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Volumn 131, Issue 1, 2016, Pages 5-25

Propagation of Aß pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; PRION PROTEIN; TAU PROTEIN;

EID: 84952987879     PISSN: 00016322     EISSN: 14320533     Source Type: Journal    
DOI: 10.1007/s00401-015-1516-y     Document Type: Review
Times cited : (61)

References (135)
  • 1
    • 77954554036 scopus 로고    scopus 로고
    • Immunohistochemical visualization of amyloid-beta protein precursor and amyloid-beta in extra- and intracellular compartments in the human brain
    • PID: 20413866
    • Aho L, Pikkarainen M, Hiltunen M, Leinonen V, Alafuzoff I (2010) Immunohistochemical visualization of amyloid-beta protein precursor and amyloid-beta in extra- and intracellular compartments in the human brain. J Alzheimers Dis 20:1015–1028. doi:10.3233/JAD-2010-091681
    • (2010) J Alzheimers Dis , vol.20 , pp. 1015-1028
    • Aho, L.1    Pikkarainen, M.2    Hiltunen, M.3    Leinonen, V.4    Alafuzoff, I.5
  • 2
    • 77953675879 scopus 로고    scopus 로고
    • Probing the biology of Alzheimer’s disease in mice
    • PID: 20547123
    • Ashe KH, Zahs KR (2010) Probing the biology of Alzheimer’s disease in mice. Neuron 66:631–645. doi:10.1016/j.neuron.2010.04.031
    • (2010) Neuron , vol.66 , pp. 631-645
    • Ashe, K.H.1    Zahs, K.R.2
  • 3
    • 33745920161 scopus 로고    scopus 로고
    • Quantifying CNS protein production and clearance rates in humans using in vivo stable isotope labeling, immunoprecipitation, and tandem mass spectrometry
    • PID: 16799555
    • Bateman RJ, Munsell LY, Morris JC, Swarm R, Kevin E, Holtzman DM (2006) Quantifying CNS protein production and clearance rates in humans using in vivo stable isotope labeling, immunoprecipitation, and tandem mass spectrometry. Nat Med 12:856–861. doi:10.1038/nm1438.Quantifying
    • (2006) Nat Med , vol.12 , pp. 856-861
    • Bateman, R.J.1    Munsell, L.Y.2    Morris, J.C.3    Swarm, R.4    Kevin, E.5    Holtzman, D.M.6
  • 4
    • 84858031332 scopus 로고    scopus 로고
    • Striatal amyloid plaque density predicts Braak neurofibrillary stage and clinicopathological Alzheimer’s disease: implications for amyloid imaging
    • PID: 22112552
    • Beach TG, Sue LI, Walker DG, Sabbagh MN, Serrano G, Dugger BN et al (2012) Striatal amyloid plaque density predicts Braak neurofibrillary stage and clinicopathological Alzheimer’s disease: implications for amyloid imaging. J Alzheimers Dis 28:869–876. doi:10.3233/JAD-2011-111340
    • (2012) J Alzheimers Dis , vol.28 , pp. 869-876
    • Beach, T.G.1    Sue, L.I.2    Walker, D.G.3    Sabbagh, M.N.4    Serrano, G.5    Dugger, B.N.6
  • 5
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer’s disease: an emperor in need of clothes
    • PID: 22286176
    • Benilova I, Karran E, De Strooper B (2012) The toxic Aβ oligomer and Alzheimer’s disease: an emperor in need of clothes. Nat Neurosci 15:349–357. doi:10.1038/nn.3028
    • (2012) Nat Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 6
    • 84859584667 scopus 로고    scopus 로고
    • The genetics of Alzheimer’s disease
    • PID: 22482448
    • Bertram L, Tanzi RE (2012) The genetics of Alzheimer’s disease. Prog Mol Biol Transl Sci 107:79–100. doi:10.1016/B978-0-12-385883-2.00008-4
    • (2012) Prog Mol Biol Transl Sci , vol.107 , pp. 79-100
    • Bertram, L.1    Tanzi, R.E.2
  • 7
    • 38349013141 scopus 로고    scopus 로고
    • Induction of tau pathology by intracerebral infusion of amyloid-beta-containing brain extract and by amyloid-beta deposition in APP × Tau transgenic mice
    • PID: 18055549
    • Bolmont T, Clavaguera F, Meyer-Luehmann M, Herzig MC, Radde R, Staufenbiel M et al (2007) Induction of tau pathology by intracerebral infusion of amyloid-beta-containing brain extract and by amyloid-beta deposition in APP × Tau transgenic mice. Am J Pathol 171:2012–2020. doi:10.2353/ajpath.2007.070403
    • (2007) Am J Pathol , vol.171 , pp. 2012-2020
    • Bolmont, T.1    Clavaguera, F.2    Meyer-Luehmann, M.3    Herzig, M.C.4    Radde, R.5    Staufenbiel, M.6
  • 8
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • PID: 1759558
    • Braak H, Braak E (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82:239–259
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 10
    • 79451471618 scopus 로고    scopus 로고
    • The pathological process underlying Alzheimer’s disease in individuals under thirty
    • PID: 21170538
    • Braak H, Del Tredici K (2011) The pathological process underlying Alzheimer’s disease in individuals under thirty. Acta Neuropathol 121:171–181. doi:10.1007/s00401-010-0789-4
    • (2011) Acta Neuropathol , vol.121 , pp. 171-181
    • Braak, H.1    Del Tredici, K.2
  • 11
    • 84881085093 scopus 로고    scopus 로고
    • Amyloid-β may be released from non-junctional varicosities of axons generated from abnormal tau-containing brainstem nuclei in sporadic Alzheimer’s disease: a hypothesis
    • PID: 23824268
    • Braak H, Del Tredici K (2013) Amyloid-β may be released from non-junctional varicosities of axons generated from abnormal tau-containing brainstem nuclei in sporadic Alzheimer’s disease: a hypothesis. Acta Neuropathol 126:303–306. doi:10.1007/s00401-013-1153-2
    • (2013) Acta Neuropathol , vol.126 , pp. 303-306
    • Braak, H.1    Del Tredici, K.2
  • 12
    • 84952898119 scopus 로고    scopus 로고
    • The preclinical phase of the pathological process underlying sporadic Alzheimer’s disease
    • PID: 26283673
    • Braak H, Del Tredici K (2015) The preclinical phase of the pathological process underlying sporadic Alzheimer’s disease. Brain 138:2814–2833. doi:10.1093/brain/awv236
    • (2015) Brain , vol.138 , pp. 2814-2833
    • Braak, H.1    Del Tredici, K.2
  • 13
    • 84922785301 scopus 로고    scopus 로고
    • Human secreted tau increases amyloid-beta production
    • PID: 25442111
    • Bright J, Hussain S, Dang V, Wright S, Cooper B, Byun T et al (2015) Human secreted tau increases amyloid-beta production. Neurobiol Aging 36:693–709. doi:10.1016/j.neurobiolaging.2014.09.007
    • (2015) Neurobiol Aging , vol.36 , pp. 693-709
    • Bright, J.1    Hussain, S.2    Dang, V.3    Wright, S.4    Cooper, B.5    Byun, T.6
  • 15
    • 84882240842 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy, prion angiopathy, CADASIL and the spectrum of protein elimination failure angiopathies (PEFA) in neurodegenerative disease with a focus on therapy
    • PID: 23489283
    • Carare RO, Hawkes CA, Jeffrey M, Kalaria RN, Weller RO (2013) Cerebral amyloid angiopathy, prion angiopathy, CADASIL and the spectrum of protein elimination failure angiopathies (PEFA) in neurodegenerative disease with a focus on therapy. Neuropathol Appl Neurobiol 39:593–611. doi:10.1111/nan.12042
    • (2013) Neuropathol Appl Neurobiol , vol.39 , pp. 593-611
    • Carare, R.O.1    Hawkes, C.A.2    Jeffrey, M.3    Kalaria, R.N.4    Weller, R.O.5
  • 16
    • 84886179076 scopus 로고    scopus 로고
    • Modeling Alzheimer’s disease in transgenic rats
    • PID: 24161192
    • Do Carmo S, Cuello AC (2013) Modeling Alzheimer’s disease in transgenic rats. Mol Neurodegener 8:37. doi:10.1186/1750-1326-8-37
