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Volumn 228, Issue 6, 2013, Pages 1143-1148

Amyloid toxicity and platelet-activating factor signaling

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; GINKGO BILOBA EXTRACT; MITOGEN ACTIVATED PROTEIN KINASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; OLIGOMER; REACTIVE OXYGEN METABOLITE; THROMBOCYTE ACTIVATING FACTOR; THROMBOCYTE ACTIVATING FACTOR ANTAGONIST;

EID: 84874218692     PISSN: 00219541     EISSN: 10974652     Source Type: Journal    
DOI: 10.1002/jcp.24284     Document Type: Article
Times cited : (7)

References (121)
  • 1
    • 0034049694 scopus 로고    scopus 로고
    • Interaction between neurone and microglia mediated by platelet-activating factor
    • Aihara M, Ishii S, Kume K, Shimizu T. 2000. Interaction between neurone and microglia mediated by platelet-activating factor. Genes Neurons 5:397-406.
    • (2000) Genes Neurons , vol.5 , pp. 397-406
    • Aihara, M.1    Ishii, S.2    Kume, K.3    Shimizu, T.4
  • 3
    • 0036669403 scopus 로고    scopus 로고
    • Platelet-activating factor acetylhydrolase
    • Arai H. 2002. Platelet-activating factor acetylhydrolase. Prostaglandins Other Lipid Mediat 68-69:83-94.
    • (2002) Prostaglandins Other Lipid Mediat , Issue.68-69 , pp. 83-94
    • Arai, H.1
  • 4
    • 0034282438 scopus 로고    scopus 로고
    • Platelet-activating factor (PAF)-dependent transacetylase and its relationship with PAF acetylhydrolases
    • Bae K, Longobardi L, Karasawa K, Malone B, Inoue T, Aoki J, Arai H, Inoue K, Lee T. 2000. Platelet-activating factor (PAF)-dependent transacetylase and its relationship with PAF acetylhydrolases. J Biol Chem 275:26704-26709.
    • (2000) J Biol Chem , vol.275 , pp. 26704-26709
    • Bae, K.1    Longobardi, L.2    Karasawa, K.3    Malone, B.4    Inoue, T.5    Aoki, J.6    Arai, H.7    Inoue, K.8    Lee, T.9
  • 5
    • 0030878241 scopus 로고    scopus 로고
    • The role of platelet-activating factor-dependent transacetylase in the biosynthesis of 1-acyl-2-acetyl-sn-glycero-3-phosphocholine by stimulated endothelial cells
    • Balestrieri ML, Servillo L, Lee T. 1997. The role of platelet-activating factor-dependent transacetylase in the biosynthesis of 1-acyl-2-acetyl-sn-glycero-3-phosphocholine by stimulated endothelial cells. J Biol Chem 272:17431-17437.
    • (1997) J Biol Chem , vol.272 , pp. 17431-17437
    • Balestrieri, M.L.1    Servillo, L.2    Lee, T.3
  • 6
    • 77955516608 scopus 로고    scopus 로고
    • Endothelial progenitor cells express PAF receptor and respond to PAF via Ca(2+)-dependent signaling
    • Balestrieri ML, Giovane A, Milone L, Servillo L. 2010. Endothelial progenitor cells express PAF receptor and respond to PAF via Ca(2+)-dependent signaling. Biochim Biophys Acta 1801:1123-1132.
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 1123-1132
    • Balestrieri, M.L.1    Giovane, A.2    Milone, L.3    Servillo, L.4
  • 7
    • 1542357584 scopus 로고    scopus 로고
    • The role of platelet activating factor in prion and amyloid-beta neurotoxicity
    • Bate C, Salmona M, Williams A. 2004a. The role of platelet activating factor in prion and amyloid-beta neurotoxicity. Neuroreport 15:509-513.
    • (2004) Neuroreport , vol.15 , pp. 509-513
    • Bate, C.1    Salmona, M.2    Williams, A.3
  • 8
    • 4344600436 scopus 로고    scopus 로고
    • Ginkgolide B inhibits the neurotoxicity of prions or amyloid-beta 1-42
    • Bate C, Salmona M, Williams A. 2004b. Ginkgolide B inhibits the neurotoxicity of prions or amyloid-beta 1-42. J Neuroinflam 1:4.
    • (2004) J Neuroinflam , vol.1 , pp. 4
    • Bate, C.1    Salmona, M.2    Williams, A.3
  • 9
    • 4344624313 scopus 로고    scopus 로고
    • Phospholipase A2 inhibitors or platelet-activating factor antagonists prevent prion replication
    • Bate C, Reid S, Williams A. 2004c. Phospholipase A2 inhibitors or platelet-activating factor antagonists prevent prion replication. J Biol Chem 279:36405-36411.
    • (2004) J Biol Chem , vol.279 , pp. 36405-36411
    • Bate, C.1    Reid, S.2    Williams, A.3
  • 10
    • 33745939303 scopus 로고    scopus 로고
    • Platelet-activating factor antagonists protect amyloid-beta damaged neurons from microglia-mediated death
    • Bate C, Kempster S, Williams A. 2006. Platelet-activating factor antagonists protect amyloid-beta damaged neurons from microglia-mediated death. Neuropharmacology 51:173-181.
    • (2006) Neuropharmacology , vol.51 , pp. 173-181
    • Bate, C.1    Kempster, S.2    Williams, A.3
  • 11
    • 33846821715 scopus 로고    scopus 로고
    • Cholesterol synthesis inhibitors protect against platelet-activating factor-induced neuronal damage
    • Bate C, Rumbold L, Williams A. 2007. Cholesterol synthesis inhibitors protect against platelet-activating factor-induced neuronal damage. J Neuroinflam 18:4-5.
