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Volumn 5, Issue 2, 1999, Pages 112-124

The presenilins

Author keywords

Amyloid peptide; Apoptosis; Excitotoxicity; Mitochondrial transmembrane potential; Muscarinic cholinergic; Reactive oxygen species

Indexed keywords

AMYLOID PRECURSOR PROTEIN; PRESENILIN 1; PRESENILIN 2;

EID: 0032964702     PISSN: 10738584     EISSN: None     Source Type: Journal    
DOI: 10.1177/107385849900500215     Document Type: Review
Times cited : (15)

References (61)
  • 1
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 1995;375:754-760.
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3    Rogaeva, E.A.4    Levesque, G.5    Ikeda, M.6
  • 3
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev EI, Sherrington R, Rogaeva EA, Levesque G, Ikeda M, Liang Y, et al. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 1995;376:775-778.
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3    Levesque, G.4    Ikeda, M.5    Liang, Y.6
  • 4
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci 1997;20:154-159.
    • (1997) Trends Neurosci , vol.20 , pp. 154-159
    • Hardy, J.1
  • 6
    • 8044231311 scopus 로고    scopus 로고
    • The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum
    • Walter J, Capell A, Grunberg J, Pesold B, Schindzielorz A, Prior R, et al. The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol Med 1996;2:673-691.
    • (1996) Mol Med , vol.2 , pp. 673-691
    • Walter, J.1    Capell, A.2    Grunberg, J.3    Pesold, B.4    Schindzielorz, A.5    Prior, R.6
  • 7
    • 15444341611 scopus 로고    scopus 로고
    • Phosphorylation, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins
    • De Strooper B, Beullens M, Contreras B, Levesque L, Craessaerts K, Cordell B, et al. Phosphorylation, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins. J Biol Chem 1997;272:3590-3598.
    • (1997) J Biol Chem , vol.272 , pp. 3590-3598
    • De Strooper, B.1    Beullens, M.2    Contreras, B.3    Levesque, L.4    Craessaerts, K.5    Cordell, B.6
  • 8
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran G, Borchelt DR, Lee MK, Slunt HH, Spitzer L, Kim G, et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 1996;17:181-190.
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3    Slunt, H.H.4    Spitzer, L.5    Kim, G.6
  • 9
    • 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 KH, Staufenbiel M, Yankner BA. Developmental regulation of presenilin-1 processing in the brain suggests a role in neuronal differentiation. J Biol Chem 1997;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
  • 10
    • 0029812077 scopus 로고    scopus 로고
    • Expression and analysis of presenilin 1 in a human neuronal system: Localization in cell bodies and dendrites
    • Cook DB, Sung JC, Golde TE, Felsenstein KM, Wojczyk BS, Tanzi RE, et al. Expression and analysis of presenilin 1 in a human neuronal system: localization in cell bodies and dendrites. Proc Natl Acad Sci U S A 1996;93:9223-9228.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 9223-9228
    • Cook, D.B.1    Sung, J.C.2    Golde, T.E.3    Felsenstein, K.M.4    Wojczyk, B.S.5    Tanzi, R.E.6
  • 11
    • 10144234151 scopus 로고    scopus 로고
    • Identification and neuron specific expression of the S182/presenilin 1 protein in human and rodent brains
    • Elder GA, Tezapsidis N, Carter J, Shioi J, Bouras C, Li HC, et al. Identification and neuron specific expression of the S182/presenilin 1 protein in human and rodent brains. J Neurosci Res 1996;45:308-320.
    • (1996) J Neurosci Res , vol.45 , pp. 308-320
    • Elder, G.A.1    Tezapsidis, N.2    Carter, J.3    Shioi, J.4    Bouras, C.5    Li, H.C.6
  • 12
    • 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 RE, Hyman BT. In situ hybridization of presenilin 1 mRNA in Alzheimer's disease and lesioned rat brain. Proc Natl Acad Sci U S A 1996;93:14020-14024.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 14020-14024
    • Page, K.1    Hollister, R.2    Tanzi, R.E.3    Hyman, B.T.4
  • 14
    • 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, et al. Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease. J Neurosci 1997;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
  • 15
    • 0031569390 scopus 로고    scopus 로고
    • Analysis of the 5′ sequence, genomic structure, and alternative splicing of the presenilin-1 gene associated with early onset Alzheimer's disease
    • Rogaev EI, Sherrington R, Wu C, Levesque G, Liang Y, Rogaeva EA, et al. Analysis of the 5′ sequence, genomic structure, and alternative splicing of the presenilin-1 gene associated with early onset Alzheimer's disease. Genomics 1997;40:415-424.
