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Volumn 4, Issue 6, 2008, Pages 1033-1042

An update on the toxicity of Aβ in Alzheimer's disease

Author keywords

Amyloid; Mitochondria; Oligomer; Proteomic; Tau; Transgenic

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; ALPHA SECRETASE; AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; BETA SECRETASE; GAMMA SECRETASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; TAU PROTEIN; TRANSCRIPTION FACTOR YY1;

EID: 60249086597     PISSN: 11766328     EISSN: None     Source Type: Journal    
DOI: 10.2147/ndt.s3016     Document Type: Review
Times cited : (37)

References (137)
  • 1
    • 10044244916 scopus 로고    scopus 로고
    • Calcium signals induced by amyloid beta peptide and their consequences in neurons and astrocytes in culture
    • Abramov AY, Canevari L, Duchen MR. 2004. Calcium signals induced by amyloid beta peptide and their consequences in neurons and astrocytes in culture. Biochim Biophys Acta, 1742:81-7.
    • (2004) Biochim Biophys Acta , vol.1742 , pp. 81-87
    • Abramov, A.Y.1    Canevari, L.2    Duchen, M.R.3
  • 2
    • 22144455300 scopus 로고    scopus 로고
    • Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: A membrane-disrupting peptide
    • Ambroggio EE, Kim DH, Separovic F, et al. 2005. Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide. Biophys J, 88:2706-13.
    • (2005) Biophys J , vol.88 , pp. 2706-2713
    • Ambroggio, E.E.1    Kim, D.H.2    Separovic, F.3
  • 3
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada HK, Biswas G, Robin MA, et al. 2003. Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J Cell Biol, 161:41-54.
    • (2003) J Cell Biol , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3
  • 4
    • 8144223671 scopus 로고    scopus 로고
    • RAGE potentiates Abeta-induced perturbation of neuronal function in transgenic mice
    • Arancio O, Zhang HP, Chen X, et al. 2004. RAGE potentiates Abeta-induced perturbation of neuronal function in transgenic mice. Embo J, 23:4096-105.
    • (2004) Embo J , vol.23 , pp. 4096-4105
    • Arancio, O.1    Zhang, H.P.2    Chen, X.3
  • 5
    • 0348108123 scopus 로고    scopus 로고
    • Synaptic plasticity and cell cycle activation in neurons are alternative effector pathways: The 'Dr Jekyll and Mr. Hyde concept' of Alzheimer's disease or the yin and yang of neuroplasticity
    • Arendt T. 2003. Synaptic plasticity and cell cycle activation in neurons are alternative effector pathways: the 'Dr Jekyll and Mr. Hyde concept' of Alzheimer's disease or the yin and yang of neuroplasticity. Prog Neurobiol, 71:83-248.
    • (2003) Prog Neurobiol , vol.71 , pp. 83-248
    • Arendt, T.1
  • 6
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe N, Rojas E, Pollard HB. 1993. Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc Natl Acad Sci U S A, 90:567-71.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 7
    • 0025717816 scopus 로고
    • The topographical and neuroanatomical distribution of neurofibrillary tangles and neuritic plaques in the cerebral cortex of patients with Alzheimer's disease
    • Arnold SE, Hyman BT, Flory J, et al. 1991. The topographical and neuroanatomical distribution of neurofibrillary tangles and neuritic plaques in the cerebral cortex of patients with Alzheimer's disease. Cereb Cortex, 1:103-16.
    • (1991) Cereb Cortex , vol.1 , pp. 103-116
    • Arnold, S.E.1    Hyman, B.T.2    Flory, J.3
  • 8
    • 33746919083 scopus 로고    scopus 로고
    • Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
    • Baker M, Mackenzie IR, Pickering-Brown SM, et al. 2006. Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17. Nature, 442:916-9.
    • (2006) Nature , vol.442 , pp. 916-919
    • Baker, M.1    Mackenzie, I.R.2    Pickering-Brown, S.M.3
  • 9
    • 27644493692 scopus 로고    scopus 로고
    • Globular amyloid beta-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease
    • Barghorn S, Nimmrich V, Striebinger A, et al. 2005. Globular amyloid beta-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease. J Neurochem, 95:834-47.
    • (2005) J Neurochem , vol.95 , pp. 834-847
    • Barghorn, S.1    Nimmrich, V.2    Striebinger, A.3
  • 10
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: Evidence for AbetaP channel-mediated cellular toxicity
    • Bhatia R, Lin H, Lal R. 2000. Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity. Faseb J, 14:1233-43.
    • (2000) Faseb J , vol.14 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 11
    • 0037135272 scopus 로고    scopus 로고
    • Uptake and pathogenic effects ofamyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
    • Bi X, Gall CM, Zhou J, et al. 2002. Uptake and pathogenic effects ofamyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists. Neuroscience, 112:827-40.
    • (2002) Neuroscience , vol.112 , pp. 827-840
    • Bi, X.1    Gall, C.M.2    Zhou, J.3
  • 12
    • 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
    • Bolmont T, Clavaguera F, Meyer-Luehmann 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, 171:2012-20.
    • (2007) Am J Pathol , vol.171 , pp. 2012-2020
    • Bolmont, T.1    Clavaguera, F.2    Meyer-Luehmann, M.3
  • 13
    • 0025863618 scopus 로고    scopus 로고
    • 199 I. Neuropathological stageing of Alzheimer-related changes
    • Braak H, and Braak E. 199 I. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol (Berl), 82:239-59.
    • Acta Neuropathol (Berl) , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 14
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • discussion 8-84
    • Braak H, Braak E. 1995. Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol Aging, 16:271-8; discussion 8-84.
    • (1995) Neurobiol Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 16
    • 38949205552 scopus 로고    scopus 로고
    • Delineating the mechanism of Alzheimer's disease A beta peptide neurotoxicity
    • Cappai R, and Bamham KJ. 2008. Delineating the mechanism of Alzheimer's disease A beta peptide neurotoxicity. Neurochem Res, 33:526-32.