    • (2013) Mol Neurodegener , vol.8 , pp. 37
    • Do Carmo, S.1    Cuello, A.C.2
  • 17
    • 84964848239 scopus 로고    scopus 로고
    • The genetic landscape of Alzheimer disease: clinical implications and perspectives
    • PID: 26312828
    • van Cauwenberghe C, Van Broeckhoven C, Sleegers K (2015) The genetic landscape of Alzheimer disease: clinical implications and perspectives. Genet Med. doi:10.1038/gim.2015.117
    • (2015) Genet Med
    • van Cauwenberghe, C.1    Van Broeckhoven, C.2    Sleegers, K.3
  • 19
    • 34548258322 scopus 로고    scopus 로고
    • Accelerating amyloid-beta fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models
    • PID: 17548355
    • Cheng IH, Scearce-Levie K, Legleiter J, Palop JJ, Gerstein H, Bien-Ly N et al (2007) Accelerating amyloid-beta fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models. J Biol Chem 282:23818–23828. doi:10.1074/jbc.M701078200
    • (2007) J Biol Chem , vol.282 , pp. 23818-23828
    • Cheng, I.H.1    Scearce-Levie, K.2    Legleiter, J.3    Palop, J.J.4    Gerstein, H.5    Bien-Ly, N.6
  • 20
    • 84934444350 scopus 로고    scopus 로고
    • Selecting a mouse model of Alzheimer’s disease
    • PID: 20967591
    • Chin J (2011) Selecting a mouse model of Alzheimer’s disease. Methods Mol Biol 670:169–189. doi:10.1007/978-1-60761-744-0_13
    • (2011) Methods Mol Biol , vol.670 , pp. 169-189
    • Chin, J.1
  • 21
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • PID: 16756495
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333–366. doi:10.1146/annurev.biochem.75.101304.123901
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 22
    • 0141529993 scopus 로고    scopus 로고
    • In vivo assessment of brain interstitial fluid with microdialysis reveals plaque-associated changes in amyloid-beta metabolism and half-life
    • PID: 14523085
    • Cirrito JR, May PC, O’Dell M, Taylor JW, Parsadanian M, Cramer JW et al (2003) In vivo assessment of brain interstitial fluid with microdialysis reveals plaque-associated changes in amyloid-beta metabolism and half-life. J Neurosci 23:8844–8853. doi:10.1186/1750-1326-8-13
    • (2003) J Neurosci , vol.23 , pp. 8844-8853
    • Cirrito, J.R.1    May, P.C.2    O’Dell, M.3    Taylor, J.W.4    Parsadanian, M.5    Cramer, J.W.6
  • 23
    • 0027310868 scopus 로고
    • The distribution of amyloid plaques in the cerebellum and brain stem in Down’s syndrome and Alzheimer’s disease: a light microscopical analysis
    • PID: 8493862
    • Cole G, Neal JW, Singhrao SK, Jasani B, Newman GR (1993) The distribution of amyloid plaques in the cerebellum and brain stem in Down’s syndrome and Alzheimer’s disease: a light microscopical analysis. Acta Neuropathol 85:542–552. doi:10.1007/BF00230495
    • (1993) Acta Neuropathol , vol.85 , pp. 542-552
    • Cole, G.1    Neal, J.W.2    Singhrao, S.K.3    Jasani, B.4    Newman, G.R.5
  • 24
    • 0141455115 scopus 로고    scopus 로고
    • Analysis of the generation and segregation of propagons: entities that propagate the [PSI+] prion in yeast
    • PID: 14504215
    • Cox B, Ness F, Tuite M (2003) Analysis of the generation and segregation of propagons: entities that propagate the [PSI+] prion in yeast. Genetics 165:23–33
    • (2003) Genetics , vol.165 , pp. 23-33
    • Cox, B.1    Ness, F.2    Tuite, M.3
  • 25
    • 84878374182 scopus 로고    scopus 로고
    • Electrophysiological changes precede morphological changes to frontal cortical pyramidal neurons in the rTg4510 mouse model of progressive tauopathy
    • PID: 22976049
    • Crimins JL, Rocher AB, Luebke JI (2012) Electrophysiological changes precede morphological changes to frontal cortical pyramidal neurons in the rTg4510 mouse model of progressive tauopathy. Acta Neuropathol 124:777–795. doi:10.1007/s00401-012-1038-9
    • (2012) Acta Neuropathol , vol.124 , pp. 777-795
    • Crimins, J.L.1    Rocher, A.B.2    Luebke, J.I.3
  • 26
    • 0029835167 scopus 로고    scopus 로고
    • Diffuse plaques contain C-terminal A beta 42 and not A beta 40: evidence from cats and dogs
    • PID: 8832640
    • Cummings BJ, Satou T, Head E, Milgram NW, Cole GM, Savage MJ et al (1996) Diffuse plaques contain C-terminal A beta 42 and not A beta 40: evidence from cats and dogs. Neurobiol Aging 17:653–659
    • (1996) Neurobiol Aging , vol.17 , pp. 653-659
    • Cummings, B.J.1    Satou, T.2    Head, E.3    Milgram, N.W.4    Cole, G.M.5    Savage, M.J.6
  • 27
    • 0026065020 scopus 로고
    • Subtypes and differential laminar distributions of βA4 deposits in Alzheimer’s disease: relationship with the intellectual status of 26 cases
    • PID: 1711758
    • Delaère P, Duyckaerts C, He Y, Pierre F, Hauw JJ (1991) Subtypes and differential laminar distributions of βA4 deposits in Alzheimer’s disease: relationship with the intellectual status of 26 cases. Acta Neuropathol 81:328–335
    • (1991) Acta Neuropathol , vol.81 , pp. 328-335
    • Delaère, P.1    Duyckaerts, C.2    He, Y.3    Pierre, F.4    Hauw, J.J.5
  • 28
    • 0025289562 scopus 로고
    • Large amounts of neocortical beta A4 deposits without neuritic plaques nor tangles in a psychometrically assessed, non-demented person
    • PID: 2259457
    • Delaère P, Duyckaerts C, Masters C, Beyreuther K, Piette F, Hauw JJ (1990) Large amounts of neocortical beta A4 deposits without neuritic plaques nor tangles in a psychometrically assessed, non-demented person. Neurosci Lett 116:87–93
    • (1990) Neurosci Lett , vol.116 , pp. 87-93
    • Delaère, P.1    Duyckaerts, C.2    Masters, C.3    Beyreuther, K.4    Piette, F.5    Hauw, J.J.6
  • 29
    • 0026512066 scopus 로고
    • Identification of normal and pathological aging in prospectively studied nondemented elderly humans
    • PID: 1311804
    • Dickson DW, Crystal HA, Mattiace LA, Masur DM, Blau AD, Davies P et al (1992) Identification of normal and pathological aging in prospectively studied nondemented elderly humans. Neurobiol Aging 13:179–189
    • (1992) Neurobiol Aging , vol.13 , pp. 179-189
    • Dickson, D.W.1    Crystal, H.A.2    Mattiace, L.A.3    Masur, D.M.4    Blau, A.D.5    Davies, P.6
  • 30
    • 0031891362 scopus 로고    scopus 로고
    • Laminar spongiosis of the dentate gyrus: a sign of disconnection, present in cases of severe Alzheimer’s disease
    • PID: 9560020
    • Duyckaerts C, Colle M-A, Seilhean D, Hauw J-J (1998) Laminar spongiosis of the dentate gyrus: a sign of disconnection, present in cases of severe Alzheimer’s disease. Acta Neuropathol 95:413–420. doi:10.1007/s004010050818
    • (1998) Acta Neuropathol , vol.95 , pp. 413-420
    • Duyckaerts, C.1    Colle, M.-A.2    Seilhean, D.3    Hauw, J.-J.4
  • 31
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • PID: 19381658
    • Duyckaerts C, Delatour B, Potier M-C (2009) Classification and basic pathology of Alzheimer disease. Acta Neuropathol 118:5–36. doi:10.1007/s00401-009-0532-1
    • (2009) Acta Neuropathol , vol.118 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.-C.3
  • 32
    • 0030823304 scopus 로고    scopus 로고
    • Prevalence, incidence and duration of Braak’s stages in the general population: can we know?
