메뉴 건너뛰기




Volumn 46, Issue 1, 2009, Pages 39-48

Intracellular Ca2+ stores modulate SOCCs and NMDA receptors via tyrosine kinases in rat hippocampal neurons

Author keywords

Calcium; Culture; Hippocampus; Kinases; Metabotropic glutamate receptors; Phosphatases; Phosphorylation; Store operated calcium channel; Tyrosine

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; METABOTROPIC RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; STORE OPERATED CALCIUM CHANNEL; UNCLASSIFIED DRUG; 2 AMINOETHOXYDIPHENYLBORANE; 2-AMINOETHOXYDIPHENYL BORATE; BORON DERIVATIVE; CALCIUM; GENISTEIN; N METHYLASPARTIC ACID; POTASSIUM CHLORIDE; THAPSIGARGIN; VANADIC ACID;

EID: 67649124244     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2009.04.001     Document Type: Article
Times cited : (19)

References (57)
  • 1
    • 0032127595 scopus 로고    scopus 로고
    • Neuronal calcium signaling
    • Berridge M.J. Neuronal calcium signaling. Neuron 21 (1998) 13-26
    • (1998) Neuron , vol.21 , pp. 13-26
    • Berridge, M.J.1
  • 2
    • 15544368216 scopus 로고    scopus 로고
    • Store-operated calcium channels
    • Parekh A.B., and Putney J.W.J. Store-operated calcium channels. Physiol. Rev. 85 (2005) 757-810
    • (2005) Physiol. Rev. , vol.85 , pp. 757-810
    • Parekh, A.B.1    Putney, J.W.J.2
  • 4
    • 0034737703 scopus 로고    scopus 로고
    • 2+ entry pathway by store depletion in cultured hippocampal neurones
    • 2+ entry pathway by store depletion in cultured hippocampal neurones. FEBS Lett. 470 (2000) 269-272
    • (2000) FEBS Lett. , vol.470 , pp. 269-272
    • Bouron, A.1
  • 5
    • 33748136477 scopus 로고    scopus 로고
    • STIM1 carboxyl-terminus activates native SOC, I(crac) and TRPC1 channels
    • Huang G.N., Zeng W., Kim J.Y., et al. STIM1 carboxyl-terminus activates native SOC, I(crac) and TRPC1 channels. Nat. Cell Biol. 8 (2006) 1003-1010
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1003-1010
    • Huang, G.N.1    Zeng, W.2    Kim, J.Y.3
  • 6
    • 42949155291 scopus 로고    scopus 로고
    • Functional interactions among Orai1, TRPCs, and STIM1 suggest a STIM-regulated heteromeric Orai/TRPC model for SOCE
    • Liao Y., Erxleben C., Abramowitz J., et al. Functional interactions among Orai1, TRPCs, and STIM1 suggest a STIM-regulated heteromeric Orai/TRPC model for SOCE. Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 2895-2900
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 2895-2900
    • Liao, Y.1    Erxleben, C.2    Abramowitz, J.3
  • 7
    • 27144515996 scopus 로고    scopus 로고
    • 2+ store to the plasma membrane
    • 2+ store to the plasma membrane. Nature 437 (2005) 902-905
    • (2005) Nature , vol.437 , pp. 902-905
    • Zhang, S.L.1    Yu, Y.2    Roos, J.3
  • 8
    • 0033954554 scopus 로고    scopus 로고
    • Effects of serine/threonine protein phosphatases on ion channels in excitable membranes
    • Herzig S., and Neumann J. Effects of serine/threonine protein phosphatases on ion channels in excitable membranes. Physiol. Rev. 80 (2000) 173-210
    • (2000) Physiol. Rev. , vol.80 , pp. 173-210
    • Herzig, S.1    Neumann, J.2
  • 9
    • 34547395389 scopus 로고    scopus 로고
    • Modulation of hippocampal calcium signalling and plasticity by serine/threonine protein phosphatases
    • Koss D.J., Hindley K.P., Riedel G., and Platt B. Modulation of hippocampal calcium signalling and plasticity by serine/threonine protein phosphatases. J. Neurochem. 102 (2007) 1009-1023
