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Volumn 278, Issue , 2014, Pages 276-290

Mitogen-activated protein kinase signaling pathways are involved in regulating α7 nicotinic acetylcholine receptor-mediated amyloid-β uptake in SH-SY5Y cells

Author keywords

Alzheimer's disease; Beta amyloid protein; Mitogen activated protein kinase signaling pathways; Uptake; 7 nicotinic acetylcholine receptor

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); BUNGAROTOXIN RECEPTOR; PEPTIDE FRAGMENT; PROTEIN BINDING;

EID: 84908157891     PISSN: 03064522     EISSN: 18737544     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2014.08.013     Document Type: Article
Times cited : (35)

References (60)
  • 1
    • 0034352549 scopus 로고    scopus 로고
    • Cellular expression of alpha 7 nicotinic acetylcholine receptor protein in the temporal cortex in Alzheimer's and Parkinson's disease-a stereological approach
    • Banerjee C., Nyengaard J.R., Wevers A., de Vos R.A.I., Steur E., Lindstrom J., Pilz K., Nowacki S., Bloch W., Schroder H. Cellular expression of alpha 7 nicotinic acetylcholine receptor protein in the temporal cortex in Alzheimer's and Parkinson's disease-a stereological approach. Neurobiol Dis 2000, 7:666-672.
    • (2000) Neurobiol Dis , vol.7 , pp. 666-672
    • Banerjee, C.1    Nyengaard, J.R.2    Wevers, A.3    de Vos, R.A.I.4    Steur, E.5    Lindstrom, J.6    Pilz, K.7    Nowacki, S.8    Bloch, W.9    Schroder, H.10
  • 2
    • 84859980871 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of A beta uptake and degradation by astrocytes
    • Basak J.M., Verghese P.B., Yoon H., Kim J., Holtzman D.M. Low-density lipoprotein receptor represents an apolipoprotein E-independent pathway of A beta uptake and degradation by astrocytes. J Biol Chem 2012, 287:13959-13971.
    • (2012) J Biol Chem , vol.287 , pp. 13959-13971
    • Basak, J.M.1    Verghese, P.B.2    Yoon, H.3    Kim, J.4    Holtzman, D.M.5
  • 3
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • Billings L.M., Oddo S., Green K.N., McGaugh J.L., LaFerla F.M. Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 2005, 45:675-688.
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 5
    • 0033960773 scopus 로고    scopus 로고
    • Phorbol ester activation of the neuronal nicotinic acetylcholine receptor alpha 7 sub-unit gene: involvement of transcription factor Egr-1
    • Carrasco Serrano C., Viniegra S., Ballesta J.J., Criado M. Phorbol ester activation of the neuronal nicotinic acetylcholine receptor alpha 7 sub-unit gene: involvement of transcription factor Egr-1. J Neurochem 2000, 74:932-939.
    • (2000) J Neurochem , vol.74 , pp. 932-939
    • Carrasco Serrano, C.1    Viniegra, S.2    Ballesta, J.J.3    Criado, M.4
  • 6
    • 56749152364 scopus 로고    scopus 로고
    • Transient intraneuronal Aβ rather than extracellular plaque pathology correlates with neuron loss in the frontal cortex of APP/PS1KI mice
    • Christensen D.Z., Kraus S.L., Flohr A., Cotel M.C., Wirths O., Bayer T.A. Transient intraneuronal Aβ rather than extracellular plaque pathology correlates with neuron loss in the frontal cortex of APP/PS1KI mice. Acta Neuropathol 2008, 116:647-655.
