메뉴 건너뛰기




Volumn , Issue , 2007, Pages 333-361

Metal ions and Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84858787589     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-0-387-70830-0_15     Document Type: Chapter
Times cited : (1)

References (252)
  • 1
    • 0038452658 scopus 로고    scopus 로고
    • Changes in intracellular calcium and glutathione in astrocytes as the primary mechanism of amyloid neurotoxicity
    • Abramov, A.Y., Canevari, L. and Duchen, M.R., 2003, Changes in intracellular calcium and glutathione in astrocytes as the primary mechanism of amyloid neurotoxicity. J. Neurosci. 23: 5088.
    • (2003) J. Neurosci. , vol.23 , pp. 5088
    • Abramov, A.Y.1    Canevari, L.2    Duchen, M.R.3
  • 2
    • 2542625173 scopus 로고    scopus 로고
    • Alzheimer's disease - A sum greater than its parts?
    • Adlard, P.A. and Cummings, B.J., 2004, Alzheimer's disease - a sum greater than its parts? Neurobiol. Aging 25: 725.
    • (2004) Neurobiol. Aging , vol.25 , pp. 725
    • Adlard, P.A.1    Cummings, B.J.2
  • 3
    • 0032413587 scopus 로고    scopus 로고
    • Increased density of metallothionein I/II-immunopositive cortical glial cells in the early stages of Alzheimer's disease
    • Adlard, P.A., West, A.K. and Vickers, J.C., 1998, Increased density of metallothionein I/II-immunopositive cortical glial cells in the early stages of Alzheimer's disease. Neurobiol. Dis. 5: 349.
    • (1998) Neurobiol. Dis. , vol.5 , pp. 349
    • Adlard, P.A.1    West, A.K.2    Vickers, J.C.3
  • 5
    • 14844299775 scopus 로고    scopus 로고
    • Mechanism of zinc-induced phosphorylation of p70 S6 kinase and glycogen synthase kinase 3beta in SH-SY5Y neuroblastoma cells
    • An, W.L., Bjorkdahl, C., Liu, R., Cowburn, R.F., Winblad, B. and Pei, J.J., 2005, Mechanism of zinc-induced phosphorylation of p70 S6 kinase and glycogen synthase kinase 3beta in SH-SY5Y neuroblastoma cells. J. Neurochem. 92: 1104.
    • (2005) J. Neurochem. , vol.92 , pp. 1104
    • An, W.L.1    Bjorkdahl, C.2    Liu, R.3    Cowburn, R.F.4    Winblad, B.5    Pei, J.J.6
  • 7
    • 0035985698 scopus 로고    scopus 로고
    • Lipid peroxidation in neurodegeneration: New insights into Alzheimer's disease
    • Arlt, S., Beisiegel, U. and Kontush, A., 2002, Lipid peroxidation in neurodegeneration: new insights into Alzheimer's disease. Curr. Opin. Lipidol. 13: 289.
    • (2002) Curr. Opin. Lipidol. , vol.13 , pp. 289
    • Arlt, S.1    Beisiegel, U.2    Kontush, A.3
  • 8
    • 15244341973 scopus 로고    scopus 로고
    • Gene expression profiling in chronic copper overload reveals upregulation of Prnp and App
    • Armendariz, A.D., Gonzalez, M., Loguinov, A.V. and Vulpe, C.D., 2004, Gene expression profiling in chronic copper overload reveals upregulation of Prnp and App. Physiol. Genomics. 20: 45.
    • (2004) Physiol. Genomics. , vol.20 , pp. 45
    • Armendariz, A.D.1    Gonzalez, M.2    Loguinov, A.V.3    Vulpe, C.D.4
  • 11
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with alzheimer amyloid beta peptides: Identification of an attomolaraffinity 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. and Bush, A.I., 2000b, Characterization of copper interactions with alzheimer amyloid beta peptides: identification of an attomolaraffinity copper binding site on amyloid beta1-42. J. Neurochem. 75: 1219.
    • (2000) J. Neurochem. , vol.75 , pp. 1219
    • 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
  • 13
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack, J.C., Schneider, A., Mandelkow, E.M. and Hyman, B.T., 2002, Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol. (Berl). 103: 26.
    • (2002) Acta Neuropathol. (Berl). , vol.103 , pp. 26
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 17
    • 12844273354 scopus 로고    scopus 로고
    • The fetal basis of amyloidogenesis: Exposure to lead and latent overexpression of amyloid precursor protein and beta-amyloid in the aging brain
    • Basha, M.R., Wei, W., Bakheet, S.A., Benitez, N., Siddiqi, H.K., Ge, Y.W., Lahiri, D.K. and Zawia, N.H., 2005a, The fetal basis of amyloidogenesis: exposure to lead and latent overexpression of amyloid precursor protein and beta-amyloid in the aging brain. J. Neurosci. 25: 823.
    • (2005) J. Neurosci. , vol.25 , pp. 823
    • Basha, M.R.1    Wei, W.2    Bakheet, S.A.3    Benitez, N.4    Siddiqi, H.K.5    Ge, Y.W.6    Lahiri, D.K.7    Zawia, N.H.8
  • 21
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl, C., Davis, J.B., Lesley, R. and Schubert, D., 1994, Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77: 817.
    • (1994) Cell , vol.77 , pp. 817
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 22
    • 2442586535 scopus 로고    scopus 로고
    • Copper depletion down-regulates expression of the Alzheimer's disease amyloid-beta precursor protein gene
    • Bellingham, S.A., Lahiri, D.K., Maloney, B., La Fontaine, S., Multhaup, G. and Camakaris, J., 2004a, Copper depletion down-regulates expression of the Alzheimer's disease amyloid-beta precursor protein gene. J. Biol. Chem. 279: 20378.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20378
    • Bellingham, S.A.1    Lahiri, D.K.2    Maloney, B.3    La Fontaine, S.4    Multhaup, G.5    Camakaris, J.6
  • 23
    • 5444235015 scopus 로고    scopus 로고
    • Gene knockout of amyloid precursor protein and amyloid precursor-like protein-2 increases cellular copper levels in primary mouse cortical neurons and embryonic fibroblasts
    • Bellingham, S.A., Ciccotosto, G.D., Needham, B.E., Fodero, L.R., White, A.R., Masters, C.L., Cappai, R. and Camakaris, J., 2004b, Gene knockout of amyloid precursor protein and amyloid precursor-like protein-2 increases cellular copper levels in primary mouse cortical neurons and embryonic fibroblasts. J. Neurochem. 91: 423.
