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Volumn 67, Issue 4, 2017, Pages 185-193

Plaque formation and the intraneuronal accumulation of β-amyloid in Alzheimer's disease

Author keywords

Alzheimer's disease; intraneuronal accumulation; multivesicular body; synapse; amyloid

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 2; MICROTUBULE PROTEIN; OLIGOMER; TAU PROTEIN;

EID: 85014573134     PISSN: 13205463     EISSN: 14401827     Source Type: Journal    
DOI: 10.1111/pin.12520     Document Type: Review
Times cited : (275)

References (59)
  • 1
    • 85016663285 scopus 로고    scopus 로고
    • The Government's role in regulating, coordinating, and standardizing the response to Alzheimer's disease: Anticipated international cooperation in the area of intractable and rare diseases
    • Tang Q, Song PP, Xu LZ. The Government's role in regulating, coordinating, and standardizing the response to Alzheimer's disease: Anticipated international cooperation in the area of intractable and rare diseases. Intractable Rare Dis Res 2016; 5: 238–43.
    • (2016) Intractable Rare Dis Res , vol.5 , pp. 238-243
    • Tang, Q.1    Song, P.P.2    Xu, L.Z.3
  • 2
    • 25144502499 scopus 로고
    • Concerning special findings in a case of probable cerebral syphilis
    • In, Bick K, Amaducci L, Pepeu G, eds., Padova, Liviana Press
    • Bonfiglio F. Concerning special findings in a case of probable cerebral syphilis. In: Bick K, Amaducci L, Pepeu G, eds. The Early Story of Alzheimer's Disease. Padova: Liviana Press, 1987; 19–32.
    • (1987) The Early Story of Alzheimer's Disease , pp. 19-32
    • Bonfiglio, F.1
  • 3
    • 25144462639 scopus 로고
    • Miliary necrosis with nodular proliferation of neurofibrils, a common change of the cerebral cortex in senile dementia
    • In, Bick K, Amaducci L, Pepeu G, editors., Padova, Liviana Press
    • Fischer O. Miliary necrosis with nodular proliferation of neurofibrils, a common change of the cerebral cortex in senile dementia. In: Bick K, Amaducci L, Pepeu G, editors. The Early Story of Alzheimer's Disease. Padova: Liviana Press 1987; 5–19.
    • (1987) The Early Story of Alzheimer's Disease , pp. 5-19
    • Fischer, O.1
  • 4
    • 25144501662 scopus 로고    scopus 로고
    • Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease
    • Gouras GK, Almeida CG, Takahashi RH. Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease. Neurobiol Aging 2005; 26: 1235–44.
    • (2005) Neurobiol Aging , vol.26 , pp. 1235-1244
    • Gouras, G.K.1    Almeida, C.G.2    Takahashi, R.H.3
  • 5
    • 0023106967 scopus 로고
    • A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease
    • Davies CA, Mann DM, Sumpter PQ et al. A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease. J Neurol Sci 1987; 78: 151–64.
    • (1987) J Neurol Sci , vol.78 , pp. 151-164
    • Davies, C.A.1    Mann, D.M.2    Sumpter, P.Q.3
  • 6
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky ST, Scheff SW. Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity. Ann Neurol 1990; 27: 457–64.
    • (1990) Ann Neurol , vol.27 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 7
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry RD, Masliah E, Salmon DP et al. Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment. Ann Neurol 1991; 30: 572–80.
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3
  • 8
    • 0034518216 scopus 로고    scopus 로고
    • The genetics and molecular pathology of Alzheimer's disease: Roles of amyloid and the presenilins
    • Selkoe DJ. The genetics and molecular pathology of Alzheimer's disease: Roles of amyloid and the presenilins. Neurol Clin 2000; 18: 903–22.
    • (2000) Neurol Clin , vol.18 , pp. 903-922
    • Selkoe, D.J.1
  • 9
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh DM, Selkoe DJ. Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 2004; 44: 181–93.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 10
    • 84938702198 scopus 로고    scopus 로고
    • Neuronal amyloid-β accumulation within cholinergic basal forebrain in ageing and Alzheimer's disease
    • Baker-Nigh A, Vahedi S, Davis EG et al. Neuronal amyloid-β accumulation within cholinergic basal forebrain in ageing and Alzheimer's disease. Brain 2015; 138: 1722–37.