    • (2008) Neurochem Res , vol.33 , pp. 526-532
    • Cappai, R.1    Bamham, K.J.2
  • 17
    • 4644276796 scopus 로고    scopus 로고
    • Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model
    • Casas C, Sergeant N, Itier JM, et al. 2004. Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model. Am J Pathol, 165:1289-300.
    • (2004) Am J Pathol , vol.165 , pp. 1289-1300
    • Casas, C.1    Sergeant, N.2    Itier, J.M.3
  • 18
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Abeta: A potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • Caspersen C, Wang N, Yao J, et al. 2005. Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. Faseb J, 19:2040-1.
    • (2005) Faseb J , vol.19 , pp. 2040-2041
    • Caspersen, C.1    Wang, N.2    Yao, J.3
  • 19
    • 3442876436 scopus 로고    scopus 로고
    • Posttranslational modifications of tau - Role in human tauopathies and modeling in transgenic animals
    • Chen F, David D, Ferrari A, et al. 2004a. Posttranslational modifications of tau - Role in human tauopathies and modeling in transgenic animals. Curr Drug Targets, 5:503-15.
    • (2004) Curr Drug Targets , vol.5 , pp. 503-515
    • Chen, F.1    David, D.2    Ferrari, A.3
  • 21
    • 2442711560 scopus 로고    scopus 로고
    • Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice
    • Chin J, Palop JJ, Yu GQ, et al. 2004. Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice. J Neurosci, 24:4692-7.
    • (2004) J Neurosci , vol.24 , pp. 4692-4697
    • Chin, J.1    Palop, J.J.2    Yu, G.Q.3
  • 22
    • 33745985711 scopus 로고    scopus 로고
    • ERK1/2 activation mediates Abeta oligomer-induced neurotoxicity via caspase-3 activation and tau cleavage in rat organotypic hippocampal slice cultures
    • Chong YH, Shin YJ, Lee EO, et al. 2006. ERK1/2 activation mediates Abeta oligomer-induced neurotoxicity via caspase-3 activation and tau cleavage in rat organotypic hippocampal slice cultures. J Biol Chem, 281:20315-25.
    • (2006) J Biol Chem , vol.281 , pp. 20315-20325
    • Chong, Y.H.1    Shin, Y.J.2    Lee, E.O.3
  • 23
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • Cleary JP, Walsh DM, Hofmeister JJ, et al. 2005. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci, 8:79-84.
    • (2005) Nat Neurosci , vol.8 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3
  • 24
    • 33745894132 scopus 로고    scopus 로고
    • Does the p 75 neurotrophin receptor mediate Abeta-induced toxicity in Alzheimer's disease?
    • Coulson EJ 2006. Does the p 75 neurotrophin receptor mediate Abeta-induced toxicity in Alzheimer's disease? J Neurochem, 98:654-60.
    • (2006) J Neurochem , vol.98 , pp. 654-660
    • Coulson, E.J.1
  • 25
    • 19944433571 scopus 로고    scopus 로고
    • Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta 1-42
    • Crouch PJ, Blake R, Duce JA, et al. 2005. Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta 1-42. J Neurosci, 25:672-9.
    • (2005) J Neurosci , vol.25 , pp. 672-679
    • Crouch, P.J.1    Blake, R.2    Duce, J.A.3
  • 26
    • 33746910649 scopus 로고    scopus 로고
    • Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21
    • Cruts M, Gijselinck I, van der Zee J, et al. 2006. Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21. Nature, 442:920-4.
    • (2006) Nature , vol.442 , pp. 920-924
    • Cruts, M.1    Gijselinck, I.2    van der Zee, J.3
  • 27
    • 25444464112 scopus 로고    scopus 로고
    • Functional Genomics meets neurodegenerative disorders Part I: Transcriptomic and proteomic technology
    • David D, Hoerndli F, Gotz J. 2005a. Functional Genomics meets neurodegenerative disorders Part I: Transcriptomic and proteomic technology. Prog Neurobiol, 76:153-68.
    • (2005) Prog Neurobiol , vol.76 , pp. 153-168
    • David, D.1    Hoerndli, F.2    Gotz, J.3
  • 28
    • 21244486781 scopus 로고    scopus 로고
    • Proteomic and functional analysis reveal a mitochondrial dysfunction in P301L tau transgenic mice
    • David DC, Hauptmann S, Scherping I, et al. 2005b. Proteomic and functional analysis reveal a mitochondrial dysfunction in P301L tau transgenic mice. J Biol Chem, 280:23802-14.
    • (2005) J Biol Chem , vol.280 , pp. 23802-23814
    • David, D.C.1    Hauptmann, S.2    Scherping, I.3
  • 29
    • 33846019607 scopus 로고    scopus 로고
    • β-Amyloid treatment of two complementary P301L tau-expressing Alzheimer's disease models reveals similar deregulated cellular processes
    • David DC, Ittner LM, Gehrig P, et al. 2006. β-Amyloid treatment of two complementary P301L tau-expressing Alzheimer's disease models reveals similar deregulated cellular processes. Proteomics, 6:6566-77.
    • (2006) Proteomics , vol.6 , pp. 6566-6577
    • David, D.C.1    Ittner, L.M.2    Gehrig, P.3
  • 30
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP, et al. 2007. Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem, 282:11590-601.
    • (2007) J Biol Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3
  • 31
    • 4043061467 scopus 로고    scopus 로고
    • LRP/amyloid beta-peptide interaction mediates differential brain efflux ofAbeta isoforms
    • Deane R, Wu Z, Sagare A, et al. 2004. LRP/amyloid beta-peptide interaction mediates differential brain efflux ofAbeta isoforms. Neuron, 43:333-44.
