메뉴 건너뛰기




Volumn 6, Issue 1, 2011, Pages

Microarray analysis on human neuroblastoma cells exposed to aluminum, β 1-42-Amyloid or the β1-42-Amyloid aluminum complex

Author keywords

[No Author keywords available]

Indexed keywords

ALUMINUM; AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); CALCIUM; GLUTAMIC ACID; PEPTIDE FRAGMENT;

EID: 79551524309     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015965     Document Type: Article
Times cited : (28)

References (109)
  • 2
    • 0026573467 scopus 로고
    • Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study
    • Good PF, Perl DP, Bierer LM, Schmeidler J (1992) Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: a laser microprobe (LAMMA) study. Ann Neurol 31: 286-292.
    • (1992) Ann Neurol , vol.31 , pp. 286-292
    • Good, P.F.1    Perl, D.P.2    Bierer, L.M.3    Schmeidler, J.4
  • 5
    • 3042666730 scopus 로고    scopus 로고
    • Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Abeta42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease
    • House E, Collingwood J, Khan A, Korchazkina O, Berthon G, et al. (2004) Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Abeta42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease. J Alzheimers Dis 6: 291-301.
    • (2004) J Alzheimers Dis , vol.6 , pp. 291-301
    • House, E.1    Collingwood, J.2    Khan, A.3    Korchazkina, O.4    Berthon, G.5
  • 6
    • 23844434035 scopus 로고    scopus 로고
    • Aluminum-triggered structural modifications and aggregation of beta-amyloids
    • Ricchelli F, Drago D, Filippi B, Tognon G, Zatta P (2005) Aluminum-triggered structural modifications and aggregation of beta-amyloids. Cell Mol Life Sci 62: 1724-1733.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1724-1733
    • Ricchelli, F.1    Drago, D.2    Filippi, B.3    Tognon, G.4    Zatta, P.5
  • 7
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush AI (2003) The metallobiology of Alzheimer's disease. Trends Neurosci 26: 207-214.
    • (2003) Trends Neurosci , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 8
    • 39649088251 scopus 로고    scopus 로고
    • Potential pathogenic role of beta-amyloid(1-42)-aluminum complex in Alzheimer's disease
    • Drago D, Bettella M, Bolognin S, Cendron L, Scancar J, et al. (2008) Potential pathogenic role of beta-amyloid(1-42)-aluminum complex in Alzheimer's disease. Int J Biochem Cell Biol 40: 731-746.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 731-746
    • Drago, D.1    Bettella, M.2    Bolognin, S.3    Cendron, L.4    Scancar, J.5
  • 9
    • 1242341923 scopus 로고    scopus 로고
    • Incipient Alzheimer's disease: Microarray correlation analyses reveal major transcriptional and tumor suppressor responses
    • Blalock EM, Geddes JW, Chen KC, Porter NM, Markesbery WR, et al. (2004) Incipient Alzheimer's disease: microarray correlation analyses reveal major transcriptional and tumor suppressor responses. Proc Natl Acad Sci U S A 101: 2173-2178.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2173-2178
    • Blalock, E.M.1    Geddes, J.W.2    Chen, K.C.3    Porter, N.M.4    Markesbery, W.R.5
  • 11
    • 7444225172 scopus 로고    scopus 로고
    • Reference genes identified in SH-SY5Y cells using custom-made gene arrays with validation by quantitative polymerase chain reaction
    • Hoerndli FJ, Toigo M, Schild A, Gotz J, Day PJ (2004) Reference genes identified in SH-SY5Y cells using custom-made gene arrays with validation by quantitative polymerase chain reaction. Anal Biochem 335: 30-41.
    • (2004) Anal Biochem , vol.335 , pp. 30-41
    • Hoerndli, F.J.1    Toigo, M.2    Schild, A.3    Gotz, J.4    Day, P.J.5
  • 12
    • 32444445371 scopus 로고    scopus 로고
    • Synergistic effects of iron and aluminum on stress-related gene expression in primary human neural cells
    • discussion
    • Alexandrov PN, Zhao Y, Pogue AI, Tarr MA, Kruck TP, et al. (2005) Synergistic effects of iron and aluminum on stress-related gene expression in primary human neural cells. J Alzheimers Dis 8: 117-127; discussion 209-115.
    • (2005) J Alzheimers Dis , vol.8
    • Alexandrov, P.N.1    Zhao, Y.2    Pogue, A.I.3    Tarr, M.A.4    Kruck, T.P.5
  • 13
    • 0031733707 scopus 로고    scopus 로고
    • Run-on gene transcription in human neocortical nuclei. Inhibition by nanomolar aluminum and implications for neurodegenerative disease
    • Lukiw WJ, LeBlanc HJ, Carver LA, McLachlan DR, Bazan NG (1998) Run-on gene transcription in human neocortical nuclei. Inhibition by nanomolar aluminum and implications for neurodegenerative disease. J Mol Neurosci 11: 67-78.
    • (1998) J Mol Neurosci , vol.11 , pp. 67-78
    • Lukiw, W.J.1    Leblanc, H.J.2    Carver, L.A.3    McLachlan, D.R.4    Bazan, N.G.5
  • 14
    • 24344482909 scopus 로고    scopus 로고
    • Nanomolar aluminum induces proinflammatory and pro-apoptotic gene expression in human brain cells in primary culture
    • Lukiw WJ, Percy ME, Kruck TP (2005) Nanomolar aluminum induces proinflammatory and pro-apoptotic gene expression in human brain cells in primary culture. J Inorg Biochem 99: 1895-1898.
    • (2005) J Inorg Biochem , vol.99 , pp. 1895-1898
    • Lukiw, W.J.1    Percy, M.E.2    Kruck, T.P.3
  • 15
    • 63849213473 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor signalling: Roles in Alzheimer's disease and amyloid neuroprotection
    • Buckingham SD, Jones AK, Brown LA, Sattelle DB (2009) Nicotinic acetylcholine receptor signalling: roles in Alzheimer's disease and amyloid neuroprotection. Pharmacol Rev 61: 39-61.
