitors prevent the maintenance of hippocampal long-term potentiation
    • Matthies H., and Reymann K.G. Protein kinase A inhibitors prevent the maintenance of hippocampal long-term potentiation. NeuroReport 4 (1993) 712-714
    • (1993) NeuroReport , vol.4 , pp. 712-714
    • Matthies, H.1    Reymann, K.G.2
  • 185
    • 3242672694 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines
    • Mauceri D., Cattabeni F., Di Luca M., and Gardoni F. Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines. J Biol Chem 279 (2004) 23813-23821
    • (2004) J Biol Chem , vol.279 , pp. 23813-23821
    • Mauceri, D.1    Cattabeni, F.2    Di Luca, M.3    Gardoni, F.4
  • 187
    • 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., and 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
  • 188
    • 0034787414 scopus 로고    scopus 로고
    • Identification of protein kinase C phosphorylation sites within the AMPA receptor GluR2 subunit
    • McDonald B.J., Chung H.J., and Huganir R.L. Identification of protein kinase C phosphorylation sites within the AMPA receptor GluR2 subunit. Neuropharmacology 41 (2001) 672-679
    • (2001) Neuropharmacology , vol.41 , pp. 672-679
    • McDonald, B.J.1    Chung, H.J.2    Huganir, R.L.3
  • 189
    • 0030245775 scopus 로고    scopus 로고
    • Synaptic economics: competition and cooperation in synaptic plasticity
    • Miller K.D. Synaptic economics: competition and cooperation in synaptic plasticity. Neuron 17 (1996) 371-374
    • (1996) Neuron , vol.17 , pp. 371-374
    • Miller, K.D.1
  • 190
    • 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
  • 191
    • 0036813653 scopus 로고    scopus 로고
    • Group I metabotropic glutamate receptor signaling via Galpha q/Galpha 11 secures the induction of long-term potentiation in the hippocampal area CA1
    • Miura M., Watanabe M., Offermanns S., Simon M.I., and Kano M. Group I metabotropic glutamate receptor signaling via Galpha q/Galpha 11 secures the induction of long-term potentiation in the hippocampal area CA1. J Neurosci 22 (2002) 8379-8390
    • (2002) J Neurosci , vol.22 , pp. 8379-8390
    • Miura, M.1    Watanabe, M.2    Offermanns, S.3    Simon, M.I.4    Kano, M.5
  • 192
    • 0028343648 scopus 로고
    • Developmental and regional expression in the rat brain and functional properties of four NMDA receptors
    • Monyer H., Burnashev N., Laurie D.J., Sakmann B., and Seeburg P.H. Developmental and regional expression in the rat brain and functional properties of four NMDA receptors. Neuron 12 (1994) 529-540
    • (1994) Neuron , vol.12 , pp. 529-540
    • Monyer, H.1    Burnashev, N.2    Laurie, D.J.3    Sakmann, B.4    Seeburg, P.H.5
  • 193
    • 23044455322 scopus 로고    scopus 로고
    • Distinct triggering and expression mechanisms underlie LTD of AMPA and NMDA synaptic responses
    • Morishita W., Marie H., and Malenka R.C. Distinct triggering and expression mechanisms underlie LTD of AMPA and NMDA synaptic responses. Nat Neurosci 8 (2005) 1043-1050
    • (2005) Nat Neurosci , vol.8 , pp. 1043-1050
    • Morishita, W.1    Marie, H.2    Malenka, R.C.3
  • 194
    • 0027389679 scopus 로고
    • Phosphorylation of recombinant non-NMDA glutamate receptors on serine and tyrosine residues
    • Moss S.J., Blackstone C.D., and Huganir R.L. Phosphorylation of recombinant non-NMDA glutamate receptors on serine and tyrosine residues. Neurochem Res 18 (1993) 105-110
    • (1993) Neurochem Res , vol.18 , pp. 105-110
    • Moss, S.J.1    Blackstone, C.D.2    Huganir, R.L.3
  • 195
    • 0344688265 scopus 로고    scopus 로고
    • Activity-dependent mRNA splicing controls ER export and synaptic delivery of NMDA receptors
    • Mu Y., Otsuka T., Horton A.C., Scott D.B., and Ehlers M.D. Activity-dependent mRNA splicing controls ER export and synaptic delivery of NMDA receptors. Neuron 40 (2003) 581-594
    • (2003) Neuron , vol.40 , pp. 581-594
    • Mu, Y.1    Otsuka, T.2    Horton, A.C.3    Scott, D.B.4    Ehlers, M.D.5
  • 196
    • 0026458086 scopus 로고
    • Mechanisms underlying induction of homosynaptic long-term depression in area CA1 of the hippocampus
    • Mulkey R.M., and Malenka R.C. Mechanisms underlying induction of homosynaptic long-term depression in area CA1 of the hippocampus. Neuron 9 (1992) 967-975
    • (1992) Neuron , vol.9 , pp. 967-975
    • Mulkey, R.M.1    Malenka, R.C.2
  • 197
    • 0027432518 scopus 로고
    • An essential role for protein phosphatases in hippocampal long-term depression
    • Mulkey R.M., Herron C.E., and Malenka R.C. An essential role for protein phosphatases in hippocampal long-term depression. Science 261 (1993) 1051-1055
    • (1993) Science , vol.261 , pp. 1051-1055
    • Mulkey, R.M.1    Herron, C.E.2    Malenka, R.C.3
  • 198
    • 0028176087 scopus 로고
    • Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression
    • Mulkey R.M., Endo S., Shenolikar S., and Malenka R.C. Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression. Nature 369 (1994) 486-488
    • (1994) Nature , vol.369 , pp. 486-488
    • Mulkey, R.M.1    Endo, S.2    Shenolikar, S.3    Malenka, R.C.4
  • 199
    • 0942290621 scopus 로고    scopus 로고
    • Regulation by metabotropic glutamate receptor 5 of LTP in the dentate gyrus of freely moving rats: relevance for learning and memory formation
    • Naie K., and Manahan-Vaughan D. Regulation by metabotropic glutamate receptor 5 of LTP in the dentate gyrus of freely moving rats: relevance for learning and memory formation. Cereb Cortex 14 (2004) 189-198
    • (2004) Cereb Cortex , vol.14 , pp. 189-198
    • Naie, K.1    Manahan-Vaughan, D.2
  • 200
    • 13444302564 scopus 로고    scopus 로고
    • Structure and different conformational states of native AMPA receptor complexes
    • Nakagawa T., Cheng Y., Ramm E., Sheng M., and Walz T. Structure and different conformational states of native AMPA receptor complexes. Nature 433 (2005) 545-549
    • (2005) Nature , vol.433 , pp. 545-549
    • Nakagawa, T.1    Cheng, Y.2    Ramm, E.3    Sheng, M.4    Walz, T.5
  • 201
    • 0025221685 scopus 로고
    • A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties
    • Nakanishi N., Shneider N.A., and Axel R. A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties. Neuron 5 (1990) 569-581
    • (1990) Neuron , vol.5 , pp. 569-581
    • Nakanishi, N.1    Shneider, N.A.2    Axel, R.3
  • 202
    • 0035808467 scopus 로고    scopus 로고
    • Characterization of Fyn-mediated tyrosine phosphorylation sites on GluR epsilon 2 (NR2B) subunit of the N-methyl-D-aspartate receptor
    • Nakazawa T., Komai S., Tezuka T., Hisatsune C., Umemori H., Semba K., et al. Characterization of Fyn-mediated tyrosine phosphorylation sites on GluR epsilon 2 (NR2B) subunit of the N-methyl-D-aspartate receptor. J Biol Chem 276 (2001) 693-699
    • (2001) J Biol Chem , vol.276 , pp. 693-699
    • Nakazawa, T.1    Komai, S.2    Tezuka, T.3    Hisatsune, C.4    Umemori, H.5    Semba, K.6
  • 203
    • 32544450453 scopus 로고    scopus 로고
    • Relating NMDA receptor function to receptor subunit composition: limitations of the pharmacological approach
    • Neyton J., and Paoletti P. Relating NMDA receptor function to receptor subunit composition: limitations of the pharmacological approach. J Neurosci 26 (2006) 1331-1333
    • (2006) J Neurosci , vol.26 , pp. 1331-1333
    • Neyton, J.1    Paoletti, P.2
  • 204
    • 0842330769 scopus 로고    scopus 로고
    • Regulation of hippocampal synaptic plasticity by cyclic AMP-dependent protein kinases
