메뉴 건너뛰기




Volumn 57, Issue 5, 2000, Pages 705-715

Molecular basis of Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid peptide; Apolipoprotein E; Cholesterol homeostasis; Presenilin

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E; MEMBRANE PHOSPHOLIPID; PRESENILIN 1; PRESENILIN 2;

EID: 0034042881     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050035     Document Type: Review
Times cited : (84)

References (91)
  • 2
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome I related to the Alzheimer's disease type 3 gene
    • 2 Rogaev E. I., Sherrington R., Rogaeva E. A., Levesque G., Ikeda M., Liang Y. et al. (1995) Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome I 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    Levesque, G.4    Ikeda, M.5    Liang, Y.6
  • 3
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familiar Alzheimer's disease
    • 3 Sherrington R., Rogaev E. I., Liang Y., Rogaeva E. A., Levesque G., Ikeda M. et al. (1995) Cloning of a gene bearing missense mutations in early-onset familiar Alzheimer's disease. Nature 375: 754-759
    • (1995) Nature , vol.375 , pp. 754-759
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3    Rogaeva, E.A.4    Levesque, G.5    Ikeda, M.6
  • 4
    • 0032563226 scopus 로고    scopus 로고
    • New gene tied to common form of Alzheimer's
    • 4 Marx J. (1998) New gene tied to common form of Alzheimer's. Science 281: 508-509
    • (1998) Science , vol.281 , pp. 508-509
    • Marx, J.1
  • 5
    • 17344362232 scopus 로고    scopus 로고
    • Alpha-2 macroglobulin is genetically associated with Alzheimer disease
    • 5 Blacker D., Wilcox M., Laird N. M., Rodes L., Horvath S. M., Go R. C. P. et al. (1998) Alpha-2 macroglobulin is genetically associated with Alzheimer disease. Nat. Genet. 19: 357-360
    • (1998) Nat. Genet. , vol.19 , pp. 357-360
    • Blacker, D.1    Wilcox, M.2    Laird, N.M.3    Rodes, L.4    Horvath, S.M.5    Go, R.C.P.6
  • 6
    • 0027372206 scopus 로고
    • The immunopathology of Alzheimer's disease and some related disorders
    • 6 Kalaria R. J. (1993) The immunopathology of Alzheimer's disease and some related disorders. Brain Pathol. 3: 333-347
    • (1993) Brain Pathol. , vol.3 , pp. 333-347
    • Kalaria, R.J.1
  • 7
    • 0031007546 scopus 로고    scopus 로고
    • Regulated phosphorylation and dephosphorylation of tau protein: Effects on microtubule interaction, intracellular trafficking and neurodegeneration
    • 7 Billlingsley M. L. and Kincaid R. (1997) Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem. J. 323: 577-591
    • (1997) Biochem. J. , vol.323 , pp. 577-591
    • Billlingsley, M.L.1    Kincaid, R.2
  • 9
    • 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
    • 9 Scheuner D., Eckman C., Jensen M., Song X., Citron M., Suzuki N. 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. Nat. Med. 2: 864-868
    • (1996) Nat. Med. , vol.2 , pp. 864-868
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5    Suzuki, N.6
  • 11
    • 0030725311 scopus 로고    scopus 로고
    • Perlecan binds to the β-amyloid proteins (Aβ) of Alzheimer's disease, accelerates Aβ fibril formation, and maintains Aβ fibril stability
    • 11 Castillo G. M., Ngo C., Cummings J., Wight T. N. and Snow A. D. (1997) Perlecan binds to the β-amyloid proteins (Aβ) of Alzheimer's disease, accelerates Aβ fibril formation, and maintains Aβ fibril stability. J. Neurochem. 69: 2452-2465
    • (1997) J. Neurochem. , vol.69 , pp. 2452-2465
    • Castillo, G.M.1    Ngo, C.2    Cummings, J.3    Wight, T.N.4    Snow, A.D.5
  • 12
    • 0032080309 scopus 로고    scopus 로고
    • Stable complexes involving acetyl-cholineterase and amyloid-β peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils
    • 12 Alvarez A., Alarcon R., Opazo C., Campos E., Munoz F. J., Calderon F. et al. (1998) Stable complexes involving acetyl-cholineterase and amyloid-β peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J. Neurosci. 18: 3213-3223
    • (1998) J. Neurosci. , vol.18 , pp. 3213-3223
    • Alvarez, A.1    Alarcon, R.2    Opazo, C.3    Campos, E.4    Munoz, F.J.5    Calderon, F.6
  • 13
    • 0031594756 scopus 로고    scopus 로고
    • α2-macroglobulin attenuates β-amyloid peptide 1 - 40 fibril formation and associated neurotoxicity of cultured fetal rat cortical neurons
    • 13 Du Y., Bales K. R., Dodel R., Liu X., Glinn M. A., Horn J. et al. (1998) α2-Macroglobulin attenuates β-amyloid peptide 1 - 40 fibril formation and associated neurotoxicity of cultured fetal rat cortical neurons. J. Neurochem. 70: 1182-1188