    • (2009) Pharmacol Rev , vol.61 , pp. 39-61
    • Buckingham, S.D.1    Jones, A.K.2    Brown, L.A.3    Sattelle, D.B.4
  • 16
    • 0028051292 scopus 로고
    • Molecular cloning of human calmitine, a mitochondrial calcium binding protein, reveals identity with calsequestrine
    • Bataille N, Schmitt N, Aumercier-Maes P, Ollivier B, Lucas-Heron B, et al. (1994) Molecular cloning of human calmitine, a mitochondrial calcium binding protein, reveals identity with calsequestrine. Biochem Biophys Res Commun 203: 1477-1482.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 1477-1482
    • Bataille, N.1    Schmitt, N.2    Aumercier-Maes, P.3    Ollivier, B.4    Lucas-Heron, B.5
  • 17
    • 77249158836 scopus 로고    scopus 로고
    • Amyloid beta induces the morphological neurodegenerative triad of spine loss, dendritic simplification, and neuritic dystrophies through calcineurin activation
    • Wu HY, Hudry E, Hashimoto T, Kuchibhotla K, Rozkalne A, et al. (2010) Amyloid beta induces the morphological neurodegenerative triad of spine loss, dendritic simplification, and neuritic dystrophies through calcineurin activation. J Neurosci 30: 2636-2649.
    • (2010) J Neurosci , vol.30 , pp. 2636-2649
    • Wu, H.Y.1    Hudry, E.2    Hashimoto, T.3    Kuchibhotla, K.4    Rozkalne, A.5
  • 18
    • 0035831033 scopus 로고    scopus 로고
    • Inducible and reversible enhancement of learning, memory, and long-term potentiation by genetic inhibition of calcineurin
    • Malleret G, Haditsch U, Genoux D, Jones MW, Bliss TV, et al. (2001) Inducible and reversible enhancement of learning, memory, and long-term potentiation by genetic inhibition of calcineurin. Cell 104: 675-686.
    • (2001) Cell , vol.104 , pp. 675-686
    • Malleret, G.1    Haditsch, U.2    Genoux, D.3    Jones, M.W.4    Bliss, T.V.5
  • 19
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • Putney JW, Jr. (1986) A model for receptor-regulated calcium entry. Cell Calcium 7: 1-12.
    • (1986) Cell Calcium , vol.7 , pp. 1-12
    • Putney Jr., J.W.1
  • 20
    • 0036679142 scopus 로고    scopus 로고
    • Prominent neurodegeneration and increased plaque formation in complementinhibited Alzheimer's mice
    • Wyss-Coray T, Yan F, Lin AH, Lambris JD, Alexander JJ, et al. (2002) Prominent neurodegeneration and increased plaque formation in complementinhibited Alzheimer's mice. Proc Natl Acad Sci U S A 99: 10837-10842.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10837-10842
    • Wyss-Coray, T.1    Yan, F.2    Lin, A.H.3    Lambris, J.D.4    Alexander, J.J.5
  • 21
    • 34547512353 scopus 로고    scopus 로고
    • Functional specialization of beta-arrestin interactions revealed by proteomic analysis
    • Xiao K, McClatchy DB, Shukla AK, Zhao Y, Chen M, et al. (2007) Functional specialization of beta-arrestin interactions revealed by proteomic analysis. Proc Natl Acad Sci U S A 104: 12011-12016.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12011-12016
    • Xiao, K.1    McClatchy, D.B.2    Shukla, A.K.3    Zhao, Y.4    Chen, M.5
  • 22
    • 33846901907 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors: Intracellular signaling pathways
    • Gerber U, Gee CE, Benquet P (2007) Metabotropic glutamate receptors: intracellular signaling pathways. Curr Opin Pharmacol 7: 56-61.
    • (2007) Curr Opin Pharmacol , vol.7 , pp. 56-61
    • Gerber, U.1    Gee, C.E.2    Benquet, P.3
  • 23
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran G, Koo EH (2008) Amyloid precursor protein trafficking, processing, and function. J Biol Chem 283: 29615-29619.
    • (2008) J Biol Chem , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 24
    • 0030779726 scopus 로고    scopus 로고
    • Amyloid precursor-like protein 1 accumulates in neuritic plaques in Alzheimer's disease
    • Bayer TA, Paliga K, Weggen S, Wiestler OD, Beyreuther K, et al. (1997) Amyloid precursor-like protein 1 accumulates in neuritic plaques in Alzheimer's disease. Acta Neuropathol 94: 519-524.
    • (1997) Acta Neuropathol , vol.94 , pp. 519-524
    • Bayer, T.A.1    Paliga, K.2    Weggen, S.3    Wiestler, O.D.4    Beyreuther, K.5
  • 25
    • 33646349010 scopus 로고    scopus 로고
    • Amyloid precursor-like protein 1 influences endocytosis and proteolytic processing of the amyloid precursor protein
    • Neumann S, Schobel S, Jager S, Trautwein A, Haass C, et al. (2006) Amyloid precursor-like protein 1 influences endocytosis and proteolytic processing of the amyloid precursor protein. J Biol Chem 281: 7583-7594.
    • (2006) J Biol Chem , vol.281 , pp. 7583-7594
    • Neumann, S.1    Schobel, S.2    Jager, S.3    Trautwein, A.4    Haass, C.5
  • 26
    • 34249851328 scopus 로고    scopus 로고
    • IGF-1-induced processing of the amyloid precursor protein family is mediated by different signaling pathways
    • Adlerz L, Holback S, Multhaup G, Iverfeldt K (2007) IGF-1-induced processing of the amyloid precursor protein family is mediated by different signaling pathways. J Biol Chem 282: 10203-10209.
    • (2007) J Biol Chem , vol.282 , pp. 10203-10209
    • Adlerz, L.1    Holback, S.2    Multhaup, G.3    Iverfeldt, K.4
  • 28
    • 70349969737 scopus 로고    scopus 로고
    • Nitric oxide as an initiator of brain lesions during the development of Alzheimer disease
    • Aliev G, Palacios HH, Lipsitt AE, Fischbach K, Lamb BT, et al. (2009) Nitric oxide as an initiator of brain lesions during the development of Alzheimer disease. Neurotox Res 16: 293-305.