    • (2007) J Neuroinflam , vol.18 , pp. 4-5
    • Bate, C.1    Rumbold, L.2    Williams, A.3
  • 12
    • 40149094037 scopus 로고    scopus 로고
    • Ginkgolides protect against amyloid-beta 1-42-mediated synapse damage in vitro
    • Bate C, Tayebi M, Williams A. 2008. Ginkgolides protect against amyloid-beta 1-42-mediated synapse damage in vitro. Mol Neurodegener 3:1.
    • (2008) Mol Neurodegener , vol.3 , pp. 1
    • Bate, C.1    Tayebi, M.2    Williams, A.3
  • 13
    • 77950638702 scopus 로고    scopus 로고
    • Phospholipase A2 inhibitors protect against prion and Abeta mediated synapse degeneration
    • Bate C, Tayebi M, Williams A. 2010. Phospholipase A2 inhibitors protect against prion and Abeta mediated synapse degeneration. Mol Neurodegener 8:5-13.
    • (2010) Mol Neurodegener , vol.8 , pp. 5-13
    • Bate, C.1    Tayebi, M.2    Williams, A.3
  • 14
    • 78650813872 scopus 로고    scopus 로고
    • Inhibition of phospholipase A2 increased the removal of the prion derived peptide PrP82-146 from cultured neurons
    • Bate C, Ingham V, Williams A. 2011. Inhibition of phospholipase A2 increased the removal of the prion derived peptide PrP82-146 from cultured neurons. Neuropharmacology 60:365-372.
    • (2011) Neuropharmacology , vol.60 , pp. 365-372
    • Bate, C.1    Ingham, V.2    Williams, A.3
  • 15
    • 23444444518 scopus 로고    scopus 로고
    • Lipid signaling in neural plasticity, brain repair, and neuroprotection
    • Bazan NG. 2005. Lipid signaling in neural plasticity, brain repair, and neuroprotection. Mol Neurobiol 32:89-103.
    • (2005) Mol Neurobiol , vol.32 , pp. 89-103
    • Bazan, N.G.1
  • 16
    • 0036456629 scopus 로고    scopus 로고
    • What synaptic lipid signaling tells us about seizure-induced damage and epileptogenesis
    • Bazan NG, Tu B, Rodriguez de Turco EB. 2002. What synaptic lipid signaling tells us about seizure-induced damage and epileptogenesis. Prog Brain Res 135:175-185.
    • (2002) Prog Brain Res , vol.135 , pp. 175-185
    • Bazan, N.G.1    Tu, B.2    Rodriguez de Turco, E.B.3
  • 17
    • 80052266131 scopus 로고    scopus 로고
    • The selective and competitive N-methyl-D-aspartate receptor antagonist, (-)-6-phosphonomethyl-deca-hydroisoquinoline-3-carboxylic acid, prevents synaptic toxicity induced by amyloid-beta in mice
    • Bicca MA, Figueiredo CP, Piermartiri TC, Meotti FC, Bouzon ZL, Tasca CI, Medeiros R, Calixto JB. 2011. The selective and competitive N-methyl-D-aspartate receptor antagonist, (-)-6-phosphonomethyl-deca-hydroisoquinoline-3-carboxylic acid, prevents synaptic toxicity induced by amyloid-beta in mice. Neuroscience 192:631-641.
    • (2011) Neuroscience , vol.192 , pp. 631-641
    • Bicca, M.A.1    Figueiredo, C.P.2    Piermartiri, T.C.3    Meotti, F.C.4    Bouzon, Z.L.5    Tasca, C.I.6    Medeiros, R.7    Calixto, J.B.8
  • 18
    • 0024231988 scopus 로고    scopus 로고
    • Platelet activating factor antagonist BN52021 decreases accumulation of free polyunsaturated fatty acid in mouse brain during ischemia and electroconvulsive shock
    • Birkle DL, Kurian P, Braquet P, Bazan NG. 1998. Platelet activating factor antagonist BN52021 decreases accumulation of free polyunsaturated fatty acid in mouse brain during ischemia and electroconvulsive shock. J Neurochem 51:1900-1905.
    • (1998) J Neurochem , vol.51 , pp. 1900-1905
    • Birkle, D.L.1    Kurian, P.2    Braquet, P.3    Bazan, N.G.4
  • 19
    • 10644247497 scopus 로고    scopus 로고
    • Anti-apoptotic actions of the platelet activating factor acetylhydrolase I alpha 2 catalytic subunit
    • Bonin F, Ryan SD, Migahed L, Mo F, Lallier J, Franks DJ, Arai H, Bennett SA. 2004. Anti-apoptotic actions of the platelet activating factor acetylhydrolase I alpha 2 catalytic subunit. J Biol Chem 279:52425-52436.
    • (2004) J Biol Chem , vol.279 , pp. 52425-52436
    • Bonin, F.1    Ryan, S.D.2    Migahed, L.3    Mo, F.4    Lallier, J.5    Franks, D.J.6    Arai, H.7    Bennett, S.A.8
  • 20
    • 78649417803 scopus 로고    scopus 로고
    • Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid-beta production
    • Bordji K, Becerril-Ortega J, Nicole O, Buisson A. 2010. Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid-beta production. J Neurosci 30:15927-15942.
    • (2010) J Neurosci , vol.30 , pp. 15927-15942
    • Bordji, K.1    Becerril-Ortega, J.2    Nicole, O.3    Buisson, A.4
  • 21
    • 0036734851 scopus 로고    scopus 로고
    • Platelet activating factor-induced apoptosis is inhibited by ectopic expression of the platelet activating factor G-protein coupled receptor
    • Brewer C, Bonin F, Bullock P, Nault MC, Morin J, Imbeault S, Shen TY, Franks DJ, Bennett SAL. 2002. Platelet activating factor-induced apoptosis is inhibited by ectopic expression of the platelet activating factor G-protein coupled receptor. J Neurochem 82:1502-1511.