    • PID: 9380250
    • Duyckaerts C, Hauw J-J (1997) Prevalence, incidence and duration of Braak’s stages in the general population: can we know? Neurobiol Aging 18:362–369
    • (1997) Neurobiol Aging , vol.18 , pp. 362-369
    • Duyckaerts, C.1    Hauw, J.-J.2
  • 33
    • 0030902162 scopus 로고    scopus 로고
    • Dissociation of Alzheimer type pathology in a disconnected piece of cortex
    • PID: 9144589
    • Duyckaerts C, Uchihara T, Seilhean D, He Y, Hauw JJ (1997) Dissociation of Alzheimer type pathology in a disconnected piece of cortex. Acta Neuropathol 93:501–507
    • (1997) Acta Neuropathol , vol.93 , pp. 501-507
    • Duyckaerts, C.1    Uchihara, T.2    Seilhean, D.3    He, Y.4    Hauw, J.J.5
  • 34
    • 69149098707 scopus 로고    scopus 로고
    • Induction of cerebral beta-amyloidosis: intracerebral versus systemic Abeta inoculation
    • PID: 19622727
    • Eisele YS, Bolmont T, Heikenwalder M, Langer F, Jacobson LH, Yan Z-XX et al (2009) Induction of cerebral beta-amyloidosis: intracerebral versus systemic Abeta inoculation. Proc Natl Acad Sci USA 106:12926–12931. doi:10.1073/pnas.0903200106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12926-12931
    • Eisele, Y.S.1    Bolmont, T.2    Heikenwalder, M.3    Langer, F.4    Jacobson, L.H.5    Yan, Z.-X.X.6
  • 35
    • 84905053905 scopus 로고    scopus 로고
    • Multiple factors contribute to the peripheral induction of cerebral β-amyloidosis
    • PID: 25080588
    • Eisele YS, Fritschi SK, Hamaguchi T, Obermüller U, Füger P, Skodras A et al (2014) Multiple factors contribute to the peripheral induction of cerebral β-amyloidosis. J Neurosci 34:10264–10273. doi:10.1523/JNEUROSCI.1608-14.2014
    • (2014) J Neurosci , vol.34 , pp. 10264-10273
    • Eisele, Y.S.1    Fritschi, S.K.2    Hamaguchi, T.3    Obermüller, U.4    Füger, P.5    Skodras, A.6
  • 37
    • 78149392229 scopus 로고    scopus 로고
    • Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis
    • PID: 20966215
    • Eisele YS, Obermüller U, Heilbronner G, Baumann F, Kaeser SA, Wolburg H et al (2010) Peripherally applied Abeta-containing inoculates induce cerebral beta-amyloidosis. Science 330:980–982. doi:10.1126/science.1194516
    • (2010) Science , vol.330 , pp. 980-982
    • Eisele, Y.S.1    Obermüller, U.2    Heilbronner, G.3    Baumann, F.4    Kaeser, S.A.5    Wolburg, H.6
  • 38
    • 84929275414 scopus 로고    scopus 로고
    • Acute amnestic encephalopathy in amyloid-ß oligomers injected mice is due to their widespread diffusion in vivo
    • PID: 25862419
    • Epelbaum S, Youssef I, Lacor P, Chaurand P, Duplus E, Brugg B et al (2015) Acute amnestic encephalopathy in amyloid-ß oligomers injected mice is due to their widespread diffusion in vivo. Neurobiol Aging 36:2043–2052. doi:10.1016/j.neurobiolaging.2015.03.005
    • (2015) Neurobiol Aging , vol.36 , pp. 2043-2052
    • Epelbaum, S.1    Youssef, I.2    Lacor, P.3    Chaurand, P.4    Duplus, E.5    Brugg, B.6
  • 40
    • 84930444822 scopus 로고    scopus 로고
    • Highly potent soluble amyloid-beta seeds in human Alzheimer brain but not cerebrospinal fluid
    • PID: 25212850
    • Fritschi SK, Langer F, Kaeser SA, Maia LF, Portelius E, Pinotsi D et al (2014) Highly potent soluble amyloid-beta seeds in human Alzheimer brain but not cerebrospinal fluid. Brain 137:2909–2915. doi:10.1093/brain/awu255
    • (2014) Brain , vol.137 , pp. 2909-2915
    • Fritschi, S.K.1    Langer, F.2    Kaeser, S.A.3    Maia, L.F.4    Portelius, E.5    Pinotsi, D.6
  • 41
    • 84921298275 scopus 로고    scopus 로고
    • Lesion of the subiculum reduces the spread of amyloid beta pathology to interconnected brain regions in a mouse model of Alzheimer’s disease
    • PID: 24517102
    • George S, Ronnback A, Gouras GK, Petit GH, Grueninger F, Winblad B et al (2014) Lesion of the subiculum reduces the spread of amyloid beta pathology to interconnected brain regions in a mouse model of Alzheimer’s disease. Acta Neuropathol Commun 2:17. doi:10.1186/2051-5960-2-17
    • (2014) Acta Neuropathol Commun , vol.2 , pp. 17
    • George, S.1    Ronnback, A.2    Gouras, G.K.3    Petit, G.H.4    Grueninger, F.5    Winblad, B.6
  • 42
    • 0023247155 scopus 로고
    • Alzheimer’s disease: neurofibrillary changes in nuclei that project to the cerebral cortex
    • PID: 3302759
    • German DC, White CL, Sparkman DR (1987) Alzheimer’s disease: neurofibrillary changes in nuclei that project to the cerebral cortex. Neuroscience 21:305–312
    • (1987) Neuroscience , vol.21 , pp. 305-312
    • German, D.C.1    White, C.L.2    Sparkman, D.R.3
  • 43
    • 84923043538 scopus 로고    scopus 로고
    • Invited review: frontotemporal dementia caused by microtubule-associated protein tau gene (MAPT) mutations: a chameleon for neuropathology and neuroimaging
    • PID: 25556536
    • Ghetti B, Oblak AL, Boeve BF, Johnson KA, Dickerson BC, Goedert M (2015) Invited review: frontotemporal dementia caused by microtubule-associated protein tau gene (MAPT) mutations: a chameleon for neuropathology and neuroimaging. Neuropathol Appl Neurobiol 41:24–46. doi:10.1111/nan.12213
    • (2015) Neuropathol Appl Neurobiol , vol.41 , pp. 24-46
    • Ghetti, B.1    Oblak, A.L.2    Boeve, B.F.3    Johnson, K.A.4    Dickerson, B.C.5    Goedert, M.6
  • 44
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J, Chen F, van Dorpe J, Nitsch RM, Götz J, Chen F et al (2001) Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils. Science (80-) 293:1491–1495. doi: 10.1126/science.1062097
    • (2001) Science (80-) , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4    Götz, J.5    Chen, F.6
  • 45
    • 84869506753 scopus 로고    scopus 로고
    • Critical role of intraneuronal Aβ in Alzheimer’s disease: technical challenges in studying intracellular Aβ
    • PID: 22727791
    • Gouras GK, Willén K, Tampellini D (2012) Critical role of intraneuronal Aβ in Alzheimer’s disease: technical challenges in studying intracellular Aβ. Life Sci 91:1153–1158. doi:10.1016/j.lfs.2012.06.004
    • (2012) Life Sci , vol.91 , pp. 1153-1158
    • Gouras, G.K.1    Willén, K.2    Tampellini, D.3
  • 46
    • 67649945522 scopus 로고    scopus 로고
    • The dorsal raphe nucleus shows phospho-tau neurofibrillary changes before the transentorhinal region in Alzheimer’s disease. A precocious onset?
