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Glycosylation of microtubule-associated protein tau: An abnormal posttranslational modification in Alzheimer's disease
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Wang J-Z, Grundke-Iqbal I, Iqbal K. Glycosylation of microtubule-associated protein tau: an abnormal posttranslational modification in Alzheimer's disease. Nat Med. 2:1996;871-875.
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Wang, J.-Z.1
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Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal - Lysosomal system
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of special interest. The increased expression of the endosomal - lysosomal protease cathepsin D and its accumulation in otherwise healthy-appearing neurons is observed in populations selectively prone to degeneration in AD, and provides further evidence for early metabolic dysfunction.
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Cataldo AM, Barnett JL, Berman SA, Li J, Quarless S, Bursztajn S, Lippa C, Nixon RA. Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal - lysosomal system. of special interest Neuron. 14:1995;671-680 The increased expression of the endosomal - lysosomal protease cathepsin D and its accumulation in otherwise healthy-appearing neurons is observed in populations selectively prone to degeneration in AD, and provides further evidence for early metabolic dysfunction.
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Neuron
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Cataldo, A.M.1
Barnett, J.L.2
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Li, J.4
Quarless, S.5
Bursztajn, S.6
Lippa, C.7
Nixon, R.A.8
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0029004341
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Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
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2+ channel protein are discussed.
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2+ channel protein are discussed.
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Nature
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Sherrington, R.1
Rogaev, E.I.2
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Rogaeva, E.A.4
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Ikeda, M.6
Chi, H.7
Lin, C.8
Li, G.9
Holman, K.10
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5
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0029115555
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The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families
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of special interest. The structure of the PS1 gene is reported and the relative positions of the intron/exon boundaries that interrupt the coding sequence are illustrated. Evidence for alternative splicing based on cDNA structures and gene sequence is included. The authors also describe the apparent clustering of some of the FAD mutations and propose a model for pathogenesis through disruption of an ion channel.
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Clark RF. The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families. of special interest Nat Genet. 11:1995;219-222 The structure of the PS1 gene is reported and the relative positions of the intron/exon boundaries that interrupt the coding sequence are illustrated. Evidence for alternative splicing based on cDNA structures and gene sequence is included. The authors also describe the apparent clustering of some of the FAD mutations and propose a model for pathogenesis through disruption of an ion channel.
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Nat Genet
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Clark, R.F.1
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Complete analysis of the presenilin 1 gene in early onset Alzheimer's disease
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Hutton, M.1
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Prihar, G.7
Talbot, C.8
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0028892351
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Failure to detect missense mutations in the S182 gene in a series of late-onset Alzheimer's disease cases
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Tsuda T, Chi H, Liang Y, Rogaeva EA, Sherrington R, Levesque G, Ikeda M, Rogaeva EI, Pollen D, Freeman M, et al. Failure to detect missense mutations in the S182 gene in a series of late-onset Alzheimer's disease cases. Neurosci Lett. 201:1995;188-190.
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Tsuda, T.1
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Rogaeva, E.I.8
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8
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Three different mutations of presenilin 1 gene in early-onset Alzheimer's disease families
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Kamino K, Sato S, Sakaki Y, Yoshiwa A, Nishiwaki Y, Takeda M, Tanabe H, Nishimura T, Ii K, George-Hyslop PHS, et al. Three different mutations of presenilin 1 gene in early-onset Alzheimer's disease families. Neurosci Lett. 208:1996;195-198.
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Kamino, K.1
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Nishiwaki, Y.5
Takeda, M.6
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Nishimura, T.8
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0029087026
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Candidate gene for the chromosome 1 familial Alzheimer's disease locus
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of outstanding interest. The gene on chromosome 1 responsible for FAD in the Volga German kindreds is identified (PS2). Its high homology to PS1 and the occurrence of the FAD mutations at conserved amino acids strongly supports a causative role of the mutant proteins in early-onset FAD.
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Levy-Lahad E, Wasco W, Poorkaj P, Romano DM, Oshima J, Pettingell WH, Yu C, Jondro PD, Schmidt SD, Wang K, et al. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. of outstanding interest Science. 269:1995;973-977 The gene on chromosome 1 responsible for FAD in the Volga German kindreds is identified (PS2). Its high homology to PS1 and the occurrence of the FAD mutations at conserved amino acids strongly supports a causative role of the mutant proteins in early-onset FAD.
