메뉴 건너뛰기




Volumn 12, Issue 2, 2004, Pages 146-156

Clinical, Pathological, and Biochemical Spectrum of Alzheimer Disease Associated with PS-1 Mutations

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; PRESENILIN 1; PRESENILIN 2;

EID: 1342344129     PISSN: 10647481     EISSN: None     Source Type: Journal    
DOI: 10.1097/00019442-200403000-00006     Document Type: Article
Times cited : (75)

References (127)
  • 1
    • 0033358671 scopus 로고    scopus 로고
    • Early-onset autosomal-dominant Alzheimer disease: Prevalence, genetic heterogeneity, and mutation spectrum
    • Campion D, Dumanchin C, Hannequin D, et al: Early-onset autosomal-dominant Alzheimer disease: prevalence, genetic heterogeneity, and mutation spectrum. Am J Hum Genet 1999; 65:664-670
    • (1999) Am J Hum Genet , vol.65 , pp. 664-670
    • Campion, D.1    Dumanchin, C.2    Hannequin, D.3
  • 2
    • 6844255860 scopus 로고    scopus 로고
    • Estimation of the genetic contribution of presenilin-1 and -2 mutations in a population-based study of presenile Alzheimer disease
    • Cruts M, van Duijn CM, Backhovens H, et al: Estimation of the genetic contribution of presenilin-1 and -2 mutations in a population-based study of presenile Alzheimer disease. Hum Mol Genet 1998; 7:43-51
    • (1998) Hum Mol Genet , vol.7 , pp. 43-51
    • Cruts, M.1    Van Duijn, C.M.2    Backhovens, H.3
  • 3
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A, Chartier-Harlin MC, Mullan M, et al: Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991; 349:704-707
    • (1991) Nature , vol.349 , pp. 704-707
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3
  • 4
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington R, Rogaev EI, Lyang Y, et al: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 1995; 375:754-760
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Lyang, Y.3
  • 5
    • 0029087026 scopus 로고
    • Candidate gene for the Chromosome 1 familial Alzheimer's disease locus
    • Levy-Lahad E, Wasco W, Poorkaj P, et al: Candidate gene for the Chromosome 1 familial Alzheimer's disease locus. Science 1995; 269:973-977
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 6
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on Chromosome 1 related to the Alzheimer's disease Type 3 gene
    • Rogaev EI, Sherrington R, Rogaeva EA, 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. Nature 1995; 376:775-778
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3
  • 7
    • 8944241774 scopus 로고    scopus 로고
    • Alzheimer's disease associated with mutations in presenilin-2 is rare and variably penetrant
    • Sherrington R, Froelich S, Sorbi S, et al: Alzheimer's disease associated with mutations in presenilin-2 is rare and variably penetrant. Hum Mol Genet 1996; 5:985-988
    • (1996) Hum Mol Genet , vol.5 , pp. 985-988
    • Sherrington, R.1    Froelich, S.2    Sorbi, S.3
  • 8
    • 0026648493 scopus 로고
    • Assessment of amyloid β-protein precursor gene mutations in a large set of familial and sporadic Alzheimer disease cases
    • Tanzi RE, Vaula G, Romano DM, et al: Assessment of amyloid β-protein precursor gene mutations in a large set of familial and sporadic Alzheimer disease cases. Am J Hum Genet 1992; 1:273-282
    • (1992) Am J Hum Genet , vol.1 , pp. 273-282
    • Tanzi, R.E.1    Vaula, G.2    Romano, D.M.3
  • 9
    • 0036845601 scopus 로고    scopus 로고
    • Frequency of mutations in the presenilin and amyloid precursor protein genes in early-onset Alzheimer's disease in Spain
    • Lleó A, Blesa R, Queralt R, et al: Frequency of mutations in the presenilin and amyloid precursor protein genes in early-onset Alzheimer's disease in Spain. Arch Neurol 2002; 59:1759-1763
    • (2002) Arch Neurol , vol.59 , pp. 1759-1763
    • Lleó, A.1    Blesa, R.2    Queralt, R.3
  • 10
    • 0037469171 scopus 로고    scopus 로고
    • Early-onset familial Alzheimer's disease: Mutation frequency in 31 families
    • Janssen JC, Beck JA, Campbell TA, et al: Early-onset familial Alzheimer's disease: mutation frequency in 31 families. Neurology 2003; 60:235-239
    • (2003) Neurology , vol.60 , pp. 235-239
    • Janssen, J.C.1    Beck, J.A.2    Campbell, T.A.3
  • 11
    • 0001855205 scopus 로고    scopus 로고
    • Molecular genetics of Alzheimer's disease
    • Edited by Growdon JH, Rossor M. Woburn, MA, Butterworth-Heinemann
    • Cruts M, Van Broeckhoven C: Molecular genetics of Alzheimer's disease, in The Dementias. Edited by Growdon JH, Rossor M. Woburn, MA, Butterworth-Heinemann, 1998, pp 155-170
    • (1998) The Dementias , pp. 155-170
    • Cruts, M.1    Van Broeckhoven, C.2
  • 12
    • 2542509819 scopus 로고    scopus 로고
    • The impact of different presenilin-1 and presenilin-2 mutations on amyloid deposition, neurofibrillary changes, and neuronal loss in the familial Alzheimer's disease brain: Evidence for other phenotype-modifying factors
    • Gomez-Isla T, Growdon WB, McNamara MJ, et al: The impact of different presenilin-1 and presenilin-2 mutations on amyloid deposition, neurofibrillary changes, and neuronal loss in the familial Alzheimer's disease brain: evidence for other phenotype-modifying factors. Brain 1999; 122:1709-1719
    • (1999) Brain , vol.122 , pp. 1709-1719
    • Gomez-Isla, T.1    Growdon, W.B.2    McNamara, M.J.3
  • 13
    • 0033848935 scopus 로고    scopus 로고
    • Familial Alzheimer's disease: Site of mutation influences clinical phenotype
    • Lippa CF, Swearer JM, Kane KJ, et al: Familial Alzheimer's disease: site of mutation influences clinical phenotype. Ann Neurol 2000; 48:376-379
    • (2000) Ann Neurol , vol.48 , pp. 376-379
    • Lippa, C.F.1    Swearer, J.M.2    Kane, K.J.3
  • 14
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-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
    • Scheuner D, Eckman C, Jensen M, et al: Secreted amyloid beta-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. Nat Med 1996; 2:864-870
    • (1996) Nat Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 15
    • 0031594142 scopus 로고    scopus 로고
    • Increased ABeta42(43) from cell lines expressing presenilin-1 mutations
    • Mehta ND, Refolo LM, Eckman C, et al: Increased ABeta42(43) from cell lines expressing presenilin-1 mutations. Ann Neurol 1998; 43:256-258
    • (1998) Ann Neurol , vol.43 , pp. 256-258
    • Mehta, N.D.1    Refolo, L.M.2    Eckman, C.3
  • 16
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin-1
    • Duff K, Eckman C, Zehr C, et al: Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin-1. Nature 1996; 383:710-713
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3
  • 17
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice
    • Citron M, Westaway D, Xia W, et al: Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice. Nat Med 1997; 3:67-72
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3
  • 18
    • 0025179972 scopus 로고
    • Genetic linkage studies suggest that Alzheimer's disease is not a single homogeneous disorder
    • St. George-Hyslop P, Haines JL, Farrer LA, et al: Genetic linkage studies suggest that Alzheimer's disease is not a single homogeneous disorder. Nature 1990; 347:194-197
    • (1990) Nature , vol.347 , pp. 194-197
