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Volumn 22, Issue SUPPL. 3, 2010, Pages

Alzheimer's disease: A general introduction and pathomechanism

Author keywords

Alzheimer's disease; amyloid ; amyloid protein precursor; fibrils; neurotoxicity; oligomers; protein misfolding; tau

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; TAU PROTEIN;

EID: 78650462753     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2010-100975     Document Type: Review
Times cited : (153)

References (167)
  • 1
    • 77949336151 scopus 로고    scopus 로고
    • 2010 Alzheimer's disease facts and figures
    • 2010 Alzheimer's disease facts and figures (2010) Alzheimers Dement 6, 158-194.
    • (2010) Alzheimers Dement , vol.6 , pp. 158-194
  • 2
    • 53749102630 scopus 로고    scopus 로고
    • Therapeutic strategies for Alzheimer's disease
    • Barten DM, Albright CF (2008) Therapeutic strategies for Alzheimer's disease. Mol Neurobiol 37, 171-186.
    • (2008) Mol Neurobiol , vol.37 , pp. 171-186
    • Barten, D.M.1    Albright, C.F.2
  • 3
    • 65549116931 scopus 로고    scopus 로고
    • Alzheimer's disease research: Scientific productivity and impact of the top 100 investigators in the field
    • Sorensen AA (2009) Alzheimer's disease research: scientific productivity and impact of the top 100 investigators in the field. J Alzheimers Dis 16, 451-465.
    • (2009) J Alzheimers Dis , vol.16 , pp. 451-465
    • Sorensen, A.A.1
  • 4
    • 0027490614 scopus 로고
    • Staging of Alzheimer-related cortical destruction
    • Braak H, Braak E, Bohl J (1993) Staging of Alzheimer-related cortical destruction. Eur Neurol 33, 403-408.
    • (1993) Eur Neurol , vol.33 , pp. 403-408
    • Braak, H.1    Braak, E.2    Bohl, J.3
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. AnnuRevBiochem 75, 333-366.
    • (2006) AnnuRevBiochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 0029078972 scopus 로고
    • Correlations of synaptic and pathological markers with cognition of the elderly
    • discussion 298-304
    • Dickson DW, Crystal HA, Bevona C, Honer W, Vincent I, Davies P (1995) Correlations of synaptic and pathological markers with cognition of the elderly. Neurobiol Aging 16, 285-298; discussion 298-304.
    • (1995) Neurobiol Aging , vol.16 , pp. 285-298
    • Dickson, D.W.1    Crystal, H.A.2    Bevona, C.3    Honer, W.4    Vincent, I.5    Davies, P.6
  • 7
    • 0000961432 scopus 로고
    • Uber eine im Gehirn und RUckenmark des Menschen aufgefundene Substanz mit der chemischen Reaktion der Cellulose
    • Virchow R (1854) Uber eine im Gehirn und RUckenmark des Menschen aufgefundene Substanz mit der chemischen Reaktion der Cellulose. Virchows Arch Pathol Anat 6, 135137.
    • (1854) Virchows Arch Pathol Anat , vol.6 , pp. 135137
    • Virchow, R.1
  • 9
    • 0010665141 scopus 로고
    • Uber miliare Sklerose der Hirnrinde bei seniler Atrophie
    • Redlich E (1898) Uber miliare Sklerose der Hirnrinde bei seniler Atrophie. Jarbucher Psychiatr Neurol 17.
    • (1898) Jarbucher Psychiatr Neurol , vol.17
    • Redlich, E.1
  • 10
    • 0000304402 scopus 로고
    • Eine spezifische amyloidfarbung mit Kongorot Specific staining of amyloid with Congo red
    • Bennhold HH (1922) Eine spezifische amyloidfarbung mit Kongorot Specific staining of amyloid with Congo red]. Miinchener Medizinische Wochenschrifte 69, 1537-1538.
    • (1922) Miinchener Medizinische Wochenschrifte , vol.69 , pp. 1537-1538
    • Bennhold, H.H.1
  • 13
    • 0001611370 scopus 로고
    • Electron microscopic observations on a fibrous component in amyloid of diverse origins
    • Cohen AS, Calkins E (1959) Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 183, 1202-1203.
    • (1959) Nature , vol.183 , pp. 1202-1203
    • Cohen, A.S.1    Calkins, E.2
  • 14
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes ED, Glenner GG (1968) X-ray diffraction studies on amyloid filaments. JHistochem Cytochem 16, 673-677.