    • Nguyen P.V., and Woo N.H. Regulation of hippocampal synaptic plasticity by cyclic AMP-dependent protein kinases. Prog Neurobiol 71 (2003) 401-437
    • (2003) Prog Neurobiol , vol.71 , pp. 401-437
    • Nguyen, P.V.1    Woo, N.H.2
  • 205
    • 33644674232 scopus 로고    scopus 로고
    • Auxiliary subunits assist AMPA-type glutamate receptors
    • Nicoll R.A., Tomita S., and Bredt D.S. Auxiliary subunits assist AMPA-type glutamate receptors. Science 311 (2006) 1253-1256
    • (2006) Science , vol.311 , pp. 1253-1256
    • Nicoll, R.A.1    Tomita, S.2    Bredt, D.S.3
  • 206
    • 0021260967 scopus 로고
    • Magnesium gates glutamate-activated channels in mouse central neurones
    • Nowak L., Bregestovski P., Ascher P., Herbet A., and Prochiantz A. Magnesium gates glutamate-activated channels in mouse central neurones. Nature 307 (1984) 462-465
    • (1984) Nature , vol.307 , pp. 462-465
    • Nowak, L.1    Bregestovski, P.2    Ascher, P.3    Herbet, A.4    Prochiantz, A.5
  • 208
    • 0025995324 scopus 로고
    • Long-term potentiation in the hippocampus is blocked by tyrosine kinase inhibitors
    • O'Dell T.J., Kandel E.R., and Grant S.G. Long-term potentiation in the hippocampus is blocked by tyrosine kinase inhibitors. Nature 353 (1991) 558-560
    • (1991) Nature , vol.353 , pp. 558-560
    • O'Dell, T.J.1    Kandel, E.R.2    Grant, S.G.3
  • 209
    • 24944528380 scopus 로고    scopus 로고
    • Dominant role of the GluR2 subunit in regulation of AMPA receptors by CaMKII
    • Oh M.C., and Derkach V.A. Dominant role of the GluR2 subunit in regulation of AMPA receptors by CaMKII. Nat Neurosci 8 (2005) 853-854
    • (2005) Nat Neurosci , vol.8 , pp. 853-854
    • Oh, M.C.1    Derkach, V.A.2
  • 210
    • 33644851262 scopus 로고    scopus 로고
    • Extrasynaptic membrane trafficking regulated by GluR1 serine 845 phosphorylation primes AMPA receptors for long-term potentiation
    • Oh M.C., Derkach V.A., Guire E.S., and Soderling T.R. Extrasynaptic membrane trafficking regulated by GluR1 serine 845 phosphorylation primes AMPA receptors for long-term potentiation. J Biol Chem 281 (2006) 752-758
    • (2006) J Biol Chem , vol.281 , pp. 752-758
    • Oh, M.C.1    Derkach, V.A.2    Guire, E.S.3    Soderling, T.R.4
  • 211
    • 0029905992 scopus 로고    scopus 로고
    • Identification of a phosphorylation site for calcium/calmodulindependent 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., and Kennedy M.B. Identification of a phosphorylation site for calcium/calmodulindependent 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
  • 212
    • 0033724730 scopus 로고    scopus 로고
    • Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor
    • Osten P., Khatri L., Perez J.L., Kohr G., Giese G., Daly C., et al. Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor. Neuron 27 (2000) 313-325
    • (2000) Neuron , vol.27 , pp. 313-325
    • Osten, P.1    Khatri, L.2    Perez, J.L.3    Kohr, G.4    Giese, G.5    Daly, C.6
  • 213
    • 0030857360 scopus 로고    scopus 로고
    • Postsynaptic inhibitors of calcium/calmodulin-dependent protein kinase type II block induction but not maintenance of pairing-induced long-term potentiation
    • Otmakhov N., Griffith L.C., and Lisman J.E. Postsynaptic inhibitors of calcium/calmodulin-dependent protein kinase type II block induction but not maintenance of pairing-induced long-term potentiation. J Neurosci 17 (1997) 5357-5365
    • (1997) J Neurosci , vol.17 , pp. 5357-5365
    • Otmakhov, N.1    Griffith, L.C.2    Lisman, J.E.3
  • 214
    • 7044270772 scopus 로고    scopus 로고
    • Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation
    • Otmakhov N., Tao-Cheng J.H., Carpenter S., Asrican B., Dosemeci A., Reese T.S., et al. Persistent accumulation of calcium/calmodulin-dependent protein kinase II in dendritic spines after induction of NMDA receptor-dependent chemical long-term potentiation. J Neurosci 24 (2004) 9324-9331
    • (2004) J Neurosci , vol.24 , pp. 9324-9331
    • Otmakhov, N.1    Tao-Cheng, J.H.2    Carpenter, S.3    Asrican, B.4    Dosemeci, A.5    Reese, T.S.6
  • 215
    • 0034660162 scopus 로고    scopus 로고
    • Inhibition of the cAMP pathway decreases early long-term potentiation at CA1 hippocampal synapses
    • Otmakhova N.A., Otmakhov N., Mortenson L.H., and Lisman J.E. Inhibition of the cAMP pathway decreases early long-term potentiation at CA1 hippocampal synapses. J Neurosci 20 (2000) 4446-4451
    • (2000) J Neurosci , vol.20 , pp. 4446-4451
    • Otmakhova, N.A.1    Otmakhov, N.2    Mortenson, L.H.3    Lisman, J.E.4
  • 216
    • 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., and 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
  • 218
    • 0034633680 scopus 로고    scopus 로고
    • Involvement of neurogranin in the modulation of calcium/calmodulin-dependent protein kinase II, synaptic plasticity, and spatial learning: a study with knockout mice
    • Pak J.H., Huang F.L., Li J., Balschun D., Reymann K.G., Chiang C., et al. Involvement of neurogranin in the modulation of calcium/calmodulin-dependent protein kinase II, synaptic plasticity, and spatial learning: a study with knockout mice. Proc Natl Acad Sci U S A 97 (2000) 11232-11237
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11232-11237
    • Pak, J.H.1    Huang, F.L.2    Li, J.3    Balschun, D.4    Reymann, K.G.5    Chiang, C.6
  • 219
    • 2542609999 scopus 로고    scopus 로고
    • Multiple, developmentally regulated expression mechanisms of long-term potentiation at CA1 synapses
    • Palmer M.J., Isaac J.T., and Collingridge G.L. Multiple, developmentally regulated expression mechanisms of long-term potentiation at CA1 synapses. J Neurosci 24 (2004) 4903-4911
    • (2004) J Neurosci , vol.24 , pp. 4903-4911
    • Palmer, M.J.1    Isaac, J.T.2    Collingridge, G.L.3
  • 220
    • 0025294106 scopus 로고
    • 2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain
    • 2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain. J Biol Chem 265 (1990) 11204-11212
    • (1990) J Biol Chem , vol.265 , pp. 11204-11212
    • Patton, B.L.1    Miller, S.G.2    Kennedy, M.B.3
  • 221
    • 0037187645 scopus 로고    scopus 로고
    • Tyrosine phosphatase STEP is a tonic brake on induction of long-term potentiation
    • Pelkey K.A., Askalan R., Paul S., Kalia L.V., Nguyen T.H., Pitcher G.M., et al. Tyrosine phosphatase STEP is a tonic brake on induction of long-term potentiation. Neuron 34 (2002) 127-138
    • (2002) Neuron , vol.34 , pp. 127-138
    • Pelkey, K.A.1    Askalan, R.2    Paul, S.3    Kalia, L.V.4    Nguyen, T.H.5    Pitcher, G.M.6
  • 222
    • 2442683994 scopus 로고    scopus 로고
    • Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry
    • Peng J., Kim M.J., Cheng D., Duong D.M., Gygi S.P., and Sheng M. Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry. J Biol Chem 279 (2004) 21003-21011
    • (2004) J Biol Chem , vol.279 , pp. 21003-21011
    • Peng, J.1    Kim, M.J.2    Cheng, D.3    Duong, D.M.4    Gygi, S.P.5    Sheng, M.6
  • 223
    • 0035425710 scopus 로고    scopus 로고
    • PICK1 targets activated protein kinase Calpha to AMPA receptor clusters in spines of hippocampal neurons and reduces surface levels of the AMPA-type glutamate receptor subunit 2
    • Perez J.L., Khatri L., Chang C., Srivastava S., Osten P., and Ziff E.B. PICK1 targets activated protein kinase Calpha to AMPA receptor clusters in spines of hippocampal neurons and reduces surface levels of the AMPA-type glutamate receptor subunit 2. J Neurosci 21 (2001) 5417-5428
