메뉴 건너뛰기




Volumn 740, Issue , 2012, Pages 1193-1217

Neuronal calcium signaling and Alzheimer's disease

Author keywords

Amyloid beta (A ); Amyloid precursor protein (APP); Calcineurin; Calmodulin kinase; Endoplasmic reticulum (ER); FAD (familial Alzheimer's disease) mutations; IP 3; IP 3 receptor (IP 3R); LTD; LTP; Mitochondria; NMDA receptors (NMDAR); Postsynaptic density (PSD); Presenilin; Ryanodine receptor (RyR)

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM CHANNEL; CALCIUM CHANNEL CAV1; CALCIUM CHANNEL CAV2; CALCIUM CHANNEL CAV3; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2; PRESENILIN; UNCLASSIFIED DRUG;

EID: 84859882828     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-2888-2_54     Document Type: Article
Times cited : (69)

References (169)
  • 1
    • 0001533582 scopus 로고
    • On the role of calcium in the activity of adenosine 5 -triphosphate hydrolysis by actomyosin
    • Weber A (1959) On the role of calcium in the activity of adenosine 5 -triphosphate hydrolysis by actomyosin. J Biol Chem 234:2764-2769
    • (1959) J Biol Chem , vol.234 , pp. 2764-2769
    • Weber, A.1
  • 2
    • 0040193560 scopus 로고
    • Does EDTA bind to actomyosin?
    • Ebashi F (1961) Does EDTA bind to actomyosin? J Biochem 50:77-78
    • (1961) J Biochem , vol.50 , pp. 77-78
    • Ebashi, F.1
  • 3
    • 72949126637 scopus 로고
    • The calcium pump of the "relaxing granules" of muscle and its dependence on ATP-splitting
    • Hasselbach W, Makinose M (1961) The calcium pump of the "relaxing granules" of muscle and its dependence on ATP-splitting. Biochem Z 333:518-528
    • (1961) Biochem Z , vol.333 , pp. 518-528
    • Hasselbach, W.1    Makinose, M.2
  • 4
    • 84968965880 scopus 로고
    • Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle
    • Ebashi S, Lipmann F (1962) Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle. J Cell Biol 14:389-400
    • (1962) J Cell Biol , vol.14 , pp. 389-400
    • Ebashi, S.1    Lipmann, F.2
  • 5
    • 36949077764 scopus 로고
    • Removal of calcium and relaxation in actomyosin systems
    • Ebashi F, Ebashi S (1962) Removal of calcium and relaxation in actomyosin systems. Nature 194:378-379
    • (1962) Nature , vol.194 , pp. 378-379
    • Ebashi, F.1    Ebashi, S.2
  • 6
    • 0026074512 scopus 로고
    • Calcium pump of the plasma membrane
    • Carafoli E (1991) Calcium pump of the plasma membrane. Physiol Rev 71:129-153
    • (1991) Physiol Rev , vol.71 , pp. 129-153
    • Carafoli, E.1
  • 7
    • 0025975040 scopus 로고
    • The calcium pumping ATPase of the plasma membrane
    • Carafoli E (1991) The calcium pumping ATPase of the plasma membrane. Annu Rev Physiol 53:531-547
    • (1991) Annu Rev Physiol , vol.53 , pp. 531-547
    • Carafoli, E.1
  • 8
    • 0026328124 scopus 로고
    • Molecular characterization of plasma membrane calcium pump isoforms
    • Strehler EE, Heim R, Carafoli E (1991) Molecular characterization of plasma membrane calcium pump isoforms. Adv Exp Med Biol 307:251-261
    • (1991) Adv Exp Med Biol , vol.307 , pp. 251-261
    • Strehler, E.E.1    Heim, R.2    Carafoli, E.3
  • 9
    • 1942421320 scopus 로고    scopus 로고
    • Calcium pumps of plasma membrane and cell interior
    • Strehler EE, Treiman M (2004) Calcium pumps of plasma membrane and cell interior. Curr Mol Med 4:323-335
    • (2004) Curr Mol Med , vol.4 , pp. 323-335
    • Strehler, E.E.1    Treiman, M.2
  • 10
    • 1242317673 scopus 로고    scopus 로고
    • The SLC24 Na+/Ca2+K+ exchanger family: Vision and beyond
    • Schnetkamp PP (2004) The SLC24 Na+/Ca2+K+ exchanger family: vision and beyond. Pflugers Arch 447:683-688
    • (2004) Pflugers Arch , vol.447 , pp. 683-688
    • Schnetkamp, P.P.1
  • 11
    • 0029026638 scopus 로고
    • Structure and function of voltage-gated ion channels
    • Catterall WA (1995) Structure and function of voltage-gated ion channels. Annu Rev Biochem 64:493-531
    • (1995) Annu Rev Biochem , vol.64 , pp. 493-531
    • Catterall, W.A.1
  • 12
    • 0029134828 scopus 로고
    • Molecular biology of calcium channels
    • Perez-Reyes E, Schneider T (1995) Molecular biology of calcium channels. Kidney Int 48:1111-1124
    • (1995) Kidney Int , vol.48 , pp. 1111-1124
    • Perez-Reyes, E.1    Schneider, T.2
  • 13
    • 0029000508 scopus 로고
    • The inositol 1,4,5-trisphosphate (InsP3) receptor
    • Bezprozvanny I, Ehrlich BE (1995) The inositol 1,4,5-trisphosphate (InsP3) receptor. J Membr Biol 145:205-216
    • (1995) J Membr Biol , vol.145 , pp. 205-216
    • Bezprozvanny, I.1    Ehrlich, B.E.2
  • 15
    • 0030810066 scopus 로고    scopus 로고
    • Store depletion and calcium influx
    • Parekh AB, Penner R (1997) Store depletion and calcium influx. Physiol Rev 77:901-930
    • (1997) Physiol Rev , vol.77 , pp. 901-930
    • Parekh, A.B.1    Penner, R.2
  • 17
    • 0037143647 scopus 로고    scopus 로고
    • Calcium signalling: More messengers, more channels, more complexity
    • Bootman MD, Berridge MJ, Roderick HL (2002) Calcium signalling: more messengers, more channels, more complexity. Curr Biol 12:R563-R565
    • (2002) Curr Biol , vol.12
    • Bootman, M.D.1    Berridge, M.J.2    Roderick, H.L.3
  • 18
    • 0035033022 scopus 로고    scopus 로고
    • Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers
    • Lee HC (2001) Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers. Annu Rev Pharmacol Toxicol 41:317-345
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 317-345
    • Lee, H.C.1
  • 19
    • 25444504009 scopus 로고    scopus 로고
    • Calcium signalling by nicotinic acid adenine dinucleotide phosphate (NAADP)
    • Yamasaki M, Churchill GC, Galione A (2005) Calcium signalling by nicotinic acid adenine dinucleotide phosphate (NAADP). FEBS J 272:4598-4606