    • (2008) Acta Neuropathol , vol.116 , pp. 647-655
    • Christensen, D.Z.1    Kraus, S.L.2    Flohr, A.3    Cotel, M.C.4    Wirths, O.5    Bayer, T.A.6
  • 7
    • 16944365446 scopus 로고    scopus 로고
    • Differential expression of alpha-bungarotoxin-sensitive neuronal nicotinic receptors in adrenergic chromaffin cells: a role for transcription factor Egr-1
    • Criado M., delToro E.D., Carrasco Serrano C., Smillie F.I., Juiz J.M., Viniegra S., Ballesta J.J. Differential expression of alpha-bungarotoxin-sensitive neuronal nicotinic receptors in adrenergic chromaffin cells: a role for transcription factor Egr-1. J Neurosci 1997, 17:6554-6564.
    • (1997) J Neurosci , vol.17 , pp. 6554-6564
    • Criado, M.1    delToro, E.D.2    Carrasco Serrano, C.3    Smillie, F.I.4    Juiz, J.M.5    Viniegra, S.6    Ballesta, J.J.7
  • 8
    • 0035120525 scopus 로고    scopus 로고
    • Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease
    • D'Andrea M.R., Nagele R.G., Wang H.Y., Peterson P.A., Lee D.H.S. Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease. Histopathology 2001, 38:120-134.
    • (2001) Histopathology , vol.38 , pp. 120-134
    • D'Andrea, M.R.1    Nagele, R.G.2    Wang, H.Y.3    Peterson, P.A.4    Lee, D.H.S.5
  • 9
    • 77958559619 scopus 로고    scopus 로고
    • An apolipoprotein E4 fragment can promote intracellular accumulation of amyloid peptide β 42
    • Dafnis I., Stratikos E., Tzinia A., Tsilibary E.C., Zannis V.I., Chroni A. An apolipoprotein E4 fragment can promote intracellular accumulation of amyloid peptide β 42. J Neurochem 2010, 115:873-884.
    • (2010) J Neurochem , vol.115 , pp. 873-884
    • Dafnis, I.1    Stratikos, E.2    Tzinia, A.3    Tsilibary, E.C.4    Zannis, V.I.5    Chroni, A.6
  • 10
    • 0035875962 scopus 로고    scopus 로고
    • β-Amyloid activates the mitogen-activated protein kinase cascade via hippocampal α7 nicotinic acetylcholine receptors: in vitro and in vivo mechanisms related to Alzheimer's disease
    • Dineley K.T., Westerman M., Bui D., Bell K., Ashe K.H., Sweatt J.D. β-Amyloid activates the mitogen-activated protein kinase cascade via hippocampal α7 nicotinic acetylcholine receptors: in vitro and in vivo mechanisms related to Alzheimer's disease. J Neurosci 2001, 21:4125-4133.
    • (2001) J Neurosci , vol.21 , pp. 4125-4133
    • Dineley, K.T.1    Westerman, M.2    Bui, D.3    Bell, K.4    Ashe, K.H.5    Sweatt, J.D.6
  • 11
    • 0031847559 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of substituted benzoate analogues of the selective nicotinic acetylcholine receptor antagonist, methyllycaconitine
    • Doisy X., Blagbrough I.S., Wonnacott S., Potter B.V.L. Design, synthesis, and biological evaluation of substituted benzoate analogues of the selective nicotinic acetylcholine receptor antagonist, methyllycaconitine. Pharm Pharmacol Commun 1998, 4:313-317.
    • (1998) Pharm Pharmacol Commun , vol.4 , pp. 313-317
    • Doisy, X.1    Blagbrough, I.S.2    Wonnacott, S.3    Potter, B.V.L.4
  • 13
    • 65349171510 scopus 로고    scopus 로고
    • Pharmacology of α7 nicotinic acetylcholine receptor mediated extracellular signal-regulated kinase signalling in PC12 cells
    • El Kouhen R., Hu M., Anderson D.J., Li J., Gopalakrishnan M. Pharmacology of α7 nicotinic acetylcholine receptor mediated extracellular signal-regulated kinase signalling in PC12 cells. Br J Pharmacol 2009, 156:638-648.