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Science
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Levy-Lahad, E.1
Wasco, W.2
Poorkaj, P.3
Romano, D.M.4
Oshima, J.5
Pettingell, W.H.6
Yu, C.7
Jondro, P.D.8
Schmidt, S.D.9
Wang, K.10
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10
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0029101491
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Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
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of special interest. Another report describing the linkage of missense mutations to the PS2 gene on chromosome 1. A second chromosome 1-linked FAD family is found to have a mutation in PS2 that is distinct from the mutation in the Volga German kindreds.
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Rogaev EI, Sherrington R, Rogaeva EA, Levesque G, Ikeda M, Liang Y, Chi H, Lin C, Holman K, Tsuda T, et al. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. of special interest Nature. 376:1995;775-778 Another report describing the linkage of missense mutations to the PS2 gene on chromosome 1. A second chromosome 1-linked FAD family is found to have a mutation in PS2 that is distinct from the mutation in the Volga German kindreds.
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(1995)
Nature
, vol.376
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Rogaev, E.I.1
Sherrington, R.2
Rogaeva, E.A.3
Levesque, G.4
Ikeda, M.5
Liang, Y.6
Chi, H.7
Lin, C.8
Holman, K.9
Tsuda, T.10
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11
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0028891759
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Nucleotide sequence of the chromosome 14-encoded S182 cDNA and revised secondary structure prediction
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of special interest. The complete nucleotide sequence of the PS1 cDNA is reported. An alternative model for the secondary structure of PS1 suggests that there may be nine transmembrane domains. According to this structural model, many of the FAD mutations previously described as occurring in a cytoplasmic loop between the sixth and seventh transmembrane domains (TM6 and TM7) would now be found within a transmembrane domain.
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Slunt HH, Thinakaran G, Lee MK, Sisodia SS. Nucleotide sequence of the chromosome 14-encoded S182 cDNA and revised secondary structure prediction. of special interest Amyloid - Int J Exp Clin Invest. 2:1995;188-190 The complete nucleotide sequence of the PS1 cDNA is reported. An alternative model for the secondary structure of PS1 suggests that there may be nine transmembrane domains. According to this structural model, many of the FAD mutations previously described as occurring in a cytoplasmic loop between the sixth and seventh transmembrane domains (TM6 and TM7) would now be found within a transmembrane domain.
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Amyloid - Int J Exp Clin Invest
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Slunt, H.H.1
Thinakaran, G.2
Lee, M.K.3
Sisodia, S.S.4
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12
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13344282063
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Alzheimer-associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells
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of special interest. In situ hybridization and immunohistochemical techniques are used to detect the expression of PS1 and PS2 in the rat and human brain. The tissue and cellular distributions of the two proteins are virtually identical. Expression is enriched in neurons throughout the brain and the proteins accumulate on intracellular structures resembling the Golgi complex and endoplasmic reticulum.
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Kovacs DM, Fausett HJ, Page KJ, Kim TW, Moir RD, Merriam DE, Hollister RD, Hallmark OG, Mancini R, Felsenstein KM, et al. Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. of special interest Nat Med. 2:1996;224-229 In situ hybridization and immunohistochemical techniques are used to detect the expression of PS1 and PS2 in the rat and human brain. The tissue and cellular distributions of the two proteins are virtually identical. Expression is enriched in neurons throughout the brain and the proteins accumulate on intracellular structures resembling the Golgi complex and endoplasmic reticulum.
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(1996)
Nat Med
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Kovacs, D.M.1
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Merriam, D.E.6
Hollister, R.D.7
Hallmark, O.G.8
Mancini, R.9
Felsenstein, K.M.10
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13
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16044373524
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Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
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of special interest. The finding that mutations in the genes for PS1 and PS2 lead to the increased production of long Aβ in vitro and elevated circulating long Aβ in vivo supports the primacy of long Aβ in the pathogenesis of all forms of AD. Efforts must now be directed towards defining the involvement of normal and mutant presenilins in protein processing.
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Scheuner D, Eckman C, Jensen M, Song X, Citron M, Suzuki N, Bird TD, Hardy J, Hutton M, Kukull W. Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. of special interest Nat Med. 2:1996;864-870 The finding that mutations in the genes for PS1 and PS2 lead to the increased production of long Aβ in vitro and elevated circulating long Aβ in vivo supports the primacy of long Aβ in the pathogenesis of all forms of AD. Efforts must now be directed towards defining the involvement of normal and mutant presenilins in protein processing.
