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Volumn 8, Issue 7, 2007, Pages 499-509

Intracellular amyloid-β in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

ADAM PROTEIN; ADVANCED GLYCATION END PRODUCT; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN PS2; REACTIVE OXYGEN METABOLITE;

EID: 34250819839     PISSN: 1471003X     EISSN: 14710048     Source Type: Journal    
DOI: 10.1038/nrn2168     Document Type: Review
Times cited : (1710)

References (146)
  • 2
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G. G. & Wong, C. W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890 (1984).
    • (1984) Biochem. Biophys. Res. Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 3
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • Masters, C. L. et al. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc. Natl Acad. Sci. USA 82, 4245-4249 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 4245-4249
    • Masters, C.L.1
  • 4
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau
    • Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E. & Klug, A. Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc. Natl Acad. Sci. USA 85, 4051-4055 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 5
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein τ (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal, I. et al. Abnormal phosphorylation of the microtubule-associated protein τ (tau) in Alzheimer cytoskeletal pathology. Proc. Natl Acad. Sci. USA 83, 4913-4917 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1
  • 6
    • 0022724941 scopus 로고
    • Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease
    • Ihara, Y., Nukina, N., Miura, R. & Ogawara, M. Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease. J. Biochem. (Tokyo) 99, 1807-1810 (1986).
    • (1986) J. Biochem. (Tokyo) , vol.99 , pp. 1807-1810
    • Ihara, Y.1    Nukina, N.2    Miura, R.3    Ogawara, M.4
  • 7
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (τ) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik, K. S., Joachim, C. L. & Selkoe, D. J. Microtubule-associated protein tau (τ) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc. Natl Acad. Sci. USA 83, 4044-4048 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 8
    • 0022504686 scopus 로고
    • Role of microglia in plaque formation in senile dementia of the Alzheimer type. An immunohistochemical study
    • Rozemuller, J. M., Eikelenboom, P. & Stam, F. C. Role of microglia in plaque formation in senile dementia of the Alzheimer type. An immunohistochemical study. Virchows Arch. B Cell Pathol. 51, 247-254 (1986).
    • (1986) Virchows Arch. B Cell Pathol , vol.51 , pp. 247-254
    • Rozemuller, J.M.1    Eikelenboom, P.2    Stam, F.C.3
  • 9
    • 33748471099 scopus 로고    scopus 로고
    • Inflammation in Alzheimer disease: Driving force, bystander or beneficial response?
    • Wyss-Coray, T. Inflammation in Alzheimer disease: driving force, bystander or beneficial response? Nature Med. 12, 1005-1015 (2006).
    • (2006) Nature Med , vol.12 , pp. 1005-1015
    • Wyss-Coray, T.1
  • 10
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery, W. R. Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med. 23, 134-147 (1997).
    • (1997) Free Radic. Biol. Med , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 11
    • 84880185810 scopus 로고    scopus 로고
    • Inflammation, anti-inflammatory agents and Alzheimer disease: The last 12 years
    • McGeer, P. L., Rogers, J. & McGeer, E. G. Inflammation, anti-inflammatory agents and Alzheimer disease: the last 12 years. J. Alzheimers Dis. 9, 271-276 (2006).
    • (2006) J. Alzheimers Dis , vol.9 , pp. 271-276
    • McGeer, P.L.1    Rogers, J.2    McGeer, E.G.3
  • 12
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein α-secretases
    • Allinson, T. M., Parkin, E. T., Turner, A. J. & Hooper, N. M. ADAMs family members as amyloid precursor protein α-secretases. J. Neurosci. Res. 74, 342-352 (2003).
    • (2003) J. Neurosci. Res , vol.74 , pp. 342-352
    • Allinson, T.M.1    Parkin, E.T.2    Turner, A.J.3    Hooper, N.M.4
  • 13
    • 0033595706 scopus 로고    scopus 로고
    • β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar, R. et al. β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999).
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1
  • 14
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp 2) as β-secretase
    • Hussain, I. et al. Identification of a novel aspartic protease (Asp 2) as β-secretase. Mol. Cell. Neurosci. 14, 419-427 (1999).
    • (1999) Mol. Cell. Neurosci , vol.14 , pp. 419-427
    • Hussain, I.1
  • 15
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein β-secretase from human brain
    • Sinha, S. et al. Purification and cloning of amyloid precursor protein β-secretase from human brain. Nature 402, 537-540 (1999).
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1
  • 16
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517 (1999).
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 17
    • 0037131218 scopus 로고    scopus 로고
    • PEN-2 is an integral component of the γ-secretase complex required for coordinated expression of presenilin and nicastrin
    • Steiner, H. et al. PEN-2 is an integral component of the γ-secretase complex required for coordinated expression of presenilin and nicastrin. J. Biol. Chem. 277, 39062-39065 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 39062-39065
    • Steiner, H.1
  • 18
    • 18444417998 scopus 로고    scopus 로고
    • aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation
    • Francis, R. et al. aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1
  • 19
    • 0035834145 scopus 로고    scopus 로고
    • PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling
    • Levitan, D. et al. PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling. Proc. Natl Acad. Sci. USA 98, 12186-12190 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12186-12190
    • Levitan, D.1
  • 20
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407, 48-54 (2000).
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 21
    • 15944413832 scopus 로고    scopus 로고
    • The non-amyloidogenic pathway: Structure and function of α-secretases
    • Kojro, E. & Fahrenholz, F. The non-amyloidogenic pathway: structure and function of α-secretases. Subcell. Biochem. 38, 105-127 (2005).
    • (2005) Subcell. Biochem , vol.38 , pp. 105-127
    • Kojro, E.1    Fahrenholz, F.2
  • 22
    • 0027535111 scopus 로고
    • β-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms
    • Haass, C., Hung, A. Y., Schlossmacher, M. G., Teplow, D. B. & Selkoe, D. J. β-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J. Biol. Chem. 268, 3021-3024 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 3021-3024
    • Haass, C.1    Hung, A.Y.2    Schlossmacher, M.G.3    Teplow, D.B.4    Selkoe, D.J.5
  • 23
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J. T., Berger, E. P. & Lansbury, P. T. Jr. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697 (1993).
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 24
    • 0032105394 scopus 로고    scopus 로고
    • The role of Aβ 42 in Alzheimer's disease
    • Younkin, S. G. The role of Aβ 42 in Alzheimer's disease. J. Physiol. Paris 92, 289-292 (1998).
    • (1998) J. Physiol. Paris , vol.92 , pp. 289-292
    • Younkin, S.G.1
  • 25
    • 13844255273 scopus 로고    scopus 로고
    • Molecular biology and genetics of Alzheimer's disease
    • St George-Hyslop, P. H. & Petit, A. Molecular biology and genetics of Alzheimer's disease. C. R. Biol. 328, 119-130 (2005).
    • (2005) C. R. Biol , vol.328 , pp. 119-130
    • St George-Hyslop, P.H.1    Petit, A.2
  • 26
    • 0028866435 scopus 로고    scopus 로고
    • Haass, C. et al. The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway. Nature Med. 1, 1291-1296 (1995).