    • (2004) J. Neurochem. , vol.91 , pp. 423
    • Bellingham, S.A.1    Ciccotosto, G.D.2    Needham, B.E.3    Fodero, L.R.4    White, A.R.5    Masters, C.L.6    Cappai, R.7    Camakaris, J.8
  • 25
    • 17844382385 scopus 로고    scopus 로고
    • Zinc induces neurofilament phosphorylation independent of p70 S6 kinase in N2a cells
    • Bjorkdahl, C., Sjogren, M.J., Winblad, B. and Pei, J.J., 2005, Zinc induces neurofilament phosphorylation independent of p70 S6 kinase in N2a cells. Neuroreport 16: 591.
    • (2005) Neuroreport , vol.16 , pp. 591
    • Bjorkdahl, C.1    Sjogren, M.J.2    Winblad, B.3    Pei, J.J.4
  • 26
    • 13844281550 scopus 로고    scopus 로고
    • How chronic inflammation can affect the brain and support the development of Alzheimer's disease in old age: The role of microglia and astrocytes
    • Blasko, I., Stampfer-Kountchev, M., Robatscher, P., Veerhuis, R., Eikelenboom, P. and Grubeck-Loebenstein, B., 2004, How chronic inflammation can affect the brain and support the development of Alzheimer's disease in old age: the role of microglia and astrocytes. Aging Cell 3: 169.
    • (2004) Aging Cell , vol.3 , pp. 169
    • Blasko, I.1    Stampfer-Kountchev, M.2    Robatscher, P.3    Veerhuis, R.4    Eikelenboom, P.5    Grubeck-Loebenstein, B.6
  • 28
    • 0033430087 scopus 로고    scopus 로고
    • Copper inhibits beta-amyloid production and stimulates the nonamyloidogenic pathway of amyloid-precursor-protein secretion
    • Borchardt, T., Camakaris, J., Cappai, R.C., Masters, L., Beyreuther, K. and Multhaup, G., 1999, Copper inhibits beta-amyloid production and stimulates the nonamyloidogenic pathway of amyloid-precursor-protein secretion. Biochem. J. 344: 461.
    • (1999) Biochem. J. , vol.344 , pp. 461
    • Borchardt, T.1    Camakaris, J.2    Cappai, R.C.3    Masters, L.4    Beyreuther, K.5    Multhaup, G.6
  • 29
    • 0030832287 scopus 로고    scopus 로고
    • A laser microprobe mass analysis of brain aluminum and iron in dementia pugilistica: Comparison with Alzheimer's disease
    • Bouras, C., Giannakopoulos, P., Good, P.F., Hsu, A., Hof, P.R. and Perl, D.P., 1997, A laser microprobe mass analysis of brain aluminum and iron in dementia pugilistica: comparison with Alzheimer's disease. Eur. Neurol. 38: 53.
    • (1997) Eur. Neurol. , vol.38 , pp. 53
    • Bouras, C.1    Giannakopoulos, P.2    Good, P.F.3    Hsu, A.4    Hof, P.R.5    Perl, D.P.6
  • 30
  • 31
    • 0031695197 scopus 로고    scopus 로고
    • Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset
    • Brookmeyer, R., Gray, S. and Kawas, C., 1998, Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset. Am. J. Public Health 88: 1337.
    • (1998) Am. J. Public Health , vol.88 , pp. 1337
    • Brookmeyer, R.1    Gray, S.2    Kawas, C.3
  • 32
    • 0030757388 scopus 로고    scopus 로고
    • Selective aggregation of endogenous beta-amyloid peptide and soluble amyloid precursor protein in cerebrospinal fluid by zinc
    • Brown, A.M., Tummolo, D.M., Rhodes, K.J., Hofmann, J.R., Jacobsen, J.S. and Sonnenberg-Reines, J., 1997, Selective aggregation of endogenous beta-amyloid peptide and soluble amyloid precursor protein in cerebrospinal fluid by zinc. J. Neurochem. 69: 1204.
    • (1997) J. Neurochem. , vol.69 , pp. 1204
    • Brown, A.M.1    Tummolo, D.M.2    Rhodes, K.J.3    Hofmann, J.R.4    Jacobsen, J.S.5    Sonnenberg-Reines, J.6
  • 34
    • 0023251560 scopus 로고
    • Metabolic balance studies for zinc and copper in housebound elderly people and the relationship between zinc balance and leukocyte zinc concentrations
    • Bunker, V.W., Hinks, L.J., Stansfield, M.F., Lawson, M.S. and Clayton, B.E., 1987, Metabolic balance studies for zinc and copper in housebound elderly people and the relationship between zinc balance and leukocyte zinc concentrations. Am. J. Clin. Nutr. 46: 353.
    • (1987) Am. J. Clin. Nutr. , vol.46 , pp. 353
    • Bunker, V.W.1    Hinks, L.J.2    Stansfield, M.F.3    Lawson, M.S.4    Clayton, B.E.5
  • 36
    • 0028171064 scopus 로고
    • The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily
    • Bush, A.I., Pettingell, W.H., Jr., de Paradis, M., Tanzi, R.E. and Wasco, W., 1994a, The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily. J. Biol. Chem. 269: 26618.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26618
    • Bush, A.I.1    Pettingell Jr., W.H.2    De Paradis, M.3    Tanzi, R.E.4    Wasco, W.5
  • 38
    • 0028180196 scopus 로고
    • Modulation of A beta adhesiveness and secretase site cleavage by zinc
    • Bush, A.I., Pettingell, W.H., Jr., Paradis, M.D. and Tanzi, R.E., 1994c, Modulation of A beta adhesiveness and secretase site cleavage by zinc. J. Biol. Chem. 269: 12152.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12152
    • Bush, A.I.1    Pettingell Jr., W.H.2    Paradis, M.D.3    Tanzi, R.E.4
  • 39
    • 0036753272 scopus 로고    scopus 로고
    • Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
    • Butterfield, D.A., Castegna, A., Lauderback, C.M. and Drake, J., 2002, Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death. Neurobiol. Aging 23: 655.
    • (2002) Neurobiol. Aging , vol.23 , pp. 655
    • Butterfield, D.A.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 40
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum, J.D., Liu, K.N., Luo, Y., Slack, J.L., Stocking, K.L., Peschon, J.J., Johnson, R.S., Castner, B.J., Cerretti, D.P. and Black, R.A., 1998, Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273: 27765.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6    Johnson, R.S.7    Castner, B.J.8    Cerretti, D.P.9    Black, R.A.10
  • 41
    • 13644266898 scopus 로고    scopus 로고
    • Age- and region-dependent alterations in Abeta-degrading enzymes: Implications for Abeta-induced disorders
    • Caccamo, A., Oddo, S., Sugarman, M.C., Akbari, Y. and LaFerla, F.M., 2005, Age- and region-dependent alterations in Abeta-degrading enzymes: implications for Abeta-induced disorders. Neurobiol. Aging 26: 645.