    • (2001) J Neurosci , vol.21 , pp. 5417-5428
    • Perez, J.L.1    Khatri, L.2    Chang, C.3    Srivastava, S.4    Osten, P.5    Ziff, E.B.6
  • 224
    • 21544468215 scopus 로고    scopus 로고
    • Homeostatic plasticity and NMDA receptor trafficking
    • Perez-Otano I., and Ehlers M.D. Homeostatic plasticity and NMDA receptor trafficking. Trends Neurosci 28 (2005) 229-238
    • (2005) Trends Neurosci , vol.28 , pp. 229-238
    • Perez-Otano, I.1    Ehlers, M.D.2
  • 225
    • 0026560573 scopus 로고
    • Light and electron immunocytochemical localization of AMPA-selective glutamate receptors in the rat brain
    • Petralia R.S., and Wenthold R.J. Light and electron immunocytochemical localization of AMPA-selective glutamate receptors in the rat brain. J Comp Neurol 318 (1992) 329-354
    • (1992) J Comp Neurol , vol.318 , pp. 329-354
    • Petralia, R.S.1    Wenthold, R.J.2
  • 226
    • 0028579743 scopus 로고
    • Potentiated transmission and prevention of further LTP by increased CaMKII activity in postsynaptic hippocampal slice neurons
    • Pettit D.L., Perlman S., and Malinow R. Potentiated transmission and prevention of further LTP by increased CaMKII 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
  • 227
    • 0035132867 scopus 로고    scopus 로고
    • Visual experience and deprivation bidirectionally modify the composition and function of NMDA receptors in visual cortex
    • Philpot B.D., Sekhar A.K., Shouval H.Z., and Bear M.F. Visual experience and deprivation bidirectionally modify the composition and function of NMDA receptors in visual cortex. Neuron 29 (2001) 157-169
    • (2001) Neuron , vol.29 , pp. 157-169
    • Philpot, B.D.1    Sekhar, A.K.2    Shouval, H.Z.3    Bear, M.F.4
  • 228
    • 0038045581 scopus 로고    scopus 로고
    • Evidence for altered NMDA receptor function as a basis for metaplasticity in visual cortex
    • Philpot B.D., Espinosa J.S., and Bear M.F. Evidence for altered NMDA receptor function as a basis for metaplasticity in visual cortex. J Neurosci 23 (2003) 5583-5588
    • (2003) J Neurosci , vol.23 , pp. 5583-5588
    • Philpot, B.D.1    Espinosa, J.S.2    Bear, M.F.3
  • 229
    • 0023718841 scopus 로고
    • Phosphorylation of protein B-50 (GAP-43) from adult rat brain cortex by casein kinase II
    • Pisano M.R., Hegazy M.G., Reimann E.M., and Dokas L.A. Phosphorylation of protein B-50 (GAP-43) from adult rat brain cortex by casein kinase II. Biochem Biophys Res Commun 155 (1988) 1207-1212
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 1207-1212
    • Pisano, M.R.1    Hegazy, M.G.2    Reimann, E.M.3    Dokas, L.A.4
  • 231
    • 0033583238 scopus 로고    scopus 로고
    • Interactions between neurogranin and calmodulin in vivo
    • Prichard L., Deloulme J.C., and Storm D.R. Interactions between neurogranin and calmodulin in vivo. J Biol Chem 274 (1999) 7689-7694
    • (1999) J Biol Chem , vol.274 , pp. 7689-7694
    • Prichard, L.1    Deloulme, J.C.2    Storm, D.R.3
  • 232
    • 14944366485 scopus 로고    scopus 로고
    • Stargazin reduces desensitization and slows deactivation of the AMPA-type glutamate receptors
    • Priel A., Kolleker A., Ayalon G., Gillor M., Osten P., and Stern-Bach Y. Stargazin reduces desensitization and slows deactivation of the AMPA-type glutamate receptors. J Neurosci 25 (2005) 2682-2686
    • (2005) J Neurosci , vol.25 , pp. 2682-2686
    • Priel, A.1    Kolleker, A.2    Ayalon, G.3    Gillor, M.4    Osten, P.5    Stern-Bach, Y.6
  • 233
    • 24644491679 scopus 로고    scopus 로고
    • The synaptic localization of NR2B-containing NMDA receptors is controlled by interactions with PDZ proteins and AP-2
    • Prybylowski K., Chang K., Sans N., Kan L., Vicini S., and Wenthold R.J. The synaptic localization of NR2B-containing NMDA receptors is controlled by interactions with PDZ proteins and AP-2. Neuron 47 (2005) 845-857
    • (2005) Neuron , vol.47 , pp. 845-857
    • Prybylowski, K.1    Chang, K.2    Sans, N.3    Kan, L.4    Vicini, S.5    Wenthold, R.J.6
  • 234
    • 9044233633 scopus 로고    scopus 로고
    • Impaired hippocampal plasticity in mice lacking the Cbeta1 catalytic subunit of cAMP-dependent protein kinase
    • Qi M., Zhuo M., Skalhegg B.S., Brandon E.P., Kandel E.R., McKnight G.S., et al. Impaired hippocampal plasticity in mice lacking the Cbeta1 catalytic subunit of cAMP-dependent protein kinase. Proc Natl Acad Sci U S A 93 (1996) 1571-1576
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1571-1576
    • Qi, M.1    Zhuo, M.2    Skalhegg, B.S.3    Brandon, E.P.4    Kandel, E.R.5    McKnight, G.S.6
  • 235
    • 0033607178 scopus 로고    scopus 로고
    • Bidirectional, experience-dependent regulation of N-methyl-d-aspartate receptor subunit composition in the rat visual cortex during postnatal development
    • Quinlan E.M., Olstein D.H., and Bear M.F. Bidirectional, experience-dependent regulation of N-methyl-d-aspartate receptor subunit composition in the rat visual cortex during postnatal development. Proc Natl Acad Sci U S A 96 (1999) 12876-12880
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 12876-12880
    • Quinlan, E.M.1    Olstein, D.H.2    Bear, M.F.3
  • 236
    • 0033359937 scopus 로고    scopus 로고
    • Rapid, experience-dependent expression of synaptic NMDA receptors in visual cortex in vivo
    • Quinlan E.M., Philpot B.D., Huganir R.L., and Bear M.F. Rapid, experience-dependent expression of synaptic NMDA receptors in visual cortex in vivo. Nat Neurosci 2 (1999) 352-357
    • (1999) Nat Neurosci , vol.2 , pp. 352-357
    • Quinlan, E.M.1    Philpot, B.D.2    Huganir, R.L.3    Bear, M.F.4
  • 237
    • 1642452716 scopus 로고    scopus 로고
    • A molecular mechanism for stabilization of learning-induced synaptic modifications
    • Quinlan E.M., Lebel D., Brosh I., and Barkai E. A molecular mechanism for stabilization of learning-induced synaptic modifications. Neuron 41 (2004) 185-192
    • (2004) Neuron , vol.41 , pp. 185-192
    • Quinlan, E.M.1    Lebel, D.2    Brosh, I.3    Barkai, E.4
  • 238
    • 0030998361 scopus 로고    scopus 로고
    • Protein kinase C in synaptic plasticity: changes in the in situ phosphorylation state of identified pre- and postsynaptic substrates
    • Ramakers G.M., Pasinelli P., Hens J.J., Gispen W.H., and De Graan P.N. Protein kinase C in synaptic plasticity: changes in the in situ phosphorylation state of identified pre- and postsynaptic substrates. Prog Neuropsychopharmacol Biol Psychiatry 21 (1997) 455-486
    • (1997) Prog Neuropsychopharmacol Biol Psychiatry , vol.21 , pp. 455-486
    • Ramakers, G.M.1    Pasinelli, P.2    Hens, J.J.3    Gispen, W.H.4    De Graan, P.N.5
  • 239
    • 0033593462 scopus 로고    scopus 로고
    • Substrate phosphorylation in the protein kinase Cgamma knockout mouse
    • Ramakers G.M., Gerendasy D.D., and de Graan P.N. Substrate phosphorylation in the protein kinase Cgamma knockout mouse. J Biol Chem 274 (1999) 1873-1874
    • (1999) J Biol Chem , vol.274 , pp. 1873-1874
    • Ramakers, G.M.1    Gerendasy, D.D.2    de Graan, P.N.3
  • 240
    • 0029670940 scopus 로고    scopus 로고
    • Beta-adrenergic regulation of synaptic NMDA receptors by cAMP-dependent protein kinase
    • Raman I.M., Tong G., and Jahr C.E. Beta-adrenergic regulation of synaptic NMDA receptors by cAMP-dependent protein kinase. Neuron 16 (1996) 415-421
