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Volumn 67, Issue 2, 2009, Pages 127-135

Morphologic and molecular neuropathology of Alzheimer's disease;Neuropathologie morphologique et moléculaire de la maladie d'Alzheimer

Author keywords

A peptide; Alzheimer disease; Neurofibrillary tangle; Neuropathology; Senile plaque; Tau protein

Indexed keywords

AMYLOID BETA PROTEIN; TAU PROTEIN;

EID: 68649089942     PISSN: 00034509     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pharma.2009.01.001     Document Type: Article
Times cited : (6)

References (63)
  • 1
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy in Alzheimer's disease
    • Kidd M. Paired helical filaments in electron microscopy in Alzheimer's disease. Nature 197 (1963) 262-268
    • (1963) Nature , vol.197 , pp. 262-268
    • Kidd, M.1
  • 2
    • 0022257253 scopus 로고
    • Mise en évidence immunologique de la protéine tau au niveau des lésions de dégénérescence neurofibrillaire de la maladie d'Alzheimer
    • Brion J.P., Passareiro H., Nunez J., and Flament-Durand J. Mise en évidence immunologique de la protéine tau au niveau des lésions de dégénérescence neurofibrillaire de la maladie d'Alzheimer. Arch Biol (Brux) 95 (1985) 229-235
    • (1985) Arch Biol (Brux) , vol.95 , pp. 229-235
    • Brion, J.P.1    Passareiro, H.2    Nunez, J.3    Flament-Durand, J.4
  • 3
    • 0025284610 scopus 로고
    • Pathological proteins Tau 64 and 69 are specifically expressed in the somatodendritic domain of the degenerating cortical neurons during Alzheimer's disease. Demonstration with a panel of antibodies against Tau proteins
    • Delacourte A., Flament S., Dibe E.M., Hublau P., Sablonniere B., Hemon B., et al. Pathological proteins Tau 64 and 69 are specifically expressed in the somatodendritic domain of the degenerating cortical neurons during Alzheimer's disease. Demonstration with a panel of antibodies against Tau proteins. Acta Neuropathol 80 (1990) 111-117
    • (1990) Acta Neuropathol , vol.80 , pp. 111-117
    • Delacourte, A.1    Flament, S.2    Dibe, E.M.3    Hublau, P.4    Sablonniere, B.5    Hemon, B.6
  • 4
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein Tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain
    • Goedert M., Spillantini M.G., Potier M.C., Ulrich J., and Crowther R.A. Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein Tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. Embo J 8 (1989) 393-399
    • (1989) Embo J , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 5
    • 0023912552 scopus 로고
    • Neuropil threads occur in dendrites of tangle-bearing nerve cells
    • Braak H., and Braak E. Neuropil threads occur in dendrites of tangle-bearing nerve cells. Neuropathol Appl Neurobiol 14 (1988) 39-44
    • (1988) Neuropathol Appl Neurobiol , vol.14 , pp. 39-44
    • Braak, H.1    Braak, E.2
  • 6
    • 0025905505 scopus 로고
    • Comparative epitope analysis of neuronal cytoskeletal proteins in Alzheimer's disease senile plaque, neurites and neuropil threads
    • Schmidt M., Lee V., and Trojanowski J. Comparative epitope analysis of neuronal cytoskeletal proteins in Alzheimer's disease senile plaque, neurites and neuropil threads. Lab Invest 64 (1991) 352-357
    • (1991) Lab Invest , vol.64 , pp. 352-357
    • Schmidt, M.1    Lee, V.2    Trojanowski, J.3
  • 7
    • 0000930795 scopus 로고
    • Étude histochimique des plaques séniles
    • Divry P. Étude histochimique des plaques séniles. J Belge Neurol Psych 9 (1927) 643-657
    • (1927) J Belge Neurol Psych , vol.9 , pp. 643-657
    • Divry, P.1
  • 8
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis. The ß-fibrilloses
    • 1333-1343
    • Glenner G.G. Amyloid deposits and amyloidosis. The ß-fibrilloses. N Engl J Med 302 (1980) 1283-1292 1333-1343
    • (1980) N Engl J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 9
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G.G., and Wong C.W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120 (1984) 885-890
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 10