    • (2005) Neurobiol. Aging , vol.26 , pp. 645
    • Caccamo, A.1    Oddo, S.2    Sugarman, M.C.3    Akbari, Y.4    Laferla, F.M.5
  • 43
    • 0035872474 scopus 로고    scopus 로고
    • Mechanisms by which metals promote events connected to neurodegenerative diseases
    • Campbell, A.M., Smith, A., Sayre, L.M., Bondy, S.C. and Perry, G., 2001, Mechanisms by which metals promote events connected to neurodegenerative diseases. Brain Res. Bull. 55: 125.
    • (2001) Brain Res. Bull. , vol.55 , pp. 125
    • Campbell, A.M.1    Smith, A.2    Sayre, L.M.3    Bondy, S.C.4    Perry, G.5
  • 45
    • 0036077536 scopus 로고    scopus 로고
    • Beta-amyloid catabolism: Roles for neprilysin (NEP) and other metallopeptidases?
    • Carson, J.A. and Turner, A.J., 2002, Beta-amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases? J. Neurochem. 81: 1.
    • (2002) J. Neurochem. , vol.81 , pp. 1
    • Carson, J.A.1    Turner, A.J.2
  • 49
    • 23744441694 scopus 로고    scopus 로고
    • Preclinical Alzheimer's disease: Diagnosis and prediction of progression
    • Chong, M.S. and Sahadevan, S., 2005, Preclinical Alzheimer's disease: diagnosis and prediction of progression. Lancet Neurol. 4: 576.
    • (2005) Lancet Neurol. , vol.4 , pp. 576
    • Chong, M.S.1    Sahadevan, S.2
  • 50
    • 0346457011 scopus 로고    scopus 로고
    • Neuron-glia communication: Metallothionein expression is specifically upregulated by astrocytes in response to neuronal injury
    • Chung, R.S., Adlard, P.A., Dittmann, J., Vickers, J.C., Chuah, M. and West, A., 2004, Neuron-glia communication: metallothionein expression is specifically upregulated by astrocytes in response to neuronal injury. J. Neurochem. 88: 454.
    • (2004) J. Neurochem. , vol.88 , pp. 454
    • Chung, R.S.1    Adlard, P.A.2    Dittmann, J.3    Vickers, J.C.4    Chuah, M.5    West, A.6
  • 52
    • 4344580888 scopus 로고    scopus 로고
    • Strategies for disease modification in Alzheimer's disease
    • Citron, M., 2004, Strategies for disease modification in Alzheimer's disease. Nat. Rev. Neurosci. 5: 677.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 677
    • Citron, M.1
  • 53
    • 13244287771 scopus 로고    scopus 로고
    • Metal-binding properties of the peptide APP(170-188): A model of the Zn(II)-binding site of amyloid precursor protein (APP)
    • Ciuculescu, E.D., Mekmouche, Y. and Faller, P., 2005, Metal-binding properties of the peptide APP(170-188): a model of the Zn(II)-binding site of amyloid precursor protein (APP). Chemistry 11: 903.
    • (2005) Chemistry , vol.11 , pp. 903
    • Ciuculescu, E.D.1    Mekmouche, Y.2    Faller, P.3
  • 54
    • 5344272541 scopus 로고    scopus 로고
    • A focus on the synapse for neuroprotection in Alzheimer's disease and other dementias
    • Coleman, P., Federoff, H. and Kurlan, R., 2004, A focus on the synapse for neuroprotection in Alzheimer's disease and other dementias. Neurology 63: 1155.
    • (2004) Neurology , vol.63 , pp. 1155
    • Coleman, P.1    Federoff, H.2    Kurlan, R.3
  • 55
    • 0027327899 scopus 로고
    • Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer's disease
    • Connor, J.R., Tucker, P., Johnson, M. and Snyder, B., 1993, Ceruloplasmin levels in the human superior temporal gyrus in aging and Alzheimer's disease. Neurosci. Lett. 159: 88.
    • (1993) Neurosci. Lett. , vol.159 , pp. 88
    • Connor, J.R.1    Tucker, P.2    Johnson, M.3    Snyder, B.4
  • 56
    • 0035943058 scopus 로고    scopus 로고
    • Mitochondrial enzyme-deficient hippocampal neurons and choroidal cells in AD
    • Cottrell, D.A., Blakely, E.L., Johnson, M.A., Ince, P.G. and Turnbull, D.M., 2001, Mitochondrial enzyme-deficient hippocampal neurons and choroidal cells in AD. Neurology 57: 260.
    • (2001) Neurology , vol.57 , pp. 260
    • Cottrell, D.A.1    Blakely, E.L.2    Johnson, M.A.3    Ince, P.G.4    Turnbull, D.M.5
  • 57
    • 0037130658 scopus 로고    scopus 로고
    • The active site of a zinc-dependent metalloproteinase influences the computed pK(a) of ligands coordinated to the catalytic zinc ion
    • Cross, J.B., Duca, J.S., Kaminski, J.J. and Madison, V.S., 2002, The active site of a zinc-dependent metalloproteinase influences the computed pK(a) of ligands coordinated to the catalytic zinc ion. J. Am. Chem. Soc. 124: 11004.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11004
    • Cross, J.B.1    Duca, J.S.2    Kaminski, J.J.3    Madison, V.S.4
  • 59
    • 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. and Barnham, K.J., 2001, 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: 20466.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466
    • 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
  • 60
    • 0037474240 scopus 로고    scopus 로고
    • Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid
    • Curtain, C.C., Ali, F.E., Smith, D.G., Bush, A.I., Masters, C.L. and Barnham, K.J., 2003, Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid. J. Biol. Chem. 278: 2977.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2977
    • Curtain, C.C.1    Ali, F.E.2    Smith, D.G.3    Bush, A.I.4    Masters, C.L.5    Barnham, K.J.6
  • 61
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren, K.N., Manelli, A.M., Stine, W.B., Jr., Baker, L.K., Krafft, G.A. and LaDu, M.J., 2002, Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 277: 32046.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.A.5    Ladu, M.J.6
  • 62
    • 0030804608 scopus 로고    scopus 로고
    • Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains: A protoninduced X-ray emission spectroscopic analysis of cryostat sections from autopsy material
    • Danscher, G., Jensen, K.B., Frederickson, C.J., Kemp, K. Andreasen, A., Juhl, S., Stoltenberg, M. and Ravid, R., 1997, Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains: a protoninduced X-ray emission spectroscopic analysis of cryostat sections from autopsy material. J. Neurosci. Methods 76: 53.
