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Volumn , Issue , 2011, Pages

Aß internalization by neurons and glia

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ALPHA 2 MACROGLOBULIN; ALPHA SECRETASE; AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; APOLIPOPROTEIN E4; CHOLERA TOXIN B SUBUNIT; CLATHRIN; CLUSTERIN; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C3B; FORMYLPEPTIDE RECEPTOR LIKE 1; INTEGRIN; LEUCINE RICH REPEAT KINASE 2; MEMANTINE; NICOTINIC RECEPTOR; OXIDIZED LOW DENSITY LIPOPROTEIN RECEPTOR 1; PROTEASOME; PROTEIN; TOLL LIKE RECEPTOR;

EID: 79953280394     PISSN: None     EISSN: 20900252     Source Type: Journal    
DOI: 10.4061/2011/127984     Document Type: Review
Times cited : (85)

References (216)
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D. J., Alzheimer's disease: genes, proteins, and therapy Physiological Reviews 2001 81 2 741 766 (Pubitemid 32267077)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy J., Allsop D., Amyloid deposition as the central event in the aetiology of Alzheimer's disease Trends in Pharmacological Sciences 1991 12 10 383 388
    • (1991) Trends in Pharmacological Sciences , vol.12 , Issue.10 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 4
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy J. A., Higgins G. A., Alzheimer's disease: the amyloid cascade hypothesis Science 1992 256 5054 184 185
    • (1992) Science , vol.256 , Issue.5054 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 5
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D. J., The molecular pathology of Alzheimer's disease Neuron 1991 6 4 487 498
    • (1991) Neuron , vol.6 , Issue.4 , pp. 487-498
    • Selkoe, D.J.1
  • 6
    • 7244236841 scopus 로고    scopus 로고
    • A modified β-amyloid hypothesis: Intraneuronal accumulation of the β-amyloid peptide - The first step of a fatal cascade
    • DOI 10.1111/j.1471-4159.2004.02737.x
    • Wirths O., Multhaup G., Bayer T. A., A modified -amyloid hypothesis: intraneuronal accumulation of the -amyloid peptidethe first step of a fatal cascade Journal of Neurochemistry 2004 91 3 513 520 (Pubitemid 39431147)
    • (2004) Journal of Neurochemistry , vol.91 , Issue.3 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 7
    • 25144501662 scopus 로고    scopus 로고
    • Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2005.05.022, PII S0197458005001624
    • Gouras G. K., Almeida C. G., Takahashi R. H., Intraneuronal A accumulation and origin of plaques in Alzheimer's disease Neurobiology of Aging 2005 26 9 1235 1244 (Pubitemid 41338539)
    • (2005) Neurobiology of Aging , vol.26 , Issue.9 , pp. 1235-1244
    • Gouras, G.K.1    Almeida, C.G.2    Takahashi, R.H.3
  • 8
    • 13544260852 scopus 로고    scopus 로고
    • Intracellular and extracellular Aβ, a tale of two neuropathologies
    • Cuello A. C., Intracellular and extracellular A, a tale of two neuropathologies Brain Pathology 2005 15 1 66 71 (Pubitemid 40224068)
    • (2005) Brain Pathology , vol.15 , Issue.1 , pp. 66-71
    • Cuello, A.C.1
  • 10
    • 77954554036 scopus 로고    scopus 로고
    • Immunohistochemical visualization of amyloid- protein precursor and amyloid- in extra- and intracellular compartments in the human brain
    • Aho L., Pikkarainen M., Hiltunen M., Leinonen V., Alafuzoff I., Immunohistochemical visualization of amyloid- protein precursor and amyloid- in extra- and intracellular compartments in the human brain Journal of Alzheimer's Disease 2010 20 4 1015 1028
    • (2010) Journal of Alzheimer's Disease , vol.20 , Issue.4 , pp. 1015-1028
    • Aho, L.1    Pikkarainen, M.2    Hiltunen, M.3    Leinonen, V.4    Alafuzoff, I.5
  • 13
    • 0035120525 scopus 로고    scopus 로고
    • Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease
    • DOI 10.1046/j.1365-2559.2001.01082.x
    • 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 2 120 134 (Pubitemid 32193626)
    • (2001) Histopathology , vol.38 , Issue.2 , 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
  • 15
    • 84899571989 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloid-Betaa predictor for synaptic dysfunction and neuron loss in Alzheimer's disease
    • Bayer T. A., Wirths O., Intracellular accumulation of amyloid-Betaa predictor for synaptic dysfunction and neuron loss in Alzheimer's disease Frontiers in Aging Neuroscience 2010 2 8
    • (2010) Frontiers in Aging Neuroscience , vol.2 , Issue.8
    • Bayer, T.A.1    Wirths, O.2
  • 16
    • 84885915876 scopus 로고    scopus 로고
    • Synapses, synaptic activity and intraneuronal abeta in Alzheimer's disease
    • Tampellini D., Gouras G. K., Synapses, synaptic activity and intraneuronal abeta in Alzheimer's disease Frontiers in Aging Neuroscience 2010 2
    • (2010) Frontiers in Aging Neuroscience , vol.2
    • Tampellini, D.1    Gouras, G.K.2
  • 17
    • 40449092370 scopus 로고    scopus 로고
    • Impact of intracellular β-amyloid in transgenic animals and cell models
    • DOI 10.1159/000113686
    • Cuello A. C., Canneva F., Impact of intracellular -amyloid in transgenic animals and cell models Neurodegenerative Diseases 2008 5 3-4 146 148 (Pubitemid 351347834)
    • (2008) Neurodegenerative Diseases , vol.5 , Issue.3-4 , pp. 146-148
    • Cuello, A.C.1    Canneva, F.2
  • 18
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's Disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • DOI 10.1016/S0896-6273(03)00434-3
    • Oddo S., Caccamo A., Shepherd J. D., Murphy M. P., Golde T. E., Kayed R., Metherate R., Mattson M. P., Akbari Y., LaFerla F. M., Triple-transgenic model of Alzheimer's Disease with plaques and tangles: intracellular A and synaptic dysfunction Neuron 2003 39 3 409 421 (Pubitemid 36937044)
    • (2003) Neuron , vol.39 , Issue.3 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6    Metherate, R.7    Mattson, M.P.8    Akbari, Y.9    LaFerla, F.M.10
  • 19
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • DOI 10.1016/j.neuron.2005.01.040
    • Billings L. M., Oddo S., Green K. N., McGaugh J. L., LaFerla F. M., Intraneuronal A causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice Neuron 2005 45 5 675 688 (Pubitemid 40320703)
    • (2005) Neuron , vol.45 , Issue.5 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 20
    • 4043167747 scopus 로고    scopus 로고
    • Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • DOI 10.1016/j.neuron.2004.07.003, PII S0896627304004246
    • Oddo S., Billings L., Kesslak J. P., Cribbs D. H., LaFerla F. M., A immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome Neuron 2004 43 3 321 332 (Pubitemid 39061125)
    • (2004) Neuron , vol.43 , Issue.3 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 22
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid β protein that accumulates with time in culture
    • DOI 10.1083/jcb.141.4.1031
    • Skovronsky D. M., Doms R. W., Lee V. M. Y., Detection of a novel intraneuronal pool of insoluble amyloid protein that accumulates with time in culture Journal of Cell Biology 1998 141 4 1031 1039 (Pubitemid 28243969)
    • (1998) Journal of Cell Biology , vol.141 , Issue.4 , pp. 1031-1039
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.-Y.3
  • 24
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain
    • DOI 10.1523/JNEUROSCI.5167-03.2004
    • Takahashi R. H., Almeida C. G., Kearney P. F., Yu F., Lin M. T., Milner T. A., Gouras G. K., Oligomerization of Alzheimer's -amyloid within processes and synapses of cultured neurons and brain Journal of Neuroscience 2004 24 14 3592 3599 (Pubitemid 38481116)
    • (2004) Journal of Neuroscience , vol.24 , Issue.14 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.4    Lin, M.T.5    Milner, T.A.6    Gouras, G.K.7
  • 25
    • 0037186074 scopus 로고    scopus 로고
    • Altered metabolism of the amyloid β precursor protein is associated with mitochondrial dysfunction in Down's syndrome
    • DOI 10.1016/S0896-6273(02)00604-9
    • Busciglio J., Pelsman A., Wong C., Pigino G., Yuan M., Mori H., Yankner B. A., Altered metabolism of the amyloid precursor protein is associated with mitochondrial dysfunction in Down's syndrome Neuron 2002 33 5 677 688 (Pubitemid 34219240)
    • (2002) Neuron , vol.33 , Issue.5 , pp. 677-688
    • Busciglio, J.1    Pelsman, A.2    Wong, C.3    Pigino, G.4    Yuan, M.5    Mori, H.6    Yankner, B.A.7
  • 27
    • 0037017399 scopus 로고    scopus 로고
    • 1-42 through p53 and Bax in cultured primary human neurons
    • DOI 10.1083/jcb.200110119
    • Zhang Y., McLaughlin R., Goodyer C., LeBlanc A., Selective cytotoxicity of intracellular amyloid peptide142 through p53 and Bax in cultured primary human neurons Journal of Cell Biology 2002 156 3 519 529 (Pubitemid 34839899)
    • (2002) Journal of Cell Biology , vol.156 , Issue.3 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    LeBlanc, A.4
  • 28
    • 0028981717 scopus 로고
    • The Alzheimer's A peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • LaFerla F. M., Tinkle B. T., Bieberich C. J., Haudenschild C. C., Jay G., The Alzheimer's A peptide induces neurodegeneration and apoptotic cell death in transgenic mice Nature Genetics 1995 9 1 21 29
    • (1995) Nature Genetics , vol.9 , Issue.1 , pp. 21-29
    • Laferla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 32
    • 26944467176 scopus 로고    scopus 로고
    • Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses
    • DOI 10.1016/j.nbd.2005.02.008, PII S0969996105000720
    • Almeida C. G., Tampellini D., Takahashi R. H., Greengard P., Lin M. T., Snyder E. M., Gouras G. K., Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses Neurobiology of Disease 2005 20 2 187 198 (Pubitemid 41476246)
    • (2005) Neurobiology of Disease , vol.20 , Issue.2 , pp. 187-198
    • Almeida, C.G.1    Tampellini, D.2    Takahashi, R.H.3    Greengard, P.4    Lin, M.T.5    Snyder, E.M.6    Gouras, G.K.7
  • 33
    • 34547110577 scopus 로고    scopus 로고
    • Internalized antibodies to the Aβ domain of APP reduce neuronal Aβ and protect against synaptic alterations
    • DOI 10.1074/jbc.M700373200
    • Tampellini D., Magran J., Takahashi R. H., Li F., Lin M. T., Almeida C. G., Gouras G. K., Internalized antibodies to the A domain of APP reduce neuronal A and protect against synaptic alterations Journal of Biological Chemistry 2007 282 26 18895 18906 (Pubitemid 47100144)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.26 , pp. 18895-18906
    • Tampellini, D.1    Magrane, J.2    Takahashi, R.H.3    Li, F.4    Lin, M.T.5    Almeida, C.G.6    Gouras, G.K.7
  • 34
    • 0036772311 scopus 로고    scopus 로고
    • Intracellular A-beta amyloid, a sign for worse things to come?