    • (2015) Brain , vol.138 , pp. 1722-1737
    • Baker-Nigh, A.1    Vahedi, S.2    Davis, E.G.3
  • 11
    • 85023193935 scopus 로고    scopus 로고
    • The ability of apolipoprotein E fragments to promote intraneuronal accumulation of amyloid beta peptide 42 is both isoform and size-specific
    • Dafnis I, Argyri L, Sagnou M et al. The ability of apolipoprotein E fragments to promote intraneuronal accumulation of amyloid beta peptide 42 is both isoform and size-specific. Sci Rep 2016; 6: 30654.
    • (2016) Sci Rep , vol.6 , pp. 30654
    • Dafnis, I.1    Argyri, L.2    Sagnou, M.3
  • 12
    • 0033622324 scopus 로고    scopus 로고
    • Intraneuronal Aβ42 accumulation in human brain
    • Gouras GK, Tsai J, Naslund J et al. Intraneuronal Aβ42 accumulation in human brain. Am J Pathol 2000; 156: 15–20.
    • (2000) Am J Pathol , vol.156 , pp. 15-20
    • Gouras, G.K.1    Tsai, J.2    Naslund, J.3
  • 13
    • 0042697305 scopus 로고    scopus 로고
    • Triple-Transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • Oddo S, Caccamo A, Shepherd JD et al. Triple-Transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction. Neuron 2003; 39: 409–21.
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3
  • 14
    • 0036827031 scopus 로고    scopus 로고
    • Intraneuronal Alzheimer Aβ42 accumulates in multivesicular bodies and is associated with synaptic pathology
    • Takahashi RH, Milner TA, Li F et al. Intraneuronal Alzheimer Aβ42 accumulates in multivesicular bodies and is associated with synaptic pathology. Am J Pathol 2002; 161: 1869–79.
    • (2002) Am J Pathol , vol.161 , pp. 1869-1879
    • Takahashi, R.H.1    Milner, T.A.2    Li, F.3
  • 15
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Comm 1984; 120: 885–90.
    • (1984) Biochem Biophys Res Comm , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 16
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire H-G, Unterbeck A et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987; 325: 733–6.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.-G.2    Unterbeck, A.3
  • 17
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • Haass C, Schlossmacher MG, Hung AY et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 1992; 359: 322–5.
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1    Schlossmacher, M.G.2    Hung, A.Y.3
  • 18
    • 0024559652 scopus 로고
    • Predisposing locus for Alzheimer's disease on chromosome 21
    • Goate AM, Haynes AR, Owen MJ et al. Predisposing locus for Alzheimer's disease on chromosome 21. Lancet 1989; 1: 352–5.
    • (1989) Lancet , vol.1 , pp. 352-355
    • Goate, A.M.1    Haynes, A.R.2    Owen, M.J.3
  • 19
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike CJ, Burdick D, Walencewicz AJ et al. Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state. J Neurosci 1993; 13: 1676–87.
    • (1993) J Neurosci , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3
  • 20
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean CA, Cherny RA, Fraser FW et al. Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann Neurol 1999; 46: 860–66.
    • (1999) Ann Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3
  • 21
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: Formation and toxicity of Aβ oligomers
    • Sakono M, Zako T. Amyloid oligomers: Formation and toxicity of Aβ oligomers. FEBS J 2010; 277: 1348–58.
    • (2010) FEBS J , vol.277 , pp. 1348-1358
    • Sakono, M.1    Zako, T.2
  • 22
    • 0033458064 scopus 로고    scopus 로고
    • Intracellular biology of Alzheimer's disease amyloid beta peptide
    • Hartmann T. Intracellular biology of Alzheimer's disease amyloid beta peptide. Eur Arch Psychiatry Clin Neurosci 1999; 249: 291–8.
    • (1999) Eur Arch Psychiatry Clin Neurosci , vol.249 , pp. 291-298
    • Hartmann, T.1
  • 23
    • 0032800818 scopus 로고    scopus 로고
    • Intracellular APP processing and Aβ production in Alzheimer disease
    • Wilson CA, Doms RW, Lee VM. Intracellular APP processing and Aβ production in Alzheimer disease. J Neuropathol Exp Neurol 1999; 58: 787–94.
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 787-794
    • Wilson, C.A.1    Doms, R.W.2    Lee, V.M.3
  • 24
    • 0027361386 scopus 로고
    • Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular β-amyloid or A4 peptides
    • Wertkin AM, Turner RS, Pleasure SJ et al. Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular β-amyloid or A4 peptides. Proc Natl Acad Sci USA 1993; 90: 9513–7.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9513-9517
    • Wertkin, A.M.1    Turner, R.S.2    Pleasure, S.J.3
  • 25
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid β protein that accumulates with time in culture
    • Skovronsky DM, Doms RW, Lee VM. Detection of a novel intraneuronal pool of insoluble amyloid β protein that accumulates with time in culture. J Cell Biol 1998; 141: 1031–9.
