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Volumn 41, Issue 2, 2007, Pages 294-307

Molecular basis of Alzheimer's disease

Author keywords

Alzheimer's disease; APP; IMP IMPAS SPP SPPL; Intramembrane proteolysis; Presenilins

Indexed keywords


EID: 34247512523     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893307020100     Document Type: Article
Times cited : (11)

References (81)
  • 1
    • 29144508843 scopus 로고    scopus 로고
    • Global prevalence of dementia: A Delphi consensus study
    • Ferri C.P., Prince M., Brayne C., et al. 2005. Global prevalence of dementia: A Delphi consensus study. Lancet. 366, 2112-2117.
    • (2005) Lancet , vol.366 , pp. 2112-2117
    • Ferri, C.P.1    Prince, M.2    Brayne, C.3
  • 2
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • Serpell L.C. 2000. Alzheimer's amyloid fibrils: Structure and assembly. Biochim. Biophys. Acta. 1502, 16-30.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 3
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G.G., Wong C.W. 1984. Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 4
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner G.G., Wong C.W. 1984. Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122, 1131-1135.
    • (1984) Biochem. Biophys. Res. Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D., Lerman M.I., McBride O.W., et al. 1987. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science. 235, 877-880.
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3
  • 6
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J., Lemaire H.G., Unterbeck A., et al. 1987. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature. 325, 733-736.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 7
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A., Chartier-Harlin M.C., Mullan M., et al. 1991. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature. 349, 704-706.
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3
  • 8
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy J.A., Higgins G.A. 1992. Alzheimer's disease: The amyloid cascade hypothesis. Science. 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 9
    • 34247470620 scopus 로고    scopus 로고
    • Hardy J. 2003. The Genetics of Alzheimer's Disease. In: Alzheimer's Disease and Related Disorders: Research Advances. Eds. Iqbal K., Winblad B. Bucharest: Ana. Aslan. Intl. Acad. of Aging, 29-47.
    • Hardy J. 2003. The Genetics of Alzheimer's Disease. In: Alzheimer's Disease and Related Disorders: Research Advances. Eds. Iqbal K., Winblad B. Bucharest: Ana. Aslan. Intl. Acad. of Aging, 29-47.
  • 10
    • 0027032695 scopus 로고
    • Genetic evidence for a novel familial Alzheimer's disease locus on chromosome 14
    • St. George-Hyslop P., Haines J., Rogaev E., et al. 1992. Genetic evidence for a novel familial Alzheimer's disease locus on chromosome 14. Nature Genet. 2, 330-334.
    • (1992) Nature Genet , vol.2 , pp. 330-334
    • St. George-Hyslop, P.1    Haines, J.2    Rogaev, E.3
  • 11
    • 0026471656 scopus 로고
    • Genetic linkage evidence for a familial Alzhe imer's disease locus on chromosome 14
    • Schellenberg G.D., Bird T.D., Wijsman E.M., et al. 1992. Genetic linkage evidence for a familial Alzhe imer's disease locus on chromosome 14. Science. 258, 668-671.
    • (1992) Science , vol.258 , pp. 668-671
    • Schellenberg, G.D.1    Bird, T.D.2    Wijsman, E.M.3
  • 12
    • 0027024651 scopus 로고    scopus 로고
    • Mullan M., Houlden H., Windelspecht M., et al. 1992. A locus for familial early-onset Alzheimer's disease on the long arm of chromosome 14, proximal to the α1-antichymotrypsin gene. Nature Genet. 2, 340-342.
    • Mullan M., Houlden H., Windelspecht M., et al. 1992. A locus for familial early-onset Alzheimer's disease on the long arm of chromosome 14, proximal to the α1-antichymotrypsin gene. Nature Genet. 2, 340-342.
  • 13
    • 0027031612 scopus 로고
    • Alzheimer's disease to chromosome 14q24.3
    • Mapping of a gene predisposing to early-onset
    • Van Broeckhoven C., Backhovens H., Cruts M., et al. 1992. Mapping of a gene predisposing to early-onset Alzheimer's disease to chromosome 14q24.3. Nature Genet. 2, 335-339.