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Nat Med
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Scheuner, D.1
Eckman, C.2
Jensen, M.3
Song, X.4
Citron, M.5
Suzuki, N.6
Bird, T.D.7
Hardy, J.8
Hutton, M.9
Kukull, W.10
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14
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0029116848
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Facilitation of lin-12-mediated signaling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
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of outstanding interest. The homology between PS1 and sel-12 suggests that presenilins are part of a family of signal-regulating proteins, and offers the opportunity of applying the powerful genetic approaches available in C. elegans research to questions surrounding presenilin function.
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Levitan D, Greenwald I. Facilitation of lin-12-mediated signaling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. of outstanding interest Nature. 377:1995;351-354 The homology between PS1 and sel-12 suggests that presenilins are part of a family of signal-regulating proteins, and offers the opportunity of applying the powerful genetic approaches available in C. elegans research to questions surrounding presenilin function.
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Nature
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Levitan, D.1
Greenwald, I.2
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The role of APP processing and trafficking pathways in the formation of amyloid beta-protein
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Selkoe DJ, Yamazaki T, Citron M, Podisny MB, Koo EH, Teplow DB, Haass C. The role of APP processing and trafficking pathways in the formation of amyloid beta-protein. Ann NY Acad Sci. 777:1996;57-64.
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Selkoe, D.J.1
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Koo, E.H.5
Teplow, D.B.6
Haass, C.7
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0026547582
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Familial Alzheimer's disease with the amyloid precursor protein position 717 mutation and sporadic Alzheimer's disease have the same cytoskeletal pathology
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Lantos PL, Luthert PJ, Hanger D, Anderton BH, Mullan M, Rossor M. Familial Alzheimer's disease with the amyloid precursor protein position 717 mutation and sporadic Alzheimer's disease have the same cytoskeletal pathology. Neurosci Lett. 137:1992;221-224.
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Lannfelt L, Bogdanovic N, Appelgren H, Axelman K, Likius L, Hansson G, Schenk D, Hardy J, Winblad B. Amyloid precursor protein mutation causes Alzheimer's disease in a Swedish family. Neurosci Lett. 168:1994;254-256.
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Hardy, J.8
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0028985574
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Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
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of outstanding interest. This is the first robust demonstration of a rodent exhibiting the hallmark core-containing amyloid deposits of AD. Neuropathology findings in the model are consistent with the idea that amyloid deposition triggers many of the neuronal abnormalities of AD. The mice provide a model for studying the inter-relationships among various neuropathological features of AD, and facilitate the testing of agents that may impede amyloid deposition.
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Games D, Adams D, Alessandrini R, Barbour R, Berthelette P, Blackwell C, Carr T, Clemens J, Donaldson T, Gillespie F, et al. Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. of outstanding interest Nature. 373:1995;523-527 This is the first robust demonstration of a rodent exhibiting the hallmark core-containing amyloid deposits of AD. Neuropathology findings in the model are consistent with the idea that amyloid deposition triggers many of the neuronal abnormalities of AD. The mice provide a model for studying the inter-relationships among various neuropathological features of AD, and facilitate the testing of agents that may impede amyloid deposition.
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Nature
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Games, D.1
Adams, D.2
Alessandrini, R.3
Barbour, R.4
Berthelette, P.5
Blackwell, C.6
Carr, T.7
Clemens, J.8
Donaldson, T.9
Gillespie, F.10
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0028875687
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Levels and alternative splicing of amyloid β-protein precursor (APP) transcripts in brains of APP transgenic mice and humans with Alzheimer's disease
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Rockenstein EM, McConlogue L, Tan H, Power M, Masliah E, Mucke L. Levels and alternative splicing of amyloid β-protein precursor (APP) transcripts in brains of APP transgenic mice and humans with Alzheimer's disease. J Biol Chem. 270:1995;28257-28267.
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Rockenstein, E.M.1
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Mucke, L.6
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20
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0029742199
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Correlative memory deficits, Aβ levels, and amyloid plaques in transgenic mice
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Another instance of the overexpression of an FAD-linked form of APP leading to extensive age-related amyloid deposition, and the first demonstration that deposition correlates with an age-dependent decline in cognition. The model offers the exciting opportunity of studying the mechanism relating Aβ amyloid deposition to cognitive abnormalities, and supports the etiologic primacy of Aβ deposition. of outstanding interest
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Hsiao K, Chapman P, Nilsen S, Eckman C, Harigaya Y, Younkin S, Yang F, Cole G. Correlative memory deficits, Aβ levels, and amyloid plaques in transgenic mice. of outstanding interest Science. 1996; Another instance of the overexpression of an FAD-linked form of APP leading to extensive age-related amyloid deposition, and the first demonstration that deposition correlates with an age-dependent decline in cognition. The model offers the exciting opportunity of studying the mechanism relating Aβ amyloid deposition to cognitive abnormalities, and supports the etiologic primacy of Aβ deposition.