    • St. George-Hyslop, P.1    Haines, J.L.2    Farrer, L.A.3
  • 19
    • 0026471656 scopus 로고
    • Genetic linkage evidence for a familial Alzheimer's disease locus on Chromosome 14
    • Schellenberg G, Bird T, Wijsman EM, et al: Genetic linkage evidence for a familial Alzheimer's disease locus on Chromosome 14. Science 1992; 258:668-671
    • (1992) Science , vol.258 , pp. 668-671
    • Schellenberg, G.1    Bird, T.2    Wijsman, E.M.3
  • 20
    • 0027031612 scopus 로고
    • Mapping of a gene predisposing to early-onset Alzheimer's disease to Chromosome 14q24.3
    • Van Broeckhoven C, Backhovens H, Cruts M, et al: Mapping of a gene predisposing to early-onset Alzheimer's disease to Chromosome 14q24.3. Nat Genet 1992; 2:335-339
    • (1992) Nat Genet , vol.2 , pp. 335-339
    • Van Broeckhoven, C.1    Backhovens, H.2    Cruts, M.3
  • 21
    • 0027032695 scopus 로고
    • Genetic evidence for a novel familial Alzheimer's disease locus on Chromosome 14
    • St. George-Hyslop P, Haines JL, Rogaev E, et al: Genetic evidence for a novel familial Alzheimer's disease locus on Chromosome 14. Nat Genet 1992; 2:330-334
    • (1992) Nat Genet , vol.2 , pp. 330-334
    • St. George-Hyslop, P.1    Haines, J.L.2    Rogaev, E.3
  • 22
    • 0027024651 scopus 로고
    • A locus for Alzheimer's disease on the long arm of Chromosome 14, proximal to the a1-antichymotrypsin gene
    • Mullan M, Houlden H, Windelspecht M, et al: A locus for Alzheimer's disease on the long arm of Chromosome 14, proximal to the a1-antichymotrypsin gene. Nat Genet 1992; 2:340-342
    • (1992) Nat Genet , vol.2 , pp. 340-342
    • Mullan, M.1    Houlden, H.2    Windelspecht, M.3
  • 23
    • 13344282063 scopus 로고    scopus 로고
    • Alzheimer-associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • Kovacs DM, Fausett HJ, Page KJ, et al: Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nat Med 1996; 2:224-229
    • (1996) Nat Med , vol.2 , pp. 224-229
    • Kovacs, D.M.1    Fausett, H.J.2    Page, K.J.3
  • 24
    • 0032499750 scopus 로고    scopus 로고
    • Additional evidence for an eight-transmembrane-domain topology for Caenorhabditis elegans and human presenilins
    • Li X, Greenwald I. Additional evidence for an eight-transmembrane-domain topology for Caenorhabditis elegans and human presenilins. Proc Natl Acad Sci U S A 1998; 95:7109-7114
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7109-7114
    • Li, X.1    Greenwald, I.2
  • 25
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin-1 and accumulation of processed derivatives in vivo
    • Thinakaran G, Borchelt DR, Lee MK, et al: Endoproteolysis of presenilin-1 and accumulation of processed derivatives in vivo. Neuron 1996; 17:181-190
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3
  • 26
    • 0030848149 scopus 로고    scopus 로고
    • Early-onset Alzheimer's disease with a presenilin-1 mutation at the site corresponding to the Volga German presenilin-2 mutation
    • Crook R, Ellis R, Shanks M, et al: Early-onset Alzheimer's disease with a presenilin-1 mutation at the site corresponding to the Volga German presenilin-2 mutation. Ann Neurol 1997; 42:124-128
    • (1997) Ann Neurol , vol.42 , pp. 124-128
    • Crook, R.1    Ellis, R.2    Shanks, M.3
  • 27
    • 0035968117 scopus 로고    scopus 로고
    • Presenilin mutations line up along transmembrane alpha-helices
    • Hardy J, Crook R: Presenilin mutations line up along transmembrane alpha-helices. Neurosci Lett 2001; 306:203-205
    • (2001) Neurosci Lett , vol.306 , pp. 203-205
    • Hardy, J.1    Crook, R.2
  • 28
    • 0036155190 scopus 로고    scopus 로고
    • A novel mutation (V89L) in the presenilin-1 gene in a family with early-onset Alzheimer's disease and marked behavioral disturbances
    • Queralt R, Ezquerra M, Lleó A, et al: A novel mutation (V89L) in the presenilin-1 gene in a family with early-onset Alzheimer's disease and marked behavioral disturbances. J Neurol Neurosurg Psychiatry 2002; 72:266-269
    • (2002) J Neurol Neurosurg Psychiatry , vol.72 , pp. 266-269
    • Queralt, R.1    Ezquerra, M.2    Lleó, A.3
  • 29
    • 0033553306 scopus 로고    scopus 로고
    • A novel candidate presenilin-1-interacting protein containing tetratricopeptide repeats
    • Prihar G, Gonzalez de Chavez F, Baker M, et al: A novel candidate presenilin-1-interacting protein containing tetratricopeptide repeats. Neuroreport 1999; 10:1409-1415
    • (1999) Neuroreport , vol.10 , pp. 1409-1415
    • Prihar, G.1    Gonzalez De Chavez, F.2    Baker, M.3
  • 30
    • 0031949628 scopus 로고    scopus 로고
    • A variant of Alzheimer's disease with spastic paraparesis and unusual plaques due to deletion of exon 9 of presenilin-1
    • Crook R, Verkkoniemi A, Perez-Tur J, et al: A variant of Alzheimer's disease with spastic paraparesis and unusual plaques due to deletion of exon 9 of presenilin-1. Nat Med 1998; 4:452-455
    • (1998) Nat Med , vol.4 , pp. 452-455
    • Crook, R.1    Verkkoniemi, A.2    Perez-Tur, J.3
  • 31
    • 0035115610 scopus 로고    scopus 로고
    • Variable phenotype of Alzheimer's disease with spastic paraparesis
    • Smith MJ, Kwok JB, McLean CA, et al: Variable phenotype of Alzheimer's disease with spastic paraparesis. Ann Neurol 2001; 49:125-129
    • (2001) Ann Neurol , vol.49 , pp. 125-129
    • Smith, M.J.1    Kwok, J.B.2    McLean, C.A.3
  • 32
    • 0033762710 scopus 로고    scopus 로고
    • Variant Alzheimer's disease with spastic paraparesis and cotton wool plaques is caused by PS-1 mutations that lead to exceptionally high amyloid-beta concentrations
    • Houlden H, Baker M, McGowan E, et al: Variant Alzheimer's disease with spastic paraparesis and cotton wool plaques is caused by PS-1 mutations that lead to exceptionally high amyloid-beta concentrations. Ann Neurol 2000; 48:806-808
    • (2000) Ann Neurol , vol.48 , pp. 806-808
    • Houlden, H.1    Baker, M.2    McGowan, E.3
  • 33
    • 0029554875 scopus 로고
    • A mutation in Alzheimer's disease destroying a splice-acceptor site in the presenilin-1 gene
    • Perez-Tur J, Froelich S, Prihar G, et al: A mutation in Alzheimer's disease destroying a splice-acceptor site in the presenilin-1 gene. Neuroreport 1995; 7:297-301
    • (1995) Neuroreport , vol.7 , pp. 297-301
    • Perez-Tur, J.1    Froelich, S.2    Prihar, G.3
  • 34
    • 0030857182 scopus 로고    scopus 로고
    • Increased ABeta42(43)-plaque deposition in early-onset familial Alzheimer's disease brains with the deletion of exon 9 and the missense point mutation (H163R) in the PS-1 gene
    • Ishii K, Ii K, Hasegawa T, et al: Increased ABeta42(43)-plaque deposition in early-onset familial Alzheimer's disease brains with the deletion of exon 9 and the missense point mutation (H163R) in the PS-1 gene. Neurosci Lett 1997; 228:17-20
    • (1997) Neurosci Lett , vol.228 , pp. 17-20
    • Ishii, K.1    Ii, K.2    Hasegawa, T.3
  • 35
    • 0031975957 scopus 로고    scopus 로고
    • Splicing mutation of presenilin-1 gene for early-onset familial Alzheimer's disease
    • Sato S, Kamino K, Miki T, et al: Splicing mutation of presenilin-1 gene for early-onset familial Alzheimer's disease. Hum Mutat 1998; suppl:S91-S94
    • (1998) Hum Mutat , Issue.SUPPL.