    • (1998) J. Neurochem. , vol.70 , pp. 1182-1188
    • Du, Y.1    Bales, K.R.2    Dodel, R.3    Liu, X.4    Glinn, M.A.5    Horn, J.6
  • 14
    • 0030775361 scopus 로고    scopus 로고
    • Amyloid β-protein (Aβ) 1 - 40 but not AβI 42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain
    • 14 Shin R.-W., Ogino K., Kondo A., Saido T. C., Trojanowski J. W., Kitamoto T. et al. (1997) Amyloid β-protein (Aβ) 1 - 40 but not AβI 42 contributes to the experimental formation of Alzheimer disease amyloid fibrils in rat brain. J. Neurosci. 17: 8187-8193
    • (1997) J. Neurosci. , vol.17 , pp. 8187-8193
    • Shin, R.-W.1    Ogino, K.2    Kondo, A.3    Saido, T.C.4    Trojanowski, J.W.5    Kitamoto, T.6
  • 15
    • 0030723983 scopus 로고    scopus 로고
    • Binding of β-amyloid to the p75 neurotrophin receptor induces apoptosis
    • 15 Yaar M., Zhai S., Pilch P. F., Doyle S. M., Eisenhauer P. B., Fine R. E. et al. (1997) Binding of β-amyloid to the p75 neurotrophin receptor induces apoptosis. Neurobiol. Dis. 100: 2333-2340
    • (1997) Neurobiol. Dis. , vol.100 , pp. 2333-2340
    • Yaar, M.1    Zhai, S.2    Pilch, P.F.3    Doyle, S.M.4    Eisenhauer, P.B.5    Fine, R.E.6
  • 16
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
    • 16 Van S., Chen X., Zhu H., Roher A., Slattery T., Zhao L. et al. (1996) RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease. Nature 382: 685-691
    • (1996) Nature , vol.382 , pp. 685-691
    • Van, S.1    Chen, X.2    Zhu, H.3    Roher, A.4    Slattery, T.5    Zhao, L.6
  • 17
    • 0029787599 scopus 로고    scopus 로고
    • Scavenger receptor-mediated adhesion of microglia to beta-amyloid fibrils
    • 17 El Khoury J., Hickman S., Thomas C., Cao L., Silverstein S. and Loike J. (1996) Scavenger receptor-mediated adhesion of microglia to beta-amyloid fibrils. Nature 382: 716-719
    • (1996) Nature , vol.382 , pp. 716-719
    • El Khoury, J.1    Hickman, S.2    Thomas, C.3    Cao, L.4    Silverstein, S.5    Loike, J.6
  • 19
    • 0032534629 scopus 로고    scopus 로고
    • Beta-amyloid binds to p75NTR and activates NfkappaB in human neuroblastoma cells
    • 19 Kuner P., Schubenel R. and Hertel C. (1998) Beta-amyloid binds to p75NTR and activates NfkappaB in human neuroblastoma cells. J. Neurosci. Res. 54: 789-804
    • (1998) J. Neurosci. Res. , vol.54 , pp. 789-804
    • Kuner, P.1    Schubenel, R.2    Hertel, C.3
  • 20
    • 0029802659 scopus 로고    scopus 로고
    • Fusogenic properties of the C-terminal domain of the Alzheimer β-amyloid peptide
    • 20 Pillot T., Goethals M., Vanloo B., Talussot C., Brasseur R., Rosseneu M. et al. (1996) Fusogenic properties of the C-terminal domain of the Alzheimer β-amyloid peptide. J. Biol. Chem. 271: 13379-13382
    • (1996) J. Biol. Chem. , vol.271 , pp. 13379-13382
    • Pillot, T.1    Goethals, M.2    Vanloo, B.3    Talussot, C.4    Brasseur, R.5    Rosseneu, M.6
  • 21
    • 0029861772 scopus 로고    scopus 로고
    • Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides
    • 21 McLaurin J. and Chakrabartty A. (1996) Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides. J. Biol. Chem. 271: 26482-26489
    • (1996) J. Biol. Chem. , vol.271 , pp. 26482-26489
    • McLaurin, J.1    Chakrabartty, A.2
  • 22
    • 0032014429 scopus 로고    scopus 로고
    • Effects of beta-amyloid peptides on the fluidity of membranes from frontal and parietal lobes of human brain: High potencies of A-beta 1 43
    • 22 Muller W. E., Eckert G. P., Scheuer K., Cairns N. J., Maras A. and Gattaz W. F. (1998) Effects of beta-amyloid peptides on the fluidity of membranes from frontal and parietal lobes of human brain: high potencies of A-beta 1 43. J. Exp. Clin. Invest. 5: 10-15
    • (1998) J. Exp. Clin. Invest. , vol.5 , pp. 10-15
    • Muller, W.E.1    Eckert, G.P.2    Scheuer, K.3    Cairns, N.J.4    Maras, A.5    Gattaz, W.F.6
  • 23
    • 17344371804 scopus 로고    scopus 로고
    • Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: Suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction
    • 23 Keller J. N., Kindy M. S., Holtsberg F. W., St. Clair D. K., yen H.-C., Germeyer A. et al. (1998) Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction. J. Neurosci 18: 687-697
    • (1998) J. Neurosci , vol.18 , pp. 687-697
    • Keller, J.N.1    Kindy, M.S.2    Holtsberg, F.W.3    St. Clair, D.K.4    Yen, H.-C.5    Germeyer, A.6
  • 24
    • 0031962324 scopus 로고    scopus 로고
    • Bcl-2 protects isolated plasma and mitochondrial membranes against lipid peroxidation induced by hydrogen peroxide and amyloid β-peptide