    • (1998) J Cell Biol , vol.141 , pp. 1031-1039
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.3
  • 26
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides
    • Hartmann T, Bieger SC, Bruhl B et al. Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides. Nat Med 1997; 3: 1016–20.
    • (1997) Nat Med , vol.3 , pp. 1016-1020
    • Hartmann, T.1    Bieger, S.C.2    Bruhl, B.3
  • 27
    • 0030963605 scopus 로고    scopus 로고
    • Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation
    • Xu H, Sweeney D, Wang R et al. Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation. Proc Natl Acad Sci USA 1997; 94: 3748–52.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3748-3752
    • Xu, H.1    Sweeney, D.2    Wang, R.3
  • 28
    • 84874302223 scopus 로고    scopus 로고
    • Endothelin-converting enzymes degrade intracellular β-amyloid produced within the endosomal/lysosomal pathway and autophagosomes
    • Pacheco-Quinto J, Eckman EA. Endothelin-converting enzymes degrade intracellular β-amyloid produced within the endosomal/lysosomal pathway and autophagosomes. J Biol Chem 2013; 288: 5606–15.
    • (2013) J Biol Chem , vol.288 , pp. 5606-5615
    • Pacheco-Quinto, J.1    Eckman, E.A.2
  • 29
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's Aβ (1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook DG, Forman MS, Sung JC et al. Alzheimer's Aβ (1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat Med 1997; 3: 1021–3.
    • (1997) Nat Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3
  • 30
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • Koo EH, Squazzo SL. Evidence that production and release of amyloid β-protein involves the endocytic pathway. J Biol Chem 1994; 269: 17386–9.
    • (1994) J Biol Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 31
    • 0023684537 scopus 로고
    • Differences between vascular and plaque core amyloid in Alzheimer's disease
    • Prelli F, Castano E, Glenner GG et al. Differences between vascular and plaque core amyloid in Alzheimer's disease. J Neurochem 1988; 51: 648–51.
    • (1988) J Neurochem , vol.51 , pp. 648-651
    • Prelli, F.1    Castano, E.2    Glenner, G.G.3
  • 32
    • 0030015163 scopus 로고    scopus 로고
    • Pathologic processes leading to cerebral hemorrhage in amyloid angiopathy
    • Takashashi RH, Sawa H, Kuroda S et al. Pathologic processes leading to cerebral hemorrhage in amyloid angiopathy. Neuropathology 1996; 16: 99–105.
    • (1996) Neuropathology , vol.16 , pp. 99-105
    • Takashashi, R.H.1    Sawa, H.2    Kuroda, S.3
  • 33
    • 84869770850 scopus 로고    scopus 로고
    • Enhanced antigen retrieval of amyloid β immunohistochemistry: Re-evaluation of amyloid β pathology in Alzheimer disease and its mouse model
    • Kai H, Shin RW, Ogino K et al. Enhanced antigen retrieval of amyloid β immunohistochemistry: Re-evaluation of amyloid β pathology in Alzheimer disease and its mouse model. J Histoch Cytochem 2012; 60: 761–9.
    • (2012) J Histoch Cytochem , vol.60 , pp. 761-769
    • Kai, H.1    Shin, R.W.2    Ogino, K.3
  • 34
    • 71849100745 scopus 로고    scopus 로고
    • Formic acid is essential for immunohistochemical detection of aggregated intraneuronal Aβ peptides in mouse models of Alzheimer's disease
    • Christensen DZ, Bayer TA, Wirths O. Formic acid is essential for immunohistochemical detection of aggregated intraneuronal Aβ peptides in mouse models of Alzheimer's disease. Brain Res 2009; 1301: 116–25.
    • (2009) Brain Res , vol.1301 , pp. 116-125
    • Christensen, D.Z.1    Bayer, T.A.2    Wirths, O.3
  • 35
    • 0037448062 scopus 로고    scopus 로고
    • The use of formic acid to embellish amyloid plaque detection in Alzheimer's disease tissues misguides key observations
    • D'Andrea MR, Reiser PA, Polkovitch DA et al. The use of formic acid to embellish amyloid plaque detection in Alzheimer's disease tissues misguides key observations. Neurosci Lett 2003; 342: 114–8.