    • Sato, S.1    Kamino, K.2    Miki, T.3
  • 36
    • 0032854745 scopus 로고    scopus 로고
    • Aberrant splicing in the presenilin-1 intron-4 mutation causes presenile Alzheimer's disease by increased ABeta42 secretion
    • De Jonghe C, Cruts M, Rogaeva EA, et al: Aberrant splicing in the presenilin-1 intron-4 mutation causes presenile Alzheimer's disease by increased ABeta42 secretion. Hum Mol Genet 1999; 8:1529-1540
    • (1999) Hum Mol Genet , vol.8 , pp. 1529-1540
    • De Jonghe, C.1    Cruts, M.2    Rogaeva, E.A.3
  • 37
    • 0035964209 scopus 로고    scopus 로고
    • Screening for PS-1 mutations in a referral-based series of AD cases: 21 Novel mutations
    • Rogaeva EA, Fafel KC, Song YQ, et al: Screening for PS-1 mutations in a referral-based series of AD cases: 21 novel mutations. Neurology 2001; 57:621-625
    • (2001) Neurology , vol.57 , pp. 621-625
    • Rogaeva, E.A.1    Fafel, K.C.2    Song, Y.Q.3
  • 38
    • 18444391830 scopus 로고    scopus 로고
    • Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on ABeta42 production
    • Moehlmann T, Winkler E, Xia X, et al: Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on ABeta42 production. Proc Natl Acad Sci U S A 2002; 99:8025-8030
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 8025-8030
    • Moehlmann, T.1    Winkler, E.2    Xia, X.3
  • 39
    • 0031955162 scopus 로고    scopus 로고
    • Wide range of disease onset in a family with Alzheimer disease and a His163Tyr mutation in the presenilin-1 gene
    • Axelman K, Basun H, Lannfelt L: Wide range of disease onset in a family with Alzheimer disease and a His163Tyr mutation in the presenilin-1 gene. Arch Neurol 1998; 55:698-702
    • (1998) Arch Neurol , vol.55 , pp. 698-702
    • Axelman, K.1    Basun, H.2    Lannfelt, L.3
  • 40
    • 0034966352 scopus 로고    scopus 로고
    • Autopsy-confirmed familial early-onset Alzheimer disease caused by the 1153V presenilin-1 mutation
    • Janssen JC, Lantos PL, Fox NC, et al: Autopsy-confirmed familial early-onset Alzheimer disease caused by the 1153V presenilin-1 mutation. Arch Neurol 2001; 58:953-958
    • (2001) Arch Neurol , vol.58 , pp. 953-958
    • Janssen, J.C.1    Lantos, P.L.2    Fox, N.C.3
  • 41
    • 0030944258 scopus 로고    scopus 로고
    • Clinicopathological features of familial Alzheimer's disease associated with the M139V mutation in the presenilin-1 gene: Pedigree but not mutation-specific age at onset provides evidence for a further genetic factor
    • Fox NC, Kennedy AM, Harvey RJ, et al: Clinicopathological features of familial Alzheimer's disease associated with the M139V mutation in the presenilin-1 gene: pedigree but not mutation-specific age at onset provides evidence for a further genetic factor. Brain 1997; 120:491-501
    • (1997) Brain , vol.120 , pp. 491-501
    • Fox, N.C.1    Kennedy, A.M.2    Harvey, R.J.3
  • 42
    • 8044226013 scopus 로고    scopus 로고
    • Clinical features of early-onset Alzheimer disease in a large kindred with an E280A presenilin-1 mutation
    • Lopera F, Ardilla A, Martinez A, et al: Clinical features of early-onset Alzheimer disease in a large kindred with an E280A presenilin-1 mutation. JAMA 1997; 277:793-799
    • (1997) JAMA , vol.277 , pp. 793-799
    • Lopera, F.1    Ardilla, A.2    Martinez, A.3
  • 43
    • 0029899593 scopus 로고    scopus 로고
    • Incomplete penetrance of familial Alzheimer's disease in a pedigree with a novel presenilin-1 gene mutation
    • Rossor MN, Fox NC, Beck J, et al: Incomplete penetrance of familial Alzheimer's disease in a pedigree with a novel presenilin-1 gene mutation. Lancet 1996; 347:1560
    • (1996) Lancet , vol.347 , pp. 1560
    • Rossor, M.N.1    Fox, N.C.2    Beck, J.3
  • 44
    • 6844258883 scopus 로고    scopus 로고
    • Missense mutations in the Chromosome 14 familial Alzheimer's disease presenilin-1 gene
    • Poorkaj P, Sharma V, Anderson L, et al: Missense mutations in the Chromosome 14 familial Alzheimer's disease presenilin-1 gene. Hum Mutat 1998; 11:216-221
    • (1998) Hum Mutat , vol.11 , pp. 216-221
    • Poorkaj, P.1    Sharma, V.2    Anderson, L.3
  • 45
    • 0029166112 scopus 로고
    • Apolipoprotein-E genotypes and age of onset in early-onset familial Alzheimer's disease
    • Levy-Lahad E, Lahad A, Wijsman EM, et al: Apolipoprotein-E genotypes and age of onset in early-onset familial Alzheimer's disease. Ann Neurol 1995; 38:678-680
    • (1995) Ann Neurol , vol.38 , pp. 678-680
    • Levy-Lahad, E.1    Lahad, A.2    Wijsman, E.M.3
  • 46
    • 0007486598 scopus 로고    scopus 로고
    • A presenilin-1 Thr116Asn substitution in a family with early-onset Alzheimer's disease
    • Romero I, Jorgensen P, Bolwig G, et al: A presenilin-1 Thr116Asn substitution in a family with early-onset Alzheimer's disease. Neuroreport 1999; 10:2255-2260
    • (1999) Neuroreport , vol.10 , pp. 2255-2260
    • Romero, I.1    Jorgensen, P.2    Bolwig, G.3
  • 47
    • 8244260610 scopus 로고    scopus 로고
    • Two novel (M233T and R278T) presenilin-1 mutations in early-onset Alzheimer's disease pedigrees and preliminary evidence for association of presenilin-1 mutations with a novel phenotype
    • Kwok JB, Taddei K, Hallupp M, et al: Two novel (M233T and R278T) presenilin-1 mutations in early-onset Alzheimer's disease pedigrees and preliminary evidence for association of presenilin-1 mutations with a novel phenotype. Neuroreport 1997; 8:1537-1542
    • (1997) Neuroreport , vol.8 , pp. 1537-1542
    • Kwok, J.B.1    Taddei, K.2    Hallupp, M.3
  • 48
    • 0027971051 scopus 로고
    • Phenotype of Chromosome 14-linked familial Alzheimer's disease in a large kindred
    • Lampe TH, Bird TD, Nochlin D, et al: Phenotype of Chromosome 14-linked familial Alzheimer's disease in a large kindred. Ann Neurol 1994; 36:368-378
    • (1994) Ann Neurol , vol.36 , pp. 368-378
    • Lampe, T.H.1    Bird, T.D.2    Nochlin, D.3
  • 49
    • 0028067657 scopus 로고
    • Chromosome 14-encoded Alzheimer's disease: Genetic and clinicopathological description
    • Haltia M, Viitanen M, Sulkava R, et al: Chromosome 14-encoded Alzheimer's disease: genetic and clinicopathological description. Ann Neurol 1994; 36:362-367
    • (1994) Ann Neurol , vol.36 , pp. 362-367
    • Haltia, M.1    Viitanen, M.2    Sulkava, R.3
  • 50
    • 0024581819 scopus 로고
    • Phenotypic heterogeneity in familial Alzheimer's disease: A study of 24 kindreds