    • (2009) Br J Pharmacol , vol.156 , pp. 638-648
    • El Kouhen, R.1    Hu, M.2    Anderson, D.J.3    Li, J.4    Gopalakrishnan, M.5
  • 14
    • 84901777978 scopus 로고    scopus 로고
    • Decrease of ERK/MAPK overactivation in prefrontal cortex reverses early memory deficit in a mouse model of Alzheimer's disease
    • Feld M., Krawczyk M.C., Fustinana M.S., Blake M.G., Baratti C.M., Romano A., Boccia M.M. Decrease of ERK/MAPK overactivation in prefrontal cortex reverses early memory deficit in a mouse model of Alzheimer's disease. J Alzheimers Dis 2014, 40:69-82.
    • (2014) J Alzheimers Dis , vol.40 , pp. 69-82
    • Feld, M.1    Krawczyk, M.C.2    Fustinana, M.S.3    Blake, M.G.4    Baratti, C.M.5    Romano, A.6    Boccia, M.M.7
  • 15
    • 77955604553 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal Aβ 42 uptake and lysosomal trafficking
    • Fuentealba R.A., Liu Q., Zhang J., Kanekiyo T., Hu X., Lee J.M., LaDu M.J., Bu G. Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal Aβ 42 uptake and lysosomal trafficking. PLoS One 2010, 5:e11884.
    • (2010) PLoS One , vol.5 , pp. e11884
    • Fuentealba, R.A.1    Liu, Q.2    Zhang, J.3    Kanekiyo, T.4    Hu, X.5    Lee, J.M.6    LaDu, M.J.7    Bu, G.8
  • 16
    • 77954590726 scopus 로고    scopus 로고
    • Coexpression of VGLUT1 and VGLUT2 in trigeminothalamic projection neurons in the principal sensory trigeminal nucleus of the rat
    • Ge S.N., Ma Y.F., Hioki H., Wei Y.Y., Kaneko T., Mizuno N., Gao G.D., Li J.L. Coexpression of VGLUT1 and VGLUT2 in trigeminothalamic projection neurons in the principal sensory trigeminal nucleus of the rat. J Comp Neurol 2010, 518:3149-3168.
    • (2010) J Comp Neurol , vol.518 , pp. 3149-3168
    • Ge, S.N.1    Ma, Y.F.2    Hioki, H.3    Wei, Y.Y.4    Kaneko, T.5    Mizuno, N.6    Gao, G.D.7    Li, J.L.8
  • 19
    • 77950593768 scopus 로고    scopus 로고
    • α7 nAChR-mediated activation of MAP kinase pathways in PC12 cells
    • Gubbins E.J., Gopalakrishnan M., Li J. α7 nAChR-mediated activation of MAP kinase pathways in PC12 cells. Brain Res 2010, 1328:1-11.
    • (2010) Brain Res , vol.1328 , pp. 1-11
    • Gubbins, E.J.1    Gopalakrishnan, M.2    Li, J.3
  • 20
    • 84892871401 scopus 로고    scopus 로고
    • GW1929 inhibits alpha 7 nAChR expression through PPAR gamma-independent activation of p38 MAPK and inactivation of P13-K/mTOR: the role of Egr-1
    • Hahn S.S., Tang Q., Zheng F., Zhao S.Y., Wu J.L. GW1929 inhibits alpha 7 nAChR expression through PPAR gamma-independent activation of p38 MAPK and inactivation of P13-K/mTOR: the role of Egr-1. Cell Signal 2014, 26:730-739.
    • (2014) Cell Signal , vol.26 , pp. 730-739
    • Hahn, S.S.1    Tang, Q.2    Zheng, F.3    Zhao, S.Y.4    Wu, J.L.5
  • 22
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event the etiology of Alzheimer's disease
    • Hardy J., Allsop D. Amyloid deposition as the central event the etiology of Alzheimer's disease. Trends Pharmacol Sci 1991, 12:383-388.