    • (2004) Neuron , vol.43 , pp. 333-344
    • Deane, R.1    Wu, Z.2    Sagare, A.3
  • 32
    • 0037072278 scopus 로고    scopus 로고
    • Nonoverlapping but synergetie tau and APP pathologies in sporadic Alzheimer's disease
    • Delacourte A, Sergeant N, Champain D, et al. 2002. Nonoverlapping but synergetie tau and APP pathologies in sporadic Alzheimer's disease. Neurology, 59:398-407.
    • (2002) Neurology , vol.59 , pp. 398-407
    • Delacourte, A.1    Sergeant, N.2    Champain, D.3
  • 33
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A, Mina E, Kayed R, et al. 2005. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem, 280:17294-300.
    • (2005) J Biol Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3
  • 34
    • 54049104444 scopus 로고    scopus 로고
    • Divergent phosphorylation pattern of tau in P301L tau transgenic mice
    • Deters N, Ittner LM, and Gotz J. 2008. Divergent phosphorylation pattern of tau in P301L tau transgenic mice. Eur J Neurosci, 28:137-47.
    • (2008) Eur J Neurosci , vol.28 , pp. 137-147
    • Deters, N.1    Ittner, L.M.2    Gotz, J.3
  • 35
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L, Prabhu BM, Galati DF, et al. 2006. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J Neurosci, 26:9057-68.
    • (2006) J Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3
  • 36
    • 54249137157 scopus 로고    scopus 로고
    • 42) both impair mitochondrial function in P301L tau transgenic mice
    • 42) both impair mitochondrial function in P301L tau transgenic mice. J Mol Med, 86:1255-67.
    • (2008) J Mol Med , vol.86 , pp. 1255-1267
    • Eckert, A.1    Drose, S.2    Brandt, U.3
  • 37
    • 40449090190 scopus 로고    scopus 로고
    • Soluble beta-amyloid leads to mitochondrial defects in amyloid precursor protein and tau transgenie mice
    • Eckert A, Hauptmann S, Scherping I, et al. 2008b. Soluble beta-amyloid leads to mitochondrial defects in amyloid precursor protein and tau transgenie mice. Neurodegener Dis, 5:157-9.
    • (2008) Neurodegener Dis , vol.5 , pp. 157-159
    • Eckert, A.1    Hauptmann, S.2    Scherping, I.3
  • 38
    • 0038664363 scopus 로고    scopus 로고
    • Reconstitution of gamma-secretase activity
    • Edbauer D, Winkler E, Regula JT, et al. 2003. Reconstitution of gamma-secretase activity. Nat Cell Biol, 5:486-8.
    • (2003) Nat Cell Biol , vol.5 , pp. 486-488
    • Edbauer, D.1    Winkler, E.2    Regula, J.T.3
  • 39
    • 0141960033 scopus 로고    scopus 로고
    • Beta-amyloid induces PHF-like tau filaments in tissue culture
    • Ferrari A, Hoerndli F, Baechi T, et al. 2003. Beta-amyloid induces PHF-like tau filaments in tissue culture. J Biol Chem, 278:40162-8.
    • (2003) J Biol Chem , vol.278 , pp. 40162-40168
    • Ferrari, A.1    Hoerndli, F.2    Baechi, T.3
  • 40
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein [see comments]
    • Games D, Adams D, Alessandrini R, et al. 1995. Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein [see comments]. Nature, 373:523-7.
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 41
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, and Wong CW. 1984. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun, 120:885-90.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 42
    • 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, et al. 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 U S A, 85:4051-5.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3
  • 43
    • 33847732649 scopus 로고    scopus 로고
    • Ultrastructural localization of intraneuronal Abeta-peptide in Alzheimer disease brains
    • Gomez-Ramos P, and Asuneion Moran M. 2007. Ultrastructural localization of intraneuronal Abeta-peptide in Alzheimer disease brains. J Alzheimers Dis, 11:53-9.
    • (2007) J Alzheimers Dis , vol.11 , pp. 53-59
    • Gomez-Ramos, P.1    Asuneion Moran, M.2
  • 44
    • 0034992339 scopus 로고    scopus 로고
    • Tau and transgenic animal models
    • Gotz J 2001. Tau and transgenic animal models. Brain Res Brain Res Rev, 35:266-86.
    • (2001) Brain Res Brain Res Rev , vol.35 , pp. 266-286
    • Gotz, J.1
  • 45
    • 0035808361 scopus 로고    scopus 로고
    • Tau filament formation in transgenic mice expressing P301L Tan
    • Gotz J, Chen F, Barmettler R, et al. 2001a. Tau filament formation in transgenic mice expressing P301L Tan. J Biol Chem, 276:529-34.
    • (2001) J Biol Chem , vol.276 , pp. 529-534
    • Gotz, J.1    Chen, F.2    Barmettler, R.3
  • 46
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Abeta42 fibrils
    • Gotz J, Chen F, van Dorpe J, et al. 2001b. Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Abeta42 fibrils. Science, 293:1491-5.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3
  • 47
    • 33847199377 scopus 로고    scopus 로고
    • A decade of tau transgenic animal models and beyond
    • Gotz J, Deters N, Doldissen A, et al. 2007. A decade of tau transgenic animal models and beyond. Brain Pathol, 17:91-103.
    • (2007) Brain Pathol , vol.17 , pp. 91-103
    • Gotz, J.1    Deters, N.2    Doldissen, A.3
  • 48
    • 45749151056 scopus 로고    scopus 로고
    • Animal models of Alzheimer's disease and frontotemporal dementia
    • Gotz J, and Ittner LM. 2008. Animal models of Alzheimer's disease and frontotemporal dementia. Nat Rev Neurosci, 9:532-44.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 532-544
    • Gotz, J.1    Ittner, L.M.2
  • 49
    • 49149124192 scopus 로고    scopus 로고
    • Is tau aggregation toxic or protective: A sensible question in the absence of sensitive methods?
    • Gotz J, Ittner LM, Fandrich M, et al. 2008. Is tau aggregation toxic or protective: a sensible question in the absence of sensitive methods? J A lzheimers Dis, 14:423-9.