    • 24 Bruce-Keller A., Begley J. G., Fu W., Butterfield A. D., Bredesen D. E., Hutchins J. B. et al. (1998) Bcl-2 protects isolated plasma and mitochondrial membranes against lipid peroxidation induced by hydrogen peroxide and amyloid β-peptide. J. Neurochem. 70: 31-39
    • (1998) J. Neurochem. , vol.70 , pp. 31-39
    • Bruce-Keller, A.1    Begley, J.G.2    Fu, W.3    Butterfield, A.D.4    Bredesen, D.E.5    Hutchins, J.B.6
  • 25
    • 0032524319 scopus 로고    scopus 로고
    • Secreted β-amyloid precursor protein counteracts the proapoptotic action of mutant presenilin-1 by activation of NF-κB and stabilization of calcium homeostasis
    • 25 Guo Q., Robinson N. and Mattson M. (1998) Secreted β-amyloid precursor protein counteracts the proapoptotic action of mutant presenilin-1 by activation of NF-κB and stabilization of calcium homeostasis. J. Biol. Chem. 273: 12341-12351
    • (1998) J. Biol. Chem. , vol.273 , pp. 12341-12351
    • Guo, Q.1    Robinson, N.2    Mattson, M.3
  • 26
    • 0030611750 scopus 로고    scopus 로고
    • Activation of NF-κB protects hippocampal neurons against oxidative stress-induced apoptosis: Evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration
    • 26 Mattson M. P., Goodman Y., Luo H., Fu W. and Furukawa K. (1997) Activation of NF-κB protects hippocampal neurons against oxidative stress-induced apoptosis: evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration. J. Neurosci. Res. 49: 681-697
    • (1997) J. Neurosci. Res. , vol.49 , pp. 681-697
    • Mattson, M.P.1    Goodman, Y.2    Luo, H.3    Fu, W.4    Furukawa, K.5
  • 27
    • 0032510692 scopus 로고    scopus 로고
    • Amyloid β-peptide stimulates nitric oxide production in astrocytes through an NFκB-dependent mechanism
    • 27 Akama K., Albanese C., Pestall R. G. and Van Eldik L. J. (1998) Amyloid β-peptide stimulates nitric oxide production in astrocytes through an NFκB-dependent mechanism. Proc. Natl. Acad. Sci. USA 95: 5795-5800
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5795-5800
    • Akama, K.1    Albanese, C.2    Pestall, R.G.3    Van Eldik, L.J.4
  • 28
    • 0030924506 scopus 로고    scopus 로고
    • β-amyloid neurotoxicity in vitro: Evidence of oxidative stress but not protection by antioxidants
    • 28 Pike C.J., Ramezan-Arab N. and Cotman C. W. (1997) β-amyloid neurotoxicity in vitro: evidence of oxidative stress but not protection by antioxidants. J. Neurochem. 69: 1601-1611
    • (1997) J. Neurochem. , vol.69 , pp. 1601-1611
    • Pike, C.J.1    Ramezan-Arab, N.2    Cotman, C.W.3
  • 29
  • 31
    • 0028207907 scopus 로고
    • Amyloid β peptide induces necrosis rather than apoptosis
    • 31 Behl C., Davis J. B., Klier G. F. and Schubert D. (1994) Amyloid β peptide induces necrosis rather than apoptosis. Brain Res. 645: 253-264
    • (1994) Brain Res. , vol.645 , pp. 253-264
    • Behl, C.1    Davis, J.B.2    Klier, G.F.3    Schubert, D.4
  • 32
    • 0030808462 scopus 로고    scopus 로고
    • Aggregated amyloid-β protein induces cortical neuronal apoptosis and concomitant 'apoptotic' pattern of gene induction
    • 32 Estus S., Tucker H. M., Rooyen C. van, Wright S., Brigham E., Wogulis M. et al. (1997) Aggregated amyloid-β protein induces cortical neuronal apoptosis and concomitant 'apoptotic' pattern of gene induction. J. Neurosci. 17: 7736-7745
    • (1997) J. Neurosci. , vol.17 , pp. 7736-7745
    • Estus, S.1    Tucker, H.M.2    Van Rooyen, C.3    Wright, S.4    Brigham, E.5    Wogulis, M.6
  • 33
    • 0029860523 scopus 로고    scopus 로고
    • Amyloid β peptide of Alzheimer's disease downregulates Bcl-2 and upregulates Bax expression in human neurons
    • 33 Paradis E., Douillard H., Koutroumanis M., Goodyer C. and LeBlanc A. (1996) Amyloid β peptide of Alzheimer's disease downregulates Bcl-2 and upregulates Bax expression in human neurons. J. Neurosci. 16: 7533-7539
    • (1996) J. Neurosci. , vol.16 , pp. 7533-7539
    • Paradis, E.1    Douillard, H.2    Koutroumanis, M.3    Goodyer, C.4    LeBlanc, A.5
  • 34
    • 0030831489 scopus 로고    scopus 로고
    • Correlates of p53-and Fas (CD95)-mediated apoptosis in Alzheimer's disease
    • 34 Monte S. M. de la, Sohn Y. K. and Wands J. R. (1997) Correlates of p53-and Fas (CD95)-mediated apoptosis in Alzheimer's disease. J. Neurol. Sci. 152: 73-83
    • (1997) J. Neurol. Sci. , vol.152 , pp. 73-83
    • De La Monte, S.M.1    Sohn, Y.K.2    Wands, J.R.3
  • 35
    • 0006325405 scopus 로고    scopus 로고
    • Alzheimer's disease: A re-examination of the amyloid hypothesis