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 23
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 24
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • Hu X.Y., Crick S.L., Bu G.J., Frieden C., Pappu R.V., Lee J.M. Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc Natl Acad Sci USA 2009, 106:20324-20329.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20324-20329
    • Hu, X.Y.1    Crick, S.L.2    Bu, G.J.3    Frieden, C.4    Pappu, R.V.5    Lee, J.M.6
  • 25
    • 84866784086 scopus 로고    scopus 로고
    • Inhibition of extracellular signal-regulated kinase activity improves cognitive function in Tg2576 mice
    • Jin P., Choi D.Y., Hong J.T. Inhibition of extracellular signal-regulated kinase activity improves cognitive function in Tg2576 mice. Clin Exp Pharmacol Physiol 2012, 39:852-857.
    • (2012) Clin Exp Pharmacol Physiol , vol.39 , pp. 852-857
    • Jin, P.1    Choi, D.Y.2    Hong, J.T.3
  • 26
    • 77950590873 scopus 로고    scopus 로고
    • P38MAPK signaling and desmoglein-3 internalization are linked events in pemphigus acantholysis
    • Jolly P.S., Berkowitz P., Bektas M., Lee H.E., Chua M., Diaz L.A., Rubenstein D.S. p38MAPK signaling and desmoglein-3 internalization are linked events in pemphigus acantholysis. J Biol Chem 2010, 285:8936-8941.
    • (2010) J Biol Chem , vol.285 , pp. 8936-8941
    • Jolly, P.S.1    Berkowitz, P.2    Bektas, M.3    Lee, H.E.4    Chua, M.5    Diaz, L.A.6    Rubenstein, D.S.7
  • 27
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-β in Alzheimer's disease
    • LaFerla F.M., Green K.N., Oddo S. Intracellular amyloid-β in Alzheimer's disease. Nat Rev Neurosci 2007, 8:499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 28
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression
    • Manczak M., Anekonda T.S., Henson E., Park B.S., Quinn J., Reddy P.H. Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 2006, 15:1437-1449.
    • (2006) Hum Mol Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 29
    • 79958721260 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage
    • Manczak M., Calkins M.J., Reddy P.H. Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage. Hum Mol Genet 2011, 20:2495-2509.
    • (2011) Hum Mol Genet , vol.20 , pp. 2495-2509
    • Manczak, M.1    Calkins, M.J.2    Reddy, P.H.3
  • 30
    • 40849120814 scopus 로고    scopus 로고
    • Intracellular mechanisms regulating corticotropin-releasing hormone receptor-2 β endocytosis and interaction with extracellularly regulated kinase 1/2 and p38 mitogen-activated protein kinase signaling cascades
    • Markovic D., Punn A., Lehnert H., Grammatopoulos D.K. Intracellular mechanisms regulating corticotropin-releasing hormone receptor-2 β endocytosis and interaction with extracellularly regulated kinase 1/2 and p38 mitogen-activated protein kinase signaling cascades. Mol Endocrinol 2008, 22:689-706.
    • (2008) Mol Endocrinol , vol.22 , pp. 689-706
    • Markovic, D.1    Punn, A.2    Lehnert, H.3    Grammatopoulos, D.K.4
  • 31
    • 84893736391 scopus 로고    scopus 로고
    • Apolipoproteins E and J interfere with amyloid-beta uptake by primary human astrocytes and microglia in vitro
    • Mulder S.D., Nielsen H.M., Blankenstein M.A., Eikelenboom P., Veerhuis R. Apolipoproteins E and J interfere with amyloid-beta uptake by primary human astrocytes and microglia in vitro. Glia 2014, 62:493-503.
    • (2014) Glia , vol.62 , pp. 493-503
    • Mulder, S.D.1    Nielsen, H.M.2    Blankenstein, M.A.3    Eikelenboom, P.4    Veerhuis, R.5
  • 32
    • 0037066072 scopus 로고    scopus 로고
    • Intracellular accumulation of β-amyloid(1-42) in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer's disease
    • Nagele R.G., D'Andrea M.R., Anderson W.J., Wang H.Y. Intracellular accumulation of β-amyloid(1-42) in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer's disease. Neuroscience 2002, 110:199-211.