    • (2007) J. Neurochem. , vol.102 , pp. 1009-1023
    • Koss, D.J.1    Hindley, K.P.2    Riedel, G.3    Platt, B.4
  • 10
    • 0028910081 scopus 로고
    • Tyrosine kinase inhibition reduces the plateau phase of the calcium increase in response to progesterone in human sperm
    • Bonaccorsi L., Luconi M., Forti G., and Baldi E. Tyrosine kinase inhibition reduces the plateau phase of the calcium increase in response to progesterone in human sperm. FEBS Lett. 364 (1995) 83-86
    • (1995) FEBS Lett. , vol.364 , pp. 83-86
    • Bonaccorsi, L.1    Luconi, M.2    Forti, G.3    Baldi, E.4
  • 11
    • 0030586619 scopus 로고    scopus 로고
    • Tyrphostin A9 inhibits calcium release-dependent phosphorylations and calcium entry via calcium release-activated channel in Jurkat T cells
    • Marhaba R., Mary F., Pelassy C., Stanescu A.T., Aussel C., and Breittmayer J.P. Tyrphostin A9 inhibits calcium release-dependent phosphorylations and calcium entry via calcium release-activated channel in Jurkat T cells. J. Immunol. 157 (1996) 1468-1473
    • (1996) J. Immunol. , vol.157 , pp. 1468-1473
    • Marhaba, R.1    Mary, F.2    Pelassy, C.3    Stanescu, A.T.4    Aussel, C.5    Breittmayer, J.P.6
  • 12
    • 0030613771 scopus 로고    scopus 로고
    • The role of pp60c-src in the regulation of calcium entry via store-operated calcium channels
    • Babnigg G., Bowersox S.R., and Villereal M.L. The role of pp60c-src in the regulation of calcium entry via store-operated calcium channels. J. Biol. Chem. 272 (1997) 29434-29437
    • (1997) J. Biol. Chem. , vol.272 , pp. 29434-29437
    • Babnigg, G.1    Bowersox, S.R.2    Villereal, M.L.3
  • 13
    • 0034667659 scopus 로고    scopus 로고
    • 2+ entry in human platelets through the reorganization of the actin cytoskeleton
    • 2+ entry in human platelets through the reorganization of the actin cytoskeleton. Biochem. J. 351 Pt 2 (2000) 429-437
    • (2000) Biochem. J. , vol.351 , Issue.PART 2 , pp. 429-437
    • Rosado, J.A.1    Graves, D.2    Sage, S.O.3
  • 14
    • 0142122317 scopus 로고    scopus 로고
    • Tyrosine phosphatase PTP1B modulates store-operated calcium influx
    • Hsu S., Schmid A., Sternfeld L., et al. Tyrosine phosphatase PTP1B modulates store-operated calcium influx. Cell. Signal. 15 (2003) 1149-1156
    • (2003) Cell. Signal. , vol.15 , pp. 1149-1156
    • Hsu, S.1    Schmid, A.2    Sternfeld, L.3
  • 15
    • 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
  • 16
    • 0024232854 scopus 로고
    • Functional modulation of the nicotinic acetylcholine receptor by tyrosine phosphorylation
    • Hopfield J.F., Tank D.W., Greengard P., and Huganir R.L. Functional modulation of the nicotinic acetylcholine receptor by tyrosine phosphorylation. Nature 336 (1988) 677-680
    • (1988) Nature , vol.336 , pp. 677-680
    • Hopfield, J.F.1    Tank, D.W.2    Greengard, P.3    Huganir, R.L.4
  • 17
    • 0028982140 scopus 로고
    • Modulation of GABAA receptors by tyrosine phosphorylation
    • Moss S.J., Gorrie G.H., Amato A., and Smart T.G. Modulation of GABAA receptors by tyrosine phosphorylation. Nature 377 (1995) 344-348
    • (1995) Nature , vol.377 , pp. 344-348
    • Moss, S.J.1    Gorrie, G.H.2    Amato, A.3    Smart, T.G.4
  • 18
    • 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
  • 19
    • 0029929415 scopus 로고    scopus 로고