    • (2008) J A lzheimers Dis , vol.14 , pp. 423-429
    • Gotz, J.1    Ittner, L.M.2    Fandrich, M.3
  • 50
    • 33746411112 scopus 로고    scopus 로고
    • Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease?
    • Gotz J, Ittner LM, Kins S. 2006. Do axonal defects in tau and amyloid precursor protein transgenic animals model axonopathy in Alzheimer's disease? J Neurochem, 98:993-1006.
    • (2006) J Neurochem , vol.98 , pp. 993-1006
    • Gotz, J.1    Ittner, L.M.2    Kins, S.3
  • 51
    • 0035800219 scopus 로고    scopus 로고
    • Compartmentalized tau hyperphosphorylation and increased levels of kinases in transgenic mice
    • Gotz J, and Nitsch RM. 2001. Compartmentalized tau hyperphosphorylation and increased levels of kinases in transgenic mice. Neuroreport, 12:2007-16.
    • (2001) Neuroreport , vol.12 , pp. 2007-2016
    • Gotz, J.1    Nitsch, R.M.2
  • 52
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Gotz J, Probst A, Spillantini MG, et al. 1995. Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. Embo J, 14:1304-13.
    • (1995) Embo J , vol.14 , pp. 1304-1313
    • Gotz, J.1    Probst, A.2    Spillantini, M.G.3
  • 53
    • 4744370969 scopus 로고    scopus 로고
    • Amyloid-induced neurofibrillary tangle formation in Alzheimer's disease: Insight from transgenic mouse and tissue-culture models
    • Gotz J, Schild A, Hoerndli F, et al. 2004a. Amyloid-induced neurofibrillary tangle formation in Alzheimer's disease: insight from transgenic mouse and tissue-culture models. Int J Dev Neurosci, 22:453-65.
    • (2004) Int J Dev Neurosci , vol.22 , pp. 453-465
    • Gotz, J.1    Schild, A.2    Hoerndli, F.3
  • 54
    • 3142655729 scopus 로고    scopus 로고
    • Transgenic animal models of Alzheimer's disease and related disorders: Histopathology, behavior and therapy
    • Gotz J, Streffer JR, David D, et al. 2004b. Transgenic animal models of Alzheimer's disease and related disorders: Histopathology, behavior and therapy. Mol Psychiatry, 9:664-83.
    • (2004) Mol Psychiatry , vol.9 , pp. 664-683
    • Gotz, J.1    Streffer, J.R.2    David, D.3
  • 55
    • 0034948975 scopus 로고    scopus 로고
    • e. Oligodendroglial tau filament formation in transgenic mice expressing G272V tau
    • Gotz J, Tolnay M, Barmettler R, et al. 2001 e. Oligodendroglial tau filament formation in transgenic mice expressing G272V tau. Eur J Neurosci, 13:2131-40.
    • (2001) Eur J Neurosci , vol.13 , pp. 2131-2140
    • Gotz, J.1    Tolnay, M.2    Barmettler, R.3
  • 57
    • 37649019187 scopus 로고    scopus 로고
    • Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils
    • Habicht G, Haupt C, Friedrich RP, et al. 2007. Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils. Proc Natl Acad Sci U S A, 104:19232-7.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19232-19237
    • Habicht, G.1    Haupt, C.2    Friedrich, R.P.3
  • 58
    • 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, 297:353-6.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 59
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and serapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD, and Lansbury PT, Jr. 1997. Models of amyloid seeding in Alzheimer's disease and serapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem, 66:385-407.
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 60
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, et al. 1999. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci, 19:8876-84.
    • (1999) J Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3
  • 61
    • 25444467721 scopus 로고    scopus 로고
    • Functional genomics meets neurodegenerative disorders. Part II: Application and data integration
    • Hoerndli F, David D, Gotz J. 2005. Functional genomics meets neurodegenerative disorders. Part II: Application and data integration. Prog Neurobiol, 76:169-88.
    • (2005) Prog Neurobiol , vol.76 , pp. 169-188
    • Hoerndli, F.1    David, D.2    Gotz, J.3
  • 62
    • 34447116398 scopus 로고    scopus 로고
    • Abeta treatment and P301L tau exPression in an Alzheimer's disease tissue culture model act synergistically to promote aberrant cell cycle re-entry
    • Hoerndli FJ, Pelech S, Papassotiropoulos A, et al. 2007. Abeta treatment and P301L tau exPression in an Alzheimer's disease tissue culture model act synergistically to promote aberrant cell cycle re-entry. Eur J Neurosci, 26:60-72.
    • (2007) Eur J Neurosci , vol.26 , pp. 60-72
    • Hoerndli, F.J.1    Pelech, S.2    Papassotiropoulos, A.3
  • 63
    • 7444225172 scopus 로고    scopus 로고
    • Reference genes identified in SH-SY5Y cells using custom-made gene arrays with validation by quantitative polymerase chain reaction
    • Hoerndli FJ, Toigo M, Schild A, et al. 2004. Reference genes identified in SH-SY5Y cells using custom-made gene arrays with validation by quantitative polymerase chain reaction. Anal Biochem, 335:30-41.
    • (2004) Anal Biochem , vol.335 , pp. 30-41
    • Hoerndli, F.J.1    Toigo, M.2    Schild, A.3
  • 64
    • 0344936729 scopus 로고    scopus 로고
    • Possible causes of Alzheimer's disease: Amyloid fragments, free radicals, and calcium homeostasis
    • Holscher C. 1998. Possible causes of Alzheimer's disease: amyloid fragments, free radicals, and calcium homeostasis. Neurobiol Dis, 5:129-41.
    • (1998) Neurobiol Dis , vol.5 , pp. 129-141
    • Holscher, C.1
  • 65
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation
    • Hortschansky P, Schroeckh V, Christopeit T, et al. 2005. The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation. Protein Sci, 14:1753-9.