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J., Lemaire H.-G., Unterbeck A., Salbaum J.M., Masters C.L., Grzeschik K.H., et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325 (1987) 733-736
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.-G.2    Unterbeck, A.3    Salbaum, J.M.4    Masters, C.L.5    Grzeschik, K.H.6
  • 11
    • 0026075602 scopus 로고
    • Early-onset Alzheimer's disease caused by mutations at codon 717 of the ß-amyloid precursor protein gene
    • Chartier-Harlin M.C., Crawford F., Houlden H., Warren A., Hughes D., Fidani L., et al. Early-onset Alzheimer's disease caused by mutations at codon 717 of the ß-amyloid precursor protein gene. Nature 353 (1991) 844-846
    • (1991) Nature , vol.353 , pp. 844-846
    • Chartier-Harlin, M.C.1    Crawford, F.2    Houlden, H.3    Warren, A.4    Hughes, D.5    Fidani, L.6
  • 12
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R., Bennett B.D., Babu-Khan S., Kahn S., Mendiaz E.A., Denis P., et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286 (1999) 735-741
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3    Kahn, S.4    Mendiaz, E.A.5    Denis, P.6
  • 14
    • 33947597857 scopus 로고    scopus 로고
    • GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42
    • Munter L.M., Voigt P., Harmeier A., Kaden D., Gottschalk K.E., Weise C., et al. GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42. Embo J 26 (2007) 1702-1712
    • (2007) Embo J , vol.26 , pp. 1702-1712
    • Munter, L.M.1    Voigt, P.2    Harmeier, A.3    Kaden, D.4    Gottschalk, K.E.5    Weise, C.6
  • 15
    • 12444337654 scopus 로고    scopus 로고
    • Truncated beta-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach
    • Sergeant N., Bombois S., Ghestem A., Drobecq H., Kostanjevecki V., Missiaen C., et al. Truncated beta-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach. J Neurochem 85 (2003) 1581-1591
    • (2003) J Neurochem , vol.85 , pp. 1581-1591
    • Sergeant, N.1    Bombois, S.2    Ghestem, A.3    Drobecq, H.4    Kostanjevecki, V.5    Missiaen, C.6
  • 16
    • 0026065020 scopus 로고
    • Subtypes and differential laminar distributions of ßA4 deposits in Alzheimer's disease: relationship with the intellectual status of 26 cases
    • Delaère P., Duyckaerts C., He Y., Piette F., and Hauw J.-J. Subtypes and differential laminar distributions of ßA4 deposits in Alzheimer's disease: relationship with the intellectual status of 26 cases. Acta Neuropathol (Berl) 81 (1991) 328-335
    • (1991) Acta Neuropathol (Berl) , vol.81 , pp. 328-335
    • Delaère, P.1    Duyckaerts, C.2    He, Y.3    Piette, F.4    Hauw, J.-J.5
  • 17
    • 0037411517 scopus 로고    scopus 로고
    • A grading system of Alzheimer disease lesions in neocortical areas
    • Metsaars W.P., Hauw J.J., Welsem M.E., and Duyckaerts C. A grading system of Alzheimer disease lesions in neocortical areas. Neurobiol Aging 24 (2003) 563-572
    • (2003) Neurobiol Aging , vol.24 , pp. 563-572
    • Metsaars, W.P.1    Hauw, J.J.2    Welsem, M.E.3    Duyckaerts, C.4
  • 19
    • 0034295217 scopus 로고    scopus 로고
    • Microglia cells are the driving force in fibrillar plaque formation, whereas astrocytes are a leading factor in plaque degradation
    • Wegiel J., Wang K.C., Tarnawski M., and Lach B. Microglia cells are the driving force in fibrillar plaque formation, whereas astrocytes are a leading factor in plaque degradation. Acta Neuropathol (Berl) 100 (2000) 356-364
    • (2000) Acta Neuropathol (Berl) , vol.100 , pp. 356-364
    • Wegiel, J.1    Wang, K.C.2    Tarnawski, M.3    Lach, B.4
  • 20
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D., Barbour R., Dunn W., Gordon G., Grajeda H., Guido T., et al. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400 (1999) 173-177
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    Gordon, G.4    Grajeda, H.5    Guido, T.6
  • 21
    • 7244236841 scopus 로고    scopus 로고
    • A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide: the first step of a fatal cascade