    • (2002) J Neurochem , vol.82 , pp. 1502-1511
    • Brewer, C.1    Bonin, F.2    Bullock, P.3    Nault, M.C.4    Morin, J.5    Imbeault, S.6    Shen, T.Y.7    Franks, D.J.8    Bennett, S.A.L.9
  • 24
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid b-peptide
    • Butterfield AD, Drake J, Pocernich C, Castegna A. 2001. Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid b-peptide. Trends Mol Med 7:548-554.
    • (2001) Trends Mol Med , vol.7 , pp. 548-554
    • Butterfield, A.D.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 25
    • 0035176111 scopus 로고    scopus 로고
    • Attenuated LTP in hippocampal dentate gyrus neurons of mice deficient in the PAF receptor
    • Chen C, Magee JC, Marcheselli V, Hardy M, Bazan NG. 2001. Attenuated LTP in hippocampal dentate gyrus neurons of mice deficient in the PAF receptor. J Neurophysiol 85:384-390.
    • (2001) J Neurophysiol , vol.85 , pp. 384-390
    • Chen, C.1    Magee, J.C.2    Marcheselli, V.3    Hardy, M.4    Bazan, N.G.5
  • 26
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human diseases
    • Chiti F, Dobson C. 2006. Protein misfolding, functional amyloid, and human diseases. Annu Rev Biochem 75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.2
  • 28
    • 0026497926 scopus 로고
    • Excitotoxic cell death
    • Choi DW. 1992. Excitotoxic cell death. J Neurobiol 23:1261-1276.
    • (1992) J Neurobiol , vol.23 , pp. 1261-1276
    • Choi, D.W.1
  • 29
    • 0028642274 scopus 로고
    • Calcium and excitotoxic neuronal injury
    • Choi DW. 1994. Calcium and excitotoxic neuronal injury. Ann N Y Acad Sci 747:162-171.
    • (1994) Ann N Y Acad Sci , vol.747 , pp. 162-171
    • Choi, D.W.1
  • 30
    • 0027081205 scopus 로고
    • Enhancement of hippocampal excitatory synaptic transmission by platelet-activating factor
    • Clark GD, Happel LT, Zorumski CF, Bazan NG. 1992. Enhancement of hippocampal excitatory synaptic transmission by platelet-activating factor. Neuron 9:1211-1216.
    • (1992) Neuron , vol.9 , pp. 1211-1216
    • Clark, G.D.1    Happel, L.T.2    Zorumski, C.F.3    Bazan, N.G.4
  • 31
    • 34249672242 scopus 로고    scopus 로고
    • Ab oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP, Viola K, Fernandez SJ, Ferreira ST, Klein WL. 2007. Ab oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282:11590-11601.
    • (2007) J Biol Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 32
    • 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
  • 33
    • 77951251848 scopus 로고    scopus 로고
    • Calcium signaling and amyloid toxicity in Alzheimer disease
    • Demuro A, Parker I, Stutzmann GE. 2010. Calcium signaling and amyloid toxicity in Alzheimer disease. J Biol Chem 285:12463-12468.
    • (2010) J Biol Chem , vol.285 , pp. 12463-12468
    • Demuro, A.1    Parker, I.2    Stutzmann, G.E.3
  • 34
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM. 2003. Protein folding and misfolding. Nature 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 36
    • 33646594976 scopus 로고    scopus 로고
    • Phospholipase A2-generated lipid mediators in the brain: The good, the bad, and the ugly
    • Farooqui AA, Horrocks LA. 2006. Phospholipase A2-generated lipid mediators in the brain: The good, the bad, and the ugly. Neuroscientist 12:245-260.
    • (2006) Neuroscientist , vol.12 , pp. 245-260
    • Farooqui, A.A.1    Horrocks, L.A.2
  • 37
    • 33748804968 scopus 로고    scopus 로고
    • Inhibitors of brain phospholipase A2 activity: Their neuropharmacological effects and therapeutic importance for the treatment of neurologic disorders
    • Farooqui AA, Ong WY, Horrocks LA. 2006. Inhibitors of brain phospholipase A2 activity: Their neuropharmacological effects and therapeutic importance for the treatment of neurologic disorders. Pharmacol Rev 58:591-620.
    • (2006) Pharmacol Rev , vol.58 , pp. 591-620
    • Farooqui, A.A.1    Ong, W.Y.2    Horrocks, L.A.3
  • 38
    • 77953240725 scopus 로고    scopus 로고
    • Lipid mediators in the nucleus: Their potential contribution to Alzheimer's disease
    • Farooqui AA, Ong WY, Farooqui T. 2010. Lipid mediators in the nucleus: Their potential contribution to Alzheimer's disease. Biochim Biophys Acta 1801:906-916.
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 906-916
    • Farooqui, A.A.1    Ong, W.Y.2    Farooqui, T.3
  • 39
    • 0030249717 scopus 로고    scopus 로고
    • Relative contribution of the de novo and remodelling pathways to the synthesis of platelet-activating factor in brain areas and during ischemia
    • Francescangeli E, Domanska-Janik K, Goracci G. 1996. Relative contribution of the de novo and remodelling pathways to the synthesis of platelet-activating factor in brain areas and during ischemia. J Lipid Mediat Cell Signal 14:89-98.
    • (1996) J Lipid Mediat Cell Signal , vol.14 , pp. 89-98
    • Francescangeli, E.1    Domanska-Janik, K.2    Goracci, G.3
  • 43
    • 79952375934 scopus 로고    scopus 로고
    • Prolonged exposure of cortical neurons to oligomeric amyloid-β impairs NMDA receptor function via NADPH oxidase-mediated ROS production: Protective effect of green tea (-)-epigallocatechin-3-gallate
    • He Y, Cui J, Lee JC, Ding S, Chalimoniuk M, Simonyi A, Sun AY, Gu Z, Weisman GA, Wood WG, Sun GY. 2011. Prolonged exposure of cortical neurons to oligomeric amyloid-β impairs NMDA receptor function via NADPH oxidase-mediated ROS production: Protective effect of green tea (-)-epigallocatechin-3-gallate. ASN Neuro 3:e00050.