    • Bird TD, Sumi SM, Nemens EJ, et al: Phenotypic heterogeneity in familial Alzheimer's disease: a study of 24 kindreds. Ann Neurol 1989; 25:12-25
    • (1989) Ann Neurol , vol.25 , pp. 12-25
    • Bird, T.D.1    Sumi, S.M.2    Nemens, E.J.3
  • 51
    • 0028910851 scopus 로고
    • Chromosome 14-linked familial Alzheimer's disease: A clinico-pathological study of a single pedigree
    • Kennedy AM, Newman SK, Frackowiak RS, et al: Chromosome 14-linked familial Alzheimer's disease: a clinico-pathological study of a single pedigree. Brain 1995; 118:185-205
    • (1995) Brain , vol.118 , pp. 185-205
    • Kennedy, A.M.1    Newman, S.K.2    Frackowiak, R.S.3
  • 52
    • 0033010135 scopus 로고    scopus 로고
    • A presenilin-1 mutation (Ser169Pro) associated with early-onset AD and myoclonic seizures
    • Ezquerra M, Carnero C, Blesa R, et al: A presenilin-1 mutation (Ser169Pro) associated with early-onset AD and myoclonic seizures. Neurology 1999; 52:566-570
    • (1999) Neurology , vol.52 , pp. 566-570
    • Ezquerra, M.1    Carnero, C.2    Blesa, R.3
  • 53
    • 0035798271 scopus 로고    scopus 로고
    • A novel presenilin mutation (M233V) causing very-early-onset Alzheimer's disease with Lewy bodies
    • Houlden H, Crook R, Dolan RJ, et al: A novel presenilin mutation (M233V) causing very-early-onset Alzheimer's disease with Lewy bodies. Neurosci Lett 2001; 313:93-95
    • (2001) Neurosci Lett , vol.313 , pp. 93-95
    • Houlden, H.1    Crook, R.2    Dolan, R.J.3
  • 54
    • 0021882237 scopus 로고
    • Heterogeneity in dementia of the Alzheimer type: Evidence of subgroups
    • Mayeux R, Stern Y, Spanton S: Heterogeneity in dementia of the Alzheimer type: evidence of subgroups. Neurology 1985; 35:453-461
    • (1985) Neurology , vol.35 , pp. 453-461
    • Mayeux, R.1    Stern, Y.2    Spanton, S.3
  • 55
    • 0027426406 scopus 로고
    • Age of onset in familial early-onset Alzheimer's disease correlates with genetic aetiology
    • Mullan M, Houlden H, Crawford F, et al: Age of onset in familial early-onset Alzheimer's disease correlates with genetic aetiology. Am J Med Genet 1993; 48:129-130
    • (1993) Am J Med Genet , vol.48 , pp. 129-130
    • Mullan, M.1    Houlden, H.2    Crawford, F.3
  • 56
    • 0034727634 scopus 로고    scopus 로고
    • A presenilin-1 mutation (Leu392Pro) in a familial AD kindred with psychiatric symptoms at onset
    • Tedde A, Forleo P, Nacmias B, et al: A presenilin-1 mutation (Leu392Pro) in a familial AD kindred with psychiatric symptoms at onset. Neurology 2000; 55:1590-1591
    • (2000) Neurology , vol.55 , pp. 1590-1591
    • Tedde, A.1    Forleo, P.2    Nacmias, B.3
  • 57
    • 0034727610 scopus 로고    scopus 로고
    • Dementia with prominent frontotemporal features associated with L113P presenilin-1 mutation
    • Raux G, Gantier R, Thomas-Anterion C, et al: Dementia with prominent frontotemporal features associated with L113P presenilin-1 mutation. Neurology 2000; 55:1577-1578
    • (2000) Neurology , vol.55 , pp. 1577-1578
    • Raux, G.1    Gantier, R.2    Thomas-Anterion, C.3
  • 58
    • 0036194338 scopus 로고    scopus 로고
    • A presenilin-1 mutation associated with familial frontotemporal dementia inhibits gamma-secretase cleavage of APP and notch
    • Amtul Z, Lewis PA, Piper S, et al: A presenilin-1 mutation associated with familial frontotemporal dementia inhibits gamma-secretase cleavage of APP and notch. Neurobiol Dis 2002; 9:269-273
    • (2002) Neurobiol Dis , vol.9 , pp. 269-273
    • Amtul, Z.1    Lewis, P.A.2    Piper, S.3
  • 59
    • 0034705011 scopus 로고    scopus 로고
    • Variable expression of familial Alzheimer disease associated with presenilin-2 mutation M2391
    • Finckh U, Alberici A, Antoniazzi M, et al: Variable expression of familial Alzheimer disease associated with presenilin-2 mutation M2391. Neurology 2000; 54:2006-2008
    • (2000) Neurology , vol.54 , pp. 2006-2008
    • Finckh, U.1    Alberici, A.2    Antoniazzi, M.3
  • 60
    • 0030499031 scopus 로고    scopus 로고
    • Wide range in age of onset for Chromosome 1-related familial Alzheimer's disease
    • Bird TD, Levy-Lahad E, Poorkaj P, et al: Wide range in age of onset for Chromosome 1-related familial Alzheimer's disease. Ann Neurol 1996; 40:932-936
    • (1996) Ann Neurol , vol.40 , pp. 932-936
    • Bird, T.D.1    Levy-Lahad, E.2    Poorkaj, P.3
  • 61
    • 0043025496 scopus 로고    scopus 로고
    • A novel mutation in the PSEN2 gene (T430M) associated with variable expression in a family with early-onset Alzheimer's disease
    • Ezquerra M, Lleó A, Castellvi M, et al: A novel mutation in the PSEN2 gene (T430M) associated with variable expression in a family with early-onset Alzheimer's disease. Arch Neurol 2003; 60:1149-1151
    • (2003) Arch Neurol , vol.60 , pp. 1149-1151
    • Ezquerra, M.1    Lleó, A.2    Castellvi, M.3
  • 62
    • 0032828163 scopus 로고    scopus 로고
    • Alzheimer disease PS-1 exon 9 deletion defined
    • Prihar G, Verkkoniemi A, Perez-Tur J, et al: Alzheimer disease PS-1 exon 9 deletion defined. Nat Med 1999; 5:1090
    • (1999) Nat Med , vol.5 , pp. 1090
    • Prihar, G.1    Verkkoniemi, A.2    Perez-Tur, J.3
  • 63
    • 0034813045 scopus 로고    scopus 로고
    • Very-early-onset Alzheimer's disease with spastic paraparesis associated with a novel presenilin-1 mutation (Phe237Ile)
    • Sodeyama N, Iwata T, Ishikawa K, et al: Very-early-onset Alzheimer's disease with spastic paraparesis associated with a novel presenilin-1 mutation (Phe237Ile). J Neurol Neurosurg Psychiatry 2001; 71:556-557
    • (2001) J Neurol Neurosurg Psychiatry , vol.71 , pp. 556-557
    • Sodeyama, N.1    Iwata, T.2    Ishikawa, K.3
  • 64
    • 0035831499 scopus 로고    scopus 로고
    • A pathogenic presenilin-1 deletion causes aberrant ABeta42 production in the absence of congophilic amyloid plaques
    • Steiner H, Revesz T, Neumann M, et al: A pathogenic presenilin-1 deletion causes aberrant ABeta42 production in the absence of congophilic amyloid plaques. J Biol Chem 2001; 276:7233-7239
    • (2001) J Biol Chem , vol.276 , pp. 7233-7239
    • Steiner, H.1    Revesz, T.2    Neumann, M.3
  • 65
    • 0037044295 scopus 로고    scopus 로고
    • Presenilin-1 mutation (E280G), spastic paraparesis, and cranial MRI white-matter abnormalities
    • O'Riordan S, McMonagle P, Janssen JC, et al: Presenilin-1 mutation (E280G), spastic paraparesis, and cranial MRI white-matter abnormalities. Neurology 2002; 59:1108-1110
