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Volumn 43, Issue 1, 2003, Pages 1-16

Amyloid-β: A chameleon walking in two worlds: A review of the trophic and toxic properties of amyloid-β

Author keywords

Acute phase response; Alzheimer's disease; Antioxidant; A ; A PP expression; Chelation; Copper; Head trauma; Injury; Iron; Metal ions; Neurotoxic; Neurotrophic; Oxidation; Oxidative stress; Reactive oxygen species; Zinc

Indexed keywords

AMYLOID BETA PROTEIN; ANTIINFLAMMATORY AGENT; CHELATING AGENT; COPPER; HYDROGEN PEROXIDE; IRON; METAL ION; OXYGEN; TOXIC SUBSTANCE;

EID: 0141853765     PISSN: 01650173     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-0173(03)00174-7     Document Type: Review
Times cited : (281)

References (191)
  • 1
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G.G., Wong C.W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120:1984;885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 3
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner G.G., Wong C.W. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122:1984;1131-1135.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 4
    • 0025840201 scopus 로고
    • BetaA4 amyloid protein deposition in brain after head trauma
    • Roberts G.W., Gentleman S.M., Lynch A., Graham D.I. BetaA4 amyloid protein deposition in brain after head trauma. Lancet. 338:1991;1422-1423.
    • (1991) Lancet , vol.338 , pp. 1422-1423
    • Roberts, G.W.1    Gentleman, S.M.2    Lynch, A.3    Graham, D.I.4
  • 5
    • 0023737806 scopus 로고
    • A4 amyloid protein deposition and the diagnosis of Alzheimer's disease: Prevalence in aged brains determined by immunocytochemistry compared with conventional neuropathologic techniques
    • Davies L., Wolska B., Hilbich C., Multhaup G., Martins R., Simms G., Beyreuther K., Masters C.L. A4 amyloid protein deposition and the diagnosis of Alzheimer's disease: prevalence in aged brains determined by immunocytochemistry compared with conventional neuropathologic techniques. Neurology. 38:1988;1688-1693.
    • (1988) Neurology , vol.38 , pp. 1688-1693
    • Davies, L.1    Wolska, B.2    Hilbich, C.3    Multhaup, G.4    Martins, R.5    Simms, G.6    Beyreuther, K.7    Masters, C.L.8
  • 6
    • 0027250352 scopus 로고
    • Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments
    • Siman R., Mistretta S., Durkin J.T., Savage M.J., Loh T., Trusko S., Scott R.W. Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments. J. Biol. Chem. 268:1993;16602-16609.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16602-16609
    • Siman, R.1    Mistretta, S.2    Durkin, J.T.3    Savage, M.J.4    Loh, T.5    Trusko, S.6    Scott, R.W.7
  • 7
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D., Lerman M.I., McBride O.W., Saffiotti U., Gajdusek D.C. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science. 235:1987;877-880.
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 15
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • Wolfe M.S., Xia W., Ostaszewski B.L., Diehl T.S., Kimberly W.T., Selkoe D.J. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature. 398:1999;513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 19
    • 0033751421 scopus 로고    scopus 로고
    • Metabolic, metallic, and mitotic sources of oxidative stress in Alzheimer disease
    • Smith M.A., Nunomura A., Zhu X., Takeda A., Perry G. Metabolic, metallic, and mitotic sources of oxidative stress in Alzheimer disease. Antioxid. Redox Signal. 2:2000;413-420.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 413-420
    • Smith, M.A.1    Nunomura, A.2    Zhu, X.3    Takeda, A.4    Perry, G.5
  • 22
    • 0033957486 scopus 로고    scopus 로고
    • Mercury induces cell cytotoxicity and oxidative stress and increases beta-amyloid secretion and tau phosphorylation in SHSY5Y neuroblastoma cells
    • Olivieri G., Brack C., Muller-Spahn F., Stahelin H.B., Herrmann M., Renard P., Brockhaus M., Hock C. Mercury induces cell cytotoxicity and oxidative stress and increases beta-amyloid secretion and tau phosphorylation in SHSY5Y neuroblastoma cells. J. Neurochem. 74:2000;231-236.
    • (2000) J. Neurochem. , vol.74 , pp. 231-236
    • Olivieri, G.1    Brack, C.2    Muller-Spahn, F.3    Stahelin, H.B.4    Herrmann, M.5    Renard, P.6    Brockhaus, M.7    Hock, C.8
  • 23
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith M.A., Harris P.L.R., Sayre L.M., Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc. Natl. Acad. Sci. USA. 94:1997;9866-9868.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.R.2    Sayre, L.M.3    Perry, G.4
  • 25
    • 0032613038 scopus 로고    scopus 로고
    • The role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Interrelations between free radicals and metal ions in life processes
    • A. Sigel, & H. Sigel. New York, Basel, Hong Kong: Marcel Dekker
    • Atwood C.S., Huang X., Moir R.D., Tanzi R.E., Bush A.I. The role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Interrelations between free radicals and metal ions in life processes. Sigel A., Sigel H. Metal Ions in Biological Systems. Vol. 36:1999;309-364 Marcel Dekker, New York, Basel, Hong Kong.
    • (1999) Metal Ions in Biological Systems , vol.36 , pp. 309-364
    • Atwood, C.S.1    Huang, X.2    Moir, R.D.3    Tanzi, R.E.4    Bush, A.I.5
  • 26
    • 0026041595 scopus 로고
    • Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease
    • Review
    • Basun H., Forssell L.G., Wetterberg L., Winblad B. Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease. J. Neural Transm. Park. Dis. Dement. Sect. 3:(4):1991;231-258. Review.
    • (1991) J. Neural Transm. Park. Dis. Dement. Sect. , vol.3 , Issue.4 , pp. 231-258
    • Basun, H.1    Forssell, L.G.2    Wetterberg, L.3    Winblad, B.4
  • 28
    • 0033006576 scopus 로고    scopus 로고
    • Is increased redox-active iron in Alzheimer disease a failure of the copper-binding protein ceruloplasmin?
    • Castellani R.J., Smith M.A., Nunomura A., Harris P.L., Perry G. Is increased redox-active iron in Alzheimer disease a failure of the copper-binding protein ceruloplasmin? Free Radic. Biol. Med. 26:1999;1508-1512.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 1508-1512
    • Castellani, R.J.1    Smith, M.A.2    Nunomura, A.3    Harris, P.L.4    Perry, G.5
  • 30
    • 0031038634 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and calcium perturbation induced by traumatic brain injury
    • Xiong Y., Gu Q., Peterson P.L., Muizelaar J.P., Lee C.P. Mitochondrial dysfunction and calcium perturbation induced by traumatic brain injury. J. Neurotrauma. 14:1997;23-34.
    • (1997) J. Neurotrauma , vol.14 , pp. 23-34
    • Xiong, Y.1    Gu, Q.2    Peterson, P.L.3    Muizelaar, J.P.4    Lee, C.P.5
  • 31
    • 0025845529 scopus 로고
    • Induction of amyloid precursor protein mRNA after heat shock in cultured human lymphoblastoid cells
    • Abe K., St. George-Hyslop P.H., Tanzi R.E., Kogure K. Induction of amyloid precursor protein mRNA after heat shock in cultured human lymphoblastoid cells. Neurosci. Lett. 125:1991;169-171.