    • (1997) J. Neurosci. Methods , vol.76 , pp. 53
    • Danscher, G.1    Jensen, K.B.2    Frederickson, C.J.3    Kemp Andreasen, K.A.4    Juhl, S.5    Stoltenberg, M.6    Ravid, R.7
  • 63
    • 0033998205 scopus 로고    scopus 로고
    • Changes in dietary zinc and copper affect zinc-status indicators of postmenopausal women, notably, extracellular superoxide dismutase and amyloid precursor proteins
    • Davis, C.D., Milne, D.B. and Nielsen, F.H., 2000, Changes in dietary zinc and copper affect zinc-status indicators of postmenopausal women, notably, extracellular superoxide dismutase and amyloid precursor proteins. Am. J. Clin. Nutr. 71: 781.
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 781
    • Davis, C.D.1    Milne, D.B.2    Nielsen, F.H.3
  • 66
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex
    • De Strooper, B., 2003, Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex. Neuron 38: 9.
    • (2003) Neuron , vol.38 , pp. 9
    • De Strooper, B.1
  • 67
    • 0030297178 scopus 로고    scopus 로고
    • Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: Possible relation to oxidative stress
    • Deibel, M.A., Ehmann, W.D. and Markesbery, W.R., 1996, Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: possible relation to oxidative stress. J. Neurol. Sci. 143: 137.
    • (1996) J. Neurol. Sci. , vol.143 , pp. 137
    • Deibel, M.A.1    Ehmann, W.D.2    Markesbery, W.R.3
  • 69
    • 21044454884 scopus 로고    scopus 로고
    • Diagnosis and treatment of Alzheimer's disease
    • Desai, A.K. and Grossberg, G.T., 2005, Diagnosis and treatment of Alzheimer's disease. Neurology 64: S34.
    • (2005) Neurology , vol.64
    • Desai, A.K.1    Grossberg, G.T.2
  • 70
    • 0035898257 scopus 로고    scopus 로고
    • The morphological phenotype of beta-amyloid plaques and associated neuritic changes in Alzheimer's disease
    • Dickson, T.C. and Vickers, J.C., 2001, The morphological phenotype of beta-amyloid plaques and associated neuritic changes in Alzheimer's disease. Neuroscience 105: 99.
    • (2001) Neuroscience , vol.105 , pp. 99
    • Dickson, T.C.1    Vickers, J.C.2
  • 71
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence
    • Dong, J., Atwood, C.S., Anderson, V.E., Siedlak, S.L., Smith, M.A., Perry, G. and Carey, P.R., 2003, Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42: 2768.
    • (2003) Biochemistry , vol.42 , pp. 2768
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6    Carey, P.R.7
  • 72
    • 0021094370 scopus 로고
    • Tubulin-zinc interactions: Binding and polymerization studies
    • Eagle, G.R., Zombola, R.R. and Himes, R.H., 1983, Tubulin-zinc interactions: binding and polymerization studies. Biochemistry 22: 221.
    • (1983) Biochemistry , vol.22 , pp. 221
    • Eagle, G.R.1    Zombola, R.R.2    Himes, R.H.3
  • 73
    • 0037357190 scopus 로고    scopus 로고
    • Iron-induced oxidative stress modify tau phosphorylation patterns in hippocampal cell cultures
    • Egana, J.T., Zambrano, C., Nunez, M.T., Gonzalez-Billault, C. and Maccioni, R.B., 2003, Iron-induced oxidative stress modify tau phosphorylation patterns in hippocampal cell cultures. Biometals 16: 215.
    • (2003) Biometals , vol.16 , pp. 215
    • Egana, J.T.1    Zambrano, C.2    Nunez, M.T.3    Gonzalez-Billault, C.4    Maccioni, R.B.5
  • 74
    • 0041907100 scopus 로고    scopus 로고
    • The role of trace elements for the health of elderly individuals
    • Ekmekcioglu, C., 2001, The role of trace elements for the health of elderly individuals. Nahrung 45: 309.
    • (2001) Nahrung , vol.45 , pp. 309
    • Ekmekcioglu, C.1
  • 76
    • 0345258060 scopus 로고    scopus 로고
    • Copper-induced oxidative damage on astrocytes: Protective effect exerted by human high density lipoproteins
    • Ferretti, G., Bacchetti, T., Moroni, C., Vignini, A. and Curatola, G., 2003, Copper-induced oxidative damage on astrocytes: protective effect exerted by human high density lipoproteins. Biochim. Biophys. Acta 1635: 48.
    • (2003) Biochim. Biophys. Acta , vol.1635 , pp. 48
    • Ferretti, G.1    Bacchetti, T.2    Moroni, C.3    Vignini, A.4    Curatola, G.5
  • 77
    • 0031966153 scopus 로고    scopus 로고
    • Is exposure to aluminum a risk factor for the development of Alzheimer's disease? - Yes
    • Forbes, W.F. and Hill, G.B., 1998, Is exposure to aluminum a risk factor for the development of Alzheimer's disease? - Yes. Arch. Neurol. 55: 740.
    • (1998) Arch. Neurol. , vol.55 , pp. 740
    • Forbes, W.F.1    Hill, G.B.2
  • 83
    • 0031754202 scopus 로고    scopus 로고
    • Increased nuclear DNA oxidation in the brain in Alzheimer's disease
    • Gabbita, S.P., Lovell, M.A. and Markesbery, W.R., 1998, Increased nuclear DNA oxidation in the brain in Alzheimer's disease. J. Neurochem. 71: 2034.
    • (1998) J. Neurochem. , vol.71 , pp. 2034
    • Gabbita, S.P.1    Lovell, M.A.2    Markesbery, W.R.3
  • 84
    • 18244389436 scopus 로고    scopus 로고
    • The role of cerebral amyloid beta accumulation in common forms of Alzheimer's disease
    • Gandy, S., 2005, The role of cerebral amyloid beta accumulation in common forms of Alzheimer's disease. J. Clin. Invest. 115: 1121.
    • (2005) J. Clin. Invest. , vol.115 , pp. 1121
    • Gandy, S.1
  • 85
    • 0033517053 scopus 로고    scopus 로고
    • Binding of Zn(II), Cu(II), and Fe(II) ions to Alzheimer's A beta peptide studied by fluorescence
    • Garzon-Rodriguez, W., Yatsimirsky, A.K. and Glabe, C.G., 1999, Binding of Zn(II), Cu(II), and Fe(II) ions to Alzheimer's A beta peptide studied by fluorescence. Bioorg. Med. Chem. Lett. 9: 2243.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2243
    • Garzon-Rodriguez, W.1    Yatsimirsky, A.K.2    Glabe, C.G.3
  • 86
    • 0019516870 scopus 로고
    • In vitro microtubule assembly regulation by divalent cations and nucleotides
    • Gaskin, F., 1981, In vitro microtubule assembly regulation by divalent cations and nucleotides. Biochemistry 20: 1318.