    • Protein-tyrosine kinases activate while protein-tyrosine phosphatases inhibit L-type calcium channel activity in pituitary GH3 cells
    • Cataldi M., Taglialatela M., Guerriero S., et al. Protein-tyrosine kinases activate while protein-tyrosine phosphatases inhibit L-type calcium channel activity in pituitary GH3 cells. J. Biol. Chem. 271 (1996) 9441-9446
    • (1996) J. Biol. Chem. , vol.271 , pp. 9441-9446
    • Cataldi, M.1    Taglialatela, M.2    Guerriero, S.3
  • 20
    • 0033596590 scopus 로고    scopus 로고
    • Protein tyrosine kinase inhibitors reduce high-voltage activating calcium currents in CA1 pyramidal neurones from rat hippocampal slices
    • Potier B., and Rovira C. Protein tyrosine kinase inhibitors reduce high-voltage activating calcium currents in CA1 pyramidal neurones from rat hippocampal slices. Brain Res. 816 (1999) 587-597
    • (1999) Brain Res. , vol.816 , pp. 587-597
    • Potier, B.1    Rovira, C.2
  • 21
    • 0030473947 scopus 로고    scopus 로고
    • Association of src tyrosine kinase with a human potassium channel mediated by SH3 domain
    • Holmes T.C., Fadool D.A., Ren R., and Levitan I.B. Association of src tyrosine kinase with a human potassium channel mediated by SH3 domain. Science 274 (1996) 2089-2091
    • (1996) Science , vol.274 , pp. 2089-2091
    • Holmes, T.C.1    Fadool, D.A.2    Ren, R.3    Levitan, I.B.4
  • 22
    • 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
  • 23
    • 0034899681 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the N-methyl-d-aspartate receptor by exogenous and postsynaptic density-associated src-family kinases
    • Cheung H.H., and Gurd J.W. Tyrosine phosphorylation of the N-methyl-d-aspartate receptor by exogenous and postsynaptic density-associated src-family kinases. J. Neurochem. 78 (2001) 524-534
    • (2001) J. Neurochem. , vol.78 , pp. 524-534
    • Cheung, H.H.1    Gurd, J.W.2
  • 24
    • 1642536318 scopus 로고    scopus 로고
    • Dopamine D1-dependent trafficking of striatal N-methyl-d-aspartate glutamate receptors requires fyn protein tyrosine kinase but not DARPP-32
    • Dunah A.W., Sirianni A.C., Fienberg A.A., Bastia E., Schwarzschild M.A., and Standaert D.G. Dopamine D1-dependent trafficking of striatal N-methyl-d-aspartate glutamate receptors requires fyn protein tyrosine kinase but not DARPP-32. Mol. Pharmacol. 65 (2004) 121-129
    • (2004) Mol. Pharmacol. , vol.65 , pp. 121-129
    • Dunah, A.W.1    Sirianni, A.C.2    Fienberg, A.A.3    Bastia, E.4    Schwarzschild, M.A.5    Standaert, D.G.6
  • 25
    • 0036662898 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 1-induced upregulation of NMDA receptor current: Mediation through the Pyk2
    • Heidinger V., Manzerra P., Wang X.Q., et al. Metabotropic glutamate receptor 1-induced upregulation of NMDA receptor current: Mediation through the Pyk2. J. Neurosci. 22 (2002) 5452-5461
    • (2002) J. Neurosci. , vol.22 , pp. 5452-5461
    • Heidinger, V.1    Manzerra, P.2    Wang, X.Q.3
  • 26
    • 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., 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
  • 27
    • 0034635557 scopus 로고    scopus 로고
    • 2+ signaling: direct interactions with fura-2
    • 2+ signaling: direct interactions with fura-2. Eur. J. Pharmacol. 389 (2000) 35-40
    • (2000) Eur. J. Pharmacol. , vol.389 , pp. 35-40
    • Berts, A.1    Minneman, K.P.2
  • 28
    • 0041819867 scopus 로고    scopus 로고
    • 2+ entry: implications in synaptic plasticity