    • (2005) Protein Sci , vol.14 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3
  • 66
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice [see comments]
    • Hsiao K, Chapman P, Nilsen S, et al. 1996. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice [see comments]. Science, 274:99-102.
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 67
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5'-splice-site mutations in tan with the inherited dementia FTDP-17
    • Hutton M, Lendon CL, Rizzu P, et al. 1998. Association of missense and 5'-splice-site mutations in tan with the inherited dementia FTDP-17. Nature, 393:702-5.
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 68
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the - human tau isoform
    • Ishihara T, Hong M, Zhang B, et al. 1999. Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the - human tau isoform. Neuron, 24:751-62.
    • (1999) Neuron , vol.24 , pp. 751-762
    • Ishihara, T.1    Hong, M.2    Zhang, B.3
  • 69
    • 57349172663 scopus 로고    scopus 로고
    • Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia
    • Ittner LM, Fath T, Ke YD, et al. 2008. Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia. Proc Natl Acad Sci U S A, 105:15997-16002.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15997-16002
    • Ittner, L.M.1    Fath, T.2    Ke, Y.D.3
  • 70
    • 0032433258 scopus 로고    scopus 로고
    • Beta-amyloid induces local neurite degeneration in cultured hippocampal neurons: Evidence for neuritic apoptosis
    • Ivins KJ, Bui ET, Cotman CW. 1998. Beta-amyloid induces local neurite degeneration in cultured hippocampal neurons: evidence for neuritic apoptosis. Neurobiol Dis, 5:365-78.
    • (1998) Neurobiol Dis , vol.5 , pp. 365-378
    • Ivins, K.J.1    Bui, E.T.2    Cotman, C.W.3
  • 71
    • 0034700471 scopus 로고    scopus 로고
    • A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus C, Pearson J, McLaurin J, et al. 2000. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature, 408:979-82.
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    McLaurin, J.3
  • 72
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha GA, Bowser R, Kazam IG, et al. 1997. Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J Neurosci Res, 48:128-32.
    • (1997) J Neurosci Res , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3
  • 73
    • 9644272489 scopus 로고    scopus 로고
    • Amyloid beta-induced changes in nitric oxide production and mitochondrial activity lead to apoptosis
    • Keil U, Bonert A, Marques CA, et al. 2004. Amyloid beta-induced changes in nitric oxide production and mitochondrial activity lead to apoptosis. J Biol Chem, 279:50310-20.
    • (2004) J Biol Chem , vol.279 , pp. 50310-50320
    • Keil, U.1    Bonert, A.2    Marques, C.A.3
  • 74
    • 0035851175 scopus 로고    scopus 로고
    • 200l. Reduced PP2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • Kins S, Crameri A, Evans DR, et al. 200l. Reduced PP2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J Biol Chem, 276:38193-200.
    • J Biol Chem , vol.276 , pp. 38193-38200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3
  • 75
    • 0042679510 scopus 로고    scopus 로고
    • Activation of the ERK and JNK signaling pathways caused by neuron specific inhibition of PP2A in transgenic mice
    • Kins S, Kurosinski P, Nitsch RM, et al. 2003. Activation of the ERK and JNK signaling pathways caused by neuron specific inhibition of PP2A in transgenic mice. Am J Pathol, 163:833-43.
    • (2003) Am J Pathol , vol.163 , pp. 833-843
    • Kins, S.1    Kurosinski, P.2    Nitsch, R.M.3
  • 76
    • 21044453723 scopus 로고    scopus 로고
    • Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo
    • Klyubin I, Walsh DM, Lemere CA, et al. 2005. Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo. Nat Med, 11:556-61.
    • (2005) Nat Med , vol.11 , pp. 556-561
    • Klyubin, I.1    Walsh, D.M.2    Lemere, C.A.3
  • 77
    • 33645049049 scopus 로고    scopus 로고
    • Active immunization trial in Abeta42-injected P301L tau transgenic mice
    • Kulic L, Kurosinski P, Chen F, et al. 2006. Active immunization trial in Abeta42-injected P301L tau transgenic mice. Neurobiol Dis, 22:50-6.
    • (2006) Neurobiol Dis , vol.22 , pp. 50-56
    • Kulic, L.1    Kurosinski, P.2    Chen, F.3
  • 78
    • 0036792783 scopus 로고    scopus 로고
    • Glial cells under physiologic and pathological conditions
    • Kurosinski P, Gotz J. 2002. Glial cells under physiologic and pathological conditions. Arch Neurol, 59:1524-8.
    • (2002) Arch Neurol , vol.59 , pp. 1524-1528
    • Kurosinski, P.1    Gotz, J.2
  • 79
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta-1 -42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, et al. 1998. Diffusible, nonfibrillar ligands derived from Abeta-1 -42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A, 95:6448-53.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 80
    • 31344436145 scopus 로고    scopus 로고
    • Amyloid-beta peptide disruption of lipid membranes and the effect of metal ions
    • Lau TL, Ambroggio EE, Tew D J, et al. 2006. Amyloid-beta peptide disruption of lipid membranes and the effect of metal ions. J Mol Biol, 356:759-70.
    • (2006) J Mol Biol , vol.356 , pp. 759-770
    • Lau, T.L.1    Ambroggio, E.E.2    Tew, D.J.3
  • 81
    • 0344505849 scopus 로고    scopus 로고
    • Tan interacts with src-family non-receptor tyrosine kinases
    • Lee G, Newman ST, Gard DL, et al. 1998. Tan interacts with src-family non-receptor tyrosine kinases. J Cell Sci, 111:3167-77.