    • 35 Neve R. L. and Robakis N. (1998) Alzheimer's disease: a re-examination of the amyloid hypothesis. Trends Neurosci. 21: 15-19
    • (1998) Trends Neurosci. , vol.21 , pp. 15-19
    • Neve, R.L.1    Robakis, N.2
  • 36
    • 0029670992 scopus 로고    scopus 로고
    • Deposits of Aβ fibrils are not toxic to cortical and hippocampal neurons in vitro
    • 36 Wujek J. R., Dority M. D., Frederickson R. C. A. and Brunden K. (1996) Deposits of Aβ fibrils are not toxic to cortical and hippocampal neurons in vitro. Neurobiol. Aging 17: 107-113
    • (1996) Neurobiol. Aging , vol.17 , pp. 107-113
    • Wujek, J.R.1    Dority, M.D.2    Frederickson, R.C.A.3    Brunden, K.4
  • 37
    • 0031596988 scopus 로고    scopus 로고
    • The α5β1 integrin mediates elimination of amyloid-β peptide and protects against apoptosis
    • 37 Matter M. L., Zhang Z., Nordsedt C. and Ruolahti E. (1998) The α5β1 integrin mediates elimination of amyloid-β peptide and protects against apoptosis. J. Cell Biol. 141: 119-1030
    • (1998) J. Cell Biol. , vol.141 , pp. 119-1030
    • Matter, M.L.1    Zhang, Z.2    Nordsedt, C.3    Ruolahti, E.4
  • 38
    • 0030793522 scopus 로고    scopus 로고
    • Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Abeta stabilization
    • 38 LaFerla F. M., Troncoso J. C., Strickland D. K., Kawas C. H. and Jay G. (1997) Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Abeta stabilization. J. Clin. Invest. 100: 310-320
    • (1997) J. Clin. Invest. , vol.100 , pp. 310-320
    • LaFerla, F.M.1    Troncoso, J.C.2    Strickland, D.K.3    Kawas, C.H.4    Jay, G.5
  • 39
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4 β protein
    • 39 Knauer M., Soreghan B., Burdick D., Kosmoki J. and Glabe C. (1992) Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4 β protein. Proc. Natl. Acad. Sci. USA 89: 7437-7441
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7437-7441
    • Knauer, M.1    Soreghan, B.2    Burdick, D.3    Kosmoki, J.4    Glabe, C.5
  • 40
    • 0032516821 scopus 로고    scopus 로고
    • Molecular dissection of domains in mutant presenilin 2 that mediate overproduction of amyloidogenic forms of amyloid β peptides
    • 40 Tomita T., Tokuhiro S., Hashimoto T., Aiba K., Saido T. C., Maruyama K. et al. (1998) Molecular dissection of domains in mutant presenilin 2 that mediate overproduction of amyloidogenic forms of amyloid β peptides. J. Biol. Chem. 273: 21153-21160
    • (1998) J. Biol. Chem. , vol.273 , pp. 21153-21160
    • Tomita, T.1    Tokuhiro, S.2    Hashimoto, T.3    Aiba, K.4    Saido, T.C.5    Maruyama, K.6
  • 42
    • 17344372115 scopus 로고    scopus 로고
    • Interaction of presenilins with the filamin family of actin-binding proteins
    • 42 Zhang W., Han S. W., McKeel D. W., Goate A. and Wu J. Y. (1998) Interaction of presenilins with the filamin family of actin-binding proteins. J. Neurosci. 18: 914-922
    • (1998) J. Neurosci. , vol.18 , pp. 914-922
    • Zhang, W.1    Han, S.W.2    McKeel, D.W.3    Goate, A.4    Wu, J.Y.5
  • 43
    • 0032531793 scopus 로고    scopus 로고
    • Destabilization of β-catenin by mutations in presenilin-1 potentiates neuronal apoptosis
    • 43 Zhang Z., Hartmann H., Do V. M., Abramowski D., Sturchler-Pierrat C., Staufenbiel M. et al. (1998) Destabilization of β-catenin by mutations in presenilin-1 potentiates neuronal apoptosis. Nature 395: 698-702
    • (1998) Nature , vol.395 , pp. 698-702
    • Zhang, Z.1    Hartmann, H.2    Do, V.M.3    Abramowski, D.4    Sturchler-Pierrat, C.5    Staufenbiel, M.6
  • 44
    • 0032568846 scopus 로고    scopus 로고
    • Regulation of brain G-protein go by Alzheimer's disease gene presenilin-1
    • 44 Smine A., Xu X., Nishiyama K., Katada T., Gambetti P., Yadav S. P. et al. (1998) Regulation of brain G-protein go by Alzheimer's disease gene presenilin-1. J. Biol. Chem. 273: 16281-16288
    • (1998) J. Biol. Chem. , vol.273 , pp. 16281-16288
    • Smine, A.1    Xu, X.2    Nishiyama, K.3    Katada, T.4    Gambetti, P.5    Yadav, S.P.6
  • 45
    • 0031721511 scopus 로고    scopus 로고
    • Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment
    • 45 Buxbaum J. D., Choi E.-K., Luo Y., Lilliehook C., Crowley A. C., Merriam D. E. et al. (1998) Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment. Nat. Med. 4: 1177-1181
    • (1998) Nat. Med. , vol.4 , pp. 1177-1181
    • Buxbaum, J.D.1    Choi, E.-K.2    Luo, Y.3    Lilliehook, C.4    Crowley, A.C.5    Merriam, D.E.6
  • 48
  • 49
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • 49 Kim T.-W., Pettingell W. H., Jung Y.-K.., Kovacs D. and Tanzi R. E. (1997) Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 277: 373-376