    • (2011) ASN Neuro , vol.3
    • He, Y.1    Cui, J.2    Lee, J.C.3    Ding, S.4    Chalimoniuk, M.5    Simonyi, A.6    Sun, A.Y.7    Gu, Z.8    Weisman, G.A.9    Wood, W.G.10    Sun, G.Y.11
  • 44
    • 0036562620 scopus 로고    scopus 로고
    • Platelet-activating factor induces cell death in cultured astrocytes and oligodendrocytes: Involvement of caspase-3
    • Hostettler ME, Knapp PE, Carlson SL. 2002. Platelet-activating factor induces cell death in cultured astrocytes and oligodendrocytes: Involvement of caspase-3. Glia 38:228-239.
    • (2002) Glia , vol.38 , pp. 228-239
    • Hostettler, M.E.1    Knapp, P.E.2    Carlson, S.L.3
  • 45
    • 84866375316 scopus 로고    scopus 로고
    • Resolution of the effects induced by W→F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F
    • Infusini G, Iannuzzi C, Vilasi S, Birolo L, Pagnozzi D, Pucci P, Irace G, Sirangelo I. 2012. Resolution of the effects induced by W→F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F. Eur Biophys J 41:615-627.
    • (2012) Eur Biophys J , vol.41 , pp. 615-627
    • Infusini, G.1    Iannuzzi, C.2    Vilasi, S.3    Birolo, L.4    Pagnozzi, D.5    Pucci, P.6    Irace, G.7    Sirangelo, I.8
  • 46
    • 38949167084 scopus 로고    scopus 로고
    • New structures help the modeling of toxic amyloid_ion channels
    • Jang H, Zheng J, Lal R, Nussinov R. 2008. New structures help the modeling of toxic amyloid_ion channels. Trends Biochem Sci 33:91-100.
    • (2008) Trends Biochem Sci , vol.33 , pp. 91-100
    • Jang, H.1    Zheng, J.2    Lal, R.3    Nussinov, R.4
  • 49
    • 78449282609 scopus 로고    scopus 로고
    • Metals, oxidative stress and neurodegenerative disorders
    • Jomova K, Vondrakova D, Lawson M, Valko M. 2010. Metals, oxidative stress and neurodegenerative disorders. Mol Cell Biochem 345:91-104.
    • (2010) Mol Cell Biochem , vol.345 , pp. 91-104
    • Jomova, K.1    Vondrakova, D.2    Lawson, M.3    Valko, M.4
  • 51
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: Current status
    • Kagan BL, Hirakura Y, Azimov R, Azimova R, Lin MC. 2002. The channel hypothesis of Alzheimer's disease: Current status. Peptides 23:1311-1315.
    • (2002) Peptides , vol.23 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.C.5
  • 52
    • 0028009186 scopus 로고
    • Platelet-activating factor as a potential retrograde messenger in CA1 hippocampal long-term potentiation
    • Kato K, Clark GD, Bazan NG, Zorumski CF. 1994. Platelet-activating factor as a potential retrograde messenger in CA1 hippocampal long-term potentiation. Nature 367:175-179.
    • (1994) Nature , vol.367 , pp. 175-179
    • Kato, K.1    Clark, G.D.2    Bazan, N.G.3    Zorumski, C.F.4
  • 53
    • 0034640372 scopus 로고    scopus 로고
    • Alzheimer's b-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line
    • Kawahara M, Kuroda Y, Arispe N, Rojas E. 2000. Alzheimer's b-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. J Biol Chem 275:14077-14083.
    • (2000) J Biol Chem , vol.275 , pp. 14077-14083
    • Kawahara, M.1    Kuroda, Y.2    Arispe, N.3    Rojas, E.4
  • 55
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze MD, Bitan G, Teplow DB. 2002. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J Neurosci Res 69:567-577.
    • (2002) J Neurosci Res , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 56
    • 38049134367 scopus 로고    scopus 로고
    • PLA(2) signaling is involved in calpain-mediated degradation of synaptic dihydropyrimidinase-like 3 protein in response to NMDA excitotoxicity
    • Kowara R, Moraleja KL, Chakravarthy B. 2008. PLA(2) signaling is involved in calpain-mediated degradation of synaptic dihydropyrimidinase-like 3 protein in response to NMDA excitotoxicity. Neurosci Lett 430:197-202.
    • (2008) Neurosci Lett , vol.430 , pp. 197-202
    • Kowara, R.1    Moraleja, K.L.2    Chakravarthy, B.3
  • 58
    • 0029665941 scopus 로고    scopus 로고
    • Activation of phospholipase A2 by amyloid beta-peptides in vitro
    • Lehtonen JY, Holopainen JM, Kinnunen PK. 1996. Activation of phospholipase A2 by amyloid beta-peptides in vitro. Biochemistry 35:9407-9414.
    • (1996) Biochemistry , vol.35 , pp. 9407-9414
    • Lehtonen, J.Y.1    Holopainen, J.M.2    Kinnunen, P.K.3
  • 59
    • 0038607977 scopus 로고    scopus 로고
    • The epidermal platelet-activating factor receptor augments chemotherapy-induced apoptosis in human carcinoma cell lines
    • Li T, Southall MD, Yi Q, Pei Y, Lewis D, Al-Hassani M, Spandau D, Travers JB. 2003. The epidermal platelet-activating factor receptor augments chemotherapy-induced apoptosis in human carcinoma cell lines. J Biol Chem 278:16614-16621.