    • (1998) J Cell Sci , vol.111 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3
  • 83
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S, Koh MT, Kotilinek L, et al. 2006. A specific amyloid-beta protein assembly in the brain impairs memory. Nature, 440:352-7.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 84
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant Tau and APP
    • Lewis J, Dickson DW, Lin W-L, et al. 2001. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant Tau and APP. Science, 293:1487-91.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.-L.3
  • 85
    • 44749083630 scopus 로고    scopus 로고
    • Human but not rat amylin shares neurotoxic properties with Abeta42 in long-term hippocampal and cortical cultures
    • Lim YA, Ittner LM, Lim YL, et al. 2008. Human but not rat amylin shares neurotoxic properties with Abeta42 in long-term hippocampal and cortical cultures. FEBS Lett, 582:2188-94.
    • (2008) FEBS Lett , vol.582 , pp. 2188-2194
    • Lim, Y.A.1    Ittner, L.M.2    Lim, Y.L.3
  • 86
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin H, Bhatia R, Lal R. 2001. Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. Faseb J, 15:2433-44.
    • (2001) Faseb J , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 87
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C, et al. 2004. ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science, 304:448-52.
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 88
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E, et al. 2006. Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet, 15:1437-49.
    • (2006) Hum Mol Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3
  • 89
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • Masters CL, Simms G, Weinman NA, et al. 1985. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc Natl Acad Sci U S A, 82:4245-9.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 4245-4249
    • Masters, C.L.1    Simms, G.2    Weinman, N.A.3
  • 90
    • 0041344592 scopus 로고    scopus 로고
    • Activation of the c-Jun N-terminal kinase signaling cascade mediates the effect of amyloid-beta on long term potentiation and cell death in hippocampus: A role for interleukin- 1beta?
    • Minogue AM, Schmid AW, Fogarty MP, et al. 2003. Activation of the c-Jun N-terminal kinase signaling cascade mediates the effect of amyloid-beta on long term potentiation and cell death in hippocampus: a role for interleukin- 1beta? J Biol Chem, 278:27971-80.
    • (2003) J Biol Chem , vol.278 , pp. 27971-27980
    • Minogue, A.M.1    Schmid, A.W.2    Fogarty, M.P.3
  • 91
    • 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
    • Mucke L, Masliah E, Yu GQ, 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, 20:4050-8.
    • (2000) J Neurosci , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3
  • 92
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula M, Kayed R, Milton S, et al. 2007. Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem, 282:10311-24.
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3
  • 93
    • 33846815066 scopus 로고    scopus 로고
    • TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations
    • Neumann M, Mackenzie IR, Cairns N J, et al. 2007. TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations. J Neuropathol Exp Neurol, 66:152-7.
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 152-157
    • Neumann, M.1    Mackenzie, I.R.2    Cairns, N.J.3
  • 94
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampatbu DM, Kwong LK, et al. 2006. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science, 314:130-3.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampatbu, D.M.2    Kwong, L.K.3
  • 95
    • 34548503149 scopus 로고    scopus 로고
    • Treatment and prevention of mental disorders in low-income and middle-income countries
    • Patel V, Araya R, Chatterjee S, et al. 2007. Treatment and prevention of mental disorders in low-income and middle-income countries. Lancet, 370:991-1005.
    • (2007) Lancet , vol.370 , pp. 991-1005
    • Patel, V.1    Araya, R.2    Chatterjee, S.3
  • 96
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the aggregation kinetics of amyloid peptides
    • Pellarin R, Caflisch A. 2006. Interpreting the aggregation kinetics of amyloid peptides. J Mol Biol, 360:882-92.
    • (2006) J Mol Biol , vol.360 , pp. 882-892
    • Pellarin, R.1    Caflisch, A.2
  • 97
    • 27144469504 scopus 로고    scopus 로고
    • Different tau epitopes define Abeta(42)-mediated tau insolubility
    • Pennanen L, Gotz J. 2005. Different tau epitopes define Abeta(42)-mediated tau insolubility. Biochem Biophys Res Coramun, 337:1097-101.
    • (2005) Biochem Biophys Res Coramun , vol.337 , pp. 1097-1101
    • Pennanen, L.1    Gotz, J.2
  • 98
    • 1842431831 scopus 로고    scopus 로고
    • Accelerated extinction of conditioned taste aversion in P301L tau transgenic mice
    • Pennanen L, Welzl H, D'Adamo P, et al. 2004. Accelerated extinction of conditioned taste aversion in P301L tau transgenic mice. Neurobiol Dis, 15:500-9.
    • (2004) Neurobiol Dis , vol.15 , pp. 500-509
    • Pennanen, L.1    Welzl, H.2    D'Adamo, P.3
  • 99
    • 33745699023 scopus 로고    scopus 로고
    • Impaired spatial reference memory and increased exploratory behavior in P301L tau transgenic mice
    • Pennanen L, Wolfer DP, Nitsch RIM, et al. 2006. Impaired spatial reference memory and increased exploratory behavior in P301L tau transgenic mice. Genes Brain Behav, 5:369-79.
    • (2006) Genes Brain Behav , vol.5 , pp. 369-379
    • Pennanen, L.1    Wolfer, D.P.2    Nitsch, R.I.M.3
  • 100
    • 0036534870 scopus 로고    scopus 로고
    • Role ofp 75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines
    • Perini G, Della-Bianca V, Politi V, et al. 2002. Role ofp 75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines. J Exp Med, 195:907-18.
    • (2002) J Exp Med , vol.195 , pp. 907-918
    • Perini, G.1    Della-Bianca, V.2    Politi, V.3
  • 101
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike C J, Burdick D, Walencewicz AJ, et al. 1993. Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J Neurosci, 13:1676-87.
    • (1993) J Neurosci , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3
  • 102
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures
    • Pike CJ, Walencewicz AJ, Glabe CG, et al. 1991a. Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures. Eur J Pharmacol, 207:367-8.
    • (1991) Eur J Pharmacol , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3
  • 103
    • 0025992417 scopus 로고
    • In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG, et al. 1991b. In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res, 563:311-4.