    • (2005) FEBS J , vol.272 , pp. 4598-4606
    • Yamasaki, M.1    Churchill, G.C.2    Galione, A.3
  • 20
    • 26644460215 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate (NAADP)-mediated calcium signaling
    • Lee HC (2005) Nicotinic acid adenine dinucleotide phosphate (NAADP)-mediated calcium signaling. J Biol Chem 280:33693-33696
    • (2005) J Biol Chem , vol.280 , pp. 33693-33696
    • Lee, H.C.1
  • 21
    • 0028298064 scopus 로고
    • Spatial and temporal signalling by calcium
    • Berridge MJ, Dupont G (1994) Spatial and temporal signalling by calcium. Curr Opin Cell Biol 6:267-274
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 267-274
    • Berridge, M.J.1    Dupont, G.2
  • 23
    • 0029689693 scopus 로고    scopus 로고
    • Structural and functional diversity of voltage-activated calcium channels
    • De Waard M, Gurnett CA, Campbell KP (1996) Structural and functional diversity of voltage-activated calcium channels. Ion Channels 4:41-87
    • (1996) Ion Channels , vol.4 , pp. 41-87
    • De Waard, M.1    Gurnett, C.A.2    Campbell, K.P.3
  • 24
    • 22644444450 scopus 로고    scopus 로고
    • Voltage-dependent calcium channels
    • Lacinova L (2005) Voltage-dependent calcium channels. Gen Physiol Biophys 24(Suppl 1):1-78
    • (2005) Gen Physiol Biophys , vol.24 , Issue.SUPPL. 1 , pp. 1-78
    • Lacinova, L.1
  • 26
    • 0034518423 scopus 로고    scopus 로고
    • Structure and regulation of voltage-gated Ca2+ channels
    • Catterall WA (2000) Structure and regulation of voltage-gated Ca2+ channels. Annu Rev Cell Dev Biol 16:521-555
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 521-555
    • Catterall, W.A.1
  • 27
    • 0029861645 scopus 로고    scopus 로고
    • Elementary events underlying voltage-dependent G-protein inhibition of N-type calcium channels
    • Patil PG, de Leon M, Reed RR, Dubel S, Snutch TP, Yue DT (1996) Elementary events underlying voltage-dependent G-protein inhibition of N-type calcium channels. Biophys J 71:2509-2521
    • (1996) Biophys J , vol.71 , pp. 2509-2521
    • Patil, P.G.1    De Leon, M.2    Reed, R.R.3    Dubel, S.4    Snutch, T.P.5    Yue, D.T.6
  • 28
    • 0032617253 scopus 로고    scopus 로고
    • Voltage-dependent modulation of N-type calcium channels: Role of G protein subunits
    • Ikeda SR, Dunlap K (1999) Voltage-dependent modulation of N-type calcium channels: role of G protein subunits. Adv Second Messenger Phosphoprotein Res 33:131-151
    • (1999) Adv Second Messenger Phosphoprotein Res , vol.33 , pp. 131-151
    • Ikeda, S.R.1    Dunlap, K.2
  • 30
    • 0034664238 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent facilitation and inactivation of P/Q-type Ca2+ channels
    • Lee A, Scheuer T, Catterall WA (2000) Ca2+/calmodulin-dependent facilitation and inactivation of P/Q-type Ca2+ channels. J Neurosci 20:6830-6838
    • (2000) J Neurosci , vol.20 , pp. 6830-6838
    • Lee, A.1    Scheuer, T.2    Catterall, W.A.3
  • 31
    • 0028810956 scopus 로고
    • Synaptic structure and function: Dynamic organization yields architectural precision
    • Burns ME, Augustine GJ (1995) Synaptic structure and function: dynamic organization yields architectural precision. Cell 83:187-194
    • (1995) Cell , vol.83 , pp. 187-194
    • Burns, M.E.1    Augustine, G.J.2
  • 33
    • 0028950269 scopus 로고
    • The biochemistry of neurotransmitter secretion
    • Bajjalieh SM, Scheller RH (1995) The biochemistry of neurotransmitter secretion. J Biol Chem 270:1971-1974
    • (1995) J Biol Chem , vol.270 , pp. 1971-1974
    • Bajjalieh, S.M.1    Scheller, R.H.2
  • 34
    • 0032588572 scopus 로고    scopus 로고
    • Interactions of presynaptic Ca2+ channels and snare proteins in neurotransmitter release
    • Catterall WA (1999) Interactions of presynaptic Ca2+ channels and snare proteins in neurotransmitter release. Ann N Y Acad Sci 868:144-159
    • (1999) Ann N y Acad Sci , vol.868 , pp. 144-159
    • Catterall, W.A.1
  • 35
    • 0028068586 scopus 로고
    • Calcium-dependent interaction of the cytoplasmic region of synaptotagmin with membranes. Autonomous function of a single C2-homologous domain
    • Chapman ER, Jahn R (1994) Calcium-dependent interaction of the cytoplasmic region of synaptotagmin with membranes. Autonomous function of a single C2-homologous domain. J Biol Chem 269:5735-5741
    • (1994) J Biol Chem , vol.269 , pp. 5735-5741
    • Chapman, E.R.1    Jahn, R.2
  • 36
    • 0026494322 scopus 로고
    • The synaptic activation of NMDA receptors and Ca2+ signalling in neurons
    • discussion 172-165
    • Collingridge GL, Randall AD, Davies CH, Alford S (1992) The synaptic activation of NMDA receptors and Ca2+ signalling in neurons. Ciba Found Symp 164:162-171; discussion 172-165
    • (1992) Ciba Found Symp , vol.164 , pp. 162-171
    • Collingridge, G.L.1    Randall, A.D.2    Ch, D.3    Alford, S.4
  • 37
    • 0028987937 scopus 로고
    • Calcium signaling in neurons: Molecular mechanisms and cellular consequences
    • Ghosh A, Greenberg ME (1995) Calcium signaling in neurons: molecular mechanisms and cellular consequences. Science 268:239-247
    • (1995) Science , vol.268 , pp. 239-247
    • Ghosh, A.1    Greenberg, M.E.2
  • 38
    • 0026653052 scopus 로고
    • Protein kinase C modulation of NMDA currents: An important link for LTP induction
    • Ben-Ari Y, Aniksztejn L, Bregestovski P (1992) Protein kinase C modulation of NMDA currents: an important link for LTP induction. Trends Neurosci 15:333-339
    • (1992) Trends Neurosci , vol.15 , pp. 333-339
    • Ben-Ari, Y.1    Aniksztejn, L.2    Bregestovski, P.3
  • 39
    • 0028670773 scopus 로고
    • A secondary phosphorylation of CREB341 at Ser129 is required for the cAMP-mediated control of gene expression. A role for glycogen synthase kinase-3 in the control of gene expression