    • (2009) Neurotox Res , vol.16 , pp. 293-305
    • Aliev, G.1    Palacios, H.H.2    Lipsitt, A.E.3    Fischbach, K.4    Lamb, B.T.5
  • 29
    • 76749139924 scopus 로고    scopus 로고
    • Earlystage inflammation and experimental therapy in transgenic models of the Alzheimer-like amyloid pathology
    • Cuello AC, Ferretti MT, Leon WC, Iulita MF, Melis T, et al. (2010) Earlystage inflammation and experimental therapy in transgenic models of the Alzheimer-like amyloid pathology. Neurodegener Dis 7: 96-98.
    • (2010) Neurodegener Dis , vol.7 , pp. 96-98
    • Cuello, A.C.1    Ferretti, M.T.2    Leon, W.C.3    Iulita, M.F.4    Melis, T.5
  • 30
    • 34249093924 scopus 로고    scopus 로고
    • Pathologically-activated therapeutics for neuroprotection: Mechanism of NMDA receptor block by memantine and S-nitrosylation
    • Lipton SA (2007) Pathologically-activated therapeutics for neuroprotection: mechanism of NMDA receptor block by memantine and S-nitrosylation. Curr Drug Targets 8: 621-632.
    • (2007) Curr Drug Targets , vol.8 , pp. 621-632
    • Lipton, S.A.1
  • 31
    • 0033546347 scopus 로고    scopus 로고
    • Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein
    • Sattler R, Xiong Z, Lu WY, Hafner M, MacDonald JF, et al. (1999) Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein. Science 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
  • 32
    • 67349129779 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis and Alzheimer's disease: An update
    • Wu F, Yao PJ (2009) Clathrin-mediated endocytosis and Alzheimer's disease: an update. Ageing Res Rev 8: 147-149.
    • (2009) Ageing Res Rev , vol.8 , pp. 147-149
    • Wu, F.1    Yao, P.J.2
  • 33
    • 33644560354 scopus 로고    scopus 로고
    • Glutamate receptor exocytosis and spine enlargement during chemically induced long-term potentiation
    • Kopec CD, Li B, Wei W, Boehm J, Malinow R (2006) Glutamate receptor exocytosis and spine enlargement during chemically induced long-term potentiation. J Neurosci 26: 2000-2009.
    • (2006) J Neurosci , vol.26 , pp. 2000-2009
    • Kopec, C.D.1    Li, B.2    Wei, W.3    Boehm, J.4    Malinow, R.5
  • 34
    • 29144487182 scopus 로고    scopus 로고
    • Synaptic activity regulates interstitial fluid amyloid-beta levels in vivo
    • Cirrito JR, Yamada KA, Finn MB, Sloviter RS, Bales KR, et al. (2005) Synaptic activity regulates interstitial fluid amyloid-beta levels in vivo. Neuron 48: 913-922.
    • (2005) Neuron , vol.48 , pp. 913-922
    • Cirrito, J.R.1    Yamada, K.A.2    Finn, M.B.3    Sloviter, R.S.4    Bales, K.R.5
  • 35
    • 62249200515 scopus 로고    scopus 로고
    • Expression of inflammatory genes induced by beta-amyloid peptides in human brain endothelial cells and in Alzheimer's brain is mediated by the JNK-AP1 signaling pathway
    • Vukic V, Callaghan D, Walker D, Lue LF, Liu QY, et al. (2009) Expression of inflammatory genes induced by beta-amyloid peptides in human brain endothelial cells and in Alzheimer's brain is mediated by the JNK-AP1 signaling pathway. Neurobiol Dis 34: 95-106.
    • (2009) Neurobiol Dis , vol.34 , pp. 95-106
    • Vukic, V.1    Callaghan, D.2    Walker, D.3    Lue, L.F.4    Liu, Q.Y.5
  • 36
    • 34347358646 scopus 로고    scopus 로고
    • JNK signalling: A possible target to prevent neurodegeneration
    • Borsello T, Forloni G (2007) JNK signalling: a possible target to prevent neurodegeneration. Curr Pharm Des 13: 1875-1886.
    • (2007) Curr Pharm Des , vol.13 , pp. 1875-1886
    • Borsello, T.1    Forloni, G.2
  • 37
    • 33646862834 scopus 로고    scopus 로고
    • Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration
    • Chang KA, Kim HS, Ha TY, Ha JW, Shin KY, et al. (2006) Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration. Mol Cell Biol 26: 4327-4338.
    • (2006) Mol Cell Biol , vol.26 , pp. 4327-4338
    • Chang, K.A.1    Kim, H.S.2    Ha, T.Y.3    Ha, J.W.4    Shin, K.Y.5
  • 38
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas G (2002) Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat Rev Mol Cell Biol 3: 753-766.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 753-766
    • Thomas, G.1
  • 39
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum JD, Liu KN, Luo Y, Slack JL, Stocking KL, et al. (1998) Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 273: 27765-27767.
    • (1998) J Biol Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5
  • 40
    • 0034528425 scopus 로고    scopus 로고
    • Alphasecretase activity of the disintegrin metalloprotease ADAM 10. Influences of domain structure
    • Fahrenholz F, Gilbert S, Kojro E, Lammich S, Postina R (2000) Alphasecretase activity of the disintegrin metalloprotease ADAM 10. Influences of domain structure. Ann N Y Acad Sci 920: 215-222.
    • (2000) Ann N Y Acad Sci , vol.920 , pp. 215-222
    • Fahrenholz, F.1    Gilbert, S.2    Kojro, E.3    Lammich, S.4    Postina, R.5
  • 41
    • 33748427469 scopus 로고    scopus 로고
    • Furin is an endogenous regulator of alpha-secretase associated APP processing
    • Hwang EM, Kim SK, Sohn JH, Lee JY, Kim Y, et al. (2006) Furin is an endogenous regulator of alpha-secretase associated APP processing. Biochem Biophys Res Commun 349: 654-659.