    • (1997) Genomics , vol.40 , pp. 415-424
    • Rogaev, E.I.1    Sherrington, R.2    Wu, C.3    Levesque, G.4    Liang, Y.5    Rogaeva, E.A.6
  • 16
    • 0029843172 scopus 로고    scopus 로고
    • Widespread immunoreactivity of presenilin in neurons of normal and Alzheimer's disease brains: Double-labeling immunohistochemical study
    • Uchihara T, el Hachimi HK, Duyckaerts C, Foncin JF, Fraser PE, Levesque L, et al. Widespread immunoreactivity of presenilin in neurons of normal and Alzheimer's disease brains: double-labeling immunohistochemical study. Acta Neuropathol 1996;92:325-330.
    • (1996) Acta Neuropathol , vol.92 , pp. 325-330
    • Uchihara, T.1    El Hachimi, H.K.2    Duyckaerts, C.3    Foncin, J.F.4    Fraser, P.E.5    Levesque, L.6
  • 17
  • 21
    • 0028989016 scopus 로고
    • Notch1 is required for the coordinate segmentation of somites
    • Conlon RA, Reaume AG, Rossant J. Notch1 is required for the coordinate segmentation of somites. Development 1995;121:1533-1545.
    • (1995) Development , vol.121 , pp. 1533-1545
    • Conlon, R.A.1    Reaume, A.G.2    Rossant, J.3
  • 23
    • 0033016172 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice
    • Guo Q, Fu W, Sopher BL, et al. Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice. Nat Med 1999;5:101-106.
    • (1999) Nat Med , vol.5 , pp. 101-106
    • Guo, Q.1    Fu, W.2    Sopher, B.L.3
  • 24
    • 0031054505 scopus 로고    scopus 로고
    • Formation of stable complexes between two Alzheimer's disease gene products, presenilin-2 and b-amyloid precursor protein
    • Weidemann A, Paliga K, Durrwang U, Czech C, Evin G, Masters CL, et al. Formation of stable complexes between two Alzheimer's disease gene products, presenilin-2 and b-amyloid precursor protein. Nature Med 1997;3:328-332.
    • (1997) Nature 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
  • 25
    • 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 EH, Selkoe DJ. Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer's disease. Proc Natl Acad Sci U S A 1997;94:8208-8213.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8208-8213
    • Xia, W.1    Zhang, J.2    Perez, R.3    Koo, E.H.4    Selkoe, D.J.5
  • 26
    • 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 AD, Lovett M, et al. Presenilin 1 interaction in the brain with a novel member of the Armadillo family. Neuroreport 1997;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
  • 27
    • 17344372115 scopus 로고    scopus 로고
    • Interaction of presenilins with the filamin family of actin-binding proteins
    • Zhang W, Han SW, McKeel DW, Goate A, Wu JY. Interaction of presenilins with the filamin family of actin-binding proteins. J Neurosci 1998;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
  • 28
    • 16044373524 scopus 로고    scopus 로고
    • The amyloid β protein deposited in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D, Eckman C, Jensen M, Song X, Citron M, Suzuki N, et al. The amyloid β protein deposited 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 1996;2:864-870.
    • (1996) Nature Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5    Suzuki, N.6
  • 29
    • 0031921466 scopus 로고    scopus 로고
    • Mutant genes in familial Alzheimer's disease and transgenic models
    • Price DL, Sisodia SS. Mutant genes in familial Alzheimer's disease and transgenic models. Annu Rev Neurosci 1998;21:479-505.
    • (1998) Annu Rev Neurosci , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.S.2
  • 30
    • 0030807917 scopus 로고    scopus 로고
    • The actin-severing protein gelsolin modulates calcium channel activity and vulnerability to excitotoxicity in hippocampal neurons
    • Furukawa K, Fu W, Witke W, Kwiatkowski DJ, Mattson MP. The actin-severing protein gelsolin modulates calcium channel activity and vulnerability to excitotoxicity in hippocampal neurons. J Neurosci 1997;17:8178-8186.