    • (1991) Brain Res , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3
  • 104
    • 0029586704 scopus 로고
    • Ion channel hypothesis for Alzheimer amyloid peptide neurotoxicity
    • Pollard HB, Arispe N, Roj as E. 1995. Ion channel hypothesis for Alzheimer amyloid peptide neurotoxicity. Cell Mol Neurobiol, 15:513-26.
    • (1995) Cell Mol Neurobiol , vol.15 , pp. 513-526
    • Pollard, H.B.1    Arispe, N.2    Roj as, E.3
  • 105
    • 14444284106 scopus 로고    scopus 로고
    • Tau is a candidate gene for chromosome 17 frontotemporal dementia
    • Poorkaj P, Bird TD, Wijsman E, et al. 1998. Tau is a candidate gene for chromosome 17 frontotemporal dementia. Ann Neurol, 43:815-25.
    • (1998) Ann Neurol , vol.43 , pp. 815-825
    • Poorkaj, P.1    Bird, T.D.2    Wijsman, E.3
  • 106
    • 0342803685 scopus 로고    scopus 로고
    • Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein
    • Probst A, Gotz J, Wiederhold KH, et al. 2000. Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein. Acta Neuropathol (Berl), 99:469-81.
    • (2000) Acta Neuropathol (Berl) , vol.99 , pp. 469-481
    • Probst, A.1    Gotz, J.2    Wiederhold, K.H.3
  • 107
  • 108
    • 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 J J, et al. 2007. Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science, 316:750-4.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3
  • 109
    • 0038240721 scopus 로고    scopus 로고
    • Causative and susceptibility genes for Alzheimer's disease: A review
    • Rocchi A, Pellegrini S, Siciliano G, et al. 2003. Causative and susceptibility genes for Alzheimer's disease: a review. Brain Res Bull, 61:1-24.
    • (2003) Brain Res Bull , vol.61 , pp. 1-24
    • Rocchi, A.1    Pellegrini, S.2    Siciliano, G.3
  • 110
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ. 2002. Alzheimer's disease is a synaptic failure. Science, 298: 789 91.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 111
    • 0034521392 scopus 로고    scopus 로고
    • Clearance of Alzheimer's amyloid-beta(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier
    • Shibata M, Yamada S, Kumar SR, et al. 2000. Clearance of Alzheimer's amyloid-beta(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier. J Clin Invest, 106:1489-99.
    • (2000) J Clin Invest , vol.106 , pp. 1489-1499
    • Shibata, M.1    Yamada, S.2    Kumar, S.R.3
  • 112
    • 0035433962 scopus 로고    scopus 로고
    • OPINION Alzheimer's disease and Abeta toxicity: From top to bottom
    • Small DH, Mok SS, Bornstein JC. 2001. OPINION Alzheimer's disease and Abeta toxicity: from top to bottom. Nat Rev Neurosci, 2:595-8.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 595-598
    • Small, D.H.1    Mok, S.S.2    Bornstein, J.C.3
  • 113
    • 33947265861 scopus 로고    scopus 로고
    • Concentration dependent Cu2+ induced aggregation and dityrosine formation of the Alzheimer's disease amyloid-beta peptide
    • Smith DP, Ciccotosto GD, Tew DJ, et al. 2007. Concentration dependent Cu2+ induced aggregation and dityrosine formation of the Alzheimer's disease amyloid-beta peptide. Biochemistry, 46:2881-91.
    • (2007) Biochemistry , vol.46 , pp. 2881-2891
    • Smith, D.P.1    Ciccotosto, G.D.2    Tew, D.J.3
  • 114
    • 0035086145 scopus 로고    scopus 로고
    • Distinct behavioural profiles in frontotemporal dementia and semantic dementia
    • Snowden JS, Bathgate D, Varma A, et al. 2001. Distinct behavioural profiles in frontotemporal dementia and semantic dementia. J Neurol Neurosurg Psychiatry, 70:323-32.
    • (2001) J Neurol Neurosurg Psychiatry , vol.70 , pp. 323-332
    • Snowden, J.S.1    Bathgate, D.2    Varma, A.3
  • 115
    • 23044445669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking by amyloid-beta
    • Snyder EM, Nong Y, Almeida CG, et al. 2005. Regulation of NMDA receptor trafficking by amyloid-beta. Nat Neurosci, 8:1051-8.
    • (2005) Nat Neurosci , vol.8 , pp. 1051-1058
    • Snyder, E.M.1    Nong, Y.2    Almeida, C.G.3
  • 116
    • 43049180249 scopus 로고    scopus 로고
    • Beta-amyloid (1-42) induces neuronal death through the p 75 neurotrophin receptor
    • Sotthibundhu A, Sykes AM, Fox B, et al. 2008. Beta-amyloid (1-42) induces neuronal death through the p 75 neurotrophin receptor. J Neurosci, 28:3941-6.
    • (2008) J Neurosci , vol.28 , pp. 3941-3946
    • Sotthibundhu, A.1    Sykes, A.M.2    Fox, B.3
  • 117
    • 0032560487 scopus 로고    scopus 로고
    • Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
    • Spillantini MG, Murrell JR, Goedert M, et al. 1998. Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc Natl Acad Sci U S A, 95:7737-41.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7737-7741
    • Spillantini, M.G.1    Murrell, J.R.2    Goedert, M.3
  • 118
    • 0032786370 scopus 로고    scopus 로고
    • Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein
    • Spittaels K, Van den Haute C, Van Dorpe J, et al. 1999. Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein. Am J Pathol, 155:2153-65.
    • (1999) Am J Pathol , vol.155 , pp. 2153-2165
    • Spittaels, K.1    Van den Haute, C.2    Van Dorpe, J.3
  • 119
    • 0032983536 scopus 로고    scopus 로고
    • Association of microglia with amyloid plaques in brains of APP23 transgenic mice
    • Stalder M, Phinney A, Probst A, et al. 1999. Association of microglia with amyloid plaques in brains of APP23 transgenic mice. Am J Pathol, 154:1673-84.