    • DOI 10.1385/MN:26:2-3:299
    • Echeverria V., Cuello A. C., Intracellular A-beta amyloid, a sign for worse things to come? Molecular Neurobiology 2002 26 2-3 299 316 (Pubitemid 35239806)
    • (2002) Molecular Neurobiology , vol.26 , Issue.2-3 , pp. 299-316
    • Echeverria, V.1    Cuello, A.C.2
  • 38
    • 0036550597 scopus 로고    scopus 로고
    • Significance of intracellular Abeta42 accumulation in Alzheimer's disease
    • Tabira T., Chui D. H., Kuroda S., Significance of intracellular Abeta42 accumulation in Alzheimer's disease Front Biosci 2002 7 a44 49
    • (2002) Front Biosci , vol.7 , pp. 44-49
    • Tabira, T.1    Chui, D.H.2    Kuroda, S.3
  • 39
    • 49949083479 scopus 로고    scopus 로고
    • Amyloid -peptide levels in laser capture microdissected cornu ammonis 1 pyramidal neurons of Alzheimer's brain
    • Aoki M., Volkmann I., Tjernberg L. O., Winblad B., Bogdanovic N., Amyloid -peptide levels in laser capture microdissected cornu ammonis 1 pyramidal neurons of Alzheimer's brain NeuroReport 2008 19 11 1085 1089
    • (2008) NeuroReport , vol.19 , Issue.11 , pp. 1085-1089
    • Aoki, M.1    Volkmann, I.2    Tjernberg, L.O.3    Winblad, B.4    Bogdanovic, N.5
  • 40
    • 0032551528 scopus 로고    scopus 로고
    • Amyloid β protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein
    • DOI 10.10 02/(SICI)109 6-9861(199807 20)397:1<139::AID-CN E10>3.0.CO;2-K
    • Bahr B. A., Hoffman K. B., Yang A. J., Hess U. S., Glabe C. G., Lynch G., Amyloid protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein Journal of Comparative Neurology 1998 397 1 139 147 (Pubitemid 28304057)
    • (1998) Journal of Comparative Neurology , vol.397 , Issue.1 , pp. 139-147
    • Bahr, B.A.1    Hoffman, K.B.2    Yang, A.J.3    Hess, U.S.4    Glabe, C.G.5    Lynch, G.6
  • 41
    • 0035159785 scopus 로고    scopus 로고
    • Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease
    • DOI 10.1385/JMN:17:2:137
    • Glabe C., Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease Journal of Molecular Neuroscience 2001 17 2 137 145 (Pubitemid 33063518)
    • (2001) Journal of Molecular Neuroscience , vol.17 , Issue.2 , pp. 137-145
    • Glabe, C.1
  • 43
    • 0028303123 scopus 로고
    • Development of a monoclonal antibody specific for the COOH-terminal of - Amyloid 1-42 and its immunohistochemical reactivity in Alzheimer's disease and related disorders
    • Murphy G. M., Forno L. S., Higgins L., Scardina J. M., Eng L. F., Cordell B., Development of a monoclonal antibody specific for the COOH-terminal of -amyloid 1-42 and its immunohistochemical reactivity in Alzheimer's disease and related disorders American Journal of Pathology 1994 144 5 1082 1088
    • (1994) American Journal of Pathology , vol.144 , Issue.5 , pp. 1082-1088
    • Murphy, G.M.1    Forno, L.S.2    Higgins, L.3    Scardina, J.M.4    Eng, L.F.5    Cordell, B.6
  • 44
    • 30344448543 scopus 로고    scopus 로고
    • A dynamic relationship between intracellular and extracellular pools of Aβ
    • DOI 10.2353/ajpath.2006.050593
    • Oddo S., Caccamo A., Smith I. F., Green K. N., LaFerla F. M., A dynamic relationship between intracellular and extracellular pools of A American Journal of Pathology 2006 168 1 184 194 (Pubitemid 43062572)
    • (2006) American Journal of Pathology , vol.168 , Issue.1 , pp. 184-194
    • Oddo, S.1    Caccamo, A.2    Smith, I.F.3    Green, K.N.4    LaFerla, F.M.5
  • 45
    • 0028972233 scopus 로고
    • Intracellular accumulation of beta-amyloid in cells expressing the Swedish mutant amyloid precursor protein
    • DOI 10.1074/jbc.270.45.26727
    • Martin B. L., Schrader-Fischer G., Busciglio J., Duke M., Paganetti P., Yankner B. A., Intracellular accumulation of -amyloid in cells expressing the Swedish mutant amyloid precursor protein Journal of Biological Chemistry 1995 270 45 26727 26730 (Pubitemid 3007225)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.45 , pp. 26727-26730
    • Martin, B.L.1    Schrader-Fischer, G.2    Busciglio, J.3    Duke, M.4    Paganetti, P.5    Yankner, B.A.6
  • 47
    • 0029664624 scopus 로고    scopus 로고
    • Amyloids 40 and 42 are generated intracellularly in cultured human neurons and their secretion increases with maturation
    • Turner R. S., Suzuki N., Chyung A. S. C., Younkin S. G., Lee V. M.-Y., Amyloids 40 and 42 are generated intracellularly in cultured human neurons and their secretion increases with maturation Journal of Biological Chemistry 1996 271 15 8966 8970
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.15 , pp. 8966-8970
    • Turner, R.S.1    Suzuki, N.2    Chyung, A.S.C.3    Younkin, S.G.4    Lee, V.M.-Y.5
  • 48
    • 0032564388 scopus 로고    scopus 로고
    • Presenilin 1 regulates the processing of β-amyloid precursor protein C- terminal fragments and the generation of amyloid β-protein in endoplasmic reticulum and Golgi
    • DOI 10.1021/bi9816195
    • Xia W., Zhang J., Ostaszewski B. L., Kimberly W. T., Seubert P., Koo E. H., Shen J., Selkoe D. J., Presenilin 1 regulates the processing of -amyloid precursor protein C- terminal fragments and the generation of amyloid -protein in endoplasmic reticulum and Golgi Biochemistry 1998 37 47 16465 16471 (Pubitemid 28543904)
    • (1998) Biochemistry , vol.37 , Issue.47 , pp. 16465-16471
    • Xia, W.1    Zhang, J.2    Ostaszewski, B.L.3    Kimberly, W.T.4    Seubert, P.5    Koo, E.H.6    Shen, J.7    Selkoe, D.J.8
  • 49
    • 1442323991 scopus 로고    scopus 로고
    • Intraneuronal amyloid-β1-42 production triggered by sustained increase of cytosolic calcium concentration induces neuronal death
    • DOI 10.1046/j.1471-4159.2003.02227.x
    • Pierrot N., Ghisdal P., Caumont A. S., Octave J. N., Intraneuronal amyloid- 1-42 production triggered by sustained increase of cytosolic calcium concentration induces neuronal death Journal of Neurochemistry 2004 88 5 1140 1150 (Pubitemid 38280681)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.5 , pp. 1140-1150
    • Pierrot, N.1    Ghisdal, P.2    Caumont, A.-S.3    Octave, J.-N.4
  • 50
    • 42149164312 scopus 로고    scopus 로고
    • Processing of amyloid precursor protein and amyloid peptide neurotoxicity
    • DOI 10.2174/156720508783954721
    • Nathalie P., Jean-Nol O., Processing of amyloid precursor protein and amyloid peptide neurotoxicity Current Alzheimer Research 2008 5 2 92 99 (Pubitemid 351536335)
    • (2008) Current Alzheimer Research , vol.5 , Issue.2 , pp. 92-99
    • Nathalie, P.1    Jean-Noel, O.2
  • 51
    • 0033527744 scopus 로고    scopus 로고
    • Expression of -amyloid precursor protein-CD3 chimeras to demonstrate the selective generation of amyloid/ and amyloid peptides within secretory and endocytic compartments
    • Soriano S., Chyung A. S. C., Chen X., Stokin G. B., Lee V. M. Y., Koo E. H., Expression of -amyloid precursor protein-CD3 chimeras to demonstrate the selective generation of amyloid/ and amyloid peptides within secretory and endocytic compartments Journal of Biological Chemistry 1999 274 45 32295 32300
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.45 , pp. 32295-32300
    • Soriano, S.1    Chyung, A.S.C.2    Chen, X.3    Stokin, G.B.4    Lee, V.M.Y.5    Koo, E.H.6
  • 53
    • 0030952217 scopus 로고    scopus 로고
    • Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42
    • DOI 10.1074/jbc.272.26.16085
    • Wild-Bode C., Yamazaki T., Capell A., Leimer U., Steiner H., Ihara Y., Haass C., Intracellular generation and accumulation of amyloid -peptide terminating at amino acid 42 Journal of Biological Chemistry 1997 272 26 16085 16088 (Pubitemid 27276419)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.26 , pp. 16085-16088
    • Wild-Bode, C.1    Yamazaki, T.2    Capell, A.3    Leimer, U.4    Steiner, H.5    Ihara, Y.6    Haass, C.7
  • 54
    • 0030793522 scopus 로고    scopus 로고
    • Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Aβ stabilization
    • LaFerla F. M., Troncoso J. C., Strickland D. K., Kawas C. H., Jay G., Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular A stabilization Journal of Clinical Investigation 1997 100 2 310 320 (Pubitemid 27349077)
    • (1997) Journal of Clinical Investigation , vol.100 , Issue.2 , pp. 310-320
    • LaFerla, F.M.1    Troncoso, J.C.2    Strickland, D.K.3    Kawas, C.H.4    Jay, G.5
  • 55
    • 0037066072 scopus 로고    scopus 로고
    • 1-42 in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer's disease
    • DOI 10.1016/S0306-4522(01)00460-2, PII S0306452201004602
    • Nagele R. G., D'Andrea M. R., Anderson W. J., Wang H. Y., Intracellular accumulation of -amyloid in neurons is facilitated by the 7 nicotinic acetylcholine receptor in Alzheimer's disease Neuroscience 2002 110 2 199 211 (Pubitemid 34214939)
    • (2002) Neuroscience , vol.110 , Issue.2 , pp. 199-211
    • Nagele, R.G.1    D'Andrea, M.R.2    Anderson, W.J.3    Wang, H.-Y.4
  • 56
    • 0037135272 scopus 로고    scopus 로고
    • Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
    • DOI 10.1016/S0306-4522(02)00132-X, PII S030645220200132X
    • Bi X., Gall C. M., Zhou J., Lynch G., Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists Neuroscience 2002 112 4 827 840 (Pubitemid 34667047)
    • (2002) Neuroscience , vol.112 , Issue.4 , pp. 827-840
    • Bi, X.1    Gall, C.M.2    Zhou, J.3    Lynch, G.4
  • 57
    • 33947164189 scopus 로고    scopus 로고
    • Aβ peptides can enter the brain through a defective blood-brain barrier and bind selectively to neurons
    • DOI 10.1016/j.brainres.2007.01.070, PII S0006899307001278
    • Clifford P. M., Zarrabi S., Siu G., Kinsler K. J., Kosciuk M. C., Venkataraman V., D'Andrea M. R., Dinsmore S., Nagele R. G., A peptides can enter the brain through a defective blood-brain barrier and bind selectively to neurons Brain Research 2007 1142 1 223 236 (Pubitemid 46413194)
    • (2007) Brain Research , vol.1142 , Issue.1 , pp. 223-236
    • Clifford, P.M.1    Zarrabi, S.2    Siu, G.3    Kinsler, K.J.4    Kosciuk, M.C.5    Venkataraman, V.6    D'Andrea, M.R.7    Dinsmore, S.8    Nagele, R.G.9
  • 58
    • 0029057814 scopus 로고
    • Intracellular A 142 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • Yang A. J., Knauer M., Burdick D. A., Glabe C., Intracellular A 142 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells Journal of Biological Chemistry 1995 270 24 14786 14792
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.24 , pp. 14786-14792
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 59
    • 0033575336 scopus 로고    scopus 로고
    • Intracellular accumulation of insoluble, newly synthesized A n-42 in amyloid precursor protein-transfected cells that have been treated with A 142