    • Haass, C. et al. The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway. Nature Med. 1, 1291-1296 (1995).
  • 27
    • 17944368176 scopus 로고    scopus 로고
    • The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
    • Nilsberth, C. et al. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation. Nature Neurosci. 4, 887-893 (2001).
    • (2001) Nature Neurosci , vol.4 , pp. 887-893
    • Nilsberth, C.1
  • 28
    • 0033016172 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice
    • Guo, Q. et al. Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice. Nature Med. 5, 101-106 (1999).
    • (1999) Nature Med , vol.5 , pp. 101-106
    • Guo, Q.1
  • 29
    • 1642555780 scopus 로고    scopus 로고
    • Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: Evidence for augmentation of a 42-specific γ secretase
    • Jankowsky, J. L. et al. Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: evidence for augmentation of a 42-specific γ secretase. Hum. Mol. Genet. 13, 159-170 (2004).
    • (2004) Hum. Mol. Genet , vol.13 , pp. 159-170
    • Jankowsky, J.L.1
  • 30
    • 29444442794 scopus 로고    scopus 로고
    • APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy
    • Rovelet-Lecrux, A. et al. APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy. Nature Genet. 38, 24-26 (2006).
    • (2006) Nature Genet , vol.38 , pp. 24-26
    • Rovelet-Lecrux, A.1
  • 31
    • 33749066060 scopus 로고    scopus 로고
    • Phenotype associated with APP duplication in five families
    • Cabrejo, L. et al. Phenotype associated with APP duplication in five families. Brain 129, 2966-2976 (2006).
    • (2006) Brain , vol.129 , pp. 2966-2976
    • Cabrejo, L.1
  • 32
    • 0034745017 scopus 로고    scopus 로고
    • Intraneuronal Aβ-amyloid precedes development of amyloid plaques in Down syndrome
    • Gyure, K. A., Durham, R., Stewart, W. F., Smialek, J. E. & Troncoso, J. C. Intraneuronal Aβ-amyloid precedes development of amyloid plaques in Down syndrome. Arch. Pathol. Lab. Med. 125, 489-492 (2001).
    • (2001) Arch. Pathol. Lab. Med , vol.125 , pp. 489-492
    • Gyure, K.A.1    Durham, R.2    Stewart, W.F.3    Smialek, J.E.4    Troncoso, J.C.5
  • 33
    • 0035997524 scopus 로고    scopus 로고
    • Intraneuronal Aβ42 accumulation in Down syndrome brain
    • Mori, C. et al. Intraneuronal Aβ42 accumulation in Down syndrome brain. Amyloid 9, 88-102 (2002).
    • (2002) Amyloid , vol.9 , pp. 88-102
    • Mori, C.1
  • 34
    • 0024563160 scopus 로고
    • Amyloid protein and neurofibrillary tangles coexist in the same neuron in Alzheimer disease
    • Grundke-Iqbal, I. et al. Amyloid protein and neurofibrillary tangles coexist in the same neuron in Alzheimer disease. Proc. Natl Acad. Sci. USA 86, 2853-2857 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 2853-2857
    • Grundke-Iqbal, I.1
  • 35
    • 33846047004 scopus 로고    scopus 로고
    • Pathways by which Aβ facilitates tau pathology
    • Blurton-Jones, M. & Laferla, F. M. Pathways by which Aβ facilitates tau pathology. Curr. Alzheimer Res. 3, 437-448 (2006).
    • (2006) Curr. Alzheimer Res , vol.3 , pp. 437-448
    • Blurton-Jones, M.1    Laferla, F.M.2
  • 36
    • 0033622324 scopus 로고    scopus 로고
    • Intraneuronal Aβ42 accumulation in human brain
    • Gouras, G. K. et al. Intraneuronal Aβ42 accumulation in human brain. Am. J. Pathol. 156, 15-20 (2000).
    • (2000) Am. J. Pathol , vol.156 , pp. 15-20
    • Gouras, G.K.1
  • 37
    • 0036827031 scopus 로고    scopus 로고
    • Takahashi, R. H. et al. Intraneuronal Alzheimer Aβ42 accumulates in multivesicular bodies and is associated with synaptic pathology. Am. J. Pathol. 161, 869-1879 (2002). Using electron microscope analysis, this paper shows that in AD brains, intraneuronal Aβ accumulates within the multivesicular bodies.
    • Takahashi, R. H. et al. Intraneuronal Alzheimer Aβ42 accumulates in multivesicular bodies and is associated with synaptic pathology. Am. J. Pathol. 161, 869-1879 (2002). Using electron microscope analysis, this paper shows that in AD brains, intraneuronal Aβ accumulates within the multivesicular bodies.
  • 38
    • 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, M. R. et al. The use of formic acid to embellish amyloid plaque detection in Alzheimer's disease tissues misguides key observations. Neurosci. Lett. 342, 114-118 (2003).
    • (2003) Neurosci. Lett , vol.342 , pp. 114-118
    • D'Andrea, M.R.1
  • 39
    • 33751248758 scopus 로고    scopus 로고
    • Intraneuronal amyloid β42 enhanced by heating but counteracted by formic acid
    • Ohyagi, Y. et al. Intraneuronal amyloid β42 enhanced by heating but counteracted by formic acid. J. Neurosci. Methods 159, 134-138 (2007).
    • (2007) J. Neurosci. Methods , vol.159 , pp. 134-138
    • Ohyagi, Y.1
  • 40
    • 0032895651 scopus 로고    scopus 로고
    • Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
    • Chui, D. H. et al. Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation. Nature Med. 5, 560-564 (1999).
    • (1999) Nature Med , vol.5 , pp. 560-564
    • Chui, D.H.1
  • 41
    • 34447564164 scopus 로고    scopus 로고
    • Knobloch, M., Konietzko, U., Krebs, D. C. & Nitsch, R. M. Intracellular Aβ and cognitive deficits precede β-amyloid deposition in transgenic arcAβ mice. Neurobiol. Aging, 31 July 2006 (doi:10.1016/j.n eurobiolaging.2006.06.019). Provides evidence linking intraneuronal Aβ accumulation to cognitive deficits in transgenic mice.
    • Knobloch, M., Konietzko, U., Krebs, D. C. & Nitsch, R. M. Intracellular Aβ and cognitive deficits precede β-amyloid deposition in transgenic arcAβ mice. Neurobiol. Aging, 31 July 2006 (doi:10.1016/j.n eurobiolaging.2006.06.019). Provides evidence linking intraneuronal Aβ accumulation to cognitive deficits in transgenic mice.
  • 42
    • 0035718905 scopus 로고    scopus 로고
    • The evolution of Aβ peptide burden in the APP23 transgenic mice: Implications for Aβ deposition in Alzheimer disease
    • Kuo, Y. M. et al. The evolution of Aβ peptide burden in the APP23 transgenic mice: implications for Aβ deposition in Alzheimer disease. Mol. Med. 7, 609-618 (2001).
