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Volumn 70, Issue 1, 1998, Pages 1-14

Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease

Author keywords

Amyloid precursor protein; Amyloid peptide; Apoptosis; Calcium homeostasis; Inositol trisphosphate; Muscarinic cholinergic; Nerve growth factor; Reactive oxygen species; Vitamin E

Indexed keywords

AMYLOID BETA PROTEIN; PRESENILIN 1; PRESENILIN 2;

EID: 0031982670     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.70010001.x     Document Type: Review
Times cited : (239)

References (111)
  • 1
    • 0030222080 scopus 로고    scopus 로고
    • Induction of neuroprotective κB-dependent transcription by secreted forms of the Alzheimer's β-amyloid precursor
    • Barger S. W. and Mattson M. P. (1996) Induction of neuroprotective κB-dependent transcription by secreted forms of the Alzheimer's β-amyloid precursor. Mol. Brain Res. 40, 116-126.
    • (1996) Mol. Brain Res. , vol.40 , pp. 116-126
    • Barger, S.W.1    Mattson, M.P.2
  • 2
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction
    • Bartus R. T., Dean R. L., Beer B., and Lippa A. S. (1982) The cholinergic hypothesis of geriatric memory dysfunction. Science 214, 408-417.
    • (1982) Science , vol.214 , pp. 408-417
    • Bartus, R.T.1    Dean, R.L.2    Beer, B.3    Lippa, A.S.4
  • 3
    • 0029145084 scopus 로고
    • Are reactive oxygen species involved in Alzheimer's disease?
    • Benzi G. and Moretti A. (1995) Are reactive oxygen species involved in Alzheimer's disease? Neurobiol. Aging 16, 661-674.
    • (1995) Neurobiol. Aging , vol.16 , pp. 661-674
    • Benzi, G.1    Moretti, A.2
  • 8
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • Bowling A. C. and Beal M. F. (1995) Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci. 56, 1151-1171.
    • (1995) Life Sci. , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 9
    • 0031006343 scopus 로고    scopus 로고
    • Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease
    • Busciglio J., Hartmann H., Lorenzo A., Wong C., Baumann K., Sommer B., Staufenbiel M., and Yankner B. A. (1997) Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease. J. Neurosci. 17, 5101-5107.
    • (1997) J. Neurosci. , vol.17 , pp. 5101-5107
    • Busciglio, J.1    Hartmann, H.2    Lorenzo, A.3    Wong, C.4    Baumann, K.5    Sommer, B.6    Staufenbiel, M.7    Yankner, B.A.8
  • 12
    • 0028989016 scopus 로고
    • Notch1 is required for the coordinate segmentation of somites
    • Conlon R. A., Reaume A. G., and Rossant J. (1995) Notch1 is required for the coordinate segmentation of somites. Development 121, 1533-1545.
    • (1995) Development , vol.121 , pp. 1533-1545
    • Conlon, R.A.1    Reaume, A.G.2    Rossant, J.3
  • 14
    • 0029982341 scopus 로고    scopus 로고
    • Widespread neuronal expression of the presenilin-1 early-onset Alzheimer's disease in the murine brain
    • Cribbs D. H., Chen L., Bendle S. M., and La Ferla F. M. (1996) Widespread neuronal expression of the presenilin-1 early-onset Alzheimer's disease in the murine brain. Am. J. Pathol 148, 1797-1806.
    • (1996) Am. J. Pathol , vol.148 , pp. 1797-1806
    • Cribbs, D.H.1    Chen, L.2    Bendle, S.M.3    La Ferla, F.M.4
  • 16
    • 0030580281 scopus 로고    scopus 로고
    • Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells
    • Deng G., Pike C. J., and Cotman C. W. (1996) Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells. FEBS Lett. 397, 50-54.
    • (1996) FEBS Lett. , vol.397 , pp. 50-54
    • Deng, G.1    Pike, C.J.2    Cotman, C.W.3
  • 18
    • 0029861413 scopus 로고    scopus 로고
    • Specific transcellular binding between membrane proteins crucial to Alzheimer disease
    • Dewji N. N. and Singer S. J. (1996) Specific transcellular binding between membrane proteins crucial to Alzheimer disease. Proc. Natl. Acad. Sci. USA 93, 12575-12580.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12575-12580
    • Dewji, N.N.1    Singer, S.J.2
  • 22
    • 0029841562 scopus 로고    scopus 로고
    • Increased activity-regulating and neuroprotective efficacy of α-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain
    • Furukawa K., Sopher B. L., Rydel R. E., Begley J. G., Pham D. G., Martin G. M., Fox M., and Mattson M. P. (1996) Increased activity-regulating and neuroprotective efficacy of α-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain. J. Neurochem. 67, 1882-1896.