    • (2002) Neuroscience , vol.110 , pp. 199-211
    • Nagele, R.G.1    D'Andrea, M.R.2    Anderson, W.J.3    Wang, H.Y.4
  • 33
    • 84862868531 scopus 로고    scopus 로고
    • Spreading of neurodegenerative pathology via neuron-to-neuron transmission of β-Amyloid
    • Nath S., Agholme L., Kurudenkandy F.R., Granseth B., Marcusson J., Hallbeck M. Spreading of neurodegenerative pathology via neuron-to-neuron transmission of β-Amyloid. J Neurosci 2012, 32:8767-8777.
    • (2012) J Neurosci , vol.32 , pp. 8767-8777
    • Nath, S.1    Agholme, L.2    Kurudenkandy, F.R.3    Granseth, B.4    Marcusson, J.5    Hallbeck, M.6
  • 34
    • 77954375412 scopus 로고    scopus 로고
    • Astrocytic A beta 1-42 uptake is determined by A beta-aggregation state and the presence of amyloid-associated proteins
    • Nielsen H.M., Mulder S.D., Belien J.A.M., Musters R.J.P., Eikelenboom P., Veerhuis R. Astrocytic A beta 1-42 uptake is determined by A beta-aggregation state and the presence of amyloid-associated proteins. Glia 2010, 58:1235-1246.
    • (2010) Glia , vol.58 , pp. 1235-1246
    • Nielsen, H.M.1    Mulder, S.D.2    Belien, J.A.M.3    Musters, R.J.P.4    Eikelenboom, P.5    Veerhuis, R.6
  • 35
    • 62549147038 scopus 로고    scopus 로고
    • The E693 delta mutation in amyloid precursor protein increases intracellular accumulation of amyloid beta oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells
    • Nishitsuji K., Tomiyama T., Ishibashi K., Ito K., Teraoka R., Lambert M.P., Klein W.L., Mori H. The E693 delta mutation in amyloid precursor protein increases intracellular accumulation of amyloid beta oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells. Am J Pathol 2009, 174:957-969.
    • (2009) Am J Pathol , vol.174 , pp. 957-969
    • Nishitsuji, K.1    Tomiyama, T.2    Ishibashi, K.3    Ito, K.4    Teraoka, R.5    Lambert, M.P.6    Klein, W.L.7    Mori, H.8
  • 36
    • 4043167747 scopus 로고    scopus 로고
    • A β immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S., Billings L., Kesslak J.P., Cribbs D.H., LaFerla F.M. A β immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 2004, 43:321-332.
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 38
    • 0033964077 scopus 로고    scopus 로고
    • Neuronal nicotinic receptors in the human brain
    • Paterson D., Nordberg A. Neuronal nicotinic receptors in the human brain. Prog Neurobiol 2000, 61:75-111.
    • (2000) Prog Neurobiol , vol.61 , pp. 75-111
    • Paterson, D.1    Nordberg, A.2
  • 39
    • 57749197574 scopus 로고    scopus 로고
    • Internalization of beta amyloid protein in primary cultured cortical neurons in mouse
    • Qian Y.H., Shi L.L., Yang J., Hu X.D., Han H., Liu Y. Internalization of beta amyloid protein in primary cultured cortical neurons in mouse. J Cent South Univ (Med Sci) 2008, 33:1019-1027.
    • (2008) J Cent South Univ (Med Sci) , vol.33 , pp. 1019-1027
    • Qian, Y.H.1    Shi, L.L.2    Yang, J.3    Hu, X.D.4    Han, H.5    Liu, Y.6
  • 40
    • 79953298262 scopus 로고    scopus 로고
    • Morphological observation of cellular uptake of beta amyloid protein in cultured human neuroblastoma cells
    • Qian Y.H., Hu X., Hua H., Yong L. Morphological observation of cellular uptake of beta amyloid protein in cultured human neuroblastoma cells. J South Med Univ 2009, 29:1857-1859.