    • (1992) Nature Genet , vol.2 , pp. 335-339
    • Van Broeckhoven, C.1    Backhovens, H.2    Cruts, M.3
  • 14
    • 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 E.I., Sherrington R., Rogaeva E.A., et al. 1995. 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. 376, 775-778.
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3
  • 15
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington R., Rogaev E.I., Liang Y., et al. 1995. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 375, 754-760.
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 16
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • Levy-Lahad E., Wasco W., Poorkaj P., et al. 1995. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science. 269, 973-977.
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 19
    • 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. 1998. A variant of Alzheimer's disease with spastic paraparesis and unusual plaques due to deletion of exon 9 of presenilin 1. Nature Med. 4, 452-455.
    • (1998) Nature Med , vol.4 , pp. 452-455
    • Crook, R.1    Verkkoniemi, A.2    Perez-Tur, J.3
  • 20
    • 0025735884 scopus 로고
    • Linkage studies in familial Alzheimer disease: Evidence for chromosome 19 linkage
    • Pericak-Vance M.A., Bebout J.L., Gaskell P.C. Jr., et al. 1991. Linkage studies in familial Alzheimer disease: Evidence for chromosome 19 linkage. Am. J. Hum. Genet. 48, 1034-1050.
    • (1991) Am. J. Hum. Genet , vol.48 , pp. 1034-1050
    • Pericak-Vance, M.A.1    Bebout, J.L.2    Gaskell Jr., P.C.3
  • 21
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families
    • Corder E.H., Saunders A.M., Strittmatter W.J., et al. 1993. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science. 261, 921-923.
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1    Saunders, A.M.2    Strittmatter, W.J.3
  • 22
    • 0028178047 scopus 로고
    • Apolipoprotein E, ε4 allele as a major risk factor for sporadic early- and late-onset forms of Alzheimer's disease: Analysis of the 19q13.2 chromosomal region
    • Chartier-Harlin M.C., Parfitt M., Legrain S., et al. 1994. Apolipoprotein E, ε4 allele as a major risk factor for sporadic early- and late-onset forms of Alzheimer's disease: Analysis of the 19q13.2 chromosomal region. Human Mol. Genet. 3, 569-574.
    • (1994) Human Mol. Genet , vol.3 , pp. 569-574
    • Chartier-Harlin, M.C.1    Parfitt, M.2    Legrain, S.3
  • 23
    • 0033220122 scopus 로고    scopus 로고
    • Genetic factors and a polygenic model of Alzheimer's disease
    • Rogaev E.I. Genetic factors and a polygenic model of Alzheimer's disease. Genetika. 35, 1558-1571.
    • Genetika , vol.35 , pp. 1558-1571
    • Rogaev, E.I.1
  • 24
    • 0036385788 scopus 로고    scopus 로고
    • Regulatory region variability in the human presenilin-2 (PSEN2) gene: Potential contribution to the gene activity and risk for AD
    • Riazanskaia N., Lukiw W.J., Grigorenko A., et al. 2002. Regulatory region variability in the human presenilin-2 (PSEN2) gene: Potential contribution to the gene activity and risk for AD. Mol. Psychiatry. 7, 891-898.
    • (2002) Mol. Psychiatry , vol.7 , pp. 891-898
    • Riazanskaia, N.1    Lukiw, W.J.2    Grigorenko, A.3
  • 25
    • 0028305380 scopus 로고
    • Alzheimer disease
    • Protective effect of apolipoprotein E type 2 allele for late onset
    • Corder E.H., Saunders A.M., Risch N.J., et al. 1994. Protective effect of apolipoprotein E type 2 allele for late onset Alzheimer disease. Nature Genet. 7, 180-184.