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.-W.1    Pettingell, W.H.2    Jung, Y.-K.3    Kovacs, D.4    Tanzi, R.E.5
  • 50
    • 0345055313 scopus 로고    scopus 로고
    • Increased sensitivity to mitochondrial toxin-induced apoptosis in neural cells expressing mutant presenilin-1
    • 50 Keller J. N., Guo Q., Holtsberg F. W., Bruce-Keller A. J. and Mattson M. P. (1998) Increased sensitivity to mitochondrial toxin-induced apoptosis in neural cells expressing mutant presenilin-1. J. Neurosci. 18: 4439-4450
    • (1998) J. Neurosci. , vol.18 , pp. 4439-4450
    • Keller, J.N.1    Guo, Q.2    Holtsberg, F.W.3    Bruce-Keller, A.J.4    Mattson, M.P.5
  • 51
    • 0031927628 scopus 로고    scopus 로고
    • Par-4 is a mediator of neuronal degeneration associated with the pathogenesis of Alzheimer disease
    • 51 Guo Q., Fu W., Xie J., Luo H., Sells S. F., Geddes J. et al. (1998) Par-4 is a mediator of neuronal degeneration associated with the pathogenesis of Alzheimer disease. Nat. Med. 4: 957-962
    • (1998) Nat. Med. , vol.4 , pp. 957-962
    • Guo, Q.1    Fu, W.2    Xie, J.3    Luo, H.4    Sells, S.F.5    Geddes, J.6
  • 52
    • 0032127320 scopus 로고    scopus 로고
    • Both N-terminal and C-terminal fragments of presenilin 1 colocalize with neurofibrillary tangles in neurons and dystrophic neurites of senile plaques in Alzheimer's disease
    • 52 Chui D. H., Shirotani K., Tanahashi H., Akiyama H., Ozawa K., Kunishi T. et al. (1998) Both N-terminal and C-terminal fragments of presenilin 1 colocalize with neurofibrillary tangles in neurons and dystrophic neurites of senile plaques in Alzheimer's disease. J. Neurosci. Res. 53: 99-106
    • (1998) J. Neurosci. Res. , vol.53 , pp. 99-106
    • Chui, D.H.1    Shirotani, K.2    Tanahashi, H.3    Akiyama, H.4    Ozawa, K.5    Kunishi, T.6
  • 53
    • 0030753089 scopus 로고    scopus 로고
    • Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer disease
    • 53 Xia W., Zhang J., Perez R., Koo E. H. and Selkoe D. J. (1997) Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer disease. Proc. Natl. Acad. Sci. USA 94: 8208-8213
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8208-8213
    • Xia, W.1    Zhang, J.2    Perez, R.3    Koo, E.H.4    Selkoe, D.J.5
  • 54
    • 0030830304 scopus 로고    scopus 로고
    • Tau phosphorylation in transgenic mice expressing glycogen syntase kinase-3beta transgenes
    • 54 Brownless J., Irving N.G., Brion J.P., Gibb B. J., Wagner U., Woodgett J. et al. (1997) Tau phosphorylation in transgenic mice expressing glycogen syntase kinase-3beta transgenes. Neuroreports 8: 3251-3255
    • (1997) Neuroreports , vol.8 , pp. 3251-3255
    • Brownless, J.1    Irving, N.G.2    Brion, J.P.3    Gibb, B.J.4    Wagner, U.5    Woodgett, J.6
  • 55
    • 17344365975 scopus 로고
    • Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis
    • 55 Canu N., Dus L., Barbato C., Ciotti M. T., Brancolini C., Rinaldi A. M. et al. (1988) Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis. J. Neurosci. 18: 7061-7074
    • (1988) J. Neurosci. , vol.18 , pp. 7061-7074
    • Canu, N.1    Dus, L.2    Barbato, C.3    Ciotti, M.T.4    Brancolini, C.5    Rinaldi, A.M.6
  • 56
    • 0031906761 scopus 로고    scopus 로고
    • Protection against β-amyloid toxicity in primary neurons by paclitaxel (taxol)
    • 56 Michaelis M. L., Ranciat N., Chen Y., Betchel M., Ragan R., Hepperle M. et al. (1998) Protection against β-amyloid toxicity in primary neurons by paclitaxel (taxol). J. Neurochem. 70: 1623-1627
    • (1998) J. Neurochem. , vol.70 , pp. 1623-1627
    • Michaelis, M.L.1    Ranciat, N.2    Chen, Y.3    Betchel, M.4    Ragan, R.5    Hepperle, M.6
  • 57
    • 0031920383 scopus 로고    scopus 로고
    • Stable association of presenilin derivatives and absence of presenilin interactions with APP
    • 57 Thinakaran G., Regard J. B., Bouton C. M., Harris C. L., Price D. L., Borchelt D. R. et al. (1998) Stable association of presenilin derivatives and absence of presenilin interactions with APP. Neurobiol. Dis. 4: 438-453
    • (1998) Neurobiol. Dis. , vol.4 , pp. 438-453
    • Thinakaran, G.1    Regard, J.B.2    Bouton, C.M.3    Harris, C.L.4    Price, D.L.5    Borchelt, D.R.6
  • 58
    • 0030788767 scopus 로고    scopus 로고
    • Presenilin 1 interaction in the brain with a novel member of the armadillo family
    • 58 Zhou J., Liyanage U., Medina M., Ho C., Simmons A., Lovett M. et al. (1997) Presenilin 1 interaction in the brain with a novel member of the armadillo family. Neuroreports 8: 2085-2090