    • (2006) Biochem Biophys Res Commun , vol.349 , pp. 654-659
    • Hwang, E.M.1    Kim, S.K.2    Sohn, J.H.3    Lee, J.Y.4    Kim, Y.5
  • 42
    • 0033595764 scopus 로고    scopus 로고
    • Neuronal activity-dependent cell survival mediated by transcription factor MEF2
    • Mao Z, Bonni A, Xia F, Nadal-Vicens M, Greenberg ME (1999) Neuronal activity-dependent cell survival mediated by transcription factor MEF2. Science 286: 785-790.
    • (1999) Science , vol.286 , pp. 785-790
    • Mao, Z.1    Bonni, A.2    Xia, F.3    Nadal-Vicens, M.4    Greenberg, M.E.5
  • 43
    • 33144467591 scopus 로고    scopus 로고
    • Activitydependent regulation of MEF2 transcription factors suppresses excitatory synapse number
    • Flavell SW, Cowan CW, Kim TK, Greer PL, Lin Y, et al. (2006) Activitydependent regulation of MEF2 transcription factors suppresses excitatory synapse number. Science 311: 1008-1012.
    • (2006) Science , vol.311 , pp. 1008-1012
    • Flavell, S.W.1    Cowan, C.W.2    Kim, T.K.3    Greer, P.L.4    Lin, Y.5
  • 44
    • 34447326686 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor stimulates the transcriptional and neuroprotective activity of myocyte-enhancer factor 2C through an ERK1/2-RSK2 signaling cascade
    • Wang Y, Liu L, Xia Z (2007) Brain-derived neurotrophic factor stimulates the transcriptional and neuroprotective activity of myocyte-enhancer factor 2C through an ERK1/2-RSK2 signaling cascade. J Neurochem 102: 957-966.
    • (2007) J Neurochem , vol.102 , pp. 957-966
    • Wang, Y.1    Liu, L.2    Xia, Z.3
  • 45
    • 48249087704 scopus 로고    scopus 로고
    • MEF2C, a transcription factor that facilitates learning and memory by negative regulation of synapse numbers and function
    • Barbosa AC, Kim MS, Ertunc M, Adachi M, Nelson ED, et al. (2008) MEF2C, a transcription factor that facilitates learning and memory by negative regulation of synapse numbers and function. Proc Natl Acad Sci U S A 105: 9391-9396.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9391-9396
    • Barbosa, A.C.1    Kim, M.S.2    Ertunc, M.3    Adachi, M.4    Nelson, E.D.5
  • 46
    • 70149106202 scopus 로고    scopus 로고
    • Nuclear calcium signaling controls expression of a large gene pool: Identification of a gene program for acquired neuroprotection induced by synaptic activity
    • Zhang SJ, Zou M, Lu L, Lau D, Ditzel DA, et al. (2009) Nuclear calcium signaling controls expression of a large gene pool: identification of a gene program for acquired neuroprotection induced by synaptic activity. PLoS Genet 5: e1000604.
    • (2009) PLoS Genet , vol.5
    • Zhang, S.J.1    Zou, M.2    Lu, L.3    Lau, D.4    Ditzel, D.A.5
  • 47
    • 0028176821 scopus 로고
    • Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • Kurochkin IV, Goto S (1994) Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett 345: 33-37.
    • (1994) FEBS Lett , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 48
    • 0037390039 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo
    • Farris W, Mansourian S, Chang Y, Lindsley L, Eckman EA, et al. (2003) Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo. Proc Natl Acad Sci U S A 100: 4162-4167.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4162-4167
    • Farris, W.1    Mansourian, S.2    Chang, Y.3    Lindsley, L.4    Eckman, E.A.5
  • 49
    • 0034704198 scopus 로고    scopus 로고
    • Evidence for genetic linkage of Alzheimer's disease to chromosome 10q
    • Bertram L, Blacker D, Mullin K, Keeney D, Jones J, et al. (2000) Evidence for genetic linkage of Alzheimer's disease to chromosome 10q. Science 290: 2302-2303.
    • (2000) Science , vol.290 , pp. 2302-2303
    • Bertram, L.1    Blacker, D.2    Mullin, K.3    Keeney, D.4    Jones, J.5
  • 51
    • 77649295213 scopus 로고    scopus 로고
    • Concordant association of insulin degrading enzyme gene (IDE) variants with IDE mRNA, Abeta, and Alzheimer's disease
    • Carrasquillo MM, Belbin O, Zou F, Allen M, Ertekin-Taner N, et al. (2010) Concordant association of insulin degrading enzyme gene (IDE) variants with IDE mRNA, Abeta, and Alzheimer's disease. PLoS One 5: e8764.
    • (2010) PLoS One , vol.5
    • Carrasquillo, M.M.1    Belbin, O.2    Zou, F.3    Allen, M.4    Ertekin-Taner, N.5
  • 52
    • 69449102820 scopus 로고    scopus 로고
    • Neprilysin and insulindegrading enzyme levels are increased in Alzheimer disease in relation to disease severity
    • Miners JS, Baig S, Tayler H, Kehoe PG, Love S (2009) Neprilysin and insulindegrading enzyme levels are increased in Alzheimer disease in relation to disease severity. J Neuropathol Exp Neurol 68: 902-914.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 902-914
    • Miners, J.S.1    Baig, S.2    Tayler, H.3    Kehoe, P.G.4    Love, S.5
  • 54
    • 58249118862 scopus 로고    scopus 로고
    • Transcription factors in long-term memory and synaptic plasticity
    • Alberini CM (2009) Transcription factors in long-term memory and synaptic plasticity. Physiol Rev 89: 121-145.
    • (2009) Physiol Rev , vol.89 , pp. 121-145
    • Alberini, C.M.1
  • 55
  • 56
    • 77952168294 scopus 로고    scopus 로고
    • Altered histone acetylation is associated with age-dependent memory impairment in mice
    • Peleg S, Sananbenesi F, Zovoilis A, Burkhardt S, Bahari-Javan S, et al. (2010) Altered histone acetylation is associated with age-dependent memory impairment in mice. Science 328: 753-756.