    • (1994) Nature Genet , vol.7 , pp. 180-184
    • Corder, E.H.1    Saunders, A.M.2    Risch, N.J.3
  • 26
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-β protein assembly in the brain impairs memory
    • Lesne S., Koh M.T., Kotilinek L., et al. 2006. A specific amyloid-β protein assembly in the brain impairs memory. Nature. 440, 352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 27
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline
    • Naslund J., Haroutunian V., Mohs R., et al. 2000. Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. J. Am. Med. Ass. 283, 1571-1577.
    • (2000) J. Am. Med. Ass , vol.283 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3
  • 28
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associ ated protein tau (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I., Iqbal K., Tung Y.C., et al. 1986. Abnormal phosphorylation of the microtubule-associ ated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. USA. 83, 4913-4917.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3
  • 29
    • 0033041179 scopus 로고    scopus 로고
    • Association of an extended haplotype in the tau gene with progressive supranuclear palsy
    • Baker M., Litvan I., Houlden H., et al. 1999. Association of an extended haplotype in the tau gene with progressive supranuclear palsy. Human Mol. Genet. 8, 711-715.
    • (1999) Human Mol. Genet , vol.8 , pp. 711-715
    • Baker, M.1    Litvan, I.2    Houlden, H.3
  • 30
    • 33646886350 scopus 로고    scopus 로고
    • Promoter mutations that increase amyloid precursor-protein expression are associated with Alzheimer disease
    • Theuns J., Brouwers N., Engelborghs S., et al. 2006. Promoter mutations that increase amyloid precursor-protein expression are associated with Alzheimer disease. Am. J. Hum. Genet. 78, 936-946.
    • (2006) Am. J. Hum. Genet , vol.78 , pp. 936-946
    • Theuns, J.1    Brouwers, N.2    Engelborghs, S.3
  • 31
    • 0034704198 scopus 로고    scopus 로고
    • Evidence for genetic linkage of Alzheimer's disease to chromosome 10q
    • Bertram L., Blacker D., Mullin K., et al. 2000. Evidence for genetic linkage of Alzheimer's disease to chromosome 10q. Science. 290, 2302-2303.
    • (2000) Science , vol.290 , pp. 2302-2303
    • Bertram, L.1    Blacker, D.2    Mullin, K.3
  • 32
    • 0030770726 scopus 로고    scopus 로고
    • Complete genomic screen in late-onset familial Alzheimer disease: Evidence for a new locus on chromosome 12
    • Pericak-Vance M.A., Bass M.P., Yamaoka L.H., et al. 1997. Complete genomic screen in late-onset familial Alzheimer disease: Evidence for a new locus on chromosome 12. J. Am. Med. Assoc. 278, 1237-1241.
    • (1997) J. Am. Med. Assoc , vol.278 , pp. 1237-1241
    • Pericak-Vance, M.A.1    Bass, M.P.2    Yamaoka, L.H.3
  • 33
    • 0032899712 scopus 로고    scopus 로고
    • Alzheimer's disease
    • A full genome scan for late onset
    • Kehoe P., Wavrant-De Vrieze V.F., Crook R., et al. 1999. A full genome scan for late onset Alzheimer's disease. Human Mol. Genet. 8, 237-245.
    • (1999) Human Mol. Genet , vol.8 , pp. 237-245
    • Kehoe, P.1    Wavrant-De Vrieze, V.F.2    Crook, R.3
  • 34
    • 0031939059 scopus 로고    scopus 로고
    • Molecular mapping of Alzheimer-type dementia in Down's syndrome
    • Prasher V.P., Farrer M.J., Kessling A.M., et al. 1998. Molecular mapping of Alzheimer-type dementia in Down's syndrome. Ann. Neural. 43, 380-383.
    • (1998) Ann. Neural , vol.43 , pp. 380-383
    • Prasher, V.P.1    Farrer, M.J.2    Kessling, A.M.3
  • 35
    • 29444442794 scopus 로고    scopus 로고
    • Alzheimer disease with cerebral amyloid angiopathy
    • APP locus duplication causes autosomal dominant early-onset
    • Rovelet-Lecrux A., Hannequin D., Raux G., et al. 2006. APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy. Nature Genet. 38, 24-26.