    • (1996) Neuron , vol.16 , pp. 415-421
    • Raman, I.M.1    Tong, G.2    Jahr, C.E.3
  • 241
    • 0034143238 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors trigger homosynaptic protein synthesis to prolong long-term potentiation
    • Raymond C.R., Thompson V.L., Tate W.P., and Abraham W.C. Metabotropic glutamate receptors trigger homosynaptic protein synthesis to prolong long-term potentiation. J Neurosci 20 (2000) 969-976
    • (2000) J Neurosci , vol.20 , pp. 969-976
    • Raymond, C.R.1    Thompson, V.L.2    Tate, W.P.3    Abraham, W.C.4
  • 242
    • 0025624890 scopus 로고
    • Neurogranin: immunocytochemical localization of a brain-specific protein kinase C substrate
    • Represa A., Deloulme J.C., Sensenbrenner M., Ben-Ari Y., and Baudier J. Neurogranin: immunocytochemical localization of a brain-specific protein kinase C substrate. J Neurosci 10 (1990) 3782-3792
    • (1990) J Neurosci , vol.10 , pp. 3782-3792
    • Represa, A.1    Deloulme, J.C.2    Sensenbrenner, M.3    Ben-Ari, Y.4    Baudier, J.5
  • 243
    • 0023732532 scopus 로고
    • Inhibitors of calmodulin and protein kinase C block different phases of hippocampal long-term potentiation
    • Reymann K.G., Brodemann R., Kase H., and Matthies H. Inhibitors of calmodulin and protein kinase C block different phases of hippocampal long-term potentiation. Brain Res 461 (1988) 388-392
    • (1988) Brain Res , vol.461 , pp. 388-392
    • Reymann, K.G.1    Brodemann, R.2    Kase, H.3    Matthies, H.4
  • 244
    • 0023836533 scopus 로고
    • Polymyxin B, an inhibitor of protein kinase C, prevents the maintenance of synaptic long-term potentiation in hippocampal CA1 neurons
    • Reymann K.G., Frey U., Jork R., and Matthies H. Polymyxin B, an inhibitor of protein kinase C, prevents the maintenance of synaptic long-term potentiation in hippocampal CA1 neurons. Brain Res 440 (1988) 305-314
    • (1988) Brain Res , vol.440 , pp. 305-314
    • Reymann, K.G.1    Frey, U.2    Jork, R.3    Matthies, H.4
  • 246
    • 0029828780 scopus 로고    scopus 로고
    • Transient activation of cyclic AMP-dependent protein kinase during hippocampal long-term potentiation
    • Roberson E.D., and Sweatt J.D. Transient activation of cyclic AMP-dependent protein kinase during hippocampal long-term potentiation. J Biol Chem 271 (1996) 30436-30441
    • (1996) J Biol Chem , vol.271 , pp. 30436-30441
    • Roberson, E.D.1    Sweatt, J.D.2
  • 247
    • 0012087319 scopus 로고    scopus 로고
    • Second messengers in LTP and LTD
    • Fazeli M.S., and Collingridge G.L. (Eds), BIOS Scientific Publishers, Oxford
    • Roberson E.D., English J.D., and Sweatt J.D. Second messengers in LTP and LTD. In: Fazeli M.S., and Collingridge G.L. (Eds). Cortical Plasiticity (1996), BIOS Scientific Publishers, Oxford 35-60
    • (1996) Cortical Plasiticity , pp. 35-60
    • Roberson, E.D.1    English, J.D.2    Sweatt, J.D.3
  • 248
    • 0030175899 scopus 로고    scopus 로고
    • Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit
    • Roche K.W., O'Brien R.J., Mammen A.L., Bernhardt J., and Huganir R.L. Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. Neuron 16 (1996) 1179-1188
    • (1996) Neuron , vol.16 , pp. 1179-1188
    • Roche, K.W.1    O'Brien, R.J.2    Mammen, A.L.3    Bernhardt, J.4    Huganir, R.L.5
  • 250
    • 0031471239 scopus 로고    scopus 로고
    • Fear conditioning induces associative long-term potentiation in the amygdala
    • Rogan M.T., Staubli U.V., and LeDoux J.E. Fear conditioning induces associative long-term potentiation in the amygdala. Nature 390 (1997) 604-607
    • (1997) Nature , vol.390 , pp. 604-607
    • Rogan, M.T.1    Staubli, U.V.2    LeDoux, J.E.3
  • 251
    • 0029789826 scopus 로고    scopus 로고
    • Long-term potentiation increases tyrosine phosphorylation of the N-methyl-d-aspartate receptor subunit 2B in rat dentate gyrus in vivo
    • Rosenblum K., Dudai Y., and Richter-Levin G. Long-term potentiation increases tyrosine phosphorylation of the N-methyl-d-aspartate receptor subunit 2B in rat dentate gyrus in vivo. Proc Natl Acad Sci U S A 93 (1996) 10457-10460
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10457-10460
    • Rosenblum, K.1    Dudai, Y.2    Richter-Levin, G.3
  • 252
    • 0028274544 scopus 로고
    • Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons
    • Rosenmund C., Carr D.W., Bergeson S.E., Nilaver G., Scott J.D., and Westbrook G.L. Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons. Nature 368 (1994) 853-856
    • (1994) Nature , vol.368 , pp. 853-856
    • Rosenmund, C.1    Carr, D.W.2    Bergeson, S.E.3    Nilaver, G.4    Scott, J.D.5    Westbrook, G.L.6
  • 253
    • 0029833009 scopus 로고    scopus 로고
    • Enhanced tyrosine phosphorylation of the 2B subunit of the N-methyl-d-aspartate receptor in long-term potentiation
    • Rostas J.A., Brent V.A., Voss K., Errington M.L., Bliss T.V., and Gurd J.W. Enhanced tyrosine phosphorylation of the 2B subunit of the N-methyl-d-aspartate receptor in long-term potentiation. Proc Natl Acad Sci U S A 93 (1996) 10452-10456
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10452-10456
    • Rostas, J.A.1    Brent, V.A.2    Voss, K.3    Errington, M.L.4    Bliss, T.V.5    Gurd, J.W.6
  • 254
    • 27644598355 scopus 로고    scopus 로고
    • TARP gamma-8 controls hippocampal AMPA receptor number, distribution and synaptic plasticity
    • Rouach N., Byrd K., Petralia R.S., Elias G.M., Adesnik H., Tomita S., et al. TARP gamma-8 controls hippocampal AMPA receptor number, distribution and synaptic plasticity. Nat Neurosci 8 (2005) 1525-1533
    • (2005) Nat Neurosci , vol.8 , pp. 1525-1533
    • Rouach, N.1    Byrd, K.2    Petralia, R.S.3    Elias, G.M.4    Adesnik, H.5    Tomita, S.6
  • 255
    • 0032168158 scopus 로고    scopus 로고
    • BDNF has opposite effects on the quantal amplitude of pyramidal neuron and interneuron excitatory synapses
    • Rutherford L.C., Nelson S.B., and Turrigiano G.G. BDNF has opposite effects on the quantal amplitude of pyramidal neuron and interneuron excitatory synapses. Neuron 21 (1998) 521-530
    • (1998) Neuron , vol.21 , pp. 521-530
    • Rutherford, L.C.1    Nelson, S.B.2    Turrigiano, G.G.3
  • 256
    • 0027305085 scopus 로고
    • Persistent activation of the zeta isoform of protein kinase C in the maintenance of long-term potentiation
    • Sacktor T.C., Osten P., Valsamis H., Jiang X., Naik M.U., and Sublette E. Persistent activation of the zeta isoform of protein kinase C in the maintenance of long-term potentiation. Proc Natl Acad Sci U S A 90 (1993) 8342-8346
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8342-8346
    • Sacktor, T.C.1    Osten, P.2    Valsamis, H.3    Jiang, X.4    Naik, M.U.5    Sublette, E.6
  • 257
    • 1842731881 scopus 로고    scopus 로고
    • Src kinases: a hub for NMDA receptor regulation
    • Salter M.W., and Kalia L.V. Src kinases: a hub for NMDA receptor regulation. Nat Rev Neurosci 5 (2004) 317-328
    • (2004) Nat Rev Neurosci , vol.5 , pp. 317-328
    • Salter, M.W.1    Kalia, L.V.2
  • 258
    • 20544432404 scopus 로고    scopus 로고
    • Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms
    • Sanchez-Perez A.M., and Felipo V. Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms. Neurochem Int 47 (2005) 84-91
    • (2005) Neurochem Int , vol.47 , pp. 84-91
    • Sanchez-Perez, A.M.1    Felipo, V.2
  • 259
    • 0033365730 scopus 로고    scopus 로고
    • Can molecules explain long-term potentiation?