    • (1968) JHistochem Cytochem , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 15
    • 0015219685 scopus 로고
    • Amyloid fibril proteins: Proof of homology with im-munoglobulin light chains by sequence analyses
    • Glenner GG, Terry W, Harada M, Isersky C, Page D (1971) Amyloid fibril proteins: proof of homology with im-munoglobulin light chains by sequence analyses. Science 172, 1150-1151.
    • (1971) Science , vol.172 , pp. 1150-1151
    • Glenner, G.G.1    Terry, W.2    Harada, M.3    Isersky, C.4    Page, D.5
  • 16
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cere-brovascular amyloid protein
    • Glenner GG, Wong CW (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cere-brovascular amyloid protein. Biochem Biophys Res Commun 120, 885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 17
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW (1984) Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 122, 11311135.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 11311135
    • Glenner, G.G.1    Wong, C.W.2
  • 19
    • 0022257253 scopus 로고
    • Mise en evidence de la immunologique de la protein tau au lesions de degeneresescence neurofibrillaire de la maladie Alzheimer
    • Brion JP, Passareiro, H., Nunez, J., and Flament Durand, J. (1985) Mise en evidence de la immunologique de la protein tau au lesions de degeneresescence neurofibrillaire de la maladie Alzheimer. ArchBiol (Brux) 95, 229-235.
    • (1985) ArchBiol (Brux) , vol.95 , pp. 229-235
    • Brion, J.P.1    Passareiro, H.2    Nunez, J.3    Flament Durand, J.4
  • 20
    • 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 CM, Crowther RA, Walker JE, Klug A (1988) 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) 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
  • 26
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA (1992) Alzheimer's disease: the amyloid cascade hypothesis. Science 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 27
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe DJ (1991) The molecular pathology of Alzheimer's disease. Neuron 6, 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 28
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 32
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: Evidence that an initially deposited species is A beta 42(43)
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y (1994) Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43). Neuron 13, 45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 34
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J, Chen F, van Dorpe J, Nitsch RM (2001) Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science 293, 1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 35
    • 0031949084 scopus 로고    scopus 로고
    • Frontotemporal dementia and Parkinsonism linked to chromosome 17: A new group of tauopathies
    • Spillantini MG, Bird TD, Ghetti B (1998) Frontotemporal dementia and Parkinsonism linked to chromosome 17: a new group of tauopathies. Brain Pathol 8, 387-402.
    • (1998) Brain Pathol , vol.8 , pp. 387-402
    • Spillantini, M.G.1    Bird, T.D.2    Ghetti, B.3
  • 36
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypo thesis: A genetic perspective
    • Tanzi RE, Bertram L (2005) Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120, 545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 37
    • 67651180986 scopus 로고    scopus 로고
    • The amyloid hypothesis for Alzheimer's disease: A critical reappraisal
    • Hardy J (2009) The amyloid hypothesis for Alzheimer's disease: a critical reappraisal. JNeurochem 110, 1129-1134.
    • (2009) JNeurochem , vol.110 , pp. 1129-1134
    • Hardy, J.1
  • 38
    • 64449088789 scopus 로고    scopus 로고
    • Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis
    • Vattemi G, Nogalska A, King Engel W, D'Agostino C, Checler F, Askanas V (2009) Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis. Acta Neuropathol 117, 569-574.
    • (2009) Acta Neuropathol , vol.117 , pp. 569-574
    • Vattemi, G.1    Nogalska, A.2    King Engel, W.3    D'Agostino, C.4    Checler, F.5    Askanas, V.6
  • 39
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in Alzheimer disease
    • De Strooper B, Vassar R, Golde T (2010) The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat Rev Neurol 6, 99-107.
    • (2010) Nat Rev Neurol , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 40
    • 0027333557 scopus 로고
    • Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide
    • Haass C, Selkoe DJ (1993) Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide. Cell 75, 1039-1042.
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 42
    • 0038045587 scopus 로고    scopus 로고
    • The production of amyloid beta peptide is a critical require-mentforthe viability of central neurons
    • Plant LD, Boyle JP, Smith IF, Peers C, Pearson HA (2003) The production of amyloid beta peptide is a critical require-mentforthe viability of central neurons. JNeurosci 23, 55315535.
    • (2003) JNeurosci , vol.23 , pp. 55315535
    • Plant, L.D.1    Boyle, J.P.2    Smith, I.F.3    Peers, C.4    Pearson, H.A.5
  • 44
    • 0035282739 scopus 로고    scopus 로고
    • Characterization of the neurotrophic interaction between nerve growth factor and secreted alpha-amyloid precursor protein
    • Luo JJ, Wallace MS, Hawver DB, Kusiak JW, Wallace WC (2001) Characterization of the neurotrophic interaction between nerve growth factor and secreted alpha-amyloid precursor protein. J Neurosci Res 63, 410-420.