    • (2001) Mol. Med , vol.7 , pp. 609-618
    • Kuo, Y.M.1
  • 43
    • 0033051445 scopus 로고    scopus 로고
    • Intracellular accumulation of detergent-soluble amyloidogenic Aβ fragment of Alzheimer's disease precursor protein in the hippocampus of aged transgenic mice
    • Li, Q. X. et al. Intracellular accumulation of detergent-soluble amyloidogenic Aβ fragment of Alzheimer's disease precursor protein in the hippocampus of aged transgenic mice. J. Neurochem. 72, 2479-2487 (1999).
    • (1999) J. Neurochem , vol.72 , pp. 2479-2487
    • Li, Q.X.1
  • 44
    • 27744512118 scopus 로고    scopus 로고
    • The Arctic Alzheimer mutation facilitates early intraneuronal Aβ aggregation and senile plaque formation in transgenic mice
    • Lord, A. et al. The Arctic Alzheimer mutation facilitates early intraneuronal Aβ aggregation and senile plaque formation in transgenic mice. Neurobiol. Aging 27, 67-77 (2006).
    • (2006) Neurobiol. Aging , vol.27 , pp. 67-77
    • Lord, A.1
  • 45
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal β-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: Potential factors in amyloid plaque formation
    • Oakley, H. et al. Intraneuronal β-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J. Neurosci. 26, 10129-10140 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 10129-10140
    • Oakley, H.1
  • 46
    • 0042697305 scopus 로고    scopus 로고
    • Oddo, S. et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Aβ and synaptic dysfunction. Neuron 39, 409-421 (2003). Provides the earliest in vivo evidence that links intraneuronal Aβ to synaptic dysfunction, showing that intraneuronal Aβ accumulation leads to a profound LTP deficit in 3xTg-AD mice.
    • Oddo, S. et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Aβ and synaptic dysfunction. Neuron 39, 409-421 (2003). Provides the earliest in vivo evidence that links intraneuronal Aβ to synaptic dysfunction, showing that intraneuronal Aβ accumulation leads to a profound LTP deficit in 3xTg-AD mice.
  • 47
    • 0035933279 scopus 로고    scopus 로고
    • Intraneuronal Aβ accumulation precedes plaque formation in β-amyloid precursor protein and presenilin-1 double-transgenic mice
    • Wirths, O. et al. Intraneuronal Aβ accumulation precedes plaque formation in β-amyloid precursor protein and presenilin-1 double-transgenic mice. Neurosci. Lett. 306, 116-120 (2001).
    • (2001) Neurosci. Lett , vol.306 , pp. 116-120
    • Wirths, O.1
  • 48
    • 30344448543 scopus 로고    scopus 로고
    • A dynamic relationship between intracellular and extracellular pools of Aβ
    • Oddo, S., Caccamo, A., Smith, I. F., Green, K. N. & LaFerla, F. M. A dynamic relationship between intracellular and extracellular pools of Aβ. Am. J. Pathol. 168, 184-194 (2006).
    • (2006) Am. J. Pathol , vol.168 , pp. 184-194
    • Oddo, S.1    Caccamo, A.2    Smith, I.F.3    Green, K.N.4    LaFerla, F.M.5
  • 49
    • 33947261641 scopus 로고    scopus 로고
    • Intraneuronal Aβ immunoreactivity is not a predictor of brain amyloidosis-β or neurofibrillary degeneration
    • Wegiel, J. et al. Intraneuronal Aβ immunoreactivity is not a predictor of brain amyloidosis-β or neurofibrillary degeneration. Acta Neuropathol. (Berl) 113, 389-402 (2007).
    • (2007) Acta Neuropathol. (Berl) , vol.113 , pp. 389-402
    • Wegiel, J.1
  • 50
    • 0042887148 scopus 로고    scopus 로고
    • Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes
    • Kinoshita, A. et al. Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes. J. Cell Sci. 116, 3339-3346 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 3339-3346
    • Kinoshita, A.1
  • 51
    • 0025965521 scopus 로고
    • β amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion
    • Breen, K. C., Bruce, M. & Anderton, B. H. β amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion. J. Neurosci. Res. 28, 90-100 (1991).
    • (1991) J. Neurosci. Res , vol.28 , pp. 90-100
    • Breen, K.C.1    Bruce, M.2    Anderton, B.H.3
  • 52
    • 0035954426 scopus 로고    scopus 로고
    • The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement
    • Sabo, S. L., Ikin, A. F., Buxbaum, J. D. & Greengard, P. The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J. Cell Biol. 153, 1403-1414 (2001).
    • (2001) J. Cell Biol , vol.153 , pp. 1403-1414
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 53
    • 0028859466 scopus 로고
    • Regulated formation of Golgi secretory vesicles containing Alzheimer β-amyloid precursor protein
    • Xu, H., Greengard, P. & Gandy, S. Regulated formation of Golgi secretory vesicles containing Alzheimer β-amyloid precursor protein. J. Biol. Chem. 270, 23243-23245 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 23243-23245
    • Xu, H.1    Greengard, P.2    Gandy, S.3
  • 54
    • 0026683606 scopus 로고
    • Differential distribution of cellular forms of β-amyloid precursor protein in murine glial cell cultures
    • Mizuguchi, M., Ikeda, K. & Kim, S. U. Differential distribution of cellular forms of β-amyloid precursor protein in murine glial cell cultures. Brain Res. 584, 219-225 (1992).
    • (1992) Brain Res , vol.584 , pp. 219-225
    • Mizuguchi, M.1    Ikeda, K.2    Kim, S.U.3
  • 55
    • 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, A. M. 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 90, 9513-9517 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9513-9517
    • Wertkin, A.M.1
  • 56
    • 0028972233 scopus 로고
    • Intracellular accumulation of β-amyloid in cells expressing the Swedish mutant amyloid precursor protein
    • Martin, B. L. et al. Intracellular accumulation of β-amyloid in cells expressing the Swedish mutant amyloid precursor protein. J. Biol. Chem. 270, 26727-26730 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 26727-26730
    • Martin, B.L.1
  • 57
    • 33846613222 scopus 로고    scopus 로고
    • The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease
    • Rogaeva, E. et al. The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease. Nature Genet. 39, 168-177 (2007).
    • (2007) Nature Genet , vol.39 , pp. 168-177
    • Rogaeva, E.1
  • 58
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde, T. E., Estus, S., Younkin, L. H., Selkoe, D. J. & Younkin, S. G. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 255, 728-730 (1992).