    • Fiol CJ, Williams JS, Chou CH, Wang QM, Roach PJ, Andrisani OM (1994) A secondary phosphorylation of CREB341 at Ser129 is required for the cAMP-mediated control of gene expression. A role for glycogen synthase kinase-3 in the control of gene expression. J Biol Chem 269:32187-32193
    • (1994) J Biol Chem , vol.269 , pp. 32187-32193
    • Fiol, C.J.1    Williams, J.S.2    Chou, C.H.3    Wang, Q.M.4    Roach, P.J.5    Andrisani, O.M.6
  • 40
    • 0026516710 scopus 로고
    • Characteristics and function of Ca(2+)-and inositol 1,4,5-trisphosphate- releasable stores of Ca2+ in neurons
    • Henzi V, MacDermott AB (1992) Characteristics and function of Ca(2+)-and inositol 1,4,5-trisphosphate-releasable stores of Ca2+ in neurons. Neuroscience 46:251-273
    • (1992) Neuroscience , vol.46 , pp. 251-273
    • Henzi, V.1    MacDermott, A.B.2
  • 41
    • 0027926582 scopus 로고
    • Cell signaling. A tale of two messengers
    • Berridge MJ (1993) Cell signalling. A tale of two messengers. Nature 365:388-389
    • (1993) Nature , vol.365 , pp. 388-389
    • Berridge, M.J.1
  • 42
    • 0028361066 scopus 로고
    • Cyclic ADP-ribose modulates Ca2+ release channels for activation by physiological Ca2+ entry in bullfrog sympathetic neurons
    • Hua SY, Tokimasa T, Takasawa S, Furuya Y, Nohmi M, Okamoto H, Kuba K (1994) Cyclic ADP-ribose modulates Ca2+ release channels for activation by physiological Ca2+ entry in bullfrog sympathetic neurons. Neuron 12:1073-1079
    • (1994) Neuron , vol.12 , pp. 1073-1079
    • Hua, S.Y.1    Tokimasa, T.2    Takasawa, S.3    Furuya, Y.4    Nohmi, M.5    Okamoto, H.6    Kuba, K.7
  • 43
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • Putney JW Jr (1986) A model for receptor-regulated calcium entry. Cell Calcium 7:1-12
    • (1986) Cell Calcium , vol.7 , pp. 1-12
    • Putney, Jr.J.W.1
  • 44
    • 0042035632 scopus 로고    scopus 로고
    • Capacitative calcium entry in the nervous system
    • Putney JW Jr (2003) Capacitative calcium entry in the nervous system. Cell Calcium 34:339-344
    • (2003) Cell Calcium , vol.34 , pp. 339-344
    • Putney, Jr.J.W.1
  • 45
    • 0027962368 scopus 로고
    • Bird GS: Calcium mobilization by inositol phosphates and other intracellular messengers
    • Putney JW Jr (1994) Bird GS: calcium mobilization by inositol phosphates and other intracellular messengers. Trends Endocrinol Metab 5:256-260
    • (1994) Trends Endocrinol Metab , vol.5 , pp. 256-260
    • Putney, Jr.J.W.1
  • 46
    • 0028853445 scopus 로고
    • Degradation of a calcium influx factor (CIF) can be blocked by phosphatase inhibitors or chelation of Ca2+
    • Randriamampita C, Tsien RY (1995) Degradation of a calcium influx factor (CIF) can be blocked by phosphatase inhibitors or chelation of Ca2+. J Biol Chem 270:29-32
    • (1995) J Biol Chem , vol.270 , pp. 29-32
    • Randriamampita, C.1    Tsien, R.Y.2
  • 47
    • 0027386025 scopus 로고
    • A GTP-dependent step in the activation mechanism of capacitative calcium influx
    • Fasolato C, Hoth M, Penner R (1993) A GTP-dependent step in the activation mechanism of capacitative calcium influx. J Biol Chem 268:20737-20740
    • (1993) J Biol Chem , vol.268 , pp. 20737-20740
    • Fasolato, C.1    Hoth, M.2    Penner, R.3
  • 48
    • 0025195367 scopus 로고
    • Quantal' Ca2+ release and the control of Ca2+ entry by inositol phosphates-a possible mechanism
    • Irvine RF (1990) Quantal' Ca2+ release and the control of Ca2+ entry by inositol phosphates-a possible mechanism. FEBS Lett 263:5-9
    • (1990) FEBS Lett , vol.263 , pp. 5-9
    • Irvine, R.F.1
  • 49
    • 0028826727 scopus 로고
    • Capacitative calcium entry
    • Berridge MJ (1995) Capacitative calcium entry. Biochem J 312(Pt 1):1-11
    • (1995) Biochem J , vol.312 , Issue.PART 1 , pp. 1-11
    • Berridge, M.J.1
  • 50
    • 0032127595 scopus 로고    scopus 로고
    • Neuronal calcium signaling
    • Berridge MJ (1998) Neuronal calcium signaling. Neuron 21:13-26
    • (1998) Neuron , vol.21 , pp. 13-26
    • Berridge, M.J.1
  • 51
    • 0032032393 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and calcium-induced calcium release regulate neurotransmitter release at a cholinergic synapse of Aplysia
    • Mothet JP, Fossier P, Meunier FM, Stinnakre J, Tauc L, Baux G (1998) Cyclic ADP-ribose and calcium-induced calcium release regulate neurotransmitter release at a cholinergic synapse of Aplysia. J Physiol 507(Pt 2):405-414
    • (1998) J Physiol , vol.507 , Issue.PART 2 , pp. 405-414
    • Mothet, J.P.1    Fossier, P.2    Meunier, F.M.3    Stinnakre, J.4    Tauc, L.5    Baux, G.6
  • 52
    • 0028336754 scopus 로고
    • Purification of the N-type calcium channel associated with syntaxin and synaptotagmin. A complex implicated in synaptic vesicle exocytosis
    • Leveque C, el Far O, Martin-Moutot N, Sato K, Kato R, Takahashi M, Seagar MJ (1994) Purification of the N-type calcium channel associated with syntaxin and synaptotagmin. A complex implicated in synaptic vesicle exocytosis. J Biol Chem 269:6306-6312
    • (1994) J Biol Chem , vol.269 , pp. 6306-6312
    • Leveque, C.1    El Far, O.2    Martin-Moutot, N.3    Sato, K.4    Kato, R.5    Takahashi, M.6    Seagar, M.J.7
  • 53
    • 0030048838 scopus 로고    scopus 로고
    • Calcium-dependent interaction of N-type calcium channels with the synaptic core complex
    • Sheng ZH, Rettig J, Cook T, Catterall WA (1996) Calcium-dependent interaction of N-type calcium channels with the synaptic core complex. Nature 379:451-454
    • (1996) Nature , vol.379 , pp. 451-454
    • Zh, S.1    Rettig, J.2    Cook, T.3    Catterall, W.A.4
  • 54
    • 0035368680 scopus 로고    scopus 로고
    • How does calcium trigger neurotransmitter release?