    • (1996) J. Neurochem. , vol.67 , pp. 1882-1896
    • Furukawa, K.1    Sopher, B.L.2    Rydel, R.E.3    Begley, J.G.4    Pham, D.G.5    Martin, G.M.6    Fox, M.7    Mattson, M.P.8
  • 23
    • 0028200649 scopus 로고
    • Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative
    • Gabuzda D., Busciglio J., Chen L., Matsudaira P., and Yankner B. A. (1994) Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J. Biol. Chem. 269, 13623-13628.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13623-13628
    • Gabuzda, D.1    Busciglio, J.2    Chen, L.3    Matsudaira, P.4    Yankner, B.A.5
  • 24
    • 0011209984 scopus 로고
    • Imaging of calcium and aluminum in neurofibrillary tangle-bearing neurons in parkinsonism-dementia of Guam
    • Garruto R. M., Fukatsu R., Yanagihara R., Gajdusek D. C., Hook G., and Fiori C. E. (1984) Imaging of calcium and aluminum in neurofibrillary tangle-bearing neurons in parkinsonism-dementia of Guam. Proc. Natl. Acad. Sci. USA 81, 1875-1879.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1875-1879
    • Garruto, R.M.1    Fukatsu, R.2    Yanagihara, R.3    Gajdusek, D.C.4    Hook, G.5    Fiori, C.E.6
  • 26
    • 0030891662 scopus 로고    scopus 로고
    • Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide
    • Guo Q., Furukawa K., Sopher B. L., Pham D. G., Xie J., Robinson N., Martin G. M., and Mattson M. P. (1996) Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide. Neuroreport 8, 379-383.
    • (1996) Neuroreport , vol.8 , pp. 379-383
    • Guo, Q.1    Furukawa, K.2    Sopher, B.L.3    Pham, D.G.4    Xie, J.5    Robinson, N.6    Martin, G.M.7    Mattson, M.P.8
  • 27
    • 0030917601 scopus 로고    scopus 로고
    • Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid β-peptide: Involvement of calcium and oxyradicals
    • Guo G., Sopher B. L., Pham D. G., Furukawa K., Robinson N., Martin G. M., and Mattson M. P. (1997) Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid β-peptide: involvement of calcium and oxyradicals. J. Neurosci. 17, 4212-4222.
    • (1997) J. Neurosci. , vol.17 , pp. 4212-4222
    • Guo, G.1    Sopher, B.L.2    Pham, D.G.3    Furukawa, K.4    Robinson, N.5    Martin, G.M.6    Mattson, M.P.7
  • 28
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J. (1997) Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20, 154-159.
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 29
    • 0031004532 scopus 로고    scopus 로고
    • Developmental regulation of presenilin-1 processing in the brain suggests a role in neuronal differentiation
    • Hartmann H., Busciglio J., Baumann K. H., Staufenbiel M., and Yankner B. A. (1997) Developmental regulation of presenilin-1 processing in the brain suggests a role in neuronal differentiation. J. Biol. Chem. 272, 14505-14508.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14505-14508
    • Hartmann, H.1    Busciglio, J.2    Baumann, K.H.3    Staufenbiel, M.4    Yankner, B.A.5
  • 30
    • 0009713456 scopus 로고    scopus 로고
    • Decreased inositol (1,4,5)-trisphosphate receptor levels in Alzheimer's disease cerebral cortex: Selectivity of changes and possible correlation to pathological severity
    • Haug L. S., Ostvold A. C., Cowburn R. F., Garlind A., Winblad B., Bogdanovich N., and Walaas S. I. (1996) Decreased inositol (1,4,5)-trisphosphate receptor levels in Alzheimer's disease cerebral cortex: selectivity of changes and possible correlation to pathological severity. Neurodegeneration 5, 169-176.