    • (1997) J Neurosci , vol.17 , pp. 8178-8186
    • Furukawa, K.1    Fu, W.2    Witke, W.3    Kwiatkowski, D.J.4    Mattson, M.P.5
  • 31
    • 0030891662 scopus 로고    scopus 로고
    • Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid b-peptide
    • Guo Q, Furukawa K, Sopher BL, Pham DG, Xie J, Robinson N, et al. Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid b-peptide. Neuroreport 1996;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
  • 32
    • 0032539814 scopus 로고    scopus 로고
    • Calbindin blocks the pro-apoptotic actions of mutant presenilin-1: Reduced oxidative stress and preserved mitochondrial function
    • Guo Q, Christakos S, Robinson N, Mattson MP. Calbindin blocks the pro-apoptotic actions of mutant presenilin-1: reduced oxidative stress and preserved mitochondrial function. Proc Natl Acad Sci USA 1998;95:3227-3232.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3227-3232
    • Guo, Q.1    Christakos, S.2    Robinson, N.3    Mattson, M.P.4
  • 33
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-b42(43) in brains of mice expressing mutant presenilin 1
    • Duff K, Eckman C, Zehr C, Yu X, Prada CM, Perez-Tur J, et al. Increased amyloid-b42(43) in brains of mice expressing mutant presenilin 1. Nature 1996;383:710-713.
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3    Yu, X.4    Prada, C.M.5    Perez-Tur, J.6
  • 34
    • 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 DR, Thinakaran G, Eckman CB, Lee MK, Davenport F, Ratovitsky T, et al. Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 1996;17:1005-1013.
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3    Lee, M.K.4    Davenport, F.5    Ratovitsky, T.6
  • 35
    • 0000131472 scopus 로고    scopus 로고
    • Calcium homeostasis and free radical metabolism as convergence points in the pathophysiology of dementia
    • Wasco W, Tanzi R, editors. Totowa (NJ): Humana Press
    • Mattson MP, Furukawa K, Bruce AJ, Mark RJ, Blanc EM. Calcium homeostasis and free radical metabolism as convergence points in the pathophysiology of dementia. In: Wasco W, Tanzi R, editors. Molecular mechanisms of dementia. Totowa (NJ): Humana Press; 1996. p. 103-143.
    • (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
  • 36
    • 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, Yankner BA. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J Biol Chem 1994;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
  • 37
    • 0028204224 scopus 로고
    • Calcium ionophore increases amyloid β peptide production by cultured cells
    • Querfurth HW, Selkoe DJ. Calcium ionophore increases amyloid β peptide production by cultured cells. Biochemistry 1994;33:4550-4561.
    • (1994) Biochemistry , vol.33 , pp. 4550-4561
    • Querfurth, H.W.1    Selkoe, D.J.2
  • 38
    • 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 Q, Sopher BL, Furukawa K, Pham DG, Robinson N, Martin GM, et al. 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 1997;17:4212-4222.
    • (1997) J Neurosci , vol.17 , pp. 4212-4222
    • Guo, Q.1    Sopher, B.L.2    Furukawa, K.3    Pham, D.G.4    Robinson, N.5    Martin, G.M.6
  • 39
    • 0345055313 scopus 로고    scopus 로고
    • Increased sensitivity to mitochondrial toxin-induced apoptosis in neural cells expressing mutant presenilin-1 is linked to perturbed calcium homeostasis and enhanced oxyradical production
    • Keller JN, Guo Q, Holtsberg FW, Bruce-Keller AJ, Mattson MP. Increased sensitivity to mitochondrial toxin-induced apoptosis in neural cells expressing mutant presenilin-1 is linked to perturbed calcium homeostasis and enhanced oxyradical production. J Neurosci 1998;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
  • 40
    • 0029841562 scopus 로고    scopus 로고
    • Increased activity-regulating and neuroprotective efficacy of α-secretase-derived secreted APP is conferred by a C-terminal heparin-binding domain
    • Furukawa K, Sopher B, Rydel RE, Begley JG, Martin GM, Mattson MP. Increased activity-regulating and neuroprotective efficacy of α-secretase-derived secreted APP is conferred by a C-terminal heparin-binding domain. J Neurochem 1996;67:1882-1896.