    • (2006) Nature Genet , vol.38 , pp. 24-26
    • Rovelet-Lecrux, A.1    Hannequin, D.2    Raux, G.3
  • 36
    • 1642573171 scopus 로고    scopus 로고
    • Impas 1 possesses endoproteolytic activity against multipass membrane protein substrate cleaving the presenilin 1 holoprotein
    • Moliaka Y.K., Grigorenko A., Madera D., Rogaev E.I. 2004. Impas 1 possesses endoproteolytic activity against multipass membrane protein substrate cleaving the presenilin 1 holoprotein. FEBS Lett. 557, 185-192.
    • (2004) FEBS Lett , vol.557 , pp. 185-192
    • Moliaka, Y.K.1    Grigorenko, A.2    Madera, D.3    Rogaev, E.I.4
  • 37
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran G., Borchelt D.R., Lee M.K., et al. 1996. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron. 17, 181-190.
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3
  • 39
    • 0042536471 scopus 로고    scopus 로고
    • Neuronal and glial calcium signaling in Alzheimer's disease
    • Mattson M.P., Chan S.L. 2003. Neuronal and glial calcium signaling in Alzheimer's disease. Cell Calcium. 34, 385-397.
    • (2003) Cell Calcium , vol.34 , pp. 385-397
    • Mattson, M.P.1    Chan, S.L.2
  • 40
    • 16044373524 scopus 로고    scopus 로고
    • 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
    • Scheuner D., Eckman C., Jensen M., et al. 1996. 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. Nature Med. 2, 864-870.
    • (1996) Nature Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 41
    • 0035955693 scopus 로고    scopus 로고
    • Kimberly W.T., Zheng J.B., Guenette S.Y., Selkoe D.J. 2001. The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J. Biol. Chem. 276, 40, 288-40, 292.
    • Kimberly W.T., Zheng J.B., Guenette S.Y., Selkoe D.J. 2001. The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J. Biol. Chem. 276, 40, 288-40, 292.
  • 42
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of amyloid-β precursor protein-dependent transcriptional transactivation
    • Cao X., Sudhof T.C. 2004. Dissection of amyloid-β precursor protein-dependent transcriptional transactivation. J. Biol. Chem. 279, 24,601-24,611.
    • (2004) J. Biol. Chem , vol.279
    • Cao, X.1    Sudhof, T.C.2
  • 43
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo
    • Borchelt D.R., Thinakaran G., Eckman C.B., et al. 1996. Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron. 17, 1005-1013.
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3
  • 44
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper B., Saftig P., Craessaerts K., et al. 1998. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature. 391, 387-390.
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1    Saftig, P.2    Craessaerts, K.3
  • 45
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for y-secretase cleavage of β- APP and transmembrane cleavage of Notch-1
    • Zhang Z., Nadeau P., Song W., et al. 2000. Presenilins are required for y-secretase cleavage of β- APP and transmembrane cleavage of Notch-1. Nature Cell Biol. 2, 463-465.
    • (2000) Nature Cell Biol , vol.2 , pp. 463-465
    • Zhang, Z.1    Nadeau, P.2    Song, W.3
  • 46
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and y-secretase activity
    • Wolfe M.S., Xia W., Ostaszewski B.L., et al. 1999. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and y-secretase activity. Nature.398,513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3
  • 47
    • 0037173071 scopus 로고    scopus 로고
    • The aspartate-257 of presenilin 1 is indispensable for mouse development and production of β-amyloid peptides through β-catenin-independent mechanisms
    • Xia X., Wang P., Sun X., et al. 2002. The aspartate-257 of presenilin 1 is indispensable for mouse development and production of β-amyloid peptides through β-catenin-independent mechanisms. Proc. Natl. Acad. Sci. USA. 99, 8760-8765.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8760-8765
    • Xia, X.1    Wang, P.2    Sun, X.3
  • 48
    • 0033214070 scopus 로고    scopus 로고
    • A loss of function mutation of presenilin-2 interferes with amyloid β-peptide production and Notch signaling
    • Steiner H., Duff K., Capell A., et al. 1999. A loss of function mutation of presenilin-2 interferes with amyloid β-peptide production and Notch signaling. J. Biol. Chem. 274, 28,669-28,673.