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 59
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • Koo, E. H. & Squazzo, S. L. Evidence that production and release of amyloid β-protein involves the endocytic pathway. J. Biol. Chem. 269, 17386-17389 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 60
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for β-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Aβ42
    • Perez, R. G. et al. Mutagenesis identifies new signals for β-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Aβ42. J. Biol. Chem. 274, 18851-18856 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 18851-18856
    • Perez, R.G.1
  • 61
    • 3142717640 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein 1B retains β-amyloid precursor protein at the cell surface and reduces amyloid-β peptide production
    • Cam, J. A. et al. The low density lipoprotein receptor-related protein 1B retains β-amyloid precursor protein at the cell surface and reduces amyloid-β peptide production. J. Biol. Chem. 279, 29639-29646 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 29639-29646
    • Cam, J.A.1
  • 62
    • 0027407570 scopus 로고    scopus 로고
    • Busciglio, J., Gabuzda, D. H., Matsudaira, P. & Yankner, B. A. Generation of β-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl Acad. Sci. USA 90, 2092-2096 (1993). Provides strong evidence that Aβ in neurons is generated by the secretory pathway.
    • Busciglio, J., Gabuzda, D. H., Matsudaira, P. & Yankner, B. A. Generation of β-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl Acad. Sci. USA 90, 2092-2096 (1993). Provides strong evidence that Aβ in neurons is generated by the secretory pathway.
  • 63
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's A β(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook, D. G. et al. Alzheimer's A β(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nature Med. 3, 1021-1023 (1997).
    • (1997) Nature Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1
  • 64
    • 0031746979 scopus 로고    scopus 로고
    • A detergent-insoluble membrane compartment contains A β in vivo
    • Lee, S. J. et al. A detergent-insoluble membrane compartment contains A β in vivo. Nature Med. 4, 730-734 (1998).
    • (1998) Nature Med , vol.4 , pp. 730-734
    • Lee, S.J.1
  • 65
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid β protein that accumulates with time in culture
    • Skovronsky, D. M., Doms, R. W. & Lee, V. M. Detection of a novel intraneuronal pool of insoluble amyloid β protein that accumulates with time in culture. J. Cell Biol. 141, 1031-1039 (1998).
    • (1998) J. Cell Biol , vol.141 , pp. 1031-1039
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.3
  • 66
    • 0030952217 scopus 로고    scopus 로고
    • Intracellular generation and accumulation of amyloid beta-peptide terminating at amino acid 42
    • Wild-Bode, C. et al. Intracellular generation and accumulation of amyloid beta-peptide terminating at amino acid 42. J. Biol. Chem. 272, 16085-16088 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 16085-16088
    • Wild-Bode, C.1
  • 67
    • 0030769091 scopus 로고    scopus 로고
    • 42 are generated intracellularly but at different sites.
    • 42 are generated intracellularly but at different sites.
  • 68
    • 34250811784 scopus 로고    scopus 로고
    • LRP in amyloid-β production and metabolism
    • Bu, G., Cam, J. & Zerbinatti, C. LRP in amyloid-β production and metabolism. Ann. N. Y. Acad. Sci. 1086, 35-53 (2006).
    • (2006) Ann. N. Y. Acad. Sci , vol.1086 , pp. 35-53
    • Bu, G.1    Cam, J.2    Zerbinatti, C.3
  • 69
    • 0037703255 scopus 로고    scopus 로고
    • RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
    • Deane, R. et al. RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain. Nature Med. 9, 907-913 (2003).
    • (2003) Nature Med , vol.9 , pp. 907-913
    • Deane, R.1
  • 70
    • 0037066072 scopus 로고    scopus 로고
    • 1-42 in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer's disease. Neuroscience 110, 199-211 (2002). Shows that Aβ binds to α7nAChR and suggests that it is subsequently internalized, thus providing a mechanism for intraneuronal Aβ accumulation.
    • 1-42 in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer's disease. Neuroscience 110, 199-211 (2002). Shows that Aβ binds to α7nAChR and suggests that it is subsequently internalized, thus providing a mechanism for intraneuronal Aβ accumulation.
  • 71
    • 0035158645 scopus 로고    scopus 로고
    • β amyloid peptide (Aβ42) is internalized via the G-protein-coupled receptor FPRL1 and forms fibrillar aggregates in macrophages
    • Yazawa, H. et al. β amyloid peptide (Aβ42) is internalized via the G-protein-coupled receptor FPRL1 and forms fibrillar aggregates in macrophages. FASEB J. 15, 2454-2462 (2001).
    • (2001) FASEB J , vol.15 , pp. 2454-2462
    • Yazawa, H.1
  • 72
    • 33947164189 scopus 로고    scopus 로고
    • Aβ peptides can enter the brain through a defective blood-brain barrier and bind selectively to neurons
    • Clifford, P. M. et al. Aβ peptides can enter the brain through a defective blood-brain barrier and bind selectively to neurons. Brain Res. 1142, 223-236 (2007).
    • (2007) Brain Res , vol.1142 , pp. 223-236
    • Clifford, P.M.1
  • 73
    • 0034006944 scopus 로고    scopus 로고
    • 1-42 binds to α7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology
    • 1-42 binds to α7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J. Biol. Chem. 275, 5626-5632 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 5626-5632
    • Wang, H.Y.1
  • 74
    • 14544304591 scopus 로고    scopus 로고
    • Chronic nicotine administration exacerbates tau pathology in a transgenic model of Alzheimer's disease
    • Oddo, S. et al. Chronic nicotine administration exacerbates tau pathology in a transgenic model of Alzheimer's disease. Proc. Natl Acad. Sci. USA 102, 3046-3051 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3046-3051
    • Oddo, S.1
  • 75
    • 33846021307 scopus 로고    scopus 로고
    • Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Aβ42 accumulation in amyloid model mice
    • Zerbinatti, C. V. et al. Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Aβ42 accumulation in amyloid model mice. J. Biol. Chem. 281, 36180-36186 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 36180-36186
    • Zerbinatti, C.V.1
  • 76
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • Yan, S. D. et al. RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382, 685-691 (1996).
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1
  • 77
    • 0035847269 scopus 로고    scopus 로고
    • Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease
    • Sasaki, N. et al. Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease. Brain Res. 888, 256-262 (2001).
    • (2001) Brain Res , vol.888 , pp. 256-262
    • Sasaki, N.1
  • 78
    • 0000920292 scopus 로고    scopus 로고
    • Amyloid-β peptide-receptor for advanced glycation endproduct interaction elicits neuronal expression of macrophage-colony stimulating factor: A proinflammatory pathway in Alzheimer disease
    • Du Yan, S. et al. Amyloid-β peptide-receptor for advanced glycation endproduct interaction elicits neuronal expression of macrophage-colony stimulating factor: a proinflammatory pathway in Alzheimer disease. Proc. Natl Acad. Sci. USA 94, 5296-5301 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5296-5301
    • Du Yan, S.1
  • 79
    • 18244407519 scopus 로고    scopus 로고
    • Role of formyl peptide receptor-like 1 (FPRL1/FPR2) in mononuclear phagocyte responses in Alzheimer disease
    • Iribarren, P., Zhou, Y., Hu, J., Le, Y. & Wang, J. M. Role of formyl peptide receptor-like 1 (FPRL1/FPR2) in mononuclear phagocyte responses in Alzheimer disease. Immunol. Res. 31, 165-176 (2005).