    • (1991) Neurosci. Lett. , vol.125 , pp. 169-171
    • Abe, K.1    St. George-Hyslop, P.H.2    Tanzi, R.E.3    Kogure, K.4
  • 32
    • 0028802605 scopus 로고
    • Increased amyloid protein precursor and apolipoprotein E immunoreactivity in the selectively vulnerable hippocampus following transient forebrain ischemia in gerbils
    • Hall E.D., Oostveen J.A., Dunn E., Carter D.B. Increased amyloid protein precursor and apolipoprotein E immunoreactivity in the selectively vulnerable hippocampus following transient forebrain ischemia in gerbils. Exp. Neurol. 135:1995;17-27.
    • (1995) Exp. Neurol. , vol.135 , pp. 17-27
    • Hall, E.D.1    Oostveen, J.A.2    Dunn, E.3    Carter, D.B.4
  • 34
    • 0031770501 scopus 로고    scopus 로고
    • Experimental brain injury induces expression of amyloid precursor protein, which may be related to neuronal loss in the hippocampus
    • Murakami N., Yamaki T., Iwamoto Y., Sakakibara T., Kobori N., Fushiki S., Ueda S. Experimental brain injury induces expression of amyloid precursor protein, which may be related to neuronal loss in the hippocampus. J. Neurotrauma. 15:1998;993-1003.
    • (1998) J. Neurotrauma , vol.15 , pp. 993-1003
    • Murakami, N.1    Yamaki, T.2    Iwamoto, Y.3    Sakakibara, T.4    Kobori, N.5    Fushiki, S.6    Ueda, S.7
  • 35
    • 0030727701 scopus 로고    scopus 로고
    • Hypoglycemia enhances the expression of mRNA encoding beta-amyloid precursor protein in rat primary cortical astroglial cells
    • Shi J., Xiang Y., Simpkins J.W. Hypoglycemia enhances the expression of mRNA encoding beta-amyloid precursor protein in rat primary cortical astroglial cells. Brain Res. 772:1997;247-251.
    • (1997) Brain Res. , vol.772 , pp. 247-251
    • Shi, J.1    Xiang, Y.2    Simpkins, J.W.3
  • 36
    • 0032501198 scopus 로고    scopus 로고
    • Estrogen attenuates over-expression of beta-amyloid precursor protein messenger RNA in an animal model of focal ischemia
    • Shi J., Panickar K.S., Yang S.H., Rabbani O., Day A.L., Simpkins J.W. Estrogen attenuates over-expression of beta-amyloid precursor protein messenger RNA in an animal model of focal ischemia. Brain Res. 810:1998;87-92.
    • (1998) Brain Res. , vol.810 , pp. 87-92
    • Shi, J.1    Panickar, K.S.2    Yang, S.H.3    Rabbani, O.4    Day, A.L.5    Simpkins, J.W.6
  • 37
    • 0034603414 scopus 로고    scopus 로고
    • Vascular abnormalities: The insidious pathogenesis of Alzheimer's disease
    • Shi J., Perry G., Smith M.A., Friedland R.P. Vascular abnormalities: the insidious pathogenesis of Alzheimer's disease. Neurobiol. Aging. 21:2000;357-361.
    • (2000) Neurobiol. Aging , vol.21 , pp. 357-361
    • Shi, J.1    Perry, G.2    Smith, M.A.3    Friedland, R.P.4
  • 38
    • 0029907514 scopus 로고    scopus 로고
    • Cytotoxic fragment of amyloid precursor protein accumulates in hippocampus after global forebrain ischemia
    • Yokota M., Saido T.C., Tani E., Yamaura I., Minami N. Cytotoxic fragment of amyloid precursor protein accumulates in hippocampus after global forebrain ischemia. J. Cereb. Blood Flow Metab. 16:1996;1219-1223.
    • (1996) J. Cereb. Blood Flow Metab. , vol.16 , pp. 1219-1223
    • Yokota, M.1    Saido, T.C.2    Tani, E.3    Yamaura, I.4    Minami, N.5
  • 39
    • 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.B., Matsudaira P., Yankner B.A. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J. Biol. Chem. 269:1994;13623-13628.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13623-13628
    • Gabuzda, D.1    Busciglio, J.2    Chen, L.B.3    Matsudaira, P.4    Yankner, B.A.5
  • 40
    • 0032454039 scopus 로고    scopus 로고
    • Effects of amyloid precursor protein derivatives and oxidative stress on basal forebrain cholinergic systems in Alzheimer's disease
    • Mattson M.P., Pedersen W.A. Effects of amyloid precursor protein derivatives and oxidative stress on basal forebrain cholinergic systems in Alzheimer's disease. Int. J. Dev. Neurosci. 16:1998;737-753.
    • (1998) Int. J. Dev. Neurosci. , vol.16 , pp. 737-753
    • Mattson, M.P.1    Pedersen, W.A.2
  • 41
    • 0029985732 scopus 로고    scopus 로고
    • Oxidative stress increases production of β-amyloid precursor protein and β-amyloid (Aβ) in mammalian lenses, and Aβ has toxic effects on lens epithelial cells
    • Frederiske P.H., Garland D., Zigler J.S. Jr., Piatigorsky J. Oxidative stress increases production of β-amyloid precursor protein and β-amyloid (Aβ) in mammalian lenses, and Aβ has toxic effects on lens epithelial cells. J. Biol. Chem. 271:1996;10169-10174.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10169-10174
    • Frederiske, P.H.1    Garland, D.2    Zigler J.S., Jr.3    Piatigorsky, J.4
  • 42
    • 0034643895 scopus 로고    scopus 로고
    • Oxidative stress induces intracellular accumulation of amyloid beta-protein (Abeta) in human neuroblastoma cells
    • Misonou H., Morishima-Kawashima M., Ihara Y. Oxidative stress induces intracellular accumulation of amyloid beta-protein (Abeta) in human neuroblastoma cells. Biochemistry. 39:2000;6951-6959.
    • (2000) Biochemistry , vol.39 , pp. 6951-6959
    • Misonou, H.1    Morishima-Kawashima, M.2    Ihara, Y.3
  • 43
    • 0034754471 scopus 로고    scopus 로고
    • Melatonin protects SHSY5Y neuroblastoma cells from cobalt-induced oxidative stress, neurotoxicity and increased beta-amyloid secretion
    • Olivieri G., Hess C., Savaskan E., Ly C., Meier F., Baysang G., Brockhaus M., Muller-Spahn F. Melatonin protects SHSY5Y neuroblastoma cells from cobalt-induced oxidative stress, neurotoxicity and increased beta-amyloid secretion. J. Pineal Res. 31:2001;320-325.
    • (2001) J. Pineal Res. , vol.31 , pp. 320-325
    • Olivieri, G.1    Hess, C.2    Savaskan, E.3    Ly, C.4    Meier, F.5    Baysang, G.6    Brockhaus, M.7    Muller-Spahn, F.8
  • 44
    • 0031587950 scopus 로고    scopus 로고
    • Processing of Alzheimer's amyloid precursor protein during H2O2-induced apoptosis in human neuronal cells
    • Zhang L., Zhao B., Yew D.T., Kusiak J.W., Roth G.S. Processing of Alzheimer's amyloid precursor protein during H2O2-induced apoptosis in human neuronal cells. Biochem. Biophys. Res. Commun. 235:1997;845-848.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 845-848
    • Zhang, L.1    Zhao, B.2    Yew, D.T.3    Kusiak, J.W.4    Roth, G.S.5
  • 46
    • 0029076397 scopus 로고
    • Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide
    • Yan S.D., Yan S.F., Chen X., Fu J., Chen M., Kuppusamy P., Smith M.A., Perry G., Godman G.C., Nawroth P., et al. Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide. Nat. Med. 1:1995;693-699.
