메뉴 건너뛰기




Volumn 146, Issue 3, 2007, Pages 1158-1168

Identification of C-terminal domain residues involved in protein kinase A-mediated potentiation of kainate receptor subtype 6

Author keywords

glutamate receptor; kainate receptor; phosphorylation; receptor regulation

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; KAINIC ACID RECEPTOR;

EID: 34247880273     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2007.02.012     Document Type: Article
Times cited : (14)

References (66)
  • 2
    • 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
  • 3
    • 0033555424 scopus 로고    scopus 로고
    • Agonist-induced changes in substituted cysteine accessibility reveal dynamic extracellular structure of M3-M4 loop of glutamate receptor GluR6
    • Basiry S.S., Mendoza P., Lee P.D., and Raymond L.A. Agonist-induced changes in substituted cysteine accessibility reveal dynamic extracellular structure of M3-M4 loop of glutamate receptor GluR6. J Neurosci 19 (1999) 644-652
    • (1999) J Neurosci , vol.19 , pp. 644-652
    • Basiry, S.S.1    Mendoza, P.2    Lee, P.D.3    Raymond, L.A.4
  • 4
    • 0028819612 scopus 로고
    • Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining re-entrant membrane loop
    • Bennett J.A., and Dingledine R. Topology profile for a glutamate receptor: Three transmembrane domains and a channel-lining re-entrant membrane loop. Neuron 14 (1995) 373-384
    • (1995) Neuron , vol.14 , pp. 373-384
    • Bennett, J.A.1    Dingledine, R.2
  • 7
    • 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
  • 8
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C., and Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7 (1987) 2745-2752
    • (1987) Mol Cell Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 9
    • 0026552808 scopus 로고
    • ++ block of NMDA-receptor channels as a mechanism of modulation
    • ++ block of NMDA-receptor channels as a mechanism of modulation. Nature 356 (1992) 521-523
    • (1992) Nature , vol.356 , pp. 521-523
    • Chen, L.1    Huang, L.Y.M.2
  • 10
    • 0015385368 scopus 로고
    • Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA
    • Cohen S.N., Chang A.C., and Hsu L. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci U S A 69 (1972) 2110-2114
    • (1972) Proc Natl Acad Sci U S A , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.2    Hsu, L.3
  • 11
    • 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
  • 13
    • 0025765017 scopus 로고
    • Cloning of a cDNA for a receptor subunit activated by kainate but not AMPA
    • Egebjerg J., Bettler B., Hermans-Borgmeyer I., and Heinemann S. Cloning of a cDNA for a receptor subunit activated by kainate but not AMPA. Nature 351 (1991) 745-748
    • (1991) Nature , vol.351 , pp. 745-748
    • Egebjerg, J.1    Bettler, B.2    Hermans-Borgmeyer, I.3    Heinemann, S.4
  • 14
    • 0034959695 scopus 로고    scopus 로고
    • Specific activation of the alpha 7 nicotinic acetylcholine receptor by a quaternary analog of cocaine
    • Francis M.M., Cheng E.Y., Weiland G.A., and Oswald R.E. Specific activation of the alpha 7 nicotinic acetylcholine receptor by a quaternary analog of cocaine. Mol Pharmacol 60 (2001) 71-79
    • (2001) Mol Pharmacol , vol.60 , pp. 71-79
    • Francis, M.M.1    Cheng, E.Y.2    Weiland, G.A.3    Oswald, R.E.4
  • 15
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill O.P., Marty E., Neher B., Sakmann B., and Sigworth F.J. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch 391 (1981) 85-100
    • (1981) Pflugers Arch , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, E.2    Neher, B.3    Sakmann, B.4    Sigworth, F.J.5
  • 16
    • 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
  • 17
    • 0026530085 scopus 로고
    • The KA-2 subunit of excitatory amino acid receptors shows widespread expression in brain and forms ion channels with distantly related subunits
    • Herb A., Burnashev N., Werner P., Sakmann B., Wisden W., and Seeburg P.H. The KA-2 subunit of excitatory amino acid receptors shows widespread expression in brain and forms ion channels with distantly related subunits. Neuron 8 (1992) 775-785
    • (1992) Neuron , vol.8 , pp. 775-785
    • Herb, A.1    Burnashev, N.2    Werner, P.3    Sakmann, B.4    Wisden, W.5    Seeburg, P.H.6
  • 19
    • 0028596211 scopus 로고