    • (1996) J Neurochem , vol.67 , pp. 1882-1896
    • Furukawa, K.1    Sopher, B.2    Rydel, R.E.3    Begley, J.G.4    Martin, G.M.5    Mattson, M.P.6
  • 41
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of β-amyloid precursor protein, and its soluble and fibrillogenic peptide derivatives
    • Mattson MP. Cellular actions of β-amyloid precursor protein, and its soluble and fibrillogenic peptide derivatives. Physiol Rev 1997;77:1081-1132.
    • (1997) Physiol Rev , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 42
    • 0032524319 scopus 로고    scopus 로고
    • Secreted APPα counteracts the pro-apoptotic action of mutant presenilin-1 by activation of NF-κB and stabilization of calcium homeostasis
    • Guo Q, Robinson N, Mattson MP. Secreted APPα counteracts the pro-apoptotic action of mutant presenilin-1 by activation of NF-κB and stabilization of calcium homeostasis. J Biol Chem 1998;273:12341-12351.
    • (1998) J Biol Chem , vol.273 , pp. 12341-12351
    • Guo, Q.1    Robinson, N.2    Mattson, M.P.3
  • 43
    • 0030611750 scopus 로고    scopus 로고
    • Activation of NF-kB protects hippocampal neurons against oxidative stress-induced apoptosis: Evidence for induction of Mn-SOD and suppression of peroxynitrite production and protein tyrosine nitration
    • Mattson MP, Goodman Y, Luo H, Fu W, Furukawa K. Activation of NF-kB 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 1997;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
  • 44
    • 0030667339 scopus 로고    scopus 로고
    • Checler F. a-secretase-derived product of β-amyloid precursor protein is dereased by presenilin-1 mutations linked to familial Alzheimer's disease
    • Ancolio K, Marambaud P, Dauch P, Checler F. a-secretase-derived product of β-amyloid precursor protein is dereased by presenilin-1 mutations linked to familial Alzheimer's disease. J Neurochem 1997;69:2494-2499.
    • (1997) J Neurochem , vol.69 , pp. 2494-2499
    • Ancolio, K.1    Marambaud, P.2    Dauch, P.3
  • 45
    • 0029912056 scopus 로고    scopus 로고
    • Mechanisms of neuronal death in Alzheimer's disease
    • Cotman CW, Su JH. Mechanisms of neuronal death in Alzheimer's disease. Brain Pathol. 1996;6:493-506.
    • (1996) Brain Pathol. , vol.6 , pp. 493-506
    • Cotman, C.W.1    Su, J.H.2
  • 46
    • 0030580281 scopus 로고    scopus 로고
    • Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells
    • Deng G, Pike CJ, Cotman CW. Alzheimer-associated presenilin-2 confers increased sensitivity to apoptosis in PC12 cells. FEBS Lett 1996;397:50-54.
    • (1996) FEBS Lett , vol.397 , pp. 50-54
    • Deng, G.1    Pike, C.J.2    Cotman, C.W.3
  • 47
    • 10544224542 scopus 로고    scopus 로고
    • Participation of presenilin 2 in apoptosis: Enhanced basal activity conferred by an Alzheimer mutation
    • Wolozin B, Iwasaki K, Vito P, Ganjei JK, Lacana E, Sunderland T, et al. Participation of presenilin 2 in apoptosis: enhanced basal activity conferred by an Alzheimer mutation. Science 1996;274:1710-1713.
    • (1996) Science , vol.274 , pp. 1710-1713
    • Wolozin, B.1    Iwasaki, K.2    Vito, P.3    Ganjei, J.K.4    Lacana, E.5    Sunderland, T.6
  • 48
    • 0031465727 scopus 로고    scopus 로고
    • Estrogens stabilize mitochondrial function and protect neural cells against the pro-apoptotic action of mutant presenilin-1
    • Mattson MP, Robinson N, Guo Q. Estrogens stabilize mitochondrial function and protect neural cells against the pro-apoptotic action of mutant presenilin-1. Neuroreport 1997;8:3817-3821.