    • (2003) J Biol Chem , vol.278 , pp. 16614-16621
    • Li, T.1    Southall, M.D.2    Yi, Q.3    Pei, Y.4    Lewis, D.5    Al-Hassani, M.6    Spandau, D.7    Travers, J.B.8
  • 60
    • 67449123350 scopus 로고    scopus 로고
    • Protection of PMS777, a new AChE inhibitor with PAF antagonism, against amyloid-beta-induced neuronal apoptosis and neuroinflammation
    • Li J, Hu J, Shao B, Zhou W, Cui Y, Dong C, Ezoulin JM, Zhu X, Ding W, Heymans F, Chen H. 2009. Protection of PMS777, a new AChE inhibitor with PAF antagonism, against amyloid-beta-induced neuronal apoptosis and neuroinflammation. Cell Mol Neurobiol 29:589-595.
    • (2009) Cell Mol Neurobiol , vol.29 , pp. 589-595
    • Li, J.1    Hu, J.2    Shao, B.3    Zhou, W.4    Cui, Y.5    Dong, C.6    Ezoulin, J.M.7    Zhu, X.8    Ding, W.9    Heymans, F.10    Chen, H.11
  • 61
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid like fibrils by self association of a partially unfolded fibronectin type III module
    • Litvinovich SV, Brew SA, Aota S, Akiyama SK, Haudenschild C, Ingham KC. 1998. Formation of amyloid like fibrils by self association of a partially unfolded fibronectin type III module. J Mol Biol 280:245-258.
    • (1998) J Mol Biol , vol.280 , pp. 245-258
    • Litvinovich, S.V.1    Brew, S.A.2    Aota, S.3    Akiyama, S.K.4    Haudenschild, C.5    Ingham, K.C.6
  • 62
    • 0034905715 scopus 로고    scopus 로고
    • Selective and biphasic effect of the membrane lipid peroxidation product 4-hydroxy-2,3-nonenal on N-methyl-D-aspartate channels
    • Lu C, Chan SL, Haughey N, Lee WT, Mattson MP. 2001. Selective and biphasic effect of the membrane lipid peroxidation product 4-hydroxy-2, 3-nonenal on N-methyl-D-aspartate channels. J Neurochem 78:577-589.
    • (2001) J Neurochem , vol.78 , pp. 577-589
    • Lu, C.1    Chan, S.L.2    Haughey, N.3    Lee, W.T.4    Mattson, M.P.5
  • 63
    • 0036211150 scopus 로고    scopus 로고
    • Platelet-activating factor (PAF) enhances apoptosis induced by ultraviolet radiation in corneal epithelial cells through cytochrome c-caspase activation
    • Ma X, Bazan HE. 2001. Platelet-activating factor (PAF) enhances apoptosis induced by ultraviolet radiation in corneal epithelial cells through cytochrome c-caspase activation. Curr Eye Res 23:326-335.
    • (2001) Curr Eye Res , vol.23 , pp. 326-335
    • Ma, X.1    Bazan, H.E.2
  • 65
    • 84863459157 scopus 로고    scopus 로고
    • New developments on the role of NMDA receptors in Alzheimer's disease
    • Malinow R. 2012. New developments on the role of NMDA receptors in Alzheimer's disease. Curr Opi Neurobiol 22:559-563.
    • (2012) Curr Opi Neurobiol , vol.22 , pp. 559-563
    • Malinow, R.1
  • 66
    • 0028981159 scopus 로고
    • Amyloid beta-peptide impairs ion-motive ATPase activities: Evidence for a role in loss of neuronal Ca2+ homeostasis and cell death
    • Mark RJ, Hensley K, Butterfield DA, Mattson MP. 1995. Amyloid beta-peptide impairs ion-motive ATPase activities: Evidence for a role in loss of neuronal Ca2+ homeostasis and cell death. J Neurosci 15:6239-6249.
    • (1995) J Neurosci , vol.15 , pp. 6239-6249
    • Mark, R.J.1    Hensley, K.2    Butterfield, D.A.3    Mattson, M.P.4
  • 67
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson MP. 2004. Pathways towards and away from Alzheimer's disease. Nature 430:631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 68
    • 34249092704 scopus 로고    scopus 로고
    • Calcium and neurodegeneration
    • Mattson MP. 2007. Calcium and neurodegeneration. Aging Cell 6:337-350.
    • (2007) Aging Cell , vol.6 , pp. 337-350
    • Mattson, M.P.1
  • 69
    • 4444333049 scopus 로고    scopus 로고
    • Cyclooxygenase-2 (COX-2) in inflammatory and degenerative brain diseases
    • Minghetti L. 2004. Cyclooxygenase-2 (COX-2) in inflammatory and degenerative brain diseases. J Neuropathol Exp Neurol 63:901-910.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 901-910
    • Minghetti, L.1
  • 70
    • 0035876476 scopus 로고    scopus 로고
    • Glutamate release and neuronal damage in ischemia
    • Nishizawa Y. 2001. Glutamate release and neuronal damage in ischemia. Life Sci 69:369-381.
    • (2001) Life Sci , vol.69 , pp. 369-381
    • Nishizawa, Y.1
  • 71
    • 0030891741 scopus 로고    scopus 로고
    • Involvement of platelet-activating factor (PAF) in glutamate neurotoxicity in rat neuronal cultures
    • Nogami K, Hirashima Y, Endo S, Takaku A. 1997. Involvement of platelet-activating factor (PAF) in glutamate neurotoxicity in rat neuronal cultures. Brain Res 754:72-78.
    • (1997) Brain Res , vol.754 , pp. 72-78
    • Nogami, K.1    Hirashima, Y.2    Endo, S.3    Takaku, A.4
  • 72
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V, Bocharova OV, Bronstein I, Baskakov IV. 2006. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J Biol Chem 281:13828-13836.
