메뉴 건너뛰기




Volumn 15, Issue 3, 2010, Pages 1168-1195

Control of intracellular calcium signaling as a neuroprotective strategy

Author keywords

Accessory proteins; Associated proteins; Ca2+; Calcium; Cytoprotection; Extracellular; G protein coupled receptors; Imaging; Intracellular; Intracellular calcium channel; Ion channel; Microscopy; Neurodegeneration; Neuroprotection; Signaling

Indexed keywords

NEUROPROTECTIVE AGENT;

EID: 77950362173     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules15031168     Document Type: Article
Times cited : (51)

References (238)
  • 1
    • 0031019855 scopus 로고    scopus 로고
    • Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression
    • DOI 10.1038/385260a0
    • Hardingham, G. E.; Chawla, S.; Johnson, C. M. Bading, H. Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression. Nature 1997, 385, 260-265. (Pubitemid 27043726)
    • (1997) Nature , vol.385 , Issue.6613 , pp. 260-265
    • Hardingham, G.E.1    Chawla, S.2    Johnson, C.M.3    Bading, H.4
  • 2
    • 0033858553 scopus 로고    scopus 로고
    • Transcription-dependent neuronal plasticity the nuclear calcium hypothesis
    • Bading, H. Transcription-dependent neuronal plasticity the nuclear calcium hypothesis. Eur. J. Biochem. 2000, 267, 5280-5283.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5280-5283
    • Bading, H.1
  • 4
    • 0036902175 scopus 로고    scopus 로고
    • The contribution of intracellular calcium stores to mEPSCs recorded in layer II neurones of rat barrel cortex
    • DOI 10.1113/jphysiol.2002.022103
    • Simkus, C. R.; Stricker, C. The contribution of intracellular calcium stores to mEPSCs recorded in layer II neurones of rat barrel cortex. J. Physiol. 2002, 545, 521-535. (Pubitemid 36004386)
    • (2002) Journal of Physiology , vol.545 , Issue.2 , pp. 521-535
    • Simkus, C.R.L.1    Stricker, C.2
  • 5
    • 7444229746 scopus 로고    scopus 로고
    • Calcium release from presynaptic ryanodine-sensitive stores is required for long-term depression at hippocampal CA3-CA3 pyramidal neuron synapses
    • DOI 10.1523/JNEUROSCI.5583-03.2004
    • Unni, V. K.; Zakharenko, S. S.; Zablow, L.; DeCostanzo, A. J.; Siegelbaum, S. A. Calcium release from presynaptic ryanodine-sensitive stores is required for long-term depression at hippocampal CA3-CA3 pyramidal neuron synapses. J. Neurosci. 2004, 24, 9612-9622. (Pubitemid 39441515)
    • (2004) Journal of Neuroscience , vol.24 , Issue.43 , pp. 9612-9622
    • Unni, V.K.1    Zakharenko, S.S.2    Zablow, L.3    DeCostanzo, A.J.4    Siegelbaum, S.A.5
  • 8
    • 22544446151 scopus 로고    scopus 로고
    • Presynaptic ryanodine receptors are required for normal quantal size at the Caenorhabditis elegans neuromuscular junction
    • DOI 10.1523/JNEUROSCI.1730-05.2005
    • Liu, Q.; Chen, B.; Yankova, M.; Morest, D. K.; Maryon, E.; Hand, A. R.; Nonet, M. L.; Wang, Z. W. Presynaptic ryanodine receptors are required for normal quantal size at the Caenorhabditis elegans neuromuscular junction. J. Neurosci. 2005, 25, 6745-6754. (Pubitemid 41023142)
    • (2005) Journal of Neuroscience , vol.25 , Issue.29 , pp. 6745-6754
    • Liu, Q.1    Chen, B.2    Yankova, M.3    Morest, D.K.4    Maryon, E.5    Hand, A.R.6    Nonet, M.L.7    Wang, Z.-W.8
  • 9
    • 32544438897 scopus 로고    scopus 로고
    • Synaptic transmission mediated by internal calcium stores in rod photoreceptors
    • DOI 10.1523/JNEUROSCI.3895-05.2006
    • Suryanarayanan, A.; Slaughter, M. M. Synaptic transmission mediated by internal calcium stores in rod photoreceptors. J. Neurosci. 2006, 26, 1759-1766. (Pubitemid 43236988)
    • (2006) Journal of Neuroscience , vol.26 , Issue.6 , pp. 1759-1766
    • Suryanarayanan, A.1    Slaughter, M.M.2
  • 10
    • 45649084538 scopus 로고    scopus 로고
    • Calcium release via activation of presynaptic IP3 receptors contributes to kainate-induced IPSC facilitation in rat neocortex
    • Mathew, S. S.; Hablitz, J. J. Calcium release via activation of presynaptic IP3 receptors contributes to kainate-induced IPSC facilitation in rat neocortex. Neuropharmacology 2008, 55, 106-116.
    • (2008) Neuropharmacology , vol.55 , pp. 106-116
    • Mathew, S.S.1    Hablitz, J.J.2
  • 11
    • 0033059445 scopus 로고    scopus 로고
    • Alterations in the ryanodine receptor calcium release channel correlate with Alzheimer's disease neurofibrillary and β-amyloid pathologies
    • DOI 10.1016/S0306-4522(99)00042-1, PII S0306452299000421
    • Kelliher, M.; Fastbom, J.; Cowburn, R. F.; Bonkale, W.; Ohm, T. G.; Ravid, R.; Sorrentino, V.; O'Neill, C. Alterations in the ryanodine receptor calcium release channel correlate with Alzheimer's disease neurofibrillary and beta-amyloid pathologies. Neuroscience 1999, 92, 499-513. (Pubitemid 29268039)
    • (1999) Neuroscience , vol.92 , Issue.2 , pp. 499-513
    • Kelliher, M.1    Fastbom, J.2    Cowburn, R.F.3    Bonkale, W.4    Ohm, T.G.5    Ravid, R.6    Sorrentino, V.7    O'Neill, C.8
  • 12
    • 4444302167 scopus 로고    scopus 로고
    • Deranged neuronal calcium signaling and Huntington disease
    • DOI 10.1016/j.bbrc.2004.08.035, PII S0006291X04017735
    • Bezprozvanny, I.; Hayden, M. R. Deranged neuronal calcium signaling and Huntington disease. Biochem. Biophys. Res. Commun. 2004, 322, 1310-1317. (Pubitemid 39164659)
    • (2004) Biochemical and Biophysical Research Communications , vol.322 , Issue.4 , pp. 1310-1317
    • Bezprozvanny, I.1    Hayden, M.R.2
  • 16
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • DOI 10.1016/j.nbd.2006.05.011, PII S0969996106001331
    • Ferreiro, E.; Resende, R.; Costa, R.; Oliveira, C. R.; Pereira, C. M. An endoplasmic-reticulumspecific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol. Dis. 2006, 23, 669-678. (Pubitemid 44234104)
    • (2006) Neurobiology of Disease , vol.23 , Issue.3 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.R.4    Pereira, C.M.F.5
  • 18
    • 33846018429 scopus 로고    scopus 로고
    • Amyloid-β-(1- 42) increases ryanodine receptor-3 expression and function in neurons of TgCRND8 mice
    • DOI 10.1074/jbc.M606736200
    • Supnet, C.; Grant, J.; Kong, H.; Westaway, D.; Mayne, M. Amyloid-beta-(1-42) increases ryanodine receptor-3 expression and function in neurons of TgCRND8 mice. J. Biol. Chem. 2006, 281, 38440-38447. (Pubitemid 46041967)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38440-38447
    • Supnet, C.1    Grant, J.2    Kong, H.3    Westaway, D.4    Mayne, M.5
  • 19
    • 0023521088 scopus 로고
    • Reduced phosphoinositide concentrations in anterior temporal cortex of Alzheimer-diseased brains
    • Stokes, C. E.; Hawthorne, J. N. Reduced phosphoinositide concentrations in anterior temporal cortex of Alzheimer-diseased brains. J. Neurochem. 1987, 48, 1018-1021.
    • (1987) J. Neurochem. , vol.48 , pp. 1018-1021
    • Stokes, C.E.1    Hawthorne, J.N.2
  • 20
    • 0023823738 scopus 로고
    • Decreased brain [3H]inositol 1,4,5-trisphosphate binding in Alzheimer's disease
    • Young, L. T.; Kish, S. J.; Li, P. P.; Warsh, J. J. Decreased brain [3H]inositol 1,4,5-trisphosphate binding in Alzheimer's disease. Neurosci. Lett. 1988, 94, 198-202.
    • (1988) Neurosci. Lett. , vol.94 , pp. 198-202
    • Young, L.T.1    Kish, S.J.2    Li, P.P.3    Warsh, J.J.4
  • 21
    • 0027132379 scopus 로고
    • Diminished muscarinic receptor-stimulated [3H]-PIP2 hydrolysis in Alzheimer's disease
    • Ferrari-DiLeo, G.; Flynn, D. D. Diminished muscarinic receptor-stimulated [3H]-PIP2 hydrolysis in Alzheimer's disease. Life Sci. 1993, 53, 439-444. (Pubitemid 2019042)
    • (1993) Life Sciences , vol.53 , Issue.25 , pp. 439-444
    • Ferrari-DiLeo, G.1    Flynn, D.D.2
  • 22
    • 0028027552 scopus 로고
    • Cholinergic and serotonergic stimulation of phosphoinostide hydrolysis is decreased in Alzheimer's disease
    • DOI 10.1016/0024-3205(94)00379-3
    • Crews, F. T.; Kurian, P.; Freund, G. Cholinergic and serotonergic stimulation of phosphoinositide hydrolysis is decreased in Alzheimer's disease. Life Sci 1994, 55, 1993-2002. (Pubitemid 24372588)
    • (1994) Life Sciences , vol.55 , Issue.25-26 , pp. 1993-2002
    • Crews, F.T.1    Kurian, P.2    Freund, G.3
  • 23
    • 0028978364 scopus 로고
    • Diminished [3H]inositol (1, 4, 5) P3 but not [3H]inositol (1, 3, 4, 5) P4 binding in Alzheimer's disease brain
    • Garlind, A.; Cowburn, R. F.; Forsell, C.; Ravid, R.; Winblad, B.; Fowler, C. J. Diminished [3H]inositol (1, 4, 5) P3 but not [3H]inositol (1, 3, 4, 5) P4 binding in Alzheimer's disease brain. Brain Res. 1995, 681, 160-166.
    • (1995) Brain Res. , vol.681 , pp. 160-166
    • Garlind, A.1    Cowburn, R.F.2    Forsell, C.3    Ravid, R.4    Winblad, B.5    Fowler, C.J.6
  • 24
    • 0032526841 scopus 로고    scopus 로고
    • Loss of inositol 1,4,5-trisphosphate receptor sites and decreased PKC levels correlate with staging of Alzheimer's disease neurofibrillary pathology
    • DOI 10.1016/S0006-8993(98)00347-3, PII S0006899398003473
    • Kurumatani, T.; Fastbom, J.; Bonkale, W. L.; Bogdanovic, N.; Winblad, B.; Ohm, T. G.; Cowburn, R. F. Loss of inositol 1,4,5-trisphosphate receptor sites and decreased PKC levels correlate with staging of Alzheimer's disease neurofibrillary pathology. Brain Res. 1998, 796, 209-221. (Pubitemid 28343250)
    • (1998) Brain Research , vol.796 , Issue.1-2 , pp. 209-211
    • Kurumatani, T.1    Fastbom, J.2    Bonkale, W.L.3    Bogdanovic, N.4    Winblad, B.5    Ohm, T.G.6    Cowburn, R.F.7
  • 25
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny, I.; Mattson, M. P. Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci. 2008, 31, 454-463.