    • (1996) Neurodegeneration , vol.5 , pp. 169-176
    • Haug, L.S.1    Ostvold, A.C.2    Cowburn, R.F.3    Garlind, A.4    Winblad, B.5    Bogdanovich, N.6    Walaas, S.I.7
  • 33
    • 0028339255 scopus 로고
    • Thapsigargm-induced persistent intracellular calcium pool depletion and apoptosis in human hepatoma cells
    • Kaneko Y. and Tsukamoto A. (1994) Thapsigargm-induced persistent intracellular calcium pool depletion and apoptosis in human hepatoma cells. Cancer Lett. 97, 147-155.
    • (1994) Cancer Lett. , vol.97 , pp. 147-155
    • Kaneko, Y.1    Tsukamoto, A.2
  • 34
    • 0345590985 scopus 로고    scopus 로고
    • Changes in neurotransmitter signal transduction pathways in the aging brain
    • (Mattson M. P. and Geddes J. W., eds), JAI Press
    • Kelly J. F. and Roth G. S. (1997) Changes in neurotransmitter signal transduction pathways in the aging brain, in The Aging Brain (Mattson M. P. and Geddes J. W., eds), JAI Press; Adv. Cell Aging Gerontol. 2, 243-278.
    • (1997) The Aging Brain
    • Kelly, J.F.1    Roth, G.S.2
  • 35
    • 0345590985 scopus 로고    scopus 로고
    • Kelly J. F. and Roth G. S. (1997) Changes in neurotransmitter signal transduction pathways in the aging brain, in The Aging Brain (Mattson M. P. and Geddes J. W., eds), JAI Press; Adv. Cell Aging Gerontol. 2, 243-278.
    • Adv. Cell Aging Gerontol. , vol.2 , pp. 243-278
  • 37
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim T.-W., Pettingell W. H., Jung Y.-K., Kovacs D. M., 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.M.4    Tanzi, R.E.5
  • 38
    • 0030861571 scopus 로고    scopus 로고
    • Bcl-2 and Bax function independently to regulate cell death
    • Knudson C. M. and Korsmeyer S. J. (1997) Bcl-2 and Bax function independently to regulate cell death. Nat. Genet. 16, 358-363.
    • (1997) Nat. Genet. , vol.16 , pp. 358-363
    • Knudson, C.M.1    Korsmeyer, S.J.2
  • 40
    • 0030986669 scopus 로고    scopus 로고
    • Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis
    • Kruman I., Bruce-Keller A. J., Bredesen D. E., Waeg G., and Mattson M. P. (1997) Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis. J. Neurosci. 17, 5097-5108.
    • (1997) J. Neurosci. , vol.17 , pp. 5097-5108
    • Kruman, I.1    Bruce-Keller, A.J.2    Bredesen, D.E.3    Waeg, G.4    Mattson, M.P.5
  • 41
    • 0026670151 scopus 로고
    • Demonstration of a calcium requirement for secretory protein processing and export
    • Kuznetsov G., Brostrom M. A., and Brostrom C. O. (1992) Demonstration of a calcium requirement for secretory protein processing and export. J. Biol. Chem. 267, 3932-3939.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3932-3939
    • Kuznetsov, G.1    Brostrom, M.A.2    Brostrom, C.O.3
  • 43
    • 0030467394 scopus 로고    scopus 로고
    • Regulation of STAT-dependent pathways by growth factors and cytokines
    • Leaman D. W., Leung S., Li X., and Stark G. R. (1996) Regulation of STAT-dependent pathways by growth factors and cytokines. FASEB J. 10, 1578-1588.
    • (1996) FASEB J. , vol.10 , pp. 1578-1588
    • Leaman, D.W.1    Leung, S.2    Li, X.3    Stark, G.R.4
  • 45
    • 0030922146 scopus 로고    scopus 로고
    • Evidence for a six-transmembrane domain structure of presenilin 1
    • Lehmann S., Chiesa R., and Harris D. A. (1997) Evidence for a six-transmembrane domain structure of presenilin 1. J. Biol. Chem. 272, 12047-12051.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12047-12051
    • Lehmann, S.1    Chiesa, R.2    Harris, D.A.3
  • 46
    • 0029116848 scopus 로고
    • Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • Levitan D. and Greenwald I. (1995) Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 377, 351-354.
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 50
    • 0026688633 scopus 로고
    • Mutation of a putative sperm membrane protein in Caenorhabditis elegans prevents sperm differentiation but not its associated meiotic divisions
    • L'Hernault S. W. and Arduengo P. M. (1992) Mutation of a putative sperm membrane protein in Caenorhabditis elegans prevents sperm differentiation but not its associated meiotic divisions. J. Cell Biol. 119, 55-68.