    • (2003) Neurosci Lett , vol.342 , pp. 114-118
    • D'Andrea, M.R.1    Reiser, P.A.2    Polkovitch, D.A.3
  • 36
    • 33646461282 scopus 로고    scopus 로고
    • β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida CG, Takahashi RH, Gouras GK. β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci 2006; 26: 4277–88.
    • (2006) J Neurosci , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 37
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • Gruenberg J, Stenmark H. The biogenesis of multivesicular endosomes. Nat Rev Mol Cell Biol 2004; 5: 317–23.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 38
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • Piper RC, Katzmann DJ. Biogenesis and function of multivesicular bodies. Annu Rev Cell Dev Biol 2007; 23: 519–47.
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 39
    • 0027327268 scopus 로고
    • Cell biology of neuronal endocytosis
    • Parton RG, Dotti CG. Cell biology of neuronal endocytosis. J Neurosci Res 1993; 36: 1–9.
    • (1993) J Neurosci Res , vol.36 , pp. 1-9
    • Parton, R.G.1    Dotti, C.G.2
  • 40
    • 76649116890 scopus 로고    scopus 로고
    • Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity
    • Friedrich RP, Tepper K, Ronicke R et al. Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity. Proc Natl Acad Sci USA 2010; 107: 1942–7.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1942-1947
    • Friedrich, R.P.1    Tepper, K.2    Ronicke, R.3
  • 41
    • 4644319713 scopus 로고    scopus 로고
    • Abeta localization in abnormal endosomes: Association with earliest Aβ elevations in AD and Down syndrome
    • Cataldo AM, Petanceska S, Terio NB et al. Abeta localization in abnormal endosomes: Association with earliest Aβ elevations in AD and Down syndrome. Neurobiol Aging 2004; 25: 1263–72.
    • (2004) Neurobiol Aging , vol.25 , pp. 1263-1272
    • Cataldo, A.M.1    Petanceska, S.2    Terio, N.B.3
  • 42
    • 0028988801 scopus 로고
    • β-amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity
    • Zheng H, Jiang M, Trumbauer ME et al. β-amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity. Cell 1995; 81: 525–31.
    • (1995) Cell , vol.81 , pp. 525-531
    • Zheng, H.1    Jiang, M.2    Trumbauer, M.E.3
  • 43
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo
    • Umeda T, Tomiyama T, Sakama N et al. Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo. J Neurosci Res 2011; 89: 1031–42.
    • (2011) J Neurosci Res , vol.89 , pp. 1031-1042
    • Umeda, T.1    Tomiyama, T.2    Sakama, N.3
  • 44
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi RH, Almeida CG, Kearney PF et al. Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain. J Neurosci 2004; 24: 3592–9.
    • (2004) J Neurosci , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3
  • 45
    • 38949123792 scopus 로고    scopus 로고
    • Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer's disease
    • Meyer-Luehmann M, Spires-Jones TL, Prada C et al. Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer's disease. Nature 2008; 451: 720–24.
    • (2008) Nature , vol.451 , pp. 720-724
    • Meyer-Luehmann, M.1    Spires-Jones, T.L.2    Prada, C.3
  • 46
    • 0344826476 scopus 로고    scopus 로고
    • Time sequence of maturation of dystrophic neurites associated with Aβ deposits in APP/PS1 transgenic mice
    • Blanchard V, Moussaoui S, Czech C et al. Time sequence of maturation of dystrophic neurites associated with Aβ deposits in APP/PS1 transgenic mice. Exp Neurol 2003; 184: 247–63.
    • (2003) Exp Neurol , vol.184 , pp. 247-263
    • Blanchard, V.1    Moussaoui, S.2    Czech, C.3
  • 47
    • 77952878634 scopus 로고    scopus 로고
    • Co-occurrence of Alzheimer's disease β-amyloid and tau pathologies at synapses
    • Takahashi RH, Capetillo-Zarate E, Lin MT et al. Co-occurrence of Alzheimer's disease β-amyloid and tau pathologies at synapses. Neurobiol Aging 2010; 31: 1145–52.
    • (2010) Neurobiol Aging , vol.31 , pp. 1145-1152
    • Takahashi, R.H.1    Capetillo-Zarate, E.2    Lin, M.T.3
  • 48
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin W-L et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 2001; 293: 1487–91.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.-L.3
  • 49
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils
    • Gotz J, Chen F, van Dorpe J et al. Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils. Science 2001; 293: 1491–5.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3
  • 50
    • 0034745017 scopus 로고    scopus 로고
    • Intraneuronal Aβ-amyloid precedes development of amyloid plaques in Down syndrome
    • Gyure KA, Durham R, Stewart WF et al. Intraneuronal Aβ-amyloid precedes development of amyloid plaques in Down syndrome. Arch Pathol Lab Med 2001; 125: 489–92.