    • (2005) Immunol. Res , vol.31 , pp. 165-176
    • Iribarren, P.1    Zhou, Y.2    Hu, J.3    Le, Y.4    Wang, J.M.5
  • 80
    • 23044445669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking by amyloid-β
    • Snyder, E. M. et al. Regulation of NMDA receptor trafficking by amyloid-β. Nature Neurosci. 8, 1051-1058 (2005).
    • (2005) Nature Neurosci , vol.8 , pp. 1051-1058
    • Snyder, E.M.1
  • 81
    • 0037135272 scopus 로고    scopus 로고
    • Uptake and pathogenic effects of amyloid β peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
    • Bi, X., Gall, C. M., Zhou, J. & Lynch, G. Uptake and pathogenic effects of amyloid β peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists. Neuroscience 112, 827-840 (2002).
    • (2002) Neuroscience , vol.112 , pp. 827-840
    • Bi, X.1    Gall, C.M.2    Zhou, J.3    Lynch, G.4
  • 82
    • 0037417238 scopus 로고    scopus 로고
    • Memantine in moderate-to-severe Alzheimer's disease
    • Reisberg, B. et al. Memantine in moderate-to-severe Alzheimer's disease. N. Engl. J. Med. 348, 1333-1341 (2003).
    • (2003) N. Engl. J. Med , vol.348 , pp. 1333-1341
    • Reisberg, B.1
  • 83
    • 6344247564 scopus 로고    scopus 로고
    • Memantine improves spatial learning in a transgenic mouse model of Alzheimer's disease
    • Minkeviciene, R., Banerjee, P. & Tanila, H. Memantine improves spatial learning in a transgenic mouse model of Alzheimer's disease. J. Pharmacol. Exp. Ther. 311, 677-682 (2004).
    • (2004) J. Pharmacol. Exp. Ther , vol.311 , pp. 677-682
    • Minkeviciene, R.1    Banerjee, P.2    Tanila, H.3
  • 84
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
    • Cleary, J. P. et al. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nature Neurosci. 8, 79-84 (2005).
    • (2005) Nature Neurosci , vol.8 , pp. 79-84
    • Cleary, J.P.1
  • 85
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M. et al. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539 (2002).
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 86
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-β protein assembly in the brain impairs memory
    • Lesne, S. et al. A specific amyloid-β protein assembly in the brain impairs memory. Nature 440, 352-357 (2006).
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1
  • 87
    • 0034609516 scopus 로고    scopus 로고
    • Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B. & Selkoe, D. J. The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain. Biochemistry 39, 10831-10839 (2000). Using cells from the human brain, this paper shows that Aβ oligomerization starts intraneuronally.
    • Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B. & Selkoe, D. J. The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain. Biochemistry 39, 10831-10839 (2000). Using cells from the human brain, this paper shows that Aβ oligomerization starts intraneuronally.
  • 88
    • 33144487701 scopus 로고    scopus 로고
    • Temporal profile of amyloid-β (Aβ) oligomerization in an in vivo model of Alzheimer disease. A link between Aβ and tau pathology
    • Oddo, S. et al. Temporal profile of amyloid-β (Aβ) oligomerization in an in vivo model of Alzheimer disease. A link between Aβ and tau pathology. J. Biol. Chem. 281, 1599-1604 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 1599-1604
    • Oddo, S.1
  • 89
    • 1842732209 scopus 로고    scopus 로고
    • Takahashi, R. H. et al. Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain. J. Neurosci. 24, 3592-3599 (2004). Shows that Aβ oligomers accumulate intraneuronally in AD brain.
    • Takahashi, R. H. et al. Oligomerization of Alzheimer's β-amyloid within processes and synapses of cultured neurons and brain. J. Neurosci. 24, 3592-3599 (2004). Shows that Aβ oligomers accumulate intraneuronally in AD brain.
  • 90
    • 33749467048 scopus 로고    scopus 로고
    • Amyloid β oligomerization is induced by brain lipid rafts
    • Kim, S. I., Yi, J. S. & Ko, Y. G. Amyloid β oligomerization is induced by brain lipid rafts. J. Cell Biochem. 99, 878-889 (2006).
    • (2006) J. Cell Biochem , vol.99 , pp. 878-889
    • Kim, S.I.1    Yi, J.S.2    Ko, Y.G.3
  • 91
    • 11144356498 scopus 로고    scopus 로고
    • Dimeric amyloid β protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease
    • Kawarabayashi, T. et al. Dimeric amyloid β protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease. J. Neurosci. 24, 3801-3809 (2004).
    • (2004) J. Neurosci , vol.24 , pp. 3801-3809
    • Kawarabayashi, T.1
  • 93
    • 33845424356 scopus 로고    scopus 로고
    • Inhibitors of amyloid β-protein aggregation mediated by GM1-containing raft-like membranes
    • Matsuzaki, K. et al. Inhibitors of amyloid β-protein aggregation mediated by GM1-containing raft-like membranes. Biochim. Biophys. Acta 1768, 122-130 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 122-130
    • Matsuzaki, K.1
  • 94
    • 13744255467 scopus 로고    scopus 로고
    • Wakabayashi, M., Okada, T., Kozutsumi, Y. & Matsuzaki, K. GM1 ganglioside-mediated accumulation of amyloid β-protein on cell membranes. Biochem. Biophys. Res. Commun. 328, 1019-1023 (2005).
    • Wakabayashi, M., Okada, T., Kozutsumi, Y. & Matsuzaki, K. GM1 ganglioside-mediated accumulation of amyloid β-protein on cell membranes. Biochem. Biophys. Res. Commun. 328, 1019-1023 (2005).
  • 95
    • 3042553742 scopus 로고    scopus 로고
    • Accelerated Aβ aggregation in the presence of GM1-ganglioside-accumulated synaptosomes of aged apoE4-knock-in mouse brain
    • Yamamoto, N. et al. Accelerated Aβ aggregation in the presence of GM1-ganglioside-accumulated synaptosomes of aged apoE4-knock-in mouse brain. FEBS Lett. 569, 135-139 (2004).
    • (2004) FEBS Lett , vol.569 , pp. 135-139
    • Yamamoto, N.1
  • 96
    • 0035120525 scopus 로고    scopus 로고
    • D'Andrea, M. R., Nagele, R. G., Wang, H. Y., Peterson, P. A. & Lee, D. H. Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease. Histopathology 38, 120-134 (2001). Provides evidence suggesting that in the brains of patients with AD, intracellular Aβ accumulation may lead to neuronal death, and that after being released in the extracellular compartment, it can contribute to the formation of plaques.
    • D'Andrea, M. R., Nagele, R. G., Wang, H. Y., Peterson, P. A. & Lee, D. H. Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease. Histopathology 38, 120-134 (2001). Provides evidence suggesting that in the brains of patients with AD, intracellular Aβ accumulation may lead to neuronal death, and that after being released in the extracellular compartment, it can contribute to the formation of plaques.