    • Wirths O., Multhaup G., and Bayer T.A. A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide: the first step of a fatal cascade. J Neurochem 91 (2004) 513-520
    • (2004) J Neurochem , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 22
    • 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., Frackowiak J., Mazur-Kolecka B., Imaki H., et al. Intraneuronal Abeta immunoreactivity is not a predictor of brain amyloidosis-beta or neurofibrillary degeneration. Acta Neuropathol (Berl) 113 (2007) 389-402
    • (2007) Acta Neuropathol (Berl) , vol.113 , pp. 389-402
    • Wegiel, J.1    Kuchna, I.2    Nowicki, K.3    Frackowiak, J.4    Mazur-Kolecka, B.5    Imaki, H.6
  • 23
    • 27944496889 scopus 로고    scopus 로고
    • Apolipoprotein E co-localizes with newly formed amyloid beta-protein (Abeta) deposits lacking immunoreactivity against N-terminal epitopes of Abeta in a genotype-dependent manner
    • Thal D.R., Capetillo-Zarate E., Schultz C., Rub U., Saido T.C., Yamaguchi H., et al. Apolipoprotein E co-localizes with newly formed amyloid beta-protein (Abeta) deposits lacking immunoreactivity against N-terminal epitopes of Abeta in a genotype-dependent manner. Acta Neuropathol 110 (2005) 459-471
    • (2005) Acta Neuropathol , vol.110 , pp. 459-471
    • Thal, D.R.1    Capetillo-Zarate, E.2    Schultz, C.3    Rub, U.4    Saido, T.C.5    Yamaguchi, H.6
  • 25
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H., and Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol (Berl) 82 (1991) 239-259
    • (1991) Acta Neuropathol (Berl) , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 26
    • 0037172826 scopus 로고    scopus 로고
    • Phases of Abeta-deposition in the human brain and its relevance for the development of AD
    • Thal D.R., Rub U., Orantes M., and Braak H. Phases of Abeta-deposition in the human brain and its relevance for the development of AD. Neurology 58 (2002) 1791-1800
    • (2002) Neurology , vol.58 , pp. 1791-1800
    • Thal, D.R.1    Rub, U.2    Orantes, M.3    Braak, H.4
  • 27
    • 0344653664 scopus 로고    scopus 로고
    • Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
    • Gomez-Isla T., Hollister R., West H., Mui S., Growdon J.H., Petersen R.C., et al. Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease. Ann Neurol 41 (1997) 17-24
    • (1997) Ann Neurol , vol.41 , pp. 17-24
    • Gomez-Isla, T.1    Hollister, R.2    West, H.3    Mui, S.4    Growdon, J.H.5    Petersen, R.C.6
  • 28
    • 0031913355 scopus 로고    scopus 로고
    • Cytoarchitectonic alterations in the supramarginal gyrus of late onset Alzheimer's disease
    • Grignon Y., Duyckaerts C., Bennecib M., and Hauw J.-J. Cytoarchitectonic alterations in the supramarginal gyrus of late onset Alzheimer's disease. Acta Neuropathol (Berl) 95 (1998) 395-406
    • (1998) Acta Neuropathol (Berl) , vol.95 , pp. 395-406
    • Grignon, Y.1    Duyckaerts, C.2    Bennecib, M.3    Hauw, J.-J.4
  • 29
    • 0028918383 scopus 로고
    • Extracellular neurofibrillary tangles reflect neuronal loss and provide further evidence of extensive protein cross-linking in Alzheimer disease
    • Cras P., Smith M.A., Richey P.L., Siedlak S.L., Mulvihill P., and Perry G. Extracellular neurofibrillary tangles reflect neuronal loss and provide further evidence of extensive protein cross-linking in Alzheimer disease. Acta Neuropathol (Berl) 89 (1995) 291-295
    • (1995) Acta Neuropathol (Berl) , vol.89 , pp. 291-295
    • Cras, P.1    Smith, M.A.2    Richey, P.L.3    Siedlak, S.L.4    Mulvihill, P.5    Perry, G.6
  • 30
    • 0031958152 scopus 로고    scopus 로고
    • Apoptosis decision cascades and neuronal degeneration in Alzheimer's disease
    • Cotman C.W. Apoptosis decision cascades and neuronal degeneration in Alzheimer's disease. Neurobiol Aging 19 (1998) S29-32
    • (1998) Neurobiol Aging , vol.19
    • Cotman, C.W.1
  • 31
    • 0032747486 scopus 로고    scopus 로고
    • Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease: evidence for apoptotic cell death
    • Stadelmann C., Deckwerth T.L., Srinivasan A., Bancher C., Bruck W., Jellinger K., et al. Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease: evidence for apoptotic cell death. Am J Pathol 155 (1999) 1459-1466