    • PID: 19508444
    • Grinberg LT, Rüb U, Ferretti REL, Nitrini R, Farfel JM, Polichiso L et al (2009) The dorsal raphe nucleus shows phospho-tau neurofibrillary changes before the transentorhinal region in Alzheimer’s disease. A precocious onset? Neuropathol Appl Neurobiol 35:406–416. doi:10.1111/j.1365-2990.2009.00997.x
    • (2009) Neuropathol Appl Neurobiol , vol.35 , pp. 406-416
    • Grinberg, L.T.1    Rüb, U.2    Ferretti, R.E.L.3    Nitrini, R.4    Farfel, J.M.5    Polichiso, L.6
  • 48
    • 84857034922 scopus 로고    scopus 로고
    • The presence of Abeta seeds, and not age per se, is critical to the initiation of Abeta deposition in the brain
    • PID: 22101366
    • Hamaguchi T, Eisele YS, Varvel NH, Lamb BT, Walker LC, Jucker M (2012) The presence of Abeta seeds, and not age per se, is critical to the initiation of Abeta deposition in the brain. Acta Neuropathol 123:31–37. doi:10.1007/s00401-011-0912-1
    • (2012) Acta Neuropathol , vol.123 , pp. 31-37
    • Hamaguchi, T.1    Eisele, Y.S.2    Varvel, N.H.3    Lamb, B.T.4    Walker, L.C.5    Jucker, M.6
  • 49
    • 0026597063 scopus 로고
    • Alzheimer’ s Disease: The Amyloid Cascade Hypothesis
    • Hardy JA, Higgins GA (1992) Alzheimer’ s Disease: The Amyloid Cascade Hypothesis. Science (80-) 256:184–185
    • (1992) Science (80-) , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 50
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer’s disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • PID: 9242912
    • Harper JD, Lansbury PT Jr (1997) Models of amyloid seeding in Alzheimer’s disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66:385–407. doi:10.1146/annurev.biochem.66.1.385
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 51
    • 84887031600 scopus 로고    scopus 로고
    • Seeded strain-like transmission of β-amyloid morphotypes in APP transgenic mice
    • PID: 23999102
    • Heilbronner G, Eisele YS, Langer F, Kaeser SA, Novotny R, Nagarathinam A et al (2013) Seeded strain-like transmission of β-amyloid morphotypes in APP transgenic mice. EMBO Rep 14:1017–1022. doi:10.1038/embor.2013.137
    • (2013) EMBO Rep , vol.14 , pp. 1017-1022
    • Heilbronner, G.1    Eisele, Y.S.2    Langer, F.3    Kaeser, S.A.4    Novotny, R.5    Nagarathinam, A.6
  • 52
    • 84885451692 scopus 로고    scopus 로고
    • Increased misfolding and truncation of tau in APP/PS1/tau transgenic mice compared to mutant tau mice
    • PID: 24076100
    • Héraud C, Goufak D, Ando K, Leroy K, Suain V, Yilmaz Z et al (2013) Increased misfolding and truncation of tau in APP/PS1/tau transgenic mice compared to mutant tau mice. Neurobiol Dis 62:100–112. doi:10.1016/j.nbd.2013.09.010
    • (2013) Neurobiol Dis , vol.62 , pp. 100-112
    • Héraud, C.1    Goufak, D.2    Ando, K.3    Leroy, K.4    Suain, V.5    Yilmaz, Z.6
  • 53
    • 33646560610 scopus 로고    scopus 로고
    • Mechanism of cerebral beta-amyloid angiopathy: murine and cellular models
    • PID: 16612981
    • Herzig MC, Van Nostrand WE, Jucker M (2006) Mechanism of cerebral beta-amyloid angiopathy: murine and cellular models. Brain Pathol 16:40–54
    • (2006) Brain Pathol , vol.16 , pp. 40-54
    • Herzig, M.C.1    Van Nostrand, W.E.2    Jucker, M.3
  • 54
    • 4344648449 scopus 로고    scopus 로고
    • Abeta is targeted to the vasculature in a mouse model of hereditary cerebral hemorrhage with amyloidosis
    • PID: 15311281
    • Herzig MC, Winkler DT, Burgermeister P, Pfeifer M, Kohler E, Schmidt SD et al (2004) Abeta is targeted to the vasculature in a mouse model of hereditary cerebral hemorrhage with amyloidosis. Nat Neurosci 7:954–960. doi:10.1038/nn1302
    • (2004) Nat Neurosci , vol.7 , pp. 954-960
    • Herzig, M.C.1    Winkler, D.T.2    Burgermeister, P.3    Pfeifer, M.4    Kohler, E.5    Schmidt, S.D.6
  • 55
    • 84857126830 scopus 로고    scopus 로고
    • Nonhuman primate models of Alzheimer-like cerebral proteopathy
    • PID: 22288403
    • Heuer E, Rosen RF, Cintron A, Walker LC (2012) Nonhuman primate models of Alzheimer-like cerebral proteopathy. Curr Pharm Des 18:1159–1169
    • (2012) Curr Pharm Des , vol.18 , pp. 1159-1169
    • Heuer, E.1    Rosen, R.F.2    Cintron, A.3    Walker, L.C.4
  • 56
    • 84860764162 scopus 로고    scopus 로고
    • Role of common and rare APP DNA sequence variants in Alzheimer disease
    • PID: 22491860
    • Hooli BV, Mohapatra G, Mattheisen M, Parrado AR, Roehr JT, Shen Y et al (2012) Role of common and rare APP DNA sequence variants in Alzheimer disease. Neurology 78:1250–1257. doi:10.1212/WNL.0b013e3182515972
    • (2012) Neurology , vol.78 , pp. 1250-1257
    • Hooli, B.V.1    Mohapatra, G.2    Mattheisen, M.3    Parrado, A.R.4    Roehr, J.T.5    Shen, Y.6
  • 57
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice
    • Hsiao K, Chapman P, Nilsen S, Eckman C, Harigaya Y, Younkin S et al (1996) Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science (80-) 274:99–102
    • (1996) Science (80-) , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6
  • 58
    • 0024320230 scopus 로고
    • A4 amyloid protein immunoreactivity is present in Alzheimer’s disease neurofibrillary tangles
    • PID: 2671814
    • Hyman BT, Van Hoesen GW, Beyreuther K, Masters CL (1989) A4 amyloid protein immunoreactivity is present in Alzheimer’s disease neurofibrillary tangles. Neurosci Lett 101:352–355
    • (1989) Neurosci Lett , vol.101 , pp. 352-355
    • Hyman, B.T.1    Van Hoesen, G.W.2    Beyreuther, K.3    Masters, C.L.4
  • 59
    • 0021145680 scopus 로고
    • Alzheimer’s disease: cell-specific pathology isolates the hippocampal formation
    • Hyman BT, Van Hoesen GW, Damasio AR, Barnes CL (1984) Alzheimer’s disease: cell-specific pathology isolates the hippocampal formation. Science (80-) 225:1168–70
    • (1984) Science (80-) , vol.225 , pp. 1168-1170
    • Hyman, B.T.1    Van Hoesen, G.W.2    Damasio, A.R.3    Barnes, C.L.4
  • 60
    • 84856002055 scopus 로고    scopus 로고
    • National Institute on Aging-Alzheimer’s Association guidelines for the neuropathologic assessment of Alzheimer’s disease
    • PID: 22265587
    • Hyman BT, Phelps CH, Beach TG, Bigio EH, Cairns NJ, Carrillo MC et al (2012) National Institute on Aging-Alzheimer’s Association guidelines for the neuropathologic assessment of Alzheimer’s disease. Alzheimers Dement 8:1–13. doi:10.1016/j.jalz.2011.10.007
    • (2012) Alzheimers Dement , vol.8 , pp. 1-13
    • Hyman, B.T.1    Phelps, C.H.2    Beach, T.G.3    Bigio, E.H.4    Cairns, N.J.5    Carrillo, M.C.6
  • 61
    • 84876137748 scopus 로고    scopus 로고
    • Evaluation of potential infectivity of Alzheimer and Parkinson disease proteins in recipients of cadaver-derived human growth hormone
    • PID: 23380910
    • Irwin DJ, Abrams JY, Schonberger LB, Leschek W, Mills JL, Lee VM et al (2013) Evaluation of potential infectivity of Alzheimer and Parkinson disease proteins in recipients of cadaver-derived human growth hormone. JAMA Neurol 70:462–468. doi:10.1001/jamaneurol.2013.1933.Evaluation
    • (2013) JAMA Neurol , vol.70 , pp. 462-468
    • Irwin, D.J.1    Abrams, J.Y.2    Schonberger, L.B.3    Leschek, W.4    Mills, J.L.5    Lee, V.M.6
  • 62
    • 84888177803 scopus 로고    scopus 로고
    • Cerebral amyloid PET imaging in Alzheimer’ s disease
    • PID: 24100688
    • Jack CR, Jorge J, Vladimir RB (2013) Cerebral amyloid PET imaging in Alzheimer’ s disease. Acta Neuropathol 126:643–657. doi: 10.1007/s00401-013-1185-7
    • (2013) Acta Neuropathol , vol.126 , pp. 643-657
    • Jack, C.R.1    Jorge, J.2    Vladimir, R.B.3
  • 63
    • 84937529452 scopus 로고    scopus 로고
    • Prevalence of cerebral amyloid pathology in persons without dementia: a meta-analysis