    • (2009) J South Med Univ , vol.29 , pp. 1857-1859
    • Qian, Y.H.1    Hu, X.2    Hua, H.3    Yong, L.4
  • 41
    • 67349162522 scopus 로고    scopus 로고
    • Dexamethasone inhibits camptothecin-induced apoptosis in C6-glioma via activation of Stat5/Bcl-xL pathway
    • Qian Y.H., Xiao Q., Chen H., Xu J. Dexamethasone inhibits camptothecin-induced apoptosis in C6-glioma via activation of Stat5/Bcl-xL pathway. Biochim Biophys Acta Mol Cell Res 2009, 1793:764-771.
    • (2009) Biochim Biophys Acta Mol Cell Res , vol.1793 , pp. 764-771
    • Qian, Y.H.1    Xiao, Q.2    Chen, H.3    Xu, J.4
  • 42
    • 67649803186 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease
    • Reddy P.H. Amyloid beta, mitochondrial structural and functional dynamics in Alzheimer's disease. Exp Neurol 2009, 218:286-292.
    • (2009) Exp Neurol , vol.218 , pp. 286-292
    • Reddy, P.H.1
  • 43
    • 84875981923 scopus 로고    scopus 로고
    • Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1
    • Rushworth J.V., Griffiths H.H., Watt N.T., Hooper N.M. Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1. J Biol Chem 2013, 288:8935-8951.
    • (2013) J Biol Chem , vol.288 , pp. 8935-8951
    • Rushworth, J.V.1    Griffiths, H.H.2    Watt, N.T.3    Hooper, N.M.4
  • 44
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's-disease
    • Selkoe D.J. The molecular pathology of Alzheimer's-disease. Neuron 1991, 6:487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 45
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001, 81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 46
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture
    • Skovronsky D.M., Doms R.W., Lee V.M.Y. Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture. J Cell Biol 1998, 141:1031-1039.
    • (1998) J Cell Biol , vol.141 , pp. 1031-1039
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.Y.3
  • 48
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi R.H., Almeida C.G., Kearney P.F., Yu F.M., Lin M.T., Milner T.A., Gouras G.K. Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain. J Neurosci 2004, 24:3592-3599.
    • (2004) J Neurosci , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.M.4    Lin, M.T.5    Milner, T.A.6    Gouras, G.K.7
  • 50
    • 0035837274 scopus 로고    scopus 로고
    • Beta-amyloid deposits in transgenic mice expressing human beta-amyloid precursor protein have the same characteristics as those in Alzheimer's disease
    • Terai K., Iwai A., Kawabata S., Tasaki Y., Watanabe T., Miyata K., Yamaguchi T. Beta-amyloid deposits in transgenic mice expressing human beta-amyloid precursor protein have the same characteristics as those in Alzheimer's disease. Neuroscience 2001, 104:299-310.
    • (2001) Neuroscience , vol.104 , pp. 299-310
    • Terai, K.1    Iwai, A.2    Kawabata, S.3    Tasaki, Y.4    Watanabe, T.5    Miyata, K.6    Yamaguchi, T.7
  • 51
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo
    • Umeda T., Tomiyama T., Sakama N., Tanaka S., Lambert M.P., Klein W.L., Mori H. Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo. J Neurosci Res 2011, 89:1031-1042.
    • (2011) J Neurosci Res , vol.89 , pp. 1031-1042
    • Umeda, T.1    Tomiyama, T.2    Sakama, N.3    Tanaka, S.4    Lambert, M.P.5    Klein, W.L.6    Mori, H.7
  • 52
    • 0036169622 scopus 로고    scopus 로고
    • Cerebellar diffuse amyloid plaques are derived from dendritic Aβ 42 accumulations in Purkinje cells
    • Wang H.Y., D'Andrea M.R., Nagele R.G. Cerebellar diffuse amyloid plaques are derived from dendritic Aβ 42 accumulations in Purkinje cells. Neurobiol Aging 2002, 23:213-223.