    • (2010) Science , vol.328 , pp. 753-756
    • Peleg, S.1    Sananbenesi, F.2    Zovoilis, A.3    Burkhardt, S.4    Bahari-Javan, S.5
  • 58
    • 0028338536 scopus 로고
    • Diversity of group types, regulation, and function of phospholipase A2
    • Dennis EA (1994) Diversity of group types, regulation, and function of phospholipase A2. J Biol Chem 269: 13057-13060.
    • (1994) J Biol Chem , vol.269 , pp. 13057-13060
    • Dennis, E.A.1
  • 59
    • 0033543550 scopus 로고    scopus 로고
    • Group V phospholipase A(2)-dependent induction of cyclooxygenase-2 in macrophages
    • Balsinde J, Shinohara H, Lefkowitz LJ, Johnson CA, Balboa MA, et al. (1999) Group V phospholipase A(2)-dependent induction of cyclooxygenase-2 in macrophages. J Biol Chem 274: 25967-25970.
    • (1999) J Biol Chem , vol.274 , pp. 25967-25970
    • Balsinde, J.1    Shinohara, H.2    Lefkowitz, L.J.3    Johnson, C.A.4    Balboa, M.A.5
  • 60
    • 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
  • 61
    • 59449085082 scopus 로고    scopus 로고
    • Phospholipase A2 activation as a therapeutic approach for cognitive enhancement in early-stage Alzheimer disease
    • Schaeffer EL, Forlenza OV, Gattaz WF (2009) Phospholipase A2 activation as a therapeutic approach for cognitive enhancement in early-stage Alzheimer disease. Psychopharmacology (Berl) 202: 37-51.
    • (2009) Psychopharmacology (Berl) , vol.202 , pp. 37-51
    • Schaeffer, E.L.1    Forlenza, O.V.2    Gattaz, W.F.3
  • 63
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
    • Hayashi Y, Shi SH, Esteban JA, Piccini A, Poncer JC, et al. (2000) Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science 287: 2262-2267.
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1    Shi, S.H.2    Esteban, J.A.3    Piccini, A.4    Poncer, J.C.5
  • 65
    • 67449084098 scopus 로고    scopus 로고
    • β-Amyloid impairs AMPA receptor trafficking and function by reducing Ca2+/calmodulin-dependent protein kinase II synaptic distribution
    • Gu Z, Liu W, Yan Z (2009) β-Amyloid impairs AMPA receptor trafficking and function by reducing Ca2+/calmodulin-dependent protein kinase II synaptic distribution. J Biol Chem 284: 10639-10649.
    • (2009) J Biol Chem , vol.284 , pp. 10639-10649
    • Gu, Z.1    Liu, W.2    Yan, Z.3
  • 66
    • 67650330252 scopus 로고    scopus 로고
    • Disassembly of shank and homer synaptic clusters is driven by soluble beta-amyloid(1-40) through divergent NMDAR-dependent signalling pathways
    • Roselli F, Hutzler P, Wegerich Y, Livrea P, Almeida OF (2009) Disassembly of shank and homer synaptic clusters is driven by soluble beta-amyloid(1-40) through divergent NMDAR-dependent signalling pathways. PLoS One 4: e6011.
    • (2009) PLoS One , vol.4
    • Roselli, F.1    Hutzler, P.2    Wegerich, Y.3    Livrea, P.4    Almeida, O.F.5
  • 67
    • 14944372499 scopus 로고    scopus 로고
    • The scaffold protein Homer1b/c links metabotropic glutamate receptor 5 to extracellular signal-regulated protein kinase cascades in neurons
    • Mao L, Yang L, Tang Q, Samdani S, Zhang G, et al. (2005) The scaffold protein Homer1b/c links metabotropic glutamate receptor 5 to extracellular signal-regulated protein kinase cascades in neurons. J Neurosci 25: 2741-2752.
    • (2005) J Neurosci , vol.25 , pp. 2741-2752
    • Mao, L.1    Yang, L.2    Tang, Q.3    Samdani, S.4    Zhang, G.5
  • 68
    • 0034879863 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology and synaptic function by Shank and Homer
    • Sala C, Piech V, Wilson NR, Passafaro M, Liu G, et al. (2001) Regulation of dendritic spine morphology and synaptic function by Shank and Homer. Neuron 31: 115-130.
    • (2001) Neuron , vol.31 , pp. 115-130
    • Sala, C.1    Piech, V.2    Wilson, N.R.3    Passafaro, M.4    Liu, G.5
  • 69
    • 38349029199 scopus 로고    scopus 로고
    • Homer interactions are necessary for metabotropic glutamate receptor-induced long-term depression and translational activation
    • Ronesi JA, Huber KM (2008) Homer interactions are necessary for metabotropic glutamate receptor-induced long-term depression and translational activation. J Neurosci 28: 543-547.
    • (2008) J Neurosci , vol.28 , pp. 543-547
    • Ronesi, J.A.1    Huber, K.M.2
  • 70
    • 0342617716 scopus 로고    scopus 로고
    • Non-plaque dystrophic dendrites in Alzheimer hippocampus: A new pathological structure revealed by glutamate receptor immunocytochemistry
    • Aronica E, Dickson DW, Kress Y, Morrison JH, Zukin RS (1998) Non-plaque dystrophic dendrites in Alzheimer hippocampus: a new pathological structure revealed by glutamate receptor immunocytochemistry. Neuroscience 82: 979-991.
    • (1998) Neuroscience , vol.82 , pp. 979-991
    • Aronica, E.1    Dickson, D.W.2    Kress, Y.3    Morrison, J.H.4    Zukin, R.S.5
  • 71
    • 30644475475 scopus 로고    scopus 로고
    • Soluble betaamyloid1-40 induces NMDA-dependent degradation of postsynaptic density-95 at glutamatergic synapses
    • Roselli F, Tirard M, Lu J, Hutzler P, Lamberti P, et al. (2005) Soluble betaamyloid1-40 induces NMDA-dependent degradation of postsynaptic density-95 at glutamatergic synapses. J Neurosci 25: 11061-11070.