    • Augustine GJ (2001) How does calcium trigger neurotransmitter release? Curr Opin Neurobiol 11:320-326
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 320-326
    • Augustine, G.J.1
  • 55
    • 0037174634 scopus 로고    scopus 로고
    • Postsynaptic signaling and plasticity mechanisms
    • Sheng M, Kim MJ (2002) Postsynaptic signaling and plasticity mechanisms. Science 298:776-780
    • (2002) Science , vol.298 , pp. 776-780
    • Sheng, M.1    Kim, M.J.2
  • 56
    • 0029122186 scopus 로고
    • Spatial profile of dendritic calcium transients evoked by action potentials in rat neocortical pyramidal neurones
    • Schiller J, Helmchen F, Sakmann B (1995) Spatial profile of dendritic calcium transients evoked by action potentials in rat neocortical pyramidal neurones. J Physiol 487(Pt 3): 583-600
    • (1995) J Physiol , vol.487 , Issue.PART 3 , pp. 583-600
    • Schiller, J.1    Helmchen, F.2    Sakmann, B.3
  • 58
    • 0036906215 scopus 로고    scopus 로고
    • Complexity of calcium signaling in synaptic spines
    • Franks KM, Sejnowski TJ (2002) Complexity of calcium signaling in synaptic spines. Bioessays 24:1130-1144
    • (2002) Bioessays , vol.24 , pp. 1130-1144
    • Franks, K.M.1    Sejnowski, T.J.2
  • 59
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy MB (2000) Signal-processing machines at the postsynaptic density. Science 290:750-754
    • (2000) Science , vol.290 , pp. 750-754
    • Kennedy, M.B.1
  • 61
    • 0029664973 scopus 로고    scopus 로고
    • Ca2+ signaling requirements for long-term depression in the hippocampus
    • Cummings JA, Mulkey RM, Nicoll RA, Malenka RC (1996) Ca2+ signaling requirements for long-term depression in the hippocampus. Neuron 16:825-833
    • (1996) Neuron , vol.16 , pp. 825-833
    • Cummings, J.A.1    Mulkey, R.M.2    Nicoll, R.A.3    Malenka, R.C.4
  • 62
    • 0035369112 scopus 로고    scopus 로고
    • NMDA receptor subunits: Diversity, development and disease
    • Cull-Candy S, Brickley S, Farrant M (2001) NMDA receptor subunits: diversity, development and disease. Curr Opin Neurobiol 11:327-335
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 327-335
    • Cull-Candy, S.1    Brickley, S.2    Farrant, M.3
  • 63
    • 0036241207 scopus 로고    scopus 로고
    • Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
    • Hardingham GE, Fukunaga Y, Bading H (2002) Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways. Nat Neurosci 5:405-414
    • (2002) Nat Neurosci , vol.5 , pp. 405-414
    • Hardingham, G.E.1    Fukunaga, Y.2    Bading, H.3
  • 64
    • 33645837486 scopus 로고    scopus 로고
    • Opposing role of synaptic and extrasynaptic NMDA receptors in regulation of the extracellular signalregulated kinases (ERK) activity in cultured rat hippocampal neurons
    • Ivanov A, Pellegrino C, Rama S, Dumalska I, Salyha Y, Ben-Ari Y, Medina I (2006) Opposing role of synaptic and extrasynaptic NMDA receptors in regulation of the extracellular signalregulated kinases (ERK) activity in cultured rat hippocampal neurons. J Physiol 572:789-798
    • (2006) J Physiol , vol.572 , pp. 789-798
    • Ivanov, A.1    Pellegrino, C.2    Rama, S.3    Dumalska, I.4    Salyha, Y.5    Ben-Ari, Y.6    Medina, I.7
  • 65
    • 2442711477 scopus 로고    scopus 로고
    • NR2B-containing receptors mediate cross talk among hippocampal synapses
    • Scimemi A, Fine A, Kullmann DM, Rusakov DA (2004) NR2B-containing receptors mediate cross talk among hippocampal synapses. J Neurosci 24:4767-4777
    • (2004) J Neurosci , vol.24 , pp. 4767-4777
    • Scimemi, A.1    Fine, A.2    Kullmann, D.M.3    Rusakov, D.A.4
  • 66
    • 0032520117 scopus 로고    scopus 로고
    • Increased contribution of NR2A subunit to synaptic NMDA receptors in developing rat cortical neurons
    • Stocca G, Vicini S (1998) Increased contribution of NR2A subunit to synaptic NMDA receptors in developing rat cortical neurons. J Physiol 507(Pt 1):13-24
    • (1998) J Physiol , vol.507 , Issue.PART 1 , pp. 13-24
    • Stocca, G.1    Vicini, S.2
  • 67
    • 33645822456 scopus 로고    scopus 로고
    • Synaptic and extrasynaptic NMDA receptor NR2 subunits in cultured hippocampal neurons
    • Thomas CG, Miller AJ, Westbrook GL (2006) Synaptic and extrasynaptic NMDA receptor NR2 subunits in cultured hippocampal neurons. J Neurophysiol 95:1727-1734
    • (2006) J Neurophysiol , vol.95 , pp. 1727-1734
    • Thomas, C.G.1    Miller, A.J.2    Westbrook, G.L.3
  • 70
    • 54049087697 scopus 로고    scopus 로고
    • Regulation of NMDA receptor subunit expression and its implications for LTD
    • Yashiro K, Philpot BD (2008) Regulation of NMDA receptor subunit expression and its implications for LTD, LTP, and metaplasticity. Neuropharmacology 55:1081-1094
    • (2008) LTP, and Metaplasticity. Neuropharmacology , vol.55 , pp. 1081-1094
    • Yashiro, K.1    Philpot, B.D.2
  • 71
    • 0031283172 scopus 로고    scopus 로고
    • Identification of the Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in the alpha-amino-3-hydroxyl-5-methyl-4- isoxazole-propionate-type glutamate receptor
    • Barria A, Derkach V, Soderling T (1997) Identification of the Ca2+/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 272:32727-32730
    • (1997) J Biol Chem , vol.272 , pp. 32727-32730
    • Barria, A.1    Derkach, V.2    Soderling, T.3
  • 72
    • 0032588030 scopus 로고    scopus 로고
    • Ca2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors
    • Derkach V, Barria A, Soderling TR (1999) Ca2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4- isoxazolepropionate type glutamate receptors. Proc Natl Acad Sci USA 96:3269-3274
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3269-3274
    • Derkach, V.1    Barria, A.2    Soderling, T.R.3
  • 73
    • 0032565873 scopus 로고    scopus 로고
    • Modulation of AMPA receptor unitary conductance by synaptic activity
    • Benke TA, Luthi A, Isaac JT, Collingridge GL (1998) Modulation of AMPA receptor unitary conductance by synaptic activity. Nature 393:793-797
    • (1998) Nature , vol.393 , pp. 793-797
    • Benke, T.A.1    Luthi, A.2    Isaac, J.T.3    Collingridge, G.L.4
  • 74
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
    • Hayashi Y, Shi SH, Esteban JA, Piccini A, Poncer JC, Malinow R (2000) Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science 287:2262-2267
    • (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
  • 75
    • 0037162696 scopus 로고    scopus 로고