    • (2008) Trends Neurosci. , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 26
    • 0034674730 scopus 로고    scopus 로고
    • Presenilin-1 mutations increase levels of ryanodine receptors and calcium release in PC12 cells and cortical neurons
    • DOI 10.1074/jbc.M000040200
    • Chan, S. L.; Mayne, M.; Holden, C. P.; Geiger, J. D.; Mattson, M. P. Presenilin-1 mutations increase levels of ryanodine receptors and calcium release in PC12 cells and cortical neurons. J. Biol. Chem. 2000, 275, 18195-18200. (Pubitemid 30414771)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18195-18200
    • Chan, S.L.1    Mayne, M.2    Holden, C.P.3    Geiger, J.D.4    Mattson, M.P.5
  • 27
    • 35748954015 scopus 로고    scopus 로고
    • The cytosolic N-terminus of presenilin-1 potentiates mouse ryanodine receptor single channel activity
    • DOI 10.1016/j.biocel.2007.06.023, PII S135727250700218X
    • Rybalchenko, V.; Hwang, S. Y.; Rybalchenko, N.; Koulen, P. The cytosolic N-terminus of presenilin-1 potentiates mouse ryanodine receptor single channel activity. Int. J. Biochem. Cell Biol. 2008, 40, 84-97. (Pubitemid 350052661)
    • (2008) International Journal of Biochemistry and Cell Biology , vol.40 , Issue.1 , pp. 84-97
    • Rybalchenko, V.1    Hwang, S.-Y.2    Rybalchenko, N.3    Koulen, P.4
  • 28
    • 53549084850 scopus 로고    scopus 로고
    • The N-terminus of presenilin-2 increases single channel activity of brain ryanodine receptors through direct protein-protein interaction
    • Hayrapetyan, V.; Rybalchenko, V.; Rybalchenko, N.; Koulen, P. The N-terminus of presenilin-2 increases single channel activity of brain ryanodine receptors through direct protein-protein interaction. Cell Calcium 2008, 44, 507-518.
    • (2008) Cell. Calcium. , vol.44 , pp. 507-518
    • Hayrapetyan, V.1    Rybalchenko, V.2    Rybalchenko, N.3    Koulen, P.4
  • 29
    • 34247621471 scopus 로고    scopus 로고
    • Enhanced ryanodine-mediated calcium release in mutant PS1-expressing Alzheimer's mouse models
    • DOI 10.1196/annals.1379.025, Imaging and the Aging Brain
    • Stutzmann, G. E.; Smith, I.; Caccamo, A.; Oddo, S.; Parker, I.; Laferla, F. Enhanced ryanodinemediated calcium release in mutant PS1-expressing Alzheimer's mouse models. Ann. NY Acad. Sci. 2007, 1097, 265-277. (Pubitemid 47084900)
    • (2007) Annals of the New York Academy of Sciences , vol.1097 , pp. 265-277
    • Stutzmann, G.E.1    Smith, I.2    Caccamo, A.3    Oddo, S.4    Parker, I.5    Laferla, F.6
  • 30
    • 30744470170 scopus 로고    scopus 로고
    • PS2 mutation increases neuronal cell vulnerability to neurotoxicants through activation of caspase-3 by enhancing of ryanodine receptor-mediated calcium release
    • Lee, S. Y.; Hwang, D. Y.; Kim, Y. K.; Lee, J. W.; Shin, I. C.; Oh, K. W.; Lee, M. K.; Lim, J. S.; Yoon, D. Y.; Hwang, S. J.; Hong, J. T. PS2 mutation increases neuronal cell vulnerability to neurotoxicants through activation of caspase-3 by enhancing of ryanodine receptor-mediated calcium release. FASEB J. 2006, 20, 151-153.
    • (2006) FASEB J. , vol.20 , pp. 151-153
    • Lee, S.Y.1    Hwang, D.Y.2    Kim, Y.K.3    Lee, J.W.4    Shin, I.C.5    Oh, K.W.6    Lee, M.K.7    Lim, J.S.8    Yoon, D.Y.9    Hwang, S.J.10    Hong, J.T.11
  • 31
    • 0032704888 scopus 로고    scopus 로고
    • Presenilin-2 mutations modulate amplitude and kinetics of inositol 1,4,5-trisphosphate-mediated calcium signals
    • Leissring, M. A.; Parker, I.; LaFerla, F. M. Presenilin-2 mutations modulate amplitude and kinetics of inositol 1,4,5-trisphosphate-mediated calcium signals. J. Biol. Chem. 1999, 274, 32535-32538. (Pubitemid 129535275)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.46 , pp. 32535-32538
    • Leissring, M.A.1    Parker, I.2    LaFerla, F.M.3
  • 33
    • 5444231258 scopus 로고    scopus 로고
    • Huntingtin processing in pathogenesis of Huntington disease
    • Qin, Z. H.; Gu, Z. L. Huntingtin processing in pathogenesis of Huntington disease. Acta Pharmacol. Sin. 2004, 25, 1243-1249. (Pubitemid 39361794)
    • (2004) Acta Pharmacologica Sinica , vol.25 , Issue.10 , pp. 1243-1249
    • Qin, Z.-H.1    Gu, Z.-L.2
  • 34
    • 58849103904 scopus 로고    scopus 로고
    • Targeting oxidative stress for neuroprotection
    • Linseman, D. A. Targeting oxidative stress for neuroprotection. Antioxid. Redox. Signal 2009, 11, 421-424.
    • (2009) Antioxid. Redox. Signal , vol.11 , pp. 421-424
    • Linseman, D.A.1
  • 36
    • 0041963057 scopus 로고    scopus 로고
    • Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1
    • DOI 10.1016/S0896-6273(03)00366-0
    • Tang, T. S.; Tu, H.; Chan, E. Y.; Maximov, A.; Wang, Z.; Wellington, C. L.; Hayden, M. R.; Bezprozvanny, I. Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1, 4, 5) triphosphate receptor type 1. Neuron 2003, 39, 227-239. (Pubitemid 36897546)
    • (2003) Neuron , vol.39 , Issue.2 , pp. 227-239
    • Tang, T.-S.1    Tu, H.2    Chan, E.Y.W.3    Maximov, A.4    Wang, Z.5    Wellington, C.L.6    Hayden, M.R.7    Bezprozvanny, I.8
  • 37
    • 59649118434 scopus 로고    scopus 로고
    • Neuroprotective effects of inositol 1,4,5-trisphosphate receptor C-terminal fragment in a Huntington's disease mouse model
    • Tang, T. S.; Guo, C.; Wang, H.; Chen, X.; Bezprozvanny, I. Neuroprotective effects of inositol 1,4,5-trisphosphate receptor C-terminal fragment in a Huntington's disease mouse model. J. Neurosci. 2009, 29, 1257-1266.
    • (2009) J. Neurosci. , vol.29 , pp. 1257-1266
    • Tang, T.S.1    Guo, C.2    Wang, H.3    Chen, X.4    Bezprozvanny, I.5
  • 39
    • 65649103331 scopus 로고    scopus 로고
    • Pathophysiology of neurodegeneration in familial amyotrophic lateral sclerosis
    • Vucic, S.; Kiernan, M. C. Pathophysiology of neurodegeneration in familial amyotrophic lateral sclerosis. Curr. Mol. Med. 2009, 9, 255-272.
    • (2009) Curr. Mol. Med. , vol.9 , pp. 255-272
    • Vucic, S.1    Kiernan, M.C.2
  • 40
    • 33644829010 scopus 로고    scopus 로고
    • Calcium signaling pathways mediating synaptic potentiation triggered by amyotrophic lateral sclerosis IgG in motor nerve terminals
    • Pagani, M. R.; Reisin, R. C.; Uchitel, O. D. Calcium signaling pathways mediating synaptic potentiation triggered by amyotrophic lateral sclerosis IgG in motor nerve terminals. J. Neurosci. 2006, 26, 2661-2672.
    • (2006) J. Neurosci. , vol.26 , pp. 2661-2672
    • Pagani, M.R.1    Reisin, R.C.2    Uchitel, O.D.3
  • 42
    • 4544386279 scopus 로고    scopus 로고
    • Neuroprotection against ischemic/hypoxic brain damage: Blockers of ionotropic glutamate receptor and voltage sensitive calcium channels
    • DOI 10.2174/1389450043345209
    • Schurr, A. Neuroprotection against ischemic/hypoxic brain damage: Blockers of ionotropic glutamate receptor and voltage sensitive calcium channels. Curr. Drug Targets 2004, 5, 603-618. (Pubitemid 39242869)
    • (2004) Current Drug Targets , vol.5 , Issue.7 , pp. 603-618
    • Schurr, A.1
  • 43
    • 38849139200 scopus 로고    scopus 로고
    • Calcium channelopathies: Voltage-gated calcium channels
    • Adams, P. J.; Snutch, T. P. Calcium channelopathies: Voltage-gated calcium channels. Subcell Biochem. 2007, 45, 215-251.
    • (2007) Subcell Biochem. , vol.45 , pp. 215-251
    • Adams, P.J.1    Snutch, T.P.2
  • 44
    • 0029810979 scopus 로고    scopus 로고
    • Functional coupling between ryanodine receptors and L-type calcium channels in neurons
    • DOI 10.1038/382719a0
    • Chavis, P.; Fagni, L.; Lansman, J. B.; Bockaert, J. Functional coupling between ryanodine receptors and L-type calcium channels in neurons. Nature 1996, 382, 719-722. (Pubitemid 26282178)
    • (1996) Nature , vol.382 , Issue.6593 , pp. 719-722
    • Chavis, P.1    Fagni, L.2    Lansman, J.B.3    Bockaert, J.4
  • 45
    • 0035868325 scopus 로고    scopus 로고
    • Molecular interaction of dihydropyridine receptors with type-1 ryanodine receptors in rat brain
    • DOI 10.1042/0264-6021:3540597
    • Mouton, J.; Marty, I.; Villaz, M.; Feltz, A.; Maulet, Y. Molecular interaction of dihydropyridine receptors with type-1 ryanodine receptors in rat brain. Biochem. J. 2001, 354, 597-603. (Pubitemid 32269723)
    • (2001) Biochemical Journal , vol.354 , Issue.3 , pp. 597-603
    • Mouton, J.1    Marty, I.2    Villaz, M.3    Feltz, A.4    Maulet, Y.5
  • 46
    • 0030497661 scopus 로고    scopus 로고
    • Apparent independent action of nimodipine and glutamate antagonists to protect cultured neurons against glutamate-induced damage
    • DOI 10.1016/S0028-3908(96)00104-9, PII S0028390896001049
    • Krieglstein, J.; Lippert, K.; Poch, G. Apparent independent action of nimodipine and glutamate antagonists to protect cultured neurons against glutamate-induced damage. Neuropharmacology 1996, 35, 1737-1742. (Pubitemid 27090792)
    • (1996) Neuropharmacology , vol.35 , Issue.12 , pp. 1737-1742
    • Krieglstein, J.1    Lippert, K.2    Poch, G.3
  • 47
    • 0031564645 scopus 로고    scopus 로고
    • Identification of calcium channels involved in neuronal injury in rat hippocampal slices subjected to oxygen and glucose deprivation
    • DOI 10.1016/S0006-8993(96)01385-6, PII S0006899396013856
    • Small, D. L.; Monette, R.; Buchan, A. M.; Morley, P. Identification of calcium channels involved in neuronal injury in rat hippocampal slices subjected to oxygen and glucose deprivation. Brain Res. 1997, 753, 209-218. (Pubitemid 27151865)
    • (1997) Brain Research , vol.753 , Issue.2 , pp. 209-218
    • Small, D.L.1    Monette, R.2    Buchan, A.M.3    Morley, P.4
  • 48
    • 0024579338 scopus 로고
    • Improvement of cortical perfusion, intracellular pH, and electrocorticography by nimodipine during transient focal cerebral ischemia
    • Tally, P. W.; Sundt, T. M.; Anderson, R. E. Improvement of cortical perfusion, intracellular pH, and electrocorticography by nimodipine during transient focal cerebral ischemia. Neurosurgery 1989, 24, 80-87.