    • (2002) Neurobiol Aging , vol.23 , pp. 213-223
    • Wang, H.Y.1    D'Andrea, M.R.2    Nagele, R.G.3
  • 53
    • 0034006944 scopus 로고    scopus 로고
    • Beta-amyloid(1-42) binds to α7 nicotinic acetylcholine receptor with high affinity-implications for Alzheimer's disease pathology
    • Wang H.Y., Lee D.H.S., D'Andrea M.R., Peterson P.A., Shank R.P., Reitz A.B. Beta-amyloid(1-42) binds to α7 nicotinic acetylcholine receptor with high affinity-implications for Alzheimer's disease pathology. J Biol Chem 2000, 275:5626-5632.
    • (2000) J Biol Chem , vol.275 , pp. 5626-5632
    • Wang, H.Y.1    Lee, D.H.S.2    D'Andrea, M.R.3    Peterson, P.A.4    Shank, R.P.5    Reitz, A.B.6
  • 54
    • 0033624509 scopus 로고    scopus 로고
    • Amyloid peptide Aβ (1-42) binds selectively and with picomolar affinity to alpha 7 nicotinic acetylcholine receptors
    • Wang H.Y., Lee D.H.S., Davis C.B., Shank R.P. Amyloid peptide Aβ (1-42) binds selectively and with picomolar affinity to alpha 7 nicotinic acetylcholine receptors. J Neurochem 2000, 75:1155-1161.
    • (2000) J Neurochem , vol.75 , pp. 1155-1161
    • Wang, H.Y.1    Lee, D.H.S.2    Davis, C.B.3    Shank, R.P.4
  • 55
    • 40649099564 scopus 로고    scopus 로고
    • Analysis of gene expression profiles in rat hippocampus following treatment with nicotine and an alpha 7 nAChR selective agonist
    • Waring J.F., Abel S., Li J., Bitner R.S., Nikkel A.L., Blornme E.A., Anderson D.J., Gopalakrishnan M. Analysis of gene expression profiles in rat hippocampus following treatment with nicotine and an alpha 7 nAChR selective agonist. Neurosci Res 2008, 60:266-274.
    • (2008) Neurosci Res , vol.60 , pp. 266-274
    • Waring, J.F.1    Abel, S.2    Li, J.3    Bitner, R.S.4    Nikkel, A.L.5    Blornme, E.A.6    Anderson, D.J.7    Gopalakrishnan, M.8
  • 56
    • 77956815064 scopus 로고    scopus 로고
    • Neuron loss in transgenic mouse models of Alzheimer's disease
    • Wirths O., Bayer T.A. Neuron loss in transgenic mouse models of Alzheimer's disease. Int J Alzheimers Dis 2010, 2010:1-6.
    • (2010) Int J Alzheimers Dis , vol.2010 , pp. 1-6
    • Wirths, O.1    Bayer, T.A.2
  • 57
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • Yao J., Irwin R.W., Zhao L., Nilsen J., Hamilton R.T., Brinton R.D. Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 2009, 106:14670-14675.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 59
    • 70349952431 scopus 로고    scopus 로고
    • Oligomeric aggregates of amyloid β peptide 1-42 activate ERK/MAPK in SH-SY5Y cells via the alpha 7 nicotinic receptor
    • Young K.F., Pasternak S.H., Rylett R.J. Oligomeric aggregates of amyloid β peptide 1-42 activate ERK/MAPK in SH-SY5Y cells via the alpha 7 nicotinic receptor. Neurochem Int 2009, 55:796-801.
    • (2009) Neurochem Int , vol.55 , pp. 796-801
    • Young, K.F.1    Pasternak, S.H.2    Rylett, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.