    • N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann M., Maron C., and Heinemann S. N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron 13 (1994) 1331-1343
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 20
    • 0024367836 scopus 로고
    • Cloning by functional expression of a member of the glutamate receptor family
    • Hollmann M., O'Shea-Greenfield A., Rogers S.W., and Heinemann S. Cloning by functional expression of a member of the glutamate receptor family. Nature 342 (1989) 643-648
    • (1989) Nature , vol.342 , pp. 643-648
    • Hollmann, M.1    O'Shea-Greenfield, A.2    Rogers, S.W.3    Heinemann, S.4
  • 21
    • 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
  • 23
  • 24
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly P.J., and Krebs E.G. Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 266 (1991) 15555-15558
    • (1991) J Biol Chem , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 25
    • 0025166447 scopus 로고
    • Dopamine modulates the kinetics of ion channels gated by excitatory amino acids in retinal horizontal cells
    • Knapp A.G., Schmidt K.F., and Dowling J.E. Dopamine modulates the kinetics of ion channels gated by excitatory amino acids in retinal horizontal cells. Proc Natl Acad Sci U S A 87 (1990) 767-771
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 767-771
    • Knapp, A.G.1    Schmidt, K.F.2    Dowling, J.E.3
  • 26
    • 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
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 30844458571 scopus 로고    scopus 로고
    • Kainate receptor physiology
    • Lerma J. Kainate receptor physiology. Curr Opin Pharmacol 6 (2006) 89-97
    • (2006) Curr Opin Pharmacol , vol.6 , pp. 89-97
    • Lerma, J.1
  • 31
    • 0142126722 scopus 로고    scopus 로고
    • Channel-opening kinetics of GluR6 kainate receptor
    • Li G., Oswald R.E., and Niu L. Channel-opening kinetics of GluR6 kainate receptor. Biochemistry 42 (2003) 12367-12375
    • (2003) Biochemistry , vol.42 , pp. 12367-12375
    • Li, G.1    Oswald, R.E.2    Niu, L.3
  • 32
    • 0028236667 scopus 로고
    • Regulation of NMDA channel function by endogenous Ca(2+)-dependent phosphatase
    • Lieberman D.N., and Mody I. Regulation of NMDA channel function by endogenous Ca(2+)-dependent phosphatase. Nature 369 (1994) 235-239
    • (1994) Nature , vol.369 , pp. 235-239
    • Lieberman, D.N.1    Mody, I.2
  • 33
    • 0036305484 scopus 로고    scopus 로고
    • AMPA receptor trafficking and synaptic plasticity
    • Malinow R., and Malenka R.C. AMPA receptor trafficking and synaptic plasticity. Annu Rev Neurosci 25 (2002) 103-126
    • (2002) Annu Rev Neurosci , vol.25 , pp. 103-126
    • Malinow, R.1    Malenka, R.C.2
  • 34
    • 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
  • 35
    • 13844266202 scopus 로고    scopus 로고
    • Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity
    • Mayer M.L. Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity. Neuron 45 (2005) 539-552
    • (2005) Neuron , vol.45 , pp. 539-552
    • Mayer, M.L.1
  • 36
    • 0027480086 scopus 로고
    • Phosphorylation and regulation of glutamate receptors by calcium/calmodulin-dependent protein kinase II
    • McGlade-McCulloh E., Yamamoto H., Tan S.E., Brickey D.A., and Soderling T.R. Phosphorylation and regulation of glutamate receptors by calcium/calmodulin-dependent protein kinase II. Nature 362 (1993) 640-642
    • (1993) Nature , vol.362 , pp. 640-642
    • McGlade-McCulloh, E.1    Yamamoto, H.2    Tan, S.E.3    Brickey, D.A.4    Soderling, T.R.5
  • 37
    • 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
  • 39
    • 0029905992 scopus 로고    scopus 로고
    • Identification of a phosphorylation site for calcium/calmodulin dependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor
    • Omkumar R.V., Kiely M.J., Rosenstein A.J., Min K.T., and Kennedy M.B. Identification of a phosphorylation site for calcium/calmodulin dependent protein kinase II in the NR2B subunit of the N-methyl-D-aspartate receptor. J Biol Chem 271 (1996) 31670-31678
    • (1996) J Biol Chem , vol.271 , pp. 31670-31678
    • Omkumar, R.V.1    Kiely, M.J.2    Rosenstein, A.J.3    Min, K.T.4    Kennedy, M.B.5
  • 40
    • 0029943554 scopus 로고    scopus 로고
    • Green fluorescent protein and its derivatives as versatile markers for gene expression in living Drosophila melanogaster, plant and mammalian cells