    • (1999) J. Biol. Chem , vol.274
    • Steiner, H.1    Duff, K.2    Capell, A.3
  • 49
    • 0035980073 scopus 로고    scopus 로고
    • The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and γ-secretase activities of presenilins
    • Tomita T., Watabiki T., Takikawa R., et al. 2001. The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and γ-secretase activities of presenilins. J. Biol. Chem. 276, 33273-33281.
    • (2001) J. Biol. Chem , vol.276 , pp. 33273-33281
    • Tomita, T.1    Watabiki, T.2    Takikawa, R.3
  • 50
    • 1642555780 scopus 로고    scopus 로고
    • Mutant presenilins specifically elevate the levels of the 42-residue β-amyloid peptide in vivo: Evidence for augmentation of a 42-specific y-secretase
    • Jankowsky J.L., Fadale D.J., Anderson J., et al. 2004. Mutant presenilins specifically elevate the levels of the 42-residue β-amyloid peptide in vivo: Evidence for augmentation of a 42-specific y-secretase. Human Mol. Genet. 13, 159-170.
    • (2004) Human Mol. Genet , vol.13 , pp. 159-170
    • Jankowsky, J.L.1    Fadale, D.J.2    Anderson, J.3
  • 51
    • 0030671560 scopus 로고    scopus 로고
    • Li X., Greenwald 1.1997. HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling. Proc. Natl. Acad. Sci. USA. 94, 12204-12209.
    • Li X., Greenwald 1.1997. HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling. Proc. Natl. Acad. Sci. USA. 94, 12204-12209.
  • 52
    • 0031753831 scopus 로고    scopus 로고
    • Effects of SEL-12 presenilin on LIN-12 localization and function in Caenorhabditis elegans
    • Levitan D., Greenwald I. 1998. Effects of SEL-12 presenilin on LIN-12 localization and function in Caenorhabditis elegans. Development. 125, 3599-3606.
    • (1998) Development , vol.125 , pp. 3599-3606
    • Levitan, D.1    Greenwald, I.2
  • 53
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in Presenilin-1-deficient mice
    • Shen J., Bronson R.T., Chen D.F., et al. 1997. Skeletal and CNS defects in Presenilin-1-deficient mice. Cell. 89, 629-639.
    • (1997) Cell , vol.89 , pp. 629-639
    • Shen, J.1    Bronson, R.T.2    Chen, D.F.3
  • 54
    • 13044278313 scopus 로고    scopus 로고
    • Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency
    • Herreman A., Hartmann D., Annaert W., et al. 1999. Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency. Proc. Natl. Acad. Sci. USA. 96, 11,872-11,877.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96
    • Herreman, A.1    Hartmann, D.2    Annaert, W.3
  • 55
    • 0028216808 scopus 로고
    • Notch 1 is essential for postimplantation development in mice
    • Swiatek P.J., Lindsell C.E., del Amo F.F., et al. 1994. Notch 1 is essential for postimplantation development in mice. Genes Dev. 8, 707-719.
    • (1994) Genes Dev , vol.8 , pp. 707-719
    • Swiatek, P.J.1    Lindsell, C.E.2    del Amo, F.F.3
  • 56
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper B., Annaert W., Cupers P., et al. 1999. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature. 398, 518-522.
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1    Annaert, W.2    Cupers, P.3
  • 57
    • 0037468759 scopus 로고    scopus 로고
    • The role of presenilin cofactors in the γ-secretase complex
    • Takasugi N., Tomita T., Hayashi I., et al. 2003. The role of presenilin cofactors in the γ-secretase complex. Nature. 422, 438-441.