    • (1989) Neurosurgery , vol.24 , pp. 80-87
    • Tally, P.W.1    Sundt, T.M.2    Anderson, R.E.3
  • 49
    • 0025663403 scopus 로고
    • Diverse mechanisms of neuronal protection by nimodipine in experimental rabbit brain ischemia
    • Lazarewicz, J. W.; Pluta, R.; Puka, M.; Salinska, E. Diverse mechanisms of neuronal protection by nimodipine in experimental rabbit brain ischemia. Stroke 1990, 21, IV108-110.
    • (1990) Stroke , vol.21
    • Lazarewicz, J.W.1    Pluta, R.2    Puka, M.3    Salinska, E.4
  • 50
    • 0025793975 scopus 로고
    • The effect of a dihydropyridine calcium antagonist (isradipine) on selective neuronal necrosis
    • Ohta, S.; Smith, M. L.; Siesjo, B. K. The effect of a dihydropyridine calcium antagonist (isradipine) on selective neuronal necrosis. J. Neurol. Sci. 1991, 103, 109-115.
    • (1991) J. Neurol. Sci. , vol.103 , pp. 109-115
    • Ohta, S.1    Smith, M.L.2    Siesjo, B.K.3
  • 52
    • 0031266451 scopus 로고    scopus 로고
    • Effects of Isradipine, an L-Type Calcium Channel Blocker on Permanent and Transient Focal Cerebral Ischemia in Spontaneously Hypertensive Rats
    • Campbell, C. A.; Mackay, K. B.; Patel, S.; King, P. D.; Stretton, J. L.; Hadingham, S. J.; Hamilton, T. C. Effects of isradipine, an L-type calcium channel blocker on permanent and transient focal cerebral ischemia in spontaneously hypertensive rats. Exp. Neurol. 1997, 148, 45-50. (Pubitemid 127445113)
    • (1997) Experimental Neurology , vol.148 , Issue.1 , pp. 45-50
    • Campbell, C.A.1    Mackay, K.B.2    Patel, S.3    King, P.D.4    Stretton, J.L.5    Hadingham, S.J.6    Hamilton, T.C.7
  • 53
    • 0030700570 scopus 로고    scopus 로고
    • Attenuation of brain injury and reduction of neuron-specific enolase by nicardipine in systemic circulation following focal ischemia and reperfusion in a rat model
    • Kittaka, M.; Giannotta, S. L.; Zelman, V.; Correale, J. D.; DeGiorgio, C. M.; Weiss, M. H.; Zlokovic, B. V. Attenuation of brain injury and reduction of neuron-specific enolase by nicardipine in systemic circulation following focal ischemia and reperfusion in a rat model. J. Neurosurg. 1997, 87, 731-737. (Pubitemid 27454592)
    • (1997) Journal of Neurosurgery , vol.87 , Issue.5 , pp. 731-737
    • Kittaka, M.1    Giannotta, S.L.2    Zelman, V.3    Correale, J.D.4    DeGiorgio, C.M.5    Weiss, M.H.6    Zlokovic, B.V.7
  • 54
    • 0030784933 scopus 로고    scopus 로고
    • Neuroprotection by the novel calcium antagonist PCA50938, nimodipine and flunarizine, in gerbil global brain ischemia
    • DOI 10.1016/S0006-8993(97)00838-X, PII S000689939700838X
    • Zapater, P.; Moreno, J.; Horga, J. F. Neuroprotection by the novel calcium antagonist PCA50938, nimodipine and flunarizine, in gerbil global brain ischemia. Brain Res. 1997, 772, 57-62. (Pubitemid 27501683)
    • (1997) Brain Research , vol.772 , Issue.1-2 , pp. 57-62
    • Zapater, P.1    Moreno, J.2    Horga, J.F.3
  • 55
    • 0032966764 scopus 로고    scopus 로고
    • Use of diffusion-weighted MRI and neurological deficit scores to demonstrate beneficial effects of isradipine in a rat model of focal ischemia
    • DOI 10.1159/000028294
    • Chandra, S.; White, R. F.; Everding, D.; Feuerstein, G. Z.; Coatney, R. W.; Sarkar, S. K.; Barone, F. C. Use of diffusion-weighted MRI and neurological deficit scores to demonstrate beneficial effects of isradipine in a rat model of focal ischemia. Pharmacology 1999, 58, 292-299. (Pubitemid 29206184)
    • (1999) Pharmacology , vol.58 , Issue.6 , pp. 292-299
    • Chandra, S.1    White, R.F.2    Everding, D.3    Feuerstein, G.Z.4    Coatney, R.W.5    Sarkar, S.K.6    Barone, F.C.7
  • 56
    • 0034792905 scopus 로고    scopus 로고
    • Nimodipine in animal model experiments of focal cerebral ischemia: A systematic review
    • Horn, J.; de Haan, R. J.; Vermeulen, M.; Luiten, P. G.; Limburg, M. Nimodipine in animal model experiments of focal cerebral ischemia: A systematic review. Stroke 2001, 32, 2433-2438. (Pubitemid 32954819)
    • (2001) Stroke , vol.32 , Issue.10 , pp. 2433-2438
    • Horn, J.1    De Haan, R.J.2    Vermeulen, M.3    Luiten, P.G.M.4    Limburg, M.5
  • 57
    • 2542424800 scopus 로고    scopus 로고
    • Treatment with nicardipine protects brain in an animal model of hypertension-induced damage
    • DOI 10.1081/CEH-120034139
    • Amenta, F.; Tomassoni, D. Treatment with Nicardipine Protects Brain in an Animal Model of Hypertension-Induced Damage. Clin. Exp. Hypertens. 2004, 26, 351-361. (Pubitemid 38691116)
    • (2004) Clinical and Experimental Hypertension , vol.26 , Issue.4 , pp. 351-361
    • Amenta, F.1    Tomassoni, D.2
  • 59
    • 48849089052 scopus 로고    scopus 로고
    • Neuroprotection for ischemic stroke: Past, present and future
    • Ginsberg, M. D. Neuroprotection for ischemic stroke: Past, present and future. Neuropharmacology 2008, 55, 363-389.
    • (2008) Neuropharmacology , vol.55 , pp. 363-389
    • Ginsberg, M.D.1
  • 60
    • 0242694942 scopus 로고    scopus 로고
    • Neuroprotection by nicotine in mouse primary cortical cultures involves activation of calcineurin and L-type calcium channel inactivation
    • Stevens, T. R.; Krueger, S. R.; Fitzsimonds, R. M.; Picciotto, M. R. Neuroprotection by nicotine in mouse primary cortical cultures involves activation of calcineurin and L-type calcium channel inactivation. J. Neurosci. 2003, 23, 10093-10099.
    • (2003) J. Neurosci. , vol.23 , pp. 10093-10099
    • Stevens, T.R.1    Krueger, S.R.2    Fitzsimonds, R.M.3    Picciotto, M.R.4
  • 61
    • 0035144882 scopus 로고    scopus 로고
    • Vitamin D hormone confers neuroprotection in parallel with downregulation of L-type calcium channel expression in hippocampal neurons
    • Brewer, L. D.; Thibault, V.; Chen, K. C.; Langub, M. C.; Landfield, P. W.; Porter, N. M. Vitamin D hormone confers neuroprotection in parallel with downregulation of L-type calcium channel expression in hippocampal neurons. J. Neurosci. 2001, 21, 98-108. (Pubitemid 32098731)
    • (2001) Journal of Neuroscience , vol.21 , Issue.1 , pp. 98-108
    • Brewer, L.D.1    Thibault, V.2    Chen, K.-C.3    Langub, M.C.4    Landfield, P.W.5    Porter, N.M.6
  • 65
    • 0042536473 scopus 로고    scopus 로고
    • Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity
    • DOI 10.1016/S0143-4160(03)00141-6
    • Arundine, M.; Tymianski, M. Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity. Cell Calcium 2003, 34, 325-337. (Pubitemid 37021228)
    • (2003) Cell Calcium , vol.34 , Issue.4-5 , pp. 325-337
    • Arundine, M.1    Tymianski, M.2
  • 66
    • 13544268511 scopus 로고    scopus 로고
    • N-methyl-D-aspartate receptor subtypes: Multiple roles in excitotoxicity and neurological disease
    • Waxman, E. A.; Lynch, D. R. N-methyl-D-aspartate receptor subtypes: Multiple roles in excitotoxicity and neurological disease. Neuroscientist 2005, 11, 37-49.
    • (2005) Neuroscientist , vol.11 , pp. 37-49
    • Waxman, E.A.1    Lynch, D.R.2
  • 67
    • 34249085665 scopus 로고    scopus 로고
    • NMDA and AMPA receptors: old channels, new tricks
    • DOI 10.1016/j.tins.2007.03.012, PII S016622360700077X
    • Rao, V. R.; Finkbeiner, S. NMDA and AMPA receptors: Old channels, new tricks. Trends Neurosci. 2007, 30, 284-291. (Pubitemid 46802833)
    • (2007) Trends in Neurosciences , vol.30 , Issue.6 , pp. 284-291
    • Rao, V.R.1    Finkbeiner, S.2
  • 68
    • 0028327506 scopus 로고
    • Stimulation of NMDA receptors activates calpain in cultured hippocampal slices
    • DOI 10.1016/0304-3940(94)91049-9
    • del Cerro, S.; Arai, A.; Kessler, M.; Bahr, B. A.; Vanderklish, P.; Rivera, S.; Lynch, G. Stimulation of NMDA receptors activates calpain in cultured hippocampal slices. Neurosci. Lett. 1994, 167, 149-152. (Pubitemid 24077661)
    • (1994) Neuroscience Letters , vol.167 , Issue.1-2 , pp. 149-152
    • Del Cerro, S.1    Arai, A.2    Kessler, M.3    Bahr, B.A.4    Vanderklish, P.5    Rivera, S.6    Lynch, G.7
  • 69
    • 48949120457 scopus 로고    scopus 로고
    • Glutamatergic calcium dynamics and deregulation of rat retinal ganglion cells
    • Hartwick, A. T.; Hamilton, C. M.; Baldridge, W. H. Glutamatergic calcium dynamics and deregulation of rat retinal ganglion cells. J. Physiol. 2008, 586, 3425-3446.
    • (2008) J. Physiol. , vol.586 , pp. 3425-3446
    • Hartwick, A.T.1    Hamilton, C.M.2    Baldridge, W.H.3
  • 70
    • 70349103713 scopus 로고    scopus 로고
    • Memantine: A review of its use in moderate to severe Alzheimer's disease
    • McKeage, K. Memantine: A review of its use in moderate to severe Alzheimer's disease. CNS Drugs 2009, 23, 881-897.
    • (2009) CNS Drugs , vol.23 , pp. 881-897
    • McKeage, K.1
  • 71
    • 77950350271 scopus 로고    scopus 로고
    • Memantine: A review of studies into its safety and efficacy in treating Alzheimer's disease and other dementias
    • Thomas, S. J.; Grossberg, G. T. Memantine: A review of studies into its safety and efficacy in treating Alzheimer's disease and other dementias. Clin. Interv. Aging. 2009, 4, 367-377.