    • Sanes J.R., and Lichtman J.W. Can molecules explain long-term potentiation?. Nat Neurosci 2 (1999) 597-604
    • (1999) Nat Neurosci , vol.2 , pp. 597-604
    • Sanes, J.R.1    Lichtman, J.W.2
  • 260
    • 0034143323 scopus 로고    scopus 로고
    • A developmental change in NMDA receptor-associated proteins at hippocampal synapses
    • Sans N., Petralia R.S., Wang Y.X., Blahos II J., Hell J.W., and Wenthold R.J. A developmental change in NMDA receptor-associated proteins at hippocampal synapses. J Neurosci 20 (2000) 1260-1271
    • (2000) J Neurosci , vol.20 , pp. 1260-1271
    • Sans, N.1    Petralia, R.S.2    Wang, Y.X.3    Blahos II, J.4    Hell, J.W.5    Wenthold, R.J.6
  • 261
    • 0035478061 scopus 로고    scopus 로고
    • Synapse-associated protein 97 selectively associates with a subset of AMPA receptors early in their biosynthetic pathway
    • Sans N., Racca C., Petralia R.S., Wang Y.X., McCallum J., and Wenthold R.J. Synapse-associated protein 97 selectively associates with a subset of AMPA receptors early in their biosynthetic pathway. J Neurosci 21 (2001) 7506-7516
    • (2001) J Neurosci , vol.21 , pp. 7506-7516
    • Sans, N.1    Racca, C.2    Petralia, R.S.3    Wang, Y.X.4    McCallum, J.5    Wenthold, R.J.6
  • 264
    • 0022929859 scopus 로고
    • 2+(calmodulin)-dependent protein kinase II by an autophosphorylation mechanism
    • 2+(calmodulin)-dependent protein kinase II by an autophosphorylation mechanism. J Biol Chem 261 (1986) 8581-8584
    • (1986) J Biol Chem , vol.261 , pp. 8581-8584
    • Schworer, C.M.1    Colbran, R.J.2    Soderling, T.R.3
  • 265
    • 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
  • 266
    • 0035341508 scopus 로고    scopus 로고
    • An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
    • Scott D.B., Blanpied T.A., Swanson G.T., Zhang C., and Ehlers M.D. An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing. J Neurosci 21 (2001) 3063-3072
    • (2001) J Neurosci , vol.21 , pp. 3063-3072
    • Scott, D.B.1    Blanpied, T.A.2    Swanson, G.T.3    Zhang, C.4    Ehlers, M.D.5
  • 267
    • 1542614144 scopus 로고    scopus 로고
    • Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors
    • Scott D.B., Blanpied T.A., and Ehlers M.D. Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors. Neuropharmacology 45 (2003) 755-767
    • (2003) Neuropharmacology , vol.45 , pp. 755-767
    • Scott, D.B.1    Blanpied, T.A.2    Ehlers, M.D.3
  • 268
    • 0038721692 scopus 로고    scopus 로고
    • Regulation of ion channel/neurotransmitter receptor function by RNA editing
    • Seeburg P.H., and Hartner J. Regulation of ion channel/neurotransmitter receptor function by RNA editing. Curr Opin Neurobiol 13 (2003) 279-283
    • (2003) Curr Opin Neurobiol , vol.13 , pp. 279-283
    • Seeburg, P.H.1    Hartner, J.2
  • 269
    • 0141919571 scopus 로고    scopus 로고
    • Glutamate receptor subunit 2 Serine 880 phosphorylation modulates synaptic transmission and mediates plasticity in CA1 pyramidal cells
    • Seidenman K.J., Steinberg J.P., Huganir R., and Malinow R. Glutamate receptor subunit 2 Serine 880 phosphorylation modulates synaptic transmission and mediates plasticity in CA1 pyramidal cells. J Neurosci 23 (2003) 9220-9228
    • (2003) J Neurosci , vol.23 , pp. 9220-9228
    • Seidenman, K.J.1    Steinberg, J.P.2    Huganir, R.3    Malinow, R.4
  • 270
    • 0035110525 scopus 로고    scopus 로고
    • Mice lacking the ERK1 isoform of MAP kinase are unimpaired in emotional learning
    • Selcher J.C., Nekrasova T., Paylor R., Landreth G.E., and Sweatt J.D. Mice lacking the ERK1 isoform of MAP kinase are unimpaired in emotional learning. Learn Mem 8 (2001) 11-19
    • (2001) Learn Mem , vol.8 , pp. 11-19
    • Selcher, J.C.1    Nekrasova, T.2    Paylor, R.3    Landreth, G.E.4    Sweatt, J.D.5
  • 272
    • 0029788599 scopus 로고    scopus 로고
    • Examination of the role of cGMP in long-term potentiation in the CA1 region of the hippocampus
    • Selig D.K., Segal M.R., Liao D., Malenka R.C., Malinow R., Nicoll R.A., et al. Examination of the role of cGMP in long-term potentiation in the CA1 region of the hippocampus. Learn Mem 3 (1996) 42-48
    • (1996) Learn Mem , vol.3 , pp. 42-48
    • Selig, D.K.1    Segal, M.R.2    Liao, D.3    Malenka, R.C.4    Malinow, R.5    Nicoll, R.A.6
  • 273
    • 14244254168 scopus 로고    scopus 로고
    • Persistent phosphorylation by protein kinase Mzeta maintains late-phase long-term potentiation
    • Serrano P., Yao Y., and Sacktor T.C. Persistent phosphorylation by protein kinase Mzeta maintains late-phase long-term potentiation. J Neurosci 25 (2005) 1979-1984
    • (2005) J Neurosci , vol.25 , pp. 1979-1984
    • Serrano, P.1    Yao, Y.2    Sacktor, T.C.3
  • 274
    • 0033515884 scopus 로고    scopus 로고
    • Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
    • Shen K., and 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
  • 275
    • 0032148396 scopus 로고    scopus 로고
    • CaMKIIbeta functions as an F-actin targeting module that localizes CaMKIIalpha/beta heterooligomers to dendritic spines
    • Shen K., Teruel M.N., Subramanian K., and Meyer T. CaMKIIbeta functions as an F-actin targeting module that localizes CaMKIIalpha/beta heterooligomers to dendritic spines. Neuron 21 (1998) 593-606
    • (1998) Neuron , vol.21 , pp. 593-606
    • Shen, K.1    Teruel, M.N.2    Subramanian, K.3    Meyer, T.4
  • 276
    • 0033860922 scopus 로고    scopus 로고
    • Molecular memory by reversible translocation of calcium/calmodulin-dependent protein kinase II
    • Shen K., Teruel M.N., Connor J.H., Shenolikar S., and Meyer T. Molecular memory by reversible translocation of calcium/calmodulin-dependent protein kinase II. Nat Neurosci 3 (2000) 881-886
    • (2000) Nat Neurosci , vol.3 , pp. 881-886
    • Shen, K.1    Teruel, M.N.2    Connor, J.H.3    Shenolikar, S.4    Meyer, T.5
  • 277
    • 0028246842 scopus 로고
    • Protein kinase C transiently activated heteromeric N-methyl-d-aspartate receptor channels independent of the phosphorylatable C-terminal splice domain and of consensus phosphorylation sites
    • Sigel E., Baur R., and Malherbe P. Protein kinase C transiently activated heteromeric N-methyl-d-aspartate receptor channels independent of the phosphorylatable C-terminal splice domain and of consensus phosphorylation sites. J Biol Chem 269 (1994) 8204-8208
    • (1994) J Biol Chem , vol.269 , pp. 8204-8208
    • Sigel, E.1    Baur, R.2    Malherbe, P.3
  • 278
    • 0026637195 scopus 로고
    • Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice
    • Silva A.J., Stevens C.F., Tonegawa S., and Wang Y. Deficient hippocampal long-term potentiation in alpha-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
  • 280
    • 33645644069 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase postsynaptic localization regulated by NMDA receptor activation through translocation of an A-kinase anchoring protein scaffold protein
    • Smith K.E., Gibson E.S., and Dell'Acqua M.L. cAMP-dependent protein kinase postsynaptic localization regulated by NMDA receptor activation through translocation of an A-kinase anchoring protein scaffold protein. J Neurosci 26 (2006) 2391-2402
    • (2006) J Neurosci , vol.26 , pp. 2391-2402
    • Smith, K.E.1    Gibson, E.S.2    Dell'Acqua, M.L.3
  • 282
    • 0034043203 scopus 로고    scopus 로고
    • CaM-kinases: modulators of synaptic plasticity
    • Soderling T.R. CaM-kinases: modulators of synaptic plasticity. Curr Opin Neurobiol 10 (2000) 375-380
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 375-380
    • Soderling, T.R.1
  • 283
    • 0036829584 scopus 로고    scopus 로고
    • Regulation of AMPA receptors during synaptic plasticity
    • Song I., and Huganir R.L. Regulation of AMPA receptors during synaptic plasticity. Trends Neurosci 25 (2002) 578-588
    • (2002) Trends Neurosci , vol.25 , pp. 578-588
    • Song, I.1    Huganir, R.L.2
  • 284
    • 0032169143 scopus 로고    scopus 로고
    • Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA receptor-binding protein ABP
    • Srivastava S., Osten P., Vilim F.S., Khatri L., Inman G., States B., et al. Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA receptor-binding protein ABP. Neuron 21 (1998) 581-591