  • 97
    • 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, B. A. 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. 397, 139-147 (1998).
    • (1998) J. Comp. Neurol , vol.397 , pp. 139-147
    • Bahr, B.A.1
  • 98
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk, D. et al. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400, 173-177 (1999).
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1
  • 99
    • 0034700471 scopus 로고    scopus 로고
    • Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus, C. et al. Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 408, 979-982 (2000).
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1
  • 100
    • 4043167747 scopus 로고    scopus 로고
    • Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H. & LaFerla, F. M. Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43, 321-332 (2004). Shows that Aβ immunotherapy clears intraneuronal Aβ accumulation, which leads to the removal of tau deposits, thus linking intracellular Aβ and tau pathology.
    • Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H. & LaFerla, F. M. Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43, 321-332 (2004). Shows that Aβ immunotherapy clears intraneuronal Aβ accumulation, which leads to the removal of tau deposits, thus linking intracellular Aβ and tau pathology.
  • 101
    • 25144501662 scopus 로고    scopus 로고
    • Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease
    • Gouras, G. K., Almeida, C. G. & Takahashi, R. H. Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease. Neurobiol. Aging 26, 1235-1244 (2005).
    • (2005) Neurobiol. Aging , vol.26 , pp. 1235-1244
    • Gouras, G.K.1    Almeida, C.G.2    Takahashi, R.H.3
  • 103
    • 7244234180 scopus 로고    scopus 로고
    • Subcellular topography of neuronal A? peptide in APPxPS1 transgenic mice
    • Langui, D. et al. Subcellular topography of neuronal A? peptide in APPxPS1 transgenic mice. Am. J. Pathol. 165, 1465-1477 (2004).
    • (2004) Am. J. Pathol , vol.165 , pp. 1465-1477
    • Langui, D.1
  • 104
    • 33646461282 scopus 로고    scopus 로고
    • β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida, C. G., Takahashi, R. H. & Gouras, G. K. β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J. Neurosci. 26, 4277-4288 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 106
    • 27644522515 scopus 로고    scopus 로고
    • Amyloid peptide attenuates the proteasome activity in neuronal cells
    • Oh, S. et al. Amyloid peptide attenuates the proteasome activity in neuronal cells. Mech. Ageing Dev. 126, 1292-1299 (2005).
    • (2005) Mech. Ageing Dev , vol.126 , pp. 1292-1299
    • Oh, S.1
  • 108
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak, M. et al. Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 15, 1437-1449 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1
  • 109
    • 19944373389 scopus 로고    scopus 로고
    • Nicastrin, presenilin, APH-1, and PEN-2 form active γ-secretase complexes in mitochondria
    • Hansson, C. A. et al. Nicastrin, presenilin, APH-1, and PEN-2 form active γ-secretase complexes in mitochondria. J. Biol. Chem. 279, 51654-51660 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 51654-51660
    • Hansson, C.A.1
  • 110
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Aβ: A potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • Caspersen, C. et al. Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J. 19, 2040-2041 (2005).
    • (2005) FASEB J , vol.19 , pp. 2040-2041
    • Caspersen, C.1
  • 111
    • 33746103234 scopus 로고    scopus 로고
    • Mitochondrial dysfunction induced by disease relevant AβPP and tau protein mutations
    • Keil, U. et al. Mitochondrial dysfunction induced by disease relevant AβPP and tau protein mutations. J. Alzheimers Dis. 9, 139-146 (2006).
    • (2006) J. Alzheimers Dis , vol.9 , pp. 139-146
    • Keil, U.1
  • 112
    • 14644442872 scopus 로고    scopus 로고
    • Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L. & LaFerla, F. M. Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 45, 675-688 (2005). Shows that intraneuronal Aβ accumulation is responsible for the onset of cognitive decline in the 3xTg-AD.
    • Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L. & LaFerla, F. M. Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 45, 675-688 (2005). Shows that intraneuronal Aβ accumulation is responsible for the onset of cognitive decline in the 3xTg-AD.
  • 113
    • 0022650213 scopus 로고
    • Selective impairment of learning and blockade of long-term potentiation by an N-methyl-D-aspartate receptor antagonist, AP5
    • Morris, R. G., Anderson, E., Lynch, G. S. & Baudry, M. Selective impairment of learning and blockade of long-term potentiation by an N-methyl-D-aspartate receptor antagonist, AP5. Nature 319, 774-776 (1986).
    • (1986) Nature , vol.319 , pp. 774-776
    • Morris, R.G.1    Anderson, E.2    Lynch, G.S.3    Baudry, M.4
  • 114
    • 33747199933 scopus 로고    scopus 로고
    • Ubiquitin hydrolase Uch-L1 rescues β-amyloid-induced decreases in synaptic function and contextual memory
    • Gong, B. et al. Ubiquitin hydrolase Uch-L1 rescues β-amyloid-induced decreases in synaptic function and contextual memory. Cell 126, 775-788 (2006).
    • (2006) Cell , vol.126 , pp. 775-788
    • Gong, B.1
  • 115
    • 34247380762 scopus 로고    scopus 로고
    • Dietary docosahexaenoic acid and docosapentaenoic acid ameliorate amyloid-β and tau pathology via a mechanism involving presenilin 1 levels
    • Green, K. N. et al. Dietary docosahexaenoic acid and docosapentaenoic acid ameliorate amyloid-β and tau pathology via a mechanism involving presenilin 1 levels. J. Neurosci. 27, 4385-4395 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 4385-4395
    • Green, K.N.1
  • 116
    • 14944376646 scopus 로고    scopus 로고
    • Chronic administration of docosahexaenoic acid ameliorates the impairment of spatial cognition learning ability in amyloid β-infused rats
    • Hashimoto, M. et al. Chronic administration of docosahexaenoic acid ameliorates the impairment of spatial cognition learning ability in amyloid β-infused rats. J. Nutr. 135, 549-555 (2005).
    • (2005) J. Nutr , vol.135 , pp. 549-555
    • Hashimoto, M.1
  • 117
    • 16244416174 scopus 로고    scopus 로고
    • A diet enriched with the omega-3 fatty acid docosahexaenoic acid reduces amyloid burden in an aged Alzheimer mouse model
    • Lim, G. P. et al. A diet enriched with the omega-3 fatty acid docosahexaenoic acid reduces amyloid burden in an aged Alzheimer mouse model. J. Neurosci. 25, 3032-3040 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 3032-3040
    • Lim, G.P.1
  • 118
    • 0035871641 scopus 로고    scopus 로고
    • Stimulation of β-amyloid precursor protein trafficking by insulin reduces intraneuronal β-amyloid and requires mitogen-activated protein kinase signaling
    • Gasparini, L. et al. Stimulation of β-amyloid precursor protein trafficking by insulin reduces intraneuronal β-amyloid and requires mitogen-activated protein kinase signaling. J. Neurosci. 21, 2561-2570 (2001).