    • (1981) Biochemistry , vol.20 , pp. 1318
    • Gaskin, F.1
  • 87
    • 0017663070 scopus 로고
    • Zinc ion-induced assembly of tubulin
    • Gaskin, F. and Kress, Y., 1977, Zinc ion-induced assembly of tubulin. J. Biol. Chem. 252: 6918.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6918
    • Gaskin, F.1    Kress, Y.2
  • 88
    • 0017223879 scopus 로고
    • Microtubules and intermediate filaments
    • Gaskin, F. and Shelanski, M.L., 1976, Microtubules and intermediate filaments. Essays Biochem. 12: 115.
    • (1976) Essays Biochem. , vol.12 , pp. 115
    • Gaskin, F.1    Shelanski, M.L.2
  • 89
    • 0344688272 scopus 로고    scopus 로고
    • Tau phosphorylation, tangles, and neurodegeneration: The chicken or the egg?
    • Geschwind, D.H., 2003, Tau phosphorylation, tangles, and neurodegeneration: the chicken or the egg? Neuron 40: 457.
    • (2003) Neuron , vol.40 , pp. 457
    • Geschwind, D.H.1
  • 90
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Ruth, F.X., 2003, Structural aspects of the metzincin clan of metalloendopeptidases. Mol. Biotechnol. 24: 157.
    • (2003) Mol. Biotechnol. , vol.24 , pp. 157
    • Gomis-Ruth, F.X.1
  • 92
    • 0034624014 scopus 로고    scopus 로고
    • Structural and functional differences between 3-repeat and 4-repeat tau isoforms. Implications for normal tau function and the onset of neurodegenetative disease
    • Goode, B.L., Chau, M., Denis, P.E. and Feinstein, S.C., 2000, Structural and functional differences between 3-repeat and 4-repeat tau isoforms. Implications for normal tau function and the onset of neurodegenetative disease. J. Biol. Chem. 275: 38182.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38182
    • Goode, B.L.1    Chau, M.2    Denis, P.E.3    Feinstein, S.C.4
  • 95
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell, B. and Gutteridge, J.M., 1984, Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219: 1.
    • (1984) Biochem. J. , vol.219 , pp. 1
    • Halliwell, B.1    Gutteridge, J.M.2
  • 96
    • 7244253060 scopus 로고    scopus 로고
    • Increased tau phosphorylation in apolipoprotein E4 transgenic mice is associated with activation of extracellular signal-regulated kinase: Modulation by zinc
    • Harris, F.M., Brecht, W.J., Xu, Q., Mahley, R.W. and Huang, Y., 2004, Increased tau phosphorylation in apolipoprotein E4 transgenic mice is associated with activation of extracellular signal-regulated kinase: modulation by zinc. J. Biol. Chem. 279: 44795.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44795
    • Harris, F.M.1    Brecht, W.J.2    Xu, Q.3    Mahley, R.W.4    Huang, Y.5
  • 97
    • 13444266052 scopus 로고    scopus 로고
    • Identification of a 250 kDa putative microtubule-associated protein as bovine ferritin. Evidence for a ferritin-microtubule interaction
    • Hasan, M.R., Morishima, D., Tomita, K., Katsuki, M. and Kotani, S., 2005, Identification of a 250 kDa putative microtubule-associated protein as bovine ferritin. Evidence for a ferritin-microtubule interaction. FEBS J. 272: 822.
    • (2005) FEBS J. , vol.272 , pp. 822
    • Hasan, M.R.1    Morishima, D.2    Tomita, K.3    Katsuki, M.4    Kotani, S.5
  • 98
    • 0035287432 scopus 로고    scopus 로고
    • GLIA: Listening and talking to the synapse
    • Haydon, P.G., 2001, GLIA: listening and talking to the synapse. Nat. Rev. Neurosci. 2: 185.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 185
    • Haydon, P.G.1
  • 101
    • 0020413019 scopus 로고
    • Zinc-stimulated microtubule assembly and evidence for zinc binding to tubulin
    • Hesketh, J.E., 1982, Zinc-stimulated microtubule assembly and evidence for zinc binding to tubulin. Int. J. Biochem. 14: 983.
    • (1982) Int. J. Biochem. , vol.14 , pp. 983
    • Hesketh, J.E.1
  • 102
    • 0028177269 scopus 로고
    • The beta A4 amyloid precursor protein binding to copper
    • Hesse, L., Beher, D., Masters, C.L. and Multhaup, G., 1994, The beta A4 amyloid precursor protein binding to copper. FEBS Lett. 349: 109.
    • (1994) FEBS Lett. , vol.349 , pp. 109
    • Hesse, L.1    Beher, D.2    Masters, C.L.3    Multhaup, G.4
  • 103
    • 27644482219 scopus 로고    scopus 로고
    • In vitro gamma-secretase cleavage of the Alzheimer's amyloid precursor protein correlates to a subset of presenilin complexes and is inhibited by zinc
    • Hoke, D.E., Tan, J.L., Ilaya, N.T., Culvenor, J.G., Smith, S.J., White, A.R., Masters, C.L. and Evin, G.M., 2005, In vitro gamma-secretase cleavage of the Alzheimer's amyloid precursor protein correlates to a subset of presenilin complexes and is inhibited by zinc. FEBS J. 272: 5544.
    • (2005) FEBS J. , vol.272 , pp. 5544
    • Hoke, D.E.1    Tan, J.L.2    Ilaya, N.T.3    Culvenor, J.G.4    Smith, S.J.5    White, A.R.6    Masters, C.L.7    Evin, G.M.8
  • 107
    • 12144282992 scopus 로고    scopus 로고
    • Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Abeta peptides
    • Huang, X., Atwood, C.S., Moir, R.D., Hartshorn, M.A., Tanzi, R.E. and Bush, A.I., 2004, Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Abeta peptides. J. Biol. Inorg. Chem. 9: 954.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 954
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3    Hartshorn, M.A.4    Tanzi, R.E.5    Bush, A.I.6
  • 108
    • 11144283513 scopus 로고    scopus 로고
    • Transcriptional and conformational changes of the tau molecule in Alzheimer's disease
    • Hyman, B.T., Augustinack, J.C. and Ingelsson, M., 2005, Transcriptional and conformational changes of the tau molecule in Alzheimer's disease. Biochim. Biophys. Acta 1739: 150.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 150
    • Hyman, B.T.1    Augustinack, J.C.2    Ingelsson, M.3
  • 109
    • 27444445191 scopus 로고    scopus 로고
    • Copper brain homeostasis: Role of amyloid precursor protein and prion protein
    • Inestrosa, N.C., Cerpa, W. and Varela-Nallar, L., 2005, Copper brain homeostasis: role of amyloid precursor protein and prion protein. IUBMB Life 57: 645.
    • (2005) IUBMB Life , vol.57 , pp. 645
    • Inestrosa, N.C.1    Cerpa, W.2    Varela-Nallar, L.3
  • 110
    • 0037237927 scopus 로고    scopus 로고
    • Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?