    • Ras and Rap control AMPA receptor Trafficking during synaptic plasticity
    • Zhu JJ, Qin Y, Zhao M, Van Aelst L, Malinow R (2002) Ras and Rap control AMPA receptor Trafficking during synaptic plasticity. Cell 110:443-455
    • (2002) Cell , vol.110 , pp. 443-455
    • Zhu, J.J.1    Qin, Y.2    Zhao, M.3    Van Aelst, L.4    Malinow, R.5
  • 77
    • 4744347673 scopus 로고    scopus 로고
    • Activity-dependent regulation of calcium/calmodulin-dependent protein kinase II localization
    • Schulman H (2004) Activity-dependent regulation of calcium/calmodulin- dependent protein kinase II localization. J Neurosci 24:8399-8403
    • (2004) J Neurosci , vol.24 , pp. 8399-8403
    • Schulman, H.1
  • 78
    • 0028176087 scopus 로고
    • Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression
    • Mulkey RM, Endo S, Shenolikar S, Malenka RC (1994) Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression. Nature 369:486-488
    • (1994) Nature , vol.369 , pp. 486-488
    • Mulkey, R.M.1    Endo, S.2    Shenolikar, S.3    Malenka, R.C.4
  • 79
    • 0033639083 scopus 로고    scopus 로고
    • Reinsertion or degradation of AMPA receptors determined by activitydependent endocytic sorting
    • Ehlers MD (2000) Reinsertion or degradation of AMPA receptors determined by activitydependent endocytic sorting. Neuron 28:511-525
    • (2000) Neuron , vol.28 , pp. 511-525
    • Ehlers, M.D.1
  • 80
    • 0027432518 scopus 로고
    • An essential role for protein phosphatases in hippocampal long-term depression
    • Mulkey RM, Herron CE, Malenka RC (1993) An essential role for protein phosphatases in hippocampal long-term depression. Science 261:1051-1055
    • (1993) Science , vol.261 , pp. 1051-1055
    • Mulkey, R.M.1    Herron, C.E.2    Malenka, R.C.3
  • 81
    • 0034237258 scopus 로고    scopus 로고
    • PDZ domains in synapse assembly and signalling
    • Garner CC, Nash J, Huganir RL (2000) PDZ domains in synapse assembly and signalling. Trends Cell Biol 10:274-280
    • (2000) Trends Cell Biol , vol.10 , pp. 274-280
    • Garner, C.C.1    Nash, J.2    Huganir, R.L.3
  • 82
    • 0024039736 scopus 로고
    • Active site-directed inhibition of Ca2+/calmodulin-dependent protein kinase type II by a bifunctional calmodulin-binding peptide
    • Kelly PT, Weinberger RP, Waxham MN (1988) Active site-directed inhibition of Ca2+/calmodulin-dependent protein kinase type II by a bifunctional calmodulin-binding peptide. Proc Natl Acad Sci USA 85:4991-4995
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4991-4995
    • Kelly, P.T.1    Weinberger, R.P.2    Waxham, M.N.3
  • 83
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • Lisman J, Schulman H, Cline H (2002) The molecular basis of CaMKII function in synaptic and behavioural memory. Nat Rev Neurosci 3:175-190
    • (2002) Nat Rev Neurosci , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 84
    • 0022519298 scopus 로고
    • Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: A Ca2+triggered molecular switch
    • Miller SG, Kennedy MB (1986) Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+triggered molecular switch. Cell 44:861-870
    • (1986) Cell , vol.44 , pp. 861-870
    • Miller, S.G.1    Kennedy, M.B.2
  • 85
    • 0030911904 scopus 로고    scopus 로고
    • Differential inactivation of postsynaptic density-associated and soluble Ca2+/calmodulin-dependent protein kinase II by protein phosphatases 1 and 2A
    • Strack S, Barban MA, Wadzinski BE, Colbran RJ (1997) Differential inactivation of postsynaptic density-associated and soluble Ca2+/calmodulin- dependent protein kinase II by protein phosphatases 1 and 2A. J Neurochem 68:2119-2128
    • (1997) J Neurochem , vol.68 , pp. 2119-2128
    • Strack, S.1    Barban, M.A.2    Wadzinski, B.E.3    Colbran, R.J.4
  • 89
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau HC, Schenker LT, Kennedy MB, Seeburg PH (1995) Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269:1737-1740
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 90
    • 0032055396 scopus 로고    scopus 로고
    • SynGAP: A synaptic RasGAP that associates with the PSD-95/SAP90 protein family
    • Kim JH, Liao D, Lau LF, Huganir RL (1998) SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family. Neuron 20:683-691
    • (1998) Neuron , vol.20 , pp. 683-691
    • Kim, J.H.1    Liao, D.2    Lau, L.F.3    Huganir, R.L.4
  • 91
    • 0034330386 scopus 로고    scopus 로고
    • Postsynaptic organization and regulation of excitatory synapses
    • Scannevin RH, Huganir RL (2000) Postsynaptic organization and regulation of excitatory synapses. Nat Rev Neurosci 1:133-141
    • (2000) Nat Rev Neurosci , vol.1 , pp. 133-141
    • Scannevin, R.H.1    Huganir, R.L.2
  • 92
    • 0032078872 scopus 로고    scopus 로고
    • A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM kinase II
    • Chen HJ, Rojas-Soto M, Oguni A, Kennedy MB (1998) A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM kinase II. Neuron 20:895-904
    • (1998) Neuron , vol.20 , pp. 895-904
    • Chen, H.J.1    Rojas-Soto, M.2    Oguni, A.3    Kennedy, M.B.4
  • 93
  • 95
    • 0033165926 scopus 로고    scopus 로고
    • Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
    • Naisbitt S, Kim E, Tu JC, Xiao B, Sala C, Valtschanoff J, Weinberg RJ, Worley PF, Sheng M (1999) Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. Neuron 23:569-582
    • (1999) Neuron , vol.23 , pp. 569-582
    • Naisbitt, S.1    Kim, E.2    Tu, J.C.3    Xiao, B.4    Sala, C.5    Valtschanoff, J.6    Weinberg, R.J.7    Worley, P.F.8    Sheng, M.9
  • 96
    • 0025807509 scopus 로고
    • CREB: A Ca(2+)-regulated transcription factor phosphorylated by calmodulin-dependent kinases
    • Sheng M, Thompson MA, Greenberg ME (1991) CREB: a Ca(2+)-regulated transcription factor phosphorylated by calmodulin-dependent kinases. Science 252:1427-1430
    • (1991) Science , vol.252 , pp. 1427-1430
    • Sheng, M.1    Thompson, M.A.2    Greenberg, M.E.3
  • 97
    • 0028338460 scopus 로고
    • Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB
    • Ginty DD, Bonni A, Greenberg ME (1994) Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB. Cell 77:713-725
    • (1994) Cell , vol.77 , pp. 713-725
    • Ginty, D.D.1    Bonni, A.2    Greenberg, M.E.3
  • 100
    • 0025753154 scopus 로고
    • CAMP response elementbinding protein is activated by Ca2+/calmodulin-as well as cAMP-dependent protein kinase