    • (2009) Clin. Interv. Aging , vol.4 , pp. 367-377
    • Thomas, S.J.1    Grossberg, G.T.2
  • 72
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H. C.; Schenker, L. T.; Kennedy, M. B.; Seeburg, P. H. Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 1995, 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
  • 73
    • 0030200438 scopus 로고    scopus 로고
    • Heteromultimerization and NMDA receptor-clustering activity of Chapsyn- 110, a member of the PSD-95 family of proteins
    • DOI 10.1016/S0896-6273(00)80284-6
    • Kim, E.; Cho, K. O.; Rothschild, A.; Sheng, M. Heteromultimerization and NMDA receptorclustering activity of Chapsyn-110, a member of the PSD-95 family of proteins. Neuron 1996, 17, 103-113. (Pubitemid 26251595)
    • (1996) Neuron , vol.17 , Issue.1 , pp. 103-113
    • Kim, E.1    Cho, K.-O.2    Rothschild, A.3    Sheng, M.4
  • 74
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • Niethammer, M.; Kim, E.; Sheng, M. Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J. Neurosci. 1996, 16, 2157-2163. (Pubitemid 26154327)
    • (1996) Journal of Neuroscience , vol.16 , Issue.7 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 75
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors
    • DOI 10.1038/386279a0
    • Dong, H.; O'Brien, R. J.; Fung, E. T.; Lanahan, A. A.; Worley, P. F.; Huganir, R. L. GRIP: A synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 1997, 386, 279-284. (Pubitemid 27142513)
    • (1997) Nature , vol.386 , Issue.6622 , pp. 279-284
    • Dong, H.1    O'Brien, R.J.2    Fung, E.T.3    Lanahan, A.A.4    Worley, P.F.5    Huganir, R.L.6
  • 77
    • 0032907948 scopus 로고    scopus 로고
    • Clustering of AMPA receptors by the synaptic PD domain-containing protein PICK1
    • DOI 10.1016/S0896-6273(00)80689-3
    • Xia, J.; Zhang, X.; Staudinger, J.; Huganir, R. L. Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1. Neuron 1999, 22, 179-187. (Pubitemid 29070104)
    • (1999) Neuron , vol.22 , Issue.1 , pp. 179-187
    • Xia, J.1    Zhang, X.2    Staudinger, J.3    Huganir, R.L.4
  • 78
    • 0034523581 scopus 로고    scopus 로고
    • PDZ proteins interacting with C-terminal GluR2/3 are involved in a PKC-dependent regulation of AMPA receptors at hippocampal synapses
    • DOI 10.1016/S0896-6273(00)00160-4
    • Daw, M. I.; Chittajallu, R.; Bortolotto, Z. A.; Dev, K. K.; Duprat, F.; Henley, J. M.; Collingridge, G. L.; Isaac, J. T. PDZ proteins interacting with C-terminal GluR2/3 are involved in a PKCdependent regulation of AMPA receptors at hippocampal synapses. Neuron 2000, 28, 873-886. (Pubitemid 32038078)
    • (2000) Neuron , vol.28 , Issue.3 , pp. 873-886
    • Daw, M.I.1    Chittajallu, R.2    Bortolotto, Z.A.3    Dev, K.K.4    Duprat, F.5    Henley, J.M.6    Collingridge, G.L.7    Isaac, J.T.R.8
  • 79
    • 0035083006 scopus 로고    scopus 로고
    • Enrichment of N-methyl-D-aspartate NR1 splice variants and synaptic proteins in rat postsynaptic densities
    • Al-Hallaq, R. A.; Yasuda, R. P.; Wolfe, B. B. Enrichment of N-methyl-D-aspartate NR1 splice variants and synaptic proteins in rat postsynaptic densities. J. Neurochem. 2001, 77, 110-119.
    • (2001) J. Neurochem. , vol.77 , pp. 110-119
    • Al-Hallaq, R.A.1    Yasuda, R.P.2    Wolfe, B.B.3
  • 81
    • 0038794104 scopus 로고    scopus 로고
    • Synapse-associated protein-97 isoform-specific regulation of surface AMPA receptors and synaptic function in cultured neurons
    • Rumbaugh, G.; Sia, G. M.; Garner, C. C.; Huganir, R. L. Synapse-associated protein-97 isoformspecific regulation of surface AMPA receptors and synaptic function in cultured neurons. J. Neurosci. 2003, 23, 4567-4576. (Pubitemid 36706187)
    • (2003) Journal of Neuroscience , vol.23 , Issue.11 , pp. 4567-4576
    • Rumbaugh, G.1    Sia, G.-M.2    Garner, C.C.3    Huganir, R.L.4
  • 82
    • 15444362199 scopus 로고    scopus 로고
    • Calcium-permeable AMPA receptor plasticity is mediated by subunit-specific interactions with PICK1 and NSF
    • DOI 10.1016/j.neuron.2005.02.026
    • Gardner, S. M.; Takamiya, K.; Xia, J.; Suh, J. G.; Johnson, R.; Yu, S.; Huganir, R. L. Calciumpermeable AMPA receptor plasticity is mediated by subunit-specific interactions with PICK1 and NSF. Neuron 2005, 45, 903-915. (Pubitemid 40395268)
    • (2005) Neuron , vol.45 , Issue.6 , pp. 903-915
    • Gardner, S.M.1    Takamiya, K.2    Xia, J.3    Suh, J.-G.4    Johnson, R.5    Yu, S.6    Huganir, R.L.7
  • 83
    • 25144522326 scopus 로고    scopus 로고
    • PICK1 is a calcium-sensor for NMDA-induced AMPA receptor trafficking
    • DOI 10.1038/sj.emboj.7600801, PII 7600801
    • Hanley, J. G.; Henley, J. M. PICK1 is a calcium-sensor for NMDA-induced AMPA receptor trafficking. EMBO J. 2005, 24, 3266-3278. (Pubitemid 41348701)
    • (2005) EMBO Journal , vol.24 , Issue.18 , pp. 3266-3278
    • Hanley, J.G.1    Henley, J.M.2
  • 84
    • 22844449702 scopus 로고    scopus 로고
    • 2+ permeability of AMPARs at cerebellar synapses
    • 2+ permeability of AMPARs at cerebellar synapses. Nat. Neurosci. 2005, 8, 768-775.
    • (2005) Nat. Neurosci. , vol.8 , pp. 768-775
    • Liu, S.J.1    Cull-Candy, S.G.2
  • 86
    • 0027232729 scopus 로고
    • Kainate elicits elevated nuclear calcium signals in retinal neurons via calcium-induced calcium release
    • Kocsis, J. D.; Rand, M. N.; Chen, B.; Waxman, S. G.; Pourcho, R. Kainate elicits elevated nuclear calcium signals in retinal neurons via calcium-induced calcium release. Brain Res. 1993, 616, 273-282. (Pubitemid 23200056)
    • (1993) Brain Research , vol.616 , Issue.1-2 , pp. 273-282
    • Kocsis, J.D.1    Rand, M.N.2    Chen, B.3    Waxman, S.G.4    Pourcho, R.5
  • 87
    • 0031905889 scopus 로고    scopus 로고
    • N-methyl-D-aspartate receptor-mediated, calcium-induced calcium release in rat dentate gyrus/CA4 in vivo
    • DOI 10.1002/(SICI)1097-4547(19980101)51:1<76::AID-JNR8>3.0.CO;2-I
    • Lazarewicz, J. W.; Rybkowski, W.; Sadowski, M.; Ziembowicz, A.; Alaraj, M.; Wegiel, J.; Wisniewski, H. M. N-methyl-D-aspartate receptor-mediated, calcium-induced calcium release in rat dentate gyrus/CA4 in vivo. J. Neurosci. Res. 1998, 51, 76-84. (Pubitemid 28063150)
    • (1998) Journal of Neuroscience Research , vol.51 , Issue.1 , pp. 76-84
    • Lazarewicz, J.W.1    Rybkowski, W.2    Sadowski, M.3    Ziembowicz, A.4    Alaraj, M.5    Wegiel, J.6    Wisniewski, H.M.7
  • 88
    • 0032930964 scopus 로고    scopus 로고
    • Single synaptic events evoke NMDA receptor-mediated release of calcium from internal stores in hippocampal dendritic spines
    • DOI 10.1016/S0896-6273(00)80683-2
    • Emptage, N.; Bliss, T. V.; Fine, A. Single synaptic events evoke NMDA receptor-mediated release of calcium from internal stores in hippocampal dendritic spines. Neuron 1999, 22, 115-124. (Pubitemid 29070098)
    • (1999) Neuron , vol.22 , Issue.1 , pp. 115-124
    • Emptage, N.1    Bliss, T.V.P.2    Fine, A.3
  • 89
    • 0037198591 scopus 로고    scopus 로고
    • Age-dependent occurrence of synchronized population oscillation suggestive of a developing functional coupling between NMDA and ryanodine receptors in the neocortex
    • DOI 10.1016/S0165-3806(02)00352-8, PII S0165380602003528
    • Yoshimura, H.; Sugai, T.; Onoda, N.; Segami, N.; Kato, N. Age-dependent occurrence of synchronized population oscillation suggestive of a developing functional coupling between NMDA and ryanodine receptors in the neocortex. Brain Res. Dev. Brain. Res. 2002, 136, 63-68. (Pubitemid 34556985)
    • (2002) Developmental Brain Research , vol.136 , Issue.1 , pp. 63-68
    • Yoshimura, H.1    Sugai, T.2    Onoda, N.3    Segami, N.4    Kato, N.5
  • 90
    • 10344242039 scopus 로고    scopus 로고
    • Lateral diffusion of inositol 1,4,5-trisphosphate receptor type 1 is regulated by actin filaments and 4.1N in neuronal dendrites
    • DOI 10.1074/jbc.M408364200
    • Fukatsu, K.; Bannai, H.; Zhang, S.; Nakamura, H.; Inoue, T.; Mikoshiba, K. Lateral diffusion of inositol 1,4,5-trisphosphate receptor type 1 is regulated by actin filaments and 4.1N in neuronal dendrites. J. Biol. Chem. 2004, 279, 48976-48982. (Pubitemid 39625779)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 48976-48982
    • Fukatsu, K.1    Bannai, H.2    Zhang, S.3    Nakamura, H.4    Inoue, T.5    Mikoshiba, K.6
  • 91
    • 0036678723 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium release is modulated by actin polymerization
    • Wang, Y.; Mattson, M. P.; Furukawa, K. Endoplasmic reticulum calcium release is modulated by actin polymerization. J. Neurochem. 2002, 82, 945-952.
    • (2002) J. Neurochem. , vol.82 , pp. 945-952
    • Wang, Y.1    Mattson, M.P.2    Furukawa, K.3
  • 93
    • 58149518066 scopus 로고    scopus 로고
    • The actin cytoskeleton differentially regulates NG115-401L cell ryanodine receptor and inositol 1,4,5-trisphosphate receptor induced calcium signaling pathways
    • Bose, D. D.; Thomas, D. W. The actin cytoskeleton differentially regulates NG115-401L cell ryanodine receptor and inositol 1,4,5-trisphosphate receptor induced calcium signaling pathways. Biochem. Biophys. Res. Commun. 2009, 379, 594-599.
    • (2009) Biochem. Biophys. Res. Commun. , vol.379 , pp. 594-599
    • Bose, D.D.1    Thomas, D.W.2
  • 94
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • Allison, D. W.; Gelfand, V. I.; Spector, I.; Craig, A. M. Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors. J. Neurosci. 1998, 18, 2423-2436.
    • (1998) J. Neurosci. , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 95
    • 0035503064 scopus 로고    scopus 로고
    • Regulation of NMDA receptor activity by F-actin and myosin light chain kinase
    • Lei, S.; Czerwinska, E.; Czerwinski, W.; Walsh, M. P.; MacDonald, J. F. Regulation of NMDA receptor activity by F-actin and myosin light chain kinase. J. Neurosci. 2001, 21, 8464-8472.
    • (2001) J. Neurosci. , vol.21 , pp. 8464-8472
    • Lei, S.1    Czerwinska, E.2    Czerwinski, W.3    Walsh, M.P.4    MacDonald, J.F.5
  • 96
    • 0034004473 scopus 로고    scopus 로고
    • Distinct roles of synaptic and extrasynaptic NMDA receptors in excitotoxicity
    • Sattler, R.; Xiong, Z.; Lu, W. Y.; MacDonald, J. F.; Tymianski, M. Distinct roles of synaptic and extrasynaptic NMDA receptors in excitotoxicity. J. Neurosci. 2000, 20, 22-33.
    • (2000) J. Neurosci. , vol.20 , pp. 22-33
    • Sattler, R.1    Xiong, Z.2    Lu, W.Y.3    MacDonald, J.F.4    Tymianski, M.5
  • 97
    • 0037130451 scopus 로고    scopus 로고
    • Subunit-specific NMDA receptor trafficking to synapses
    • Barria, A.; Malinow, R. Subunit-specific NMDA receptor trafficking to synapses. Neuron 2002, 35, 345-353.