    • (1997) Neuroreports , vol.8 , pp. 2085-2090
    • Zhou, J.1    Liyanage, U.2    Medina, M.3    Ho, C.4    Simmons, A.5    Lovett, M.6
  • 59
    • 0030664076 scopus 로고    scopus 로고
    • Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells
    • 59 Paresce D., Chung H. and Maxfield F. R. (1997) Slow degradation of aggregates of the Alzheimer's disease amyloid β-protein by microglial cells. J. Biol. Chem. 272: 29390-29397
    • (1997) J. Biol. Chem. , vol.272 , pp. 29390-29397
    • Paresce, D.1    Chung, H.2    Maxfield, F.R.3
  • 60
    • 0032521111 scopus 로고    scopus 로고
    • Fibrillar β-amyloid induces microglial phagocytosis, expression of inducible nitric oxide synthase, and loss of a select population of neurons in the rat CNS in vivo
    • 60 Weldon P. T., Rogers S. D., Ghilardi J. R., Finke M. P., Cleary J. P., O'Hare E. et al. (1998) Fibrillar β-amyloid induces microglial phagocytosis, expression of inducible nitric oxide synthase, and loss of a select population of neurons in the rat CNS in vivo. J. Neurosci. 18: 2161-2173
    • (1998) J. Neurosci. , vol.18 , pp. 2161-2173
    • Weldon, P.T.1    Rogers, S.D.2    Ghilardi, J.R.3    Finke, M.P.4    Cleary, J.P.5    O'Hare, E.6
  • 62
    • 0031576547 scopus 로고    scopus 로고
    • Modulation of nitric oxide production in human macrophages by apolipoprotein-E and amyloid-beta peptide
    • 62 Vitek M. P., Snell J., Dawson H. and Colton C. A. (1997) Modulation of nitric oxide production in human macrophages by apolipoprotein-E and amyloid-beta peptide. Biochem. Biophys. Res. Commun. 240: 391-394
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 391-394
    • Vitek, M.P.1    Snell, J.2    Dawson, H.3    Colton, C.A.4
  • 63
    • 0030001328 scopus 로고    scopus 로고
    • Brain expression of apolipoprotcins E, J, and A-I in Alzheimer's disease
    • 63 Harr S. D., Uint L., Hollister R., Hyman B. and Mendez A. J. (1996) Brain expression of apolipoprotcins E, J, and A-I in Alzheimer's disease. J. Neurochem. 66: 2429-2435
    • (1996) J. Neurochem. , vol.66 , pp. 2429-2435
    • Harr, S.D.1    Uint, L.2    Hollister, R.3    Hyman, B.4    Mendez, A.J.5
  • 65
    • 0028232662 scopus 로고
    • Differential effects of apolipoproteins E3 and E4 on neuronal outgrowth in vitro
    • 65 Nathan B. P., Bellosta S., Sanan D. A., Wiesgraber K. H., Mahley R. W. and Pitas R. E. (1994) Differential effects of apolipoproteins E3 and E4 on neuronal outgrowth in vitro. Science 264: 850-852
    • (1994) Science , vol.264 , pp. 850-852
    • Nathan, B.P.1    Bellosta, S.2    Sanan, D.A.3    Wiesgraber, K.H.4    Mahley, R.W.5    Pitas, R.E.6
  • 66
    • 0032512634 scopus 로고    scopus 로고
    • A minimally lipidaled form of cell-derived apolipoprotein E exhibits isoform-specific stimulation of neurite outgrowth in the absence of exogenous lipids or lipoproteins
    • 66 DeMattos R. B., Curtiss L. K. and Williams D. L. (1998) A minimally lipidaled form of cell-derived apolipoprotein E exhibits isoform-specific stimulation of neurite outgrowth in the absence of exogenous lipids or lipoproteins. J. Biol. Chem. 273: 4206-4212
    • (1998) J. Biol. Chem. , vol.273 , pp. 4206-4212
    • DeMattos, R.B.1    Curtiss, L.K.2    Williams, D.L.3
  • 67
    • 0029157112 scopus 로고
    • The inhibitory effect of apolioprotein E4 on neurite outgrowth is associated with microtubule depolymerization
    • 67 Nathan B. P., Chang K.-C., Bellosta S., Brisch E., Ge N., Mahley R. W. et al. (1995) The inhibitory effect of apolioprotein E4 on neurite outgrowth is associated with microtubule depolymerization. J. Biol. Chem. 270: 19791-19799
    • (1995) J. Biol. Chem. , vol.270 , pp. 19791-19799
    • Nathan, B.P.1    Chang, K.-C.2    Bellosta, S.3    Brisch, E.4    Ge, N.5    Mahley, R.W.6
  • 68
    • 0031963852 scopus 로고    scopus 로고
    • Isoform-specific effect of apolipoprotein E on cell survival and β-amyloid-induced toxicily in rat hippocampal pyramidal neuronal cultures
    • 68 Jordan J., Galindo M. F., Miller R. J., Reardon C. A., Getz G. S. and LaDu M. J. (1998) Isoform-specific effect of apolipoprotein E on cell survival and β-amyloid-induced toxicily in rat hippocampal pyramidal neuronal cultures. J. Neurosci. 18: 195-204
    • (1998) J. Neurosci. , vol.18 , pp. 195-204
    • Jordan, J.1    Galindo, M.F.2    Miller, R.J.3    Reardon, C.A.4    Getz, G.S.5    Ladu, M.J.6
  • 69
    • 0031252629 scopus 로고    scopus 로고
    • What do all the apolipoprotein E receptors do?