    • Yang A. J., Chandswangbhuvana D., Shu T., Henschen A., Glabe C. G., Intracellular accumulation of insoluble, newly synthesized A n-42 in amyloid precursor protein-transfected cells that have been treated with A 142 Journal of Biological Chemistry 1999 274 29 20650 20656
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.29 , pp. 20650-20656
    • Yang, A.J.1    Chandswangbhuvana, D.2    Shu, T.3    Henschen, A.4    Glabe, C.G.5
  • 63
    • 33845661843 scopus 로고    scopus 로고
    • Abeta induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597624)
    • Shaked G. M., Kummer M. P., Lu D. C., Galvan V., Bredesen D. E., Koo E. H., Abeta induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597624) FASEB Journal 2006 20 8 1254 1256
    • (2006) FASEB Journal , vol.20 , Issue.8 , pp. 1254-1256
    • Shaked, G.M.1    Kummer, M.P.2    Lu, D.C.3    Galvan, V.4    Bredesen, D.E.5    Koo, E.H.6
  • 64
    • 0031030053 scopus 로고    scopus 로고
    • Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, A β1-42, in differentiated PC12 cells
    • DOI 10.1016/S0006-8993(96)01262-0, PII S0006899396012620
    • Burdick D., Kosmoski J., Knauer M. F., Glabe C. G., Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, A 142, in differentiated PC12 cells Brain Research 1997 746 1-2 275 284 (Pubitemid 27060356)
    • (1997) Brain Research , vol.746 , Issue.1-2 , pp. 275-284
    • Burdick, D.1    Kosmoski, J.2    Knauer, M.F.3    Glabe, C.G.4
  • 66
    • 37249062072 scopus 로고    scopus 로고
    • Internalization of β-amyloid peptide by primary neurons in the absence of apolipoprotein E
    • DOI 10.1074/jbc.M701823200
    • Saavedra L., Mohamed A., Ma V., Kar S., De Chaves E. P., Internalization of -amyloid peptide by primary neurons in the absence of apolipoprotein E Journal of Biological Chemistry 2007 282 49 35722 35732 (Pubitemid 350277136)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35722-35732
    • Saavedra, L.1    Mohamed, A.2    Ma, V.3    Kar, S.4    De Chaves, E.P.5
  • 67
    • 0032589297 scopus 로고    scopus 로고
    • 2-Macroglobulin enhances the clearance of endogenous soluble β- amyloid peptide via low-density lipoprotein receptor-related protein in cortical neurons
    • DOI 10.1046/j.1471-4159.1999.0731393.x
    • Qiu Z., Strickland D. K., Hyman B. T., Rebeck G. W., -macroglobulin enhances the clearance of endogenous soluble -amyloid peptide via low-density lipoprotein receptor-related protein in cortical neurons Journal of Neurochemistry 1999 73 4 1393 1398 (Pubitemid 29440138)
    • (1999) Journal of Neurochemistry , vol.73 , Issue.4 , pp. 1393-1398
    • Qiu, Z.1    Strickland, D.K.2    Hyman, B.T.3    Rebeck, G.W.4
  • 68
    • 0030611584 scopus 로고    scopus 로고
    • 2-macroglobulin complexes with and mediates the endocytosis of β- amyloid peptide via cell surface low-density lipoprotein receptor-related protein
    • Narita M., Holtzman D. M., Schwartz A. L., Bu G., -macroglobulin complexes with and mediates the endocytosis of -amyloid peptide via cell surface low-density lipoprotein receptor-related protein Journal of Neurochemistry 1997 69 5 1904 1911 (Pubitemid 27452736)
    • (1997) Journal of Neurochemistry , vol.69 , Issue.5 , pp. 1904-1911
    • Narita, M.1    Holtzman, D.M.2    Schwartz, A.L.3    Bu, G.4
  • 70
    • 0030607177 scopus 로고    scopus 로고
    • Rapid cellular uptake of Alzheimer amyloid βA4 peptide by cultured human neuroblastoma cells
    • DOI 10.1016/0014-5793(96)00948-9
    • Ida N., Masters C. L., Beyreuther K., Rapid cellular uptake of Alzheimer amyloid A4 peptide by cultured human neuroblastoma cells FEBS Letters 1996 394 2 174 178 (Pubitemid 26341500)
    • (1996) FEBS Letters , vol.394 , Issue.2 , pp. 174-178
    • Ida, N.1    Masters, C.L.2    Beyreuther, K.3
  • 73
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • DOI 10.1038/nrm2216, PII NRM2216
    • Mayor S., Pagano R. E., Pathways of clathrin-independent endocytosis Nature Reviews Molecular Cell Biology 2007 8 8 603 612 (Pubitemid 47106613)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 75
    • 77949271604 scopus 로고    scopus 로고
    • Endocytosis unplugged: Multiple ways to enter the cell
    • Kumari S., Mg S., Mayor S., Endocytosis unplugged: multiple ways to enter the cell Cell Research 2010 20 3 256 275
    • (2010) Cell Research , vol.20 , Issue.3 , pp. 256-275
    • Kumari, S.1    Mg, S.2    Mayor, S.3
  • 76
    • 55849118128 scopus 로고    scopus 로고
    • Apolipoprotein e and cholesterol in aging and disease in the brain
    • de Chaves E. P., Narayanaswami V., Apolipoprotein E and cholesterol in aging and disease in the brain Future Lipidology 2008 3 5 505 530
    • (2008) Future Lipidology , vol.3 , Issue.5 , pp. 505-530
    • De Chaves, E.P.1    Narayanaswami, V.2
  • 77
    • 68249134074 scopus 로고    scopus 로고
    • The role of apolipoprotein e in Alzheimer's disease
    • Kim J., Basak J. M., Holtzman D. M., The role of apolipoprotein E in Alzheimer's disease Neuron 2009 63 3 287 303
    • (2009) Neuron , vol.63 , Issue.3 , pp. 287-303
    • Kim, J.1    Basak, J.M.2    Holtzman, D.M.3
  • 78
    • 67349270965 scopus 로고    scopus 로고
    • Apolipoprotein e and its receptors in Alzheimer's disease: Pathways, pathogenesis and therapy
    • Bu G., Apolipoprotein e and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy Nature Reviews Neuroscience 2009 10 5 333 344
    • (2009) Nature Reviews Neuroscience , vol.10 , Issue.5 , pp. 333-344
    • Bu, G.1
  • 80
    • 0028018114 scopus 로고
    • Apolipoprotein E is present in hippocampal neurons without neurofibrillary tangles in Alzheimer's disease and in age-matched controls
    • DOI 10.1006/exnr.1994.1108
    • Han S. H., Hulette C., Saunders A. M., Einstein G., Pericak-Vance M., Strittmatter W. J., Roses A. D., Schmechel D. E., Apolipoprotein E is present in hippocampal neurons without neurofibrillary tangles in Alzheimer's disease and in age-matched controls Experimental Neurology 1994 128 1 13 26 (Pubitemid 24278361)
    • (1994) Experimental Neurology , vol.128 , Issue.1 , pp. 13-26
    • Han, S.-H.1    Hulette, C.2    Saunders, A.M.3    Einstein, G.4    Pericak-Vance, M.5    Strittmatter, W.J.6    Roses, A.D.7    Schmechel, D.E.8
  • 82
    • 33846021307 scopus 로고    scopus 로고
    • Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Aβ42 accumulation in amyloid model mice
    • DOI 10.1074/jbc.M604436200
    • Zerbinatti C. V., Wahrle S. E., Kim H., Cam J. A., Bales K., Paul S. M., Holtzman D. M., Bu G., Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal A 42 accumulation in amyloid model mice Journal of Biological Chemistry 2006 281 47 36180 36186 (Pubitemid 46041352)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 36180-36186
    • Zerbinatti, C.V.1    Wahrle, S.E.2    Kim, H.3    Cam, J.A.4    Bales, K.5    Paul, S.M.6    Holtzman, D.M.7    Bu, G.8
  • 83
    • 0036848549 scopus 로고    scopus 로고
    • Increased extracellular amyloid deposition and neurodegeneration in human amyloid precursor protein transgenic mice deficient in receptor-associated protein
    • Van Uden E., Mallory M., Veinbergs I., Alford M., Rockenstein E., Masliah E., Increased extracellular amyloid deposition and neurodegeneration in human amyloid precursor protein transgenic mice deficient in receptor-associated protein Journal of Neuroscience 2002 22 21 9298 9304 (Pubitemid 35356173)
    • (2002) Journal of Neuroscience , vol.22 , Issue.21 , pp. 9298-9304
    • Van Uden, E.1    Mallory, M.2    Veinbergs, I.3    Alford, M.4    Rockenstein, E.5    Masliah, E.6
  • 84
    • 0037343967 scopus 로고    scopus 로고
    • Apolipoprotein E enhances uptake of soluble but not aggregated amyloid-β protein into synaptic terminals
    • DOI 10.1046/j.1471-4159.2003.01643.x
    • Gylys K. H., Fein J. A., Tan A. M., Cole G. M., Apolipoprotein E enhances uptake of soluble but not aggregated amyloid- protein into synaptic terminals Journal of Neurochemistry 2003 84 6 1442 1451 (Pubitemid 36343610)
    • (2003) Journal of Neurochemistry , vol.84 , Issue.6 , pp. 1442-1451
    • Gylys, K.H.1    Fein, J.A.2    Tan, A.M.3    Cole, G.M.4
  • 88
    • 0031882562 scopus 로고    scopus 로고
    • β-Amyloid peptides increase the binding and internalization of apolipoprotein E to hippocampal neurons
    • Beffert U., Aumont N., Dea D., Lussier-Cacan S., Davignon J., Poirier J., -amyloid peptides increase the binding and internalization of apolipoprotein E to hippocampal neurons Journal of Neurochemistry 1998 70 4 1458 1466 (Pubitemid 28136958)
    • (1998) Journal of Neurochemistry , vol.70 , Issue.4 , pp. 1458-1466
    • Beffert, U.1    Aumont, N.2    Dea, D.3    Lussier-Cacan, S.4    Davignon, J.5    Poirier, J.6
  • 89
    • 0032903412 scopus 로고    scopus 로고
    • Apolipoprotein E promotes the binding and uptake of β-amyloid into Chinese hamster ovary cells in an isoform-specific manner
    • DOI 10.1016/S0306-4522(98)00561-2, PII S0306452298005612
    • Yang D. S., Small D. H., Seydel U., Smith J. D., Hallmayer J., Gandy S. E., Martins R. N., Apolipoprotein E promotes the binding and uptake of -amyloid into Chinese hamster ovary cells in an isoform-specific manner Neuroscience 1999 90 4 1217 1226 (Pubitemid 29170140)
    • (1999) Neuroscience , vol.90 , Issue.4 , pp. 1217-1226
    • Yang, D.-S.1    Small, D.H.2    Seydel, U.3    Smith, J.D.4    Hallmayer, J.5    Gandy, S.E.6    Martins, R.N.7
  • 90
    • 0033532373 scopus 로고    scopus 로고
    • Apolipoprotein E isoform-specific reduction of extracellular amyloid in neuronal cultures
    • DOI 10.1016/S0169-328X(99)00073-X, PII S0169328X9900073X
    • Beffert U., Aumont N., Dea D., Lussier-Cacan S., Davignon J., Poirier J., Apolipoprotein E isoform-specific reduction of extracellular amyloid in neuronal cultures Molecular Brain Research 1999 68 1-2 181 185 (Pubitemid 29244006)
    • (1999) Molecular Brain Research , vol.68 , Issue.1-2 , pp. 181-185
    • Beffert, U.1    Aumont, N.2    Dea, D.3    Lussier-Cacan, S.4    Davignon, J.5    Poirier, J.6
  • 91
    • 78149255128 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein-1: A serial clearance homeostatic mechanism controlling Alzheimer's amyloid -peptide elimination from the brain
    • Zlokovic B. V., Deane R., Sagare A. P., Bell R. D., Winkler E. A., Low-density lipoprotein receptor-related protein-1: a serial clearance homeostatic mechanism controlling Alzheimer's amyloid -peptide elimination from the brain Journal of Neurochemistry 2010 115 5 1077 1089
    • (2010) Journal of Neurochemistry , vol.115 , Issue.5 , pp. 1077-1089
    • Zlokovic, B.V.1    Deane, R.2    Sagare, A.P.3    Bell, R.D.4    Winkler, E.A.5
  • 93
    • 33846680684 scopus 로고    scopus 로고
    • Do caveolins regulate cells by actions outside of caveolae?