    • (1995) Nat. Med. , vol.1 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3    Fu, J.4    Chen, M.5    Kuppusamy, P.6    Smith, M.A.7    Perry, G.8    Godman, G.C.9    Nawroth, P.10
  • 47
    • 0005342374 scopus 로고    scopus 로고
    • Antioxidants mimic the ability of chorionic gonadotropin to suppress apoptosis in the rabbit corpus luteum in vitro: A novel role for superoxide dismutase in regulating bax expression
    • Dharmarajan A.M., Hisheh S., Singh B., Parkinson S., Tilly K.I., Tilly J.L. Antioxidants mimic the ability of chorionic gonadotropin to suppress apoptosis in the rabbit corpus luteum in vitro: a novel role for superoxide dismutase in regulating bax expression. Endocrinol. J. 2:1999;295-303.
    • (1999) Endocrinol. J. , vol.2 , pp. 295-303
    • Dharmarajan, A.M.1    Hisheh, S.2    Singh, B.3    Parkinson, S.4    Tilly, K.I.5    Tilly, J.L.6
  • 48
    • 0026674020 scopus 로고
    • Superoxide dismutase activity, lipid peroxide production and corpus luteum steroidogenesis during natural luteolysis and regression induced by oestradiol deprivation of the ovary in pseudopregnant rabbits
    • Hesla J.S., Miyazaki T., Dasko L.M., Wallach E.E., Dharmarajan A.M. Superoxide dismutase activity, lipid peroxide production and corpus luteum steroidogenesis during natural luteolysis and regression induced by oestradiol deprivation of the ovary in pseudopregnant rabbits. J. Reprod. Fertil. 95:1992;915-924.
    • (1992) J. Reprod. Fertil. , vol.95 , pp. 915-924
    • Hesla, J.S.1    Miyazaki, T.2    Dasko, L.M.3    Wallach, E.E.4    Dharmarajan, A.M.5
  • 49
    • 0029609021 scopus 로고
    • Related articles increased production of 4 kDa amyloid beta peptide in serum deprived human primary neuron cultures: Possible involvement of apoptosis
    • LeBlanc A. Related articles increased production of 4 kDa amyloid beta peptide in serum deprived human primary neuron cultures: possible involvement of apoptosis. J. Neurosci. 15:1995;7837-7846.
    • (1995) J. Neurosci. , vol.15 , pp. 7837-7846
    • LeBlanc, A.1
  • 50
    • 0034720686 scopus 로고    scopus 로고
    • Ovariectomy and 17beta-estradiol modulate the levels of Alzheimer's amyloid beta peptides in brain
    • Petanceska S.S., Nagy V., Frail D., Gandy S. Ovariectomy and 17beta-estradiol modulate the levels of Alzheimer's amyloid beta peptides in brain. Neurology. 54:(12):2000;2212-2217.
    • (2000) Neurology , vol.54 , Issue.12 , pp. 2212-2217
    • Petanceska, S.S.1    Nagy, V.2    Frail, D.3    Gandy, S.4
  • 52
    • 0026663993 scopus 로고
    • The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth
    • Milward E.A., Papadopoulos R., Fuller S.J., Moir R.D. R.D., Small D., Beyreuther K., Masters C.L. The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth. Neuron. 9:1992;129-137.
    • (1992) Neuron , vol.9 , pp. 129-137
    • Milward, E.A.1    Papadopoulos, R.2    Fuller, S.J.3    Moir, R.D.R.D.4    Small, D.5    Beyreuther, K.6    Masters, C.L.7
  • 53
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP
    • Kamal A., Almenar-Queralt A., LeBlanc J.F., Roberts E.A., Goldstein L.S. Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature. 414:2001;643-648.
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    LeBlanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 56
    • 0034502428 scopus 로고    scopus 로고
    • Arson: Tracking the culprit in Alzheimer's disease
    • Smith M.A., Joseph J.A., Perry G. Arson: tracking the culprit in Alzheimer's disease. Ann. N. Y. Acad. Sci. 924:2000;35-38.
    • (2000) Ann. N. Y. Acad. Sci. , vol.924 , pp. 35-38
    • Smith, M.A.1    Joseph, J.A.2    Perry, G.3
  • 59
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood C.S., Huang X., Moir R.D., Bacarra N.M., Romano D., Tanzi R.E., Bush A.I. Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273:1998;12817-12826.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12817-12826
    • Atwood, C.S.1    Huang, X.2    Moir, R.D.3    Bacarra, N.M.4    Romano, D.5    Tanzi, R.E.6    Bush, A.I.7
  • 60
    • 0035209719 scopus 로고    scopus 로고
    • Resistance of human cerebrospinal fluid to in vitro oxidation is directly related to its amyloid-beta content
    • Kontush A., Donarski N., Beisiegel U. Resistance of human cerebrospinal fluid to in vitro oxidation is directly related to its amyloid-beta content. Free Radic. Res. 35:2001;507-517.
    • (2001) Free Radic. Res. , vol.35 , pp. 507-517
    • Kontush, A.1    Donarski, N.2    Beisiegel, U.3
  • 61
    • 0027482350 scopus 로고
    • Beta-amyloid precursor protein (beta APP) as a marker for axonal injury after head injury
    • Gentleman S.M., Nash M.J., Sweeting C.J., Graham D.I., Roberts G.W. Beta-amyloid precursor protein (beta APP) as a marker for axonal injury after head injury. Neurosci. Lett. 160:1993;139-144.
    • (1993) Neurosci. Lett. , vol.160 , pp. 139-144
    • Gentleman, S.M.1    Nash, M.J.2    Sweeting, C.J.3    Graham, D.I.4    Roberts, G.W.5
  • 62
    • 0027278450 scopus 로고
    • Molecular pathology of head trauma: Altered beta APP metabolism and the aetiology of Alzheimer's disease
    • Gentleman S.M., Graham D.I., Roberts G.W. Molecular pathology of head trauma: altered beta APP metabolism and the aetiology of Alzheimer's disease. Prog. Brain Res. 96:1993;237-246.
    • (1993) Prog. Brain Res. , vol.96 , pp. 237-246
    • Gentleman, S.M.1    Graham, D.I.2    Roberts, G.W.3
  • 67
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta1-42
    • Atwood C.S., Scarpa R.C., Huang X., Moir R.D., Jones W.D., Fairlie D.P., Tanzi R.E., Bush A.I. Characterization of copper interactions with Alzheimer amyloid beta peptides: identification of an attomolar-affinity copper binding site on amyloid beta1-42. J. Neurochem. 75:2000;1219-1233.
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 68
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes
    • Miura T., Suzuki K., Kohata N., Takeuchi H. Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes. Biochemistry. 39:2000;7024-7031.
    • (2000) Biochemistry , vol.39 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 69
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain C.C., Ali F., Volitakis I., Cherny R.A., Norton R.S., Beyreuther K., Barrow C.J., Masters C.L., Bush A.I., Barnham K.J. Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276:2001;20466-20473.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 72
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • Dong J., Atwood C.S., Anderson V.E., Siedlak S.L., Perry G., Smith M.A., Carey P.R. Metal binding and oxidation of amyloid-β within isolated senile plaque cores: raman microscopic evidence. Biochemistry. 42:2003;2768-2773.