    • PID: 25988462
    • Jansen WJ, Ossenkoppele R, Knol DL, Tijms BM, Scheltens P, Verhey FR et al (2015) Prevalence of cerebral amyloid pathology in persons without dementia: a meta-analysis. JAMA 313:1924–1938. doi:10.1001/jama.2015.4668
    • (2015) JAMA , vol.313 , pp. 1924-1938
    • Jansen, W.J.1    Ossenkoppele, R.2    Knol, D.L.3    Tijms, B.M.4    Scheltens, P.5    Verhey, F.R.6
  • 64
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer’s disease
    • PID: 8490014
    • Jarrett JT, Berger EP, Lansbury PT (1993) The carboxy terminus of the beta-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer’s disease. Biochemistry 32:4693–4697. doi:10.1021/bi00069a001
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 65
    • 0027195933 scopus 로고
    • Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer’s disease and scrapie?
    • PID: 8513491
    • Jarrett JT, Lansbury PT (1993) Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer’s disease and scrapie? Cell 73:1055–1058. doi:10.1016/0092-8674(93)90635-4
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 66
    • 84941198850 scopus 로고    scopus 로고
    • Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy
    • PID: 26354483
    • Jaunmuktane Z, Mead S, Ellis M, Wadsworth JDF, Nicoll AJ, Kenny J et al (2015) Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy. Nature 525:247–250. doi:10.1038/nature15369
    • (2015) Nature , vol.525 , pp. 247-250
    • Jaunmuktane, Z.1    Mead, S.2    Ellis, M.3    Wadsworth, J.D.F.4    Nicoll, A.J.5    Kenny, J.6
  • 67
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • PID: 22028219
    • Jucker M, Walker LC (2011) Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann Neurol 70:532–540. doi:10.1002/ana.22615
    • (2011) Ann Neurol , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 68
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of beta -amyloid by intracerebral infusion of Alzheimer brain extracts in beta-amyloid precursor protein transgenic mice
    • PID: 10804202
    • Kane MD, Lipinski WJ, Callahan MJ, Bian F, Durham RA, Schwarz RD et al (2000) Evidence for seeding of beta -amyloid by intracerebral infusion of Alzheimer brain extracts in beta-amyloid precursor protein transgenic mice. J Neurosci 20:3606–3611
    • (2000) J Neurosci , vol.20 , pp. 3606-3611
    • Kane, M.D.1    Lipinski, W.J.2    Callahan, M.J.3    Bian, F.4    Durham, R.A.5    Schwarz, R.D.6
  • 69
    • 84938490181 scopus 로고    scopus 로고
    • C-terminally truncated forms of tau, but not full-length tau or its C-terminal fragments, are released from neurons independently of cell death
    • PID: 26224867
    • Kanmert D, Cantlon A, Muratore CR, Jin M, O’Malley TT, Lee G et al (2015) C-terminally truncated forms of tau, but not full-length tau or its C-terminal fragments, are released from neurons independently of cell death. J Neurosci 35:10851–10865. doi:10.1523/JNEUROSCI.0387-15.2015
    • (2015) J Neurosci , vol.35 , pp. 10851-10865
    • Kanmert, D.1    Cantlon, A.2    Muratore, C.R.3    Jin, M.4    O’Malley, T.T.5    Lee, G.6
  • 71
    • 84923006997 scopus 로고    scopus 로고
    • Invited review: neuropathology of tauopathies: principles and practice
    • PID: 25495175
    • Kovacs GG (2015) Invited review: neuropathology of tauopathies: principles and practice. Neuropathol Appl Neurobiol 41:3–23. doi:10.1111/nan.12208
    • (2015) Neuropathol Appl Neurobiol , vol.41 , pp. 3-23
    • Kovacs, G.G.1
  • 72
  • 74
    • 0027511389 scopus 로고
    • The role of connectivity in Alzheimer’s disease pathogenesis. A review and model system
    • PID: 8450928
    • De Lacoste MC, White CL (1993) The role of connectivity in Alzheimer’s disease pathogenesis. A review and model system. Neurobiol Aging 14:1–16
    • (1993) Neurobiol Aging , vol.14 , pp. 1-16
    • De Lacoste, M.C.1    White, C.L.2
  • 75
    • 9844219728 scopus 로고    scopus 로고
    • Altered metabolism of familial Alzheimer’s disease-linked amyloid precursor protein variants in yeast artificial chromosome transgenic mice
    • PID: 9285791
    • Lamb BT, Call LM, Slunt HH, Bardel KA, Lawler AM, Eckman CB et al (1997) Altered metabolism of familial Alzheimer’s disease-linked amyloid precursor protein variants in yeast artificial chromosome transgenic mice. Hum Mol Genet 6:1535–1541
    • (1997) Hum Mol Genet , vol.6 , pp. 1535-1541
    • Lamb, B.T.1    Call, L.M.2    Slunt, H.H.3    Bardel, K.A.4    Lawler, A.M.5    Eckman, C.B.6
  • 76
    • 80054010366 scopus 로고    scopus 로고
    • Soluble Abeta seeds are potent inducers of cerebral beta-amyloid deposition
    • PID: 21994365
    • Langer F, Eisele YS, Fritschi SK, Staufenbiel M, Walker LC, Jucker M (2011) Soluble Abeta seeds are potent inducers of cerebral beta-amyloid deposition. J Neurosci 31:14488–14495. doi:10.1523/JNEUROSCI.3088-11.2011
    • (2011) J Neurosci , vol.31 , pp. 14488-14495
    • Langer, F.1    Eisele, Y.S.2    Fritschi, S.K.3    Staufenbiel, M.4    Walker, L.C.5    Jucker, M.6
  • 77
    • 0034763328 scopus 로고    scopus 로고
    • Cotton wool plaques in non-familial late-onset Alzheimer disease
    • PID: 11706935
    • Le TV, Crook R, Hardy J, Dickson DW (2001) Cotton wool plaques in non-familial late-onset Alzheimer disease. J Neuropathol Exp Neurol 60:1051–1061
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 1051-1061
    • Le, T.V.1    Crook, R.2    Hardy, J.3    Dickson, D.W.4
  • 78
    • 23844446427 scopus 로고    scopus 로고
    • The striatofugal fiber system in primates: a reevaluation of its organization based on single-axon tracing studies
    • PID: 16087877
    • Lévesque M, Parent A (2005) The striatofugal fiber system in primates: a reevaluation of its organization based on single-axon tracing studies. Proc Natl Acad Sci USA 102:11888–11893. doi:10.1073/pnas.0502710102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11888-11893
    • Lévesque, M.1    Parent, A.2
  • 79
    • 84952976186 scopus 로고    scopus 로고
    • Propagation of tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies
    • Lewis J, Dickson DW (2016) Propagation of tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies. Acta Neuropathol. doi:10.1007/s00401-015-1507-z
    • (2016) Acta Neuropathol
    • Lewis, J.1    Dickson, D.W.2
  • 80
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • PID: 7991613
    • Lorenzo A, Yankner BA (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc Natl Acad Sci USA 91:12243–12247
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 81
    • 84880527880 scopus 로고    scopus 로고
    • Changes in amyloid-beta and Tau in the cerebrospinal fluid of transgenic mice overexpressing amyloid precursor protein
    • PID: 23863834
    • Maia LF, Kaeser SA, Reichwald J, Hruscha M, Martus P, Staufenbiel M et al (2013) Changes in amyloid-beta and Tau in the cerebrospinal fluid of transgenic mice overexpressing amyloid precursor protein. Sci Transl Med 5:194re2. doi:10.1126/scitranslmed.3006446
    • (2013) Sci Transl Med , vol.5
    • Maia, L.F.1    Kaeser, S.A.2    Reichwald, J.3    Hruscha, M.4    Martus, P.5    Staufenbiel, M.6
  • 82
    • 0024503377 scopus 로고
    • The pattern of acquisition of plaques and tangles in the brains of patients under 50 years of age with Down’s syndrome
    • PID: 2522541
    • Mann DMA, Esiri MM (1989) The pattern of acquisition of plaques and tangles in the brains of patients under 50 years of age with Down’s syndrome. J Neurol Sci 89:169–179
    • (1989) J Neurol Sci , vol.89 , pp. 169-179
    • Mann, D.M.A.1    Esiri, M.M.2
  • 83
    • 84885476621 scopus 로고    scopus 로고
    • Amyloid or tau: the chicken or the egg?