    • (2005) J Neurosci , vol.25 , pp. 11061-11070
    • Roselli, F.1    Tirard, M.2    Lu, J.3    Hutzler, P.4    Lamberti, P.5
  • 72
    • 0035180875 scopus 로고    scopus 로고
    • Invited review: Estrogens effects on the brain: Multiple sites and molecular mechanisms
    • McEwen BS (2001) Invited review: Estrogens effects on the brain: multiple sites and molecular mechanisms. J Appl Physiol 91: 2785-2801.
    • (2001) J Appl Physiol , vol.91 , pp. 2785-2801
    • McEwen, B.S.1
  • 73
    • 0035958527 scopus 로고    scopus 로고
    • Hippocampal estrogen beta-receptor immunoreactivity is increased in Alzheimer's disease
    • Savaskan E, Olivieri G, Meier F, Ravid R, Muller-Spahn F (2001) Hippocampal estrogen beta-receptor immunoreactivity is increased in Alzheimer's disease. Brain Res 908: 113-119.
    • (2001) Brain Res , vol.908 , pp. 113-119
    • Savaskan, E.1    Olivieri, G.2    Meier, F.3    Ravid, R.4    Muller-Spahn, F.5
  • 74
    • 43049141541 scopus 로고    scopus 로고
    • Estrogen receptoralpha variants increase risk of Alzheimer's disease in women with Down syndrome
    • Schupf N, Lee JH, Wei M, Pang D, Chace C, et al. (2008) Estrogen receptoralpha variants increase risk of Alzheimer's disease in women with Down syndrome. Dement Geriatr Cogn Disord 25: 476-482.
    • (2008) Dement Geriatr Cogn Disord , vol.25 , pp. 476-482
    • Schupf, N.1    Lee, J.H.2    Wei, M.3    Pang, D.4    Chace, C.5
  • 75
    • 74049100935 scopus 로고    scopus 로고
    • Estrogen stimulates degradation of beta-amyloid peptide by up-regulating neprilysin
    • Liang K, Yang L, Yin C, Xiao Z, Zhang J, et al. (2010) Estrogen stimulates degradation of beta-amyloid peptide by up-regulating neprilysin. J Biol Chem 285: 935-942.
    • (2010) J Biol Chem , vol.285 , pp. 935-942
    • Liang, K.1    Yang, L.2    Yin, C.3    Xiao, Z.4    Zhang, J.5
  • 76
    • 33745024535 scopus 로고    scopus 로고
    • Estrogen receptor alpha and APOEepsilon4 polymorphisms interact to increase risk for sporadic AD in Italian females
    • Porrello E, Monti MC, Sinforiani E, Cairati M, Guaita A, et al. (2006) Estrogen receptor alpha and APOEepsilon4 polymorphisms interact to increase risk for sporadic AD in Italian females. Eur J Neurol 13: 639-644.
    • (2006) Eur J Neurol , vol.13 , pp. 639-644
    • Porrello, E.1    Monti, M.C.2    Sinforiani, E.3    Cairati, M.4    Guaita, A.5
  • 77
    • 79551563001 scopus 로고    scopus 로고
    • Decreased alternative splicing of estrogen receptor-alpha mRNA in the Alzheimer's disease brain
    • Ishunina TA, Swaab DF (2010) Decreased alternative splicing of estrogen receptor-alpha mRNA in the Alzheimer's disease brain. Neurobiol Aging.
    • (2010) Neurobiol Aging
    • Ishunina, T.A.1    Swaab, D.F.2
  • 80
    • 0033035584 scopus 로고    scopus 로고
    • Processing of wild-type and mutant familial Alzheimer's disease-associated presenilin-1 in cultured neurons
    • Weihl CC, Ghadge GD, Miller RJ, Roos RP (1999) Processing of wild-type and mutant familial Alzheimer's disease-associated presenilin-1 in cultured neurons. J Neurochem 73: 31-40.
    • (1999) J Neurochem , vol.73 , pp. 31-40
    • Weihl, C.C.1    Ghadge, G.D.2    Miller, R.J.3    Roos, R.P.4
  • 81
    • 1542381057 scopus 로고    scopus 로고
    • Cell cycle regulation of neuronal apoptosis in development and disease
    • Becker EB, Bonni A (2004) Cell cycle regulation of neuronal apoptosis in development and disease. Prog Neurobiol 72: 1-25.
    • (2004) Prog Neurobiol , vol.72 , pp. 1-25
    • Becker, E.B.1    Bonni, A.2
  • 82
    • 24744467563 scopus 로고    scopus 로고
    • Cdh1/Hct1-APC is essential for the survival of postmitotic neurons
    • Almeida A, Bolanos JP, Moreno S (2005) Cdh1/Hct1-APC is essential for the survival of postmitotic neurons. J Neurosci 25: 8115-8121.
    • (2005) J Neurosci , vol.25 , pp. 8115-8121
    • Almeida, A.1    Bolanos, J.P.2    Moreno, S.3
  • 83
    • 28144439415 scopus 로고    scopus 로고
    • Cdh1-APC/C, cyclin B-Cdc2, and Alzheimer's disease pathology
    • Aulia S, Tang BL (2006) Cdh1-APC/C, cyclin B-Cdc2, and Alzheimer's disease pathology. Biochem Biophys Res Commun 339: 1-6.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 1-6
    • Aulia, S.1    Tang, B.L.2
  • 84
    • 70350236650 scopus 로고    scopus 로고
    • N-methyl-Daspartate receptor- and metabotropic glutamate receptor-dependent long-term depression are differentially regulated by the ubiquitin-proteasome system
    • Citri A, Soler-Llavina G, Bhattacharyya S, Malenka RC (2009) N-methyl-Daspartate receptor- and metabotropic glutamate receptor-dependent long-term depression are differentially regulated by the ubiquitin-proteasome system. Eur J Neurosci 30: 1443-1450.