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Perry, G.5    Smith, M.A.6    Carey, P.R.7
  • 73
    • 0028180196 scopus 로고
    • Modulation of A beta adhesiveness and secretase site cleavage by zinc
    • Bush A.I., Pettingell W.H. Jr., Paradis M.D., Tanzi R.E. Modulation of A beta adhesiveness and secretase site cleavage by zinc. J. Biol. Chem. 269:1994;12152-12158.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12152-12158
    • Bush, A.I.1    Pettingell W.H., Jr.2    Paradis, M.D.3    Tanzi, R.E.4
  • 77
    • 0025853543 scopus 로고
    • Conservation of the sequence of the Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis
    • Johnstone E.M., Chaney M.O., Norris F.H., Pascual R., Little S.P. Conservation of the sequence of the Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis. Brain Res. Mol. Brain Res. 10:1991;299-305.
    • (1991) Brain Res. Mol. Brain Res. , vol.10 , pp. 299-305
    • Johnstone, E.M.1    Chaney, M.O.2    Norris, F.H.3    Pascual, R.4    Little, S.P.5
  • 78
    • 0033587478 scopus 로고    scopus 로고
    • Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease
    • Liu S.T., Howlett G., Barrow C.J. Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease. Biochemistry. 38:1999;9373-9378.
    • (1999) Biochemistry , vol.38 , pp. 9373-9378
    • Liu, S.T.1    Howlett, G.2    Barrow, C.J.3
  • 79
    • 0027407570 scopus 로고
    • Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • Busciglio J., Gabuzda D.H., Matsudaira P., Yankner B.A. Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. USA. 90:1993;2092-2096.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 81
    • 0021253173 scopus 로고
    • Evidence that copper-amino acid complexes are potent stimulators of the release of luteinizing hormone-releasing hormone from isolated hypothalamic granules
    • Barnea A., Cho G. Evidence that copper-amino acid complexes are potent stimulators of the release of luteinizing hormone-releasing hormone from isolated hypothalamic granules. Endocrinology. 115:1984;936-943.
    • (1984) Endocrinology , vol.115 , pp. 936-943
    • Barnea, A.1    Cho, G.2
  • 82
    • 0021287299 scopus 로고
    • Release of endogenous Zn2+ from brain tissue during activity
    • Assaf S.Y., Chung S.H. Release of endogenous Zn2+ from brain tissue during activity. Nature. 308:1984;734-736.
    • (1984) Nature , vol.308 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 83
    • 0021220724 scopus 로고
    • Stimulation-induced uptake and release of zinc in hippocampal slices
    • Howell G.A., Welch M.G., Frederickson C.J. Stimulation-induced uptake and release of zinc in hippocampal slices. Nature. 308:1984;736-738.
    • (1984) Nature , vol.308 , pp. 736-738
    • Howell, G.A.1    Welch, M.G.2    Frederickson, C.J.3
  • 84
    • 0033515564 scopus 로고    scopus 로고
    • Amyloid beta peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalyzed oxidation of hydroxylamines to nitroxides
    • Dikalov S.I., Vitek M.P., Maples K.R., Mason R.P. Amyloid beta peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalyzed oxidation of hydroxylamines to nitroxides. J. Biol. Chem. 274:1999;9392-9399.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9392-9399
    • Dikalov, S.I.1    Vitek, M.P.2    Maples, K.R.3    Mason, R.P.4
  • 87
    • 0036598956 scopus 로고    scopus 로고
    • Amyloid peptide enhances nail rusting: Novel insight into mechanisms of aging and Alzheimer's disease
    • Mattson M.P., Mattson E.P. Amyloid peptide enhances nail rusting: novel insight into mechanisms of aging and Alzheimer's disease. Ageing Res. Rev. 1:2002;327-330.
    • (2002) Ageing Res. Rev. , vol.1 , pp. 327-330
    • Mattson, M.P.1    Mattson, E.P.2
  • 89
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity
    • Review
    • Varadarajan S., Yatin S., Aksenova M., Butterfield D.A. Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J. Struct. Biol. 130:2000;184-208. Review.
    • (2000) J. Struct. Biol. , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 90
    • 0032604157 scopus 로고    scopus 로고
    • Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis
    • Lyons T.J., Gralla E.B., Valentine J.S. Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis. Metal Ions Biol. Systems. 36:1999;125-177.
    • (1999) Metal Ions Biol. Systems , vol.36 , pp. 125-177
    • Lyons, T.J.1    Gralla, E.B.2    Valentine, J.S.3
  • 93
    • 0029863551 scopus 로고    scopus 로고
    • Inhibition of amyloid beta protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger
    • Tomiyama T., Shoji A., Kataoka K., Suwa Y., Asano S., Kaneko H., Endo N. Inhibition of amyloid beta protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger. J. Biol. Chem. 271:1996;6839-6844.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6839-6844
    • Tomiyama, T.1    Shoji, A.2    Kataoka, K.3    Suwa, Y.4    Asano, S.5    Kaneko, H.6    Endo, N.7
  • 94
    • 0028085940 scopus 로고
    • Antioxidant potential of anaerobic human plasma: Role of serum albumin and thiols as scavengers of carbon radicals
    • Soriani M., Pietraforte D., Minetti M. Antioxidant potential of anaerobic human plasma: role of serum albumin and thiols as scavengers of carbon radicals. Arch. Biochem. Biophys. 312:1994;180-188.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 180-188
    • Soriani, M.1    Pietraforte, D.2    Minetti, M.3
  • 95
    • 0031127537 scopus 로고    scopus 로고
    • Physiological thiol compounds exert pro- and anti-oxidant effects, respectively, on iron- and copper-dependent oxidation of human low-density lipoprotein
    • Lynch S.M., Frei B. Physiological thiol compounds exert pro- and anti-oxidant effects, respectively, on iron- and copper-dependent oxidation of human low-density lipoprotein. Biochim. Biophys. Acta. 1345:1997;215-221.
    • (1997) Biochim. Biophys. Acta , vol.1345 , pp. 215-221
    • Lynch, S.M.1    Frei, B.2
  • 98
    • 0027288860 scopus 로고
    • Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth
    • Koo E.H., Park L., Selkoe D.J. Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth. Proc. Natl. Acad. Sci. USA. 90:1993;4748-4752.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4748-4752
    • Koo, E.H.1    Park, L.2    Selkoe, D.J.3
  • 99
    • 0030592575 scopus 로고    scopus 로고
    • Physiological levels of beta-amyloid peptide promote PC12 cell proliferation
    • Luo Y., Sunderland T., Roth G.S., Wolozin B. Physiological levels of beta-amyloid peptide promote PC12 cell proliferation. Neurosci. Lett. 217:1996;125-128.
    • (1996) Neurosci. Lett. , vol.217 , pp. 125-128
    • Luo, Y.1    Sunderland, T.2    Roth, G.S.3    Wolozin, B.4
  • 100
    • 0033982030 scopus 로고    scopus 로고
    • Substrate-bound beta-amyloid peptides inhibit cell adhesion and neurite outgrowth in primary neuronal cultures
    • Postuma R.B., He W., Nunan J., Beyreuther K., Masters C.L., Barrow C.J., Small D.H. Substrate-bound beta-amyloid peptides inhibit cell adhesion and neurite outgrowth in primary neuronal cultures. J. Neurochem. 74:2000;1122-1130.