    • PID: 23925566
    • Mann DMA, Hardy J (2013) Amyloid or tau: the chicken or the egg? Acta Neuropathol 126:609–613. doi:10.1007/s00401-013-1162-1
    • (2013) Acta Neuropathol , vol.126 , pp. 609-613
    • Mann, D.M.A.1    Hardy, J.2
  • 84
    • 22544482926 scopus 로고    scopus 로고
    • Abeta42 is essential for parenchymal and vascular amyloid deposition in mice
    • PID: 16039562
    • McGowan E, Pickford F, Kim J, Onstead L, Eriksen J, Yu C et al (2005) Abeta42 is essential for parenchymal and vascular amyloid deposition in mice. Neuron 47:191–199. doi:10.1016/j.neuron.2005.06.030
    • (2005) Neuron , vol.47 , pp. 191-199
    • McGowan, E.1    Pickford, F.2    Kim, J.3    Onstead, L.4    Eriksen, J.5    Yu, C.6
  • 85
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer’s disease
    • PID: 10589538
    • McLean CA, Cherny RA, Fraser FW, Fuller SJ, Smith MJ, Beyreuther K et al (1999) Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer’s disease. Ann Neurol 46:860–866
    • (1999) Ann Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3    Fuller, S.J.4    Smith, M.J.5    Beyreuther, K.6
  • 86
    • 0037411517 scopus 로고    scopus 로고
    • A grading system of Alzheimer disease lesions in neocortical areas
    • PID: 12714113
    • Metsaars W, Hauw J-J, Welsem M, Duyckaerts C (2003) A grading system of Alzheimer disease lesions in neocortical areas. Neurobiol Aging 24:563–572
    • (2003) Neurobiol Aging , vol.24 , pp. 563-572
    • Metsaars, W.1    Hauw, J.-J.2    Welsem, M.3    Duyckaerts, C.4
  • 87
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host
    • PID: 16990547
    • Meyer-Luehmann M, Coomaraswamy J, Bolmont T, Kaeser S, Schaefer C, Kilger E et al (2006) Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 313:1781–1784. doi:10.1126/science.1131864
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3    Kaeser, S.4    Schaefer, C.5    Kilger, E.6
  • 88
    • 38949123792 scopus 로고    scopus 로고
    • Rapid appearance and local toxicity of amyloid-beta plaques in a mouse model of Alzheimer’s disease
    • PID: 18256671
    • Meyer-Luehmann M, Spires-Jones TL, Prada C, Garcia-Alloza M, de Calignon A, Rozkalne A et al (2008) Rapid appearance and local toxicity of amyloid-beta plaques in a mouse model of Alzheimer’s disease. Nature 451:720–724. doi:10.1038/nature06616
    • (2008) Nature , vol.451 , pp. 720-724
    • Meyer-Luehmann, M.1    Spires-Jones, T.L.2    Prada, C.3    Garcia-Alloza, M.4    de Calignon, A.5    Rozkalne, A.6
  • 90
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of abeta 1–42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation
    • PID: 10818140
    • Mucke L, Masliah E, Yu GQ, Mallory M, Rockenstein EM, Tatsuno G et al (2000) High-level neuronal expression of abeta 1–42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J Neurosci 20:4050–4058
    • (2000) J Neurosci , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3    Mallory, M.4    Rockenstein, E.M.5    Tatsuno, G.6
  • 91
    • 84894545954 scopus 로고    scopus 로고
    • Transmission of systemic AA amyloidosis in animals
    • PID: 24280941
    • Murakami T, Ishiguro N, Higuchi K (2014) Transmission of systemic AA amyloidosis in animals. Vet Pathol 51:363–371. doi:10.1177/0300985813511128
    • (2014) Vet Pathol , vol.51 , pp. 363-371
    • Murakami, T.1    Ishiguro, N.2    Higuchi, K.3
  • 92
    • 84929938315 scopus 로고    scopus 로고
    • Three dimensions of the amyloid hypothesis: time, space and “wingmen
    • PID: 26007213
    • Musiek ES, Holtzman DM (2015) Three dimensions of the amyloid hypothesis: time, space and “wingmen”. Nat Neurosci 18:800–806. doi:10.1038/nn.4018
    • (2015) Nat Neurosci , vol.18 , pp. 800-806
    • Musiek, E.S.1    Holtzman, D.M.2
  • 93
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • PID: 15294141
    • Oddo S, Billings L, Kesslak JP, Cribbs DH, LaFerla FM (2004) Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43:321–332. doi:10.1016/j.neuron.2004.07.003
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 94
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer’s disease with plaques and tangles: intracellular Abeta and synaptic dysfunction
    • PID: 12895417
    • Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, Kayed R et al (2003) Triple-transgenic model of Alzheimer’s disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron 39:409–421
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6
  • 96
    • 84939653898 scopus 로고    scopus 로고
    • Age and amyloid effects on human central nervous system amyloid-beta kinetics
    • PID: 26040676
    • Patterson BW, Elbert DL, Mawuenyega KG, Kasten T, Ovod V, Ma S et al (2015) Age and amyloid effects on human central nervous system amyloid-beta kinetics. Ann Neurol 78:439–453. doi:10.1002/ana.24454
    • (2015) Ann Neurol , vol.78 , pp. 439-453
    • Patterson, B.W.1    Elbert, D.L.2    Mawuenyega, K.G.3    Kasten, T.4    Ovod, V.5    Ma, S.6
  • 97
    • 84886646774 scopus 로고    scopus 로고
    • Alzheimer’s disease pathology in the neocortex and hippocampus of the western lowland gorilla (Gorilla gorilla gorilla)
    • PID: 23881733
    • Perez SE, Raghanti MA, Hof PR, Kramer L, Ikonomovic MD, Lacor PN et al (2013) Alzheimer’s disease pathology in the neocortex and hippocampus of the western lowland gorilla (Gorilla gorilla gorilla). J Comp Neurol 521:4318–4338. doi:10.1002/cne.23428
    • (2013) J Comp Neurol , vol.521 , pp. 4318-4338
    • Perez, S.E.1    Raghanti, M.A.2    Hof, P.R.3    Kramer, L.4    Ikonomovic, M.D.5    Lacor, P.N.6
  • 98
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer’s beta-amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R (2005) Self-propagating, molecular-level polymorphism in Alzheimer’s beta-amyloid fibrils. Science (80-) 307:262–265. doi: 10.1126/science.1105850
    • (2005) Science (80-) , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 99
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • PID: 23412472
    • Pooler AM, Phillips EC, Lau DHW, Noble W, Hanger DP (2013) Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep 14:389–394. doi:10.1038/embor.2013.15
    • (2013) EMBO Rep , vol.14 , pp. 389-394
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.W.3    Noble, W.4    Hanger, D.P.5
  • 101
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science (80-) 216:136–144
    • (1982) Science (80-) , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 102
    • 41149140767 scopus 로고    scopus 로고
    • The value of incomplete mouse models of Alzheimer’s disease
    • PID: 18270700