    • DOI 10.1016/j.tcb.2006.11.008, PII S0962892406003357
    • Head B. P., Insel P. A., Do caveolins regulate cells by actions outside of caveolae? Trends in Cell Biology 2007 17 2 51 57 (Pubitemid 46199179)
    • (2007) Trends in Cell Biology , vol.17 , Issue.2 , pp. 51-57
    • Head, B.P.1    Insel, P.A.2
  • 94
    • 24944523300 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: New insights into caveolae and non-caveolar lipid raft carriers
    • DOI 10.1016/j.bbamcr.2005.06.002, PII S0167488905001047
    • Kirkham M., Parton R. G., Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers Biochimica et Biophysica Acta 2005 1745 3 273 286 (Pubitemid 41330782)
    • (2005) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1745 , Issue.3 , pp. 273-286
    • Kirkham, M.1    Parton, R.G.2
  • 95
    • 77953260312 scopus 로고    scopus 로고
    • Intracellular cholesterol homeostasis and amyloid precursor protein processing
    • Burns M. P., Rebeck G. W., Intracellular cholesterol homeostasis and amyloid precursor protein processing Biochimica et Biophysica Acta 2010 1801 8 853 859
    • (2010) Biochimica et Biophysica Acta , vol.1801 , Issue.8 , pp. 853-859
    • Burns, M.P.1    Rebeck, G.W.2
  • 96
    • 77956994435 scopus 로고    scopus 로고
    • Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: Common mechanisms in neurodegenerative diseases
    • Fantini J., Yahi N., Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases Expert Reviews in Molecular Medicine 2010 12, article e27
    • (2010) Expert Reviews in Molecular Medicine , vol.1227
    • Fantini, J.1    Yahi, N.2
  • 97
    • 77953235479 scopus 로고    scopus 로고
    • A polymerization through interaction with membrane gangliosides
    • Matsuzaki K., Kato K., Yanagisawa K., A polymerization through interaction with membrane gangliosides Biochimica et Biophysica Acta 2010 1801 8 868 877
    • (2010) Biochimica et Biophysica Acta , vol.1801 , Issue.8 , pp. 868-877
    • Matsuzaki, K.1    Kato, K.2    Yanagisawa, K.3
  • 98
    • 0036793543 scopus 로고    scopus 로고
    • Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AβP (1-40) and (1-42) peptides
    • DOI 10.1096/fj.02-0829com
    • Arispe N., Doh M., Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease A P (140) and (142) peptides FASEB Journal 2002 16 12 1526 1536 (Pubitemid 35154635)
    • (2002) FASEB Journal , vol.16 , Issue.12 , pp. 1526-1536
    • Arispe, N.1    Doh, M.2
  • 99
    • 34547118151 scopus 로고    scopus 로고
    • Formation of Amyloids by Aβ-(1-42) on NGF-differentiated PC12 Cells: Roles of Gangliosides and Cholesterol
    • DOI 10.1016/j.jmb.2007.06.008, PII S0022283607007905
    • Wakabayashi M., Matsuzaki K., Formation of amyloids by A -(142) on NGF-differentiated PC12 cells: roles of gangliosides and cholesterol Journal of Molecular Biology 2007 371 4 924 933 (Pubitemid 47101820)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.4 , pp. 924-933
    • Wakabayashi, M.1    Matsuzaki, K.2
  • 100
    • 0035943343 scopus 로고    scopus 로고
    • Cholesterol, a modulator of membrane-associated Aβ-fibrillogenesis and neurotoxicity
    • DOI 10.1006/jmbi.2001.4881
    • Yip C. M., Elton E. A., Darabie A. A., Morrison M. R., Mclaurin J., Cholesterol, a modulator of membrane-associated A -fibrillogenesis and neurotoxicity Journal of Molecular Biology 2001 311 4 723 734 (Pubitemid 32803731)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.4 , pp. 723-734
    • Yip, C.M.1    Elton, E.A.2    Darabie, A.A.3    Morrison, M.R.4    Mclaurin, J.5
  • 101
    • 0010620607 scopus 로고    scopus 로고
    • Elevation of ceramide within distal neurites inhibits neurite growth in cultured rat sympathetic neurons
    • DOI 10.1074/jbc.272.5.3028
    • Posse de Chaves E. I., Bussire M., Vance D. E., Campenot R. B., Vance J. E., Elevation of ceramide within distal neurites inhibits neurite growth in cultured rat sympathetic neurons Journal of Biological Chemistry 1997 272 5 3028 3035 (Pubitemid 27053357)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.5 , pp. 3028-3035
    • Posse De Chaves, E.I.1    Bussiere, M.2    Vance, D.E.3    Campenot, R.B.4    Vance, J.E.5
  • 102
    • 33645026907 scopus 로고    scopus 로고
    • The role of nicotinic acetylcholine receptors in Alzheimer's disease
    • Oddo S., LaFerla F. M., The role of nicotinic acetylcholine receptors in Alzheimer's disease Journal of Physiology Paris 2006 99 2-3 172 179
    • (2006) Journal of Physiology Paris , vol.99 , Issue.23 , pp. 172-179
    • Oddo, S.1    Laferla, F.M.2
  • 103
    • 63849213473 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor signalling: Roles in alzheimer's disease and amyloid neuroprotection
    • Buckingham S. D., Jones A. K., Brown L. A., Sattelle D. B., Nicotinic acetylcholine receptor signalling: roles in alzheimer's disease and amyloid neuroprotection Pharmacological Reviews 2009 61 1 39 61
    • (2009) Pharmacological Reviews , vol.61 , Issue.1 , pp. 39-61
    • Buckingham, S.D.1    Jones, A.K.2    Brown, L.A.3    Sattelle, D.B.4
  • 104
    • 67549106996 scopus 로고    scopus 로고
    • Cellular trafficking of nicotinic acetylcholine receptors
    • John P. A. S., Cellular trafficking of nicotinic acetylcholine receptors Acta Pharmacologica Sinica 2009 30 6 656 662
    • (2009) Acta Pharmacologica Sinica , vol.30 , Issue.6 , pp. 656-662
    • John, P.A.S.1
  • 105
    • 0034006944 scopus 로고    scopus 로고
    • 1-42 binds to α7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology
    • DOI 10.1074/jbc.275.8.5626
    • Wang H.-Y., Lee D. H. S., D'Andrea M. R., Peterson P. A., Shank R. P., Reitz A. B., -Amyloid142 binds to 7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology Journal of Biological Chemistry 2000 275 8 5626 5632 (Pubitemid 30115201)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.8 , 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
  • 106
    • 0033624509 scopus 로고    scopus 로고
    • 1-42 binds selectively and with picomolar affinity to α7 nicotinic acetylcholine receptors
    • DOI 10.1046/j.1471-4159.2000.0751155.x
    • Wang H.-Y., Lee D. H. S., Davis C. B., Shank R. P., Amyloid peptide A 1-42 binds selectively and with picomolar affinity to 7 nicotinic acetylcholine receptors Journal of Neurochemistry 2000 75 3 1155 1161 (Pubitemid 30660505)
    • (2000) Journal of Neurochemistry , vol.75 , Issue.3 , pp. 1155-1161
    • Wang, H.-Y.1    Lee, D.H.S.2    Davis, C.B.3    Shank, R.P.4
  • 107
    • 76849083911 scopus 로고    scopus 로고
    • S 24795 limits -amyloid- 7 nicotinic receptor interaction and reduces Alzheimer's disease-like pathologies
    • Wang H. Y., Bakshi K., Shen C., Frankfurt M., Trocm-Thibierge C., Morain P., S 24795 limits -amyloid- 7 nicotinic receptor interaction and reduces Alzheimer's disease-like pathologies Biological Psychiatry 2010 67 6 522 530
    • (2010) Biological Psychiatry , vol.67 , Issue.6 , pp. 522-530
    • Wang, H.Y.1    Bakshi, K.2    Shen, C.3    Frankfurt, M.4    Trocm-Thibierge, C.5    Morain, P.6
  • 109
    • 77249153190 scopus 로고    scopus 로고
    • Loss of 7 nicotinic receptors enhances -amyloid oligomer accumulation, exacerbating early-stage cognitive decline and septohippocampal pathology in a mouse model of Alzheimer's disease
    • Hernandez C. M., Kayed R., Zheng H., Sweatt J. D., Dineley K. T., Loss of 7 nicotinic receptors enhances -amyloid oligomer accumulation, exacerbating early-stage cognitive decline and septohippocampal pathology in a mouse model of Alzheimer's disease Journal of Neuroscience 2010 30 7 2442 2453
    • (2010) Journal of Neuroscience , vol.30 , Issue.7 , pp. 2442-2453
    • Hernandez, C.M.1    Kayed, R.2    Zheng, H.3    Sweatt, J.D.4    Dineley, K.T.5
  • 110
    • 67650484613 scopus 로고    scopus 로고
    • Deletion of the 7 nicotinic acetylcholine receptor gene improves cognitive deficits and synaptic pathology in a mouse model of Alzheimer's disease
    • Dziewczapolski G., Glogowski C. M., Masliah E., Heinemann S. F., Deletion of the 7 nicotinic acetylcholine receptor gene improves cognitive deficits and synaptic pathology in a mouse model of Alzheimer's disease Journal of Neuroscience 2009 29 27 8805 8815
    • (2009) Journal of Neuroscience , vol.29 , Issue.27 , pp. 8805-8815
    • Dziewczapolski, G.1    Glogowski, C.M.2    Masliah, E.3    Heinemann, S.F.4
  • 111
    • 0037146905 scopus 로고    scopus 로고
    • Neuroprotection by memantine against neurodegeneration induced by β-amyloid(1-40)
    • DOI 10.1016/S0006-8993(02)03731-9, PII S0006899302037319
    • Miguel-Hidalgo J. J., Alvarez X. A., Cacabelos R., Quack G., Neuroprotection by memantine against neurodegeneration induced by -amyloid(1-40) Brain Research 2002 958 1 210 221 (Pubitemid 35441230)
    • (2002) Brain Research , vol.958 , Issue.1 , pp. 210-221
    • Miguel-Hidalgo, J.J.1    Alvarez, X.A.2    Cacabelos, R.3    Quack, G.4
  • 113
    • 77954466407 scopus 로고    scopus 로고
    • Amyloid- peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3 in primary cultured hippocampal neurons
    • Decker H., Lo K. Y., Unger S. M., Ferreira S. T., Silverman M. A., Amyloid- peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3 in primary cultured hippocampal neurons Journal of Neuroscience 2010 30 27 9166 9171
    • (2010) Journal of Neuroscience , vol.30 , Issue.27 , pp. 9166-9171
    • Decker, H.1    Lo, K.Y.2    Unger, S.M.3    Ferreira, S.T.4    Silverman, M.A.5
  • 114
    • 0026570528 scopus 로고
    • Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M. P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R. E., -amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity Journal of Neuroscience 1992 12 2 376 389