    • (2000) J. Neurochem. , vol.74 , pp. 1122-1130
    • Postuma, R.B.1    He, W.2    Nunan, J.3    Beyreuther, K.4    Masters, C.L.5    Barrow, C.J.6    Small, D.H.7
  • 101
    • 0027932162 scopus 로고
    • Effect of substance P and protein kinase inhibitors on beta-amyloid peptide-induced proliferation of cultured brain cells
    • Singh V.K., Cheng J.F., Leu S.J. Effect of substance P and protein kinase inhibitors on beta-amyloid peptide-induced proliferation of cultured brain cells. Brain Res. 660:1994;353-356.
    • (1994) Brain Res. , vol.660 , pp. 353-356
    • Singh, V.K.1    Cheng, J.F.2    Leu, S.J.3
  • 102
    • 0026646280 scopus 로고
    • Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischemia in the rat
    • Stephenson D.T., Rash K., Clemens J.A. Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischemia in the rat. Brain Res. 593:1992;128-135.
    • (1992) Brain Res. , vol.593 , pp. 128-135
    • Stephenson, D.T.1    Rash, K.2    Clemens, J.A.3
  • 103
    • 0029141049 scopus 로고
    • Trophic effects of substance P and beta-amyloid peptide on dibutyryl cyclic AMP-differentiated human leukemic (HL-60) cells
    • Takenouchi T., Munekata E. Trophic effects of substance P and beta-amyloid peptide on dibutyryl cyclic AMP-differentiated human leukemic (HL-60) cells. Life Sci. 56:1995;PL479-484.
    • (1995) Life Sci. , vol.56 , pp. 479-484
    • Takenouchi, T.1    Munekata, E.2
  • 104
    • 0024543836 scopus 로고
    • Amyloid beta protein enhances the survival of hippocampal neurons in vitro
    • Whitson J.S., Selkoe D.J., Cotman C.W. Amyloid beta protein enhances the survival of hippocampal neurons in vitro. Science. 243:1989;1488-1490.
    • (1989) Science , vol.243 , pp. 1488-1490
    • Whitson, J.S.1    Selkoe, D.J.2    Cotman, C.W.3
  • 105
  • 106
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides. Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 108
    • 0037096251 scopus 로고    scopus 로고
    • A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage
    • Zou K., Gong J.S., Yanagisawa K., Michikawa M. A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage. J. Neurosci. 22:2002;4833-4841.
    • (2002) J. Neurosci. , vol.22 , pp. 4833-4841
    • Zou, K.1    Gong, J.S.2    Yanagisawa, K.3    Michikawa, M.4
  • 109
    • 0033794471 scopus 로고    scopus 로고
    • Factors affecting pro- and anti-oxidant properties of fragments of the β-protein precursor (βPP): Implication for Alzheimer's disease
    • Andorn A.C., Kalaria R.N. Factors affecting pro- and anti-oxidant properties of fragments of the β-protein precursor (βPP): implication for Alzheimer's disease. J. Alzheimer's Dis. 2:2000;69-78.
    • (2000) J. Alzheimer's Dis. , vol.2 , pp. 69-78
    • Andorn, A.C.1    Kalaria, R.N.2
  • 110
    • 0034670134 scopus 로고    scopus 로고
    • Differential alterations in antioxidant capacity in cells from Alzheimer patients
    • Gibson G.E., Zhang H., Sheu K.R., Park L.C. Differential alterations in antioxidant capacity in cells from Alzheimer patients. Biochim. Biophys. Acta. 1502:2000;319-329.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 319-329
    • Gibson, G.E.1    Zhang, H.2    Sheu, K.R.3    Park, L.C.4
  • 111
    • 0032400818 scopus 로고    scopus 로고
    • Overexpression in neurons of human presenilin-1 or a presenilin-1 familial Alzheimer disease mutant does not enhance apoptosis
    • Bursztajn S., DeSouza R., McPhie D.L., Berman S.A., et al. Overexpression in neurons of human presenilin-1 or a presenilin-1 familial Alzheimer disease mutant does not enhance apoptosis. J. Neurosci. 18:1998;9790-9799.
    • (1998) J. Neurosci. , vol.18 , pp. 9790-9799
    • Bursztajn, S.1    DeSouza, R.2    McPhie, D.L.3    Berman, S.A.4
  • 112
    • 0034613438 scopus 로고    scopus 로고
    • Reduced antioxidant enzyme activity in brains of mice transgenic for human presenilin-1 with single or multiple mutations
    • Leutner S., Czech C., Schindowski K., Touchet N., Eckert A., Muller W.E. Reduced antioxidant enzyme activity in brains of mice transgenic for human presenilin-1 with single or multiple mutations. Neurosci. Lett. 292:2000;87-90.
    • (2000) Neurosci. Lett. , vol.292 , pp. 87-90
    • Leutner, S.1    Czech, C.2    Schindowski, K.3    Touchet, N.4    Eckert, A.5    Muller, W.E.6
  • 113
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid β-protein neurotoxicity
    • Geula C., Wu C.K., Saroff D., Lorenzo A., Yuan M., Yankner B.A. Aging renders the brain vulnerable to amyloid β-protein neurotoxicity. Nat. Med. 4:1998;827-831.
    • (1998) Nat. Med. , vol.4 , pp. 827-831
    • Geula, C.1    Wu, C.K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yankner, B.A.6
  • 114
    • 0032014664 scopus 로고    scopus 로고
    • The neurotoxicity of amyloid β protein in aged primates
    • McKee A.C., Kowall N.W., Schumacher J.S., Beal M.F. The neurotoxicity of amyloid β protein in aged primates. Amyloid. 5:1998;1-9.
    • (1998) Amyloid , vol.5 , pp. 1-9
    • McKee, A.C.1    Kowall, N.W.2    Schumacher, J.S.3    Beal, M.F.4
  • 115
    • 0037388672 scopus 로고    scopus 로고
    • Deposits of fibrillar Aβ do not cause neuronal loss or ferritin expression in adult rat brain
    • Bishop G.M., Robinson S.R. Deposits of fibrillar Aβ do not cause neuronal loss or ferritin expression in adult rat brain. J. Neural Transm. 110:2003;381-400.
    • (2003) J. Neural Transm. , vol.110 , pp. 381-400
    • Bishop, G.M.1    Robinson, S.R.2
  • 116
    • 0000447492 scopus 로고    scopus 로고
    • β-Amyloid helps to protect neurons from oxidative stress
    • Bishop G.M., Robinson S.R. β-Amyloid helps to protect neurons from oxidative stress. Neurobiol. Aging. 21:(Suppl. 1S):2000;S226.
    • (2000) Neurobiol. Aging , vol.21 , Issue.SUPPL. 1S , pp. 226
    • Bishop, G.M.1    Robinson, S.R.2
  • 117
    • 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 B.L., Miller M.W., Ware C.B., Martin G.M., Mattson M.P. Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice. Nat. Med. 5:1999;101-106.
    • (1999) Nat. Med. , vol.5 , pp. 101-106
    • Guo, Q.1    Fu, W.2    Sopher, B.L.3    Miller, M.W.4    Ware, C.B.5    Martin, G.M.6    Mattson, M.P.7
  • 118
    • 0033009194 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons from presenilin-1 mutant knock-in mice to amyloid beta-peptide toxicity: Central roles of superoxide production and caspase activation
    • Guo Q., Sebastian L., Sopher B.L., Miller M.W., Ware C.B., Martin G.M., Mattson M.P. Increased vulnerability of hippocampal neurons from presenilin-1 mutant knock-in mice to amyloid beta-peptide toxicity: central roles of superoxide production and caspase activation. J. Neurochem. 72:1999;1019-1029.