    • (2006) J Biol Chem , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 74
    • 0037046151 scopus 로고    scopus 로고
    • Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
    • Padrick SB, Miranker AD. 2002. Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry 41:4694-4703.
    • (2002) Biochemistry , vol.41 , pp. 4694-4703
    • Padrick, S.B.1    Miranker, A.D.2
  • 75
    • 28944433479 scopus 로고    scopus 로고
    • The changing face of glucagon fibrillation: Structural polymorphism and conformational imprinting
    • Pedersen JS, Dikov D, Flink JL, Hjuler HA, Christiansen G, Otzen D. 2005. The changing face of glucagon fibrillation: Structural polymorphism and conformational imprinting J Mol Biol 355:501-523.
    • (2005) J Mol Biol , vol.355 , pp. 501-523
    • Pedersen, J.S.1    Dikov, D.2    Flink, J.L.3    Hjuler, H.A.4    Christiansen, G.5    Otzen, D.6
  • 76
    • 57649223693 scopus 로고    scopus 로고
    • Generic interaction of pre-fibrillar amyloid aggregates with NMDA and AMPA receptors results in free Ca2+ increase in primary neuronal cells
    • Pellistri F, Bucciantini M, Relini A, Gliozzi A, Robello M, Stefani M. 2008. Generic interaction of pre-fibrillar amyloid aggregates with NMDA and AMPA receptors results in free Ca2+ increase in primary neuronal cells. J Biol Chem 283:29950-29960.
    • (2008) J Biol Chem , vol.283 , pp. 29950-29960
    • Pellistri, F.1    Bucciantini, M.2    Relini, A.3    Gliozzi, A.4    Robello, M.5    Stefani, M.6
  • 79
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • Reixach N, Deechongkit S, Jiang X, Kelly JW, Buxbaum JN. 2004. Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc Natl Acad Sci USA 101:2817-2822.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 80
    • 34548611214 scopus 로고    scopus 로고
    • Platelet activating factor-induced neuronal apoptosis is initiated independently of its G-protein coupled PAF receptor and is inhibited by the benzoate orsellinic acid
    • Ryan SD, Harris CS, Mo F, Lee H, Hou ST, Bazan NG, Haddad PS, Arnason JT, Bennett SA. 2007. Platelet activating factor-induced neuronal apoptosis is initiated independently of its G-protein coupled PAF receptor and is inhibited by the benzoate orsellinic acid. J Neurochem 103:88-97.
    • (2007) J Neurochem , vol.103 , pp. 88-97
    • Ryan, S.D.1    Harris, C.S.2    Mo, F.3    Lee, H.4    Hou, S.T.5    Bazan, N.G.6    Haddad, P.S.7    Arnason, J.T.8    Bennett, S.A.9
  • 81
    • 58149393210 scopus 로고    scopus 로고
    • Heterogeneity in the sn-1 carbon chain of platelet-activating factor glycerophospholipids determines pro- or anti-apoptotic signaling in primary neurons
    • Ryan SD, Harris CS, Carswell CL, Baenziger JE, Bennett SA. 2008. Heterogeneity in the sn-1 carbon chain of platelet-activating factor glycerophospholipids determines pro- or anti-apoptotic signaling in primary neurons. J Lipid Res 49:2250-2258.
    • (2008) J Lipid Res , vol.49 , pp. 2250-2258
    • Ryan, S.D.1    Harris, C.S.2    Carswell, C.L.3    Baenziger, J.E.4    Bennett, S.A.5
  • 85
    • 27344434855 scopus 로고    scopus 로고
    • Platelet-activating factor enhancement of calcium influx and interleukin-6 expression, but not production, in human microglia
    • Sattayaprasert P, Choi HB, Chongthammakun S, McLarnon JG. 2005. Platelet-activating factor enhancement of calcium influx and interleukin-6 expression, but not production, in human microglia. J Neuroinflam 2:11.
    • (2005) J Neuroinflam , vol.2 , pp. 11
    • Sattayaprasert, P.1    Choi, H.B.2    Chongthammakun, S.3    McLarnon, J.G.4
  • 86
    • 77955701756 scopus 로고    scopus 로고
    • Synaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating property
    • Sepulveda FJ, Parodi J, Peoples RW, Opazo C, Aguayo LG. 2010. Synaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating property. PLoS ONE 5:e11820.
    • (2010) PLoS ONE , vol.5
    • Sepulveda, F.J.1    Parodi, J.2    Peoples, R.W.3    Opazo, C.4    Aguayo, L.G.5
  • 88
    • 70350365853 scopus 로고    scopus 로고
    • NADPH oxidase mediates b-amyloid peptide-induced activation of ERK in hippocampal organotypic cultures
    • Serrano F, Chang A, Hernandez C, Pautler RG, Sweatt JD, Klann E. 2009. NADPH oxidase mediates b-amyloid peptide-induced activation of ERK in hippocampal organotypic cultures. Mol Brain 2:31.
    • (2009) Mol Brain , vol.2 , pp. 31
    • Serrano, F.1    Chang, A.2    Hernandez, C.3    Pautler, R.G.4    Sweatt, J.D.5    Klann, E.6
  • 89
  • 90
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman MY, Goldberg AL. 2001. Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases. Neuron 29:15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 91
    • 77952875785 scopus 로고    scopus 로고
    • 2 and PAF mediate Abeta1-42-induced Ca2+ dyshomeostasis that is blocked by EGb761
    • 2 and PAF mediate Abeta1-42-induced Ca2+ dyshomeostasis that is blocked by EGb761. Neurochem Int 56:893-905.