    • (1992) Journal of Neuroscience , vol.12 , Issue.2 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 115
    • 0034307558 scopus 로고    scopus 로고
    • Transient NMDA receptor inactivation provides long-term protection cultured cortical neurons from a variety of death signals
    • Tremblay R., Chakravarthy B., Hewitt K., Tauskela J., Morley P., Atkinson T., Durkin J. P., Transient NMDA receptor inactivation provides long-term protection cultured cortical neurons from a variety of death signals Journal of Neuroscience 2000 20 19 7183 7192
    • (2000) Journal of Neuroscience , vol.20 , Issue.19 , pp. 7183-7192
    • Tremblay, R.1    Chakravarthy, B.2    Hewitt, K.3    Tauskela, J.4    Morley, P.5    Atkinson, T.6    Durkin, J.P.7
  • 116
    • 55949126654 scopus 로고    scopus 로고
    • Memantine protects rat cortical cultured neurons against -amyloid-induced toxicity by attenuating tau phosphorylation
    • Song M. S., Rauw G., Baker G. B., Kar S., Memantine protects rat cortical cultured neurons against -amyloid-induced toxicity by attenuating tau phosphorylation European Journal of Neuroscience 2008 28 10 1989 2002
    • (2008) European Journal of Neuroscience , vol.28 , Issue.10 , pp. 1989-2002
    • Song, M.S.1    Rauw, G.2    Baker, G.B.3    Kar, S.4
  • 118
    • 48949117577 scopus 로고    scopus 로고
    • The role of the cell surface LRP and soluble LRP in blood-brain barrier Aβ clearance in Alzheimer's disease
    • DOI 10.2174/138161208784705487
    • Dearie R., Sagare A., Zlokovic B. V., The role of the cell surface LRP and soluble LRP in blood-brain barrier A clearance in Alzheimer's disease Current Pharmaceutical Design 2008 14 16 1601 1605 (Pubitemid 352002987)
    • (2008) Current Pharmaceutical Design , vol.14 , Issue.16 , pp. 1601-1605
    • Dearie, R.1    Sagare, A.2    Zlokovic, B.V.3
  • 121
    • 0034840664 scopus 로고    scopus 로고
    • Involvement of microglial receptor for advanced glycation endproducts (RAGE)in Alzheimer's disease: Identification of a cellular activation mechanism
    • DOI 10.1006/exnr.2001.7732
    • Lue L. F., Walker D. G., Brachova L., Beach T. G., Rogers J., Schmidt A. M., Stern D. M., Yan S. D., Involvement of microglial receptor for advanced glycation endproducts (RAGE)in Alzheimer's disease: identification of a cellular activation mechanism Experimental Neurology 2001 171 1 29 45 (Pubitemid 32848443)
    • (2001) Experimental Neurology , vol.171 , Issue.1 , pp. 29-45
    • Lue, L.-F.1    Walker, D.G.2    Brachova, L.3    Beach, T.G.4    Rogers, J.5    Schmidt, A.M.6    Stern, D.M.7    Yan, S.D.8
  • 123
    • 0035110055 scopus 로고    scopus 로고
    • Lysosomal membrane damage in soluble Aβ-mediated cell death in Alzheimer's disease
    • DOI 10.1006/nbdi.2000.0364
    • Ditaranto K., Tekirian T. L., Yang A. J., Lysosomal membrane damage in soluble A -mediated cell death in Alzheimer's disease Neurobiology of Disease 2001 8 1 19 31 (Pubitemid 32171815)
    • (2001) Neurobiology of Disease , vol.8 , Issue.1 , pp. 19-31
    • Ditaranto, K.1    Tekirian, T.L.2    Yang, A.J.3
  • 124
    • 33646461282 scopus 로고    scopus 로고
    • β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • DOI 10.1523/JNEUROSCI.5078-05.2006
    • Almeida C. G., Takahashi R. H., Gouras G. K., -amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system Journal of Neuroscience 2006 26 16 4277 4288 (Pubitemid 44315387)
    • (2006) Journal of Neuroscience , vol.26 , Issue.16 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 128
    • 11444267601 scopus 로고    scopus 로고
    • Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases
    • DOI 10.1016/j.neurobiolaging.2004.09.018, PII S0197458004002945, Developmental Origins of Aging in the Brain and Blood Vessels
    • Nixon R. A., Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases Neurobiology of Aging 2005 26 3 373 382 (Pubitemid 40082721)
    • (2005) Neurobiology of Aging , vol.26 , Issue.3 , pp. 373-382
    • Nixon, R.A.1
  • 129
    • 2442476459 scopus 로고    scopus 로고
    • Lysosomes in cell death
    • DOI 10.1038/sj.onc.1207512
    • Guicciardi M. E., Leist M., Gores G. J., Lysosomes in cell death Oncogene 2004 23 16 2881 2890 (Pubitemid 38638850)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISSUE 2 , pp. 2881-2890
    • Guicciardi, M.E.1    Leist, M.2    Gores, G.J.3
  • 130
    • 77953782590 scopus 로고    scopus 로고
    • Membrane localization of -amyloid 142 in lysosomes: A possible mechanism for lysosome labilization
    • Liu R. Q., Zhou Q. H., Ji S. R., Zhou Q., Feng DU., Wu YI., Sui S. F., Membrane localization of -amyloid 142 in lysosomes: a possible mechanism for lysosome labilization Journal of Biological Chemistry 2010 285 26 19986 19996
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.26 , pp. 19986-19996
    • Liu, R.Q.1    Zhou, Q.H.2    Ji, S.R.3    Zhou, Q.4    Feng, D.U.5    Wu, Y.I.6    Sui, S.F.7
  • 131
    • 0033005082 scopus 로고    scopus 로고
    • Inhibitors of V-type ATPases, bafilomycin A1 and concanamycin A, protect against β-amyloid-mediated effects on 3-(4,5-dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide (MTT) reduction
    • DOI 10.1046/j.1471-4159.1999.0721939.x
    • Kane M. D., Schwarz R. D., Pierre L. S., Watson M. D., Emmerling M. R., Boxer P. A., Walker G. K., Inhibitors of V-type ATPases, bafilomycin A1 and concanamycin A, protect against -amyloid-mediated effects on 3-(4,5-dimethylthiazol-2-yl)-2,5- diphenyltetrazolium bromide (MTT) reduction Journal of Neurochemistry 1999 72 5 1939 1947 (Pubitemid 29185997)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.5 , pp. 1939-1947
    • Kane, M.D.1    Schwarz, R.D.2    St. Pierre, L.3    Watson, M.D.4    Emmerling, M.R.5    Boxer, P.A.6    Walker, G.K.7
  • 132
    • 33645553416 scopus 로고    scopus 로고
    • Reactivity of apolipoprotein E4 and amyloid β peptide: Lysosomal stability and neurodegeneration
    • DOI 10.1074/jbc.M506646200
    • Ji Z. S., Mllendorff K., Cheng I. H., Miranda R. D., Huang Y., Mahley R. W., Reactivity of apolipoprotein E4 and amyloid peptide: lysosomal stability and neurodegeneration Journal of Biological Chemistry 2006 281 5 2683 2692 (Pubitemid 43845731)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.5 , pp. 2683-2692
    • Ji, Z.-S.1    Mullendorff, K.2    Cheng, I.H.3    Miranda, R.D.4    Huang, Y.5    Mahley, R.W.6
  • 133
    • 0344505216 scopus 로고    scopus 로고
    • β-amyloid increases cathepsin D levels in hippocampus
    • DOI 10.1016/S0304-3940(98)00364-4, PII S0304394098003644
    • Hoffman K. B., Bi X., Pham J. T., Lynch G., -amyloid increases cathepsin D levels in hippocampus Neuroscience Letters 1998 250 2 75 78 (Pubitemid 28348296)
    • (1998) Neuroscience Letters , vol.250 , Issue.2 , pp. 75-78
    • Hoffman, K.B.1    Bi, X.2    Pham, J.T.3    Lynch, G.4
  • 134
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system
    • Cataldo A. M., Barnett J. L., Berman S. A., Li J., Quarless S., Bursztajn S., Lippa C., Nixon R. A., Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal-lysosomal system Neuron 1995 14 3 671 680
    • (1995) Neuron , vol.14 , Issue.3 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3    Li, J.4    Quarless, S.5    Bursztajn, S.6    Lippa, C.7    Nixon, R.A.8
  • 135
    • 0033025080 scopus 로고    scopus 로고
    • Quantitative decrease in synaptophysin message expression and increase in
    • Callahan L. M., Vaules W. A., Coleman P. D., Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles Journal of Neuropathology and Experimental Neurology 1999 58 3 275 287 (Pubitemid 29140968)
    • (1999) Journal of Neuropathology and Experimental Neurology , vol.58 , Issue.3 , pp. 275-287
    • Callahan, L.M.1    Vaules, W.A.2    Coleman, P.D.3
  • 136
    • 0033933738 scopus 로고    scopus 로고
    • Expression profile of transcripts in Alzheimer's disease tangle-bearing CA1 neurons
    • DOI 10.10 02/1531-82 49(2000 07)48:1<77::AID-AN A12>3.0.CO;2-A
    • Ginsberg S. D., Hemby S. E., Lee V. M. Y., Eberwine J. H., Trojanowski J. Q., Expression profile of transcripts in Alzheimer's disease tangle-bearing CA1 neurons Annals of Neurology 2000 48 1 77 87 (Pubitemid 30432434)
    • (2000) Annals of Neurology , vol.48 , Issue.1 , pp. 77-87
    • Ginsberg, S.D.1    Hemby, S.E.2    Lee, V.M.-Y.3    Eberwine, J.H.4    Trojanowski, J.Q.5
  • 137
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: Neuropathologic evidence for a mechanism of increased β-amyloidogenesis
    • Cataldo A. M., Barnett J. L., Pieroni C., Nixon R. A., Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased -amyloidogenesis Journal of Neuroscience 1997 17 16 6142 6151 (Pubitemid 27329890)
    • (1997) Journal of Neuroscience , vol.17 , Issue.16 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 138
    • 1242316263 scopus 로고    scopus 로고
    • Intracellular Accumulation of Amyloidogenic Fragments of Amyloid-β Precursor Protein in Neurons with Niemann-Pick Type C Defects Is Associated with Endosomal Abnormalities
    • Jin L. W., Maezawa I., Vincent I., Bird T., Intracellular accumulation of amyloidogenic fragments of amyloid- precursor protein in neurons with niemann-pick type C defects is associated with endosomal abnormalities American Journal of Pathology 2004 164 3 975 985 (Pubitemid 38235479)
    • (2004) American Journal of Pathology , vol.164 , Issue.3 , pp. 975-985
    • Jin, L.-W.1    Maezawa, I.2    Vincent, I.3    Bird, T.4
  • 139
    • 0842290742 scopus 로고    scopus 로고
    • What is the Importance of Multivesicular Bodies in Retrograde Axonal Transport In Vivo?