    • (2003) Nature , vol.422 , pp. 438-441
    • Takasugi, N.1    Tomita, T.2    Hayashi, I.3
  • 58
    • 0037363922 scopus 로고    scopus 로고
    • HES and HERP families: Multiple effectors of the Notch signaling pathway
    • Iso T., Kedes L., Hamamori Y. 2003. HES and HERP families: Multiple effectors of the Notch signaling pathway. J. Cell Physiol. 194, 237-255.
    • (2003) J. Cell Physiol , vol.194 , pp. 237-255
    • Iso, T.1    Kedes, L.2    Hamamori, Y.3
  • 60
    • 0032568821 scopus 로고    scopus 로고
    • The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains γ-catenin
    • Yu G., Chen F., Levesque G., et al. 1998. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains γ-catenin. J. Biol. Chem. 273, 16,470-16,475.
    • (1998) J. Biol. Chem , vol.273
    • Yu, G.1    Chen, F.2    Levesque, G.3
  • 61
    • 0030667426 scopus 로고    scopus 로고
    • Evidence that levels of presenilins (PS 1 and PS2) are coordinately regulated by competition for limiting cellular factors
    • Thinakaran G., Harris C.L., Ratovitski T., et al. 1997. Evidence that levels of presenilins (PS 1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272, 28,415-28,422.
    • (1997) J. Biol. Chem , vol.272
    • Thinakaran, G.1    Harris, C.L.2    Ratovitski, T.3
  • 62
    • 0343819757 scopus 로고    scopus 로고
    • Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state
    • Li Y.M., Lai M.T., Xu M., et al. 2000. Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state. Proc. Natl. Acad. Sci. USA. 97, 6138-6143.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6138-6143
    • Li, Y.M.1    Lai, M.T.2    Xu, M.3
  • 63
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated y-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li Y.M., Xu M., Lai M.T., et al. 2000. Photoactivated y-secretase inhibitors directed to the active site covalently label presenilin 1. Nature. 405, 689-694.
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1    Xu, M.2    Lai, M.T.3
  • 64
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • Yu G., Nishimura M., Arawaka S., et al. 2000. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature. 407, 48-54.
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1    Nishimura, M.2    Arawaka, S.3
  • 65
    • 0034080403 scopus 로고    scopus 로고
    • aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling
    • Goutte C., Hepler W., Mickey K.M., Priess J.R. 2000. aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling. Development. 127, 2481-2492.
    • (2000) Development , vol.127 , pp. 2481-2492
    • Goutte, C.1    Hepler, W.2    Mickey, K.M.3    Priess, J.R.4
  • 66
    • 23744491374 scopus 로고    scopus 로고
    • Nicastrin functions as a gamma-secretase-substrate receptor
    • Shah S., Lee S.F., Tabuchi K., et al. 2005. Nicastrin functions as a gamma-secretase-substrate receptor. Cell. 122, 435-447.
    • (2005) Cell , vol.122 , pp. 435-447
    • Shah, S.1    Lee, S.F.2    Tabuchi, K.3
  • 67
    • 0037173115 scopus 로고    scopus 로고
    • Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation
    • Edbauer D., Winkler E., Haass C., Steiner H. 2002. Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation. Proc. Natl. Acad. Sci. USA. 99, 8666-8671.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 68
    • 0037144422 scopus 로고    scopus 로고
    • Complex N-linked glycosylated nicastrin associates with active γ-secretase and undergoes tight cellular regulation
    • Kimberly W.T., laVoie M.J., Ostaszewski B.L., et al. 2002. Complex N-linked glycosylated nicastrin associates with active γ-secretase and undergoes tight cellular regulation. J. Biol. Chem. 277, 35,113-35,117.
    • (2002) J. Biol. Chem , vol.277
    • Kimberly, W.T.1    laVoie, M.J.2    Ostaszewski, B.L.3
  • 69
    • 0037154158 scopus 로고    scopus 로고
    • APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
    • Goutte C., Tsunozaki M., Hale V.A., Priess J.R. 2002. APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc. Natl. Acad. Sci. USA. 99, 775-779.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 70
    • 18444417998 scopus 로고    scopus 로고
    • aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation
    • Francis R., McGrath G., Zhang J., et al. 2002. aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev. Cell. 3, 85-97.
