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Volumn 1, Issue 11, 2002, Pages 859-866

Therapeutic strategies for Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SECRETASE; AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; APOLIPOPROTEIN E2; APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; BENZODIAZEPINE DERIVATIVE; BETA SECRETASE; CHOLINESTERASE INHIBITOR; CLIOQUINOL; COPPER; ENZYME INHIBITOR; GAMMA SECRETASE; HYDROCORTISONE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; LACTAM DERIVATIVE; MUSCARINIC M1 RECEPTOR AGONIST; MUSCARINIC M3 RECEPTOR; NONSTEROID ANTIINFLAMMATORY AGENT; NOTCH RECEPTOR; PEPTIDE DERIVATIVE; PPI 1019; PPI 368; PRESENILIN 1; PRESENILIN 2; STEROID; SULFONAMIDE; TAU PROTEIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; ZINC;

EID: 0036833437     PISSN: 14741776     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrd938     Document Type: Review
Times cited : (181)

References (96)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. & Selkoe, D. J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356 (2002).
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases - New features and familiar faces
    • Esler, W. P. & Wolfe, M. S. A portrait of Alzheimer secretases - new features and familiar faces. Science 293, 1449-1454 (2001).
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 3
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate, A. et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 349, 704-706 (1991).
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1
  • 4
    • 0026075602 scopus 로고
    • Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene
    • Chartier-Harlin, M. C. et al. Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene. Nature 353, 844-846 (1991).
    • (1991) Nature , vol.353 , pp. 844-846
    • Chartier-Harlin, M.C.1
  • 5
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • Murrell, J., Farlow, M., Ghetti, B. & Benson, M. D. A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Science 254, 97-99 (1991).
    • (1991) Science , vol.254 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3    Benson, M.D.4
  • 6
    • 0028170818 scopus 로고
    • Cell biology of the amyloid-β protein precursor and the mechanism of Alzheimer's disease
    • Selkoe, D. J. Cell biology of the amyloid-β protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 10, 373-403 (1994).
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 7
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid-β protein secreted by familial amyloid-β protein precursor (β-APP717) mutants
    • Suzuki, N. et al. An increased percentage of long amyloid-β protein secreted by familial amyloid-β protein precursor (β-APP717) mutants. Science 264, 1336-1340 (1994).
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1
  • 8
    • 9844261165 scopus 로고    scopus 로고
    • A new pathogenic mutation in the APP gene (I716V) increases the relative proportion of Aβ42(43)
    • Eckman, C. B. et al. A new pathogenic mutation in the APP gene (I716V) increases the relative proportion of Aβ42(43). Hum. Mol. Genet. 6, 2087-2089 (1997).
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 2087-2089
    • Eckman, C.B.1
  • 9
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington, R. et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375, 754-760 (1995).
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1
  • 10
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • Levy-Lahad, E. et al. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 269, 973-977 (1995).
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1
  • 11
    • 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. 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 376, 775-778 (1995).
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1
  • 12
    • 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. et al. 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).
    • (1996) Nature Med. , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 13
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1
    • Duff, K. et al. Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1. Nature 383, 710-713 (1996).
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1
  • 14
    • 16044365171 scopus 로고    scopus 로고
    • 42 deposition and severe cerebellar pathology
    • 42 deposition and severe cerebellar pathology. Nature Med. 2, 1146-1150 (1996).
    • (1996) Nature Med. , vol.2 , pp. 1146-1150
    • Lemere, C.A.1
  • 15
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid-β protein in both transfected cells and transgenic mice
    • Citron, M. et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid-β protein in both transfected cells and transgenic mice. Nature Med. 3, 67-72 (1997).
    • (1997) Nature Med. , vol.3 , pp. 67-72
    • Citron, M.1
  • 16
    • 12644258498 scopus 로고    scopus 로고
    • The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid-β protein ending at the 42nd (or 43rd) residue
    • Tomita, T. et al. The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid-β protein ending at the 42nd (or 43rd) residue. Proc. Natl Acad. Sci. USA 94, 2025-2030 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2025-2030
    • Tomita, T.1
  • 17
    • 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. et al. Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 17, 1005-1013 (1996).