    • DOI 10.1002/neu.10318
    • Weible M. W., Hendry I. A., What is the importance of multivesicular bodies in retrograde axonal transport in vivo? Journal of Neurobiology 2004 58 2 230 243 (Pubitemid 38173721)
    • (2004) Journal of Neurobiology , vol.58 , Issue.2 , pp. 230-243
    • Weible II, M.W.1    Hendry, I.A.2
  • 140
    • 0344288278 scopus 로고    scopus 로고
    • Amyloid beta-protein interactions with membranes and cholesterol: Causes or casualties of Alzheimer's disease
    • DOI 10.1016/S0005-2736(03)00025-7
    • Wood W. G., Eckert G. P., Igbavboa U., Mller W. E., Amyloid beta-protein interactions with membranes and cholesterol: causes or casualties of Alzheimer's disease Biochimica et Biophysica Acta 2003 1610 2 281 290 (Pubitemid 36324471)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1610 , Issue.2 , pp. 281-290
    • Wood, W.G.1    Eckert, G.P.2    Igbavboa, U.3    Muller, W.E.4
  • 142
    • 33749620373 scopus 로고    scopus 로고
    • Rab5 and Rab7 Control Endocytic Sorting along the Axonal Retrograde Transport Pathway
    • DOI 10.1016/j.neuron.2006.08.018, PII S0896627306006404
    • Deinhardt K., Salinas S., Verastegui C., Watson R., Worth D., Hanrahan S., Bucci C., Schiavo G., Rab5 and Rab7 control endocytic sorting along the axonal retrograde transport pathway Neuron 2006 52 2 293 305 (Pubitemid 44548343)
    • (2006) Neuron , vol.52 , Issue.2 , pp. 293-305
    • Deinhardt, K.1    Salinas, S.2    Verastegui, C.3    Watson, R.4    Worth, D.5    Hanrahan, S.6    Bucci, C.7    Schiavo, G.8
  • 143
    • 0030661651 scopus 로고    scopus 로고
    • Role of lipoproteins in the delivery of lipids to axons during axonal regeneration
    • DOI 10.1074/jbc.272.49.30766
    • Posse de Chaves E. I., Rusinol A. E., Vance D. E., Campenot R. B., Vance J. E., Role of lipoproteins in the delivery of lipids to axons during axonal regeneration Journal of Biological Chemistry 1997 272 49 30766 30773 (Pubitemid 27527513)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.49 , pp. 30766-30773
    • Posse De Chaves, E.I.1    Rusinol, A.E.2    Vance, D.E.3    Campenot, R.B.4    Vance, J.E.5
  • 144
    • 0037303935 scopus 로고    scopus 로고
    • Traffic at the intersection of neurotrophic factor signaling and neurodegeneration
    • DOI 10.1016/S0166-2236(02)00038-3, PII S0166223602000383
    • Salehi A., Delcroix J. D., Mobley W. C., Traffic at the intersection of neurotrophic factor signaling and neurodegeneration Trends in Neurosciences 2003 26 2 73 80 (Pubitemid 36110541)
    • (2003) Trends in Neurosciences , vol.26 , Issue.2 , pp. 73-80
    • Salehi, A.1    Delcroix, J.-D.2    Mobley, W.C.3
  • 145
    • 1542283606 scopus 로고    scopus 로고
    • Alzheimer's disease and NGF signaling
    • DOI 10.1007/s00702-003-0091-x, Modelling Alzheimers Dementia
    • Salehi A., Delcroix J. D., Swaab D. F., Alzheimer's disease and NGF signaling Journal of Neural Transmission 2004 111 3 323 345 (Pubitemid 38316609)
    • (2004) Journal of Neural Transmission , vol.111 , Issue.3 , pp. 323-345
    • Salehi, A.1    Delcroix, J.-D.2    Swaab, D.F.3
  • 147
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • DOI 10.1038/nrm973
    • Katzmann D. J., Odorizzi G., Emr S. D., Receptor downregulation and multivesicular-body sorting Nature Reviews Molecular Cell Biology 2002 3 12 893 905 (Pubitemid 35477368)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.12 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 149
    • 27644522515 scopus 로고    scopus 로고
    • Amyloid peptide attenuates the proteasome activity in neuronal cells
    • DOI 10.1016/j.mad.2005.07.006, PII S0047637405001776
    • Oh S., Hong H. S., Hwang E., Sim H. J., Lee W., Shin SU. J., Mook-Jung I., Amyloid peptide attenuates the proteasome activity in neuronal cells Mechanisms of Ageing and Development 2005 126 12 1292 1299 (Pubitemid 41572246)
    • (2005) Mechanisms of Ageing and Development , vol.126 , Issue.12 , pp. 1292-1299
    • Oh, S.1    Hong, H.S.2    Hwang, E.3    Sim, H.J.4    Lee, W.5    Shin, S.J.6    Mook-Jung, I.7
  • 152
    • 0032535717 scopus 로고    scopus 로고
    • Effects of transforming growth factor-β (isoforms 1-3) on amyloid-β deposition, inflammation, and cell targeting in organotypic hippocampal slice cultures
    • Harris-White M. E., Chu T., Baiverde Z., Sigel J. J., Flanders K. C., Frautschy S. A., Effects of transforming growth factor- (isoforms 13) on amyloid- deposition, inflammation, and cell targeting in organotypic hippocampal slice cultures Journal of Neuroscience 1998 18 24 10366 10374 (Pubitemid 29016556)
    • (1998) Journal of Neuroscience , vol.18 , Issue.24 , pp. 10366-10374
    • Harris-White, M.E.1    Chu, T.2    Baiverde, Z.3    Sigel, J.J.4    Flanders, K.C.5    Frautschy, S.A.6
  • 153
    • 0036019155 scopus 로고    scopus 로고
    • Intraneuronal APP/Aβ trafficking and plaque formation in β-amyloid precursor protein and presenilin-1 transgenic mice
    • Wirths O., Multhaup G., Czech C., Feldmann N., Blanchard V., Tremp G., Beyreuther K., Pradier L., Bayer T. A., Intraneuronal APP/A trafficking and plaque formation in -amyloid precursor protein and presenilin-1 transgenic mice Brain Pathology 2002 12 3 275 286 (Pubitemid 34743210)
    • (2002) Brain Pathology , vol.12 , Issue.3 , pp. 275-286
    • Wirths, O.1    Multhaup, G.2    Czech, C.3    Feldmann, N.4    Blanchard, V.5    Tremp, G.6    Beyreuther, K.7    Pradier, L.8    Bayer, T.A.9
  • 154
    • 33746214688 scopus 로고    scopus 로고
    • Apoptosis is secondary to non-apoptotic axonal degeneration in neurons exposed to Aβ in distal axons
    • DOI 10.1016/j.neurobiolaging.2005.06.007, PII S0197458005001788
    • Song M. S., Saavedra L., de Chaves E. I. P., Apoptosis is secondary to non-apoptotic axonal degeneration in neurons exposed to A in distal axons Neurobiology of Aging 2006 27 9 1224 1238 (Pubitemid 44088575)
    • (2006) Neurobiology of Aging , vol.27 , Issue.9 , pp. 1224-1238
    • Song, M.-S.1    Saavedra, L.2    De Chaves, E.I.P.3
  • 155
    • 68049131389 scopus 로고    scopus 로고
    • A oligomers and fibrillar aggregates induce different apoptotic pathways in LAN5 neuroblastoma cell cultures
    • Picone P., Carrotta R., Montana G., Nobile M. R., San Biagio P. L., Di Carlo M., A oligomers and fibrillar aggregates induce different apoptotic pathways in LAN5 neuroblastoma cell cultures Biophysical Journal 2009 96 10 4200 4211
    • (2009) Biophysical Journal , vol.96 , Issue.10 , pp. 4200-4211
    • Picone, P.1    Carrotta, R.2    Montana, G.3    Nobile, M.R.4    San Biagio, P.L.5    Di Carlo, M.6
  • 156
    • 50949097728 scopus 로고    scopus 로고
    • Oligomer-specific A toxicity in cell models is mediated by selective uptake
    • Chafekar S. M., Baas F., Scheper W., Oligomer-specific A toxicity in cell models is mediated by selective uptake Biochimica et Biophysica Acta 2008 1782 9 523 531
    • (2008) Biochimica et Biophysica Acta , vol.1782 , Issue.9 , pp. 523-531
    • Chafekar, S.M.1    Baas, F.2    Scheper, W.3
  • 157
    • 0024436506 scopus 로고
    • Relationship of microglia and astrocytes to amyloid deposits of Alzheimer disease
    • DOI 10.1016/0165-5728(89)90115-X
    • Itagaki S., McGeer P. L., Akiyama H., Zhu S., Selkoe D., Relationship of microglia and astrocytes to amyloid deposits of Alzheimer disease Journal of Neuroimmunology 1989 24 3 173 182 (Pubitemid 19271472)
    • (1989) Journal of Neuroimmunology , vol.24 , Issue.3 , pp. 173-182
    • Itagaki, S.1    McGeer, P.L.2    Akiyama, H.3    Zhu, S.4    Selkoe, D.5
  • 158
    • 0024573330 scopus 로고
    • Demonstration of microglial cells in and around senile (neuritic) plaques in the Alzheimer brain. An immunohistochemical study using a novel monoclonal antibody
    • DOI 10.1007/BF00687883
    • Haga S., Akai K., Ishii T., Demonstration of microglial cells in and around senile (neuritic) plaques in the Alzheimer brain. An immunohistochemical study using a novel monoclonal antibody Acta Neuropathologica 1989 77 6 569 575 (Pubitemid 19125369)
    • (1989) Acta Neuropathologica , vol.77 , Issue.6 , pp. 569-575
    • Haga, S.1    Akai, K.2    Ishii, T.3
  • 159
    • 0031927636 scopus 로고    scopus 로고
    • Confocal observation of senile plaques in Alzheimer's disease: Senile plaque morphology and relationship between senile plaques and astrocytes
    • Kato S., Gondo T., Hoshii Y., Takahashi M., Yamada M., Ishihara T., Confocal observation of senile plaques in Alzheimer's disease: senile plaque morphology and relationship between senile plaques and astrocytes Pathology International 1998 48 5 332 340 (Pubitemid 28355156)
    • (1998) Pathology International , vol.48 , Issue.5 , pp. 332-340
    • Kato, S.1    Gondo, T.2    Hoshii, Y.3    Takahashi, M.4    Yamada, M.5    Ishihara, T.6
  • 160
    • 0034295217 scopus 로고    scopus 로고
    • Microglial cells are the driving force in fibrillar plaque formation, whereas astrocytes are a leading factor in plaque degradation
    • Wegiel J., Wang K.-C., Tarnawski M., Lach B., Microglial cells are the driving force in fibrillar plaque formation, whereas astrocytes are a leading factor in plaque degradation Acta Neuropathologica 2000 100 4 356 364 (Pubitemid 30497003)
    • (2000) Acta Neuropathologica , vol.100 , Issue.4 , pp. 356-364
    • Wegiel, J.1    Wang, K.-C.2    Tarnawski, M.3    Lach, B.4
  • 161
    • 37349114621 scopus 로고    scopus 로고
    • Transplanted astrocytes internalize deposited β-amyloid peptides in a transgenic mouse model of Alzheimer's disease
    • DOI 10.1002/glia.20599
    • Pihlaja R., Koistinaho J., Malm T., Sikkil H., Vainio S., Koistinaho M., Transplanted astrocytes internalize deposited -amyloid peptides in a transgenic mouse model of Alzheimer's disease GLIA 2008 56 2 154 163 (Pubitemid 350292308)
    • (2008) GLIA , vol.56 , Issue.2 , pp. 154-163
    • Pihlaja, R.1    Koistinaho, J.2    Malm, T.3    Sikkila, H.4    Vainio, S.5    Koistinaho, M.6
  • 162
    • 0032473596 scopus 로고    scopus 로고
    • Amyloid-β peptide activates cultured astrocytes: Morphological alterations, cytokine induction and nitric oxide release
    • DOI 10.1016/S0006-8993(97)01318-8, PII S0006899397013188
    • Hu J., Akama K. T., Krafft G. A., Chromy B. A., van Eldik L. J., Amyloid- peptide activates cultured astrocytes: morphological alterations, cytokine induction and nitric oxide release Brain Research 1998 785 2 195 206 (Pubitemid 28179382)