    • (2010) Neurochem Int , vol.56 , pp. 893-905
    • Shi, C.1    Wu, F.2    Xu, J.3
  • 92
    • 34250343830 scopus 로고    scopus 로고
    • A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase
    • Shindou H, Hishikawa D, Nakanishi H, Harayama T, Ishii S, Taguchi R, Shimizu T. 2007. A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase. J Biol Chem 282:6532-6539.
    • (2007) J Biol Chem , vol.282 , pp. 6532-6539
    • Shindou, H.1    Hishikawa, D.2    Nakanishi, H.3    Harayama, T.4    Ishii, S.5    Taguchi, R.6    Shimizu, T.7
  • 93
    • 0026550980 scopus 로고
    • Platelet-activating factor receptor and signal transduction mechanisms
    • Shukla SD. 1992. Platelet-activating factor receptor and signal transduction mechanisms. FASEB J 6:2296-2301.
    • (1992) FASEB J , vol.6 , pp. 2296-2301
    • Shukla, S.D.1
  • 94
    • 78649315112 scopus 로고    scopus 로고
    • Amyloid fibril protein nomenclature: 2010. Recommendations of the nomenclature committee of the International Society of Amyloidosis
    • Sipe JD, Benson MD, Buxbaum JN, Ikeda S, Merlini G, Saraiva MJ, Westermark P. 2010. Amyloid fibril protein nomenclature: 2010. Recommendations of the nomenclature committee of the International Society of Amyloidosis. Amyloid 17:101-104.
    • (2010) Amyloid , vol.17 , pp. 101-104
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5    Saraiva, M.J.6    Westermark, P.7
  • 95
    • 78249258414 scopus 로고    scopus 로고
    • Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: Effect of tetracycline and trehalose
    • Sirangelo I, Irace G. 2010. Inhibition of aggregate formation as therapeutic target in protein misfolding diseases: Effect of tetracycline and trehalose. Expert Opin Ther Targets 14:1311-1321.
    • (2010) Expert Opin Ther Targets , vol.14 , pp. 1311-1321
    • Sirangelo, I.1    Irace, G.2
  • 97
    • 0028944870 scopus 로고
    • Platelet-activating factor: The biosynthetic and catabolic enzymes
    • Snyder F. 1995. Platelet-activating factor: The biosynthetic and catabolic enzymes. Biochem J 305:689-705.
    • (1995) Biochem J , vol.305 , pp. 689-705
    • Snyder, F.1
  • 100
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • Stefani M. 2004. Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world. Biochim Biophys Acta 1739:5-25.
    • (2004) Biochim Biophys Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 101
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein foldinf, misfolding diseases and biological evolution
    • Stefani M, Dobson CM. 2003. Protein aggregation and aggregate toxicity: New insights into protein foldinf, misfolding diseases and biological evolution. J Mol Med 81:679-699.
    • (2003) J Mol Med , vol.81 , pp. 679-699
    • Stefani, M.1    Dobson, C.M.2
  • 102
    • 0029657725 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 (cPLA2) immunoreactivity is elevated in Alzheimer's disease brain
    • Stephenson DT, Lemere CA, Selkoe DJ, Clemens JA. 1996. Cytosolic phospholipase A2 (cPLA2) immunoreactivity is elevated in Alzheimer's disease brain. Neurobiol Dis 3:51-63.
    • (1996) Neurobiol Dis , vol.3 , pp. 51-63
    • Stephenson, D.T.1    Lemere, C.A.2    Selkoe, D.J.3    Clemens, J.A.4
  • 103
    • 1242297090 scopus 로고    scopus 로고
    • Phospholipase A2 in the central nervous system: Implications for neurodegenerative diseases
    • Sun GY, Xu J, Jensen MD, Simonyi A. 2004. Phospholipase A2 in the central nervous system: Implications for neurodegenerative diseases. J Lipid Res 45:205-213.
    • (2004) J Lipid Res , vol.45 , pp. 205-213
    • Sun, G.Y.1    Xu, J.2    Jensen, M.D.3    Simonyi, A.4
  • 104
    • 34548121631 scopus 로고    scopus 로고
    • The roles of NADPH oxidase and phospholipases A2 in oxidative and inflammatory responses in neurodegenerative diseases
    • Sun GY, Horrocks LA, Farooqui AA. 2007. The roles of NADPH oxidase and phospholipases A2 in oxidative and inflammatory responses in neurodegenerative diseases. J Neurochem 103:1-16.
    • (2007) J Neurochem , vol.103 , pp. 1-16
    • Sun, G.Y.1    Horrocks, L.A.2    Farooqui, A.A.3
  • 105
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M, Blake C. 1997. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv Protein Chem 50:123-159.
    • (1997) Adv Protein Chem , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 107
    • 0034971060 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase 3 beta (GSK-3beta) by platelet activating factor mediates migration and cell death in cerebellar granule neurons
    • Tong N, Sanchez JF, Maggirwar SB, Ramirez SH, Guo H, Dewhurst S, Gelbard HA. 2001. Activation of glycogen synthase kinase 3 beta (GSK-3beta) by platelet activating factor mediates migration and cell death in cerebellar granule neurons. Eur J Neurosci 13:1913-1922.
    • (2001) Eur J Neurosci , vol.13 , pp. 1913-1922
    • Tong, N.1    Sanchez, J.F.2    Maggirwar, S.B.3    Ramirez, S.H.4    Guo, H.5    Dewhurst, S.6    Gelbard, H.A.7
  • 108
    • 0025819956 scopus 로고
    • A coenzyme A-independent transacylase is linked to the formation of platelet-activating factor (PAF) by generating the lyso-PAF intermediate in the remodeling pathway
    • Uemura Y, Lee TC, Snyder F. 1991. A coenzyme A-independent transacylase is linked to the formation of platelet-activating factor (PAF) by generating the lyso-PAF intermediate in the remodeling pathway. J Biol Chem 266:8268-8272.