    • (2009) Eur J Neurosci , vol.30 , pp. 1443-1450
    • Citri, A.1    Soler-Llavina, G.2    Bhattacharyya, S.3    Malenka, R.C.4
  • 85
    • 67749133983 scopus 로고    scopus 로고
    • Cytoskeletal pathologies of Alzheimer disease
    • Bamburg JR, Bloom GS (2009) Cytoskeletal pathologies of Alzheimer disease. Cell Motil Cytoskeleton 66: 635-649.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 635-649
    • Bamburg, J.R.1    Bloom, G.S.2
  • 86
    • 34547400388 scopus 로고    scopus 로고
    • Evidence that long-term potentiation occurs within individual hippocampal synapses during learning
    • Fedulov V, Rex CS, Simmons DA, Palmer L, Gall CM, et al. (2007) Evidence that long-term potentiation occurs within individual hippocampal synapses during learning. J Neurosci 27: 8031-8039.
    • (2007) J Neurosci , vol.27 , pp. 8031-8039
    • Fedulov, V.1    Rex, C.S.2    Simmons, D.A.3    Palmer, L.4    Gall, C.M.5
  • 87
    • 33846528583 scopus 로고    scopus 로고
    • PKC signaling deficits: A mechanistic hypothesis for the origins of Alzheimer's disease
    • Alkon DL, Sun MK, Nelson TJ (2007) PKC signaling deficits: a mechanistic hypothesis for the origins of Alzheimer's disease. Trends Pharmacol Sci 28: 51-60.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 51-60
    • Alkon, D.L.1    Sun, M.K.2    Nelson, T.J.3
  • 88
    • 70350210477 scopus 로고    scopus 로고
    • Promising multifunctional anti-Alzheimer's dimer bis(7)-Cognitin acting as an activator of protein kinase C regulates activities of alpha-secretase and BACE-1 concurrently
    • Fu H, Dou J, Li W, Cui W, Mak S, et al. (2009) Promising multifunctional anti-Alzheimer's dimer bis(7)-Cognitin acting as an activator of protein kinase C regulates activities of alpha-secretase and BACE-1 concurrently. Eur J Pharmacol 623: 14-21.
    • (2009) Eur J Pharmacol , vol.623 , pp. 14-21
    • Fu, H.1    Dou, J.2    Li, W.3    Cui, W.4    Mak, S.5
  • 89
    • 34250771556 scopus 로고    scopus 로고
    • The aging brain, a key target for the future: The protein kinase C involvement
    • Pascale A, Amadio M, Govoni S, Battaini F (2007) The aging brain, a key target for the future: the protein kinase C involvement. Pharmacol Res 55: 560-569.
    • (2007) Pharmacol Res , vol.55 , pp. 560-569
    • Pascale, A.1    Amadio, M.2    Govoni, S.3    Battaini, F.4
  • 90
    • 33746456956 scopus 로고    scopus 로고
    • Effects of endogenous beta-amyloid overproduction on tau phosphorylation in cell culture
    • Wang ZF, Li HL, Li XC, Zhang Q, Tian Q, et al. (2006) Effects of endogenous beta-amyloid overproduction on tau phosphorylation in cell culture. J Neurochem 98: 1167-1175.
    • (2006) J Neurochem , vol.98 , pp. 1167-1175
    • Wang, Z.F.1    Li, H.L.2    Li, X.C.3    Zhang, Q.4    Tian, Q.5
  • 91
    • 0034044563 scopus 로고    scopus 로고
    • The Shank family of scaffold proteins
    • Sheng M, Kim E (2000) The Shank family of scaffold proteins. J Cell Sci 113(Pt 11): 1851-1856.
    • (2000) J Cell Sci , vol.113 , Issue.Pt 11 , pp. 1851-1856
    • Sheng, M.1    Kim, E.2
  • 92
    • 0032983536 scopus 로고    scopus 로고
    • Association of microglia with amyloid plaques in brains of APP23 transgenic mice
    • Stalder M, Phinney A, Probst A, Sommer B, Staufenbiel M, et al. (1999) Association of microglia with amyloid plaques in brains of APP23 transgenic mice. Am J Pathol 154: 1673-1684.
    • (1999) Am J Pathol , vol.154 , pp. 1673-1684
    • Stalder, M.1    Phinney, A.2    Probst, A.3    Sommer, B.4    Staufenbiel, M.5
  • 93
    • 0033828113 scopus 로고    scopus 로고
    • Glutathione S-transferase polymorphisms and their biological consequences
    • Hayes JD, Strange RC (2000) Glutathione S-transferase polymorphisms and their biological consequences. Pharmacology 61: 154-166.
    • (2000) Pharmacology , vol.61 , pp. 154-166
    • Hayes, J.D.1    Strange, R.C.2
  • 94
    • 0031678044 scopus 로고    scopus 로고
    • Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease
    • Lovell MA, Xie C, Markesbery WR (1998) Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease. Neurology 51: 1562-1566.
    • (1998) Neurology , vol.51 , pp. 1562-1566
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 95
    • 21144447584 scopus 로고    scopus 로고
    • Glutathione S-transferase P1 *C allelic variant increases susceptibility for lateonset Alzheimer disease: Association study and relationship with apolipoprotein
    • Bernardini S, Bellincampi L, Ballerini S, Federici G, Iori R, et al. (2005) Glutathione S-transferase P1 *C allelic variant increases susceptibility for lateonset Alzheimer disease: association study and relationship with apolipoprotein E epsilon4 allele. Clin Chem 51: 944-951.
    • (2005) E Epsilon4 Allele. Clin Chem , vol.51 , pp. 944-951
    • Bernardini, S.1    Bellincampi, L.2    Ballerini, S.3    Federici, G.4    Iori, R.5
  • 96
    • 38449091158 scopus 로고    scopus 로고
    • Glutathione S-transferase P1 and T1 gene polymorphisms predict longitudinal course and age at onset of Alzheimer disease
    • Spalletta G, Bernardini S, Bellincampi L, Federici G, Trequattrini A, et al. (2007) Glutathione S-transferase P1 and T1 gene polymorphisms predict longitudinal course and age at onset of Alzheimer disease. Am J Geriatr Psychiatry 15: 879-887.