    • (1998) Brain Research , vol.785 , Issue.2 , pp. 195-206
    • Hu, J.1    Akama, K.T.2    Krafft, G.A.3    Chromy, B.A.4    Van Eldik, L.J.5
  • 163
    • 0037427384 scopus 로고    scopus 로고
    • Astrocytes accumulate Aβ42 and give rise to astrocytic amyloid plaques in Alzheimer disease brains
    • DOI 10.1016/S0006-8993(03)02361-8
    • Nagele R. G., D'Andrea M. R., Lee H., Venkataraman V., Wang H. Y., Astrocytes accumulate A 42 and give rise to astrocytic amyloid plaques in Alzheimer disease brains Brain Research 2003 971 2 197 209 (Pubitemid 36423321)
    • (2003) Brain Research , vol.971 , Issue.2 , pp. 197-209
    • Nagele, R.G.1    D'Andrea, M.R.2    Lee, H.3    Venkataraman, V.4    Wang, H.-Y.5
  • 166
    • 44149083565 scopus 로고    scopus 로고
    • Neuroprotective and neurotoxic properties of glial cells in the pathogenesis of Alzheimer's disease: Alzheimer's Review Series
    • DOI 10.1111/j.1582-4934.2008.00314.x
    • Farfara D., Lifshitz V., Frenkel D., Neuroprotective and neurotoxic properties of glial cells in the pathogenesis of Alzheimer's disease: Alzheimer's Review Series Journal of Cellular and Molecular Medicine 2008 12 3 762 780 (Pubitemid 351718063)
    • (2008) Journal of Cellular and Molecular Medicine , vol.12 , Issue.3 , pp. 762-780
    • Farfara, D.1    Lifshitz, V.2    Frenkel, D.3
  • 167
    • 77956238695 scopus 로고    scopus 로고
    • Norepinephrine promotes microglia to uptake and degrade amyloid peptide through upregulation of mouse formyl peptide receptor 2 and induction of insulin-degrading enzyme
    • Kong Y., Ruan L., Qian L., Liu X., Le Y., Norepinephrine promotes microglia to uptake and degrade amyloid peptide through upregulation of mouse formyl peptide receptor 2 and induction of insulin-degrading enzyme Journal of Neuroscience 2010 30 35 11848 11857
    • (2010) Journal of Neuroscience , vol.30 , Issue.35 , pp. 11848-11857
    • Kong, Y.1    Ruan, L.2    Qian, L.3    Liu, X.4    Le, Y.5
  • 169
    • 0034744296 scopus 로고    scopus 로고
    • TGF-β1 promotes microglial amyloid-β clearance and reduces plaque burden in transgenic mice
    • DOI 10.1038/87945
    • Wyss-Coray T., Lin C., Yan F., Yu G. Q., Rohde M., Mcconlogue L., Masliah E., Mucke L., TGF- 1 promotes microglial amyloid- clearance and reduces plaque burden in transgenic mice Nature Medicine 2001 7 5 612 618 (Pubitemid 32448330)
    • (2001) Nature Medicine , vol.7 , Issue.5 , pp. 612-618
    • Wyss-Coray, T.1    Lin, C.2    Yan, F.3    Yu, G.-Q.4    Rohde, M.5    Mcconlogue, L.6    Masliah, E.7    Mucke, L.8
  • 170
    • 0033527637 scopus 로고    scopus 로고
    • Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid -peptide by microglial cells
    • Chung H., Brazil M. I., Soe T. T., Maxfield F. R., Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid -peptide by microglial cells Journal of Biological Chemistry 1999 274 45 32301 32308
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.45 , pp. 32301-32308
    • Chung, H.1    Brazil, M.I.2    Soe, T.T.3    Maxfield, F.R.4
  • 172
    • 0031922062 scopus 로고    scopus 로고
    • Astrocytes containing amyloid β-protein (Aβ)-positive granules are associated with aβ40-positive diffuse plaques in the aged human brain
    • Funato H., Yoshimura M., Yamazaki T., Saido T. C., Ito Y., Yokofujita J., Okeda R., Ihara Y., Astrocytes containing amyloid -protein (A )-positive granules are associated with a 40-positive diffuse plaques in the aged human brain American Journal of Pathology 1998 152 4 983 992 (Pubitemid 28173360)
    • (1998) American Journal of Pathology , vol.152 , Issue.4 , pp. 983-992
    • Funato, H.1    Yoshimura, M.2    Yamazaki, T.3    Saido, T.C.4    Ito, Y.5    Yokofujita, J.6    Okeda, R.7    Ihara, Y.8
  • 173
    • 0032840954 scopus 로고    scopus 로고
    • β-Amyloid immunoreactivity in astrocytes in Alzheimer's disease brain biopsies: An electron microscope study
    • DOI 10.1006/exnr.1999.7096
    • Kurt M. A., Davies D. C., Kidd M., -Amyloid immunoreactivity in astrocytes in Alzheimer's disease brain biopsies: an electron microscope study Experimental Neurology 1999 158 1 221 228 (Pubitemid 29344335)
    • (1999) Experimental Neurology , vol.158 , Issue.1 , pp. 221-228
    • Kurt, M.A.1    Davies, D.C.2    Kidd, M.3
  • 174
    • 0037448014 scopus 로고    scopus 로고
    • Specific uptake of Aβ1-40 in rat brain occurs in astrocyte, but not in microglia
    • DOI 10.1016/S0304-3940(03)00240-4
    • Matsunaga W., Shirokawa T., Isobe K., Specific uptake of A 1-40 in rat brain occurs in astrocyte, but not in microglia Neuroscience Letters 2003 342 1-2 129 131 (Pubitemid 36513924)
    • (2003) Neuroscience Letters , vol.342 , Issue.1-2 , pp. 129-131
    • Matsunaga, W.1    Shirokawa, T.2    Isobe, K.3
  • 176
    • 0026783591 scopus 로고
    • Ultrastructure of the microglia that phagocytose amyloid and the microglia that produce -amyloid fibrils
    • Frackowiak J., Wisniewski H. M., Wegiel J., Merz G. S., Iqbal K., Wang K. C., Ultrastructure of the microglia that phagocytose amyloid and the microglia that produce -amyloid fibrils Acta Neuropathologica 1992 84 3 225 233
    • (1992) Acta Neuropathologica , vol.84 , Issue.3 , pp. 225-233
    • Frackowiak, J.1    Wisniewski, H.M.2    Wegiel, J.3    Merz, G.S.4    Iqbal, K.5    Wang, K.C.6
  • 177
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's disease amyloid β-protein via a scavenger receptor
    • DOI 10.1016/S0896-6273(00)80187-7
    • Paresce D. M., Ghosh R. N., Maxfield F. R., Microglial cells internalize aggregates of the Alzheimer's disease amyloid -protein via a scavenger receptor Neuron 1996 17 3 553 565 (Pubitemid 26322226)
    • (1996) Neuron , vol.17 , Issue.3 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 178
    • 0034992123 scopus 로고    scopus 로고
    • 3D-Reconstruction of microglia and amyloid in APP23 transgenic mice: No evidence of intracellular amyloid
    • DOI 10.1016/S0197-4580(01)00209-3, PII S0197458001002093
    • Stalder M., Deller T., Staufenbiel M., Jucker M., 3D-Reconstruction of microglia and amyloid in APP23 transgenic mice: no evidence of intracellular amyloid Neurobiology of Aging 2001 22 3 427 434 (Pubitemid 32510915)
    • (2001) Neurobiology of Aging , vol.22 , Issue.3 , pp. 427-434
    • Stalder, M.1    Deller, T.2    Staufenbiel, M.3    Jucker, M.4
  • 181
    • 0034613449 scopus 로고    scopus 로고
    • Expression of -secretase mRNA in transgenic Tg2576 mouse brain with Alzheimer plaque pathology
    • Bigl M., Apelt J., Luschekina E. A., Lange-Dohna C., Roner S., Schliebs R., Expression of -secretase mRNA in transgenic Tg2576 mouse brain with Alzheimer plaque pathology Neuroscience Letters 2000 292 2 107 110
    • (2000) Neuroscience Letters , vol.292 , Issue.2 , pp. 107-110
    • Bigl, M.1    Apelt, J.2    Luschekina, E.A.3    Lange-Dohna, C.4    Roner, S.5    Schliebs, R.6
  • 182
    • 0027178255 scopus 로고
    • Inability to detect β-amyloid protein precursor mRNA in Alzheimer plaque- associated microglia
    • DOI 10.1006/exnr.1993.1076
    • Scott S. A., Johnson S. A., Zarow C., Perlmutter L. S., Inability to detect -amyloid protein precursor mRNA in Alzheimer plaque- associated microglia Experimental Neurology 1993 121 1 113 118 (Pubitemid 23192197)
    • (1993) Experimental Neurology , vol.121 , Issue.1 , pp. 113-118
    • Scott, S.A.1    Johnson, S.A.2    Zarow, C.3    Perlmutter, L.S.4
  • 185
    • 44949138575 scopus 로고    scopus 로고
    • Increased expression of the -secretase components presenilin-1 and nicastrin in activated astrocytes and microglia following traumatic brain injury
    • Nadler Y., Alexandrovich A., Grigoriadis N., Hartmann T., Jagannatha Rao K. S., Shohami E., Stein R., Increased expression of the -secretase components presenilin-1 and nicastrin in activated astrocytes and microglia following traumatic brain injury GLIA 2008 56 5 552 567
    • (2008) GLIA , vol.56 , Issue.5 , pp. 552-567
    • Nadler, Y.1    Alexandrovich, A.2    Grigoriadis, N.3    Hartmann, T.4    Jagannatha Rao, K.S.5    Shohami, E.6    Stein, R.7
  • 189
    • 33846592417 scopus 로고    scopus 로고
    • Amyloid-β 1-42 induced endocytosis and clusterin/apoJ protein accumulation in cultured human astrocytes
    • DOI 10.1016/j.neuint.2006.11.002, PII S0197018606003317
    • Nuutinen T., Huuskonen J., Suuronen T., Ojala J., Miettinen R., Salminen A., Amyloid- 142 induced endocytosis and clusterin/apoJ protein accumulation in cultured human astrocytes Neurochemistry International 2007 50 3 540 547 (Pubitemid 46186605)
    • (2007) Neurochemistry International , vol.50 , Issue.3 , pp. 540-547
    • Nuutinen, T.1    Huuskonen, J.2    Suuronen, T.3    Ojala, J.4    Miettinen, R.5    Salminen, A.6
  • 191
    • 0035890306 scopus 로고    scopus 로고
    • Multiple receptors mediate apoJ-dependent clearance of cellular debris into nonprofessional phagocytes
    • DOI 10.1006/excr.2001.5358
    • Bartl M. M., Luckenbach T., Bergner O., Ullrich O., Koch-Brandt C., Multiple receptors mediate apoJ-dependent clearance of cellular debris into nonprofessional phagocytes Experimental Cell Research 2001 271 1 130 141 (Pubitemid 33071000)
    • (2001) Experimental Cell Research , vol.271 , Issue.1 , pp. 130-141
    • Bartl, M.M.1    Luckenbach, T.2    Bergner, O.3    Ullrich, O.4    Koch-Brandt, C.5
  • 192
    • 77954375412 scopus 로고    scopus 로고
    • Astrocytic A 142 uptake is determined by A -aggregation state and the presence of amyloid-associated proteins
    • Nielsen H. M., Mulder S. D., Belin J. A. M., Musters R. J. P., Eikelenboom P., Veerhuis R., Astrocytic A 142 uptake is determined by A -aggregation state and the presence of amyloid-associated proteins GLIA 2010 58 10 1235 1246
    • (2010) GLIA , vol.58 , Issue.10 , pp. 1235-1246
    • Nielsen, H.M.1    Mulder, S.D.2    Belin, J.A.M.3    Musters, R.J.P.4    Eikelenboom, P.5    Veerhuis, R.6
  • 193
    • 0036847848 scopus 로고    scopus 로고
    • Scavenger receptors in neurobiology and neuropathology: Their role on microglia and other cells of the nervous system
    • DOI 10.1002/glia.10148
    • Husemann J., Loike J. D., Anankov R., Febbraio M., Silverstein S. C., Scavenger receptors in neurobiology and neuropathology: their role on microglia and other cells of the nervous system GLIA 2002 40 2 195 205 (Pubitemid 35337377)