    • Radde R, Duma C, Goedert M, Jucker M (2008) The value of incomplete mouse models of Alzheimer’s disease. Eur J Nucl Med Mol Imaging 35(Suppl 1):S70–S74
    • (2008) Eur J Nucl Med Mol Imaging , vol.35 , pp. S70-S74
    • Radde, R.1    Duma, C.2    Goedert, M.3    Jucker, M.4
  • 103
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous Tau ameliorates amyloid beta–Induced deficits in an Alzheimer’s disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, Wu T et al (2007) Reducing endogenous Tau ameliorates amyloid beta–Induced deficits in an Alzheimer’s disease mouse model. Science (80-) 316:750–754
    • (2007) Science (80-) , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6
  • 104
    • 84856961915 scopus 로고    scopus 로고
    • Amyloid neuropathology in the single Arctic APP transgenic model affects interconnected brain regions
    • Ronnback A, Sagelius H, Bergstedt KD, Naslund J, Westermark GT, Winblad B et al (2012) Amyloid neuropathology in the single Arctic APP transgenic model affects interconnected brain regions. Neurobiol Aging 33:831.e11–831.e19. doi: 10.1016/j.neurobiolaging.2011.07.012
    • (2012) Neurobiol Aging 33:831 , vol.e19 , pp. e11-e831
    • Ronnback, A.1    Sagelius, H.2    Bergstedt, K.D.3    Naslund, J.4    Westermark, G.T.5    Winblad, B.6
  • 105
    • 29444442794 scopus 로고    scopus 로고
    • APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy
    • PID: 16369530
    • Rovelet-Lecrux A, Hannequin D, Raux G, Le Meur N, Laquerriere A, Vital A et al (2006) APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy. Nat Genet 38:24–26
    • (2006) Nat Genet , vol.38 , pp. 24-26
    • Rovelet-Lecrux, A.1    Hannequin, D.2    Raux, G.3    Le Meur, N.4    Laquerriere, A.5    Vital, A.6
  • 106
    • 80053646630 scopus 로고    scopus 로고
    • Early onset amyloid lesions lead to severe neuritic abnormalities and local, but not global neuron loss in APPPS1 transgenic mice
    • Rupp NJ, Wegenast-Braun BM, Radde R, Calhoun ME, Jucker M (2011) Early onset amyloid lesions lead to severe neuritic abnormalities and local, but not global neuron loss in APPPS1 transgenic mice. Neurobiol Aging 32:2324.e1–2324.e6. doi: 10.1016/j.neurobiolaging.2010.08.014
    • (2011) Neurobiol Aging 32:2324 , vol.e6 , pp. e1
    • Rupp, N.J.1    Wegenast-Braun, B.M.2    Radde, R.3    Calhoun, M.E.4    Jucker, M.5
  • 107
    • 84899647552 scopus 로고    scopus 로고
    • Single APP knock-in mouse models of Alzheimer’s disease
    • PID: 24728269
    • Saito T, Matsuba Y, Mihira N, Takano J, Nilsson P, Itohara S et al (2014) Single APP knock-in mouse models of Alzheimer’s disease. Nat Neurosci 17:661–663. doi:10.1038/nn.3697
    • (2014) Nat Neurosci , vol.17 , pp. 661-663
    • Saito, T.1    Matsuba, Y.2    Mihira, N.3    Takano, J.4    Nilsson, P.5    Itohara, S.6
  • 109
    • 0025905505 scopus 로고
    • Comparative epitope analysis of neuronal cytoskeletal proteins in Alzheimer’s disease senile plaque, neurites and neuropil threads
    • PID: 1706004
    • Schmidt ML, Lee VM, Trojanowski JQ (1991) Comparative epitope analysis of neuronal cytoskeletal proteins in Alzheimer’s disease senile plaque, neurites and neuropil threads. Lab Invest 64:352–357
    • (1991) Lab Invest , vol.64 , pp. 352-357
    • Schmidt, M.L.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 110
    • 57149146023 scopus 로고    scopus 로고
    • The early history of the transmissible spongiform encephalopathies exemplified by scrapie
    • PID: 18951958
    • Schneider K, Fangerau H, Michaelsen B, Raab WH-M (2008) The early history of the transmissible spongiform encephalopathies exemplified by scrapie. Brain Res Bull 77:343–355. doi:10.1016/j.brainresbull.2008.09.012
    • (2008) Brain Res Bull , vol.77 , pp. 343-355
    • Schneider, K.1    Fangerau, H.2    Michaelsen, B.3    Raab, W.H.-M.4
  • 111
    • 0029164285 scopus 로고
    • Relationship of amyloid β/A4 protein to the neurofibrillary tangles in Guamanian parkinsonism-dementia
    • PID: 8525803
    • Schwab C, Steele JC, Akiyama H, McGeer EG, McGeer PL (1995) Relationship of amyloid β/A4 protein to the neurofibrillary tangles in Guamanian parkinsonism-dementia. Acta Neuropathol 90:287–298. doi:10.1007/BF00296513
    • (1995) Acta Neuropathol , vol.90 , pp. 287-298
    • Schwab, C.1    Steele, J.C.2    Akiyama, H.3    McGeer, E.G.4    McGeer, P.L.5
  • 112
    • 0023118252 scopus 로고
    • Conservation of brain amyloid proteins in aged mammals and humans with Alzheimer’s disease
    • Selkoe DJ, Bell DS, Podlisny MB, Price DL, Cork LC (1987) Conservation of brain amyloid proteins in aged mammals and humans with Alzheimer’s disease. Science (80-) 235:873–877
    • (1987) Science (80-) , vol.235 , pp. 873-877
    • Selkoe, D.J.1    Bell, D.S.2    Podlisny, M.B.3    Price, D.L.4    Cork, L.C.5
  • 113
    • 84908547666 scopus 로고    scopus 로고
    • Nomenclature 2014: amyloid fibril proteins and clinical classification of the amyloidosis
    • PID: 25263598
    • Sipe JD, Benson MD, Buxbaum JN, Ikeda S, Merlini G, Saraiva MJM et al (2014) Nomenclature 2014: amyloid fibril proteins and clinical classification of the amyloidosis. Amyloid 21:221–224. doi:10.3109/13506129.2014.964858
    • (2014) Amyloid , vol.21 , pp. 221-224
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5    Saraiva, M.J.M.6
  • 114
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • PID: 12511861
    • Soto C (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 4:49–60. doi:10.1038/nrn1007
    • (2003) Nat Rev Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 115
    • 0033968306 scopus 로고    scopus 로고
    • Molecular genetics of Alzheimer’s disease
    • PID: 10682216
    • 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
  • 116
    • 84904333974 scopus 로고    scopus 로고
    • Distinct synthetic Abeta prion strains producing different amyloid deposits in bigenic mice
    • PID: 24982137
    • Stohr J, Condello C, Watts JC, Bloch L, Oehler A, Nick M et al (2014) Distinct synthetic Abeta prion strains producing different amyloid deposits in bigenic mice. Proc Natl Acad Sci USA 111:10329–10334. doi:10.1073/pnas.1408968111
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 10329-10334
    • Stohr, J.1    Condello, C.2    Watts, J.C.3    Bloch, L.4    Oehler, A.5    Nick, M.6
  • 118
    • 70350451482 scopus 로고    scopus 로고
    • Gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment
    • PID: 19828817
    • Takami M, Nagashima Y, Sano Y, Ishihara S, Morishima-Kawashima M, Funamoto S et al (2009) Gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment. J Neurosci 29:13042–13052. doi:10.1523/JNEUROSCI.2362-09.2009