    • (1999) J. Neurochem. , vol.72 , pp. 1019-1029
    • Guo, Q.1    Sebastian, L.2    Sopher, B.L.3    Miller, M.W.4    Ware, C.B.5    Martin, G.M.6    Mattson, M.P.7
  • 120
    • 0000128256 scopus 로고    scopus 로고
    • Neuronal cell cultures protect low density lipoprotein from oxidation
    • Berndt C., Kontush A., Beisiegel U. Neuronal cell cultures protect low density lipoprotein from oxidation. Neurobiol. Aging. 19:1998;S284.
    • (1998) Neurobiol. Aging , vol.19 , pp. 284
    • Berndt, C.1    Kontush, A.2    Beisiegel, U.3
  • 123
    • 0028609448 scopus 로고
    • The soluble form of Alzheimer's amyloid beta protein is complexed to high density lipoprotein 3 and very high density lipoprotein in normal human plasma
    • Koudinov A., Matsubara E., Franione B., Ghiso J. The soluble form of Alzheimer's amyloid beta protein is complexed to high density lipoprotein 3 and very high density lipoprotein in normal human plasma. Biochem. Biophys. Res. Commun. 205:1994;1164-1171.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1164-1171
    • Koudinov, A.1    Matsubara, E.2    Franione, B.3    Ghiso, J.4
  • 124
    • 0030601055 scopus 로고    scopus 로고
    • Biochemical characterization of Alzheimer's soluble amyloid beta protein in human cerebrospinal fluid: Association with high density lipoproteins
    • Koudinov A.R., Koudinova N.V., Kumar A., Beavis R.C., Ghiso J. Biochemical characterization of Alzheimer's soluble amyloid beta protein in human cerebrospinal fluid: association with high density lipoproteins. Biochem. Biophys. Res. Commun. 223:1996;592-597.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 592-597
    • Koudinov, A.R.1    Koudinova, N.V.2    Kumar, A.3    Beavis, R.C.4    Ghiso, J.5
  • 126
    • 0028177562 scopus 로고
    • Induction of Alzheimer-like beta-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol
    • Sparks D.L., Scheff S.W., Hunsaker J.C. 3rd, Liu H., Landers T., Gross D.R. Induction of Alzheimer-like beta-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol. Exp. Neurol. 126:1994;88-94.
    • (1994) Exp. Neurol. , vol.126 , pp. 88-94
    • Sparks, D.L.1    Scheff, S.W.2    Hunsaker J.C. III3    Liu, H.4    Landers, T.5    Gross, D.R.6
  • 128
    • 0035830844 scopus 로고    scopus 로고
    • Accumulation and aggregation of amyloid beta-protein in late endosomes of Niemann-Pick type C cells
    • Yamazaki T., Chang T.Y., Haass C., Ihara Y. Accumulation and aggregation of amyloid beta-protein in late endosomes of Niemann-Pick type C cells. J. Biol. Chem. 276:2001;4454-4460.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4454-4460
    • Yamazaki, T.1    Chang, T.Y.2    Haass, C.3    Ihara, Y.4
  • 129
    • 0029070173 scopus 로고
    • Differential effects of amyloid peptides β-(1-40) and β-(25-35) injections into the rat nucleus basalis
    • Giovannelli L., Casamenti F., Scali C., Bartolini L., Pepeu G. Differential effects of amyloid peptides β-(1-40) and β-(25-35) injections into the rat nucleus basalis. Neuroscience. 66:1995;781-792.
    • (1995) Neuroscience , vol.66 , pp. 781-792
    • Giovannelli, L.1    Casamenti, F.2    Scali, C.3    Bartolini, L.4    Pepeu, G.5
  • 130
    • 0032551649 scopus 로고    scopus 로고
    • Long-term changes in the aggregation state and toxic effects of β-amyloid injected into the rat brain
    • Giovannelli L., Scali C., Faussone-Pellegrini M.S., Pepeu G., Casamenti F. Long-term changes in the aggregation state and toxic effects of β-amyloid injected into the rat brain. Neuroscience. 87:1998;349-357.
    • (1998) Neuroscience , vol.87 , pp. 349-357
    • Giovannelli, L.1    Scali, C.2    Faussone-Pellegrini, M.S.3    Pepeu, G.4    Casamenti, F.5
  • 132
    • 0033991657 scopus 로고    scopus 로고
    • Aβ and perlecan in rat brain: Glial activation, gradual clearance and limited neurotoxicity
    • Holcomb L.A., Gordon M.N., Benkovic S.A., Morgan D.G. Aβ and perlecan in rat brain: glial activation, gradual clearance and limited neurotoxicity. Mech. Ageing Dev. 112:2000;135-152.
    • (2000) Mech. Ageing Dev. , vol.112 , pp. 135-152
    • Holcomb, L.A.1    Gordon, M.N.2    Benkovic, S.A.3    Morgan, D.G.4
  • 133
    • 0000801077 scopus 로고    scopus 로고
    • High levels of microglial iron in the cortices of old primates: Implications for the neurotoxicity of β-amyloid
    • Fox S.R., Bishop G.M., Robinson S.R. High levels of microglial iron in the cortices of old primates: implications for the neurotoxicity of β-amyloid. Proc. Aust. Neurosci. Soc. 10:1999;213.
    • (1999) Proc. Aust. Neurosci. Soc. , vol.10 , pp. 213
    • Fox, S.R.1    Bishop, G.M.2    Robinson, S.R.3
  • 134
    • 0026688163 scopus 로고
    • Effect of beta amyloid peptides on neurons in hippocampal slice cultures
    • Malouf A.T. Effect of beta amyloid peptides on neurons in hippocampal slice cultures. Neurobiol. Aging. 13:1992;543-551.
    • (1992) Neurobiol. Aging , vol.13 , pp. 543-551
    • Malouf, A.T.1
  • 135
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures
    • Pike C.J., Walencewicz A.J., Glabe C.G., Cotman C.W. Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures. Eur. J. Pharmacol. 207:1991;367-368.
    • (1991) Eur. J. Pharmacol. , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 136
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., Cotman C.W. Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13:1993;1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 138
    • 0028618190 scopus 로고
    • Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of Alzheimer's disease amyloid
    • Ueda K., Saitoh T., Mori H. Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of Alzheimer's disease amyloid. Biochem. Biophys. Res. Commun. 205:1994;1366-1372.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1366-1372
    • Ueda, K.1    Saitoh, T.2    Mori, H.3
  • 140
    • 0029670992 scopus 로고    scopus 로고
    • Deposits of A beta fibrils are not toxic to cortical and hippocampal neurons in vitro
    • Wujek J.R., Dority M.D., Frederickson R.C., Brunden K.R. Deposits of A beta fibrils are not toxic to cortical and hippocampal neurons in vitro. Neurobiol. Aging. 17:1996;107-113.
    • (1996) Neurobiol. Aging , vol.17 , pp. 107-113
    • Wujek, J.R.1    Dority, M.D.2    Frederickson, R.C.3    Brunden, K.R.4
  • 142
    • 0036827161 scopus 로고    scopus 로고
    • Amyloid beta as a bioflocculant: Implications for the amyloid hypothesis of Alzheimer's disease
    • Robinson S.R., Bishop G.M. Amyloid beta as a bioflocculant: implications for the amyloid hypothesis of Alzheimer's disease. Neurobiol. Aging. 23:2002;1051-1072.