    • (2002) Neuron , vol.35 , pp. 345-353
    • Barria, A.1    Malinow, R.2
  • 101
    • 12144271690 scopus 로고    scopus 로고
    • The PSD95-nNOS interface: A target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death
    • Cao, J.; Viholainen, J. I.; Dart, C.; Warwick, H. K.; Leyland, M. L.; Courtney, M. J. The PSD95-nNOS interface: A target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death. J. Cell Biol. 2005, 168, 117-126.
    • (2005) J. Cell. Biol. , vol.168 , pp. 117-126
    • Cao, J.1    Viholainen, J.I.2    Dart, C.3    Warwick, H.K.4    Leyland, M.L.5    Courtney, M.J.6
  • 102
    • 0033546347 scopus 로고    scopus 로고
    • Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein
    • Sattler, R.; Xiong, Z.; Lu, W. Y.; Hafner, M.; MacDonald, J. F.; Tymianski, M. Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein. Science 1999, 284, 1845-1848.
    • (1999) Science , vol.284 , pp. 1845-1848
    • Sattler, R.1    Xiong, Z.2    Lu, W.Y.3    Hafner, M.4    MacDonald, J.F.5    Tymianski, M.6
  • 103
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar, G. M.; Bloodgood, B. L.; Townsend, M.; Walsh, D. M.; Selkoe, D. J.; Sabatini, B. L. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 2007, 27, 2866-2875.
    • (2007) J. Neurosci. , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 104
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss
    • Hsieh, H.; Boehm, J.; Sato, C.; Iwatsubo, T.; Tomita, T.; Sisodia, S.; Malinow, R. AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron 2006, 52, 831-843.
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 106
    • 70449729604 scopus 로고    scopus 로고
    • PICK1-mediated GluR2 endocytosis contributes to cellular injury after neuronal trauma
    • Bell, J. D.; Park, E.; Ai, J.; Baker, A. J. PICK1-mediated GluR2 endocytosis contributes to cellular injury after neuronal trauma. Cell Death Differ. 2009, 16, 1665-1680.
    • (2009) Cell. Death Differ. , vol.16 , pp. 1665-1680
    • Bell, J.D.1    Park, E.2    Ai, J.3    Baker, A.J.4
  • 107
    • 0028296276 scopus 로고
    • Modulation of muscarinic cholinoceptorstimulated inositol 1,4,5-trisphosphate accumulation by N-methyl-D-aspartate in neonatal rat cerebral cortex
    • Challis, R. A.; Mistry, R.; Gray, D. W.; Nahorski, S. R. Modulation of muscarinic cholinoceptorstimulated inositol 1,4,5-trisphosphate accumulation by N-methyl-D-aspartate in neonatal rat cerebral cortex. Neuropharmacology 1994, 33, 15-25.
    • (1994) Neuropharmacology , vol.33 , pp. 15-25
    • Challis, R.A.1    Mistry, R.2    Gray, D.W.3    Nahorski, S.R.4
  • 109
    • 3042561726 scopus 로고    scopus 로고
    • NMDA-receptor regulation of muscarinic-receptor stimulated inositol 1,4,5-trisphosphate production and protein kinase C activation in single cerebellar granule neurons
    • Young, K. W.; Garro, M. A.; Challiss, R. A.; Nahorski, S. R. NMDA-receptor regulation of muscarinic-receptor stimulated inositol 1,4,5-trisphosphate production and protein kinase C activation in single cerebellar granule neurons. J. Neurochem. 2004, 89, 1537-1546.
    • (2004) J. Neurochem. , vol.89 , pp. 1537-1546
    • Young, K.W.1    Garro, M.A.2    Challiss, R.A.3    Nahorski, S.R.4
  • 110
    • 30444440163 scopus 로고    scopus 로고
    • NMDA receptor-mediated epileptiform persistent activity requires calcium release from intracellular stores in prefrontal neurons
    • Gao, W. J.; Goldman-Rakic, P. S. NMDA receptor-mediated epileptiform persistent activity requires calcium release from intracellular stores in prefrontal neurons. Exp. Neurol. 2006, 197, 495-504.
    • (2006) Exp. Neurol. , vol.197 , pp. 495-504
    • Gao, W.J.1    Goldman-Rakic, P.S.2
  • 111
    • 0026071055 scopus 로고
    • Inositol trisphosphate receptor: Phosphorylation by protein kinase C and calcium calmodulin-dependent protein kinases in reconstituted lipid vesicles
    • Ferris, C. D.; Huganir, R. L.; Bredt, D. S.; Cameron, A. M.; Snyder, S. H. Inositol trisphosphate receptor: Phosphorylation by protein kinase C and calcium calmodulin-dependent protein kinases in reconstituted lipid vesicles. Proc Natl. Acad. Sci. USA 1991, 88, 2232-2235.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2232-2235
    • Ferris, C.D.1    Huganir, R.L.2    Bredt, D.S.3    Cameron, A.M.4    Snyder, S.H.5
  • 112
    • 0026089312 scopus 로고
    • Regulation of the cardiac ryanodine receptor by protein kinase-dependent phosphorylation
    • Takasago, T.; Imagawa, T.; Furukawa, K.; Ogurusu, T.; Shigekawa, M. Regulation of the cardiac ryanodine receptor by protein kinase-dependent phosphorylation. J. Biochem. 1991, 109, 163-170.
    • (1991) J. Biochem. , vol.109 , pp. 163-170
    • Takasago, T.1    Imagawa, T.2    Furukawa, K.3    Ogurusu, T.4    Shigekawa, M.5
  • 113
    • 0028089680 scopus 로고
    • Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from skeletal muscle
    • Hain, J.; Nath, S.; Mayrleitner, M.; Fleischer, S.; Schindler, H. Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from skeletal muscle. Biophys. J. 1994, 67, 1823-1833.
    • (1994) Biophys. J. , vol.67 , pp. 1823-1833
    • Hain, J.1    Nath, S.2    Mayrleitner, M.3    Fleischer, S.4    Schindler, H.5
  • 114
    • 0030915445 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 inhibits type I inositol 1,4,5-trisphosphate receptor expression and enhances its phosphorylation in mesangial cells
    • Sharma, K.; Wang, L.; Zhu, Y.; Bokkala, S.; Joseph, S. K. Transforming growth factor-beta1 inhibits type I inositol 1,4,5-trisphosphate receptor expression and enhances its phosphorylation in mesangial cells. J. Biol. Chem. 1997, 272, 14617-14623.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14617-14623
    • Sharma, K.1    Wang, L.2    Zhu, Y.3    Bokkala, S.4    Joseph, S.K.5
  • 115
    • 0007191908 scopus 로고    scopus 로고
    • Phosphorylation of inositol 1,4,5-trisphosphate receptors by cAMP-dependent protein kinase. Type I, II, and III receptors are differentially susceptible to phosphorylation and are phosphorylated in intact cells
    • Wojcikiewicz, R. J.; Luo, S. G. Phosphorylation of inositol 1,4,5-trisphosphate receptors by cAMP-dependent protein kinase. Type I, II, and III receptors are differentially susceptible to phosphorylation and are phosphorylated in intact cells. J. Biol. Chem. 1998, 273, 5670-5677.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5670-5677
    • Wojcikiewicz, R.J.1    Luo, S.G.2
  • 118
    • 3042763171 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor
    • 2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor. Circ. Res. 2004, 94, e61-e70.
    • (2004) Circ. Res. , vol.94
    • Wehrens, X.H.1    Lehnart, S.E.2    Reiken, S.R.3    Marks, A.R.4
  • 119
    • 33747882331 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor type 1 phosphorylation and regulation by extracellular signal-regulated kinase
    • DOI 10.1016/j.bbrc.2006.07.208, PII S0006291X06017669
    • Bai, G. R.; Yang, L. H.; Huang, X. Y.; Sun, F. Z. Inositol 1,4,5-trisphosphate receptor type 1 phosphorylation and regulation by extracellular signal-regulated kinase. Biochem. Biophys. Res. Commun. 2006, 348, 1319-1327. (Pubitemid 44291346)
    • (2006) Biochemical and Biophysical Research Communications , vol.348 , Issue.4 , pp. 1319-1327
    • Bai, G.-R.1    Yang, L.-H.2    Huang, X.-Y.3    Sun, F.-Z.4
  • 121
    • 33748795034 scopus 로고    scopus 로고
    • ERK binds, phosphorylates InsP3 type 1 receptor and regulates intracellular calcium dynamics in DT40 cells
    • Yang, L. H.; Bai, G. R.; Huang, X. Y.; Sun, F. Z. ERK binds, phosphorylates InsP3 type 1 receptor and regulates intracellular calcium dynamics in DT40 cells. Biochem. Biophys. Res. Commun. 2006, 349, 1339-1344.
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 1339-1344
    • Yang, L.H.1    Bai, G.R.2    Huang, X.Y.3    Sun, F.Z.4
  • 123
    • 33947416509 scopus 로고    scopus 로고
    • Protein kinase C decreases the apparent affinity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells
    • DOI 10.1016/j.ceca.2007.01.002, PII S0143416007000085
    • Caron, A. Z.; Chaloux, B.; Arguin, G.; Guillemette, G. Protein kinase C decreases the apparent affinity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells. Cell Calcium. 2007, 42, 323-331. (Pubitemid 47074403)
    • (2007) Cell Calcium , vol.42 , Issue.3 , pp. 323-331
    • Caron, A.Z.1    Chaloux, B.2    Arguin, G.3    Guillemette, G.4
  • 125
    • 61449169005 scopus 로고    scopus 로고
    • Progesterone potentiates calcium release through IP3 receptors by an Akt-mediated mechanism in hippocampal neurons
    • Hwang, J. Y.; Duncan, R. S.; Madry, C.; Singh, M.; Koulen, P. Progesterone potentiates calcium release through IP3 receptors by an Akt-mediated mechanism in hippocampal neurons. Cell Calcium 2009, 45, 233-242.
    • (2009) Cell. Calcium. , vol.45 , pp. 233-242
    • Hwang, J.Y.1    Duncan, R.S.2    Madry, C.3    Singh, M.4    Koulen, P.5
  • 126
    • 18544393408 scopus 로고    scopus 로고
    • Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins
    • Xiao, B.; Tu, J. C.; Petralia, R. S.; Yuan, J. P.; Doan, A.; Breder, C. D.; Ruggiero, A.; Lanahan, A. A.; Wenthold, R. J.; Worley, P. F. Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins. Neuron 1998, 21, 707-716.
    • (1998) Neuron , vol.21 , pp. 707-716
    • Xiao, B.1    Tu, J.C.2    Petralia, R.S.3    Yuan, J.P.4    Doan, A.5    Breder, C.D.6    Ruggiero, A.7    Lanahan, A.A.8    Wenthold, R.J.9    Worley, P.F.10
  • 127
    • 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, J. C.; Xiao, B.; Sala, C.; Valtschanoff, J.; Weinberg, R. J.; Worley, P. F.; Sheng, M. Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. Neuron 1999, 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
  • 129
    • 0034879863 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology and synaptic function by Shank and Homer
    • DOI 10.1016/S0896-6273(01)00339-7
    • Sala, C.; Piech, V.; Wilson, N. R.; Passafaro, M.; Liu, G.; Sheng, M. Regulation of dendritic spine morphology and synaptic function by Shank and Homer. Neuron 2001, 31, 115-130. (Pubitemid 32757093)
    • (2001) Neuron , vol.31 , Issue.1 , pp. 115-130
    • Sala, C.1    Piech, V.2    Wilson, N.R.3    Passafaro, M.4    Liu, G.5    Sheng, M.6
  • 130
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A. G. G proteins: Transducers of receptor-generated signals. Annu. Rev. Biochem. 1987, 56, 615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 131
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon, M. I.; Strathmann, M. P.; Gautam, N. Diversity of G proteins in signal transduction. Science 1991, 252, 802-808.
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 132
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-proteincoupled receptors
    • Rosenbaum, D. M.; Rasmussen, S. G.; Kobilka, B. K. The structure and function of G-proteincoupled receptors. Nature 2009, 459, 356-363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 133
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • Oldham, W. M.; Hamm, H. E. Heterotrimeric G protein activation by G-protein-coupled receptors. Nat. Rev. Mol. Cell Biol. 2008, 9, 60-71.