    • (2002) Neurology , vol.59 , pp. 1108-1110
    • O'Riordan, S.1    McMonagle, P.2    Janssen, J.C.3
  • 66
    • 7844246535 scopus 로고    scopus 로고
    • Two novel presenilin-1 mutations (Ser169Leu and Pro436Gln) associated with very-early-onset Alzheimer's disease
    • Taddei K, Kwok JB, Kril JJ, et al: Two novel presenilin-1 mutations (Ser169Leu and Pro436Gln) associated with very-early-onset Alzheimer's disease. Neuroreport 1998; 9:3335-3339
    • (1998) Neuroreport , vol.9 , pp. 3335-3339
    • Taddei, K.1    Kwok, J.B.2    Kril, J.J.3
  • 67
    • 0037041304 scopus 로고    scopus 로고
    • Molecular evidence of presenilin-1 mutation in familial early-onset dementia
    • Matsubara-Tsutsui M, Yasuda M, Yamagata H, et al: Molecular evidence of presenilin-1 mutation in familial early-onset dementia. Am J Med Genet 2002; 114:292-298
    • (2002) Am J Med Genet , vol.114 , pp. 292-298
    • Matsubara-Tsutsui, M.1    Yasuda, M.2    Yamagata, H.3
  • 68
    • 0037435545 scopus 로고    scopus 로고
    • Pure spastic paraparesis associated with a novel presenilin-1 R278K mutation
    • Assini A, Terreni L, Borghi R, et al: Pure spastic paraparesis associated with a novel presenilin-1 R278K mutation. Neurology 2003; 60:150-151
    • (2003) Neurology , vol.60 , pp. 150-151
    • Assini, A.1    Terreni, L.2    Borghi, R.3
  • 69
    • 0034646249 scopus 로고    scopus 로고
    • Variant Alzheimer's disease with spastic paraparesis: Clinical characterization
    • Verkkoniemi A, Somer M, Rinne JO, et al: Variant Alzheimer's disease with spastic paraparesis: clinical characterization. Neurology 2000; 54:1103-1109
    • (2000) Neurology , vol.54 , pp. 1103-1109
    • Verkkoniemi, A.1    Somer, M.2    Rinne, J.O.3
  • 70
    • 0035000113 scopus 로고    scopus 로고
    • Variant Alzheimer disease with spastic paraparesis: Neuropathological phenotype
    • Verkkoniemi A, Kalimo H, Paetau A, et al: Variant Alzheimer disease with spastic paraparesis: neuropathological phenotype. J Neuropathol Exp Neurol 2001; 60:483-492
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 483-492
    • Verkkoniemi, A.1    Kalimo, H.2    Paetau, A.3
  • 71
    • 0037010284 scopus 로고    scopus 로고
    • Alzheimer's disease with spastic paresis and cotton wool-type plaques
    • Tabira T, Chui DH, Nakayama H, et al: Alzheimer's disease with spastic paresis and cotton wool-type plaques. J Neurosci Res 2002; 70:367-372
    • (2002) J Neurosci Res , vol.70 , pp. 367-372
    • Tabira, T.1    Chui, D.H.2    Nakayama, H.3
  • 72
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial British dementia
    • Vidal R, Frangione B, Rostagno A, et al: A stop-codon mutation in the BRI gene associated with familial British dementia. Nature 1999; 399:776-781
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3
  • 73
    • 15144345926 scopus 로고    scopus 로고
    • A novel presenilin-1 mutation: Increased beta-amyloid and neurofibrillary changes
    • Gomez-Isla T, Wasco W, Pettingell WP, et al: A novel presenilin-1 mutation: increased beta-amyloid and neurofibrillary changes. Ann Neurol 1997; 41:809-813
    • (1997) Ann Neurol , vol.41 , pp. 809-813
    • Gomez-Isla, T.1    Wasco, W.2    Pettingell, W.P.3
  • 74
    • 9444276544 scopus 로고    scopus 로고
    • Amyloid beta protein (ABeta) deposition in Chromosome 14-linked Alzheimer's disease: Predominance of ABeta42(43)
    • Mann DM, Iwatsubo T, Cairns NJ, et al: Amyloid beta protein (ABeta) deposition in Chromosome 14-linked Alzheimer's disease: predominance of ABeta42(43). Ann Neurol 1996; 40:149-156
    • (1996) Ann Neurol , vol.40 , pp. 149-156
    • Mann, D.M.1    Iwatsubo, T.2    Cairns, N.J.3
  • 75
    • 0034975365 scopus 로고    scopus 로고
    • Amyloid angiopathy and variability in amyloid beta deposition is determined by mutation position in presenilin-1-linked Alzheimer's disease
    • Mann DM, Pickering-Brown SM, Takeuchi A, et al: Amyloid angiopathy and variability in amyloid beta deposition is determined by mutation position in presenilin-1-linked Alzheimer's disease. Am J Pathol 2001; 158:2165-2175
    • (2001) Am J Pathol , vol.158 , pp. 2165-2175
    • Mann, D.M.1    Pickering-Brown, S.M.2    Takeuchi, A.3
  • 76
    • 16044365171 scopus 로고    scopus 로고
    • The E280A presenilin-1 Alzheimer mutation produces increased ABeta 42 deposition and severe cerebellar pathology
    • Lemere CA, Lopera F, Kosik KS, et al: The E280A presenilin-1 Alzheimer mutation produces increased ABeta 42 deposition and severe cerebellar pathology. Nat Med 1996; 2:1146-1150
    • (1996) Nat Med , vol.2 , pp. 1146-1150
    • Lemere, C.A.1    Lopera, F.2    Kosik, K.S.3
  • 77
    • 0031866674 scopus 로고    scopus 로고
    • Apolipoprotein-E genotype and deposits of ABeta40 and ABeta42 in Alzheimer disease
    • McNamara MJ, Gomez-Isla T, Hyman BT: Apolipoprotein-E genotype and deposits of ABeta40 and ABeta42 in Alzheimer disease. Arch Neurol 1998; 55:1001-1004
    • (1998) Arch Neurol , vol.55 , pp. 1001-1004
    • McNamara, M.J.1    Gomez-Isla, T.2    Hyman, B.T.3
  • 78
    • 18344417178 scopus 로고    scopus 로고
    • Lewy bodies contain altered alpha-synuclein in brains of many familial Alzheimer's disease patients with mutations in presenilin and amyloid precursor protein genes
    • Lippa CF, Fujiwara H, Mann DM, et al: Lewy bodies contain altered alpha-synuclein in brains of many familial Alzheimer's disease patients with mutations in presenilin and amyloid precursor protein genes. Am J Pathol 1998; 153:1365-1370
    • (1998) Am J Pathol , vol.153 , pp. 1365-1370
    • Lippa, C.F.1    Fujiwara, H.2    Mann, D.M.3
  • 79
    • 0034759869 scopus 로고    scopus 로고
    • Alpha-synuclein in familial Alzheimer disease: Epitope mapping parallels dementia with Lewy bodies and Parkinson disease
    • Lippa CF, Schmidt ML, Lee VM, et al: Alpha-synuclein in familial Alzheimer disease: epitope mapping parallels dementia with Lewy bodies and Parkinson disease. Arch Neurol 2001; 58:1817-1820
    • (2001) Arch Neurol , vol.58 , pp. 1817-1820
    • Lippa, C.F.1    Schmidt, M.L.2    Lee, V.M.3
  • 80
    • 0034763328 scopus 로고    scopus 로고
    • Cottonwool plaques in non-familial late-onset Alzheimer disease
    • Le TV, Crook R, Hardy J, et al: Cottonwool plaques in non-familial late-onset Alzheimer disease. J Neuropathol Exp Neurol 2001; 60:1051-1061