    • (2001) J. Neurosci , vol.21 , pp. 2561-2570
    • Gasparini, L.1
  • 119
    • 33846570982 scopus 로고    scopus 로고
    • Learning decreases Aβ*56 and tau pathology and ameliorates behavioral decline in 3xTg-AD mice
    • Billings, L. M., Green, K. N., McGaugh, J. L. & LaFerla, F. M. Learning decreases Aβ*56 and tau pathology and ameliorates behavioral decline in 3xTg-AD mice. J. Neurosci. 27, 751-761 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 751-761
    • Billings, L.M.1    Green, K.N.2    McGaugh, J.L.3    LaFerla, F.M.4
  • 120
    • 33748253471 scopus 로고    scopus 로고
    • Glucocorticoids increase amyloid-β and tau pathology in a mouse model of Alzheimer's disease
    • Green, K. N., Billings, L. M., Roozendaal, B., McGaugh, J. L. & LaFerla, F. M. Glucocorticoids increase amyloid-β and tau pathology in a mouse model of Alzheimer's disease. J. Neurosci. 26, 9047-9056 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 9047-9056
    • Green, K.N.1    Billings, L.M.2    Roozendaal, B.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 121
    • 0028177562 scopus 로고
    • Induction of Alzheimer-like β-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol
    • Sparks, D. L. et al. Induction of Alzheimer-like β-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol. Exp. Neurol. 126, 88-94 (1994).
    • (1994) Exp. Neurol , vol.126 , pp. 88-94
    • Sparks, D.L.1
  • 122
    • 0034643895 scopus 로고    scopus 로고
    • Oxidative stress induces intracellular accumulation of amyloid β-protein (A?) in human neuroblastoma cells
    • Misonou, H., Morishima-Kawashima, M. & Ihara, Y. Oxidative stress induces intracellular accumulation of amyloid β-protein (A?) in human neuroblastoma cells. Biochemistry 39, 6951-6959 (2000).
    • (2000) Biochemistry , vol.39 , pp. 6951-6959
    • Misonou, H.1    Morishima-Kawashima, M.2    Ihara, Y.3
  • 123
    • 21844474569 scopus 로고    scopus 로고
    • Homocysteic acid induces intraneuronal accumulation of neurotoxic Aβ42: Implications for the pathogenesis of Alzheimer's disease
    • Hasegawa, T. et al. Homocysteic acid induces intraneuronal accumulation of neurotoxic Aβ42: implications for the pathogenesis of Alzheimer's disease. J. Neurosci. Res. 80, 869-876 (2005).
    • (2005) J. Neurosci. Res , vol.80 , pp. 869-876
    • Hasegawa, T.1
  • 124
    • 0037195546 scopus 로고    scopus 로고
    • Consistent immunohistochemical detection of intracellular β-amyloid42 in pyramidal neurons of Alzheimer's disease entorhinal cortex
    • D'Andrea, M. R., Nagele, R. G., Wang, H. Y. & Lee, D. H. Consistent immunohistochemical detection of intracellular β-amyloid42 in pyramidal neurons of Alzheimer's disease entorhinal cortex. Neurosci. Lett. 333, 163-166 (2002).
    • (2002) Neurosci. Lett , vol.333 , pp. 163-166
    • D'Andrea, M.R.1    Nagele, R.G.2    Wang, H.Y.3    Lee, D.H.4
  • 125
    • 0037133908 scopus 로고    scopus 로고
    • Lipofuscin and Aβ42 exhibit distinct distribution patterns in normal and Alzheimer's disease brains
    • D'Andrea, M. R. et al. Lipofuscin and Aβ42 exhibit distinct distribution patterns in normal and Alzheimer's disease brains. Neurosci. Lett. 323, 45-49 (2002).
    • (2002) Neurosci. Lett , vol.323 , pp. 45-49
    • D'Andrea, M.R.1
  • 126
    • 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 Aβ stabilization. J. Clin. Invest. 100, 310-320 (1997).
    • (1997) J. Clin. Invest , vol.100 , pp. 310-320
    • LaFerla, F.M.1    Troncoso, J.C.2    Strickland, D.K.3    Kawas, C.H.4    Jay, G.5
  • 127
    • 0033621540 scopus 로고    scopus 로고
    • Aβ42-positive non-pyramidal neurons around amyloid plaques in Alzheimer's disease
    • Mochizuki, A., Tamaoka, A., Shimohata, A., Komatsuzaki, Y. & Shoji, S. Aβ42-positive non-pyramidal neurons around amyloid plaques in Alzheimer's disease. Lancet 355, 42-43 (2000).
    • (2000) Lancet , vol.355 , pp. 42-43
    • Mochizuki, A.1    Tamaoka, A.2    Shimohata, A.3    Komatsuzaki, Y.4    Shoji, S.5
  • 128
    • 0026327717 scopus 로고
    • Amyloid filaments in inclusion body myositis. Novel findings provide insight into nature of filaments
    • Mendell, J. R., Sahenk, Z., Gales, T. & Paul, L. Amyloid filaments in inclusion body myositis. Novel findings provide insight into nature of filaments. Arch. Neurol. 48, 1229-1234 (1991).
    • (1991) Arch. Neurol , vol.48 , pp. 1229-1234
    • Mendell, J.R.1    Sahenk, Z.2    Gales, T.3    Paul, L.4
  • 129
    • 0027232988 scopus 로고
    • β-Amyloid precursor protein mRNA is increased in inclusion-body myositis muscle
    • Sarkozi, E., Askanas, V., Johnson, S. A., Engel, W. K. & Alvarez, R. B. β-Amyloid precursor protein mRNA is increased in inclusion-body myositis muscle. Neuroreport 4, 815-818 (1993).
    • (1993) Neuroreport , vol.4 , pp. 815-818
    • Sarkozi, E.1    Askanas, V.2    Johnson, S.A.3    Engel, W.K.4    Alvarez, R.B.5
  • 130
    • 0027240930 scopus 로고
    • Enhanced detection of congo-red-positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique
    • Askanas, V., Engel, W. K. & Alvarez, R. B. Enhanced detection of congo-red-positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique. Neurology 43, 1265-1267 (1993).
    • (1993) Neurology , vol.43 , pp. 1265-1267
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 131
    • 15944381518 scopus 로고    scopus 로고
    • Age-related changes of intracellular Aβ in cynomolgus monkey brains
    • Kimura, N. et al. Age-related changes of intracellular Aβ in cynomolgus monkey brains. Neuropathol. Appl. Neurobiol. 31, 170-180 (2005).
    • (2005) Neuropathol. Appl. Neurobiol , vol.31 , pp. 170-180
    • Kimura, N.1
  • 132
    • 0028113719 scopus 로고
    • Synaptic pathology and glial responses to neuronal injury precede the formation of senile plaques and amyloid deposits in the aging cerebral cortex
    • Martin, L. J., Pardo, C. A., Cork, L. C. & Price, D. L. Synaptic pathology and glial responses to neuronal injury precede the formation of senile plaques and amyloid deposits in the aging cerebral cortex. Am. J. Pathol. 145, 1358-1381 (1994).