    • (1999) Am J Pathol , vol.155 , pp. 1459-1466
    • Stadelmann, C.1    Deckwerth, T.L.2    Srinivasan, A.3    Bancher, C.4    Bruck, W.5    Jellinger, K.6
  • 32
    • 0035141757 scopus 로고    scopus 로고
    • Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease
    • Rohn T.T., Head E., Su J.H., Anderson A.J., Bahr B.A., Cotman C.W., et al. Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease. Am J Pathol 158 (2001) 189-198
    • (2001) Am J Pathol , vol.158 , pp. 189-198
    • Rohn, T.T.1    Head, E.2    Su, J.H.3    Anderson, A.J.4    Bahr, B.A.5    Cotman, C.W.6
  • 33
    • 0031661968 scopus 로고    scopus 로고
    • The cell division cycle and the pathophysiology of Alzheimer's disease
    • Nagy Z., Esiri M.M., and Smith A.D. The cell division cycle and the pathophysiology of Alzheimer's disease. Neuroscience 87 (1998) 731-739
    • (1998) Neuroscience , vol.87 , pp. 731-739
    • Nagy, Z.1    Esiri, M.M.2    Smith, A.D.3
  • 34
    • 0031891362 scopus 로고    scopus 로고
    • Laminar spongiosis of the dentate gyrus: a sign of disconnection, present in cases of Alzheimer disease
    • Duyckaerts C., Colle M.A., Seilhean D., and Hauw J.-J. Laminar spongiosis of the dentate gyrus: a sign of disconnection, present in cases of Alzheimer disease. Acta Neuropathol (Berl) 95 (1998) 413-420
    • (1998) Acta Neuropathol (Berl) , vol.95 , pp. 413-420
    • Duyckaerts, C.1    Colle, M.A.2    Seilhean, D.3    Hauw, J.-J.4
  • 35
    • 0000354585 scopus 로고
    • Structural basis of the cognitive alterations in Alzheimer disease
    • Terry R.D., Katzman R., and Bick K.L. (Eds), Raven Press, New York
    • Terry D., Masliah E., and Hansen L.A. Structural basis of the cognitive alterations in Alzheimer disease. In: Terry R.D., Katzman R., and Bick K.L. (Eds). Alzheimer disease (1994), Raven Press, New York 179-196
    • (1994) Alzheimer disease , pp. 179-196
    • Terry, D.1    Masliah, E.2    Hansen, L.A.3
  • 36
    • 84880185901 scopus 로고    scopus 로고
    • Alzheimer's disease-related alterations in synaptic density: neocortex and hippocampus
    • Scheff S.W., and Price D.A. Alzheimer's disease-related alterations in synaptic density: neocortex and hippocampus. J Alzheimers Dis 9 (2006) 101-115
    • (2006) J Alzheimers Dis , vol.9 , pp. 101-115
    • Scheff, S.W.1    Price, D.A.2
  • 37
    • 0024364877 scopus 로고
    • Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease
    • Masliah E., Terry R.D., DeTeresa R.M., and Hansen L.A. Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease. Neurosci Lett 103 (1989) 234-239
    • (1989) Neurosci Lett , vol.103 , pp. 234-239
    • Masliah, E.1    Terry, R.D.2    DeTeresa, R.M.3    Hansen, L.A.4
  • 38
    • 0031577277 scopus 로고    scopus 로고
    • Differential involvement of synaptic vesicle and presynaptic plasma membrane proteins in Alzheimer's disease
    • Shimohama S., Kamiya S., Taniguchi T., Akagawa K., and Kimura J. Differential involvement of synaptic vesicle and presynaptic plasma membrane proteins in Alzheimer's disease. Biochem Biophys Res Commun 236 (1997) 239-242
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 239-242
    • Shimohama, S.1    Kamiya, S.2    Taniguchi, T.3    Akagawa, K.4    Kimura, J.5
  • 40
    • 0031710604 scopus 로고    scopus 로고
    • Evidence for synaptic apoptosis
    • Mattson M., Keller J., and Begley J. Evidence for synaptic apoptosis. Exp Neurol 153 (1998) 35-48
    • (1998) Exp Neurol , vol.153 , pp. 35-48
    • Mattson, M.1    Keller, J.2    Begley, J.3
  • 42
    • 0030805991 scopus 로고    scopus 로고
    • Frequency of stages of Alzheimer-related lesions in different age categories
    • Braak H., and Braak E. Frequency of stages of Alzheimer-related lesions in different age categories. Neurobiol Aging 18 (1997) 351-357
    • (1997) Neurobiol Aging , vol.18 , pp. 351-357
    • Braak, H.1    Braak, E.2
  • 43
    • 0030823304 scopus 로고    scopus 로고
    • Prevalence, incidence and duration of Braak's stages in the general population: can we know?