    • 2+ entry: implications in synaptic plasticity. J. Neurosci. 23 (2003) 7737-7741
    • (2003) J. Neurosci. , vol.23 , pp. 7737-7741
    • Baba, A.1    Yasui, T.2    Fujisawa, S.3
  • 30
    • 0026662286 scopus 로고
    • Calcium channels in rat melanotrophs are permeable to manganese, cobalt, cadmium, and lanthanum, but not to nickel: evidence provided by fluorescence changes in fura-2-loaded cells
    • Shibuya I., and Douglas W.W. Calcium channels in rat melanotrophs are permeable to manganese, cobalt, cadmium, and lanthanum, but not to nickel: evidence provided by fluorescence changes in fura-2-loaded cells. Endocrinology 131 (1992) 1936-1941
    • (1992) Endocrinology , vol.131 , pp. 1936-1941
    • Shibuya, I.1    Douglas, W.W.2
  • 32
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: an approach to drug development
    • Levitzki A., and Gazit A. Tyrosine kinase inhibition: an approach to drug development. Science 267 (1995) 1782-1788
    • (1995) Science , vol.267 , pp. 1782-1788
    • Levitzki, A.1    Gazit, A.2
  • 33
    • 0344642611 scopus 로고    scopus 로고
    • Inhibition of a src homology 2 domain containing protein tyrosine phosphatase by vanadate in the primary culture of hepatocytes
    • Pugazhenthi S., Tanha F., Dahl B., and Khandelwal R.L. Inhibition of a src homology 2 domain containing protein tyrosine phosphatase by vanadate in the primary culture of hepatocytes. Arch. Biochem. Biophys. 335 (1996) 273-282
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 273-282
    • Pugazhenthi, S.1    Tanha, F.2    Dahl, B.3    Khandelwal, R.L.4
  • 34
    • 0028866845 scopus 로고
    • Different susceptibility of protein kinases to staurosporine inhibition. kinetic studies and molecular bases for the resistance of protein kinase CK2
    • Meggio F., Donella Deana A., Ruzzene M., et al. Different susceptibility of protein kinases to staurosporine inhibition. kinetic studies and molecular bases for the resistance of protein kinase CK2. Eur. J. Biochem. 234 (1995) 317-322
    • (1995) Eur. J. Biochem. , vol.234 , pp. 317-322
    • Meggio, F.1    Donella Deana, A.2    Ruzzene, M.3
  • 37
    • 1242306227 scopus 로고    scopus 로고
    • IP3-dependent calcium-induced calcium release mediates bidirectional calcium waves in neurones: functional implications for synaptic plasticity
    • Barbara J.G. IP3-dependent calcium-induced calcium release mediates bidirectional calcium waves in neurones: functional implications for synaptic plasticity. Biochim. Biophys. Acta 1600 (2002) 12-18
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 12-18
    • Barbara, J.G.1
  • 38
    • 28444487510 scopus 로고    scopus 로고
    • Stabilizing role of calcium store-dependent plasma membrane calcium channels in action-potential firing and intracellular calcium oscillations
    • Kusters J.M., Dernison M.M., van Meerwijk W.P., Ypey D.L., Theuvenet A.P., and Gielen C.C. Stabilizing role of calcium store-dependent plasma membrane calcium channels in action-potential firing and intracellular calcium oscillations. Biophys. J. 89 (2005) 3741-3756
    • (2005) Biophys. J. , vol.89 , pp. 3741-3756
    • Kusters, J.M.1    Dernison, M.M.2    van Meerwijk, W.P.3    Ypey, D.L.4    Theuvenet, A.P.5    Gielen, C.C.6
  • 39
    • 0034003107 scopus 로고    scopus 로고
    • Effect of dephostatin on intracellular free calcium concentration and amylase secretion in isolated rat pancreatic acinar cells