    • Ischiropoulos, H. and Beckman, J.S., 2003, Oxidative stress and nitration in neurodegeneration: cause, effect, or association? J. Clin. Invest. 111: 163.
    • (2003) J. Clin. Invest. , vol.111 , pp. 163
    • Ischiropoulos, H.1    Beckman, J.S.2
  • 111
    • 0027746084 scopus 로고
    • Concentrations of calcium, magnesium, zinc and copper in relation to free fatty acids and cholesterol in serum of atherosclerotic men
    • Iskra, M., Patelski, J. and Majewski, W., 1993, Concentrations of calcium, magnesium, zinc and copper in relation to free fatty acids and cholesterol in serum of atherosclerotic men. J. Trace Elem. Electrolytes Health Dis. 7: 185.
    • (1993) J. Trace Elem. Electrolytes Health Dis. , vol.7 , pp. 185
    • Iskra, M.1    Patelski, J.2    Majewski, W.3
  • 114
    • 0042827324 scopus 로고    scopus 로고
    • Human neprilysin is capable of degrading amyloid beta peptide not only in the monomeric form but also the pathological oligomeric form
    • Kanemitsu, H., Tomiyama, T. and Mori, H., 2003, Human neprilysin is capable of degrading amyloid beta peptide not only in the monomeric form but also the pathological oligomeric form. Neurosci. Lett. 350: 113.
    • (2003) Neurosci. Lett. , vol.350 , pp. 113
    • Kanemitsu, H.1    Tomiyama, T.2    Mori, H.3
  • 116
    • 13644278965 scopus 로고    scopus 로고
    • Agedependent and iron-independent expression of two mRNA isoforms of divalent metal transporter 1 in rat brain
    • Ke, Y., Chang, Z., Duan, X.L., Du, J.R., Zhu, L., Wang, K., Yang, X.D., Ho, K.P. and Qian, Z.M., 2005, Agedependent and iron-independent expression of two mRNA isoforms of divalent metal transporter 1 in rat brain. Neurobiol. Aging 26: 739.
    • (2005) Neurobiol. Aging , vol.26 , pp. 739
    • Ke, Y.1    Chang, Z.2    Duan, X.L.3    Du, J.R.4    Zhu, L.5    Wang, K.6    Yang, X.D.7    Ho, K.P.8    Qian, Z.M.9
  • 117
    • 0038332170 scopus 로고    scopus 로고
    • Developmental consequences of trace mineral deficiencies in rodents: Acute and long-term effects
    • Keen, C.L., Hanna, L.A., Lanoue, L., Uriu-Adams, J.Y., Rucker, R.B. and Clegg, M.S., 2003, Developmental consequences of trace mineral deficiencies in rodents: acute and long-term effects. J. Nutr. 133: 1477S.
    • (2003) J. Nutr. , vol.133
    • Keen, C.L.1    Hanna, L.A.2    Lanoue, L.3    Uriu-Adams, J.Y.4    Rucker, R.B.5    Clegg, M.S.6
  • 118
    • 25444495866 scopus 로고    scopus 로고
    • Microglia in health and disease
    • Kim, S.U. and de Vellis, J., 2005, Microglia in health and disease. J. Neurosci. Res. 81: 302.
    • (2005) J. Neurosci. Res. , vol.81 , pp. 302
    • Kim, S.U.1    De Vellis, J.2
  • 119
    • 0242382769 scopus 로고    scopus 로고
    • Oxidative modification of neurofilament-L by copper-catalyzed reaction
    • Kim, N.H. and Kang, J.H., 2003, Oxidative modification of neurofilament-L by copper-catalyzed reaction. J. Biochem. Mol. Biol. 36: 488.
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 488
    • Kim, N.H.1    Kang, J.H.2
  • 120
    • 4544350547 scopus 로고    scopus 로고
    • Oxidative modification of neurofilament-L by the Cu,Zn-superoxide dismutase and hydrogen peroxide system
    • Kim, N.H., Jeong, M.S., Choi, S.Y. and Hoon Kang, J., 2004, Oxidative modification of neurofilament-L by the Cu,Zn-superoxide dismutase and hydrogen peroxide system. Biochimie 86: 553.
    • (2004) Biochimie , vol.86 , pp. 553
    • Kim, N.H.1    Jeong, M.S.2    Choi, S.Y.3    Kang, H.J.4
  • 121
    • 0000748464 scopus 로고
    • Experimental production of neurofibrillary degeneration. I. Light microscopic observations
    • Klatzo, I., Wisniewski, H. and Streicher, E., 1965, Experimental production of neurofibrillary degeneration. I. Light microscopic observations. J. Neuropathol. Exp. Neurol. 24: 187.
    • (1965) J. Neuropathol. Exp. Neurol. , vol.24 , pp. 187
    • Klatzo, I.1    Wisniewski, H.2    Streicher, E.3
  • 124
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the genderdisparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee, J.Y., Cole, T.B., Palmiter, R.D., Suh, S.W. and Koh, J.Y., 2002, Contribution by synaptic zinc to the genderdisparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl. Acad. Sci. USA 99: 7705.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7705
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Suh, S.W.4    Koh, J.Y.5
  • 125
    • 4644238758 scopus 로고    scopus 로고
    • The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice
    • Lee, J.Y., Friedman, J.E., Angel, I., Kozak, A. and Koh, J.Y., 2004, The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice. Neurobiol. Aging 25: 1315.
    • (2004) Neurobiol. Aging , vol.25 , pp. 1315
    • Lee, J.Y.1    Friedman, J.E.2    Angel, I.3    Kozak, A.4    Koh, J.Y.5
  • 126
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring, M.A., Farris, W., Chang, A.Y., Walsh, D.M., Wu, X., Sun, X., Frosch, M.P. and Selkoe, D.J., 2003, Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40: 1087.
    • (2003) Neuron , vol.40 , pp. 1087
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 127
    • 0030788672 scopus 로고    scopus 로고
    • Iron deposits in multiple sclerosis and Alzheimer's disease brains
    • LeVine, S.M., 1997, Iron deposits in multiple sclerosis and Alzheimer's disease brains. Brain Res. 760: 298.
    • (1997) Brain Res. , vol.760 , pp. 298
    • Levine, S.M.1
  • 128
    • 0345240924 scopus 로고    scopus 로고
    • Combined enhancement of microtubule assembly and glucose metabolism in neuronal systems in vitro: Decreased sensitivity to copper toxicity
    • Liliom, K., Wagner, G., Kovacs, J., Comin, B., Cascante, M., Orosz, F. and Ovadi, J., 1999, Combined enhancement of microtubule assembly and glucose metabolism in neuronal systems in vitro: decreased sensitivity to copper toxicity. Biochem. Biophys. Res. Commun. 264: 605.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 605
    • Liliom, K.1    Wagner, G.2    Kovacs, J.3    Comin, B.4    Cascante, M.5    Orosz, F.6    Ovadi, J.7
  • 129
    • 0027244133 scopus 로고
    • Oxidative inactivation of plasmin and other serine proteases by copper and ascorbate
    • Lind, S.E., McDonagh, J.R. and Smith, C.J., 1993, Oxidative inactivation of plasmin and other serine proteases by copper and ascorbate. Blood 82: 1522.