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1
  • 18
    • 0035927426 scopus 로고    scopus 로고
    • Secretase targets for Alzheimer's disease: Identification and therapeutic potential
    • Wolfe, M. S. Secretase targets for Alzheimer's disease: identification and therapeutic potential. J. Med. Chem. 44, 2039-2060 (2001).
    • (2001) J. Med. Chem. , vol.44 , pp. 2039-2060
    • Wolfe, M.S.1
  • 19
    • 0033595706 scopus 로고    scopus 로고
    • β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar, R. et al. β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999).
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1
  • 20
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein β-secretase from human brain
    • Sinha, S. et al. Purification and cloning of amyloid precursor protein β-secretase from human brain. Nature 402, 537-540 (1999).
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1
  • 21
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
    • Yan, R. et al. Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity. Nature 402, 533-537 (1999 ).
    • (1999) Nature , vol.402 , pp. 533-537
    • Yan, R.1
  • 22
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (ASP2) as β-secretase
    • Hussain, I. et al. Identification of a novel aspartic protease (ASP2) as β-secretase. Mol. Cell. Neurosci. 14, 419-427 (1999).
    • (1999) Mol. Cell. Neurosci. , vol.14 , pp. 419-427
    • Hussain, I.1
  • 23
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (β-secretase) complexed with inhibitor
    • Hong, L. et al. Structure of the protease domain of memapsin 2 (β-secretase) complexed with inhibitor. Science 290, 150-153 (2000).
    • (2000) Science , vol.290 , pp. 150-153
    • Hong, L.1
  • 24
    • 0035974650 scopus 로고    scopus 로고
    • Structure-based design: Potent inhibitors of human brain memapsin 2 (β-secretase)
    • Ghosh, A. K. et al. Structure-based design: potent inhibitors of human brain memapsin 2 (β-secretase). J. Med. Chem. 44, 2865-2868 (2001).
    • (2001) J. Med. Chem. , vol.44 , pp. 2865-2868
    • Ghosh, A.K.1
  • 25
    • 0035923502 scopus 로고    scopus 로고
    • Alzheimer's β-secretase, β-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase
    • Kitazume, S. et al. Alzheimer's β-secretase, β-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase. Proc. Natl Acad. Sci. USA 98, 13554-13559 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13554-13559
    • Kitazume, S.1
  • 26
    • 0035116273 scopus 로고    scopus 로고
    • Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation
    • Luo, Y. et al. Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation. Nature Neurosci. 4, 231-232 (2001).
    • (2001) Nature Neurosci. , vol.4 , pp. 231-232
    • Luo, Y.1
  • 27
    • 0035112647 scopus 로고    scopus 로고
    • BACE1 is the major β-secretase for generation of Aβ peptides by neurons
    • Cai, H. et al. BACE1 is the major β-secretase for generation of Aβ peptides by neurons. Nature Neurosci. 4, 233-234 (2001).
    • (2001) Nature Neurosci. , vol.4 , pp. 233-234
    • Cai, H.1
  • 28
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest Alzheimer's γ-secretases are intramembrane-cleaving aspartyl proteases
    • Wolfe, M. S. et al. Peptidomimetic probes and molecular modeling suggest Alzheimer's γ-secretases are intramembrane-cleaving aspartyl proteases. Biochemistry 38, 4720-4727 (1999).
    • (1999) Biochemistry , vol.38 , pp. 4720-4727
    • Wolfe, M.S.1
  • 29
    • 0034254585 scopus 로고    scopus 로고
    • L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid-β protein precursor γ-secretase activity
    • Shearman, M. S. et al. L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid-β protein precursor γ-secretase activity. Biochemistry 39, 8698-8704 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8698-8704
    • Shearman, M.S.1
  • 30
    • 0033775709 scopus 로고    scopus 로고
    • Total inactivation of γ-secretase activity in presenilin-deficient embryonic stem cells
    • Herreman, A. et al. Total inactivation of γ-secretase activity in presenilin-deficient embryonic stem cells. Nature Cell Biol. 2, 461-462 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 461-462
    • Herreman, A.1
  • 31
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1
    • Zhang, Z. et al. Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1. Nature Cell Biol. 2, 463-465 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 463-465
    • Zhang, Z.1
  • 32
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517 (1999).
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 33
    • 0032568821 scopus 로고    scopus 로고
    • The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin
    • Yu, G. et al. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin. J. Biol. Chem. 273, 16470-16475 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 16470-16475
    • Yu, G.1
  • 34
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran, G. et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17, 181-190 (1996).