    • Lajas A.I., Pozo M.J., Camello P.J., Salido G.M., Singh J., and Pariente J.A. Effect of dephostatin on intracellular free calcium concentration and amylase secretion in isolated rat pancreatic acinar cells. Mol. Cell. Biochem. 205 (2000) 163-169
    • (2000) Mol. Cell. Biochem. , vol.205 , pp. 163-169
    • Lajas, A.I.1    Pozo, M.J.2    Camello, P.J.3    Salido, G.M.4    Singh, J.5    Pariente, J.A.6
  • 40
    • 0033168582 scopus 로고    scopus 로고
    • Oxidizing effects of vanadate on calcium mobilization and amylase release in rat pancreatic acinar cells
    • Pariente J.A., Lajas A.I., Pozo M.J., Camello P.J., and Salido G.M. Oxidizing effects of vanadate on calcium mobilization and amylase release in rat pancreatic acinar cells. Biochem. Pharmacol. 58 (1999) 77-84
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 77-84
    • Pariente, J.A.1    Lajas, A.I.2    Pozo, M.J.3    Camello, P.J.4    Salido, G.M.5
  • 43
    • 2442542398 scopus 로고    scopus 로고
    • Regulation of TRPC6 channel activity by tyrosine phosphorylation
    • Hisatsune C., Kuroda Y., Nakamura K., et al. Regulation of TRPC6 channel activity by tyrosine phosphorylation. J. Biol. Chem. 279 (2004) 18887-18894
    • (2004) J. Biol. Chem. , vol.279 , pp. 18887-18894
    • Hisatsune, C.1    Kuroda, Y.2    Nakamura, K.3
  • 44
    • 21144456845 scopus 로고    scopus 로고
    • Tyrosine phosphatase PTP1B interacts with TRPV6 in vivo and plays a role in TRPV6-mediated calcium influx in HEK293 cells
    • Sternfeld L., Krause E., Schmid A., et al. Tyrosine phosphatase PTP1B interacts with TRPV6 in vivo and plays a role in TRPV6-mediated calcium influx in HEK293 cells. Cell. Signal. 17 (2005) 951-960
    • (2005) Cell. Signal. , vol.17 , pp. 951-960
    • Sternfeld, L.1    Krause, E.2    Schmid, A.3
  • 46
    • 0029814484 scopus 로고    scopus 로고
    • 2+ channels in fetal rat hippocampal neurons: implications for neurite morphogenesis in vitro
    • 2+ channels in fetal rat hippocampal neurons: implications for neurite morphogenesis in vitro. J. Neurosci. 16 (1996) 6476-6489
    • (1996) J. Neurosci. , vol.16 , pp. 6476-6489
    • Shitaka, Y.1    Matsuki, N.2    Saito, H.3    Katsuk, I.H.4
  • 47
    • 0030925096 scopus 로고    scopus 로고
    • Regulation of rat neuronal voltage-dependent calcium channels by endogenous p21-ras
    • Fitzgerald E.M., and Dolphin A.C. Regulation of rat neuronal voltage-dependent calcium channels by endogenous p21-ras. Eur. J. Neurosci. 9 (1997) 1252-1261
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 1252-1261
    • Fitzgerald, E.M.1    Dolphin, A.C.2
  • 48
    • 0026601611 scopus 로고
    • Protein kinase C-mediated enhancement of NMDA currents by metabotropic glutamate receptors in xenopus oocytes
    • Kelso S.R., Nelson T.E., and Leonard J.P. Protein kinase C-mediated enhancement of NMDA currents by metabotropic glutamate receptors in xenopus oocytes. J. Physiol. 449 (1992) 705-718
    • (1992) J. Physiol. , vol.449 , pp. 705-718
    • Kelso, S.R.1    Nelson, T.E.2    Leonard, J.P.3
  • 50
    • 0141783841 scopus 로고    scopus 로고
    • Neuroprotection against NMDA excitotoxicity by group I metabotropic glutamate receptors is associated with reduction of NMDA stimulated currents
    • Blaabjerg M., Fang L., Zimmer J., and Baskys A. Neuroprotection against NMDA excitotoxicity by group I metabotropic glutamate receptors is associated with reduction of NMDA stimulated currents. Exp. Neurol. 183 (2003) 573-580