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Science
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Hsiao, K.1
Chapman, P.2
Nilsen, S.3
Eckman, C.4
Harigaya, Y.5
Younkin, S.6
Yang, F.7
Cole, G.8
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21
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0028968005
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Protection against HIV-1 gp120-induced brain damage by neuronal expression of human amyloid precursor protein
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Mucke L, Abraham CR, Ruppe MD, Rockenstein EM, Toggas SM, Mallory M, Alford M, Masliah E. Protection against HIV-1 gp120-induced brain damage by neuronal expression of human amyloid precursor protein. J Exp Med. 181:1995;1551-1556.
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Mucke, L.1
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Rockenstein, E.M.4
Toggas, S.M.5
Mallory, M.6
Alford, M.7
Masliah, E.8
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Furukawa, K.1
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0029935396
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The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)
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Mitosis of Schwann cells and demyelination are induced by the amyloid precursor protein and other protease inhibitors in the rat sciatic nerve
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Enhanced amyloidogenic processing of the β-amyloid precursor protein in gene-targeted mice bearing the Swedish familial Alzheimer's disease mutations and a 'humanized' Aβ sequence
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of special interest
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Reaume AG, Howland DS, Trusko SP, Savage MJ, Lang DM, Greenberg BD, Siman R, Scott RW. Enhanced amyloidogenic processing of the β-amyloid precursor protein in gene-targeted mice bearing the Swedish familial Alzheimer's disease mutations and a 'humanized' Aβ sequence. of special interest J Biol Chem. 1996; A gene replacement strategy was exploited to demonstrate for the first time that a mutation linked to FAD leads to enhanced amyloidogenic processing of APP in the brain. These mice express high brain concentrations of Aβ in the absence of overt changes in temporal, spatial, or quantitative aspects of APP expression, and so represents a close genetic model of codon 670/671 FAD.
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Scott, R.W.8
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0027407565
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Apolipoprotein E: High-avidity binding to β-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease
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Clinical and pathological correlates of apolipoprotein E ε4 in Alzheimer's disease
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of outstanding interest. This prospective study relates apoE4 to an earlier age of dementia onset and to increased amyloid burden, but finds no relation between apoE and neurofibrillary tangle density. The study implies that amyloid load is important to the initial stages of dementia, and emphasizes the need to define the pathogenic mechanism of the apoE/Aβ interaction.
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Gomez-Isla T, West HL, Rebeck GW, Harr SD, Growdon JH, Locascio JJ, Perls TT, Lipsitz LA, Hyman BT. Clinical and pathological correlates of apolipoprotein E ε4 in Alzheimer's disease. of outstanding interest Ann Neurol. 39:1996;62-70 This prospective study relates apoE4 to an earlier age of dementia onset and to increased amyloid burden, but finds no relation between apoE and neurofibrillary tangle density. The study implies that amyloid load is important to the initial stages of dementia, and emphasizes the need to define the pathogenic mechanism of the apoE/Aβ interaction.
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Perls, T.T.7
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Association of apolipoprotein E genotype with brain levels of apolipoprotein E and apolipoprotein J (clusterin) in Alzheimer's disease
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Bertrand P, Poirier J, Oda T, Finch CE, Pasinetti GM. Association of apolipoprotein E genotype with brain levels of apolipoprotein E and apolipoprotein J (clusterin) in Alzheimer's disease. Mol Brain Res. 33:1995;174-178.
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Bertrand, P.1
Poirier, J.2
Oda, T.3
Finch, C.E.4
Pasinetti, G.M.5
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33
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0028157335
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Membrane lipids, selectively diminished in Alzheimer brains, suggest synapse loss as a primary event in early-onset form (type I) and demyelination in late-onset form (type II)
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Svennerholm L, Gottfries CG. Membrane lipids, selectively diminished in Alzheimer brains, suggest synapse loss as a primary event in early-onset form (type I) and demyelination in late-onset form (type II). J Neurochem. 62:1994;1039-1047.