    • 69 St Clair R. W. and Beisigel U. (1997) What do all the apolipoprotein E receptors do? Curr. Opin. Lipidol. 8: 243-245
    • (1997) Curr. Opin. Lipidol. , vol.8 , pp. 243-245
    • St Clair, R.W.1    Beisigel, U.2
  • 70
    • 0030783740 scopus 로고    scopus 로고
    • Novel members of the low density lipoprotein receptor superfamily and their potential roles in lipid metabolism
    • 70 Schneider W., Nimpf J. and Bujo H. (1997) Novel members of the low density lipoprotein receptor superfamily and their potential roles in lipid metabolism. Curr. Opin. Lipidol. 8: 315-319
    • (1997) Curr. Opin. Lipidol. , vol.8 , pp. 315-319
    • Schneider, W.1    Nimpf, J.2    Bujo, H.3
  • 71
    • 0033610841 scopus 로고    scopus 로고
    • The low density lipoprotein receptor gene family: Differential expression of two alpha2-macroglobulin receptors in the brain
    • 71 Stockinger W., Hengstsschlager-Ottnad E., Novak S., Matus A., Höttinger M., Bauer J. et al. (1998) The low density lipoprotein receptor gene family: differential expression of two alpha2-macroglobulin receptors in the brain. J. Biol. Chem. 273: 32213-32221
    • (1998) J. Biol. Chem. , vol.273 , pp. 32213-32221
    • Stockinger, W.1    Hengstsschlager-Ottnad, E.2    Novak, S.3    Matus, A.4    Höttinger, M.5    Bauer, J.6
  • 72
    • 0030863380 scopus 로고    scopus 로고
    • Ammo-terminus truncated apolipoprotein E is the major species in amyloid deposits in Alzheimer's disease-affected brains: A possible role for apolipoprotein E in Alzheimer's disease
    • 72 Aizawa Y., Fukatsu R., Takamuru Y., Tsuzuki K., Chiba H., Kobayashi K. et al. (1997) Ammo-terminus truncated apolipoprotein E is the major species in amyloid deposits in Alzheimer's disease-affected brains: a possible role for apolipoprotein E in Alzheimer's disease. Brain Res. 768: 208-214
    • (1997) Brain Res. , vol.768 , pp. 208-214
    • Aizawa, Y.1    Fukatsu, R.2    Takamuru, Y.3    Tsuzuki, K.4    Chiba, H.5    Kobayashi, K.6
  • 73
    • 0031037086 scopus 로고    scopus 로고
    • Specific modulation of the fusogenic properties of the Alzheimer -amyloid peptide by apolipoprotein E isoforms
    • 73 Pillot T., Goethals M., Vanloo B., Lins L., Brasseur R., Vandekerchkhove J. et al. (1997) Specific modulation of the fusogenic properties of the Alzheimer (-amyloid peptide by apolipoprotein E isoforms. Eur. J. Biochem. 243: 650-659
    • (1997) Eur. J. Biochem. , vol.243 , pp. 650-659
    • Pillot, T.1    Goethals, M.2    Vanloo, B.3    Lins, L.4    Brasseur, R.5    Vandekerchkhove, J.6
  • 74
    • 0032487497 scopus 로고    scopus 로고
    • ApoE associated with lipid has a reduced capacity to inhibit beta-amyloid fibril formation
    • 74 Beffert U. and Poirier J. (1998) ApoE associated with lipid has a reduced capacity to inhibit beta-amyloid fibril formation. Neuroreports 9: 3321-3323
    • (1998) Neuroreports , vol.9 , pp. 3321-3323
    • Beffert, U.1    Poirier, J.2
  • 75
    • 0031797037 scopus 로고    scopus 로고
    • Uptake and internalization of exogenous apolipoprotein E3 by cultured human central nervous system neurons
    • 75 Williams K. R., Saunders A. M., Roses A. D. and Armati P. J. (1998) Uptake and internalization of exogenous apolipoprotein E3 by cultured human central nervous system neurons. Neurobiol. Dis. 5: 271-279
    • (1998) Neurobiol. Dis. , vol.5 , pp. 271-279
    • Williams, K.R.1    Saunders, A.M.2    Roses, A.D.3    Armati, P.J.4
  • 76
    • 0025971426 scopus 로고
    • Apolipoprotein E immunoreactivity in cerebral deposits and neurofibrillary tangles in Alzheimer's disease brain
    • 76 Namba Y., Tomonaga M., Kawasaki H., Otomo E. and Ikeda K. (1991) Apolipoprotein E immunoreactivity in cerebral deposits and neurofibrillary tangles in Alzheimer's disease brain. Brain Res. 541: 163-166
    • (1991) Brain Res. , vol.541 , pp. 163-166
    • Namba, Y.1    Tomonaga, M.2    Kawasaki, H.3    Otomo, E.4    Ikeda, K.5
  • 77
    • 0031555394 scopus 로고    scopus 로고
    • Identification of a neuronal endocytic pathway activated by an apolipoprotein E (apoE) receptor binding peptide
    • 77 Wang X., Ciraolo G., Morris R. and Gruenstein E. (1997) Identification of a neuronal endocytic pathway activated by an apolipoprotein E (apoE) receptor binding peptide. Brain Res. 778: 6-15
    • (1997) Brain Res. , vol.778 , pp. 6-15
    • Wang, X.1    Ciraolo, G.2    Morris, R.3    Gruenstein, E.4
  • 78
    • 0032573452 scopus 로고    scopus 로고
    • Soluble Alzheimer's beta-amyloid constricts the cerebral vasculature in vivo
    • 78 Suo Z., Humphrey J., Kundtz A., Sethi F., Placzek A., Crawford F. et al. (1998) Soluble Alzheimer's beta-amyloid constricts the cerebral vasculature in vivo. Neurosci. Lett. 257: 77-80
    • (1998) Neurosci. Lett. , vol.257 , pp. 77-80
    • Suo, Z.1    Humphrey, J.2    Kundtz, A.3    Sethi, F.4    Placzek, A.5    Crawford, F.6
  • 79
    • 0032491512 scopus 로고    scopus 로고
    • Isoform-specific vasoconstriction induced by apolipoprotein e and modulation of this effect by Alzheimer's beta-amyloid peptide