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 134
    • 34547157646 scopus 로고    scopus 로고
    • Siderovski, Receptor-mediated activation of heterotrimeric Gproteins: Current structural insights
    • Johnston, C. A.; Siderovski, D. P. Siderovski, Receptor-mediated activation of heterotrimeric Gproteins: Current structural insights. Mol. Pharmacol. 2007, 72, 219-230.
    • (2007) Mol. Pharmacol. , vol.72 , pp. 219-230
    • Johnston, C.A.1    Siderovski, D.P.2
  • 135
    • 60149088035 scopus 로고    scopus 로고
    • Functions and Regulatory Mechanisms of Gq-Signaling Pathways
    • Mizuno, N.; Itoh, H. Functions and Regulatory Mechanisms of Gq-Signaling Pathways. Neurosignals 2009, 17, 42-54.
    • (2009) Neurosignals , vol.17 , pp. 42-54
    • Mizuno, N.1    Itoh, H.2
  • 140
    • 0021722983 scopus 로고
    • Cannabinoid inhibition of adenylate cyclase. Pharmacology of the response in neuroblastoma cell membranes
    • Howlett, A. C.; Fleming, R. M. Cannabinoid inhibition of adenylate cyclase. Pharmacology of the response in neuroblastoma cell membranes. Mol. Pharmacol. 1984, 26, 532-538.
    • (1984) Mol. Pharmacol. , vol.26 , pp. 532-538
    • Howlett, A.C.1    Fleming, R.M.2
  • 142
    • 0030746408 scopus 로고    scopus 로고
    • Cannabinoids inhibit n- and p/q-type calcium channels in cultured rat hippocampal neurons
    • Twitchell, W.; Brown, S.; Mackie, K. Cannabinoids inhibit N-and P/Q-type calcium channels in cultured rat hippocampal neurons. J. Neurophysiol. 1997, 78, 43-50. (Pubitemid 27318909)
    • (1997) Journal of Neurophysiology , vol.78 , Issue.1 , pp. 43-50
    • Twitchell, W.1    Brown, S.2    Mackie, K.3
  • 143
    • 0026603679 scopus 로고
    • Cannabinoids inhibit N-type calcium channels in neuroblastoma-glioma cells
    • Mackie, K.; Hille, B. Cannabinoids inhibit N-type calcium channels in neuroblastoma-glioma cells. Proc. Natl. Acad. Sci. USA 1992, 89, 3825-3829.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3825-3829
    • Mackie, K.1    Hille, B.2
  • 144
    • 0027185227 scopus 로고
    • Anandamide, an endogenous cannabimimetic eicosanoid, binds to the cloned human cannabinoid receptor and stimulates receptor-mediated signal transduction
    • Felder, C. C.; Briley, E. M.; Axelrod, J.; Simpson, J. T.; Mackie, K.; Devane, W. A. Anandamide, an endogenous cannabimimetic eicosanoid, binds to the cloned human cannabinoid receptor and stimulates receptor-mediated signal transduction. Proc. Natl. Acad. Sci. USA 1993, 90, 7656-7660.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7656-7660
    • Felder, C.C.1    Briley, E.M.2    Axelrod, J.3    Simpson, J.T.4    Mackie, K.5    Devane, W.A.6
  • 145
    • 33749648816 scopus 로고    scopus 로고
    • Cannabinoid receptor-mediated inhibition of calcium signaling in rat retinal ganglion cells
    • Lalonde, M. R.; Jollimore, C. A.; Stevens, K.; Barnes, S.; Kelly, M. E. Cannabinoid receptormediated inhibition of calcium signaling in rat retinal ganglion cells. Mol. Vis. 2006, 12, 1160-1166. (Pubitemid 44538153)
    • (2006) Molecular Vision , vol.12 , pp. 1160-1166
    • Lalonde, M.R.1    Jollimore, C.A.B.2    Stevens, K.3    Barnes, S.4    Kelly, M.E.M.5
  • 146
    • 30044435435 scopus 로고    scopus 로고
    • The cannabinoid agonist WIN55, 212-2 increases intracellular calcium via CB1 receptor coupling to Gq/11 G proteins
    • Lauckner, J. E.; Hille, B.; Mackie, K. The cannabinoid agonist WIN55, 212-2 increases intracellular calcium via CB1 receptor coupling to Gq/11 G proteins. Proc. Natl. Acad. Sci. USA 2005, 102, 19144-19149.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 19144-19149
    • Lauckner, J.E.1    Hille, B.2    Mackie, K.3
  • 147
    • 0035979606 scopus 로고    scopus 로고
    • 1 cannabinoid receptor protects cultured mouse spinal neurons against excitotoxicity
    • DOI 10.1016/S0304-3940(01)02065-1, PII S0304394001020651
    • Abood, M. E.; Rizvi, G.; Sallapudi, N.; McAllister, S. D. Activation of the CB1 cannabinoid receptor protects cultured mouse spinal neurons against excitotoxicity. Neurosci. Lett. 2001, 309, 197-201. (Pubitemid 32763173)
    • (2001) Neuroscience Letters , vol.309 , Issue.3 , pp. 197-201
    • Abood, M.E.1    Rizvi, G.2    Sallapudi, N.3    McAllister, S.D.4
  • 148
    • 33846066404 scopus 로고    scopus 로고
    • Thayer, Delta9-tetrahydrocannabinol protects hippocampal neurons from excitotoxicity
    • Gilbert, G. L.; Kim, H. J.; Waataja, J. J.; Thayer, S. A. Thayer, Delta9-tetrahydrocannabinol protects hippocampal neurons from excitotoxicity. Brain Res. 2007, 1128, 61-69.
    • (2007) Brain Res. , vol.1128 , pp. 61-69
    • Gilbert, G.L.1    Kim, H.J.2    Waataja, J.J.3    Thayer, S.A.4
  • 150
    • 0031706164 scopus 로고    scopus 로고
    • Cannabinoid receptor agonists protect cultured rat hippocampal neurons from excitotoxicity
    • Shen, M.; Thayer, S. A. Thayer, Cannabinoid receptor agonists protect cultured rat hippocampal neurons from excitotoxicity. Mol. Pharmacol. 1998, 54, 459-462. (Pubitemid 28442938)
    • (1998) Molecular Pharmacology , vol.54 , Issue.3 , pp. 459-462
    • Shen, M.1    Thayer, S.A.2
  • 151
    • 73349099368 scopus 로고    scopus 로고
    • Signaling pathways from CB1 receptor activation to inhibition of NMDA-mediated calcium influx and neurotoxicity in dorsal root ganglion neurons
    • Liu, Q.; Bhat, M.; Bowen, W. D.; Cheng, J. Signaling pathways from CB1 receptor activation to inhibition of NMDA-mediated calcium influx and neurotoxicity in dorsal root ganglion neurons. J. Pharmacol. Exp. Ther. 2009, 331, 1062-1070.
    • (2009) J. Pharmacol. Exp. Ther. , vol.331 , pp. 1062-1070
    • Liu, Q.1    Bhat, M.2    Bowen, W.D.3    Cheng, J.4
  • 152
    • 0029937282 scopus 로고    scopus 로고
    • Cannabinoid receptor agonists inhibit glutamatergic synaptic transmission in rat hippocampal cultures
    • Shen, M.; Piser, T. M.; Seybold, V. S.; Thayer, S. A. Cannabinoid receptor agonists inhibit glutamatergic synaptic transmission in rat hippocampal cultures. J. Neurosci. 1996, 16, 4322-4334. (Pubitemid 26243028)
    • (1996) Journal of Neuroscience , vol.16 , Issue.14 , pp. 4322-4334
    • Shen, M.1    Piser, T.M.2    Seybold, V.S.3    Thayer, S.A.4
  • 153
    • 33644837127 scopus 로고    scopus 로고
    • Molecular mechanisms of cannabinoid protection from neuronal excitotoxicity
    • DOI 10.1124/mol.105.016428
    • Kim, S. H.; Won, S. J.; Mao, X. O.; Jin, K.; Greenberg, D. A. Molecular mechanisms of cannabinoid protection from neuronal excitotoxicity. Mol. Pharmacol. 2006, 69, 691-696. (Pubitemid 43363843)
    • (2006) Molecular Pharmacology , vol.69 , Issue.3 , pp. 691-696
    • Sun, H.K.1    Seok, J.W.2    Xiao, O.M.3    Jin, K.4    Greenberg, D.A.5
  • 154
    • 19444373244 scopus 로고    scopus 로고
    • Cannabinoids produce neuroprotection by reducing intracellular calcium release from ryanodine-sensitive stores
    • DOI 10.1016/j.neuropharm.2005.01.005, PII S0028390805000316
    • Zhuang, S. Y.; Bridges, D.; Grigorenko, E.; McCloud, S.; Boon, A.; Hampson, R. E.; Deadwyler, S. A. Cannabinoids produce neuroprotection by reducing intracellular calcium release from ryanodine-sensitive stores. Neuropharmacology 2005, 48, 1086-1096. (Pubitemid 40725981)
    • (2005) Neuropharmacology , vol.48 , Issue.8 SPEC. ISS. , pp. 1086-1096
    • Zhuang, S.-Y.1    Bridges, D.2    Grigorenko, E.3    McCloud, S.4    Boon, A.5    Hampson, R.E.6    Deadwyler, S.A.7
  • 156
    • 77950354281 scopus 로고    scopus 로고
    • Clinical efficacy and neuroprotective effects of brimonidine in the management of glaucoma and ocular hypertension
    • Galanopoulos, A.; Goldberg, I. Clinical efficacy and neuroprotective effects of brimonidine in the management of glaucoma and ocular hypertension. Clin. Ophthalmol. 2009, 3, 117-122.
    • (2009) Clin. Ophthalmol. , vol.3 , pp. 117-122
    • Galanopoulos, A.1    Goldberg, I.2
  • 157
    • 0035198185 scopus 로고    scopus 로고
    • Alpha(2) -Adrenoceptor agonists inhibit vitreal glutamate and aspartate accumulation and preserve retinal function after transient ischemia
    • Donello, J. E.; Padillo, E. U.; Webster, M. L.; Wheeler, L. A.; Gil, D. W. alpha (2) -Adrenoceptor agonists inhibit vitreal glutamate and aspartate accumulation and preserve retinal function after transient ischemia. J. Pharmacol. Exp. Ther. 2001, 296, 216-223.
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 216-223
    • Donello, J.E.1    Padillo, E.U.2    Webster, M.L.3    Wheeler, L.A.4    Gil, D.W.5
  • 159
    • 0037182095 scopus 로고    scopus 로고
    • Synaptic distribution of ionotropic glutamate receptors in the inner plexiform layer of the primate retina
    • DOI 10.1002/cne.10220
    • Grunert, U.; Haverkamp, S.; Fletcher, E. L.; Wassle, H. Synaptic distribution of ionotropic glutamate receptors in the inner plexiform layer of the primate retina. J. Comp. Neurol. 2002, 447, 138-151. (Pubitemid 34457375)
    • (2002) Journal of Comparative Neurology , vol.447 , Issue.2 , pp. 138-151
    • Grunert, U.1    Haverkamp, S.2    Fletcher, E.L.3    Wassle, H.4
  • 160
    • 0043194100 scopus 로고    scopus 로고
    • Inner retinal neurons display differential responses to N-methyl-D-aspartate receptor activation
    • DOI 10.1002/cne.10830
    • Sun, D.; Rait, J. L.; Kalloniatis, M. Inner retinal neurons display differential responses to Nmethyl-D-aspartate receptor activation. J. Comp. Neurol. 2003, 465, 38-56. (Pubitemid 37075679)
    • (2003) Journal of Comparative Neurology , vol.465 , Issue.1 , pp. 38-56
    • Sun, D.1    Rait, J.L.2    Kalloniatis, M.3
  • 161
    • 0029915446 scopus 로고    scopus 로고
    • Elevated glutamate levels in the vitreous body of humans and monkeys with glaucoma
    • Dreyer, E. B.; Zurakowski, D.; Schumer, R. A.; Podos, S. M.; Lipton, S. A. Elevated glutamate levels in the vitreous body of humans and monkeys with glaucoma. Arch. Ophthalmol. 1996, 114, 299-305.