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Svennerholm, L.1
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0028916836
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Membrane alterations as causes of impaired signal transduction in Alzheimer's disease and aging
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Roth GS, Joseph JA, Mason RP. Membrane alterations as causes of impaired signal transduction in Alzheimer's disease and aging. Trends Neurosci. 18:1995;203-206.
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Trends Neurosci
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Roth, G.S.1
Joseph, J.A.2
Mason, R.P.3
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35
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0007691164
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Apolipoprotein E4 allele as a predictor of cholinergic deficits and treatment outcome in Alzheimer disease
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of outstanding interest. The ApoE genotype is shown to correlate with the cholinergic dysfunction of AD and to the efficacy of a cholinergic-based therapy. The observations have major clinical and preclinical implications, and emphasize that AD is a syndrome with heterogeneous etiology, pathogenesis and therapy.
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Poirier J, Delisle M-C, Quirion R, Aubert I, Farlow M, Lahiri D, Hui S, Bertrand P, Nalbantoglu J, Gilfix BM, Gauthier S. Apolipoprotein E4 allele as a predictor of cholinergic deficits and treatment outcome in Alzheimer disease. of outstanding interest Proc Natl Acad Sci USA. 92:1995;12260-12264 The ApoE genotype is shown to correlate with the cholinergic dysfunction of AD and to the efficacy of a cholinergic-based therapy. The observations have major clinical and preclinical implications, and emphasize that AD is a syndrome with heterogeneous etiology, pathogenesis and therapy.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 12260-12264
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Poirier, J.1
Delisle, M.-C.2
Quirion, R.3
Aubert, I.4
Farlow, M.5
Lahiri, D.6
Hui, S.7
Bertrand, P.8
Nalbantoglu, J.9
Gilfix, B.M.10
Gauthier, S.11
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36
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0028987849
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Inhibition of β-amyloid formation identifies proteolytic precursors and subcellular site of catabolism
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Higaki J, Quon D, Zhong Z, Cordell B. Inhibition of β-amyloid formation identifies proteolytic precursors and subcellular site of catabolism. Neuron. 14:1995;651-659.
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(1995)
Neuron
, vol.14
, pp. 651-659
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Higaki, J.1
Quon, D.2
Zhong, Z.3
Cordell, B.4
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37
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0028865607
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Calpain inhibitor I decreases βA4 secretion from human embryonal kidney cells expressing β-amyloid precursor protein carrying the APP670/671 double mutation
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Klafki H-W, Paganetti PA, Sommer B, Staufenbiel M. Calpain inhibitor I decreases βA4 secretion from human embryonal kidney cells expressing β-amyloid precursor protein carrying the APP670/671 double mutation. Neurosci Lett. 201:1995;29-32.
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Neurosci Lett
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Klafki, H.-W.1
Paganetti, P.A.2
Sommer, B.3
Staufenbiel, M.4
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38
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0030199986
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Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF
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Citron M, Diehl TS, Capell A, Haass C, Teplow DB, Selkoe DJ. Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF. Neuron. 17:1996;171-179.
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Neuron
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Citron, M.1
Diehl, T.S.2
Capell, A.3
Haass, C.4
Teplow, D.B.5
Selkoe, D.J.6
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39
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0028817351
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Cell-type and amyloid precursor protein-type specific inhibition of Aβ release by bafilomycin A1, a selective inhibitor of vacuolar ATPases
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Knops J, Suomensaari S, Lee M, McConlogue L, Seubert P, Sinha S. Cell-type and amyloid precursor protein-type specific inhibition of Aβ release by bafilomycin A1, a selective inhibitor of vacuolar ATPases. J Biol Chem. 270:1995;2419-2422.
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(1995)
J Biol Chem
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Knops, J.1
Suomensaari, S.2
Lee, M.3
McConlogue, L.4
Seubert, P.5
Sinha, S.6
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40
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0028971033
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Regulated secretion of β-amyloid precursor protein in rat brain
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of special interest. The many reports of alterations in the processing of APP by cultured cells have led to the study described here in a brain-slice preparation. The increased nonamyloidogenic processing of APP in response to an M2-preferring muscarinic antagonist and the minimal response to a muscarinic agonist are unexpected, given the marked effects of M1 and M3 receptor activators reported previously in cultured cell systems. The study highlights the underappreciated complexity of mechanisms regulating brain Aβ production.