    • (2002) GLIA , vol.40 , Issue.2 , pp. 195-205
    • Husemann, J.1    Loike, J.D.2    Anankov, R.3    Febbraio, M.4    Silverstein, S.C.5
  • 194
    • 24044503374 scopus 로고    scopus 로고
    • Expression of scavenger receptors in glial cells: Comparing the adhesion of astrocytes and microglia from neonatal rats to surface-bound β-amyloid
    • DOI 10.1074/jbc.M414686200
    • Alarcn R., Fuenzalida C., Santibez M., von Bernhardi R., Expression of scavenger receptors in glial cells: comparing the adhesion of astrocytes and microglia from neonatal rats to surface-bound -amyloid Journal of Biological Chemistry 2005 280 34 30406 30415 (Pubitemid 41216224)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.34 , pp. 30406-30415
    • Alarcon, R.1    Fuenzalida, C.2    Santibanez, M.3    Von Bernhardi, R.4
  • 196
    • 33751211223 scopus 로고    scopus 로고
    • Formyl peptide receptors: A promiscuous subfamily of G protein-coupled receptors controlling immune responses
    • DOI 10.1016/j.cytogfr.2006.09.009, PII S135961010600058X
    • Migeotte I., Communi D., Parmentier M., Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses Cytokine and Growth Factor Reviews 2006 17 6 501 519 (Pubitemid 44793122)
    • (2006) Cytokine and Growth Factor Reviews , vol.17 , Issue.6 , pp. 501-519
    • Migeotte, I.1    Communi, D.2    Parmentier, M.3
  • 197
    • 52949101715 scopus 로고    scopus 로고
    • Involvement of formyl-peptide-receptor-like-1 and phospholipase D in the internalization and signal transduction of amyloid beta 1-42 in glial cells
    • Brandenburg L. O., Konrad M., Wruck C., Koch T., Pufe T., Lucius R., Involvement of formyl-peptide-receptor-like-1 and phospholipase D in the internalization and signal transduction of amyloid beta 1-42 in glial cells Neuroscience 2008 156 2 266 276
    • (2008) Neuroscience , vol.156 , Issue.2 , pp. 266-276
    • Brandenburg, L.O.1    Konrad, M.2    Wruck, C.3    Koch, T.4    Pufe, T.5    Lucius, R.6
  • 199
    • 51649124533 scopus 로고    scopus 로고
    • Leucine-rich glioma inactivated 3 is involved in amyloid peptide uptake by astrocytes and endocytosis itself
    • Okabayashi S., Kimura N., Leucine-rich glioma inactivated 3 is involved in amyloid peptide uptake by astrocytes and endocytosis itself NeuroReport 2008 19 12 1175 1179
    • (2008) NeuroReport , vol.19 , Issue.12 , pp. 1175-1179
    • Okabayashi, S.1    Kimura, N.2
  • 200
    • 0036291154 scopus 로고    scopus 로고
    • A novel member of the leucine-rich repeat superfamily induced in rat astrocytes by β-amyloid
    • DOI 10.1006/bbrc.2001.6272
    • Satoh K., Hata M., Yokota H., A novel member of the leucine-rich repeat superfamily induced in rat astrocytes by -amyloid Biochemical and Biophysical Research Communications 2002 290 2 756 762 (Pubitemid 34687505)
    • (2002) Biochemical and Biophysical Research Communications , vol.290 , Issue.2 , pp. 756-762
    • Satoh, K.1    Hata, M.2    Yokota, H.3
  • 201
    • 0030437795 scopus 로고    scopus 로고
    • Structural and functional diversity in the leucine-rich repeat family of proteins
    • PII S007961079600003X
    • Buchanan S. G. S. C., Gay N. J., Structural and functional diversity in the leucine-rich repeat family of proteins Progress in Biophysics and Molecular Biology 1996 65 1-2 1 44 (Pubitemid 27161007)
    • (1996) Progress in Biophysics and Molecular Biology , vol.65 , Issue.1-2 , pp. 1-44
    • Buchanan, S.G.St.C.1    Gay, N.J.2
  • 202
    • 77953538310 scopus 로고    scopus 로고
    • LGI3 interacts with flotillin-1 to mediate APP trafficking and exosome formation
    • Okabayashi S., Kimura N., LGI3 interacts with flotillin-1 to mediate APP trafficking and exosome formation NeuroReport 2010 21 9 606 610
    • (2010) NeuroReport , vol.21 , Issue.9 , pp. 606-610
    • Okabayashi, S.1    Kimura, N.2
  • 203
    • 67650741983 scopus 로고    scopus 로고
    • Binding and uptake of A 142 by primary human astrocytes in vitro
    • Nielsen H. M., Veerhuis R., Holmqvist BO., Janciauskiene S., Binding and uptake of A 142 by primary human astrocytes in vitro GLIA 2009 57 9 978 988
    • (2009) GLIA , vol.57 , Issue.9 , pp. 978-988
    • Nielsen, H.M.1    Veerhuis, R.2    Holmqvist, B.O.3    Janciauskiene, S.4
  • 204
    • 77956955758 scopus 로고    scopus 로고
    • The role of microglia in amyloid clearance from the AD brain
    • Lee C. Y. D., Landreth G. E., The role of microglia in amyloid clearance from the AD brain Journal of Neural Transmission 2010 117 949 960
    • (2010) Journal of Neural Transmission , vol.117 , pp. 949-960
    • Lee, C.Y.D.1    Landreth, G.E.2
  • 206
    • 7744235869 scopus 로고    scopus 로고
    • 1 integrin-dependent mechanism
    • DOI 10.1523/JNEUROSCI.2557-04.2004
    • Koenigsknecht J., Landreth G., Microglial phagocytosis of fibrillar -amyloid through a 1 integrin-dependent mechanism Journal of Neuroscience 2004 24 44 9838 9846 (Pubitemid 39463564)
    • (2004) Journal of Neuroscience , vol.24 , Issue.44 , pp. 9838-9846
    • Koenigsknecht, J.1    Landreth, G.2
  • 208
    • 33645650780 scopus 로고    scopus 로고
    • Activation of toll-like receptor 2 on microglia promotes cell uptake of alzheimer disease-associated amyloid β peptide
    • DOI 10.1074/jbc.M508125200
    • Chen K., Iribarren P., Hu J., Chen J., Gong W., Cho E. H., Lockett S., Dunlop N. M., Ji M. W., Activation of toll-like receptor 2 on microglia promotes cell uptake of alzheimer disease-associated amyloid peptide Journal of Biological Chemistry 2006 281 6 3651 3659 (Pubitemid 43845983)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3651-3659
    • Chen, K.1    Iribarren, P.2    Hu, J.3    Chen, J.4    Gong, W.5    Cho, E.H.6    Lockett, S.7    Dunlop, N.M.8    Ji, M.W.9
  • 209
    • 33750576993 scopus 로고    scopus 로고
    • Role of toll-like receptor signalling in Aβ uptake and clearance
    • DOI 10.1093/brain/awl249
    • Tahara K., Kim H. D., Jin J. J., Maxwell J. A., Li L., Fukuchi K. I., Role of toll-like receptor signalling in A uptake and clearance Brain 2006 129 11 3006 3019 (Pubitemid 44684521)
    • (2006) Brain , vol.129 , Issue.11 , pp. 3006-3019
    • Tahara, K.1    Kim, H.-D.2    Jin, J.-J.3    Maxwell, J.A.4    Li, L.5    Fukuchi, K.-I.6
  • 210
    • 0037387147 scopus 로고    scopus 로고
    • A cell surface receptor complex for fibrillar β-amyloid mediates microglial activation
    • Bamberger M. E., Harris M. E., McDonald D. R., Husemann J., Landreth G. E., A cell surface receptor complex for fibrillar -amyloid mediates microglial activation Journal of Neuroscience 2003 23 7 2665 2674 (Pubitemid 36418601)
    • (2003) Journal of Neuroscience , vol.23 , Issue.7 , pp. 2665-2674
    • Bamberger, M.E.1    Harris, M.E.2    McDonald, D.R.3    Husemann, J.4    Landreth, G.E.5
  • 211
    • 70349323417 scopus 로고    scopus 로고
    • CD14 and toll-like receptors 2 and 4 are required for fibrillar A -stimulated microglial activation
    • Reed-Geaghan E. G., Savage J. C., Hise A. G., Landreth G. E., CD14 and toll-like receptors 2 and 4 are required for fibrillar A -stimulated microglial activation Journal of Neuroscience 2009 29 38 11982 11992
    • (2009) Journal of Neuroscience , vol.29 , Issue.38 , pp. 11982-11992
    • Reed-Geaghan, E.G.1    Savage, J.C.2    Hise, A.G.3    Landreth, G.E.4
  • 212
    • 0036135610 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide selectively up-regulates the function of the chemotactic peptide receptor formyl peptide receptor 2 in murine microglial cells
    • Cui Y. H., Le Y., Gong W., Proost P., Van Damme J., Murphy W. J., Ji Ming Wang., Bacterial lipopolysaccharide selectively up-regulates the function of the chemotactic peptide receptor formyl peptide receptor 2 in murine microglial cells Journal of Immunology 2002 168 1 434 442 (Pubitemid 34014146)
    • (2002) Journal of Immunology , vol.168 , Issue.1 , pp. 434-442
    • Cui, Y.-H.1    Le, Y.2    Gong, W.3    Proost, P.4    Van Damme, J.5    Murphy, W.J.6    Ji Ming Wang7
  • 213
    • 24744467358 scopus 로고    scopus 로고
    • Microglial phagocytosis induced by fibrillar β-amyloid and IgGs are differentially regulated by proinflammatory cytokines
    • DOI 10.1523/JNEUROSCI.1808-05.2005
    • Koenigsknecht-Talboo J., Landreth G. E., Microglial phagocytosis induced by fibrillar -amyloid and IgGs are differentially regulated by proinflammatory cytokines Journal of Neuroscience 2005 25 36 8240 8249 (Pubitemid 41292118)
    • (2005) Journal of Neuroscience , vol.25 , Issue.36 , pp. 8240-8249
    • Koenigsknecht-Talboo, J.1    Landreth, G.E.2
  • 214
    • 0036849021 scopus 로고    scopus 로고
    • Microglia and inflammatory mechanisms in the clearance of amyloid β peptide
    • DOI 10.1002/glia.10153
    • Rogers J., Strohmeyer R., Kovelowski C. J., Li R., Microglia and inflammatory mechanisms in the clearance of amyloid peptide GLIA 2002 40 2 260 269 (Pubitemid 35337383)
    • (2002) GLIA , vol.40 , Issue.2 , pp. 260-269
    • Rogers, J.1    Strohmeyer, R.2    Kovelowski, C.J.3    Li, R.4
  • 215
    • 0034595821 scopus 로고    scopus 로고
    • Effects of incorporation of immunoglobulin G and complement component C1q on uptake and degradation of Alzheimer's disease amyloid fibrils by microglia
    • DOI 10.1074/jbc.M000937200
    • Brazil M. I., Chung H., Maxfield F. R., Effects of incorporation of immunoglobulin G and complement component C1q on uptake and degradation of Alzheimer's disease amyloid fibrils by microglia Journal of Biological Chemistry 2000 275 22 16941 16947 (Pubitemid 30398933)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16941-16947
    • Brazil, M.I.1    Chung, H.2    Maxfield, F.R.3
  • 216
    • 0035877075 scopus 로고    scopus 로고
    • Antibody-mediated phagocytosis of the amyloid β-peptide in microglia is differentially modulated by C1q
    • Webster S. D., Galvan M. D., Ferran E., Garzon-Rodriguez W., Glabe C. G., Tenner A. J., Antibody-mediated phagocytosis of the amyloid -peptide in microglia is differentially modulated by C1q Journal of Immunology 2001 166 12 7496 7503 (Pubitemid 32525628)
    • (2001) Journal of Immunology , vol.166 , Issue.12 , pp. 7496-7503
    • Webster, S.D.1    Galvan, M.D.2    Ferran, E.3    Garzon-Rodriguez, W.4    Glabe, C.G.5    Tenner, A.J.6


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