    • (2001) J Neurosci Res , vol.63 , pp. 410-420
    • Luo, J.J.1    Wallace, M.S.2    Hawver, D.B.3    Kusiak, J.W.4    Wallace, W.C.5
  • 45
    • 79961158069 scopus 로고    scopus 로고
    • Traumatic brain injury and amyloid-beta pathology: A link to Alzheimer's disease?
    • in press
    • Johnson VE, Stewart W, Smith DH (2010) Traumatic brain injury and amyloid-beta pathology: a link to Alzheimer's disease? Nat Rev Neurosci, in press.
    • (2010) Nat Rev Neurosci
    • Johnson, V.E.1    Stewart, W.2    Smith, D.H.3
  • 51
    • 53849106834 scopus 로고    scopus 로고
    • Cystatin C-cathepsin B axis regulates amyloid beta levels and associated neuronal deficits in an animal model of Alzheimer's disease
    • Sun B, Zhou Y, Halabisky B, Lo I, Cho SH, Mueller-Steiner S, Devidze N, Wang X, Grubb A, Gan L (2008) Cystatin C-cathepsin B axis regulates amyloid beta levels and associated neuronal deficits in an animal model of Alzheimer's disease. Neuron 60, 247-257.
    • (2008) Neuron , vol.60 , pp. 247-257
    • Sun, B.1    Zhou, Y.2    Halabisky, B.3    Lo, I.4    Cho, S.H.5    Mueller-Steiner, S.6    Devidze, N.7    Wang, X.8    Grubb, A.9    Gan, L.10
  • 52
    • 0035816707 scopus 로고    scopus 로고
    • Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme
    • Eckman EA, Reed DK, Eckman CB (2001) Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme. J Biol Chem 276, 24540-24548.
    • (2001) J Biol Chem , vol.276 , pp. 24540-24548
    • Eckman, E.A.1    Reed, D.K.2    Eckman, C.B.3
  • 54
    • 4444276735 scopus 로고    scopus 로고
    • Clearance of Alzheimer's Abeta peptide: The many roads to perdition
    • Tanzi RE, Moir RD, Wagner SL (2004) Clearance of Alzheimer's Abeta peptide: the many roads to perdition. Neuron 43, 605-608.
    • (2004) Neuron , vol.43 , pp. 605-608
    • Tanzi, R.E.1    Moir, R.D.2    Wagner, S.L.3
  • 55
    • 0037306664 scopus 로고    scopus 로고
    • Apolipopro-tein e influences amyloid-beta clearance from the murine periphery
    • Hone E, Martins IJ, Fonte J, Martins RN (2003) Apolipopro-tein E influences amyloid-beta clearance from the murine periphery. J Alzheimers Dis 5, 1-8.
    • (2003) J Alzheimers Dis , vol.5 , pp. 1-8
    • Hone, E.1    Martins, I.J.2    Fonte, J.3    Martins, R.N.4
  • 56
    • 34748872706 scopus 로고    scopus 로고
    • The role of intracellular amyloid beta in Alzheimer's disease
    • Li M, Chen L, Lee DH, Yu LC, Zhang Y (2007) The role of intracellular amyloid beta in Alzheimer's disease. Prog Neurobiol 83, 131-139.
    • (2007) Prog Neurobiol , vol.83 , pp. 131-139
    • Li, M.1    Chen, L.2    Lee, D.H.3    Yu, L.C.4    Zhang, Y.5
  • 57
    • 0032855482 scopus 로고    scopus 로고
    • Methodological and chemical factors affecting amyloid beta peptide amyloidogenicity
    • Zagorski MG, Yang J, Shao H, Ma K, Zeng H, Hong A (1999) Methodological and chemical factors affecting amyloid beta peptide amyloidogenicity. Methods Enzymol 309, 189-204.
    • (1999) Methods Enzymol , vol.309 , pp. 189-204
    • Zagorski, M.G.1    Yang, J.2    Shao, H.3    Ma, K.4    Zeng, H.5    Hong, A.6
  • 58
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. NatRevMol Cell Biol 8, 101-112.
    • (2007) NatRevMol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 60
    • 67349158815 scopus 로고    scopus 로고
    • Variations in the neuropathology of familial Alzheimer's disease
    • Shepherd C, McCann H, Halliday GM (2009) Variations in the neuropathology of familial Alzheimer's disease. Acta Neuropathol 118, 37-52.