    • Dash PK, Karl KA, Colicos MA, Prywes R, Kandel ER (1991) CAMP response elementbinding protein is activated by Ca2+/calmodulin-as well as cAMP-dependent protein kinase. Proc Natl Acad Sci USA 88:5061-5065
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5061-5065
    • Dash, P.K.1    Karl, K.A.2    Colicos, M.A.3    Prywes, R.4    Kandel, E.R.5
  • 102
    • 0027943988 scopus 로고
    • Differential activation of CREB by Ca2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity
    • Sun P, Enslen H, Myung PS, Maurer RA (1994) Differential activation of CREB by Ca2+/calmodulin-dependent protein kinases type II and type IV involves phosphorylation of a site that negatively regulates activity. Genes Dev 8:2527-2539
    • (1994) Genes Dev , vol.8 , pp. 2527-2539
    • Sun, P.1    Enslen, H.2    Myung, P.S.3    Maurer, R.A.4
  • 103
    • 0029789643 scopus 로고    scopus 로고
    • Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase
    • Xing J, Ginty DD, Greenberg ME (1996) Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 273:959-963
    • (1996) Science , vol.273 , pp. 959-963
    • Xing, J.1    Ginty, D.D.2    Greenberg, M.E.3
  • 104
    • 0035956978 scopus 로고    scopus 로고
    • Activity-dependent CREB phosphorylation: Convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogenactivated protein kinase pathway
    • Wu GY, Deisseroth K, Tsien RW (2001) Activity-dependent CREB phosphorylation: convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogenactivated protein kinase pathway. Proc Natl Acad Sci USA 98:2808-2813
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2808-2813
    • Wu, G.Y.1    Deisseroth, K.2    Tsien, R.W.3
  • 105
    • 0028949133 scopus 로고
    • Adenylyl cyclases and the interaction between calcium and cAMP signalling
    • Cooper DM, Mons N, Karpen JW (1995) Adenylyl cyclases and the interaction between calcium and cAMP signalling. Nature 374:421-424
    • (1995) Nature , vol.374 , pp. 421-424
    • Cooper, D.M.1    Mons, N.2    Karpen, J.W.3
  • 106
    • 0028351190 scopus 로고
    • Targeted disruption of the BDNF gene perturbs brain and sensory neuron development but not motor neuron development
    • Jones KR, Farinas I, Backus C, Reichardt LF (1994) Targeted disruption of the BDNF gene perturbs brain and sensory neuron development but not motor neuron development. Cell 76:989-999
    • (1994) Cell , vol.76 , pp. 989-999
    • Jones, K.R.1    Farinas, I.2    Backus, C.3    Reichardt, L.F.4
  • 107
    • 0030867989 scopus 로고    scopus 로고
    • Abnormal cerebellar development and foliation in BDNF mice reveals a role for neurotrophins in CNS patterning
    • Schwartz PM, Borghesani PR, Levy RL, Pomeroy SL, Segal RA (1997) Abnormal cerebellar development and foliation in BDNF mice reveals a role for neurotrophins in CNS patterning. Neuron 19:269-281
    • (1997) Neuron , vol.19 , pp. 269-281
    • Schwartz, P.M.1    Borghesani, P.R.2    Levy, R.L.3    Pomeroy, S.L.4    Segal, R.A.5
  • 109
    • 0028217132 scopus 로고
    • Requirement for BDNF in activity-dependent survival of cortical neurons
    • Ghosh A, Carnahan J, Greenberg ME (1994) Requirement for BDNF in activity-dependent survival of cortical neurons. Science 263:1618-1623
    • (1994) Science , vol.263 , pp. 1618-1623
    • Ghosh, A.1    Carnahan, J.2    Greenberg, M.E.3
  • 110
    • 0034657129 scopus 로고    scopus 로고
    • Developmentally regulated NMDA receptordependent dephosphorylation of cAMP response element-binding protein (CREB) in hippocampal neurons
    • Sala C, Rudolph-Correia S, Sheng M (2000) Developmentally regulated NMDA receptordependent dephosphorylation of cAMP response element-binding protein (CREB) in hippocampal neurons. J Neurosci 20:3529-3536
    • (2000) J Neurosci , vol.20 , pp. 3529-3536
    • Sala, C.1    Rudolph-Correia, S.2    Sheng, M.3
  • 111
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J, Allsop D (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci 12:383-388
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 112
    • 0022869529 scopus 로고
    • Altered structural proteins in plaques and tangles: What do they tell us about the biology of Alzheimer's disease?
    • Selkoe DJ (1986) Altered structural proteins in plaques and tangles: what do they tell us about the biology of Alzheimer's disease? Neurobiol Aging 7:425-432
    • (1986) Neurobiol Aging , vol.7 , pp. 425-432
    • Selkoe, D.J.1
  • 113
    • 0024410266 scopus 로고
    • The deposition of amyloid proteins in the aging mammalian brain: Implications for Alzheimer's disease
    • Selkoe DJ (1989) The deposition of amyloid proteins in the aging mammalian brain: implications for Alzheimer's disease. Ann Med 21:73-76
    • (1989) Ann Med , vol.21 , pp. 73-76
    • Selkoe, D.J.1
  • 114
    • 0024544316 scopus 로고
    • The neurobiology of Alzheimer's disease
    • Henderson VW, Finch CE (1989) The neurobiology of Alzheimer's disease. J Neurosurg 70:335-353
    • (1989) J Neurosurg , vol.70 , pp. 335-353
    • Henderson, V.W.1    Finch, C.E.2
  • 115
    • 0026742451 scopus 로고
    • Impaired spatial learning in alphacalcium-calmodulin kinase II mutant mice
    • Silva AJ, Paylor R, Wehner JM, Tonegawa S (1992) Impaired spatial learning in alphacalcium-calmodulin kinase II mutant mice. Science 257:206-211
    • (1992) Science , vol.257 , pp. 206-211
    • Silva, A.J.1    Paylor, R.2    Wehner, J.M.3    Tonegawa, S.4
  • 117
    • 0022156464 scopus 로고
    • Neuronal origin of a cerebral amyloid: Neurofi brillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels
    • Masters CL, Multhaup G, Simms G, Pottgiesser J, Martins RN, Beyreuther K (1985) Neuronal origin of a cerebral amyloid: neurofi brillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO J 4:2757-2763
    • (1985) EMBO J , vol.4 , pp. 2757-2763
    • Masters, C.L.1    Multhaup, G.2    Simms, G.3    Pottgiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 118
    • 0023838532 scopus 로고
    • Immunochemical Identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease
    • Abraham CR, Selkoe DJ, Potter H (1988) Immunochemical Identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell 52:487-501
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.R.1    Selkoe, D.J.2    Potter, H.3
  • 119
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-infl ammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • McGeer PL, Schulzer M, McGeer EG (1996) Arthritis and anti-infl ammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies. Neurology 47:425-432