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 1051-1061
    • Le, T.V.1    Crook, R.2    Hardy, J.3
  • 81
    • 8044251536 scopus 로고    scopus 로고
    • The clinical phenotype of two missense mutations in the presenilin-1 gene in Japanese patients
    • Ikeda M, Sharma V, Sumi SM, et al: The clinical phenotype of two missense mutations in the presenilin-1 gene in Japanese patients. Ann Neurol 1996; 40:912-917
    • (1996) Ann Neurol , vol.40 , pp. 912-917
    • Ikeda, M.1    Sharma, V.2    Sumi, S.M.3
  • 82
    • 0032587237 scopus 로고    scopus 로고
    • Evidence that ABeta42 plasma levels in presenilin-1 mutation carriers do not allow for prediction of their clinical phenotype
    • De Jonghe C, Cras P, Vanderstichele H, et al: Evidence that ABeta42 plasma levels in presenilin-1 mutation carriers do not allow for prediction of their clinical phenotype. Neurobiol Dis 1999; 6:280-287
    • (1999) Neurobiol Dis , vol.6 , pp. 280-287
    • De Jonghe, C.1    Cras, P.2    Vanderstichele, H.3
  • 83
    • 0033537921 scopus 로고    scopus 로고
    • Enhancement of amyloid beta 42 secretion by 28 different presenilin-1 mutations of familial Alzheimer's disease
    • Murayama O, Tomita T, Nihonmatsu N, et al: Enhancement of amyloid beta 42 secretion by 28 different presenilin-1 mutations of familial Alzheimer's disease. Neurosci Lett 1999; 265:61-63
    • (1999) Neurosci Lett , vol.265 , pp. 61-63
    • Murayama, O.1    Tomita, T.2    Nihonmatsu, N.3
  • 84
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • Xia W, Zhang J, Kholodenko D, et al: Enhanced production and oligomerization of the 42-residue amyloid beta-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J Biol Chem 1997; 272:7977-7982
    • (1997) J Biol Chem , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3
  • 85
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin-1 variants elevate ABeta1-42/1-40 ratio in vitro and in vivo
    • Borchelt DR, Thinakaran G, Eckman CB, et al: Familial Alzheimer's disease-linked presenilin-1 variants elevate ABeta1-42/1-40 ratio in vitro and in vivo. Neuron 1996; 17:1005-1013
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3
  • 86
    • 0032875462 scopus 로고    scopus 로고
    • Proteolytic processing of presenilin-1 in human lymphoblasts is not affected by the presence of the I143T and G384A mutations
    • Vanderhoeven I, Cras P, Martin JJ, et al: Proteolytic processing of presenilin-1 in human lymphoblasts is not affected by the presence of the I143T and G384A mutations. Neurosci Lett 1999; 274:183-186
    • (1999) Neurosci Lett , vol.274 , pp. 183-186
    • Vanderhoeven, I.1    Cras, P.2    Martin, J.J.3
  • 87
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe MS, Xia W, Ostaszewski BL, et al: Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 1999; 398:513-517
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3
  • 88
    • 0034714316 scopus 로고    scopus 로고
    • Presenilin-1 regulates pharmacologically distinct gamma-secretase activities implications for the role of presenilin in gamma-secretase cleavage
    • Murphy MP, Uljon SN, Fraser PE, et al: Presenilin-1 regulates pharmacologically distinct gamma-secretase activities implications for the role of presenilin in gamma-secretase cleavage. J Biol Chem 2000; 275:26277-26284
    • (2000) J Biol Chem , vol.275 , pp. 26277-26284
    • Murphy, M.P.1    Uljon, S.N.2    Fraser, P.E.3
  • 89
    • 0028169925 scopus 로고
    • Visualization of ABeta 42(43) and ABeta 40 in senile plaques with end-specific ABeta monoclonals: Evidence that an initially deposited species is ABeta 42(43)
    • Iwatsubo T, Odaka A, Suzuki N, et al: Visualization of ABeta 42(43) and ABeta 40 in senile plaques with end-specific ABeta monoclonals: evidence that an initially deposited species is ABeta 42(43). Neuron 1994; 13:45-53
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3
  • 90
    • 0030917601 scopus 로고    scopus 로고
    • Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid beta-peptide: Involvement of calcium and oxyradicals
    • Guo Q, Sopher BL, Furukawa K, et al: Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid beta-peptide: involvement of calcium and oxyradicals. J Neurosci 1997; 17:4212-4222
    • (1997) J Neurosci , vol.17 , pp. 4212-4222
    • Guo, Q.1    Sopher, B.L.2    Furukawa, K.3
  • 91
    • 0033009194 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons from presenilin-1 mutant knock-in mice to amyloid beta-peptide toxicity: Central roles of superoxide production and caspase activation
    • Guo Q, Sebastian L, Sopher BL, et al: Increased vulnerability of hippocampal neurons from presenilin-1 mutant knock-in mice to amyloid beta-peptide toxicity: central roles of superoxide production and caspase activation. J Neurochem 1999; 72:1019-1029
    • (1999) J Neurochem , vol.72 , pp. 1019-1029
    • Guo, Q.1    Sebastian, L.2    Sopher, B.L.3
  • 92
    • 0033258544 scopus 로고    scopus 로고
    • Presenilin-1 mutations downregulate the signaling pathway of the unfolded-protein response
    • Katayama T, Imaizumi K, Sato N, et al: Presenilin-1 mutations downregulate the signaling pathway of the unfolded-protein response. Nat Cell Biol 1999; 1:479-485
    • (1999) Nat Cell Biol , vol.1 , pp. 479-485
    • Katayama, T.1    Imaizumi, K.2    Sato, N.3
  • 93
    • 0036828371 scopus 로고    scopus 로고
    • Involvement of Gadd153 in the pathogenic action of presenilin-1 mutations
    • Milhavet O, Martindale JL, Camandola S, et al: Involvement of Gadd153 in the pathogenic action of presenilin-1 mutations. J Neurochem 2002; 83:673-681
    • (2002) J Neurochem , vol.83 , pp. 673-681
    • Milhavet, O.1    Martindale, J.L.2    Camandola, S.3
  • 94
    • 0033671650 scopus 로고    scopus 로고
    • Upregulation of BiP and CHOP by the unfolded-protein response is independent of presenilin expression
    • Sato N, Urano F, Yoon Leem J, et al: Upregulation of BiP and CHOP by the unfolded-protein response is independent of presenilin expression. Nat Cell Biol 2000; 2:863-870
    • (2000) Nat Cell Biol , vol.2 , pp. 863-870
    • Sato, N.1    Urano, F.2    Yoon Leem, J.3
  • 95
    • 0035976923 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced cysteine protease activation in cortical neurons: Effect of an Alzheimer's disease-linked presenilin-1 knock-in mutation