    • Plautz J.D., Day R.N., Dailey G.M., Welsh S.B., Hall J.C., Halpain S., and Kay S.A. Green fluorescent protein and its derivatives as versatile markers for gene expression in living Drosophila melanogaster, plant and mammalian cells. Gene 173 (1996) 83-87
    • (1996) Gene , vol.173 , pp. 83-87
    • Plautz, J.D.1    Day, R.N.2    Dailey, G.M.3    Welsh, S.B.4    Hall, J.C.5    Halpain, S.6    Kay, S.A.7
  • 41
    • 0027412240 scopus 로고
    • Phosphorylation and modulation of recombinant GluR6 glutamate receptors by cAMP-dependent protein kinase
    • Raymond L.A., Blackstone C.D., and Huganir R.L. Phosphorylation and modulation of recombinant GluR6 glutamate receptors by cAMP-dependent protein kinase. Nature 361 (1993) 637-641
    • (1993) Nature , vol.361 , pp. 637-641
    • Raymond, L.A.1    Blackstone, C.D.2    Huganir, R.L.3
  • 42
    • 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
  • 44
    • 33845978455 scopus 로고    scopus 로고
    • Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway
    • Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M., Singer J.D., and Marshall J. Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway. J Biol Chem 281 (2006) 40164-40173
    • (2006) J Biol Chem , vol.281 , pp. 40164-40173
    • Salinas, G.D.1    Blair, L.A.2    Needleman, L.A.3    Gonzales, J.D.4    Chen, Y.5    Li, M.6    Singer, J.D.7    Marshall, J.8
  • 45
    • 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
  • 46
    • 0035805143 scopus 로고    scopus 로고
    • Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons
    • Shi S., Hayashi Y., Esteban J.A., and Malinow R. Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons. Cell 105 (2001) 331-343
    • (2001) Cell , vol.105 , pp. 331-343
    • Shi, S.1    Hayashi, Y.2    Esteban, J.A.3    Malinow, R.4
  • 47
    • 0032925146 scopus 로고    scopus 로고
    • The catalytic subunit of cAMP-dependent protein kinase: prototype for an extended network of communication
    • ?
    • Smith C.M., Radzio-Andzelm E., Madhusudan, Akamine P., and Taylor S.S. The catalytic subunit of cAMP-dependent protein kinase: prototype for an extended network of communication. ?. Prog Biophys Mol Biol 71 (1999) 313-341
    • (1999) Prog Biophys Mol Biol , vol.71 , pp. 313-341
    • Smith, C.M.1    Radzio-Andzelm, E.2    Madhusudan3    Akamine, P.4    Taylor, S.S.5
  • 48
    • 0032143945 scopus 로고    scopus 로고
    • Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors
    • Song I., Kamboj S., Xia J., Dong H., Liao D., and Huganir R.L. Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors. Neuron 21 (1998) 393-400
    • (1998) Neuron , vol.21 , pp. 393-400
    • Song, I.1    Kamboj, S.2    Xia, J.3    Dong, H.4    Liao, D.5    Huganir, R.L.6
  • 50
    • 0034520590 scopus 로고    scopus 로고
    • PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
    • Standley S., Roche K.W., McCallum J., Sans N., and Wenthold R.J. PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants. Neuron 28 (2000) 887-898
    • (2000) Neuron , vol.28 , pp. 887-898
    • Standley, S.1    Roche, K.W.2    McCallum, J.3    Sans, N.4    Wenthold, R.J.5
  • 51
    • 0030595059 scopus 로고    scopus 로고
    • Quantitative analysis of transient gene expression in mammalian cells using the green fluorescent protein
    • Subramanian S., and Srienc F. Quantitative analysis of transient gene expression in mammalian cells using the green fluorescent protein. J Biotechnol 49 (1996) 137-151
    • (1996) J Biotechnol , vol.49 , pp. 137-151
    • Subramanian, S.1    Srienc, F.2
  • 52
    • 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., and Huganir R.L. 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    Huganir, R.L.7
  • 53
    • 0027209184 scopus 로고
    • Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain
    • Tingley W.G., Roche K.W., Thompson A.K., and Huganir R.L. Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. Nature 364 (1993) 70-73
    • (1993) Nature , vol.364 , pp. 70-73
    • Tingley, W.G.1    Roche, K.W.2    Thompson, A.K.3    Huganir, R.L.4
  • 54
    • 0030680906 scopus 로고    scopus 로고
    • Control of rat GluR6 glutamate receptor open probability by protein kinase A and calcineurin
    • Traynelis S.F., and Wahl P. Control of rat GluR6 glutamate receptor open probability by protein kinase A and calcineurin. J Physiol (Lond) 503 (1997) 513-531