    • (2003) Exp. Neurol. , vol.183 , pp. 573-580
    • Blaabjerg, M.1    Fang, L.2    Zimmer, J.3    Baskys, A.4
  • 51
    • 3843103781 scopus 로고    scopus 로고
    • Interactions between NMDA receptors and mGlu5 receptors expressed in HEK293 cells
    • Collett V.J., and Collingridge G.L. Interactions between NMDA receptors and mGlu5 receptors expressed in HEK293 cells. Br. J. Pharmacol. 142 (2004) 991-1001
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 991-1001
    • Collett, V.J.1    Collingridge, G.L.2
  • 52
    • 1642499168 scopus 로고    scopus 로고
    • Differential calcium-dependent modulation of NMDA currents in CA1 and CA3 hippocampal pyramidal cells
    • Grishin A.A., Gee C.E., Gerber U., and Benquet P. Differential calcium-dependent modulation of NMDA currents in CA1 and CA3 hippocampal pyramidal cells. J. Neurosci. 24 (2004) 350-355
    • (2004) J. Neurosci. , vol.24 , pp. 350-355
    • Grishin, A.A.1    Gee, C.E.2    Gerber, U.3    Benquet, P.4
  • 53
    • 0034985915 scopus 로고    scopus 로고
    • mGluR1-mediated potentiation of NMDA receptors involves a rise in intracellular calcium and activation of protein kinase C
    • Skeberdis V.A., Lan J., Opitz T., Zheng X., Bennett M.V., and Zukin R.S. mGluR1-mediated potentiation of NMDA receptors involves a rise in intracellular calcium and activation of protein kinase C. Neuropharmacology 40 (2001) 856-865
    • (2001) Neuropharmacology , vol.40 , pp. 856-865
    • Skeberdis, V.A.1    Lan, J.2    Opitz, T.3    Zheng, X.4    Bennett, M.V.5    Zukin, R.S.6
  • 54
    • 0037112011 scopus 로고    scopus 로고
    • Two distinct signaling pathways upregulate NMDA receptor responses via two distinct metabotropic glutamate receptor subtypes
    • Benquet P., Gee C.E., and Gerber U. Two distinct signaling pathways upregulate NMDA receptor responses via two distinct metabotropic glutamate receptor subtypes. J. Neurosci. 22 (2002) 9679-9686
    • (2002) J. Neurosci. , vol.22 , pp. 9679-9686
    • Benquet, P.1    Gee, C.E.2    Gerber, U.3
  • 55
    • 18844391463 scopus 로고    scopus 로고
    • Integrin signaling cascades are operational in adult hippocampal synapses and modulate NMDA receptor physiology
    • Bernard-Trifilo J.A., Kramar E.A., Torp R., et al. Integrin signaling cascades are operational in adult hippocampal synapses and modulate NMDA receptor physiology. J. Neurochem. 93 (2005) 834-849
    • (2005) J. Neurochem. , vol.93 , pp. 834-849
    • Bernard-Trifilo, J.A.1    Kramar, E.A.2    Torp, R.3
  • 56
    • 0037127073 scopus 로고    scopus 로고
    • Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors
    • Takasu M.A., Dalva M.B., Zigmond R.E., and Greenberg M.E. Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors. Science 295 (2002) 491-495
    • (2002) Science , vol.295 , pp. 491-495
    • Takasu, M.A.1    Dalva, M.B.2    Zigmond, R.E.3    Greenberg, M.E.4
  • 57
    • 33750682363 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor rapidly increases NMDA receptor channel activity through fyn-mediated phosphorylation
    • Xu F., Plummer M.R., Len G.W., et al. Brain-derived neurotrophic factor rapidly increases NMDA receptor channel activity through fyn-mediated phosphorylation. Brain Res. 1121 (2006) 22-34
    • (2006) Brain Res. , vol.1121 , pp. 22-34
    • Xu, F.1    Plummer, M.R.2    Len, G.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.