    • Siman R, Flood DG, Thinakaran G, et al: Endoplasmic reticulum stress-induced cysteine protease activation in cortical neurons: effect of an Alzheimer's disease-linked presenilin-1 knock-in mutation. J Biol Chem 2001; 276:44736-44743
    • (2001) J Biol Chem , vol.276 , pp. 44736-44743
    • Siman, R.1    Flood, D.G.2    Thinakaran, G.3
  • 96
    • 0038652102 scopus 로고    scopus 로고
    • Gamma-secretase is a membrane protein complex composed of presenilin, nicastrin, aph-1, and pen-2
    • in press
    • Kimberly WT, LaVoie MJ, Ostaszewski BL, et al: Gamma-secretase is a membrane protein complex composed of presenilin, nicastrin, aph-1, and pen-2. Proc Natl Acad Sci U S A 2003; (in press)
    • (2003) Proc Natl Acad Sci U S A
    • Kimberly, W.T.1    LaVoie, M.J.2    Ostaszewski, B.L.3
  • 97
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated Notch/glp-1 signal transduction and beta-APP processing
    • Yu G, Nishimura M, Arawaka S, et al: Nicastrin modulates presenilin-mediated Notch/glp-1 signal transduction and beta-APP processing. Nature 2000; 407:48-54
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1    Nishimura, M.2    Arawaka, S.3
  • 98
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Sudhof TC: A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 2001; 293:115-120
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 99
    • 0035909901 scopus 로고    scopus 로고
    • The gamma-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus
    • Gao Y, Pimplikar SW: The gamma-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc Natl Acad Sci U S A 2001; 98:14979-14984
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14979-14984
    • Gao, Y.1    Pimplikar, S.W.2
  • 100
    • 0036677928 scopus 로고    scopus 로고
    • Direct visualization of the gamma-secretase-generated carboxyl-terminal domain of the amyloid precursor protein: Association with Fe65 and translocation to the nucleus
    • Kinoshita A, Whelan CM, Smith CJ, et al: Direct visualization of the gamma-secretase-generated carboxyl-terminal domain of the amyloid precursor protein: association with Fe65 and translocation to the nucleus. J Neurochem 2002; 82:839-847
    • (2002) J Neurochem , vol.82 , pp. 839-847
    • Kinoshita, A.1    Whelan, C.M.2    Smith, C.J.3
  • 101
    • 0034839287 scopus 로고    scopus 로고
    • The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture
    • Cupers P, Orlans I, Craessaerts K, et al: The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture. J Neurochem 2001; 78:1168-1178
    • (2001) J Neurochem , vol.78 , pp. 1168-1178
    • Cupers, P.1    Orlans, I.2    Craessaerts, K.3
  • 102
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: Cell fate control and signal integration in development
    • Artavanis-Tsanokas S, Rand MD, Lake RJ: Notch signaling: cell fate control and signal integration in development. Science 1999; 284:770-776
    • (1999) Science , vol.284 , pp. 770-776
    • Artavanis-Tsanokas, S.1    Rand, M.D.2    Lake, R.J.3
  • 103
    • 0036727125 scopus 로고    scopus 로고
    • Gamma-secretase-mediated proteolysis in cell-surface-receptor signaling
    • Fortini ME: Gamma-secretase-mediated proteolysis in cell-surface-receptor signaling. Nat Rev Neurosci 2002; 3:673-684
    • (2002) Nat Rev Neurosci , vol.3 , pp. 673-684
    • Fortini, M.E.1
  • 104
    • 0032771052 scopus 로고    scopus 로고
    • Notch1 inhibits neurite outgrowth in postmitotic primary neurons
    • Berezovska O, McLean P, Knowles R, et al: Notch1 inhibits neurite outgrowth in postmitotic primary neurons. Neuroscience 1999; 93:433-439
    • (1999) Neuroscience , vol.93 , pp. 433-439
    • Berezovska, O.1    McLean, P.2    Knowles, R.3
  • 105
    • 0031847249 scopus 로고    scopus 로고
    • Notch is expressed in adult brain, is coexpressed with presenilin-1, and is altered in Alzheimer disease
    • Berezovska O, Xia MQ, Hyman BT: Notch is expressed in adult brain, is coexpressed with presenilin-1, and is altered in Alzheimer disease. J Neuropathol Exp Neurol 1998; 57:738-745
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 738-745
    • Berezovska, O.1    Xia, M.Q.2    Hyman, B.T.3
  • 106
    • 0035809789 scopus 로고    scopus 로고
    • Effect of PS-1 deficiency and an APP gamma-secretase inhibitor on Notchl signaling in primary mammalian neurons
    • Jack C, Berezovska O, Wolfe MS, et al: Effect of PS-1 deficiency and an APP gamma-secretase inhibitor on Notchl signaling in primary mammalian neurons. Brain Res Mol Brain Res 2001; 87:166-174
    • (2001) Brain Res Mol Brain Res , vol.87 , pp. 166-174
    • Jack, C.1    Berezovska, O.2    Wolfe, M.S.3
  • 107
    • 0033944273 scopus 로고    scopus 로고
    • Aspartate mutations in presenilin and gamma-secretase inhibitors both impair Notch 1 proteolysis and nuclear translocation with relative preservation of Notch 1 signaling
    • Berezovska O, Jack C, McLean P, et al: Aspartate mutations in presenilin and gamma-secretase inhibitors both impair Notch 1 proteolysis and nuclear translocation with relative preservation of Notch 1 signaling. J Neurochem 2000; 75:583-593
    • (2000) J Neurochem , vol.75 , pp. 583-593
    • Berezovska, O.1    Jack, C.2    McLean, P.3
  • 108
    • 0029116848 scopus 로고
    • Facilitation of lin-12-mediated signaling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • Levitan D, Greenwald I: Facilitation of lin-12-mediated signaling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 1995; 377:351-354
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 109
    • 0036565893 scopus 로고    scopus 로고
    • Identification of a novel family of presenilin homologues
    • Ponting CP, Hutton M, Nyborg A, et al: Identification of a novel family of presenilin homologues. Hum Mol Genet 2002; 11:1037-1044
    • (2002) Hum Mol Genet , vol.11 , pp. 1037-1044
    • Ponting, C.P.1    Hutton, M.2    Nyborg, A.3
  • 110
    • 0030832449 scopus 로고    scopus 로고
    • Different effects of Alzheimer-associated mutations of presenilin-1 on its processing
    • Murayama O, Honda T, Mercken M, et al: Different effects of Alzheimer-associated mutations of presenilin-1 on its processing. Neurosci Lett 1997; 229:61-64
    • (1997) Neurosci Lett , vol.229 , pp. 61-64
    • Murayama, O.1    Honda, T.2    Mercken, M.3
  • 111
    • 9344237637 scopus 로고    scopus 로고
    • Complete analysis of the presenilin-1 gene in early-onset Alzheimer's disease