    • (1993) Blood , vol.82 , pp. 1522
    • Lind, S.E.1    McDonagh, J.R.2    Smith, C.J.3
  • 130
    • 0015086876 scopus 로고
    • Influence of age and sex on plasma and red-cell zinc concentrations
    • Lindeman, R.D., Clark, M.L. and Colmore, J.P., 1971, Influence of age and sex on plasma and red-cell zinc concentrations. J. Gerontol. 26: 358.
    • (1971) J. Gerontol. , vol.26 , pp. 358
    • Lindeman, R.D.1    Clark, M.L.2    Colmore, J.P.3
  • 131
    • 0038343343 scopus 로고    scopus 로고
    • Amyloid precursor protein (APP) and the biology of proteolytic processing: Relevance to Alzheimer's disease
    • Ling, Y., Morgan, K. and Kalsheker, N., 2003, Amyloid precursor protein (APP) and the biology of proteolytic processing: relevance to Alzheimer's disease. Int. J. Biochem. Cell Biol. 35: 1505.
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 1505
    • Ling, Y.1    Morgan, K.2    Kalsheker, N.3
  • 132
    • 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. and Barrow, C.J., 1999, Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease. Biochemistry 38: 9373.
    • (1999) Biochemistry , vol.38 , pp. 9373
    • Liu, S.T.1    Howlett, G.2    Barrow, C.J.3
  • 133
    • 0034789533 scopus 로고    scopus 로고
    • Relationship of the extended tau haplotype to tau biochemistry and neuropathology in progressive supranuclear palsy
    • Liu, W.K., Le, T.V., Adamson, J., Baker, M., Cookson, N., Hardy, J., Hutton, M., Yen, S.H. and Dickson, D.W., 2001, Relationship of the extended tau haplotype to tau biochemistry and neuropathology in progressive supranuclear palsy. Ann. Neurol. 50: 494.
    • (2001) Ann. Neurol. , vol.50 , pp. 494
    • Liu, W.K.1    Le, T.V.2    Adamson, J.3    Baker, M.4    Cookson, N.5    Hardy, J.6    Hutton, M.7    Yen, S.H.8    Dickson, D.W.9
  • 137
    • 27744545492 scopus 로고    scopus 로고
    • Alterations in zinc transporter protein-1 (ZnT-1) in the brain of subjects with mild cognitive impairment, early, and late-stage Alzheimer's disease
    • Lovell, M.A., Smith, J.L., Xiong, S. and Markesbery, W.R., 2005, Alterations in zinc transporter protein-1 (ZnT-1) in the brain of subjects with mild cognitive impairment, early, and late-stage Alzheimer's disease. Neurotox. Res. 7: 265.
    • (2005) Neurotox. Res. , vol.7 , pp. 265
    • Lovell, M.A.1    Smith, J.L.2    Xiong, S.3    Markesbery, W.R.4
  • 140
    • 0037802583 scopus 로고    scopus 로고
    • Function and regulation of the mammalian copper-transporting ATPases: Insights from biochemical and cell biological approaches
    • Lutsenko, S. and Petris, M.J., 2003, Function and regulation of the mammalian copper-transporting ATPases: insights from biochemical and cell biological approaches. J. Membr. Biol. 191: 1.
    • (2003) J. Membr. Biol. , vol.191 , pp. 1
    • Lutsenko, S.1    Petris, M.J.2
  • 141
    • 27744565566 scopus 로고    scopus 로고
    • Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI-TOF MS, CD, and NMR
    • Ma, Q.F., Li, Y.M., Du, J.T., Kanazawa, K., Nemoto, T., Nakanishi, H. and Zhao, Y.F., 2005, Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI-TOF MS, CD, and NMR. Biopolymers 79: 74.
    • (2005) Biopolymers , vol.79 , pp. 74
    • Ma, Q.F.1    Li, Y.M.2    Du, J.T.3    Kanazawa, K.4    Nemoto, T.5    Nakanishi, H.6    Zhao, Y.F.7
  • 142
    • 33645407628 scopus 로고    scopus 로고
    • Copper binding properties of a tau peptide associated with Alzheimer's disease studied by CD, NMR, and MALDI-TOF MS
    • Ma, Q., Li, Y., Du, J., Liu, H., Kanazawa, K., Nemoto, T., Nakanishi, H. and Zhao, Y., 2006, Copper binding properties of a tau peptide associated with Alzheimer's disease studied by CD, NMR, and MALDI-TOF MS. Peptides 27: 841.
    • (2006) Peptides , vol.27 , pp. 841
    • Ma, Q.1    Li, Y.2    Du, J.3    Liu, H.4    Kanazawa, K.5    Nemoto, T.6    Nakanishi, H.7    Zhao, Y.8
  • 143
    • 0027974414 scopus 로고
    • Serum copper, zinc, and copper/zinc ratio in males: Influence of aging
    • Madaric, A., Ginter, E. and Kadrabova, J., 1994, Serum copper, zinc, and copper/zinc ratio in males: influence of aging. Physiol. Res. 43: 107
    • (1994) Physiol. Res. , vol.43 , pp. 107
    • Madaric, A.1    Ginter, E.2    Kadrabova, J.3
  • 145
    • 0027275017 scopus 로고
    • Changes in plasma copper and zinc during rat development
    • Martinez Lista, E., Sole, J., Arola, L. and Mas, A., 1993, Changes in plasma copper and zinc during rat development. Biol. Neonate. 64: 47.
    • (1993) Biol. Neonate. , vol.64 , pp. 47
    • Martinez Lista, E.1    Sole, J.2    Arola, L.3    Mas, A.4
  • 146
    • 3943092621 scopus 로고    scopus 로고
    • Pathways toward and away from Alzheimer's disease
    • Mattson, M.P., 2004, Pathways toward and away from Alzheimer's disease. Nature 430: 631.
    • (2004) Nature , vol.430 , pp. 631
    • Mattson, M.P.1
  • 147
    • 0034612075 scopus 로고    scopus 로고
    • A selective defect of cytochrome c oxidase is present in brain of Alzheimer's disease patients
    • Maurer, I., Zierz, S. and Moller, H.J., 2000, A selective defect of cytochrome c oxidase is present in brain of Alzheimer's disease patients. Neurobiol. Aging 21: 455.