    • (1992) J. Cell Biol. , vol.119 , pp. 55-68
    • L'Hernault, S.W.1    Arduengo, P.M.2
  • 51
    • 0030293894 scopus 로고    scopus 로고
    • Membrane topology of the C. elegans SEL-12 presenilin
    • Li X. and Greenwald I. (1996) Membrane topology of the C. elegans SEL-12 presenilin. Neuron 17, 1015-1021.
    • (1996) Neuron , vol.17 , pp. 1015-1021
    • Li, X.1    Greenwald, I.2
  • 52
    • 0029899649 scopus 로고    scopus 로고
    • Alteration of acylphosphatase levels in familial Alzheimer's disease fibroblasts with presenilin gene mutations
    • Liguri G., Cecchi C., Latorraca S., Pieri A., Sorbi S., Degl'Innocenti D., and Ramponi G. (1996) Alteration of acylphosphatase levels in familial Alzheimer's disease fibroblasts with presenilin gene mutations. Neurosci. Lett. 210, 153-156.
    • (1996) Neurosci. Lett. , vol.210 , pp. 153-156
    • Liguri, G.1    Cecchi, C.2    Latorraca, S.3    Pieri, A.4    Sorbi, S.5    Degl'Innocenti, D.6    Ramponi, G.7
  • 53
    • 0025313861 scopus 로고
    • Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum
    • Lodish H. F. and Kong N. (1990) Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J. Biol. Chem. 265, 10893-10899.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10893-10899
    • Lodish, H.F.1    Kong, N.2
  • 57
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide
    • Mark R. J., Lovell M. A., Markesbery W. R., Uchida K., and Mattson M. P. (1997a) A role for 4-hydroxynonenal in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide. J. Neurochem. 68, 255-264.
    • (1997) J. Neurochem. , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 58
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid β-peptide impairs glucose uptake in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark R. J., Pang Z., Geddes J. W., and Mattson M. P. (1997b) Amyloid β-peptide impairs glucose uptake in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J. Neurosci. 17, 1046-1054.
    • (1997) J. Neurosci. , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Mattson, M.P.4
  • 59
    • 0025273543 scopus 로고
    • Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and calcium influx in cultured hippocampal neurons
    • Mattson M. P. (1990) Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and calcium influx in cultured hippocampal neurons. Neuron 4, 105-117.
    • (1990) Neuron , vol.4 , pp. 105-117
    • Mattson, M.P.1
  • 60
    • 0026636023 scopus 로고
    • Calcium as sculptor and destroyer of neural circuitry
    • Mattson M. P. (1992) Calcium as sculptor and destroyer of neural circuitry. Exp. Gerontol. 27, 29-49.
    • (1992) Exp. Gerontol. , vol.27 , pp. 29-49
    • Mattson, M.P.1
  • 61
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of β-amyloid precursor protein, and its soluble and fibrillogenic peptide derivatives
    • Mattson M. P. (1997a) Cellular actions of β-amyloid precursor protein, and its soluble and fibrillogenic peptide derivatives. Physiol. Rev. 77, 1081-1132.
    • (1997) Physiol. Rev. , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 62
    • 0030758647 scopus 로고    scopus 로고
    • Mother's legacy: Mitochondrial DNA mutations and Alzheimer's disease
    • Mattson M. P. (1997b) Mother's legacy: mitochondrial DNA mutations and Alzheimer's disease. Trends Neurosci. 20, 373-375.
    • (1997) Trends Neurosci. , vol.20 , pp. 373-375
    • Mattson, M.P.1
  • 63
    • 0031606827 scopus 로고    scopus 로고
    • Free radicals, calcium, and the synaptic plasticity-cell death continuum: Emerging roles of the transcription factor NF-κB
    • Mattson M. P. (1997c) Free radicals, calcium, and the synaptic plasticity-cell death continuum: emerging roles of the transcription factor NF-κB. Int. Rev. Neurobiol. 42, 103-168.
    • (1997) Int. Rev. Neurobiol. , vol.42 , pp. 103-168
    • Mattson, M.P.1
  • 64
    • 0029973120 scopus 로고    scopus 로고
    • Programmed cell life: Anti-apoptotic signaling and therapeutic strategies for neurodegenerative disorders
    • Mattson M. P. and Furukawa K. (1996) Programmed cell life: anti-apoptotic signaling and therapeutic strategies for neurodegenerative disorders. Restorative Neurol. Neurosci. 9, 191-205.