    • (2001) Arch Pathol Lab Med , vol.125 , pp. 489-492
    • Gyure, K.A.1    Durham, R.2    Stewart, W.F.3
  • 51
    • 67349142329 scopus 로고    scopus 로고
    • Mechanisms of tau-induced neurodegeneration
    • Iqbal K, Liu F, Gong C-X et al. Mechanisms of tau-induced neurodegeneration. Acta Neuropathol 2009; 118: 53–69.
    • (2009) Acta Neuropathol , vol.118 , pp. 53-69
    • Iqbal, K.1    Liu, F.2    Gong, C.-X.3
  • 52
    • 80054974015 scopus 로고    scopus 로고
    • High-resolution 3D reconstruction reveals intra-synaptic amyloid fibrils
    • Capetillo-Zarate E, Gracia L, Yu F et al. High-resolution 3D reconstruction reveals intra-synaptic amyloid fibrils. Am J Pathol 2011; 179: 2551–8.
    • (2011) Am J Pathol , vol.179 , pp. 2551-2558
    • Capetillo-Zarate, E.1    Gracia, L.2    Yu, F.3
  • 53
    • 84872765430 scopus 로고    scopus 로고
    • Accumulation of intraneuronal β-Amyloid 42 peptides is associated with early changes in microtubule-associated protein 2 in neurites and synapses
    • Takahashi RH, Capetillo-Zarate E, Lin MT et al. Accumulation of intraneuronal β-Amyloid 42 peptides is associated with early changes in microtubule-associated protein 2 in neurites and synapses. PLoS One 2013; 8: e51965.
    • (2013) PLoS One , vol.8
    • Takahashi, R.H.1    Capetillo-Zarate, E.2    Lin, M.T.3
  • 54
    • 33750581641 scopus 로고    scopus 로고
    • Selective vulnerability of different types of commissural neurons for amyloid β-protein-induced neurodegeneration in APP23 mice correlates with dendritic tree morphology
    • Capetillo-Zarate E, Staufenbiel M, Abramowski D et al. Selective vulnerability of different types of commissural neurons for amyloid β-protein-induced neurodegeneration in APP23 mice correlates with dendritic tree morphology. Brain 2006; 129: 2992–3005.
    • (2006) Brain , vol.129 , pp. 2992-3005
    • Capetillo-Zarate, E.1    Staufenbiel, M.2    Abramowski, D.3
  • 55
    • 5444225566 scopus 로고    scopus 로고
    • Dendrite and dendritic spine alterations in Alzheimer models
    • Moolman DL, Vitolo OV, Vonsattel JP et al. Dendrite and dendritic spine alterations in Alzheimer models. J Neurocytol 2004; 33: 377–87.
    • (2004) J Neurocytol , vol.33 , pp. 377-387
    • Moolman, D.L.1    Vitolo, O.V.2    Vonsattel, J.P.3
  • 56
    • 2342486529 scopus 로고    scopus 로고
    • Selective vulnerability of dentate granule cells prior to amyloid deposition in PDAPP mice: Digital morphometric analyses
    • Wu CC, Chawla F, Games D et al. Selective vulnerability of dentate granule cells prior to amyloid deposition in PDAPP mice: Digital morphometric analyses. Proc Natl Acad Sci USA 2004; 101: 7141–6.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7141-7146
    • Wu, C.C.1    Chawla, F.2    Games, D.3
  • 57
    • 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
    • Bahr BA, Hoffman KB, Yang AJ et al. Amyloid β protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein. J Comp Neurol 1998; 397: 139–47.
    • (1998) J Comp Neurol , vol.397 , pp. 139-147
    • Bahr, B.A.1    Hoffman, K.B.2    Yang, A.J.3
  • 58
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann M, Coomaraswamy J, Bolmont T et al. Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host. Science 2006; 313: 1781–4.
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3
  • 59
    • 84903627137 scopus 로고    scopus 로고
    • Alzheimer's disease genetics: From the bench to the clinic
    • Karch CM, Cruchaga C, Goate AM. Alzheimer's disease genetics: From the bench to the clinic. Neuron 2014; 83: 11–26.
    • (2014) Neuron , vol.83 , pp. 11-26
    • Karch, C.M.1    Cruchaga, C.2    Goate, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.