    • (1997) Neuroreport , vol.8 , pp. 3817-3821
    • Mattson, M.P.1    Robinson, N.2    Guo, Q.3
  • 49
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim T-W, Pettingell WH, Jung Y-K, Kovacs DM, Tanzi RE. Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 1997;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
  • 51
    • 0031927628 scopus 로고    scopus 로고
    • Par-4 is a novel mediator of neuronal degeneration associated with the pathogenesis of Alzheimer's disease
    • Guo Q, Fu W, Xie J, Luo H, Sells SF, Geddes JW, et al. Par-4 is a novel mediator of neuronal degeneration associated with the pathogenesis of Alzheimer's disease. Nat Med 1998;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.W.6
  • 53
    • 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, et al. Alteration of acylphosphatase levels in familial Alzheimer's disease fibroblasts with presenilin gene mutations. Neurosci Lett 1996;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
  • 54
    • 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 LS, Ostvold AC, Cowburn RF, Garlind A, Winblad B, Bogdanovich N, et al. Decreased inositol (1,4,5)-trisphosphate receptor levels in Alzheimer's disease cerebral cortex: selectivity of changes and possible correlation to pathological severity. Neurodegeneration 1996;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
  • 55
    • 0030797336 scopus 로고    scopus 로고
    • 4-hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau
    • Mattson MP, Fu W, Waeg G, Uchida K. 4-hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau. NeuroReport 1997;8:2275-2281.
    • (1997) NeuroReport , vol.8 , pp. 2275-2281
    • Mattson, M.P.1    Fu, W.2    Waeg, G.3    Uchida, K.4
  • 57
    • 77956860189 scopus 로고    scopus 로고
    • Mitochondrial alterations in brain aging
    • Mattson MP, Geddes JW, editors. Greenwich (CT): JAI Press
    • Benzi G, Moretti A. Mitochondrial alterations in brain aging. In: Mattson MP, Geddes JW, editors. Advances in cell aging and gerontology. Vol. 2. The aging brain. Greenwich (CT): JAI Press; 1997. p. 129-160.
    • (1997) Advances in Cell Aging and Gerontology. Vol. 2. the Aging Brain , vol.2 , pp. 129-160
    • Benzi, G.1    Moretti, A.2
  • 58
    • 0030758647 scopus 로고    scopus 로고
    • Mother's legacy: Mitochondrial DNA mutations and Alzheimer's disease
    • Mattson MP. Mother's legacy: mitochondrial DNA mutations and Alzheimer's disease. Trends Neurosci 1997;20:373-375.
    • (1997) Trends Neurosci , vol.20 , pp. 373-375
    • Mattson, M.P.1
  • 59
    • 0345590985 scopus 로고    scopus 로고
    • Changes in neurotransmitter signal transduction pathways in the aging brain
    • Mattson MP, Geddes JW, editors. Greenwich (CT): JAI Press
    • Kelly JF, Roth GS. Changes in neurotransmitter signal transduction pathways in the aging brain. In: Mattson MP, Geddes JW, editors. Advances in cell aging and gerontology. Vol. 2. The aging brain. Greenwich (CT): JAI Press; 1997. p. 243-278.
    • (1997) Advances in Cell Aging and Gerontology. Vol. 2. the Aging Brain , vol.2 , pp. 243-278
    • Kelly, J.F.1    Roth, G.S.2
  • 60
    • 0030963658 scopus 로고    scopus 로고
    • NGF-independent reduction in choline acetyltransferase activity in PC12 cells expressing mutant presenilin-1
    • Pedersen WA, Guo Q, Hartman BK, Mattson MP. NGF-independent reduction in choline acetyltransferase activity in PC12 cells expressing mutant presenilin-1. J Biol Chem 1997;272:22397-22400.
    • (1997) J Biol Chem , vol.272 , pp. 22397-22400
    • Pedersen, W.A.1    Guo, Q.2    Hartman, B.K.3    Mattson, M.P.4
  • 61
    • 0032100541 scopus 로고    scopus 로고
    • Presenilin-1 mutation alters NGF-induced neurite outgrowth, calcium homeostasis, and transcription factor (AP-1) activation in PC12 cells
    • Furukawa K, Guo Q, Schellenberg GD, Mattson MP. Presenilin-1 mutation alters NGF-induced neurite outgrowth, calcium homeostasis, and transcription factor (AP-1) activation in PC12 cells. J Neurosci Res 1998;52:618-624.
    • (1998) J Neurosci Res , vol.52 , pp. 618-624
    • Furukawa, K.1    Guo, Q.2    Schellenberg, G.D.3    Mattson, M.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.