    • (1998) Neuron , vol.21 , pp. 581-591
    • Srivastava, S.1    Osten, P.2    Vilim, F.S.3    Khatri, L.4    Inman, G.5    States, B.6
  • 285
    • 0015609157 scopus 로고
    • A physiological mechanism for Hebb's postulate of learning
    • Stent G.S. A physiological mechanism for Hebb's postulate of learning. Proc Natl Acad Sci U S A 70 (1973) 997-1001
    • (1973) Proc Natl Acad Sci U S A , vol.70 , pp. 997-1001
    • Stent, G.S.1
  • 286
    • 0032516819 scopus 로고    scopus 로고
    • Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor
    • Strack S., and Colbran R.J. Autophosphorylation-dependent targeting of calcium/calmodulin-dependent protein kinase II by the NR2B subunit of the N-methyl- D-aspartate receptor. J Biol Chem 273 (1998) 20689-20692
    • (1998) J Biol Chem , vol.273 , pp. 20689-20692
    • Strack, S.1    Colbran, R.J.2
  • 288
    • 0030946102 scopus 로고    scopus 로고
    • Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density
    • Strack S., Choi S., Lovinger D.M., and Colbran R.J. Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density. J Biol Chem 272 (1997) 13467-13470
    • (1997) J Biol Chem , vol.272 , pp. 13467-13470
    • Strack, S.1    Choi, S.2    Lovinger, D.M.3    Colbran, R.J.4
  • 289
    • 0034604651 scopus 로고    scopus 로고
    • Mechanism and regulation of calcium/calmodulin-dependent protein kinase II targeting to the NR2B subunit of the N-methyl-d-aspartate receptor
    • Strack S., McNeill R.B., and Colbran R.J. Mechanism and regulation of calcium/calmodulin-dependent protein kinase II targeting to the NR2B subunit of the N-methyl-d-aspartate receptor. J Biol Chem 275 (2000) 23798-23806
    • (2000) J Biol Chem , vol.275 , pp. 23798-23806
    • Strack, S.1    McNeill, R.B.2    Colbran, R.J.3
  • 290
    • 0037731790 scopus 로고
    • Molecular cloning, characterization, and expression of a cDNA encoding the "80- to 87-kDa" myristoylated alanine-rich C kinase substrate: A major cellular substrate for protein kinase C
    • Stumpo D.J., Graff J.M., Albert K.A., Greengard P., and Blackshear P.J. Molecular cloning, characterization, and expression of a cDNA encoding the "80- to 87-kDa" myristoylated alanine-rich C kinase substrate: A major cellular substrate for protein kinase C. Proc Natl Acad Sci U S A 86 (1989) 4012-4016
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 4012-4016
    • Stumpo, D.J.1    Graff, J.M.2    Albert, K.A.3    Greengard, P.4    Blackshear, P.J.5
  • 291
    • 0032584956 scopus 로고    scopus 로고
    • NMDA receptor subunits in the postsynaptic density of rat brain: expression and phosphorylation by endogenous protein kinases
    • Suen P.C., Wu K., Xu J.L., Lin S.Y., Levine E.S., and Black I.B. NMDA receptor subunits in the postsynaptic density of rat brain: expression and phosphorylation by endogenous protein kinases. Brain Res Mol Brain Res 59 (1998) 215-228
    • (1998) Brain Res Mol Brain Res , vol.59 , pp. 215-228
    • Suen, P.C.1    Wu, K.2    Xu, J.L.3    Lin, S.Y.4    Levine, E.S.5    Black, I.B.6
  • 292
    • 0035166616 scopus 로고    scopus 로고
    • The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory
    • Sweatt J.D. The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory. J Neurochem 76 (2001) 1-10
    • (2001) J Neurochem , vol.76 , pp. 1-10
    • Sweatt, J.D.1
  • 293
    • 0034672306 scopus 로고    scopus 로고
    • The AMPAR subunit GluR2: still front and center-stage
    • Tanaka H., Grooms S.Y., Bennett M.V., and Zukin R.S. The AMPAR subunit GluR2: still front and center-stage. Brain Res 886 (2000) 190-207
    • (2000) Brain Res , vol.886 , pp. 190-207
    • Tanaka, H.1    Grooms, S.Y.2    Bennett, M.V.3    Zukin, R.S.4
  • 294
    • 0037092436 scopus 로고    scopus 로고
    • Regulation of GluR1 by the A-kinase anchoring protein 79 (AKAP79) signaling complex shares properties with long-term depression
    • Tavalin S.J., Colledge M., Hell J.W., Langeberg L.K., Huganir R.L., and Scott J.D. Regulation of GluR1 by the A-kinase anchoring protein 79 (AKAP79) signaling complex shares properties with long-term depression. J Neurosci 22 (2002) 3044-3051
    • (2002) J Neurosci , vol.22 , pp. 3044-3051
    • Tavalin, S.J.1    Colledge, M.2    Hell, J.W.3    Langeberg, L.K.4    Huganir, R.L.5    Scott, J.D.6
  • 295
    • 2942625634 scopus 로고    scopus 로고
    • Regulation of synaptic strength and AMPA receptor subunit composition by PICK1
    • Terashima A., Cotton L., Dev K.K., Meyer G., Zaman S., Duprat F., et al. Regulation of synaptic strength and AMPA receptor subunit composition by PICK1. J Neurosci 24 (2004) 5381-5390
    • (2004) J Neurosci , vol.24 , pp. 5381-5390
    • Terashima, A.1    Cotton, L.2    Dev, K.K.3    Meyer, G.4    Zaman, S.5    Duprat, F.6
  • 296
    • 0037137469 scopus 로고    scopus 로고
    • alpha- and betaCaMKII. Inverse regulation by neuronal activity and opposing effects on synaptic strength
    • Thiagarajan T.C., Piedras-Renteria E.S., and Tsien R.W. alpha- and betaCaMKII. Inverse regulation by neuronal activity and opposing effects on synaptic strength. Neuron 36 (2002) 1103-1114
    • (2002) Neuron , vol.36 , pp. 1103-1114
    • Thiagarajan, T.C.1    Piedras-Renteria, E.S.2    Tsien, R.W.3
  • 297
    • 23944511446 scopus 로고    scopus 로고
    • Adaptation to synaptic inactivity in hippocampal neurons
    • Thiagarajan T.C., Lindskog M., and Tsien R.W. Adaptation to synaptic inactivity in hippocampal neurons. Neuron 47 (2005) 725-737
    • (2005) Neuron , vol.47 , pp. 725-737
    • Thiagarajan, T.C.1    Lindskog, M.2    Tsien, R.W.3
  • 299
    • 0032543722 scopus 로고    scopus 로고
    • Transient and persistent increases in protein phosphatase activity during long-term depression in the adult hippocampus in vivo
    • Thiels E., Norman E.D., Barrionuevo G., and Klann E. Transient and persistent increases in protein phosphatase activity during long-term depression in the adult hippocampus in vivo. Neuroscience 86 (1998) 1023-1029
    • (1998) Neuroscience , vol.86 , pp. 1023-1029
    • Thiels, E.1    Norman, E.D.2    Barrionuevo, G.3    Klann, E.4
  • 300
    • 0034307466 scopus 로고    scopus 로고
    • Protein phosphatase-mediated regulation of protein kinase C during long-term depression in the adult hippocampus in vivo
    • Thiels E., Kanterewicz B.I., Knapp L.T., Barrionuevo G., and Klann E. Protein phosphatase-mediated regulation of protein kinase C during long-term depression in the adult hippocampus in vivo. J Neurosci 20 (2000) 7199-7207
    • (2000) J Neurosci , vol.20 , pp. 7199-7207
    • Thiels, E.1    Kanterewicz, B.I.2    Knapp, L.T.3    Barrionuevo, G.4    Klann, E.5
  • 301
    • 33750022357 scopus 로고    scopus 로고
    • AMPA receptor phosphorylation during long-term depression in the adult hippocampus in vivo
    • Thiels E., Lee H., and Huganir R.L. AMPA receptor phosphorylation during long-term depression in the adult hippocampus in vivo. Society for Neuroscience Abstract 648.1 (2002)
    • (2002) Society for Neuroscience Abstract , vol.648 1
    • Thiels, E.1    Lee, H.2    Huganir, R.L.3
  • 302
    • 1342289413 scopus 로고    scopus 로고
    • MAPK cascade signalling and synaptic plasticity
    • Thomas G.M., and Huganir R.L. MAPK cascade signalling and synaptic plasticity. Nat Rev Neurosci 5 (2004) 173-183
    • (2004) Nat Rev Neurosci , vol.5 , pp. 173-183
    • Thomas, G.M.1    Huganir, R.L.2
  • 303
    • 0031040615 scopus 로고    scopus 로고
    • Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-d-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies
    • Tingley W.G., Ehlers M.D., Kameyama K., Doherty C., Ptak J.B., Riley C.T., et al. Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-d-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies. J Biol Chem 272 (1997) 5157-5166
    • (1997) J Biol Chem , vol.272 , pp. 5157-5166
    • Tingley, W.G.1    Ehlers, M.D.2    Kameyama, K.3    Doherty, C.4    Ptak, J.B.5    Riley, C.T.6
  • 304
    • 0038022657 scopus 로고    scopus 로고
    • Functional studies and distribution define a family of transmembrane AMPA receptor regulatory proteins