    • 79 Paris D., Town T., Parker T. A., Humphrey J. and Mullan M. (1998) Isoform-specific vasoconstriction induced by apolipoprotein e and modulation of this effect by Alzheimer's beta-amyloid peptide. Neurosci. Lett. 256: 73-76
    • (1998) Neurosci. Lett. , vol.256 , pp. 73-76
    • Paris, D.1    Town, T.2    Parker, T.A.3    Humphrey, J.4    Mullan, M.5
  • 80
    • 0031587429 scopus 로고    scopus 로고
    • Detection of apolipoprotein E/dimeric soluble amyloid complexes in Alzheimer's disease brain supernatants
    • 80 Permanne B., Perez C., Soto C., Frangione B. and Wisniewski T. (1997) Detection of apolipoprotein E/dimeric soluble amyloid ( complexes in Alzheimer's disease brain supernatants. Biochem. Biophys. Res. Commun. 240: 715-720
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 715-720
    • Permanne, B.1    Perez, C.2    Soto, C.3    Frangione, B.4    Wisniewski, T.5
  • 81
    • 0030792971 scopus 로고    scopus 로고
    • Apolipoprotein E binds to and potentiates the biological activity of ciliary neurotrophic factor
    • 81 Gutman C. A., Strittmatter W., Weisgraber K. H. and Matthew W. D. (1997) Apolipoprotein E binds to and potentiates the biological activity of ciliary neurotrophic factor. J. Neurosci. 17: 6114-6121
    • (1997) J. Neurosci. , vol.17 , pp. 6114-6121
    • Gutman, C.A.1    Strittmatter, W.2    Weisgraber, K.H.3    Matthew, W.D.4
  • 82
    • 0030885417 scopus 로고    scopus 로고
    • Transbilayer distribution of cholesterol is modified in brain synaptic plasma membranes of knockout mice deficient in the low-density lipoprotein receptor, apolipoprotein E, or both proteins
    • 82 Igbavboa U., Avdulov N. A., Chochina S. V. and Wood W. G. (1997) Transbilayer distribution of cholesterol is modified in brain synaptic plasma membranes of knockout mice deficient in the low-density lipoprotein receptor, apolipoprotein E, or both proteins. J. Neurochem. 69: 1661-1667
    • (1997) J. Neurochem. , vol.69 , pp. 1661-1667
    • Igbavboa, U.1    Avdulov, N.A.2    Chochina, S.V.3    Wood, W.G.4
  • 83
    • 0031005995 scopus 로고    scopus 로고
    • Aggregation of β-amyloid peptide is promoted by membrane phospholipid metabolites elevated in Alzheimer's disease brain
    • 83 Klunk W. E., Xu C.-J., McClure R. J., Panchalingam K., Stanley J. A. and Pettergrew J. W. (1997) Aggregation of β-amyloid peptide is promoted by membrane phospholipid metabolites elevated in Alzheimer's disease brain. J. Neurochem. 69: 266-272
    • (1997) J. Neurochem. , vol.69 , pp. 266-272
    • Klunk, W.E.1    Xu, C.-J.2    McClure, R.J.3    Panchalingam, K.4    Stanley, J.A.5    Pettergrew, J.W.6
  • 85
    • 0029671454 scopus 로고    scopus 로고
    • Cholesterol modulates β-secretase cleavage of amyloid precursor protein
    • 85 Bodovitz S. and Klein W. L. (1996) Cholesterol modulates β-secretase cleavage of amyloid precursor protein. J. Biol. Chem. 271: 4436-4440
    • (1996) J. Biol. Chem. , vol.271 , pp. 4436-4440
    • Bodovitz, S.1    Klein, W.L.2
  • 87
    • 17644429206 scopus 로고    scopus 로고
    • Secretory processing of amyloid precursor protein is inhibited by increase in cellular cholesterol content
    • 87 Racchi M., Baetta R., Salvietti N., Ianna P., Franceschini G., Paoletti R. et al. (1997) Secretory processing of amyloid precursor protein is inhibited by increase in cellular cholesterol content. Biochem. J. 322: 893-898
    • (1997) Biochem. J. , vol.322 , pp. 893-898
    • Racchi, M.1    Baetta, R.2    Salvietti, N.3    Ianna, P.4    Franceschini, G.5    Paoletti, R.6
  • 88
    • 0032573097 scopus 로고    scopus 로고
    • Amyloid beta peptide alters intracellular vesicle trafficking and cholesterol homeostasis
    • 88 Liu Y., Peterson D. A. and Schubert D. (1998) Amyloid beta peptide alters intracellular vesicle trafficking and cholesterol homeostasis. Proc. Natl. Acad. Sci. USA 95: 13266-13271
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13266-13271
    • Liu, Y.1    Peterson, D.A.2    Schubert, D.3
  • 90
    • 0013642132 scopus 로고    scopus 로고
    • Degradation of amyloid β-protein by a serine protease-α2-macroglobulin complex
    • 90 Qiu W. Q., Borth W., Ye Z., Haas C., Teplow D. B. and Selkow D. (1996) Degradation of amyloid β-protein by a serine protease-α2-macroglobulin complex. J. Biol. Chem. 271: 8443-8451
    • (1996) J. Biol. Chem. , vol.271 , pp. 8443-8451
    • Qiu, W.Q.1    Borth, W.2    Ye, Z.3    Haas, C.4    Teplow, D.B.5    Selkow, D.6
  • 91
    • 0030770726 scopus 로고    scopus 로고
    • Complete genomic screen in late-onset familial Alzheimer disease. Evidence for a new locus on chromosome 12
    • 91 Pericak-Vance M. A., Bass M. P., Yamaoka L. H., Gaskell P. C, Scott W. K., Terwedow H. A. et al. (1997) Complete genomic screen in late-onset familial Alzheimer disease. Evidence for a new locus on chromosome 12. JAMA 278: 1237-1241
    • (1997) JAMA , vol.278 , pp. 1237-1241
    • Pericak-Vance, M.A.1    Bass, M.P.2    Yamaoka, L.H.3    Gaskell, P.C.4    Scott, W.K.5    Terwedow, H.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.