    • (1991) J Biol Chem , vol.266 , pp. 8268-8272
    • Uemura, Y.1    Lee, T.C.2    Snyder, F.3
  • 109
    • 77954358960 scopus 로고    scopus 로고
    • Mysterious oligomerization of the amyloidogenic proteins
    • Uversky VN. 2010. Mysterious oligomerization of the amyloidogenic proteins. FEBS J 277:2940-2953.
    • (2010) FEBS J , vol.277 , pp. 2940-2953
    • Uversky, V.N.1
  • 110
    • 1442351177 scopus 로고    scopus 로고
    • Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease
    • Verdier Y, Penke B. 2004. Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease. Curr Protein Pept Sci 5:19-31.
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 19-31
    • Verdier, Y.1    Penke, B.2
  • 111
    • 79961228576 scopus 로고    scopus 로고
    • Opposing synaptic regulation of amyloid-beta metabolism by NMDA receptors in vivo
    • Verges DK, Restivo JL, Goebel WD, Holtzman DM, Cirrito JR. 2011. Opposing synaptic regulation of amyloid-beta metabolism by NMDA receptors in vivo. J Neurosci 31:11328-11337.
    • (2011) J Neurosci , vol.31 , pp. 11328-11337
    • Verges, D.K.1    Restivo, J.L.2    Goebel, W.D.3    Holtzman, D.M.4    Cirrito, J.R.5
  • 112
    • 38949216069 scopus 로고    scopus 로고
    • Effect of trehalose on W7FW14F apomyoglobin and insulin fibrillization: New insight into inhibition activity
    • Vilasi S, Iannuzzi C, Portaccio M, Irace G, Sirangelo I. 2008. Effect of trehalose on W7FW14F apomyoglobin and insulin fibrillization: New insight into inhibition activity. Biochemistry 47:1789-1796.
    • (2008) Biochemistry , vol.47 , pp. 1789-1796
    • Vilasi, S.1    Iannuzzi, C.2    Portaccio, M.3    Irace, G.4    Sirangelo, I.5
  • 114
    • 79960244421 scopus 로고    scopus 로고
    • Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro
    • Vilasi S, Sarcina R, Maritato R, De Simone A, Irace G, Sirangelo I. 2011. Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro. PLoS ONE 6:e22076.
    • (2011) PLoS ONE , vol.6
    • Vilasi, S.1    Sarcina, R.2    Maritato, R.3    De Simone, A.4    Irace, G.5    Sirangelo, I.6
  • 115
    • 34248190279 scopus 로고    scopus 로고
    • A β oligomers-A decade of discovery
    • Walsh DM, Selkoe DJ. 2007. A β oligomers-A decade of discovery. J Neurochem 101:1172-1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 116
    • 0348140940 scopus 로고    scopus 로고
    • Regulation of c-Jun N-terminal kinase activation in hydrogen peroxide induced neurotoxicity
    • Wang W, Hou XY, Gao C, Liu Y, Zong YY, Zhang GY. 2003. Regulation of c-Jun N-terminal kinase activation in hydrogen peroxide induced neurotoxicity. J Neurocytol 32:143-151.
    • (2003) J Neurocytol , vol.32 , pp. 143-151
    • Wang, W.1    Hou, X.Y.2    Gao, C.3    Liu, Y.4    Zong, Y.Y.5    Zhang, G.Y.6
  • 117
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid beta-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang Q, Walsh DM, Rowan MJ, Selkoe DJ, Anwyl R. 2004. Block of long-term potentiation by naturally secreted and synthetic amyloid beta-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J Neurosci 24:3370-3378.
    • (2004) J Neurosci , vol.24 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 118
    • 0032144789 scopus 로고    scopus 로고
    • Molecular mechanisms that underlie structural and functional changes at the postsynaptic membrane during synaptic plasticity
    • Wheal HV, Chen Y, Mitchell J, Schachner M, Maerz W, Wieland H, Van Rossum D, Kirsch J. 1998. Molecular mechanisms that underlie structural and functional changes at the postsynaptic membrane during synaptic plasticity. Prog Neurobiol 55:611-640.
    • (1998) Prog Neurobiol , vol.55 , pp. 611-640
    • Wheal, H.V.1    Chen, Y.2    Mitchell, J.3    Schachner, M.4    Maerz, W.5    Wieland, H.6    Van Rossum, D.7    Kirsch, J.8
  • 119
    • 0027419209 scopus 로고
    • Longterm potentiation in the hippocampus induced by platelet-activating factor
    • Wieraszko A, Li G, Kornecki E, Hogan MV, Ehrlich YH. 1993. Longterm potentiation in the hippocampus induced by platelet-activating factor. Neuron 10:553-557.
    • (1993) Neuron , vol.10 , pp. 553-557
    • Wieraszko, A.1    Li, G.2    Kornecki, E.3    Hogan, M.V.4    Ehrlich, Y.H.5
  • 120
    • 1542320274 scopus 로고    scopus 로고
    • Involvement of the NMDA receptor/nitric oxide signal pathway in platelet-activating factor-induced neurotoxicity
    • Xu Y, Tao YX. 2004. Involvement of the NMDA receptor/nitric oxide signal pathway in platelet-activating factor-induced neurotoxicity. Neuroreport 15:263-266.
    • (2004) Neuroreport , vol.15 , pp. 263-266
    • Xu, Y.1    Tao, Y.X.2
  • 121
    • 77955060978 scopus 로고    scopus 로고
    • Membrane biophysics and mechanics in Alzheimer's disease
    • Yang X, Askarova S, Lee JC. 2010. Membrane biophysics and mechanics in Alzheimer's disease. Mol Neurobiol 41:138-148.
    • (2010) Mol Neurobiol , vol.41 , pp. 138-148
    • Yang, X.1    Askarova, S.2    Lee, J.C.3


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