    • (2009) Acta Neuropathol , vol.118 , pp. 37-52
    • Shepherd, C.1    McCann, H.2    Halliday, G.M.3
  • 64
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct beta-amyloid peptide species, A beta N3(pE), in senile plaques
    • Saido TC, Iwatsubo T, Mann DM, Shimada H, Ihara Y, Kawashima S (1995) Dominant and differential deposition of distinct beta-amyloid peptide species, A beta N3(pE), in senile plaques. Neuron 14, 457-466.
    • (1995) Neuron , vol.14 , pp. 457-466
    • Saido, T.C.1    Iwatsubo, T.2    Mann, D.M.3    Shimada, H.4    Ihara, Y.5    Kawashima, S.6
  • 66
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla FM, Green KN, Oddo S (2007) Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 8, 499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 67
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid-beta precursor protein: Integrating structure with biological function
    • Reinhard C, Hebert SS, De Strooper B (2005) The amyloid-beta precursor protein: integrating structure with biological function. EMBOJ 24, 3996-4006.
    • (2005) EMBOJ , vol.24 , pp. 3996-4006
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3
  • 68
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • DOI 10.1016/0092-8674(89)90177-3
    • Weidemann A, Konig G, Bunke D, Fischer P, Salbaum JM, Masters CL, Beyreuther K (1989) Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 57, 115-126. (Pubitemid 19098873)
    • (1989) Cell , vol.57 , Issue.1 , pp. 115-126
    • Weidemann, A.1    Konig, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6    Beyreuther, K.7
  • 70
    • 8144230876 scopus 로고    scopus 로고
    • Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members
    • Herms J, Anliker B, Heber S, Ring S, Fuhrmann M, Kret-zschmar H, Sisodia S, Muller U (2004) Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members. EMBO J 23, 4106-4115.
    • (2004) EMBO J , vol.23 , pp. 4106-4115
    • Herms, J.1    Anliker, B.2    Heber, S.3    Ring, S.4    Fuhrmann, M.5    Kret-Zschmar, H.6    Sisodia, S.7    Muller, U.8
  • 72
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson MP (1997) Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. PhysiolRev 77, 1081-1132.
    • (1997) PhysiolRev , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 74
    • 0026735070 scopus 로고
    • Targeting of cell-surface beta-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ (1992) Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 357, 500-503.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 77
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neu-rofibrillary tangles of Alzheimer's disease
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neu-rofibrillary tangles of Alzheimer's disease. Neuron 3, 519526.
    • (1989) Neuron , vol.3 , pp. 519526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 80
    • 33846015514 scopus 로고    scopus 로고
    • Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles
    • Oddo S, Vasilevko V, Caccamo A, Kitazawa M, Cribbs DH, LaFerla FM (2006) Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J Biol Chem 281, 39413-39423.
    • (2006) J Biol Chem , vol.281 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3    Kitazawa, M.4    Cribbs, D.H.5    Laferla, F.M.6
  • 84
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 87
    • 3142604036 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases
    • Ross CA, Pickart CM (2004) The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends Cell Biol 14, 703-711.
    • (2004) Trends Cell Biol , vol.14 , pp. 703-711
    • Ross, C.A.1    Pickart, C.M.2
  • 88
    • 70449640181 scopus 로고    scopus 로고
    • Quality control against misfolded proteins in the cytosol: A network for cell survival
    • Kubota H (2009) Quality control against misfolded proteins in the cytosol: a network for cell survival. J Biochem 146, 609-616.
    • (2009) J Biochem , vol.146 , pp. 609-616
    • Kubota, H.1
  • 90
    • 60849128810 scopus 로고    scopus 로고
    • Autoantibodies against beta-amyloid are common in Alzheimer's disease and help control plaque burden
    • Kellner A, Matschke J, Bernreuther C, Moch H, Ferrer I, Glatzel M
    • Kellner A, Matschke J, Bernreuther C, Moch H, Ferrer I, Glatzel M (2009) Autoantibodies against beta-amyloid are common in Alzheimer's disease and help control plaque burden. Ann Neurol 65, 24-31.
    • (2009) Ann Neurol , vol.65 , pp. 24-31
  • 91
    • 59649110455 scopus 로고    scopus 로고
    • Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils
    • Meinhardt J, Sachse C, Hortschansky P, Grigorieff N, Fan-drich M (2009) Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J Mol Biol 386, 869-877.