    • (1996) Arch. Ophthalmol. , vol.114 , pp. 299-305
    • Dreyer, E.B.1    Zurakowski, D.2    Schumer, R.A.3    Podos, S.M.4    Lipton, S.A.5
  • 163
    • 0027972715 scopus 로고
    • Effects of ischaemia on neurotransmitter release from the isolated retina
    • Neal, M. J.; Cunningham, J. R.; Hutson, P. H.; Hogg, J. Effects of ischaemia on neurotransmitter release from the isolated retina. J. Neurochem. 1994, 62, 1025-1033.
    • (1994) J. Neurochem. , vol.62 , pp. 1025-1033
    • Neal, M.J.1    Cunningham, J.R.2    Hutson, P.H.3    Hogg, J.4
  • 164
    • 0029796092 scopus 로고    scopus 로고
    • Disturbances in the distribution of neurotransmitters in the rat retina after ischemia
    • Perlman, J. I.; McCole, S. M.; Pulluru, P.; Chang, C. J.; Lam, T. T.; Tso, M. O. Disturbances in the distribution of neurotransmitters in the rat retina after ischemia. Curr. Eye Res. 1996, 15, 589-596.
    • (1996) Curr. Eye Res. , vol.15 , pp. 589-596
    • Perlman, J.I.1    McCole, S.M.2    Pulluru, P.3    Chang, C.J.4    Lam, T.T.5    Tso, M.O.6
  • 165
    • 34250626907 scopus 로고    scopus 로고
    • Low dose ketamine: A therapeutic and research tool to explore N-methyl-Daspartate (NMDA) receptor-mediated plasticity in pain pathways
    • Chizh, B. A. Low dose ketamine: A therapeutic and research tool to explore N-methyl-Daspartate (NMDA) receptor-mediated plasticity in pain pathways. J. Psychopharmacol. 2007, 21, 259-271.
    • (2007) J. Psychopharmacol. , vol.21 , pp. 259-271
    • Chizh, B.A.1
  • 166
  • 167
    • 0034766994 scopus 로고    scopus 로고
    • Efficacy and safety of memantine, an NMDA-type open-channel blocker, for reduction of retinal injury associated with experimental glaucoma in rat and monkey
    • discussion S285-S286
    • Hare, W.; WoldeMussie, E.; Lai, R.; Ton, H.; Ruiz, G.; Feldmann, B.; Wijono, M.; Chun, T.; Wheeler, L. Efficacy and safety of memantine, an NMDA-type open-channel blocker, for reduction of retinal injury associated with experimental glaucoma in rat and monkey. Surv. Ophthalmol. 2001, 45 (Suppl. 3), S284-S289; discussion S285-S286.
    • (2001) Surv. Ophthalmol. , vol.45 , Issue.3 SUPPL.
    • Hare, W.1    WoldeMussie, E.2    Lai, R.3    Ton, H.4    Ruiz, G.5    Feldmann, B.6    Wijono, M.7    Chun, T.8    Wheeler, L.9
  • 168
    • 0345072185 scopus 로고    scopus 로고
    • Memantine is neuroprotective in a rat model of pressure-induced retinal ischemia
    • Lagreze, W. A.; Knorle, R.; Bach, M.; Feuerstein, T. J. Memantine is neuroprotective in a rat model of pressure-induced retinal ischemia. Invest. Ophthalmol. Vis. Sci. 1998, 39, 1063-1066.
    • (1998) Invest. Ophthalmol. Vis. Sci. , vol.39 , pp. 1063-1066
    • Lagreze, W.A.1    Knorle, R.2    Bach, M.3    Feuerstein, T.J.4
  • 169
    • 0033038186 scopus 로고    scopus 로고
    • Memantine reduces alterations to the mammalian retina, in situ, induced by ischemia
    • Osborne, N. N. Memantine reduces alterations to the mammalian retina, in situ, induced by ischemia. Vis. Neurosci. 1999, 16, 45-52.
    • (1999) Vis. Neurosci. , vol.16 , pp. 45-52
    • Osborne, N.N.1
  • 170
    • 0036913245 scopus 로고    scopus 로고
    • Neuroprotective effect of memantine in different retinal injury models in rats
    • WoldeMussie, E.; Yoles, E.; Schwartz, M.; Ruiz, G.; Wheeler, L. A. Neuroprotective effect of memantine in different retinal injury models in rats. J. Glaucoma 2002, 11, 474-480.
    • (2002) J. Glaucoma , vol.11 , pp. 474-480
    • WoldeMussie, E.1    Yoles, E.2    Schwartz, M.3    Ruiz, G.4    Wheeler, L.A.5
  • 171
    • 3242879784 scopus 로고    scopus 로고
    • Efficacy and safety of memantine treatment for reduction of changes associated with experimental glaucoma in monkey, I: Functional measures
    • DOI 10.1167/iovs.03-0566
    • Hare, W. A.; WoldeMussie, E.; Lai, R. K.; Ton, H.; Ruiz, G.; Chun, T.; Wheeler, L. Efficacy and safety of memantine treatment for reduction of changes associated with experimental glaucoma in monkey, I: Functional measures. Invest. Ophthalmol. Vis. Sci. 2004, 45, 2625-2639. (Pubitemid 38998859)
    • (2004) Investigative Ophthalmology and Visual Science , vol.45 , Issue.8 , pp. 2625-2639
    • Hare, W.A.1    WoldeMussie, E.2    Lai, R.K.3    Ton, H.4    Ruiz, G.5    Chun, T.6    Wheeler, L.7
  • 173
    • 0034754201 scopus 로고    scopus 로고
    • Neuroprotection of retinal ganglion cells by brimonidine in rats with laser-induced chronic ocular hypertension
    • WoldeMussie, E.; Ruiz, G.; Wijono, M.; Wheeler, L. A. Neuroprotection of retinal ganglion cells by brimonidine in rats with laser-induced chronic ocular hypertension. Invest. Ophthalmol. Vis. Sci. 2001, 42, 2849-2855.
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 2849-2855
    • WoldeMussie, E.1    Ruiz, G.2    Wijono, M.3    Wheeler, L.A.4
  • 174
    • 20344407819 scopus 로고    scopus 로고
    • Human ganglion cells express the alpha-2 adrenergic receptor: Relevance to neuroprotection
    • Kalapesi, F. B.; Coroneo, M. T.; Hill, M. A. Human ganglion cells express the alpha-2 adrenergic receptor: Relevance to neuroprotection. Br. J. Ophthalmol. 2005, 89, 758-763.
    • (2005) Br. J. Ophthalmol. , vol.89 , pp. 758-763
    • Kalapesi, F.B.1    Coroneo, M.T.2    Hill, M.A.3
  • 175
    • 37749033221 scopus 로고    scopus 로고
    • Efficacy and safety of brimonidine and dorzolamide for intraocular pressure lowering in glaucoma and ocular hypertension
    • Katz, L. J.; Simmons, S. T.; Craven, E. R. Efficacy and safety of brimonidine and dorzolamide for intraocular pressure lowering in glaucoma and ocular hypertension. Curr. Med. Res. Opin. 2007, 23, 2971-2983.
    • (2007) Curr. Med. Res. Opin. , vol.23 , pp. 2971-2983
    • Katz, L.J.1    Simmons, S.T.2    Craven, E.R.3
  • 176
    • 34047247369 scopus 로고    scopus 로고
    • Alpha2 adrenergic receptor-mediated modulation of cytosolic Ca++ signals at the inner plexiform layer of the rat retina
    • Dong, C. J.; Guo, Y.; Wheeler, L.; Hare, W. A. Alpha2 adrenergic receptor-mediated modulation of cytosolic Ca++ signals at the inner plexiform layer of the rat retina. Invest. Ophthalmol. Vis. Sci. 2007, 48, 1410-1415.
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , pp. 1410-1415
    • Dong, C.J.1    Guo, Y.2    Wheeler, L.3    Hare, W.A.4
  • 177
    • 0029895790 scopus 로고    scopus 로고
    • Genetic evidence for involvement of multiple effector systems in alpha 2A-adrenergic receptor inhibition of stimulus-secretion coupling
    • Lakhlani, P. P.; Lovinger, D. M.; Limbird, L. E. Genetic evidence for involvement of multiple effector systems in alpha 2A-adrenergic receptor inhibition of stimulus-secretion coupling. Mol. Pharmacol. 1996, 50, 96-103.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 96-103
    • Lakhlani, P.P.1    Lovinger, D.M.2    Limbird, L.E.3
  • 178
    • 53449088505 scopus 로고    scopus 로고
    • Alpha2 adrenergic modulation of NMDA receptor function as a major mechanism of RGC protection in experimental glaucoma and retinal excitotoxicity
    • Dong, C. J.; Guo, Y.; Agey, P.; Wheeler, L.; Hare, W. A. Alpha2 adrenergic modulation of NMDA receptor function as a major mechanism of RGC protection in experimental glaucoma and retinal excitotoxicity. Invest. Ophthalmol. Vis. Sci. 2008, 49, 4515-4522.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 4515-4522
    • Dong, C.J.1    Guo, Y.2    Agey, P.3    Wheeler, L.4    Hare, W.A.5
  • 184
    • 3342889548 scopus 로고    scopus 로고
    • Presenilin 1 is essential for cardiac morphogenesis
    • DOI 10.1002/dvdy.20098
    • Nakajima, M.; Moriizumi, E.; Koseki, H.; Shirasawa, T. Presenilin 1 is essential for cardiac morphogenesis. Dev. Dyn. 2004, 230, 795-799. (Pubitemid 38993879)
    • (2004) Developmental Dynamics , vol.230 , Issue.4 , pp. 795-799
    • Nakajima, M.1    Moriizumi, E.2    Koseki, H.3    Shirasawa, T.4
  • 185
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in Presenilin-1-deficient mice
    • Shen, J.; Bronson, R. T.; Chen, D. F.; Xia, W.; Selkoe, D. J.; Tonegawa, S. Skeletal and CNS defects in Presenilin-1-deficient mice. Cell 1997, 89, 629-639. (Pubitemid 27511773)
    • (1997) Cell , vol.89 , Issue.4 , pp. 629-639
    • Shen, J.1    Bronson, R.T.2    Chen, D.F.3    Xia, W.4    Selkoe, D.J.5    Tonegawa, S.6
  • 188
    • 0037183702 scopus 로고    scopus 로고
    • The presenilin 1 deltaE9 mutation gives enhanced basal phospholipase C activity and a resultant increase in intracellular calcium concentrations
    • Cedazo-Minguez, A.; Popescu, B. O.; Ankarcrona, M.; Nishimura, T.; Cowburn, R. F. The presenilin 1 deltaE9 mutation gives enhanced basal phospholipase C activity and a resultant increase in intracellular calcium concentrations. J. Biol. Chem. 2002, 277, 36646-36655.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36646-36655
    • Cedazo-Minguez, A.1    Popescu, B.O.2    Ankarcrona, M.3    Nishimura, T.4    Cowburn, R.F.5
  • 189
    • 14244268498 scopus 로고    scopus 로고
    • Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • Chyung, J. H.; Raper, D. M.; Selkoe, D. J. Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J. Biol. Chem. 2005, 280, 4383-4392.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4383-4392
    • Chyung, J.H.1    Raper, D.M.2    Selkoe, D.J.3
  • 191
    • 47749095383 scopus 로고    scopus 로고
    • Linking calcium to Abeta and Alzheimer's disease
    • Green, K. N.; LaFerla, F. M. Linking calcium to Abeta and Alzheimer's disease. Neuron 2008, 59, 190-194.