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1
  • 35
    • 0032488995 scopus 로고    scopus 로고
    • The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex
    • Capell, A. et al. The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex. J. Biol. Chem. 273, 3205-3211 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3205-3211
    • Capell, A.1
  • 36
    • 0030854388 scopus 로고    scopus 로고
    • Endoproteolytic processing and stabilization of wild-type and mutant presenilin
    • Ratovitski, T. et al. Endoproteolytic processing and stabilization of wild-type and mutant presenilin. J. Biol. Chem. 272, 24536-24541 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 24536-24541
    • Ratovitski, T.1
  • 37
    • 0033610863 scopus 로고    scopus 로고
    • Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
    • Steiner, H. et al. Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J. Biol. Chem. 273, 32322-32331 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 32322-32331
    • Steiner, H.1
  • 38
    • 0030667426 scopus 로고    scopus 로고
    • Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors
    • Thinakaran, G. et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272, 28415-28422 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28415-28422
    • Thinakaran, G.1
  • 39
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li, Y. M. et al. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405, 689-694 (2000).
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1
  • 40
    • 0033780472 scopus 로고    scopus 로고
    • Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
    • Esler, W. P. et al. Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1. Nature Cell Biol. 2, 428-434 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 428-434
    • Esler, W.P.1
  • 41
    • 0343819757 scopus 로고    scopus 로고
    • Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state
    • Li, Y. M. et al. Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state. Proc. Natl Acad. Sci. USA 97, 6138-6143 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6138-6143
    • Li, Y.M.1
  • 42
    • 0037022644 scopus 로고    scopus 로고
    • Activity-dependent isolation of the presenilin/γ-secretase complex reveals nicastrin and a γ substrate
    • Esler, W. P. et al. Activity-dependent isolation of the presenilin/γ-secretase complex reveals nicastrin and a γ substrate. Proc. Natl Acad. Sci. USA 99, 2720-2725 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2720-2725
    • Esler, W.P.1
  • 43
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated Notch/Glp-1 signal transduction and β-APP processing
    • Yu, G. et al. Nicastrin modulates presenilin-mediated Notch/Glp-1 signal transduction and β-APP processing. Nature 407, 48-54 (2000).
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 44
    • 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. 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).
    • (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
  • 45
    • 18444417998 scopus 로고    scopus 로고
    • APH-1 and PEN-2 are required for Notch pathway signaling, γ-secretase cleavage of β-APP, and presenilin protein accumulation
    • Francis, R. et al. APH-1 and PEN-2 are required for Notch pathway signaling, γ-secretase cleavage of β-APP, and presenilin protein accumulation. Dev. Cell 3, 85-97 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1
  • 46
    • 0034602419 scopus 로고    scopus 로고
    • Presenilin-1 and -2 are molecular targets for γ-secretase inhibitors
    • Seiffert D. et al. Presenilin-1 and -2 are molecular targets for γ-secretase inhibitors. J. Biol. Chem. 275, 34086-34091 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 34086-34091
    • Seiffert, D.1
  • 47
    • 0035163347 scopus 로고    scopus 로고
    • Functional γ-secretase inhibitors reduce β-amyloid peptide levels in brain
    • Dovey, H. F. et al. Functional γ-secretase inhibitors reduce β-amyloid peptide levels in brain. J. Neurochem. 76, 173-181 (2001).
    • (2001) J. Neurochem. , vol.76 , pp. 173-181
    • Dovey, H.F.1
  • 48
    • 0035912829 scopus 로고    scopus 로고
    • γ-Secretase inhibitors repress thymocyte development
    • Hadland, B. K. et al. γ-Secretase inhibitors repress thymocyte development. Proc. Natl Acad. Sci. USA 98, 7487-7491 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7487-7491
    • Hadland, B.K.1
  • 49
    • 0035979234 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase activity modulates thymocyte development
    • Doerfler, P., Shearman, M. S. & Perlmutter, R. M. Presenilin-dependent γ-secretase activity modulates thymocyte development. Proc. Natl Acad. Sci. USA 98, 9312-9317 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9312-9317
    • Doerfler, P.1    Shearman, M.S.2    Perlmutter, R.M.3
  • 50
    • 0035829592 scopus 로고    scopus 로고
    • 42 independently of cyclooxygenase activity
    • 42 independently of cyclooxygenase activity. Nature 414, 212-216 (2001).