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Farber SA, Nitsch RM, Schulz JG, Wurtman RJ. Regulated secretion of β-amyloid precursor protein in rat brain. of special interest J Neurosci. 15:1995;7442-7451 The many reports of alterations in the processing of APP by cultured cells have led to the study described here in a brain-slice preparation. The increased nonamyloidogenic processing of APP in response to an M2-preferring muscarinic antagonist and the minimal response to a muscarinic agonist are unexpected, given the marked effects of M1 and M3 receptor activators reported previously in cultured cell systems. The study highlights the underappreciated complexity of mechanisms regulating brain Aβ production.
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(1995)
J Neurosci
, vol.15
, pp. 7442-7451
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Farber, S.A.1
Nitsch, R.M.2
Schulz, J.G.3
Wurtman, R.J.4
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41
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0028913416
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Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease
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of special interest. Compounds have been identified that block the in vitro aggregation of two distinct amyloid fibril-forming proteins and that, upon oral administration, interfere with a type of splenic amyloid deposition in vivo. The report demonstrates the feasibility of using orally bioavailable small molecules to impede protein - protein interactions essential for amyloid fibril formation.
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Kisilevsky R, Lemieux LJ, Fraser PE, Kong X, Hultin PG, Szarek WA. Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. of special interest Nat Med. 1:1995;143-148 Compounds have been identified that block the in vitro aggregation of two distinct amyloid fibril-forming proteins and that, upon oral administration, interfere with a type of splenic amyloid deposition in vivo. The report demonstrates the feasibility of using orally bioavailable small molecules to impede protein - protein interactions essential for amyloid fibril formation.
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(1995)
Nat Med
, vol.1
, pp. 143-148
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Kisilevsky, R.1
Lemieux, L.J.2
Fraser, P.E.3
Kong, X.4
Hultin, P.G.5
Szarek, W.A.6
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42
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0029866991
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β-amyloid toxicity in organotypic hippocampal cultures: Protection by EUK-8, a synthetic catalytic free radical scavenger
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of special interest. Previous studies in dissociated cell culture systems implicating oxidative damage in the mechanism of Aβ amyloid neurotoxicity have been extended to a slice-culture preparation that more closely models the mature hippocampus. The neuroprotective efficacy of EUK-8 is attributed to an antioxidative mechanism distinct from commonly used oxygen radical scavengers. Its mimicry of the catalytic activities of superoxide dismutase and catalase may offer advantages over stoichiometric scavengers.
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Bruce AJ, Malfroy B, Baudry M. β-amyloid toxicity in organotypic hippocampal cultures: protection by EUK-8, a synthetic catalytic free radical scavenger. of special interest Proc Natl Acad Sci USA. 93:1996;2312-2316 Previous studies in dissociated cell culture systems implicating oxidative damage in the mechanism of Aβ amyloid neurotoxicity have been extended to a slice-culture preparation that more closely models the mature hippocampus. The neuroprotective efficacy of EUK-8 is attributed to an antioxidative mechanism distinct from commonly used oxygen radical scavengers. Its mimicry of the catalytic activities of superoxide dismutase and catalase may offer advantages over stoichiometric scavengers.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 2312-2316
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Bruce, A.J.1
Malfroy, B.2
Baudry, M.3
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43
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0030042249
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Expression of V642 APP mutant causes cellular apoptosis as Alzheimer trait-linked phenotype
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Yamatsuji T, Okamoto T, Takeda S, Murayama Y, Tanaka N, Nishimoto I. Expression of V642 APP mutant causes cellular apoptosis as Alzheimer trait-linked phenotype. EMBO J. 15:1996;498-509.
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(1996)
EMBO J
, vol.15
, pp. 498-509
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Yamatsuji, T.1
Okamoto, T.2
Takeda, S.3
Murayama, Y.4
Tanaka, N.5
Nishimoto, I.6
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44
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0029417023
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Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro
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Busciglio J, Yankner BA. Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature. 378:1995;776-779.
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(1995)
Nature
, vol.378
, pp. 776-779
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Busciglio, J.1
Yankner, B.A.2
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45
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0028981717
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The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice
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LaFerla FM, Tinkle BT, Bieberich CJ, Haudenschild CC, Jay G. The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nat Genet. 9:1995;21-30.