    • (1994) Am. J. Pathol , vol.145 , pp. 1358-1381
    • Martin, L.J.1    Pardo, C.A.2    Cork, L.C.3    Price, D.L.4
  • 133
    • 0027332522 scopus 로고
    • β-amyloid accumulation in aged canine brain: A model of early plaque formation in Alzheimer's disease
    • Cummings, B. J., Su, J. H., Cotman, C. W., White, R. & Russell, M. J. β-amyloid accumulation in aged canine brain: a model of early plaque formation in Alzheimer's disease. Neurobiol. Aging 14, 547-560 (1993).
    • (1993) Neurobiol. Aging , vol.14 , pp. 547-560
    • Cummings, B.J.1    Su, J.H.2    Cotman, C.W.3    White, R.4    Russell, M.J.5
  • 134
    • 0034008482 scopus 로고    scopus 로고
    • Ultrastructural evidence of fibrillar β-amyloid associated with neuronal membranes in behaviorally characterized aged dog brains
    • Torp, R. et al. Ultrastructural evidence of fibrillar β-amyloid associated with neuronal membranes in behaviorally characterized aged dog brains. Neuroscience 96, 495-506 (2000).
    • (2000) Neuroscience , vol.96 , pp. 495-506
    • Torp, R.1
  • 135
    • 33749826587 scopus 로고    scopus 로고
    • p25/cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid β in vivo
    • Cruz, J. C. et al. p25/cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid β in vivo. J. Neurosci. 26, 10536-10541 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 10536-10541
    • Cruz, J.C.1
  • 136
    • 4644276796 scopus 로고    scopus 로고
    • Casas, C. et al. Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Aβ42 accumulation in a novel Alzheimer transgenic model. Am. J. Pathol. 165, 1289-1300 (2004). Provides in vivo evidence that intraneuronal Aβ accumulation is toxic and leads to cell death.
    • Casas, C. et al. Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Aβ42 accumulation in a novel Alzheimer transgenic model. Am. J. Pathol. 165, 1289-1300 (2004). Provides in vivo evidence that intraneuronal Aβ accumulation is toxic and leads to cell death.
  • 137
    • 37549016329 scopus 로고    scopus 로고
    • Intraneuronal amyloid β and reduced brain volume in a novel APP T714I mouse model for Alzheimer's disease
    • 16 Nov, doi:10.1016/j.neurobiolaging.2006.10.016
    • Van Broeck, B. et al. Intraneuronal amyloid β and reduced brain volume in a novel APP T714I mouse model for Alzheimer's disease. Neurobiol. Aging 16 Nov 2006 (doi:10.1016/j.neurobiolaging.2006.10.016).
    • (2006) Neurobiol. Aging
    • Van Broeck, B.1
  • 138
    • 0037454477 scopus 로고    scopus 로고
    • Early intraneuronal Aβ deposition in the hippocampus of APP transgenic mice
    • Shie, F. S., LeBoeuf, R. C. & Jin, L. W. Early intraneuronal Aβ deposition in the hippocampus of APP transgenic mice. Neuroreport 14, 123-129 (2003).
    • (2003) Neuroreport , vol.14 , pp. 123-129
    • Shie, F.S.1    LeBoeuf, R.C.2    Jin, L.W.3
  • 139
    • 28044446528 scopus 로고    scopus 로고
    • Intraneuronal β-amyloid expression downregulates the Akt survival pathway and blunts the stress response
    • Magrane, J. et al. Intraneuronal β-amyloid expression downregulates the Akt survival pathway and blunts the stress response. J. Neurosci. 25, 10960-10969 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 10960-10969
    • Magrane, J.1
  • 140
    • 35148836216 scopus 로고    scopus 로고
    • GRK5 deficiency leads to early Alzheimer-like pathology and working memory impairment
    • 2 October, doi: 10.1016/j.neurobiolaging.2006.08.013
    • Suo, Z. et al. GRK5 deficiency leads to early Alzheimer-like pathology and working memory impairment. Neurobiol. Aging 2 October 2006 (doi: 10.1016/j.neurobiolaging.2006.08.013).
    • (2006) Neurobiol. Aging
    • Suo, Z.1
  • 141
    • 0037197835 scopus 로고    scopus 로고
    • Inclusion body myositis-like phenotype induced by transgenic overexpression of βAPP in skeletal muscle
    • Sugarman, M. C. et al. Inclusion body myositis-like phenotype induced by transgenic overexpression of βAPP in skeletal muscle. Proc. Natl Acad. Sci. USA 99, 6334-6339 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 6334-6339
    • Sugarman, M.C.1
  • 142
    • 33744739867 scopus 로고    scopus 로고
    • Genetically augmenting Aβ42 levels in skeletal muscle exacerbates inclusion body myositis-like pathology and motor deficits in transgenic mice
    • Kitazawa, M., Green, K. N., Caccamo, A. & LaFerla, F. M. Genetically augmenting Aβ42 levels in skeletal muscle exacerbates inclusion body myositis-like pathology and motor deficits in transgenic mice. Am. J. Pathol. 168, 1986-1997 (2006).
    • (2006) Am. J. Pathol , vol.168 , pp. 1986-1997
    • Kitazawa, M.1    Green, K.N.2    Caccamo, A.3    LaFerla, F.M.4
  • 143
    • 33845599412 scopus 로고    scopus 로고
    • Transgenic expression of β-APP in fast-twitch skeletal muscle leads to calcium dyshomeostasis and IBM-like pathology
    • Moussa, C. E. et al. Transgenic expression of β-APP in fast-twitch skeletal muscle leads to calcium dyshomeostasis and IBM-like pathology. FASEB J. 20, 2165-2167 (2006).
    • (2006) FASEB J , vol.20 , pp. 2165-2167
    • Moussa, C.E.1
  • 144
    • 8444233219 scopus 로고    scopus 로고
    • Altered mitogen-activated protein kinase signaling, tau hyperphosphorylation and mild spatial learning dysfunction in transgenic rats expressing the β-amyloid peptide intracellularly in hippocampal and cortical neurons
    • Echeverria, V. et al. Altered mitogen-activated protein kinase signaling, tau hyperphosphorylation and mild spatial learning dysfunction in transgenic rats expressing the β-amyloid peptide intracellularly in hippocampal and cortical neurons. Neuroscience 129, 583-592 (2004).
    • (2004) Neuroscience , vol.129 , pp. 583-592
    • Echeverria, V.1
  • 146
    • 33644869497 scopus 로고    scopus 로고
    • Inclusion-body myositis: A myodegenerative conformational disorder associated with Aβ, protein misfolding, and proteasome inhibition
    • Askanas, V. & Engel, W. K. Inclusion-body myositis: a myodegenerative conformational disorder associated with Aβ, protein misfolding, and proteasome inhibition. Neurology 66, S39-S48 (2006).
    • (2006) Neurology , vol.66
    • Askanas, V.1    Engel, W.K.2


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