    • (1996) Neurology , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 122
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla FM (2002) Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat Rev Neurosci 3:862-872
    • (2002) Nat Rev Neurosci , vol.3 , pp. 862-872
    • Laferla, F.M.1
  • 123
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A, Mina E, Kayed R, Milton SC, Parker I, Glabe CG (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294-17300
    • (2005) J Biol Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 124
    • 0028204224 scopus 로고
    • Calcium ionophore increases amyloid beta peptide production by cultured cells
    • Querfurth HW, Selkoe DJ (1994) Calcium ionophore increases amyloid beta peptide production by cultured cells. Biochemistry 33:4550-4561
    • (1994) Biochemistry , vol.33 , pp. 4550-4561
    • Querfurth, H.W.1    Selkoe, D.J.2
  • 126
    • 61349096009 scopus 로고    scopus 로고
    • Synchronous hyperactivity and intercellular calcium waves in astrocytes in Alzheimer mice
    • Kuchibhotla KV, Lattarulo CR, Hyman BT, Bacskai BJ (2009) Synchronous hyperactivity and intercellular calcium waves in astrocytes in Alzheimer mice. Science 323:1211-1215
    • (2009) Science , vol.323 , pp. 1211-1215
    • Kuchibhotla, K.V.1    Lattarulo, C.R.2    Hyman, B.T.3    Bacskai, B.J.4
  • 128
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gammasecretase activity
    • Wolfe MS, Xia W, Ostaszewski BL, Diehl TS, Kimberly WT, Selkoe DJ (1999) Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gammasecretase activity. Nature 398:513-517
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 130
    • 0037462753 scopus 로고    scopus 로고
    • Capacitive calcium entry is directly attenuated by mutant presenilin-1, independent of the expression of the amyloid precursor protein
    • Herms J, Schneider I, Dewachter I, Caluwaerts N, Kretzschmar H, Van Leuven F (2003) Capacitive calcium entry is directly attenuated by mutant presenilin-1, independent of the expression of the amyloid precursor protein. J Biol Chem 278:2484-2489
    • (2003) J Biol Chem , vol.278 , pp. 2484-2489
    • Herms, J.1    Schneider, I.2    Dewachter, I.3    Caluwaerts, N.4    Kretzschmar, H.5    Van Leuven, F.6
  • 131
    • 24644460177 scopus 로고    scopus 로고
    • Enhanced caffeine-induced Ca2+ release in the 3xTg-AD mouse model of Alzheimer's disease
    • Smith IF, Hitt B, Green KN, Oddo S, LaFerla FM (2005) Enhanced caffeine-induced Ca2+ release in the 3xTg-AD mouse model of Alzheimer's disease. J Neurochem 94:1711-1718
    • (2005) J Neurochem , vol.94 , pp. 1711-1718
    • Smith, I.F.1    Hitt, B.2    Green, K.N.3    Oddo, S.4    Laferla, F.M.5
  • 132
    • 0242414704 scopus 로고    scopus 로고
    • Capacitative calcium entry induces hippocampal long term potentiation in the absence of presenilin-1
    • Ris L, Dewachter I, Reverse D, Godaux E, Van Leuven F (2003) Capacitative calcium entry induces hippocampal long term potentiation in the absence of presenilin-1. J Biol Chem 278:44393-44399
    • (2003) J Biol Chem , vol.278 , pp. 44393-44399
    • Ris, L.1    Dewachter, I.2    Reverse, D.3    Godaux, E.4    Van Leuven, F.5
  • 134
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny I, Mattson MP (2008) Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci 31:454-463
    • (2008) Trends Neurosci , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 135
    • 0032972683 scopus 로고    scopus 로고
    • Alzheimer's presenilin-1 mutation potentiates inositol 1,4,5-trisphosphate-mediated calcium signaling in Xenopus oocytes
    • Leissring MA, Paul BA, Parker I, Cotman CW, LaFerla FM (1999) Alzheimer's presenilin-1 mutation potentiates inositol 1,4,5-trisphosphate-mediated calcium signaling in Xenopus oocytes. J Neurochem 72:1061-1068
    • (1999) J Neurochem , vol.72 , pp. 1061-1068
    • Leissring, M.A.1    Paul, B.A.2    Parker, I.3    Cotman, C.W.4    Laferla, F.M.5
  • 136
    • 34247621471 scopus 로고    scopus 로고
    • Enhanced ryanodinemediated calcium release in mutant PS1-expressing Alzheimer's mouse models
    • Stutzmann GE, Smith I, Caccamo A, Oddo S, Parker I, Laferla F (2007) Enhanced ryanodinemediated calcium release in mutant PS1-expressing Alzheimer's mouse models. Ann N Y Acad Sci 1097:265-277
    • (2007) Ann N y Acad Sci , vol.1097 , pp. 265-277
    • Stutzmann, G.E.1    Smith, I.2    Caccamo, A.3    Oddo, S.4    Parker, I.5    Laferla, F.6
  • 137
    • 68049134265 scopus 로고    scopus 로고
    • Deviant ryanodine receptormediated calcium release resets synaptic homeostasis in presymptomatic 3xTg-AD mice
    • Chakroborty S, Goussakov I, Miller MB, Stutzmann GE (2009) Deviant ryanodine receptormediated calcium release resets synaptic homeostasis in presymptomatic 3xTg-AD mice. J Neurosci 29:9458-9470
    • (2009) J Neurosci , vol.29 , pp. 9458-9470
    • Chakroborty, S.1    Goussakov, I.2    Miller, M.B.3    Stutzmann, G.E.4
  • 138
    • 33748767364 scopus 로고    scopus 로고
    • Acceleration of amyloid beta-peptide aggregation by physiological concentrations of calcium
    • Isaacs AM, Senn DB, Yuan M, Shine JP, Yankner BA (2006) Acceleration of amyloid beta-peptide aggregation by physiological concentrations of calcium. J Biol Chem 281:27916-27923
    • (2006) J Biol Chem , vol.281 , pp. 27916-27923
    • Isaacs, A.M.1    Senn, D.B.2    Yuan, M.3    Shine, J.P.4    Yankner, B.A.5
  • 139
    • 46249123354 scopus 로고    scopus 로고
    • SERCA pump activity is physiologically regulated by presenilin and regulates amyloid beta production
    • Green KN, Demuro A, Akbari Y, Hitt BD, Smith IF, Parker I, LaFerla FM (2008) SERCA pump activity is physiologically regulated by presenilin and regulates amyloid beta production. J Cell Biol 181:1107-1116
    • (2008) J Cell Biol , vol.181 , pp. 1107-1116
    • Green, K.N.1    Demuro, A.2    Akbari, Y.3    Hitt, B.D.4    Smith, I.F.5    Parker, I.6    Laferla, F.M.7
  • 140
    • 77449105037 scopus 로고    scopus 로고
    • Presenilin-2 dampens intracellular Ca2+ stores by increasing Ca2+ leakage and reducing Ca2+ uptake
    • Brunello L, Zampese E, Florean C, Pozzan T, Pizzo P, Fasolato C (2009) Presenilin-2 dampens intracellular Ca2+ stores by increasing Ca2+ leakage and reducing Ca2+ uptake. J Cell Mol Med 13:3358-3369
    • (2009) J Cell Mol Med , vol.13 , pp. 3358-3369
    • Brunello, L.1    Zampese, E.2    Florean, C.3    Pozzan, T.4    Pizzo, P.5    Fasolato, C.6