    • Duyckaerts C., and Hauw J.-J. Prevalence, incidence and duration of Braak's stages in the general population: can we know?. Neurobiol Aging 18 (1997) 362-369
    • (1997) Neurobiol Aging , vol.18 , pp. 362-369
    • Duyckaerts, C.1    Hauw, J.-J.2
  • 44
    • 0035915621 scopus 로고    scopus 로고
    • Pathological correlates of late-onset dementia in a multicentre, community-based population in England and Wales
    • Neuropathology group of the medical research council cognitive function and ageing study
    • Neuropathology group of the medical research council cognitive function and ageing study. Pathological correlates of late-onset dementia in a multicentre, community-based population in England and Wales. Lancet 2001;357:169-75.
    • (2001) Lancet , vol.357 , pp. 169-175
  • 45
    • 36949016215 scopus 로고    scopus 로고
    • Alzheimer disease models and human neuropathology: similarities and differences
    • Duyckaerts C., Potier M.C., and Delatour B. Alzheimer disease models and human neuropathology: similarities and differences. Acta Neuropathol 115 (2008) 5-38
    • (2008) Acta Neuropathol , vol.115 , pp. 5-38
    • Duyckaerts, C.1    Potier, M.C.2    Delatour, B.3
  • 46
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1
    • Duff K., Eckman C., Zehr C., Yu X., Prada C.M., Perez-tur J., et al. Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1. Nature 383 (1996) 710-713
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3    Yu, X.4    Prada, C.M.5    Perez-tur, J.6
  • 47
    • 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 J.M., Blanchard V., Wirths O., van der Kolk N., et al. Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model. Am J Pathol 165 (2004) 1289-1300
    • (2004) Am J Pathol , vol.165 , pp. 1289-1300
    • Casas, C.1    Sergeant, N.2    Itier, J.M.3    Blanchard, V.4    Wirths, O.5    van der Kolk, N.6
  • 48
    • 33646560610 scopus 로고    scopus 로고
    • Mechanism of cerebral beta-amyloid angiopathy: murine and cellular models
    • Herzig M.C., Van Nostrand W.E., and Jucker M. Mechanism of cerebral beta-amyloid angiopathy: murine and cellular models. Brain Pathol 16 (2006) 40-54
    • (2006) Brain Pathol , vol.16 , pp. 40-54
    • Herzig, M.C.1    Van Nostrand, W.E.2    Jucker, M.3
  • 49
    • 0033621739 scopus 로고    scopus 로고
    • Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition
    • Iwata N., Tsubuki S., Takaki Y., Watanabe K., Sekiguchi M., Hosoki E., et al. Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat Med 6 (2000) 143-150
    • (2000) Nat Med , vol.6 , pp. 143-150
    • Iwata, N.1    Tsubuki, S.2    Takaki, Y.3    Watanabe, K.4    Sekiguchi, M.5    Hosoki, E.6
  • 50
    • 36949038023 scopus 로고    scopus 로고
    • Loss of neprilysin function promotes amyloid plaque formation and causes cerebral amyloid angiopathy
    • Farris W., Schutz S.G., Cirrito J.R., Shankar G.M., Sun X., George A., et al. Loss of neprilysin function promotes amyloid plaque formation and causes cerebral amyloid angiopathy. J Neurosci 27 (2007) 2866-2875
    • (2007) J Neurosci , vol.27 , pp. 2866-2875
    • Farris, W.1    Schutz, S.G.2    Cirrito, J.R.3    Shankar, G.M.4    Sun, X.5    George, A.6
  • 51
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin-1 transgenes
    • Holcomb L., Gordon M.N., McGowan E., Yu X., Benkovic S., Jantzen P., et al. Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin-1 transgenes. Nat Med 4 (1998) 97-100
    • (1998) Nat Med , vol.4 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3    Yu, X.4    Benkovic, S.5    Jantzen, P.6