    • (2008) Neuron , vol.59 , pp. 190-194
    • Green, K.N.1    LaFerla, F.M.2
  • 194
  • 195
    • 0032488995 scopus 로고    scopus 로고
    • The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex
    • Capell, A.; Grunberg, J.; Pesold, B.; Diehlmann, A.; Citron, M.; Nixon, R.; Beyreuther, K.; Selkoe, D. J.; Haass, C. The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex. J. Biol. Chem. 1998, 273, 3205-3211.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3205-3211
    • Capell, A.1    Grunberg, J.2    Pesold, B.3    Diehlmann, A.4    Citron, M.5    Nixon, R.6    Beyreuther, K.7    Selkoe, D.J.8    Haass, C.9
  • 197
    • 0034657414 scopus 로고    scopus 로고
    • Capacitative calcium entry deficits and elevated luminal calcium content in mutant presenilin-1 knockin mice
    • Leissring, M. A.; Akbari, Y.; Fanger, C. M.; Cahalan, M. D.; Mattson, M. P.; LaFerla, F. M. Capacitative calcium entry deficits and elevated luminal calcium content in mutant presenilin-1 knockin mice. J. Cell. Biol. 2000, 149, 793-798.
    • (2000) J. Cell. Biol. , vol.149 , pp. 793-798
    • Leissring, M.A.1    Akbari, Y.2    Fanger, C.M.3    Cahalan, M.D.4    Mattson, M.P.5    LaFerla, F.M.6
  • 198
    • 0034979346 scopus 로고    scopus 로고
    • Subcellular mechanisms of presenilinmediated enhancement of calcium signaling
    • Leissring, M. A.; LaFerla, F. M.; Callamaras, N.; Parker, I. Subcellular mechanisms of presenilinmediated enhancement of calcium signaling. Neurobiol. Dis. 2001, 8, 469-478.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 469-478
    • Leissring, M.A.1    LaFerla, F.M.2    Callamaras, N.3    Parker, I.4
  • 200
    • 0034652369 scopus 로고    scopus 로고
    • Presenilin-1 mutation increases neuronal vulnerability to focal ischemia in vivo and to hypoxia and glucose deprivation in cell culture: Involvement of perturbed calcium homeostasis
    • Mattson, M. P.; Zhu, H.; Yu, J.; Kindy, M. S. Presenilin-1 mutation increases neuronal vulnerability to focal ischemia in vivo and to hypoxia and glucose deprivation in cell culture: Involvement of perturbed calcium homeostasis. J. Neurosci. 2000, 20, 1358-1364.
    • (2000) J. Neurosci. , vol.20 , pp. 1358-1364
    • Mattson, M.P.1    Zhu, H.2    Yu, J.3    Kindy, M.S.4
  • 202
    • 24644456470 scopus 로고    scopus 로고
    • Calcium dysregulation in Alzheimer's disease: Recent advances gained from genetically modified animals
    • Smith, I. F.; Green, K. N.; LaFerla, F. M. Calcium dysregulation in Alzheimer's disease: Recent advances gained from genetically modified animals. Cell Calcium 2005, 38, 427-437.
    • (2005) Cell. Calcium. , vol.38 , pp. 427-437
    • Smith, I.F.1    Green, K.N.2    LaFerla, F.M.3
  • 206
    • 33744925947 scopus 로고    scopus 로고
    • Mapping cellular transcriptosomes in autopsied Alzheimer's disease subjects and relevant animal models
    • DOI 10.1016/j.neurobiolaging.2005.04.014, PII S019745800500196X
    • Reddy, P. H.; McWeeney, S. Mapping cellular transcriptosomes in autopsied Alzheimer's disease subjects and relevant animal models. Neurobiol. Aging 2006, 27, 1060-1077. (Pubitemid 43850649)
    • (2006) Neurobiology of Aging , vol.27 , Issue.8 , pp. 1060-1077
    • Reddy, P.H.1    McWeeney, S.2
  • 207
    • 0023369739 scopus 로고
    • Hypothesis on the regulation of cytosol calcium concentration and the aging brain
    • Khachaturian, Z. S. Hypothesis on the regulation of cytosol calcium concentration and the aging brain. Neurobiol. Aging 1987, 8, 345-346.
    • (1987) Neurobiol. Aging , vol.8 , pp. 345-346
    • Khachaturian, Z.S.1
  • 208
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson, M. P. Pathways towards and away from Alzheimer's disease. Nature 2004, 430, 631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 210
    • 0026624769 scopus 로고
    • Changes in intracellular free calcium concentration during long exposures to simulated ischemia in isolated mammalian ventricular muscle
    • Lee, J. A.; Allen, D. G. Changes in intracellular free calcium concentration during long exposures to simulated ischemia in isolated mammalian ventricular muscle. Circ. Res. 1992, 71, 58-69.
    • (1992) Circ. Res. , vol.71 , pp. 58-69
    • Lee, J.A.1    Allen, D.G.2
  • 211
    • 42049108814 scopus 로고    scopus 로고
    • Mechanisms underlying acute protection from cardiac ischemiareperfusion injury
    • Murphy, E.; Steenbergen, C. Mechanisms underlying acute protection from cardiac ischemiareperfusion injury. Physiol. Rev. 2008, 88, 581-609.
    • (2008) Physiol. Rev. , vol.88 , pp. 581-609
    • Murphy, E.1    Steenbergen, C.2
  • 212
    • 33846506801 scopus 로고    scopus 로고
    • Inflammation, Proinflammatory Mediators and Myocardial Ischemia-reperfusion Injury
    • DOI 10.1016/j.hoc.2006.11.010, PII S0889858806001948, Inflamation, Hemostasis, and Blood Conservation Strategies
    • Vinten-Johansen, J.; Jiang, R.; Reeves, J. G.; Mykytenko, J.; Deneve, J.; Jobe, L. J. Inflammation, proinflammatory mediators and myocardial ischemia-reperfusion Injury. Hematol. Oncol. Clin. North Am. 2007, 21, 123-145. (Pubitemid 46156986)
    • (2007) Hematology/Oncology Clinics of North America , vol.21 , Issue.1 , pp. 123-145
    • Vinten-Johansen, J.1    Jiang, R.2    Reeves, J.G.3    Mykytenko, J.4    Deneve, J.5    Jobe, L.J.6
  • 213
    • 0037207059 scopus 로고    scopus 로고
    • Presenilins in the heart: Presenilin-2 expression is increased by low glucose and by hypoxia in cardiac cells
    • DOI 10.1016/S0167-0115(02)00225-2, PII S0167011502002252
    • Mohuczy, D.; Qian, K.; Phillips, M. I. Presenilins in the heart: Presenilin-2 expression is increased by low glucose and by hypoxia in cardiac cells. Regul. Pept. 2002, 110, 1-7. (Pubitemid 35439144)
    • (2002) Regulatory Peptides , vol.110 , Issue.1 , pp. 1-7
    • Mohuczy, D.1    Qian, K.2    Phillips, M.I.3
  • 217
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 1985, 260, 3440-3450.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 220
    • 67349274521 scopus 로고    scopus 로고
    • 2+ indicator-caused fluorescence artifact
    • 2+ indicator-caused fluorescence artifact. Anal. Biochem. 2009, 390, 212-214.
    • (2009) Anal. Biochem. , vol.390 , pp. 212-214
    • Kukkonen, J.P.1
  • 221
    • 0009448302 scopus 로고
    • Über den anschaulichen Inhalt der quantentheoretischen Kinematik und Mechanik
    • Heisenberg, W. Über den anschaulichen Inhalt der quantentheoretischen Kinematik und Mechanik. Z. Phys. A-Hadron. Nucl. 1927, 43, 172-198.
    • (1927) Z. Phys. A-Hadron. Nucl. , vol.43 , pp. 172-198
    • Heisenberg, W.1
  • 222
    • 44849120336 scopus 로고    scopus 로고
    • Genetically encoded calcium indicators
    • Mank, M.; Griesbeck, O. Genetically encoded calcium indicators. Chem. Rev 2008, 108, 1550-1564.
    • (2008) Chem. Rev. , vol.108 , pp. 1550-1564
    • Mank, M.1    Griesbeck, O.2
  • 224
    • 34249945258 scopus 로고    scopus 로고
    • Far-field optical nanoscopy
    • Hell, S. W. Far-field optical nanoscopy. Science 2007, 316, 1153-1158.
    • (2007) Science , vol.316 , pp. 1153-1158
    • Hell, S.W.1
  • 225
    • 0242322565 scopus 로고    scopus 로고
    • Toward fluorescence nanoscopy
    • Hell, S. W. Toward fluorescence nanoscopy. Nat. Biotechnol. 2003, 21, 1347-1355.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1347-1355
    • Hell, S.W.1
  • 227
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution fluorescence microscopy
    • Huang, B.; Bates, M.; Zhuang, X. Super-resolution fluorescence microscopy. Annu. Rev. Biochem. 2009, 78, 993-1016.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.3
  • 228
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated emission: Stimulated-emission-depletion fluorescence microscopy
    • Hell, S. W.; Wichmann, J. Breaking the diffraction resolution limit by stimulated emission: Stimulated-emission-depletion fluorescence microscopy. Opt. Lett. 1994, 19, 780-782.
    • (1994) Opt. Lett. , vol.19 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 229
    • 0032607671 scopus 로고    scopus 로고
    • Subdiffraction resolution in far-field fluorescence microscopy
    • Klar, T. A.; Hell, S. W. Subdiffraction resolution in far-field fluorescence microscopy. Opt. Lett. 1999, 24, 954-956.
    • (1999) Opt. Lett. , vol.24 , pp. 954-956
    • Klar, T.A.1    Hell, S.W.2
  • 230
    • 33845360042 scopus 로고    scopus 로고
    • Ultra-high resolution imaging by fluorescence photoactivation localization microscopy
    • Hess, S. T.; Girirajan, T. P.; Mason, M. D. Ultra-high resolution imaging by fluorescence photoactivation localization microscopy. Biophys. J. 2006, 91, 4258-4272.
    • (2006) Biophys. J. , vol.91 , pp. 4258-4272
    • Hess, S.T.1    Girirajan, T.P.2    Mason, M.D.3
  • 232
    • 0000412790 scopus 로고    scopus 로고
    • Method of obtaining optical sectioning by using structured light in a conventional microscope
    • Neil, M. A. A.; Juskaitis, R.; Wilson, T. Method of obtaining optical sectioning by using structured light in a conventional microscope. Opt. Lett. 1997, 22, 1905-1907.
    • (1997) Opt. Lett. , vol.22 , pp. 1905-1907
    • Neil, M.A.A.1    Juskaitis, R.2    Wilson, T.3
  • 233
    • 24944539530 scopus 로고    scopus 로고
    • Nonlinear structured-illumination microscopy: Wide-field fluorescence imaging with theoretically unlimited resolution
    • Gustafsson, M. G. Nonlinear structured-illumination microscopy: Wide-field fluorescence imaging with theoretically unlimited resolution. Proc. Natl. Acad. Sci. USA 2005, 102, 13081-13086.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13081-13086
    • Gustafsson, M.G.1
  • 235
    • 0028369038 scopus 로고
    • Confocal microscopy with an increased detection aperture: Type-B 4pi confocal microscopy
    • Hell, S. W.; Stelzer, E. H.; Lindek, S.; Confocal microscopy with an increased detection aperture: Type-B 4pi confocal microscopy. Opt. Lett. 1994, 19, 222.
    • (1994) Opt. Lett. , vol.19 , pp. 222
    • Hell, S.W.1    Stelzer, E.H.2    Lindek, S.3
  • 236
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust, M. J.; Bates, M.; Zhuang, X. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 2006, 3, 793-795.
    • (2006) Nat. Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 237
    • 33846565429 scopus 로고    scopus 로고
    • 2+ signals and neuronal death in brain ischemia
    • 2+ signals and neuronal death in brain ischemia. Stroke 2007, 38, 674-676.
    • (2007) Stroke , vol.38 , pp. 674-676
    • Bano, D.1    Nicotera, P.2
  • 238
    • 61849142791 scopus 로고    scopus 로고
    • Calcium signaling and neurodegenerative diseases
    • Bezprozvanny, I. Calcium signaling and neurodegenerative diseases. Trends Mol. Med. 2009, 15, 89-100.
    • (2009) Trends Mol. Med. , vol.15 , pp. 89-100
    • Bezprozvanny, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.