    • (2009) J Mol Biol , vol.386 , pp. 869-877
    • Meinhardt, J.1    Sachse, C.2    Hortschansky, P.3    Grigorieff, N.4    Fan-Drich, M.5
  • 92
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt L, Teng PK, Riek R, Eisenberg D (2010) Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc Natl Acad Sci USA 107, 3487-3492.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 93
    • 0030823158 scopus 로고    scopus 로고
    • Effects of age, sex, and ethnicity on the association between apolipoprotein e genotype and Alzheimer disease. A meta-analysis
    • APOE and Alzheimer Disease Meta Analysis Consortium
    • Farrer LA, Cupples LA, Haines JL, Hyman B, Kukull WA, Mayeux R, Myers RH, Pericak-Vance MA, Risch N, van Dui-jn CM (1997) Effects of age, sex, and ethnicity on the association between apolipoprotein E genotype and Alzheimer disease. A meta-analysis. APOE and Alzheimer Disease Meta Analysis Consortium. JAMA 278, 1349-1356.
    • (1997) JAMA , vol.278 , pp. 1349-1356
    • Farrer, L.A.1    Cupples, L.A.2    Haines, J.L.3    Hyman, B.4    Kukull, W.A.5    Mayeux, R.6    Myers, R.H.7    Pericak-Vance, M.A.8    Risch, N.9    Van Dui-Jn, C.M.10
  • 99
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R, Keller P, Haass C, Thiele C, Simons K (2003) Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 160, 113-123.
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 100
    • 0033968306 scopus 로고    scopus 로고
    • Molecular genetics of Alzheimer's disease
    • St George-Hyslop PH (2000) Molecular genetics of Alzheimer's disease. Biol Psychiatry 47, 183-199.
    • (2000) Biol Psychiatry , vol.47 , pp. 183-199
    • St George-Hyslop, P.H.1
  • 105
    • 0034940552 scopus 로고    scopus 로고
    • Physiological levels of beta-amyloid induce cerebral vessel dysfunction and reduce endothelial nitric oxide production
    • Price JM, Chi X, Hellermann G, Sutton ET (2001) Physiological levels of beta-amyloid induce cerebral vessel dysfunction and reduce endothelial nitric oxide production. Neurol Res 23, 506-512.
    • (2001) Neurol Res , vol.23 , pp. 506-512
    • Price, J.M.1    Chi, X.2    Hellermann, G.3    Sutton, E.T.4
  • 106
    • 0027195933 scopus 로고
    • Seeding one-dimensional crystallization of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT, Jr. (1993) Seeding one-dimensional crystallization of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 107
    • 74649086711 scopus 로고    scopus 로고
    • The recombinant amyloid-beta peptide Abeta1-42 aggregates faster and is more neurotoxic than synthetic Abeta1-42
    • Finder VH, Vodopivec I, Nitsch RM, Glockshuber R (2010) The recombinant amyloid-beta peptide Abeta1-42 aggregates faster and is more neurotoxic than synthetic Abeta1-42. J MolBiol 396, 9-18.
    • (2010) J MolBiol , vol.396 , pp. 9-18
    • Finder, V.H.1    Vodopivec, I.2    Nitsch, R.M.3    Glockshuber, R.4
  • 109
    • 34548615995 scopus 로고    scopus 로고
    • The structural basis of yeast prion strain variants
    • Toyama BH, Kelly MJ, Gross JD, Weissman JS (2007) The structural basis of yeast prion strain variants. Nature 449, 233-237.
    • (2007) Nature , vol.449 , pp. 233-237
    • Toyama, B.H.1    Kelly, M.J.2    Gross, J.D.3    Weissman, J.S.4
  • 111
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi A, Rajendran L (2009) The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64, 783790.
    • (2009) Neuron , vol.64 , pp. 783790
    • Aguzzi, A.1    Rajendran, L.2
  • 112
    • 38549169530 scopus 로고    scopus 로고
    • The two faces of protein misfolding: Gain-and loss-of-function in neurode-generative diseases
    • Winklhofer KF, Tatzelt J, Haass C (2008) The two faces of protein misfolding: gain-and loss-of-function in neurode-generative diseases. EMBOJ 27, 336-349.
    • (2008) EMBOJ , vol.27 , pp. 336-349
    • Winklhofer, K.F.1    Tatzelt, J.2    Haass, C.3
  • 113
    • 68149162581 scopus 로고    scopus 로고
    • Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
    • Tomic JL, Pensalfini A, Head E, Glabe CG (2009) Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction. Neurobiol Dis 35, 352-358.