    • (2001) Nature , vol.414 , pp. 212-216
    • Weggen, S.1
  • 51
    • 0027453490 scopus 로고
    • Activation of protein kinase C inhibits cellular production of the amyloid β-protein
    • Hung, A. Y. et al. Activation of protein kinase C inhibits cellular production of the amyloid β-protein. J. Biol. Chem. 268, 22959-22962 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 22959-22962
    • Hung, A.Y.1
  • 52
    • 0027435535 scopus 로고
    • Protein phosphorylation inhibits production of Alzheimer amyloid β/A4 peptide
    • Buxbaum, J. D., Koo, E. H. & Greengard, P. Protein phosphorylation inhibits production of Alzheimer amyloid β/A4 peptide. Proc. Natl Acad. Sci. USA 90, 9195-9198 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9195-9198
    • Buxbaum, J.D.1    Koo, E.H.2    Greengard, P.3
  • 53
    • 0028264451 scopus 로고
    • Reversal of the Swedish familial Alzheimer's disease mutant phenotype in cultured cells treated with phorbol 12,13-dibutyrate
    • Felsenstein, K. M., Ingalls, K. M., Hunihan, L. W. & Roberts, S. B. Reversal of the Swedish familial Alzheimer's disease mutant phenotype in cultured cells treated with phorbol 12,13-dibutyrate. Neurosci. Lett. 174, 173-176 (1994).
    • (1994) Neurosci. Lett. , vol.174 , pp. 173-176
    • Felsenstein, K.M.1    Ingalls, K.M.2    Hunihan, L.W.3    Roberts, S.B.4
  • 54
    • 0028246846 scopus 로고
    • The release of Alzheimer's disease β-amyloid peptide is reduced by phorbol treatment
    • Jacobsen, J. S. et al. The release of Alzheimer's disease β-amyloid peptide is reduced by phorbol treatment. J. Biol. Chem. 269, 8376-8382 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 8376-8382
    • Jacobsen, J.S.1
  • 55
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch, R. M., Slack, B. E., Wurtman, R. J. & Growdon, J. H. Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 258, 304-307 (1992).
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3    Growdon, J.H.4
  • 57
    • 0028926941 scopus 로고
    • Muscarinic regulation of Alzheimer's disease amyloid precursor protein secretion and amyloid β-protein production in human neuronal NT2N cells
    • Wolf, B. A. et al. Muscarinic regulation of Alzheimer's disease amyloid precursor protein secretion and amyloid β-protein production in human neuronal NT2N cells. J. Biol. Chem. 270, 4916-4922 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 4916-4922
    • Wolf, B.A.1
  • 58
    • 0032693398 scopus 로고    scopus 로고
    • Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation
    • Lin, L., Georgievska, B., Mattsson, A. & Isacson, O. Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation. Proc. Natl Acad. Sci. USA 96, 12108-12113 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12108-12113
    • Lin, L.1    Georgievska, B.2    Mattsson, A.3    Isacson, O.4
  • 59
    • 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. et al. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 261, 921-923 (1993).
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1
  • 60
    • 0028305380 scopus 로고
    • Protective effect of apolipoprotein E type 2 allele for late onset Alzheimer disease
    • Corder, E. H. et al. Protective effect of apolipoprotein E type 2 allele for late onset Alzheimer disease. Nature Genet. 7, 180-184 (1994).
    • (1994) Nature Genet. , vol.7 , pp. 180-184
    • Corder, E.H.1
  • 61
    • 0035897938 scopus 로고    scopus 로고
    • Midlife vascular risk factors and Alzheimer's disease in later life: Longitudinal, population based study
    • Kivipelto M. et al. Midlife vascular risk factors and Alzheimer's disease in later life: longitudinal, population based study. Br. Med. J. 322, 1447-1451 (2001).
    • (2001) Br. Med. J. , vol.322 , pp. 1447-1451
    • Kivipelto, M.1
  • 62
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors
    • Wolozin, B., Kellman, W., Ruosseau, P., Celesia, G. G. & Siegel, G. Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors. Arch. Neurol. 57, 1439-1443 (2000).