    • (2002) Neurobiol. Aging , vol.23 , pp. 1051-1072
    • Robinson, S.R.1    Bishop, G.M.2
  • 144
    • 0035874024 scopus 로고    scopus 로고
    • New evidence that the Alzheimer β-amyloid peptide does not spontaneously form free radicals: An ESR study using a series of spin-traps
    • Turnbull S., Tabner B.J., El-Agnaf O.M., Twyman L.J., Allsop D. New evidence that the Alzheimer β-amyloid peptide does not spontaneously form free radicals: an ESR study using a series of spin-traps. Free Radic. Biol. Med. 30:2001;1154-1162.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1154-1162
    • Turnbull, S.1    Tabner, B.J.2    El-Agnaf, O.M.3    Twyman, L.J.4    Allsop, D.5
  • 145
    • 18144453796 scopus 로고    scopus 로고
    • Astrocytes regulate microglial phagocytosis of senile plaque cores of Alzheimer's disease
    • DeWitt D.A., Perry G., Cohen M., Doller C., Silver J. Astrocytes regulate microglial phagocytosis of senile plaque cores of Alzheimer's disease. Exp. Neurol. 149:1998;329-340.
    • (1998) Exp. Neurol. , vol.149 , pp. 329-340
    • DeWitt, D.A.1    Perry, G.2    Cohen, M.3    Doller, C.4    Silver, J.5
  • 146
    • 0030612033 scopus 로고    scopus 로고
    • APPSw transgenic mice develop age-related A beta deposits and neuropil abnormalities, but no neuronal loss in CA1
    • Irizarry M.C., McNamara M., Fedorchak K., Hsiao K., Hyman B.T. APPSw transgenic mice develop age-related A beta deposits and neuropil abnormalities, but no neuronal loss in CA1. J. Neuropathol. Exp. Neurol. 56:1997;965-973.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 965-973
    • Irizarry, M.C.1    McNamara, M.2    Fedorchak, K.3    Hsiao, K.4    Hyman, B.T.5
  • 147
    • 0030611097 scopus 로고    scopus 로고
    • Aβ deposition is associated with neuropil changes, but not with overt neuronal loss in the human amyloid precursor protein V717F (PDAPP) transgenic mouse
    • Irizarry M.C., Soriano F., McNamara M., Page K.J., Schenk D., Games D., Hyman B.T. Aβ deposition is associated with neuropil changes, but not with overt neuronal loss in the human amyloid precursor protein V717F (PDAPP) transgenic mouse. J. Neurosci. 17:1997;7053-7059.
    • (1997) J. Neurosci. , vol.17 , pp. 7053-7059
    • Irizarry, M.C.1    Soriano, F.2    McNamara, M.3    Page, K.J.4    Schenk, D.5    Games, D.6    Hyman, B.T.7
  • 149
    • 0036358289 scopus 로고    scopus 로고
    • The influence of the carboxyl terminus of the Alzheimer Abeta peptide on its confirmation, aggregation, and neurotoxic properties
    • Soreghan B., Pike C., Kayed R., Tian W., Milton S., Cotman C., Glabe C.G. The influence of the carboxyl terminus of the Alzheimer Abeta peptide on its confirmation, aggregation, and neurotoxic properties. Neuromolecular Med. 1:2002;81-94.
    • (2002) Neuromolecular Med. , vol.1 , pp. 81-94
    • Soreghan, B.1    Pike, C.2    Kayed, R.3    Tian, W.4    Milton, S.5    Cotman, C.6    Glabe, C.G.7
  • 150
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra
    • Barrow C.J., Yasuda A., Kenny P.T., Zagorski M.G. Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra. J. Mol. Biol. 225:1992;1075-1093.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 151
    • 0026631361 scopus 로고
    • NMR studies of amyloid beta-peptides: Proton assignments, secondary structure, and mechanism of an alpha-helix - Beta-sheet conversion for a homologous, 28-residue. N-terminal fragment
    • Zagorski M.G., Barrow C.J. NMR studies of amyloid beta-peptides: proton assignments, secondary structure, and mechanism of an alpha-helix - beta-sheet conversion for a homologous, 28-residue. N-terminal fragment. Biochemistry. 31:(24):1992;5621-5631.
    • (1992) Biochemistry , vol.31 , Issue.24 , pp. 5621-5631
    • Zagorski, M.G.1    Barrow, C.J.2
  • 153
    • 0025779179 scopus 로고
    • Solution structures of beta peptide and its constituent fragments: Relation to amyloid deposition
    • Barrow C.J., Zagorski M.G. Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition. Science. 253:1991;179-182.
    • (1991) Science , vol.253 , pp. 179-182
    • Barrow, C.J.1    Zagorski, M.G.2
  • 154
    • 0033528666 scopus 로고    scopus 로고
    • Differential effects of apolipoprotein E isoforms on metal-induced aggregation of A beta using physiological concentrations
    • Moir R.D., Atwood C.S., Romano D.M., Laurans M.H., Huang X., Bush A.I., Smith J.D., Tanzi R.E. Differential effects of apolipoprotein E isoforms on metal-induced aggregation of A beta using physiological concentrations. Biochemistry. 38:1999;4595-4603.
    • (1999) Biochemistry , vol.38 , pp. 4595-4603
    • Moir, R.D.1    Atwood, C.S.2    Romano, D.M.3    Laurans, M.H.4    Huang, X.5    Bush, A.I.6    Smith, J.D.7    Tanzi, R.E.8
  • 155
    • 0032880901 scopus 로고    scopus 로고
    • Methionine residue 35 is important in amyloid beta-peptide-associated free radical oxidative stress
    • Varadarajan S., Yatin S., Kanski J., Jahanshahi F., Butterfield D.A. Methionine residue 35 is important in amyloid beta-peptide-associated free radical oxidative stress. Brain Res. Bull. 50:1999;133-141.
    • (1999) Brain Res. Bull. , vol.50 , pp. 133-141
    • Varadarajan, S.1    Yatin, S.2    Kanski, J.3    Jahanshahi, F.4    Butterfield, D.A.5
  • 156
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35)
    • Varadarajan S., Kanski J., Aksenova M., Lauderback C., Butterfield D.A. Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35). J. Am. Chem. Soc. 123:2001;5625-5631.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3    Lauderback, C.4    Butterfield, D.A.5
  • 157
    • 0030050065 scopus 로고    scopus 로고
    • A beta (25-35) peptide displays H2O2-like reactivity towards aqueous Fe2+, nitroxide spin probes, and synaptosomal membrane proteins
    • Butterfield D.A., Martin L., Carney J.M., Hensley K. A beta (25-35) peptide displays H2O2-like reactivity towards aqueous Fe2+, nitroxide spin probes, and synaptosomal membrane proteins. Life Sci. 58:1996;217-228.
    • (1996) Life Sci. , vol.58 , pp. 217-228
    • Butterfield, D.A.1    Martin, L.2    Carney, J.M.3    Hensley, K.4
  • 158
    • 0032514165 scopus 로고    scopus 로고
    • Promotion of transition metal-induced reactive oxygen species formation by beta-amyloid
    • Bondy S.C., Guo-Ross S.X., Truong A.T. Promotion of transition metal-induced reactive oxygen species formation by beta-amyloid. Brain Res. 799:1998;91-96.
    • (1998) Brain Res. , vol.799 , pp. 91-96
    • Bondy, S.C.1    Guo-Ross, S.X.2    Truong, A.T.3
  • 159
    • 0028178837 scopus 로고
    • Beta-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: Implications to Alzheimer's disease
    • Butterfield D.A., Hensley K., Harris M., Mattson M., Carney J. Beta-amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochem. Biophys. Res. Commun. 200:1994;710-715.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.4    Carney, J.5
  • 160
    • 0033977413 scopus 로고    scopus 로고
    • Time-course of oxidation of lipids in human cerebrospinal fluid in vitro
    • Arlt S., Finckh B., Beisiegel U., Kontush A. Time-course of oxidation of lipids in human cerebrospinal fluid in vitro. Free Radic. Res. 32:2000;103-114.