    • Tomita S., Chen L., Kawasaki Y., Petralia R.S., Wenthold R.J., Nicoll R.A., et al. Functional studies and distribution define a family of transmembrane AMPA receptor regulatory proteins. J Cell Biol 161 (2003) 805-816
    • (2003) J Cell Biol , vol.161 , pp. 805-816
    • Tomita, S.1    Chen, L.2    Kawasaki, Y.3    Petralia, R.S.4    Wenthold, R.J.5    Nicoll, R.A.6
  • 305
    • 12344289653 scopus 로고    scopus 로고
    • Bidirectional synaptic plasticity regulated by phosphorylation of stargazin-like TARPs
    • Tomita S., Stein V., Stocker T.J., Nicoll R.A., and Bredt D.S. Bidirectional synaptic plasticity regulated by phosphorylation of stargazin-like TARPs. Neuron 45 (2005) 269-277
    • (2005) Neuron , vol.45 , pp. 269-277
    • Tomita, S.1    Stein, V.2    Stocker, T.J.3    Nicoll, R.A.4    Bredt, D.S.5
  • 306
    • 0034131101 scopus 로고    scopus 로고
    • Hebb and homeostasis in neuronal plasticity
    • Turrigiano G.G., and Nelson S.B. Hebb and homeostasis in neuronal plasticity. Curr Opin Neurobiol 10 (2000) 358-364
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 358-364
    • Turrigiano, G.G.1    Nelson, S.B.2
  • 307
    • 0742323527 scopus 로고    scopus 로고
    • Homeostatic plasticity in the developing nervous system
    • Turrigiano G.G., and Nelson S.B. Homeostatic plasticity in the developing nervous system. Nat Rev Neurosci 5 (2004) 97-107
    • (2004) Nat Rev Neurosci , vol.5 , pp. 97-107
    • Turrigiano, G.G.1    Nelson, S.B.2
  • 308
  • 310
    • 0037040527 scopus 로고    scopus 로고
    • N-methyl-d-aspartate-induced long-term depression is associated with a decrease in postsynaptic protein kinase C substrate phosphorylation in rat hippocampal slices
    • van Dam E.J., Ruiter B., Kamal A., Ramakers G.M., Gispen W.H., and de Graan P.N. N-methyl-d-aspartate-induced long-term depression is associated with a decrease in postsynaptic protein kinase C substrate phosphorylation in rat hippocampal slices. Neurosci Lett 320 (2002) 129-132
    • (2002) Neurosci Lett , vol.320 , pp. 129-132
    • van Dam, E.J.1    Ruiter, B.2    Kamal, A.3    Ramakers, G.M.4    Gispen, W.H.5    de Graan, P.N.6
  • 311
    • 0025879427 scopus 로고
    • Structural determinants of ion flow through recombinant glutamate receptor channels
    • Verdoorn T.A., Burnashev N., Monyer H., Seeburg P.H., and Sakmann B. Structural determinants of ion flow through recombinant glutamate receptor channels. Science 252 (1991) 1715-1718
    • (1991) Science , vol.252 , pp. 1715-1718
    • Verdoorn, T.A.1    Burnashev, N.2    Monyer, H.3    Seeburg, P.H.4    Sakmann, B.5
  • 312
    • 0034986665 scopus 로고    scopus 로고
    • A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux
    • Vissel B., Krupp J.J., Heinemann S.F., and Westbrook G.L. A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux. Nat Neurosci 4 (2001) 587-596
    • (2001) Nat Neurosci , vol.4 , pp. 587-596
    • Vissel, B.1    Krupp, J.J.2    Heinemann, S.F.3    Westbrook, G.L.4
  • 314
    • 0028360327 scopus 로고
    • Regulation of NMDA receptors by tyrosine kinases and phosphatases
    • Wang Y.T., and 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
  • 315
    • 0029919507 scopus 로고    scopus 로고
    • 2+)-independent reduction of N-methyl-d-aspartate channel activity by protein tyrosine phosphatase
    • 2+)-independent reduction of N-methyl-d-aspartate channel activity by protein tyrosine phosphatase. Proc Natl Acad Sci U S A 93 (1996) 1721-1725
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1721-1725
    • Wang, Y.T.1    Yu, X.M.2    Salter, M.W.3
  • 316
    • 0031466382 scopus 로고    scopus 로고
    • Differential dependence on GluR2 expression of three characteristic features of AMPA receptors
    • Washburn M.S., Numberger M., Zhang S., and Dingledine R. Differential dependence on GluR2 expression of three characteristic features of AMPA receptors. J Neurosci 17 (1997) 9393-9406
    • (1997) J Neurosci , vol.17 , pp. 9393-9406
    • Washburn, M.S.1    Numberger, M.2    Zhang, S.3    Dingledine, R.4
  • 317
    • 0026646751 scopus 로고
    • Localization of the protein kinase C phosphorylation/calmodulin-binding substrate RC3 in dendritic spines of neostriatal neurons
    • Watson J.B., Sutcliffe J.G., and Fisher R.S. Localization of the protein kinase C phosphorylation/calmodulin-binding substrate RC3 in dendritic spines of neostriatal neurons. Proc Natl Acad Sci U S A 89 (1992) 8581-8585
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8581-8585
    • Watson, J.B.1    Sutcliffe, J.G.2    Fisher, R.S.3
  • 318
    • 0028143437 scopus 로고
    • Localization of RC3 (neurogranin) in rat brain subcellular fractions
    • Watson J.B., Szijan I., and Coulter II P.M. Localization of RC3 (neurogranin) in rat brain subcellular fractions. Brain Res Mol Brain Res 27 (1994) 323-328
    • (1994) Brain Res Mol Brain Res , vol.27 , pp. 323-328
    • Watson, J.B.1    Szijan, I.2    Coulter II, P.M.3
  • 319
    • 0033695958 scopus 로고    scopus 로고
    • Activity coregulates quantal AMPA and NMDA currents at neocortical synapses
    • Watt A.J., van Rossum M.C., MacLeod K.M., Nelson S.B., and Turrigiano G.G. Activity coregulates quantal AMPA and NMDA currents at neocortical synapses. Neuron 26 (2000) 659-670
    • (2000) Neuron , vol.26 , pp. 659-670
    • Watt, A.J.1    van Rossum, M.C.2    MacLeod, K.M.3    Nelson, S.B.4    Turrigiano, G.G.5
  • 320
    • 11144353717 scopus 로고    scopus 로고
    • A proportional but slower NMDA potentiation follows AMPA potentiation in LTP
    • Watt A.J., Sjostrom P.J., Hausser M., Nelson S.B., and Turrigiano G.G. A proportional but slower NMDA potentiation follows AMPA potentiation in LTP. Nat Neurosci 7 (2004) 518-524
    • (2004) Nat Neurosci , vol.7 , pp. 518-524
    • Watt, A.J.1    Sjostrom, P.J.2    Hausser, M.3    Nelson, S.B.4    Turrigiano, G.G.5
  • 321
    • 24944557047 scopus 로고    scopus 로고
    • Activation of NR2A-containing NMDA receptors is not obligatory for NMDA receptor-dependent long-term potentiation
    • Weitlauf C., Honse Y., Auberson Y.P., Mishina M., Lovinger D.M., and Winder D.G. Activation of NR2A-containing NMDA receptors is not obligatory for NMDA receptor-dependent long-term potentiation. J Neurosci 25 (2005) 8386-8390
    • (2005) J Neurosci , vol.25 , pp. 8386-8390
    • Weitlauf, C.1    Honse, Y.2    Auberson, Y.P.3    Mishina, M.4    Lovinger, D.M.5    Winder, D.G.6
  • 322
    • 0026531244 scopus 로고
    • Immunochemical characterization of the non-NMDA glutamate receptor using subunit-specific antibodies. Evidence for a hetero-oligomeric structure in rat brain
    • Wenthold R.J., Yokotani N., Doi K., and Wada K. Immunochemical characterization of the non-NMDA glutamate receptor using subunit-specific antibodies. Evidence for a hetero-oligomeric structure in rat brain. J Biol Chem 267 (1992) 501-507
    • (1992) J Biol Chem , vol.267 , pp. 501-507
    • Wenthold, R.J.1    Yokotani, N.2    Doi, K.3    Wada, K.4
  • 323
    • 0029977616 scopus 로고    scopus 로고
    • Evidence for multiple AMPA receptor complexes in hippocampal CA1/CA2 neurons
    • Wenthold R.J., Petralia R.S., Blahos II J., and Niedzielski A.S. Evidence for multiple AMPA receptor complexes in hippocampal CA1/CA2 neurons. J Neurosci 16 (1996) 1982-1989
    • (1996) J Neurosci , vol.16 , pp. 1982-1989
    • Wenthold, R.J.1    Petralia, R.S.2    Blahos II, J.3    Niedzielski, A.S.4
  • 325
    • 0027405347 scopus 로고
    • Developmental switch in the expression of NMDA receptors occurs in vivo and in vitro
    • Williams K., Russell S.L., Shen Y.M., and Molinoff P.B. Developmental switch in the expression of NMDA receptors occurs in vivo and in vitro. Neuron 10 (1993) 267-278
    • (1993) Neuron , vol.10 , pp. 267-278
    • Williams, K.1    Russell, S.L.2    Shen, Y.M.3    Molinoff, P.B.4
  • 326
    • 0035407298 scopus 로고    scopus 로고
    • Roles of serine/threonine phosphatases in hippocampal synaptic plasticity
    • Winder D.G., and Sweatt J.D. Roles of serine/threonine phosphatases in hippocampal synaptic plasticity. Nat Rev Neurosci 2 (2001) 461-474
    • (2001) Nat Rev Neurosci , vol.2 , pp. 461-474
    • Winder, D.G.1    Sweatt, J.D.2
  • 327
    • 0032498272 scopus 로고    scopus 로고
    • Genetic and pharmacological evidence for a novel, intermediate phase of long-term potentiation suppressed by calcineurin