    • (2000) Arch. Neurol. , vol.57 , pp. 1439-1443
    • Wolozin, B.1    Kellman, W.2    Ruosseau, P.3    Celesia, G.G.4    Siegel, G.5
  • 64
    • 0028177562 scopus 로고
    • Induction of Alzheimer-like β-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol
    • Sparks, D. L. et al. Induction of Alzheimer-like β-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol. Exp. Neurol. 126, 88-94 (1994).
    • (1994) Exp. Neurol. , vol.126 , pp. 88-94
    • Sparks, D.L.1
  • 65
    • 0032568552 scopus 로고    scopus 로고
    • Cholesterol depletion inhibits the generation of β-amyloid in hippocampal neurons
    • Simons, M. et al. Cholesterol depletion inhibits the generation of β-amyloid in hippocampal neurons. Proc. Natl Acad. Sci. USA 95, 6460-6464 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6460-6464
    • Simons, M.1
  • 67
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM10
    • Kojro E., Gimpl, G., Lammich, S., Marz, W. & Fahrenholz, F. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM10. Proc. Natl Acad. Sci. USA 98, 5815-5820 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 68
    • 0034795651 scopus 로고    scopus 로고
    • Acyl-coenzyme A:cholesterol acyltransferase modulates the generation of the amyloid β-peptide
    • Puglielli, L. et al. Acyl-coenzyme A:cholesterol acyltransferase modulates the generation of the amyloid β-peptide. Nature Cell Biol. 3, 905-912 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 905-912
    • Puglielli, L.1
  • 69
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C. J., Burdick, D., Walencewicz, A. J., Glabe, C. G. & Cotman, C. W. Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13, 1676-1687 (1993).
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 70
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo, A. & Yankner, B. A. β-Amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl Acad. Sci. USA 91, 12243-12247 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 71
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley, D. M. et al. Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19, 8876-8884 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1
  • 72
    • 0027258525 scopus 로고
    • The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J. T., Berger, E. P. & Lansbury, P. T. Jr. The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697 (1993).
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 73
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper, J. D., Wong, S. S., Lieber, C. M. & Lansbury, P. T. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125 (1997).
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 74
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid-β protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M. & Teplow, D. B. Amyloid-β protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272, 22364-22372 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 75
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D. M. et al. Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539 (2002).
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 76
    • 0036547110 scopus 로고    scopus 로고
    • Peptide inhibitors of β-amyloid aggregation
    • Findeis, M. A. Peptide inhibitors of β-amyloid aggregation. Curr. Top. Med. Chem. 2, 417-423 (2002).
    • (2002) Curr. Top. Med. Chem. , vol.2 , pp. 417-423
    • Findeis, M.A.1
  • 77
    • 0036615884 scopus 로고    scopus 로고
    • Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a β-sheet breaker peptide
    • Permanne, B. et al. Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a β-sheet breaker peptide. FASEB J. 16, 860-862 (2002).
    • (2002) FASEB J. , vol.16 , pp. 860-862
    • Permanne, B.1
  • 78
    • 0037188472 scopus 로고    scopus 로고
    • The galvanization of β-amyloid in Alzheimer's disease
    • Bush, A. I. & Tanzi, R. E. The galvanization of β-amyloid in Alzheimer's disease. Proc. Natl Acad. Sci. USA 99, 7317-7319 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7317-7319
    • Bush, A.I.1    Tanzi, R.E.2
  • 79
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny, R. A. et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30, 665-676 (2001).
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1
  • 80
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee, J. Y., Cole, T. B., Palmiter, R. D., Suh, S. W. & Koh, J. Y. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl Acad. Sci. USA 99, 7705-7710 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7705-7710
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Suh, S.W.4    Koh, J.Y.5
  • 81
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk, D. et al. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400, 173-177 (1999).
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1
  • 82
    • 0033801852 scopus 로고    scopus 로고
    • Nasal administration of amyloid-β peptide decreases cerebral amyloid burden in a mouse model of Alzheimer's disease
    • Weiner, H. L. et al. Nasal administration of amyloid-β peptide decreases cerebral amyloid burden in a mouse model of Alzheimer's disease. Ann. Neurol. 48, 567-579 (2000).
    • (2000) Ann. Neurol. , vol.48 , pp. 567-579
    • Weiner, H.L.1
  • 83
    • 84984755327 scopus 로고    scopus 로고
    • Aβ-peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan, D. et al. Aβ-peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 408, 982-985 (2000).