    • (2000) Free Radic. Res. , vol.32 , pp. 103-114
    • Arlt, S.1    Finckh, B.2    Beisiegel, U.3    Kontush, A.4
  • 161
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide
    • Mark R.J., Lovell M.A., Markesbery W.R., Uchida K., Mattson M.P. A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid beta-peptide. J. Neurochem. 68:1997;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
  • 162
    • 0034981701 scopus 로고    scopus 로고
    • Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation
    • Xu J., Chen S., Ku G., Ahmed S.H., Xu J., Chen H., Hsu C.Y. Amyloid beta peptide-induced cerebral endothelial cell death involves mitochondrial dysfunction and caspase activation. J. Cereb. Blood Flow Metab. 21:2001;702-710.
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 702-710
    • Xu, J.1    Chen, S.2    Ku, G.3    Ahmed, S.H.4    Xu, J.5    Chen, H.6    Hsu, C.Y.7
  • 164
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C., Davis J.B., Lesley R., Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell. 77:1994;817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 167
    • 0029670094 scopus 로고    scopus 로고
    • Beta-amyloid-mediated vasoactivity and vascular endothelial damage
    • Thomas T., Thomas G., McLendon C., Sutton T., Mullan M. Beta-amyloid-mediated vasoactivity and vascular endothelial damage. Nature. 380:1996;168-171.
    • (1996) Nature , vol.380 , pp. 168-171
    • Thomas, T.1    Thomas, G.2    McLendon, C.3    Sutton, T.4    Mullan, M.5
  • 168
    • 0028916920 scopus 로고
    • Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium
    • Mattson M.P., Goodman Y. Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium. Brain Res. 676:1995;219-224.
    • (1995) Brain Res. , vol.676 , pp. 219-224
    • Mattson, M.P.1    Goodman, Y.2
  • 169
    • 0030155860 scopus 로고    scopus 로고
    • Amyloid beta-peptide and oxidative cellular injury in Alzheimer's disease
    • Mark R.J., Blanc E.M., Mattson M.P. Amyloid beta-peptide and oxidative cellular injury in Alzheimer's disease. Mol. Neurobiol. 12:1996;211-224.
    • (1996) Mol. Neurobiol. , vol.12 , pp. 211-224
    • Mark, R.J.1    Blanc, E.M.2    Mattson, M.P.3
  • 170
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery W.R. Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med. 23:(1):1997;134-147.
    • (1997) Free Radic. Biol. Med. , vol.23 , Issue.1 , pp. 134-147
    • Markesbery, W.R.1
  • 173
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro
    • Busciglio J., Yankner B.A. Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature. 378:1995;776-779.
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 174
    • 0034035616 scopus 로고    scopus 로고
    • Metals and neuroscience
    • Bush A.I. Metals and neuroscience. Curr Opin. Chem. Biol. 4:2000;184-191.
    • (2000) Curr Opin. Chem. Biol. , vol.4 , pp. 184-191
    • Bush, A.I.1
  • 175
    • 0025940313 scopus 로고
    • The balance between Cu,Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress
    • Amstad P., Peskin A., Shah G., Mirault M.E., Moret R., Zbinden I., Cerutti P. The balance between Cu,Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress. Biochemistry. 30:(38):1991;9305-9313.
    • (1991) Biochemistry , vol.30 , Issue.38 , pp. 9305-9313
    • Amstad, P.1    Peskin, A.2    Shah, G.3    Mirault, M.E.4    Moret, R.5    Zbinden, I.6    Cerutti, P.7
  • 176
    • 0029980319 scopus 로고    scopus 로고
    • Characterization of the genomic structure of the mouse APLP1 gene
    • Zhong S., Wu K., Black I.B., Schaar D.G. Characterization of the genomic structure of the mouse APLP1 gene. Genomics. 32:1996;159-162.
    • (1996) Genomics , vol.32 , pp. 159-162
    • Zhong, S.1    Wu, K.2    Black, I.B.3    Schaar, D.G.4
  • 177
    • 0026469348 scopus 로고
    • Hydroxyl radical production by H2O2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme
    • Sato K., Akaike T., Kohno M., Ando M., Maeda H. Hydroxyl radical production by H2O2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme. J. Biol. Chem. 267:(35):1992;25371-25377.
    • (1992) J. Biol. Chem. , vol.267 , Issue.35 , pp. 25371-25377
    • Sato, K.1    Akaike, T.2    Kohno, M.3    Ando, M.4    Maeda, H.5
  • 179
    • 0032514907 scopus 로고    scopus 로고
    • Reactions of hydrogen peroxide with familial amyotrophic lateral sclerosis mutant human copper-zinc superoxide dismutases studied by pulse radiolysis
    • Goto J.J., Gralla E.B., Valentine J.S., Cabelli D.E. Reactions of hydrogen peroxide with familial amyotrophic lateral sclerosis mutant human copper-zinc superoxide dismutases studied by pulse radiolysis. J. Biol. Chem. 273:1998;30104-30109.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30104-30109
    • Goto, J.J.1    Gralla, E.B.2    Valentine, J.S.3    Cabelli, D.E.4
  • 181
    • 0021104498 scopus 로고
    • Hydroperoxide anion, HO-2, is an affinity reagent for the inactivation of yeast Cu. Zn-superoxide dismutase: Modification of one histidine per subunit
    • Blech D.M., Borders C.L.J. Hydroperoxide anion, HO-2, is an affinity reagent for the inactivation of yeast Cu. Zn-superoxide dismutase: modification of one histidine per subunit. Arch. Biochem. Biophys. 224:1983;579-586.
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 579-586
    • Blech, D.M.1    Borders, C.L.J.2
  • 185
    • 0033615580 scopus 로고    scopus 로고
    • The presenilins in Alzheimer's disease - Proteolysis holds the key
    • Haass C., De Strooper B. The presenilins in Alzheimer's disease - proteolysis holds the key. Science. 286:1999;916-919.
    • (1999) Science , vol.286 , pp. 916-919
    • Haass, C.1    De Strooper, B.2
  • 188
    • 0034663175 scopus 로고    scopus 로고
    • 3rd Link between heart disease, cholesterol, and Alzheimer's disease: A review
    • Sparks D.L., Martin T.A., Gross D.R., Hunsaker J.C. 3rd Link between heart disease, cholesterol, and Alzheimer's disease: a review. Microsc. Res. Tech. 50:2000;287-290.
    • (2000) Microsc. Res. Tech. , vol.50 , pp. 287-290
    • Sparks, D.L.1    Martin, T.A.2    Gross, D.R.3    Hunsaker, J.C.4
  • 191
    • 0034638379 scopus 로고    scopus 로고
    • Is oxidative damage by amyloid and prion peptides mediated by hydrogen atom transfer from glycine carbon to methionine sulfur within sheets?
    • Rauk A., Armstrong D.A., Fairlie D.P. Is oxidative damage by amyloid and prion peptides mediated by hydrogen atom transfer from glycine carbon to methionine sulfur within sheets? J. Am. Chem. Soc. 122:2000;9761-9767.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9761-9767
    • Rauk, A.1    Armstrong, D.A.2    Fairlie, D.P.3


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