    • (2009) Neurobiol Dis , vol.35 , pp. 352-358
    • Tomic, J.L.1    Pensalfini, A.2    Head, E.3    Glabe, C.G.4
  • 117
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers -a decade of discovery
    • Walsh DM, Selkoe DJ (2007) A beta oligomers -a decade of discovery. JNeurochem 101, 1172-1184.
    • (2007) JNeurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 120
    • 0025269152 scopus 로고
    • Synapselossinfrontalcortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky ST, ScheffSW(1990)Synapselossinfrontalcortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann Neurol 27, 457-464.
    • (1990) Ann Neurol , vol.27 , pp. 457-464
    • Dekosky, S.T.1    Scheff, S.W.2
  • 122
    • 77049091824 scopus 로고    scopus 로고
    • Alzheimer research series on the default network
    • McCaffrey P, Fagan T, Landhuis E (2010) Alzheimer research series on the default network. J Alzheimers Dis 19, 747-758.
    • (2010) J Alzheimers Dis , vol.19 , pp. 747-758
    • McCaffrey, P.1    Fagan, T.2    Landhuis, E.3
  • 123
    • 34547214510 scopus 로고    scopus 로고
    • Abeta ion channels. Prospects for treating Alzheimer's disease with Abeta channel blockers
    • Arispe N, Diaz JC, Simakova O (2007) Abeta ion channels. Prospects for treating Alzheimer's disease with Abeta channel blockers. Biochim Biophys Acta 1768, 1952-1965.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1952-1965
    • Arispe, N.1    Diaz, J.C.2    Simakova, O.3
  • 124
    • 47749113650 scopus 로고    scopus 로고
    • Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks
    • Kuchibhotla KV, Goldman ST, Lattarulo CR, Wu HY, Hy-man BT, Bacskai BJ (2008) Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks. Neuron 59, 214-225.
    • (2008) Neuron , vol.59 , pp. 214-225
    • Kuchibhotla, K.V.1    Goldman, S.T.2    Lattarulo, C.R.3    Wu, H.Y.4    Hy-Man, B.T.5    Bacskai, B.J.6
  • 125
    • 57449098698 scopus 로고    scopus 로고
    • In situ Abeta pores in AD brain are cylindrical assembly of Abeta protofilaments
    • Inoue S (2008) In situ Abeta pores in AD brain are cylindrical assembly of Abeta protofilaments. Amyloid 15, 223-233.
    • (2008) Amyloid , vol.15 , pp. 223-233
    • Inoue, S.1
  • 127
    • 62649172167 scopus 로고    scopus 로고
    • Small molecule blockers of the Alzheimer Abeta calcium channel potently protect neurons from Abeta cytotoxi-city
    • Diaz JC, Simakova O, Jacobson KA, Arispe N, Pollard HB (2009) Small molecule blockers of the Alzheimer Abeta calcium channel potently protect neurons from Abeta cytotoxi-city. Proc Natl Acad Sci USA 106, 3348-3353.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3348-3353
    • Diaz, J.C.1    Simakova, O.2    Jacobson, K.A.3    Arispe, N.4    Pollard, H.B.5
  • 128
    • 33748767364 scopus 로고    scopus 로고
    • Acceleration of amyloid beta-peptide aggregation by physiological concentrations of calcium
    • Isaacs AM, Senn DB, Yuan M, Shine JP, Yankner BA (2006) Acceleration of amyloid beta-peptide aggregation by physiological concentrations of calcium. J Biol Chem 281, 2791627923.
    • (2006) J Biol Chem , vol.281 , pp. 2791627923
    • Isaacs, A.M.1    Senn, D.B.2    Yuan, M.3    Shine, J.P.4    Yankner, B.A.5
  • 130
    • 67349253085 scopus 로고    scopus 로고
    • Oxidatively modified proteins in Alzheimer's disease (AD), mild cognitive impairment and animal models of AD: Role of Abeta in pathogenesis
    • Sultana R, Perluigi M, Butterfield DA (2009) Oxidatively modified proteins in Alzheimer's disease (AD), mild cognitive impairment and animal models of AD: role of Abeta in pathogenesis. Acta Neuropathol 118, 131-150.
    • (2009) Acta Neuropathol , vol.118 , pp. 131-150
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 131
    • 0028152717 scopus 로고
    • Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease
    • Mecocci P, MacGarvey U, Beal MF (1994) Oxidative damage to mitochondrial DNA is increased in Alzheimer's disease. Ann Neurol 36, 747-751.