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1
  • 84
    • 0034700471 scopus 로고    scopus 로고
    • Aβ-peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus, C. et al. Aβ-peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 408, 979-982 (2000).
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1
  • 85
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid-β peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard, F. et al. Peripherally administered antibodies against amyloid-β peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nature Med. 6, 916-919 (2000).
    • (2000) Nature Med. , vol.6 , pp. 916-919
    • Bard, F.1
  • 86
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease
    • DeMattos, R. B. et al. Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease. Proc. Natl Acad. Sci. USA 98, 8850-8855 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8850-8855
    • DeMattos, R.B.1
  • 87
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model
    • Dodart, J. C. et al. Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model. Nature Neurosci. 5, 452-457 (2002).
    • (2002) Nature Neurosci. , vol.5 , pp. 452-457
    • Dodart, J.C.1
  • 88
    • 0036672706 scopus 로고    scopus 로고
    • Alzheimer's disease drug discovery targeted to the APP mRNA 5′ untranslated region
    • Rogers, J. T. et al. Alzheimer's disease drug discovery targeted to the APP mRNA 5′ untranslated region. J. Mol. Neurosci. 19, 77-82 (2002).
    • (2002) J. Mol. Neurosci. , vol.19 , pp. 77-82
    • Rogers, J.T.1
  • 89
    • 0347928847 scopus 로고    scopus 로고
    • An iron-responsive element type II in the 5′ untranslated region of the Alzheimer's amyloid precursor protein transcript
    • Aug 26 (doi: 10.1074/jbc.M207435200)
    • Rogers, J. T. et al. An iron-responsive element type II in the 5′ untranslated region of the Alzheimer's amyloid precursor protein transcript. J. Biol. Chem. 2002 Aug 26 (doi: 10.1074/jbc.M207435200).
    • (2002) J. Biol. Chem.
    • Rogers, J.T.1
  • 90
    • 0035950225 scopus 로고    scopus 로고
    • Clearing the brain's amyloid cobwebs
    • Selkoe, D. J. Clearing the brain's amyloid cobwebs. Neuron 32, 177-180 (2001).
    • (2001) Neuron , vol.32 , pp. 177-180
    • Selkoe, D.J.1
  • 91
    • 0037118028 scopus 로고    scopus 로고
    • Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
    • Pepys, M. B. et al. Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature 417, 254-259 (2002).
    • (2002) Nature , vol.417 , pp. 254-259
    • Pepys, M.B.1
  • 92
    • 0037173115 scopus 로고    scopus 로고
    • Presenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formation
    • Edbauer, D., Winkler, E., Haass, C. & Steiner, H. Presenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formation. Proc. Natl Acad Sci USA 99, 8666-8671 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 93
    • 0037008723 scopus 로고    scopus 로고
    • Mature glycosylation and trafficking of nicastrin modulate its binding to presinilins
    • Yang, D. S. et al. Mature glycosylation and trafficking of nicastrin modulate its binding to presinilins. J. Biol. Chem. 277, 28135-28142 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 28135-28142
    • Yang, D.S.1
  • 94
    • 0037166349 scopus 로고    scopus 로고
    • Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
    • Leem, J. Y. et al. Presenilin 1 is required for maturation and cell surface accumulation of nicastrin. J. Biol. Chem. 277, 19236-19240 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 19236-19240
    • Leem, J.Y.1
  • 95
    • 0037144422 scopus 로고    scopus 로고
    • Complex N-linked glycosylated nicastrin associates with active g-secretase and undergoes tight cellular regulation
    • Kimberly, W. T. et al. Complex N-linked glycosylated nicastrin associates with active g-secretase and undergoes tight cellular regulation. J. Biol. Chem. 277, 35113-35117 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 35113-35117
    • Kimberly, W.T.1
  • 96
    • 0036180950 scopus 로고    scopus 로고
    • Cholesterol-dependent γ-secretase activity in buoyant cholesterol-rich membrane microdomains
    • Wahrle, S. et al. Cholesterol-dependent γ-secretase activity in buoyant cholesterol-rich membrane microdomains. Neurobiol. Dis. 9, 11-23 (2002).
    • (2002) Neurobiol. Dis. , vol.9 , pp. 11-23
    • Wahrle, S.1


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