    • (1996) Restorative Neurol. Neurosci. , vol.9 , pp. 191-205
    • Mattson, M.P.1    Furukawa, K.2
  • 65
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M. P., Cheng B., Davis D., Bryant K., Lieberburg I., and Rydel R. E. (1992) β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12, 376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 66
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of β-amyloid precursor protein
    • Mattson M. P., Cheng B., Culwell A., Esch F., Lieberburg I., and Rydel R. E. (1993) Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of β-amyloid precursor protein. Neuron 10, 243-254.
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.3    Esch, F.4    Lieberburg, I.5    Rydel, R.E.6
  • 67
    • 0000131472 scopus 로고    scopus 로고
    • Calcium homeostasis and free radical metabolism as convergence points in the pathophysiology of dementia
    • (Wasco W. and Tanzi R. E., eds). Humana Press, Totowa, New Jersey
    • Mattson M. P., Furukawa K., Bruce A. J., Mark R. J., and Blanc E. M. (1996) Calcium homeostasis and free radical metabolism as convergence points in the pathophysiology of dementia, in Molecular Mechanisms of Dementia (Wasco W. and Tanzi R. E., eds). pp. 103-143. Humana Press, Totowa, New Jersey.
    • (1996) Molecular Mechanisms of Dementia , pp. 103-143
    • Mattson, M.P.1    Furukawa, K.2    Bruce, A.J.3    Mark, R.J.4    Blanc, E.M.5
  • 68
    • 0030612106 scopus 로고    scopus 로고
    • Oxidative disruption of ion homeostasis and cellular mechanisms of protection therefrom
    • Mattson M. P., Mark R. J., and Furukawa K. (1997a) Oxidative disruption of ion homeostasis and cellular mechanisms of protection therefrom. Chem. Res. Toxicol. 10, 507-517.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 507-517
    • Mattson, M.P.1    Mark, R.J.2    Furukawa, K.3
  • 69
    • 0030611750 scopus 로고    scopus 로고
    • Activation of NF-κB protects hippocampal neurons against oxidative stress-induced apoptosis: Evidence for induction of Mn-SOD and suppression of peroxynitrite production and protein tyrosine nitration
    • Mattson M. P., Goodman Y., Luo H., Fu W., and Furukawa K. (1997b) Activation of NF-κB protects hippocampal neurons against oxidative stress-induced apoptosis: evidence for induction of Mn-SOD 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
  • 70
    • 0030575338 scopus 로고    scopus 로고
    • Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: Evidence that Alzheimer mutations affect proteolytic processing
    • Mercken M., Takahashi H., Honda T., Sato K., Murayama M., Nakazato Y., Noguchi K., Imahori K., and Takashirna A. (1996) Characterization of human presenilin 1 using N-terminal specific monoclonal antibodies: evidence that Alzheimer mutations affect proteolytic processing. FEBS Lett. 389, 297-303.
    • (1996) FEBS Lett. , vol.389 , pp. 297-303
    • Mercken, M.1    Takahashi, H.2    Honda, T.3    Sato, K.4    Murayama, M.5    Nakazato, Y.6    Noguchi, K.7    Imahori, K.8    Takashirna, A.9
  • 74
    • 0030459831 scopus 로고    scopus 로고
    • In situ hybridization of presenilin 1 mRNA in Alzheimer's disease and lesioned rat brain
    • Page K., Hollister R., Tanzi R. E., and Hyman B. T. (1996) In situ hybridization of presenilin 1 mRNA in Alzheimer's disease and lesioned rat brain. Proc. Natl. Acad. Sci. USA 93, 14020-14024.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14020-14024
    • Page, K.1    Hollister, R.2    Tanzi, R.E.3    Hyman, B.T.4
  • 75
    • 0030963658 scopus 로고    scopus 로고
    • NGF-independent reduction in choline acetyltransferase activity in PC12 cells expressing mutant presenilin-1
    • Pedersen W., Guo Q., Hartman B. K., and Mattson M. P. (1997) NGF-independent reduction in choline acetyltransferase activity in PC12 cells expressing mutant presenilin-1. J. Biol. Chem. 272, 22397-22400.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22397-22400
    • Pedersen, W.1    Guo, Q.2    Hartman, B.K.3    Mattson, M.P.4
  • 77
    • 0028204224 scopus 로고
    • Calcium ionophore increases amyloid β peptide production by cultured cells
    • Querfurth H. W. and Selkoe D. J. (1994) Calcium ionophore increases amyloid β peptide production by cultured cells. Biochemistry 33, 4550-4561.