    • (1994) Ann Neurol , vol.36 , pp. 747-751
    • Mecocci, P.1    MacGarvey, U.2    Beal, M.F.3
  • 132
    • 0035859221 scopus 로고    scopus 로고
    • Fib-rillar beta-amyloid evokes oxidative damage in a transgenic mouse model ofAlzheimer's disease
    • Matsuoka Y, Picciano M, La Francois J, Duff K (2001) Fib-rillar beta-amyloid evokes oxidative damage in a transgenic mouse model ofAlzheimer's disease. Neuroscience 104, 609613.
    • (2001) Neuroscience , vol.104 , pp. 609613
    • Matsuoka, Y.1    Picciano, M.2    La Francois, J.3    Duff, K.4
  • 133
    • 4544335597 scopus 로고    scopus 로고
    • Mild cognitive impairment as a diagnostic entity
    • Petersen RC (2004) Mild cognitive impairment as a diagnostic entity. J Intern Med 256, 183-194.
    • (2004) J Intern Med , vol.256 , pp. 183-194
    • Petersen, R.C.1
  • 135
    • 0036215321 scopus 로고    scopus 로고
    • Beta-Amyloid peptide induces ultrastructural changes in synaptosomes and potentiates mitochondrial dysfunction in the presence of ryanodine
    • Mungarro-Menchaca X, Ferrera P, Moran J, Arias C (2002) beta-Amyloid peptide induces ultrastructural changes in synaptosomes and potentiates mitochondrial dysfunction in the presence of ryanodine. J Neurosci Res 68, 89-96.
    • (2002) J Neurosci Res , vol.68 , pp. 89-96
    • Mungarro-Menchaca, X.1    Ferrera, P.2    Moran, J.3    Arias, C.4
  • 136
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid beta peptide
    • Smith DG, Cappai R, Barnham KJ (2007) The redox chemistry of the Alzheimer's disease amyloid beta peptide. Biochim Biophys Acta 1768, 1976-1990.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 139
    • 34447564164 scopus 로고    scopus 로고
    • In-tracellular Abeta and cognitive deficits precede beta-amyloid deposition in transgenic arcAbeta mice
    • Knobloch M, Konietzko U, Krebs DC, Nitsch RM (2007) In-tracellular Abeta and cognitive deficits precede beta-amyloid deposition in transgenic arcAbeta mice. Neurobiol Aging 28, 1297-1306.
    • (2007) Neurobiol Aging , vol.28 , pp. 1297-1306
    • Knobloch, M.1    Konietzko, U.2    Krebs, D.C.3    Nitsch, R.M.4
  • 140
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • Walsh DM, Tseng BP, Rydel RE, Podlisny MB, Selkoe DJ (2000) The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry 39, 10831-10839.
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 143
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
    • Hu X, Crick SL, Bu G, Frieden C, Pappu RV, Lee JM (2009) Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide. Proc Natl Acad Sci USA 106, 20324-20329.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.M.6
  • 144
    • 33748871295 scopus 로고    scopus 로고
    • Alzheimer's disease and anaesthesia: Implications for the central cholinergic system
    • Fodale V, Quattrone D, Trecroci C, Caminiti V, Santamaria LB (2006) Alzheimer's disease and anaesthesia: implications for the central cholinergic system. Br J Anaesth 97, 445-452.
    • (2006) Br J Anaesth , vol.97 , pp. 445-452
    • Fodale, V.1    Quattrone, D.2    Trecroci, C.3    Caminiti, V.4    Santamaria, L.B.5
  • 145
    • 0036685522 scopus 로고    scopus 로고
    • Inflammation in neurode-generative disease-a double-edged sword
    • Wyss-Coray T, Mucke L (2002) Inflammation in neurode-generative disease-a double-edged sword. Neuron 35, 419432.
    • (2002) Neuron , vol.35 , pp. 419432
    • Wyss-Coray, T.1    Mucke, L.2
  • 146
    • 77949749564 scopus 로고    scopus 로고
    • Smaller molecular-sized anaesthetics oligomerize Abeta peptide simulating Alzheimer's disease: A relevant issue
    • Mandal PK, Fodale V (2009) Smaller molecular-sized anaesthetics oligomerize Abeta peptide simulating Alzheimer's disease: a relevant issue. Eur J Anaesthesiol 26, 805-806.
    • (2009) Eur J Anaesthesiol , vol.26 , pp. 805-806
    • Mandal, P.K.1    Fodale, V.2
  • 147
    • 58549104149 scopus 로고    scopus 로고
    • Isoflurane and desflurane at clinically relevant concentrations induce amyloid beta-peptide oligomerization: An NMR study
    • Mandal PK, Fodale V (2009) Isoflurane and desflurane at clinically relevant concentrations induce amyloid beta-peptide oligomerization: an NMR study. Biochem Biophys Res Commun 379, 716-720.