    • Hutton M, Busfield F, Wragg M, et al: Complete analysis of the presenilin-1 gene in early-onset Alzheimer's disease. Neuroreport 1996; 7:801-805
    • (1996) Neuroreport , vol.7 , pp. 801-805
    • Hutton, M.1    Busfield, F.2    Wragg, M.3
  • 112
    • 0028861041 scopus 로고
    • Molecular genetic analysis of familial early-onset Alzheimer's disease linked to Chromosome 14q24.3
    • Cruts M, Backhovens H, Wang SY, et al: Molecular genetic analysis of familial early-onset Alzheimer's disease linked to Chromosome 14q24.3. Hum Mol Genet 1995; 4:2363-2371
    • (1995) Hum Mol Genet , vol.4 , pp. 2363-2371
    • Cruts, M.1    Backhovens, H.2    Wang, S.Y.3
  • 113
    • 0025959458 scopus 로고
    • Early-onset Alzheimer's disease in two large Belgian families
    • Martin JJ, Gheuens J, Bruyland M, et al: Early-onset Alzheimer's disease in two large Belgian families. Neurology 1991; 41:62-68
    • (1991) Neurology , vol.41 , pp. 62-68
    • Martin, J.J.1    Gheuens, J.2    Bruyland, M.3
  • 114
    • 0029115555 scopus 로고
    • The structure of the presenilin-1 (S182) gene and identification of six novel mutations in early-onset AD families
    • Alzheimer's Disease Collaborative Group: The structure of the presenilin-1 (S182) gene and identification of six novel mutations in early-onset AD families. Nat Genet 1995; 11:219-222
    • (1995) Nat Genet , vol.11 , pp. 219-222
  • 115
    • 0029157347 scopus 로고
    • Missense mutations of S182 gene in Italian families with early-onset Alzheimer's disease
    • Sorbi S, Nacmias B, Forleo P, et al: Missense mutations of S182 gene in Italian families with early-onset Alzheimer's disease. Lancet 1995; 346:439-440
    • (1995) Lancet , vol.346 , pp. 439-440
    • Sorbi, S.1    Nacmias, B.2    Forleo, P.3
  • 116
    • 0034041861 scopus 로고    scopus 로고
    • A novel presenilin-1 mutation (Leu166Arg) associated with early-onset Alzheimer disease
    • Ezquerra M, Carnero C, Blesa R, et al: A novel presenilin-1 mutation (Leu166Arg) associated with early-onset Alzheimer disease. Arch Neurol 2000; 57:485-488
    • (2000) Arch Neurol , vol.57 , pp. 485-488
    • Ezquerra, M.1    Carnero, C.2    Blesa, R.3
  • 117
    • 0031971693 scopus 로고    scopus 로고
    • Chromosome-14 familial Alzheimer's disease: The clinical and neuropathological characteristics of a family with a leucine > serine (L250S) substitution at codon 250 of the presenilin-1 gene
    • Harvey RJ, Ellison D, Hardy J, et al: Chromosome-14 familial Alzheimer's disease: the clinical and neuropathological characteristics of a family with a leucine > serine (L250S) substitution at codon 250 of the presenilin-1 gene. J Neurol Neurosurg Psychiatry 1998; 64:44-49
    • (1998) J Neurol Neurosurg Psychiatry , vol.64 , pp. 44-49
    • Harvey, R.J.1    Ellison, D.2    Hardy, J.3
  • 118
    • 0029094267 scopus 로고
    • Familial Alzheimer's disease associated with S182 codon 286 mutation
    • Chapman J, Asherov A, Wang N, et al: Familial Alzheimer's disease associated with S182 codon 286 mutation. Lancet 1995; 346:1040
    • (1995) Lancet , vol.346 , pp. 1040
    • Chapman, J.1    Asherov, A.2    Wang, N.3
  • 119
    • 0033623415 scopus 로고    scopus 로고
    • ABeta-generating enzymes: Recent advances in beta- and gamma-secretase research
    • Vassar R, Citron M: ABeta-generating enzymes: recent advances in beta- and gamma-secretase research. Neuron 2000; 27:419-422
    • (2000) Neuron , vol.27 , pp. 419-422
    • Vassar, R.1    Citron, M.2
  • 120
    • 0347785491 scopus 로고    scopus 로고
    • Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an ABeta-like peptide
    • Lammich S, Okochi M, Takeda M, et al: Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an ABeta-like peptide. J Biol Chem 2002; 277:44754-44759
    • (2002) J Biol Chem , vol.277 , pp. 44754-44759
    • Lammich, S.1    Okochi, M.2    Takeda, M.3
  • 121
    • 0035956921 scopus 로고    scopus 로고
    • Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex
    • Baki L, Marambaud P, Efthiniiopoulos S, et al: Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex. Proc Natl Acad Sci U S A 2001; 98:2381-2386
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2381-2386
    • Baki, L.1    Marambaud, P.2    Efthiniiopoulos, S.3
  • 122
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P, Shioi J, Serban G, et al: A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J 2002; 21:1948-1956
    • (2002) EMBO J , vol.21 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3
  • 123
    • 0035824391 scopus 로고    scopus 로고
    • Gamma-secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni CY, Murphy MP, Golde TE, et al: Gamma-secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 2001; 294:2179-2181
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3
  • 124
    • 0037155219 scopus 로고    scopus 로고
    • Presenilin-dependent gamma-secretase-like intramembrane cleavage of ErbB4
    • Lee HJ, Jung KM, Huang YZ, et al: Presenilin-dependent gamma-secretase-like intramembrane cleavage of ErbB4. J Biol Chem 2002; 277:6318-6323
    • (2002) J Biol Chem , vol.277 , pp. 6318-6323
    • Lee, H.J.1    Jung, K.M.2    Huang, Y.Z.3
  • 125
    • 0037166319 scopus 로고    scopus 로고
    • Proteolytic processing of low-density lipoprotein receptor-related protein mediates regulated release of its intracellular domain
    • May P, Reddy YK, Herz J: Proteolytic processing of low-density lipoprotein receptor-related protein mediates regulated release of its intracellular domain. J Biol Chem 2002; 277:18736-18743
    • (2002) J Biol Chem , vol.277 , pp. 18736-18743
    • May, P.1    Reddy, Y.K.2    Herz, J.3
  • 126
    • 0037146553 scopus 로고    scopus 로고
    • Nectin-1alpha, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/gamma-secretase-like cleavage
    • Kim DY, Ingano LA, Kovacs DM: Nectin-1alpha, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/gamma-secretase-like cleavage. J Biol Chem 2002; 277:49976-49981
    • (2002) J Biol Chem , vol.277 , pp. 49976-49981
    • Kim, D.Y.1    Ingano, L.A.2    Kovacs, D.M.3
  • 127
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper B, Annaert W, Cupers P, et al: A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature 1999; 398:518-522
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1    Annaert, W.2    Cupers, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.