  • 53
    • 3142668938 scopus 로고    scopus 로고
    • Cognitive correlates of Abeta deposition in male and female mice bearing amyloid precursor protein and presenilin-1 mutant transgenes
    • Howlett D.R., Richardson J.C., Austin A., Parsons A.A., Bate S.T., Davies D.C., et al. Cognitive correlates of Abeta deposition in male and female mice bearing amyloid precursor protein and presenilin-1 mutant transgenes. Brain Res 1017 (2004) 130-136
    • (2004) Brain Res , vol.1017 , pp. 130-136
    • Howlett, D.R.1    Richardson, J.C.2    Austin, A.3    Parsons, A.A.4    Bate, S.T.5    Davies, D.C.6
  • 54
    • 33846580960 scopus 로고    scopus 로고
    • Intact spatial learning in adult Tg2576 mice
    • Bizon J., Prescott S., and Nicolle M.M. Intact spatial learning in adult Tg2576 mice. Neurobiol Aging 28 (2007) 440-446
    • (2007) Neurobiol Aging , vol.28 , pp. 440-446
    • Bizon, J.1    Prescott, S.2    Nicolle, M.M.3
  • 55
    • 36949002076 scopus 로고    scopus 로고
    • Impairment of spatial memory consolidation in APP(751SL) mice results in cue-guided response
    • (Published ahead of print)
    • Blanchard J., Martel G., Guillou J.L., Nogues X., and Micheau J. Impairment of spatial memory consolidation in APP(751SL) mice results in cue-guided response. Neurobiol Aging (2007) (Published ahead of print)
    • (2007) Neurobiol Aging
    • Blanchard, J.1    Martel, G.2    Guillou, J.L.3    Nogues, X.4    Micheau, J.5
  • 56
    • 34548258322 scopus 로고    scopus 로고
    • Accelerating amyloid-beta fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models
    • Cheng I.H., Scearce-Levie K., Legleiter J., Palop J.J., Gerstein H., Bien-Ly N., et al. Accelerating amyloid-beta fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models. J Biol Chem 282 (2007) 23818-23828
    • (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
  • 58
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann M., Coomaraswamy J., Bolmont T., Kaeser S., Schaefer C., Kilger E., et al. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 313 (2006) 1781-1784
    • (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
  • 59
    • 10744230547 scopus 로고    scopus 로고
    • Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization
    • Orgogozo J.M., Gilman S., Dartigues J.F., Laurent B., Puel M., Kirby L.C., et al. Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology 61 (2003) 46-54
    • (2003) Neurology , vol.61 , pp. 46-54
    • Orgogozo, J.M.1    Gilman, S.2    Dartigues, J.F.3    Laurent, B.4    Puel, M.5    Kirby, L.C.6
  • 60
    • 36949009292 scopus 로고    scopus 로고
    • The innervation of senile plaques: a link between amyloid and neurofibrillary pathology?
    • Gauthier S., Scheltens P., and Cummings J.L. (Eds), Martin Dunitz, London
    • Delatour B., Blanchard V., Pradier L., and Duyckaerts C. The innervation of senile plaques: a link between amyloid and neurofibrillary pathology?. In: Gauthier S., Scheltens P., and Cummings J.L. (Eds). Alzheimer's disease and related disorders. Annual 2004 (2003), Martin Dunitz, London 1-19
    • (2003) Alzheimer's disease and related disorders. Annual 2004 , pp. 1-19
    • Delatour, B.1    Blanchard, V.2    Pradier, L.3    Duyckaerts, C.4
  • 61
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction
    • Oddo S., Caccamo A., Shepherd J.D., Murphy M.P., Golde T.E., Kayed R., et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron 39 (2003) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.