    • (1999) Am J Pathol , vol.154 , pp. 1673-1684
    • Stalder, M.1    Phinney, A.2    Probst, A.3
  • 120
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • Stine WB, Jr., Dahlgren KN, Krafft GA, et al. 2003. In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J Biol Chem, 278:11612-22.
    • (2003) J Biol Chem , vol.278 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3
  • 121
    • 0011444914 scopus 로고    scopus 로고
    • Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
    • Sturchler-Pierrat C, Abramowski D, Duke M, et al. 1997. Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology. Proc Natl Acad Sci U S A, 94:13287-92.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13287-13292
    • Sturchler-Pierrat, C.1    Abramowski, D.2    Duke, M.3
  • 122
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction
    • Takuma K, Yao J, Huang J, et al. 2005. ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction. Faseb J, 19:597-8.
    • (2005) Faseb J , vol.19 , pp. 597-598
    • Takuma, K.1    Yao, J.2    Huang, J.3
  • 123
    • 19944429503 scopus 로고    scopus 로고
    • ApoE isoform-specific effects. on LTP: Blockade by oligomeric amyloid-beta1-42
    • Trommer BL, Shah C, Yun SH, et al. 2005. ApoE isoform-specific effects. on LTP: blockade by oligomeric amyloid-beta1-42. Neurobiol Dis, 18:75-82.
    • (2005) Neurobiol Dis , vol.18 , pp. 75-82
    • Trommer, B.L.1    Shah, C.2    Yun, S.H.3
  • 124
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R, Bennett BD, Babu-Khan S, et al. 1999. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science, 286:735-41.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3
  • 125
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • Verdier Y, Zarandi M, Penke B. 2004. Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J Pept Sci, 10:229-48.
    • (2004) J Pept Sci , vol.10 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 126
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, et al. 2002. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature, 416:535-9.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 127
    • 27844432223 scopus 로고    scopus 로고
    • The role of cell-derived oligomers of Abeta in Alzheimer's disease and avenues for therapeutic intervention
    • Walsh DM, Klyubin I, Shankar GM, et al. 2005. The role of cell-derived oligomers of Abeta in Alzheimer's disease and avenues for therapeutic intervention. Biockem Soc Trans, 33:1087-90.
    • (2005) Biockem Soc Trans , vol.33 , pp. 1087-1090
    • Walsh, D.M.1    Klyubin, I.2    Shankar, G.M.3
  • 128
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid beta-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p 38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang Q, Walsh DM, Rowan M J, et al. 2004. Block of long-term potentiation by naturally secreted and synthetic amyloid beta-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p 38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J Neurosci, 24:3370-8.
    • (2004) J Neurosci , vol.24 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3
  • 130
    • 33947261641 scopus 로고    scopus 로고
    • Intraneuronal Abeta immunoreactivity is not a predictor of brain amyloidosis-beta or neurofibrillary degeneration
    • Wegiel J, Kuchna I, Nowicki K, et al. 2007. Intraneuronal Abeta immunoreactivity is not a predictor of brain amyloidosis-beta or neurofibrillary degeneration. Acta Neuropathol, 113:389-402.
    • (2007) Acta Neuropathol , vol.113 , pp. 389-402
    • Wegiel, J.1    Kuchna, I.2    Nowicki, K.3
  • 131
    • 0035029801 scopus 로고    scopus 로고
    • Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression ofproapoptotic markers in primary cortical neurons
    • White AR, Guirguis R, Brazier MW, et al. 2001. Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression ofproapoptotic markers in primary cortical neurons. Neurobiol Dis, 8:299-316.
    • (2001) Neurobiol Dis , vol.8 , pp. 299-316
    • White, A.R.1    Guirguis, R.2    Brazier, M.W.3
  • 132
    • 14744283139 scopus 로고    scopus 로고
    • Differential effects of oligomeric and fibrillar amyloid-beta 1-42 on astrocyte-mediated inflammation
    • White JA, Manelli AM, Holmberg KH, et al. 2005. Differential effects of oligomeric and fibrillar amyloid-beta 1-42 on astrocyte-mediated inflammation. Neurobiol Dis, 18:459-65.
    • (2005) Neurobiol Dis , vol.18 , pp. 459-465
    • White, J.A.1    Manelli, A.M.2    Holmberg, K.H.3
  • 133
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
    • Yan SD, Chen X, Fu J, et al. 1996. RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease. Nature, 382:685-91.
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3
  • 134
    • 33847051684 scopus 로고    scopus 로고
    • Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Abeta interaction
    • Yan Y, Liu Y, Sorci M, et al. 2007. Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Abeta interaction. Biochemistry, 46:1724-31.
    • (2007) Biochemistry , vol.46 , pp. 1724-1731
    • Yan, Y.1    Liu, Y.2    Sorci, M.3
  • 135
    • 34248586543 scopus 로고    scopus 로고
    • Abeta40 protects non-toxic Abeta42 monomer from aggregation
    • Yah Y, and Wang C. 2007. Abeta40 protects non-toxic Abeta42 monomer from aggregation. J Mol Biol, 369:909-16.
    • (2007) J Mol Biol , vol.369 , pp. 909-916
    • Yah, Y.1    Wang, C.2
  • 136
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner BA, Duffy LK, Kirschner DA. 1990. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science, 250:279-82.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 137
    • 0042738968 scopus 로고    scopus 로고
    • neurotrophin receptor protects primary cultures of human neurons against extracellular amyloid beta peptide cytotoxicity
    • Zhang Y, Hong Y, Bounhar Y, et al. 2003. p 75 neurotrophin receptor protects primary cultures of human neurons against extracellular amyloid beta peptide cytotoxicity. J Neurosci, 23:7385-94.
    • (2003) J Neurosci , vol.23 , pp. 7385-7394
    • Zhang, Y.1    Hong, Y.2    Bounhar, Y.3


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