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(1995)
Nat Genet
, vol.9
, pp. 21-30
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LaFerla, F.M.1
Tinkle, B.T.2
Bieberich, C.J.3
Haudenschild, C.C.4
Jay, G.5
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46
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0029671219
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2+-binding protein ALG-2 and Alzheimer's disease gene ALG-3
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of special interest. A partial cDNA that encodes the carboxyl terminus of murine PS2 is identified from an expression screen designed to select clones capable of rescuing a T-cell hybridoma from apoptosis. Rescue is observed with some but not all apoptosis-inducing agents. It is not known if resistance to cell death in this system is dependent on a positive or negative function of the truncated PS2 construct.
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2+-binding protein ALG-2 and Alzheimer's disease gene ALG-3. of special interest Science. 271:1996;521-525 A partial cDNA that encodes the carboxyl terminus of murine PS2 is identified from an expression screen designed to select clones capable of rescuing a T-cell hybridoma from apoptosis. Rescue is observed with some but not all apoptosis-inducing agents. It is not known if resistance to cell death in this system is dependent on a positive or negative function of the truncated PS2 construct.
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(1996)
Science
, vol.271
, pp. 521-525
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Vito, P.1
Lacana, E.2
D'Adamio, L.3
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47
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0028833215
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Cell death in Alzheimer's disease evaluated by DNA fragmentation in situ
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of special interest. The histochemical detection of DNA fragmentation is used to demonstrate increased DNA damage in both neurons and glia in the AD brain. A fraction of these cells also exhibit nuclear abnormalities characteristic of apoptosis, although the significance of the additional DNA fragmentation is uncertain.
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Lassmann H, Bancher C, Breitschopf H, Wegiel J, Bobinski M, Jellinger K, Wisniewski HM. Cell death in Alzheimer's disease evaluated by DNA fragmentation in situ. of special interest Acta Neuropathol (Berl). 89:1995;35-41 The histochemical detection of DNA fragmentation is used to demonstrate increased DNA damage in both neurons and glia in the AD brain. A fraction of these cells also exhibit nuclear abnormalities characteristic of apoptosis, although the significance of the additional DNA fragmentation is uncertain.
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(1995)
Acta Neuropathol (Berl)
, vol.89
, pp. 35-41
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Lassmann, H.1
Bancher, C.2
Breitschopf, H.3
Wegiel, J.4
Bobinski, M.5
Jellinger, K.6
Wisniewski, H.M.7
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48
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0029976253
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DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-jun immunoreactivity, relationship to brain area, and effect of postmortem delay
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of special interest. The co-localization of fragmented DNA with either morphological abnormalities in nuclei or elevated c-jun immunoreactivity argues strongly for neuronal death by apoptosis in AD brain. The study also addresses methodological considerations important to the interpretation of the in situ DNA fragmentation technique.
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Anderson AJ, Su JH, Cotman CW. DNA damage and apoptosis in Alzheimer's disease: colocalization with c-jun immunoreactivity, relationship to brain area, and effect of postmortem delay. of special interest J Neurosci. 16:1996;1710-1719 The co-localization of fragmented DNA with either morphological abnormalities in nuclei or elevated c-jun immunoreactivity argues strongly for neuronal death by apoptosis in AD brain. The study also addresses methodological considerations important to the interpretation of the in situ DNA fragmentation technique.
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(1996)
J Neurosci
, vol.16
, pp. 1710-1719
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Anderson, A.J.1
Su, J.H.2
Cotman, C.W.3
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49
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0029982815
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Oxidative damage in Alzheimer's
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of special interest. A new histochemical method for the detection of macromolecular carbonyls provides evidence for localized oxidative damage to neurons and glia specific to the AD brain. The finding is consistent with other studies suggesting increased oxidative stress and elevated cell death by apoptosis in the AD brain.
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Smith MA, Perry G, Richey PL, Sayre LM, Anderson VE, Beal MF, Kowall N. Oxidative damage in Alzheimer's. of special interest Nature. 382:1996;120-121 A new histochemical method for the detection of macromolecular carbonyls provides evidence for localized oxidative damage to neurons and glia specific to the AD brain. The finding is consistent with other studies suggesting increased oxidative stress and elevated cell death by apoptosis in the AD brain.
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(1996)
Nature
, vol.382
, pp. 120-121
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Smith, M.A.1
Perry, G.2
Richey, P.L.3
Sayre, L.M.4
Anderson, V.E.5
Beal, M.F.6
Kowall, N.7
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