  • 142
    • 78751562521 scopus 로고    scopus 로고
    • A novel role for {gamma}-secretase: Selective regulation of spontaneous neurotransmitter release from hippocampal neurons
    • Pratt KG, Zhu P, Watari H, Cook DG, Sullivan JM (2011) A novel role for {gamma}-secretase: selective regulation of spontaneous neurotransmitter release from hippocampal neurons. J Neurosci Off J Soc Neurosci 31:899-906
    • (2011) J Neurosci off J Soc Neurosci , vol.31 , pp. 899-906
    • Pratt, K.G.1    Zhu, P.2    Watari, H.3    Cook, D.G.4    Sullivan, J.M.5
  • 143
    • 37549007249 scopus 로고    scopus 로고
    • Effect of the knockdown of amyloid precursor protein on intracellular calcium increases in a neuronal cell line derived from the cerebral cortex of a trisomy 16 mouse
    • Rojas G, Cardenas AM, Fernandez-Olivares P, Shimahara T, Segura-Aguilar J, Caviedes R, Caviedes P (2008) Effect of the knockdown of amyloid precursor protein on intracellular calcium increases in a neuronal cell line derived from the cerebral cortex of a trisomy 16 mouse. Exp Neurol 209:234-242
    • (2008) Exp Neurol , vol.209 , pp. 234-242
    • Rojas, G.1    Cardenas, A.M.2    Fernandez-Olivares, P.3    Shimahara, T.4    Segura-Aguilar, J.5    Caviedes, R.6    Caviedes, P.7
  • 146
    • 77957790011 scopus 로고    scopus 로고
    • FAD mutations in amyloid precursor protein do not directly perturb intracellular calcium homeostasis
    • Stieren E, Werchan WP, El Ayadi A, Li F, Boehning D (2010) FAD mutations in amyloid precursor protein do not directly perturb intracellular calcium homeostasis. PLoS One 5:e11992
    • (2010) PLoS One , vol.5
    • Stieren, E.1    Werchan, W.P.2    El Ayadi, A.3    Li, F.4    Boehning, D.5
  • 148
    • 79960247207 scopus 로고    scopus 로고
    • Calcium homeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress
    • Gallego-Sandin S, Alonso MT, Garcia-Sancho J (2011) Calcium homeostasis modulator 1 (CALHM1) reduces the calcium content of the endoplasmic reticulum (ER) and triggers ER stress. Biochem J 437(3):469-475
    • (2011) Biochem J , vol.437 , Issue.3 , pp. 469-475
    • Gallego-Sandin, S.1    Alonso, M.T.2    Garcia-Sancho, J.3
  • 149
    • 77956586233 scopus 로고    scopus 로고
    • NMDA-mediated Ca(2+)influx drives aberrant ryanodine receptor activation in dendrites of young Alzheimer's disease mice
    • Goussakov I, Miller MB, Stutzmann GE (2010) NMDA-mediated Ca(2+) influx drives aberrant ryanodine receptor activation in dendrites of young Alzheimer's disease mice. J Neurosci 30:12128-12137
    • (2010) J Neurosci , vol.30 , pp. 12128-12137
    • Goussakov, I.1    Miller, M.B.2    Stutzmann, G.E.3
  • 150
    • 0033136259 scopus 로고    scopus 로고
    • Making new connections: Role of ERK/MAP kinase signaling in neuronal plasticity
    • Impey S, Obrietan K, Storm DR (1999) Making new connections: role of ERK/MAP kinase signaling in neuronal plasticity. Neuron 23:11-14
    • (1999) Neuron , vol.23 , pp. 11-14
    • Impey, S.1    Obrietan, K.2    Storm, D.R.3
  • 151
    • 0024461379 scopus 로고
    • Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP
    • Malinow R, Schulman H, Tsien RW (1989) Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP. Science 245:862-866
    • (1989) Science , vol.245 , pp. 862-866
    • Malinow, R.1    Schulman, H.2    Tsien, R.W.3
  • 152
    • 14844315768 scopus 로고    scopus 로고
    • Amyloid beta prevents activation of calcium/calmodulin-dependent protein kinase II and AMPA receptor phosphorylation during hippocampal long-term potentiation
    • Zhao D, Watson JB, Xie CW (2004) Amyloid beta prevents activation of calcium/calmodulin-dependent protein kinase II and AMPA receptor phosphorylation during hippocampal long-term potentiation. J Neurophysiol 92:2853-2858
    • (2004) J Neurophysiol , vol.92 , pp. 2853-2858
    • Zhao, D.1    Watson, J.B.2    Xie, C.W.3
  • 156
    • 34548788549 scopus 로고    scopus 로고
    • Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process
    • Jang H, Zheng J, Nussinov R (2007) Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process. Biophys J 93:1938-1949
    • (2007) Biophys J , vol.93 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 157
    • 70350133699 scopus 로고    scopus 로고
    • Increased levels of NMDA receptor NR2A subunits at pre-and postsynaptic sites of the hippocampal CA1: An early response to conditional double knockout of presenilin 1 and 2
    • Aoki C, Lee J, Nedelescu H, Ahmed T, Ho A, Shen J (2009) Increased levels of NMDA receptor NR2A subunits at pre-and postsynaptic sites of the hippocampal CA1: an early response to conditional double knockout of presenilin 1 and 2. J Comp Neurol 517:512-523
    • (2009) J Comp Neurol , vol.517 , pp. 512-523
    • Aoki, C.1    Lee, J.2    Nedelescu, H.3    Ahmed, T.4    Ho, A.5    Shen, J.6
  • 159
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y, Krapivinsky G, Clapham DE (2004) The mitochondrial calcium uniporter is a highly selective ion channel. Nature 427:360-364
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 160
    • 70349669093 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter
    • Jiang D, Zhao L, Clapham DE (2009) Genome-wide RNAi screen identifi es Letm1 as a mitochondrial Ca2+/H+ antiporter. Science 326:144-147
    • (2009) Science , vol.326 , pp. 144-147
    • Jiang, D.1    Zhao, L.2    Clapham, D.E.3
  • 161
  • 163
    • 67649687124 scopus 로고    scopus 로고
    • The Alzheimer's disease mitochondrial cascade hypothesis an update
    • Swerdlow RH, Khan SM (2009) The Alzheimer's disease mitochondrial cascade hypothesis: an update. Exp Neurol 218:308-315
    • (2009) Exp Neurol , vol.218 , pp. 308-315
    • Swerdlow, R.H.1    Khan, S.M.2
  • 166
    • 34250725402 scopus 로고    scopus 로고
    • Mitochondrial Ca2+ as a key regulator of cell life and death
    • Giacomello M, Drago I, Pizzo P, Pozzan T (2007) Mitochondrial Ca2+ as a key regulator of cell life and death. Cell Death Differ 14:1267-1274
    • (2007) Cell Death Differ , vol.14 , pp. 1267-1274
    • Giacomello, M.1    Drago, I.2    Pizzo, P.3    Pozzan, T.4
  • 168
    • 61849142791 scopus 로고    scopus 로고
    • Calcium signaling and neurodegenerative diseases
    • Bezprozvanny I (2009) Calcium signaling and neurodegenerative diseases. Trends Mol Med 15:89-100
    • (2009) Trends Mol Med , vol.15 , pp. 89-100
    • Bezprozvanny, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.