    • Winder D.G., Mansuy I.M., Osman M., Moallem T.M., and Kandel E.R. Genetic and pharmacological evidence for a novel, intermediate phase of long-term potentiation suppressed by calcineurin. Cell 92 (1998) 25-37
    • (1998) Cell , vol.92 , pp. 25-37
    • Winder, D.G.1    Mansuy, I.M.2    Osman, M.3    Moallem, T.M.4    Kandel, E.R.5
  • 328
    • 0033230165 scopus 로고    scopus 로고
    • ERK plays a regulatory role in induction of LTP by theta frequency stimulation and its modulation by beta-adrenergic receptors
    • Winder D.G., Martin K.C., Muzzio I.A., Rohrer D., Chruscinski A., Kobilka B., et al. ERK plays a regulatory role in induction of LTP by theta frequency stimulation and its modulation by beta-adrenergic receptors. Neuron 24 (1999) 715-726
    • (1999) Neuron , vol.24 , pp. 715-726
    • Winder, D.G.1    Martin, K.C.2    Muzzio, I.A.3    Rohrer, D.4    Chruscinski, A.5    Kobilka, B.6
  • 329
    • 0020183576 scopus 로고
    • Calcium/phospholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes
    • Wu W.C., Walaas S.I., Nairn A.C., and Greengard P. Calcium/phospholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes. Proc Natl Acad Sci U S A 79 (1982) 5249-5253
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 5249-5253
    • Wu, W.C.1    Walaas, S.I.2    Nairn, A.C.3    Greengard, P.4
  • 330
    • 0141767052 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent neuronal signaling in the hippocampus
    • 2+/calmodulin-dependent neuronal signaling in the hippocampus. J Neurochem 86 (2003) 1524-1533
    • (2003) J Neurochem , vol.86 , pp. 1524-1533
    • Wu, J.1    Huang, K.P.2    Huang, F.L.3
  • 331
    • 7444271017 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor acutely enhances tyrosine phosphorylation of the AMPA receptor subunit GluR1 via NMDA receptor-dependent mechanisms
    • Wu K., Len G.W., McAuliffe G., Ma C., Tai J.P., Xu F., et al. Brain-derived neurotrophic factor acutely enhances tyrosine phosphorylation of the AMPA receptor subunit GluR1 via NMDA receptor-dependent mechanisms. Brain Res Mol Brain Res 130 (2004) 178-186
    • (2004) Brain Res Mol Brain Res , vol.130 , pp. 178-186
    • Wu, K.1    Len, G.W.2    McAuliffe, G.3    Ma, C.4    Tai, J.P.5    Xu, F.6
  • 332
    • 0033178981 scopus 로고    scopus 로고
    • Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo
    • Wyszynski M., Valtschanoff J.G., Naisbitt S., Dunah A.W., Kim E., Standaert D.G., et al. Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo. J Neurosci 19 (1999) 6528-6537
    • (1999) J Neurosci , vol.19 , pp. 6528-6537
    • Wyszynski, M.1    Valtschanoff, J.G.2    Naisbitt, S.3    Dunah, A.W.4    Kim, E.5    Standaert, D.G.6
  • 333
    • 0029000862 scopus 로고
    • On the linkage between AMPA and NMDA receptor-mediated EPSPs in homosynaptic long-term depression in the hippocampal CA1 region of young rats
    • Xiao M.Y., Karpefors M., Gustafsson B., and Wigstrom H. On the linkage between AMPA and NMDA receptor-mediated EPSPs in homosynaptic long-term depression in the hippocampal CA1 region of young rats. J Neurosci 15 (1995) 4496-4506
    • (1995) J Neurosci , vol.15 , pp. 4496-4506
    • Xiao, M.Y.1    Karpefors, M.2    Gustafsson, B.3    Wigstrom, H.4
  • 334
    • 0033223820 scopus 로고    scopus 로고
    • Src potentiation of NMDA receptors in hippocampal and spinal neurons is not mediated by reducing zinc inhibition
    • Xiong Z.G., Pelkey K.A., Lu W.Y., Lu Y.M., Roder J.C., MacDonald J.F., et al. Src potentiation of NMDA receptors in hippocampal and spinal neurons is not mediated by reducing zinc inhibition. J Neurosci 19 (1999) RC37
    • (1999) J Neurosci , vol.19
    • Xiong, Z.G.1    Pelkey, K.A.2    Lu, W.Y.3    Lu, Y.M.4    Roder, J.C.5    MacDonald, J.F.6
  • 335
    • 0035050819 scopus 로고    scopus 로고
    • Identification of mouse NMDA receptor subunit NR2A C-terminal tyrosine sites phosphorylated by coexpression with v-Src
    • Yang M., and Leonard J.P. Identification of mouse NMDA receptor subunit NR2A C-terminal tyrosine sites phosphorylated by coexpression with v-Src. J Neurochem 77 (2001) 580-588
    • (2001) J Neurochem , vol.77 , pp. 580-588
    • Yang, M.1    Leonard, J.P.2
  • 337
    • 0037218831 scopus 로고    scopus 로고
    • A developmental switch in the signaling cascades for LTP induction
    • Yasuda H., Barth A.L., Stellwagen D., and Malenka R.C. A developmental switch in the signaling cascades for LTP induction. Nat Neurosci 6 (2003) 15-16
    • (2003) Nat Neurosci , vol.6 , pp. 15-16
    • Yasuda, H.1    Barth, A.L.2    Stellwagen, D.3    Malenka, R.C.4
  • 338
    • 0031053363 scopus 로고    scopus 로고
    • NMDA channel regulation by channel-associated protein tyrosine kinase Src
    • Yu X.M., Askalan R., Keil II G.J., and 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 II, G.J.3    Salter, M.W.4
  • 339
    • 0033546059 scopus 로고    scopus 로고
    • Importance of AMPA receptors for hippocampal synaptic plasticity but not for spatial learning
    • Zamanillo D., Sprengel R., Hvalby O., Jensen V., Burnashev N., Rozov A., et al. Importance of AMPA receptors for hippocampal synaptic plasticity but not for spatial learning. Science 284 (1999) 1805-1811
    • (1999) Science , vol.284 , pp. 1805-1811
    • Zamanillo, D.1    Sprengel, R.2    Hvalby, O.3    Jensen, V.4    Burnashev, N.5    Rozov, A.6
  • 341
    • 0032106760 scopus 로고    scopus 로고
    • Tyrosine kinase potentiates NMDA receptor currents by reducing tonic zinc inhibition
    • Zheng F., Gingrich M.B., Traynelis S.F., and Conn P.J. Tyrosine kinase potentiates NMDA receptor currents by reducing tonic zinc inhibition. Nat Neurosci 1 (1998) 185-191
    • (1998) Nat Neurosci , vol.1 , pp. 185-191
    • Zheng, F.1    Gingrich, M.B.2    Traynelis, S.F.3    Conn, P.J.4
  • 342
    • 0033592928 scopus 로고    scopus 로고
    • Protein kinase C potentiation of N-methyl-d-aspartate receptor activity is not mediated by phosphorylation of N-methyl-d-aspartate receptor subunits
    • Zheng X., Zhang L., Wang A.P., Bennett M.V., and Zukin R.S. Protein kinase C potentiation of N-methyl-d-aspartate receptor activity is not mediated by phosphorylation of N-methyl-d-aspartate receptor subunits. Proc Natl Acad Sci U S A 96 (1999) 15262-15267
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 15262-15267
    • Zheng, X.1    Zhang, L.2    Wang, A.P.3    Bennett, M.V.4    Zukin, R.S.5
  • 343
    • 0033773869 scopus 로고    scopus 로고
    • Postnatal synaptic potentiation: delivery of GluR4-containing AMPA receptors by spontaneous activity
    • Zhu J.J., Esteban J.A., Hayashi Y., and Malinow R. Postnatal synaptic potentiation: delivery of GluR4-containing AMPA receptors by spontaneous activity. Nat Neurosci 3 (2000) 1098-1106
    • (2000) Nat Neurosci , vol.3 , pp. 1098-1106
    • Zhu, J.J.1    Esteban, J.A.2    Hayashi, Y.3    Malinow, R.4
  • 344
    • 0028275855 scopus 로고
    • Role of guanylyl cyclase and cGMP-dependent protein kinase in long-term potentiation
    • Zhuo M., Hu Y., Schultz C., Kandel E.R., and Hawkins R.D. Role of guanylyl cyclase and cGMP-dependent protein kinase in long-term potentiation. Nature 368 (1994) 635-639
    • (1994) Nature , vol.368 , pp. 635-639
    • Zhuo, M.1    Hu, Y.2    Schultz, C.3    Kandel, E.R.4    Hawkins, R.D.5
  • 345
    • 0033551056 scopus 로고    scopus 로고
    • A selective role of calcineurin aalpha in synaptic depotentiation in hippocampus
    • Zhuo M., Zhang W., Son H., Mansuy I., Sobel R.A., Seidman J., et al. A selective role of calcineurin aalpha in synaptic depotentiation in hippocampus. Proc Natl Acad Sci U S A 96 (1999) 4650-4655
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 4650-4655
    • Zhuo, M.1    Zhang, W.2    Son, H.3    Mansuy, I.4    Sobel, R.A.5    Seidman, J.6
  • 346
    • 0029073172 scopus 로고
    • Alternatively spliced isoforms of the NMDARI receptor subunit
    • Zukin R.S., and Bennett M.V. Alternatively spliced isoforms of the NMDARI receptor subunit. Trends Neurosci 18 (1995) 306-313
    • (1995) Trends Neurosci , vol.18 , pp. 306-313
    • Zukin, R.S.1    Bennett, M.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.