    • (1994) Biochemistry , vol.33 , pp. 4550-4561
    • Querfurth, H.W.1    Selkoe, D.J.2
  • 78
    • 0026316233 scopus 로고
    • The Alzheimer amyloid precursor is associated with the detergent-insoluble cytoskeleton
    • Refolo L. M., Wittenberg L. Friedrich J., and Robakis N. K. (1991) The Alzheimer amyloid precursor is associated with the detergent-insoluble cytoskeleton. J. Neurosci. 11, 3888-3897.
    • (1991) J. Neurosci. , vol.11 , pp. 3888-3897
    • Refolo, L.M.1    Wittenberg, L.2    Friedrich, J.3    Robakis, N.K.4
  • 81
    • 0029899593 scopus 로고    scopus 로고
    • Incomplete penetrance of familial Alzheimer's disease in a pedigree with a novel presenilin-1 gene mutation
    • Rossor M. N., Fox N. C., Beck J., Campbell T. C., and Collinge J. (1996) Incomplete penetrance of familial Alzheimer's disease in a pedigree with a novel presenilin-1 gene mutation. Lancet 347, 1560.
    • (1996) Lancet , vol.347 , pp. 1560
    • Rossor, M.N.1    Fox, N.C.2    Beck, J.3    Campbell, T.C.4    Collinge, J.5
  • 84
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe D. J. (1994) Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu. Rev. Cell Biol. 10, 373-403.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 87
    • 0028988649 scopus 로고
    • Intracellular routing of human amyloid protein precursor: Axonal delivery followed by transport to the dendrites
    • Simons M., Ikonen E., Tienari P. J., Cid-Arregui A., Monning U., Beyreuther K., and Dotti C. G. (1995) Intracellular routing of human amyloid protein precursor: axonal delivery followed by transport to the dendrites. J. Neurosci. Res. 41, 121-128.
    • (1995) J. Neurosci. Res. , vol.41 , pp. 121-128
    • Simons, M.1    Ikonen, E.2    Tienari, P.J.3    Cid-Arregui, A.4    Monning, U.5    Beyreuther, K.6    Dotti, C.G.7
  • 88
    • 0029120647 scopus 로고
    • Evidence for apoptotic cell death in Alzheimer's disease
    • Smale G., Nichols N. R., and Brady D. R. (1995) Evidence for apoptotic cell death in Alzheimer's disease. Exp. Neurol. 133, 225-230.
    • (1995) Exp. Neurol. , vol.133 , pp. 225-230
    • Smale, G.1    Nichols, N.R.2    Brady, D.R.3
  • 89
    • 0031023590 scopus 로고    scopus 로고
    • Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat
    • Spacek J. and Harris K. M. (1997) Three-dimensional organization of smooth endoplasmic reticulum in hippocampal CA1 dendrites and dendritic spines of the immature and mature rat. J. Neurosci. 17, 190-203.
    • (1997) J. Neurosci. , vol.17 , pp. 190-203
    • Spacek, J.1    Harris, K.M.2
  • 90
    • 0028131169 scopus 로고
    • Stress exacerbates neuron loss and cytoskeletal pathology in the hippocampus
    • Stein-Behrens B., Mattson M. P., Chang I., Yeh M., and Sapolsky R. M. (1994) Stress exacerbates neuron loss and cytoskeletal pathology in the hippocampus. J. Neurosci. 14, 5373-5380.
    • (1994) J. Neurosci. , vol.14 , pp. 5373-5380
    • Stein-Behrens, B.1    Mattson, M.P.2    Chang, I.3    Yeh, M.4    Sapolsky, R.M.5
  • 92
    • 0028577208 scopus 로고
    • Immunocytochemical evidence for apoptosis in Alzheimer's disease
    • Su J. H., Anderson A. J., Cummings B., and Cotman C. W. (1994) Immunocytochemical evidence for apoptosis in Alzheimer's disease. Neuroreport 5, 2529-2533.
    • (1994) Neuroreport , vol.5 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.3    Cotman, C.W.4
  • 94
  • 97
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C. B. (1995) Apoptosis in the pathogenesis and treatment of disease. Science 267, 1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 100
    • 0029671219 scopus 로고    scopus 로고
    • 2+-binding protein ALG-2 and Alzheimer's disease gene ALG-3
    • 2+-binding protein ALG-2 and Alzheimer's disease gene ALG-3. Science 271, 521-525.