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1    McGrath, G.2    Zhang, J.3
  • 71
    • 0037160063 scopus 로고    scopus 로고
    • Lee S.F., Shah S., Li H., et al., et al. 2002. Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-β precursor protein and Notch. J. Biol. them. 277, 45013-45019.
    • Lee S.F., Shah S., Li H., et al., et al. 2002. Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-β precursor protein and Notch. J. Biol. them. 277, 45013-45019.
  • 72
    • 0037424275 scopus 로고    scopus 로고
    • PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1
    • Luo W.J., Wang H., Li H., et al. 2003. PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1. J. Biol. Chem. 278, 7850-7854.
    • (2003) J. Biol. Chem , vol.278 , pp. 7850-7854
    • Luo, W.J.1    Wang, H.2    Li, H.3
  • 73
    • 0037470037 scopus 로고    scopus 로고
    • APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin-nicastrin complexes
    • Gu Y., Chen F., Sanjo N., et al. 2003. APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin-nicastrin complexes. J. Biol. Chem. 278, 7374-7380.
    • (2003) J. Biol. Chem , vol.278 , pp. 7374-7380
    • Gu, Y.1    Chen, F.2    Sanjo, N.3
  • 74
    • 0038664363 scopus 로고    scopus 로고
    • Reconstitution of γ-secretase activity
    • Edbauer D., Winkler E., Regula J.T., et al. 2003. Reconstitution of γ-secretase activity. Nature Cell Biol. 5, 486-488.
    • (2003) Nature Cell Biol , vol.5 , pp. 486-488
    • Edbauer, D.1    Winkler, E.2    Regula, J.T.3
  • 75
    • 3342993335 scopus 로고    scopus 로고
    • Purification and characterization of the human γ-secretase complex
    • Fraering P.C., Ye W., Strub J.M., et al. 2004. Purification and characterization of the human γ-secretase complex. Biochemistry. 43, 9774-9789.
    • (2004) Biochemistry , vol.43 , pp. 9774-9789
    • Fraering, P.C.1    Ye, W.2    Strub, J.M.3
  • 77
    • 0036410505 scopus 로고    scopus 로고
    • Identification of a novel class of polytopic proteins with domains associated with probable proteinase activity
    • Grigorenko A.P., Molyaka Yu.K., Korovaitseva G.I., Rogaev E.I. 2002. Identification of a novel class of polytopic proteins with domains associated with probable proteinase activity. Biokhimiya. 67, 995-1005.
    • (2002) Biokhimiya , vol.67 , pp. 995-1005
    • Grigorenko, A.P.1    Molyaka, Y.K.2    Korovaitseva, G.I.3    Rogaev, E.I.4
  • 78
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen A., Binns K., Lemberg M.K., et al. 2002. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science. 296, 2215-2218.
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3
  • 79
    • 6944250394 scopus 로고    scopus 로고
    • The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins
    • Grigorenko A.P., Moliaka Y.K., Soto M.C., et al. 2004. The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins. Proc. Natl. Acad. Sci. USA. 101, 14955-14960.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14955-14960
    • Grigorenko, A.P.1    Moliaka, Y.K.2    Soto, M.C.3
  • 80
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: A case report
    • Nicoll J.A., Wilkinson D., Holmes C., et al. 2003. Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: A case report. Nature Med. 9, 448-452.
    • (2003) Nature Med , vol.9 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3
  • 81
    • 33645013015 scopus 로고    scopus 로고
    • Effects of a γ-secretase inhibitor in a randomized study of patients with Alzheimer disease
    • Siemers E.R., Quinn J.F., Kaye J., et al. 2006. Effects of a γ-secretase inhibitor in a randomized study of patients with Alzheimer disease. Neurology. 66, 602-604.
    • (2006) Neurology , vol.66 , pp. 602-604
    • Siemers, E.R.1    Quinn, J.F.2    Kaye, J.3


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