    • (2007) Am J Geriatr Psychiatry , vol.15 , pp. 879-887
    • Spalletta, G.1    Bernardini, S.2    Bellincampi, L.3    Federici, G.4    Trequattrini, A.5
  • 97
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla FM, Green KN, Oddo S (2007) Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 8: 499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 98
    • 0033153450 scopus 로고    scopus 로고
    • Superoxide mediates the cell-death-enhancing action of presenilin-1 mutations
    • Guo Q, Fu W, Holtsberg FW, Steiner SM, Mattson MP (1999) Superoxide mediates the cell-death-enhancing action of presenilin-1 mutations. J Neurosci Res 56: 457-470.
    • (1999) J Neurosci Res , vol.56 , pp. 457-470
    • Guo, Q.1    Fu, W.2    Holtsberg, F.W.3    Steiner, S.M.4    Mattson, M.P.5
  • 99
    • 0028204224 scopus 로고
    • Calcium ionophore increases amyloid beta peptide production by cultured cells
    • Querfurth HW, Selkoe DJ (1994) Calcium ionophore increases amyloid beta peptide production by cultured cells. Biochemistry 33: 4550-4561.
    • (1994) Biochemistry , vol.33 , pp. 4550-4561
    • Querfurth, H.W.1    Selkoe, D.J.2
  • 100
    • 0030987603 scopus 로고    scopus 로고
    • Caffeine stimulates amyloid beta-peptide release from beta-amyloid precursor protein-transfected HEK293 cells
    • Querfurth HW, Jiang J, Geiger JD, Selkoe DJ (1997) Caffeine stimulates amyloid beta-peptide release from beta-amyloid precursor protein-transfected HEK293 cells. J Neurochem 69: 1580-1591.
    • (1997) J Neurochem , vol.69 , pp. 1580-1591
    • Querfurth, H.W.1    Jiang, J.2    Geiger, J.D.3    Selkoe, D.J.4
  • 101
    • 47749095383 scopus 로고    scopus 로고
    • Linking calcium to Abeta and Alzheimer's disease
    • Green KN, LaFerla FM (2008) Linking calcium to Abeta and Alzheimer's disease. Neuron 59: 190-194.
    • (2008) Neuron , vol.59 , pp. 190-194
    • Green, K.N.1    Laferla, F.M.2
  • 102
    • 34249051111 scopus 로고    scopus 로고
    • Calcium homeostasis and modulation of synaptic plasticity in the aged brain
    • Foster TC (2007) Calcium homeostasis and modulation of synaptic plasticity in the aged brain. Aging Cell 6: 319-325.
    • (2007) Aging Cell , vol.6 , pp. 319-325
    • Foster, T.C.1
  • 103
    • 0026584043 scopus 로고
    • A ''calcium set-point hypothesis'' of neuronal dependence on neurotrophic factor
    • Johnson EM, Jr., Koike T, Franklin J (1992) A ''calcium set-point hypothesis'' of neuronal dependence on neurotrophic factor. Exp Neurol 115: 163-166.
    • (1992) Exp Neurol , vol.115 , pp. 163-166
    • Johnson Jr., E.M.1    Koike, T.2    Franklin, J.3
  • 104
    • 1842419435 scopus 로고    scopus 로고
    • Raising intracellular calcium attenuates neuronal apoptosis triggered by staurosporine or oxygen-glucose deprivation in the presence of glutamate receptor blockade
    • Canzoniero LM, Babcock DJ, Gottron FJ, Grabb MC, Manzerra P, et al. (2004) Raising intracellular calcium attenuates neuronal apoptosis triggered by staurosporine or oxygen-glucose deprivation in the presence of glutamate receptor blockade. Neurobiol Dis 15: 520-528.
    • (2004) Neurobiol Dis , vol.15 , pp. 520-528
    • Canzoniero, L.M.1    Babcock, D.J.2    Gottron, F.J.3    Grabb, M.C.4    Manzerra, P.5
  • 105
    • 0042536471 scopus 로고    scopus 로고
    • Neuronal and glial calcium signaling in Alzheimer's disease
    • Mattson MP, Chan SL (2003) Neuronal and glial calcium signaling in Alzheimer's disease. Cell Calcium 34: 385-397.
    • (2003) Cell Calcium , vol.34 , pp. 385-397
    • Mattson, M.P.1    Chan, S.L.2
  • 106
    • 0032145886 scopus 로고    scopus 로고
    • Glutamate transporters are oxidantvulnerable: A molecular link between oxidative and excitotoxic neurodegeneration?
    • Trotti D, Danbolt NC, Volterra A (1998) Glutamate transporters are oxidantvulnerable: a molecular link between oxidative and excitotoxic neurodegeneration? Trends Pharmacol Sci 19: 328-334.
    • (1998) Trends Pharmacol Sci , vol.19 , pp. 328-334
    • Trotti, D.1    Danbolt, N.C.2    Volterra, A.3
  • 107
  • 108
    • 54249163572 scopus 로고    scopus 로고
    • Aluminum modulates effects of beta amyloid(1-42) on neuronal calcium homeostasis and mitochondria functioning and is altered in a triple transgenic mouse model of Alzheimer's disease
    • Drago D, Cavaliere A, Mascetra N, Ciavardelli D, di Ilio C, et al. (2008) Aluminum modulates effects of beta amyloid(1-42) on neuronal calcium homeostasis and mitochondria functioning and is altered in a triple transgenic mouse model of Alzheimer's disease. Rejuvenation Res 11: 861-871.
    • (2008) Rejuvenation Res , vol.11 , pp. 861-871
    • Drago, D.1    Cavaliere, A.2    Mascetra, N.3    Ciavardelli, D.4    Di Ilio, C.5
  • 109
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.