    • (1996) Science , vol.271 , pp. 521-525
    • Vito, P.1    Lacan, E.2    D'Adamio, L.3
  • 101
    • 0029856850 scopus 로고    scopus 로고
    • Requirement of the familial Alzheimer's disease gene PS2 for apoptosis. Opposing effect of ALG-3
    • Vito P., Wolozin B., Ganjei J. K., Iwasaki K., Lacana E., and D'Adamio L. (1996b) Requirement of the familial Alzheimer's disease gene PS2 for apoptosis. Opposing effect of ALG-3. J. Biol. Chem. 271, 31025-31028.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31025-31028
    • Vito, P.1    Wolozin, B.2    Ganjei, J.K.3    Iwasaki, K.4    Lacana, E.5    D'Adamio, L.6
  • 103
    • 0031024228 scopus 로고    scopus 로고
    • Presenilin-1 immunoreactivity is localized intracellularly in Alzheimer's disease brain, but not detected in amyloid plaques
    • Weber L. L., Leissring M. A., Yang A. J., Glabe C. G., Cribbs D. H., and LaFerla F. M. (1997) Presenilin-1 immunoreactivity is localized intracellularly in Alzheimer's disease brain, but not detected in amyloid plaques. Exp. Neurol 143, 37-44.
    • (1997) Exp. Neurol , vol.143 , pp. 37-44
    • Weber, L.L.1    Leissring, M.A.2    Yang, A.J.3    Glabe, C.G.4    Cribbs, D.H.5    LaFerla, F.M.6
  • 104
    • 0031054505 scopus 로고    scopus 로고
    • Formation of stable complexes between two Alzheimer's disease gene products, presenilin-2 and β-amyloid precursor protein
    • Weidemann A., Paliga K., Durrwang U., Czech C., Evin G., Masters C. L., and Beyreuther K. (1997) Formation of stable complexes between two Alzheimer's disease gene products, presenilin-2 and β-amyloid precursor protein. Nat. Med. 3, 328-332.
    • (1997) Nat. Med. , vol.3 , pp. 328-332
    • Weidemann, A.1    Paliga, K.2    Durrwang, U.3    Czech, C.4    Evin, G.5    Masters, C.L.6    Beyreuther, K.7
  • 105
    • 0028844121 scopus 로고
    • Complementary and combinatorial pattern of Notch gene family expression during early mouse development
    • Williams R., Lendahl U., and Lardelli M. (1995) Complementary and combinatorial pattern of Notch gene family expression during early mouse development. Mech. Dev. 53, 357-368.
    • (1995) Mech. Dev. , vol.53 , pp. 357-368
    • Williams, R.1    Lendahl, U.2    Lardelli, M.3
  • 108
    • 0030753089 scopus 로고    scopus 로고
    • Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer's disease
    • 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's 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
  • 109
    • 0028945660 scopus 로고
    • Evidence that Aβ 42 is the real culprit in Alzheimer's disease
    • Younkin S. (1995) Evidence that Aβ 42 is the real culprit in Alzheimer's disease. Ann. Neurol. 37, 287-288.
    • (1995) Ann. Neurol. , vol.37 , pp. 287-288
    • Younkin, S.1
  • 110
    • 0030788767 scopus 로고    scopus 로고
    • Presenilin 1 interaction in the brain with a novel member of the armadillo family
    • Zhou J., Liyangage U., Medina M., Ho C., Simmons A. D., Lovett M., and Kosik K. S. (1997) Presenilin 1 interaction in the brain with a novel member of the armadillo family. Neuroreport 8, 1489-1494.
    • (1997) Neuroreport , vol.8 , pp. 1489-1494
    • Zhou, J.1    Liyangage, U.2    Medina, M.3    Ho, C.4    Simmons, A.D.5    Lovett, M.6    Kosik, K.S.7
  • 111
    • 0029760303 scopus 로고    scopus 로고
    • Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types
    • Zhu W., Cowie A., Wasfy G. W., Penn L. Z., Leber B., and Andrews D. W. (1996) Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types. EMBO J. 15, 4130-4141.
    • (1996) EMBO J. , vol.15 , pp. 4130-4141
    • Zhu, W.1    Cowie, A.2    Wasfy, G.W.3    Penn, L.Z.4    Leber, B.5    Andrews, D.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.