    • (2009) J Neurosci , vol.29 , pp. 13042-13052
    • Takami, M.1    Nagashima, Y.2    Sano, Y.3    Ishihara, S.4    Morishima-Kawashima, M.5    Funamoto, S.6
  • 119
    • 0344737582 scopus 로고    scopus 로고
    • Vascular pathology in Alzheimer disease: correlation of cerebral amyloid angiopathy and arteriosclerosis/lipohyalinosis with cognitive decline
    • PID: 14692704
    • Thal DR, Ghebremedhin E, Orantes M, Wiestler OD (2003) Vascular pathology in Alzheimer disease: correlation of cerebral amyloid angiopathy and arteriosclerosis/lipohyalinosis with cognitive decline. J Neuropathol Exp Neurol 62:1287–1301
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 1287-1301
    • Thal, D.R.1    Ghebremedhin, E.2    Orantes, M.3    Wiestler, O.D.4
  • 120
    • 0037172826 scopus 로고    scopus 로고
    • Phases of A beta-deposition in the human brain and its relevance for the development of AD
    • PID: 12084879
    • Thal DR, Rüb U, Orantes M, Braak H (2002) Phases of A beta-deposition in the human brain and its relevance for the development of AD. Neurology 58:1791–1800
    • (2002) Neurology , vol.58 , pp. 1791-1800
    • Thal, D.R.1    Rüb, U.2    Orantes, M.3    Braak, H.4
  • 121
    • 84926347292 scopus 로고    scopus 로고
    • Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer’s disease
    • PID: 25534025
    • Thal DR, Walter J, Saido TC, Fändrich M (2015) Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer’s disease. Acta Neuropathol 129:167–182. doi:10.1007/s00401-014-1375-y
    • (2015) Acta Neuropathol , vol.129 , pp. 167-182
    • Thal, D.R.1    Walter, J.2    Saido, T.C.3    Fändrich, M.4
  • 122
    • 84903190262 scopus 로고    scopus 로고
    • Function, therapeutic potential and cell biology of BACE proteases: current status and future prospects
    • PID: 24646365
    • Vassar R, Kuhn P-H, Haass C, Kennedy ME, Rajendran L, Wong PC et al (2014) Function, therapeutic potential and cell biology of BACE proteases: current status and future prospects. J Neurochem 130:4–28. doi:10.1111/jnc.12715
    • (2014) J Neurochem , vol.130 , pp. 4-28
    • Vassar, R.1    Kuhn, P.-H.2    Haass, C.3    Kennedy, M.E.4    Rajendran, L.5    Wong, P.C.6
  • 123
    • 83255181779 scopus 로고    scopus 로고
    • Amyloid-beta plaque growth in cognitively normal adults: longitudinal [11C] Pittsburgh compound B data
    • PID: 22162065
    • Vlassenko AG, Mintun MA, Xiong C, Sheline YI, Goate AM, Benzinger TLS et al (2011) Amyloid-beta plaque growth in cognitively normal adults: longitudinal [11C] Pittsburgh compound B data. Ann Neurol 70:857–861. doi:10.1002/ana.22608
    • (2011) Ann Neurol , vol.70 , pp. 857-861
    • Vlassenko, A.G.1    Mintun, M.A.2    Xiong, C.3    Sheline, Y.I.4    Goate, A.M.5    Benzinger, T.L.S.6
  • 124
    • 0036386817 scopus 로고    scopus 로고
    • Modeling Alzheimer’s disease and other proteopathies in vivo: is seeding the key?
    • PID: 12373522
    • Walker LC, Bian F, Callahan MJ, Lipinski WJ, Durham RA, LeVine H (2002) Modeling Alzheimer’s disease and other proteopathies in vivo: is seeding the key? Amino Acids 23:87–93. doi:10.1007/s00726-001-0113-7
    • (2002) Amino Acids , vol.23 , pp. 87-93
    • Walker, L.C.1    Bian, F.2    Callahan, M.J.3    Lipinski, W.J.4    Durham, R.A.5    LeVine, H.6
  • 126
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • PID: 10464339
    • Walsh DM, Hartley DM, Kusumoto Y, Fezoui Y, Condron MM, Lomakin A et al (1999) Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 274:25945–25952
    • (1999) J Biol Chem , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6
  • 127
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers: a decade of discovery
    • PID: 17286590
    • Walsh DM, Selkoe DJ (2007) A beta oligomers: a decade of discovery. J Neurochem 101:1172–1184
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 128
    • 84904322386 scopus 로고    scopus 로고
    • Serial propagation of distinct strains of Abeta prions from Alzheimer’s disease patients
    • PID: 24982139
    • Watts JC, Condello C, Stohr J, Oehler A, Lee J, DeArmond SJ et al (2014) Serial propagation of distinct strains of Abeta prions from Alzheimer’s disease patients. Proc Natl Acad Sci USA 111:10323–10328. doi:10.1073/pnas.1408900111
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 10323-10328
    • Watts, J.C.1    Condello, C.2    Stohr, J.3    Oehler, A.4    Lee, J.5    DeArmond, S.J.6
  • 130
    • 84944324335 scopus 로고    scopus 로고
    • η-Secretase processing of APP inhibits neuronal activity in the hippocampus
    • PID: 26322584
    • Willem M, Tahirovic S, Busche MA, Ovsepian SV, Chafai M, Kootar S et al (2015) η-Secretase processing of APP inhibits neuronal activity in the hippocampus. Nature 526:443–447. doi:10.1038/nature14864
    • (2015) Nature , vol.526 , pp. 443-447
    • Willem, M.1    Tahirovic, S.2    Busche, M.A.3    Ovsepian, S.V.4    Chafai, M.5    Kootar, S.6
  • 132
    • 84930413213 scopus 로고    scopus 로고
    • Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer’s disease
    • PID: 25938662
    • Xiao Y, Ma B, McElheny D, Parthasarathy S, Long F, Hoshi M et al (2015) Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer’s disease. Nat Struct Mol Biol 22:499–505. doi:10.1038/nsmb.2991
    • (2015) Nat Struct Mol Biol , vol.22 , pp. 499-505
    • Xiao, Y.1    Ma, B.2    McElheny, D.3    Parthasarathy, S.4    Long, F.5    Hoshi, M.6
  • 134
    • 84946493758 scopus 로고    scopus 로고
    • Progression of seed-induced abeta deposition within the limbic connectome
    • PID: 25677332
    • Ye L, Hamaguchi T, Fritschi SK, Eisele YS, Obermuller U, Jucker M et al (2015) Progression of seed-induced abeta deposition within the limbic connectome. Brain Pathol 25:743–752. doi:10.1111/bpa.12252
    • (2015) Brain Pathol , vol.25 , pp. 743-752
    • Ye, L.1    Hamaguchi, T.2    Fritschi, S.K.3    Eisele, Y.S.4    Obermuller, U.5    Jucker, M.6
  • 135
    • 84964959825 scopus 로고    scopus 로고
    • Transgene expression in the Nop-tTA driver line is not inherently restricted to the entorhinal cortex
    • PID: 25869275
    • Yetman MJ, Lillehaug S, Bjaalie JG, Leergaard TB, Jankowsky JL (2015) Transgene expression in the Nop-tTA driver line is not inherently restricted to the entorhinal cortex. Brain Struct Funct. doi:10.1007/s00429-015-1040-9
    • (2015) Brain Struct Funct
    • Yetman, M.J.1    Lillehaug, S.2    Bjaalie, J.G.3    Leergaard, T.B.4    Jankowsky, J.L.5


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