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 716-720
    • Mandal, P.K.1    Fodale, V.2
  • 148
    • 54049135146 scopus 로고    scopus 로고
    • Abeta peptide interactions with isoflurane, propofol, thiopental and combined thiopental with halothane: A NMR study
    • Mandal PK, Pettegrew JW (2008) Abeta peptide interactions with isoflurane, propofol, thiopental and combined thiopental with halothane: a NMR study. Biochim Biophys Acta 1778, 2633-2639.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2633-2639
    • Mandal, P.K.1    Pettegrew, J.W.2
  • 149
    • 58149269462 scopus 로고    scopus 로고
    • The common inhalation anesthetic isoflurane induces caspase activation and increases amyloid beta-protein level in vivo
    • Xie Z, Culley DJ, Dong Y, Zhang G, Zhang B, Moir RD, Frosch MP, Crosby G, Tanzi RE (2008) The common inhalation anesthetic isoflurane induces caspase activation and increases amyloid beta-protein level in vivo. Ann Neurol 64, 618-627.
    • (2008) Ann Neurol , vol.64 , pp. 618-627
    • Xie, Z.1    Culley, D.J.2    Dong, Y.3    Zhang, G.4    Zhang, B.5    Moir, R.D.6    Frosch, M.P.7    Crosby, G.8    Tanzi, R.E.9
  • 152
    • 68649110959 scopus 로고    scopus 로고
    • Bridging the gap: From protein misfolding to protein misfolding diseases
    • Luheshi LM, Dobson CM (2009) Bridging the gap: from protein misfolding to protein misfolding diseases. FEBSLett 583, 2581-2586.
    • (2009) FEBSLett , vol.583 , pp. 2581-2586
    • Luheshi, L.M.1    Dobson, C.M.2
  • 153
    • 2942672221 scopus 로고    scopus 로고
    • Rapid photochemical cross-linking -a new tool for studies of metastable, amyloidogenic protein assemblies
    • Bitan G, Teplow DB (2004) Rapid photochemical cross-linking -a new tool for studies of metastable, amyloidogenic protein assemblies. Acc Chem Res 37, 357-364.
    • (2004) Acc Chem Res , vol.37 , pp. 357-364
    • Bitan, G.1    Teplow, D.B.2
  • 155
    • 35648986681 scopus 로고    scopus 로고
    • Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsul-fate
    • Rangachari V, Moore BD, Reed DK, Sonoda LK, Bridges AW, Conboy E, Hartigan D, Rosenberry TL (2007) Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsul-fate. Biochemistry 46, 12451-12462.
    • (2007) Biochemistry , vol.46 , pp. 12451-12462
    • Rangachari, V.1    Moore, B.D.2    Reed, D.K.3    Sonoda, L.K.4    Bridges, A.W.5    Conboy, E.6    Hartigan, D.7    Rosenberry, T.L.8
  • 156
    • 66049093067 scopus 로고    scopus 로고
    • Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation
    • Carulla N, Zhou M, Arimon M, Gairi M, Giralt E, Robin-son CV, Dobson CM (2009) Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. Proc Natl Acad Sci U S A 106, 7828-7833.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7828-7833
    • Carulla, N.1    Zhou, M.2    Arimon, M.3    Gairi, M.4    Giralt, E.5    Robin-Son, C.V.6    Dobson, C.M.7
  • 157
    • 42149130900 scopus 로고    scopus 로고
    • BACE1 structure and function in health and Alzheimer's disease
    • Cole SL, Vassar R (2008) BACE1 structure and function in health and
    • (2008) Curr Alzheimer Res , vol.5 , pp. 100120
    • Cole, S.L.1    Vassar, R.2
  • 158
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring MA, Farris W, Chang AY, Walsh DM, Wu X, Sun X, Frosch MP, Selkoe DJ (2003) Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40, 10871093.
    • (2003) Neuron , vol.40 , pp. 10871093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 160
    • 76849091134 scopus 로고    scopus 로고
    • Can Alzheimer disease be prevented by amyloid-beta immunotherapy?
    • Lemere CA, Masliah E (2010) Can Alzheimer disease be prevented by amyloid-beta immunotherapy? Nat Rev Neurol 6, 108-119.
    • (2010) Nat Rev Neurol , vol.6 , pp. 108-119
    • Lemere, C.A.1    Masliah, E.2


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