    • (1997) J Physiol (Lond) , vol.503 , pp. 513-531
    • Traynelis, S.F.1    Wahl, P.2
  • 55
    • 0023516913 scopus 로고
    • Chemical kinetic measurements of a mammalian acetylcholine receptor by a fast-reaction technique
    • Udgaonkar J.B., and Hess G.P. Chemical kinetic measurements of a mammalian acetylcholine receptor by a fast-reaction technique. Proc Natl Acad Sci U S A USA 84 (1987) 8758-8762
    • (1987) Proc Natl Acad Sci U S A USA , vol.84 , pp. 8758-8762
    • Udgaonkar, J.B.1    Hess, G.P.2
  • 56
    • 0028204241 scopus 로고
    • Modulation of AMPA/kainate receptors in cultured murine hippocampal neurones by protein kinase C
    • Wang L.Y., Dudek E.M., Browning M.D., and MacDonald J.F. Modulation of AMPA/kainate receptors in cultured murine hippocampal neurones by protein kinase C. J Physiol 475 (1994) 431-437
    • (1994) J Physiol , vol.475 , pp. 431-437
    • Wang, L.Y.1    Dudek, E.M.2    Browning, M.D.3    MacDonald, J.F.4
  • 57
    • 0027407112 scopus 로고
    • Phosphorylation and modulation of a kainate receptor (GluR6) by cAMP-dependent protein kinase
    • Wang L.Y., Taverna F.A., Huang X.P., MacDonald J.F., and Hampson D.R. Phosphorylation and modulation of a kainate receptor (GluR6) by cAMP-dependent protein kinase. Science 259 (1993) 1173-1175
    • (1993) Science , vol.259 , pp. 1173-1175
    • Wang, L.Y.1    Taverna, F.A.2    Huang, X.P.3    MacDonald, J.F.4    Hampson, D.R.5
  • 58
    • 0025810536 scopus 로고
    • Cloning of a putative high-affinity kainate receptor expressed predominantly in hippocampal CA3 cells
    • Werner P., Voigt M., Keinänen K., Wisden W., and Seeburg P.H. Cloning of a putative high-affinity kainate receptor expressed predominantly in hippocampal CA3 cells. Nature 351 (1991) 742-744
    • (1991) Nature , vol.351 , pp. 742-744
    • Werner, P.1    Voigt, M.2    Keinänen, K.3    Wisden, W.4    Seeburg, P.H.5
  • 59
    • 33748060215 scopus 로고    scopus 로고
    • Learning induces long-term potentiation in the hippocampus
    • Whitlock J.R., Heynen A.J., Shuler M.G., and Bear M.F. Learning induces long-term potentiation in the hippocampus. Science 313 (2006) 1093-1097
    • (2006) Science , vol.313 , pp. 1093-1097
    • Whitlock, J.R.1    Heynen, A.J.2    Shuler, M.G.3    Bear, M.F.4
  • 60
    • 0033601326 scopus 로고    scopus 로고
    • Cysteine mutagenesis and homology modeling of the ligand-binding site of a kainate-binding protein
    • Wo Z.G., Chohan K.K., Chen H., Sutcliffe M.J., and Oswald R.E. Cysteine mutagenesis and homology modeling of the ligand-binding site of a kainate-binding protein. J Biol Chem 274 (1999) 37210-37218
    • (1999) J Biol Chem , vol.274 , pp. 37210-37218
    • Wo, Z.G.1    Chohan, K.K.2    Chen, H.3    Sutcliffe, M.J.4    Oswald, R.E.5
  • 61
    • 0028364252 scopus 로고
    • Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation
    • Wo Z.G., and Oswald R.E. Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation. Proc Natl Acad Sci U S A 91 (1994) 7154-7158
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7154-7158
    • Wo, Z.G.1    Oswald, R.E.2
  • 62
    • 0028909344 scopus 로고
    • A topological analysis of goldfish kainate receptors predicts three transmembrane segments
    • Wo Z.G., and Oswald R.E. A topological analysis of goldfish kainate receptors predicts three transmembrane segments. J Biol Chem 270 (1995) 2000-2009
    • (1995) J Biol Chem , vol.270 , pp. 2000-2009
    • Wo, Z.G.1    Oswald, R.E.2
  • 63
    • 0028965140 scopus 로고
    • Unraveling the modular design of glutamate-gated ion channels
    • Wo Z.G., and Oswald R.E. Unraveling the modular design of glutamate-gated ion channels. Trends Neurosci 18 (1995) 161-168
    • (1995) Trends Neurosci , vol.18 , pp. 161-168
    • Wo, Z.G.1    Oswald, R.E.2
  • 65
    • 0017078844 scopus 로고
    • The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver
    • Zetterqvist O., Ragnarsson U., Humble E., Berglund L., and Engstrom L. The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver. Biochem Biophys Res Commun 70 (1976) 696-703
    • (1976) Biochem Biophys Res Commun , vol.70 , pp. 696-703
    • Zetterqvist, O.1    Ragnarsson, U.2    Humble, E.3    Berglund, L.4    Engstrom, L.5
  • 66
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.