    • (2000) Neurobiol. Aging , vol.21 , pp. 455
    • Maurer, I.1    Zierz, S.2    Moller, H.J.3
  • 152
    • 0027858985 scopus 로고
    • Association of serum copper and zinc with serum electrolytes and with selected risk factors for cardiovascular disease in men aged 55-75 years. NFR Study Group
    • Menditto, A., Morisi, G., Alimonti, A., Caroli, S., Petrucci F., Spagnolo, A. and Menotti, A., 1993, Association of serum copper and zinc with serum electrolytes and with selected risk factors for cardiovascular disease in men aged 55-75 years. NFR Study Group. J. Trace Elem. Electrolytes Health Dis. 7: 251.
    • (1993) J. Trace Elem. Electrolytes Health Dis. , vol.7 , pp. 251
    • Menditto, A.1    Morisi, G.2    Alimonti, A.3    Caroli, S.4    Petrucci, F.5    Spagnolo, A.6    Menotti, A.7
  • 153
    • 0027315752 scopus 로고
    • Assessment of copper status: Effect of age and gender on reference ranges in healthy adults
    • Milne, D.B. and Johnson, P.E., 1993, Assessment of copper status: effect of age and gender on reference ranges in healthy adults. Clin. Chem. 39: 883.
    • (1993) Clin. Chem. , vol.39 , pp. 883
    • Milne, D.B.1    Johnson, P.E.2
  • 154
    • 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. and Takeuchi, H., 2000, Metal binding
    • (2000) Biochemistry , vol.39 , pp. 7024
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 158
    • 0028694082 scopus 로고
    • Nonhaem iron histochemistry of the normal and Alzheimer's disease hippocampus
    • Morris, C.M., Kerwin, J.M. and Edwardson, J.A., 1994, Nonhaem iron histochemistry of the normal and Alzheimer's disease hippocampus. Neurodegeneration 3: 267.
    • (1994) Neurodegeneration , vol.3 , pp. 267
    • Morris, C.M.1    Kerwin, J.M.2    Edwardson, J.A.3
  • 160
    • 11444256801 scopus 로고    scopus 로고
    • Glia and their cytokines in progression of neurodegeneration
    • Mrak, R.E. and Griffin, S.W., 2005, Glia and their cytokines in progression of neurodegeneration. Neurobiol. Aging 26: 349.
    • (2005) Neurobiol. Aging , vol.26 , pp. 349
    • Mrak, R.E.1    Griffin, S.W.2
  • 162
    • 0027984643 scopus 로고
    • Interaction between the zinc (II) and the heparin binding site of the Alzheimer's disease beta A4 amyloid precursor protein (APP)
    • Multhaup, G., Bush, A.I., Pollwein, P. and Masters, C.L., 1994, Interaction between the zinc (II) and the heparin binding site of the Alzheimer's disease beta A4 amyloid precursor protein (APP). FEBS Lett. 355: 151.
    • (1994) FEBS Lett. , vol.355 , pp. 151
    • Multhaup, G.1    Bush, A.I.2    Pollwein, P.3    Masters, C.L.4
  • 163
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)
    • Multhaup, G., Schlicksupp, A., Hesse, L., Beher, D., Ruppert, T., Masters, C.L. and Beyreuther, K., 1996, The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I). Science 271: 1406.
    • (1996) Science , vol.271 , pp. 1406
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 164
    • 0031978192 scopus 로고    scopus 로고
    • Is exposure to aluminum a risk factor for the development of Alzheimer disease? - No
    • Munoz, D.G., 1998, Is exposure to aluminum a risk factor for the development of Alzheimer disease? - No. Arch. Neurol. 55: 737.
    • (1998) Arch. Neurol. , vol.55 , pp. 737
    • Munoz, D.G.1
  • 166
    • 0037427384 scopus 로고    scopus 로고
    • Astrocytes accumulate A beta 42 and give rise to astrocytic amyloid plaques in Alzheimer's disease brains
    • Nagele, R.G., D'Andrea, M.R., Lee, H., Venkataraman, V. and Wang, H.Y., 2003, Astrocytes accumulate A beta 42 and give rise to astrocytic amyloid plaques in Alzheimer's disease brains. Brain Res. 971: 197.
    • (2003) Brain Res. , vol.971 , pp. 197
    • Nagele, R.G.1    D'andrea, M.R.2    Lee, H.3    Venkataraman, V.4    Wang, H.Y.5
  • 167
    • 2542481651 scopus 로고    scopus 로고
    • Contribution of glial cells to the development of amyloid plaques in Alzheimer's disease
    • Nagele, R.G., Wegiel, J., Venkataraman, V., Imaki, H. and Wang, K.C., 2004, Contribution of glial cells to the development of amyloid plaques in Alzheimer's disease. Neurobiol. Aging 25: 663.
    • (2004) Neurobiol. Aging , vol.25 , pp. 663
    • Nagele, R.G.1    Wegiel, J.2    Venkataraman, V.3    Imaki, H.4    Wang, K.C.5
  • 169
    • 0000629630 scopus 로고    scopus 로고
    • Amyloid-beta-peptide reduces copper(II) to copper(I) independent of its aggregation state
    • Opazo, C., Ruiz, F.H. and Inestrosa, N.C., 2000, Amyloid-beta-peptide reduces copper(II) to copper(I) independent of its aggregation state. Biol. Res. 33: 125.
    • (2000) Biol. Res. , vol.33 , pp. 125
    • Opazo, C.1    Ruiz, F.H.2    Inestrosa, N.C.3
  • 170
    • 0037174856 scopus 로고    scopus 로고
    • Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cudependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H2O2
    • Opazo, C., Huang, X., Cherny, R.A., Moir, R.D., Roher, A.E., White, A.R., Cappai, R., Masters, C.L., Tanzi, R.E., Inestrosa, N.C. and Bush, A.I., 2002, Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cudependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H2O2. J. Biol. Chem. 277: 40302.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40302
    • Opazo, C.1    Huang, X.2    Cherny, R.A.3    Moir, R.D.4    Roher, A.E.5    White, A.R.6    Cappai, R.7    Masters, C.L.8    Tanzi, R.E.9    Inestrosa, N.C.10    Bush, A.I.11
  • 172
    • 0025139904 scopus 로고
    • Influence of maternal dietary zinc intake on in vitro tubulin polymerization in fetal rat brain
    • Oteiza, P.I., Cuellar, S., Lonnerdal, B., Hurley, L.S. and Keen, C.L., 1990a, Influence of maternal dietary zinc intake on in vitro tubulin polymerization in fetal rat brain. Teratology 41: 97.
    • (1990) Teratology , vol.41 , pp. 97
    • Oteiza, P.I.1    Cuellar, S.2    Lonnerdal, B.3    Hurley, L.S.4    Keen, C.L.5
  • 173
    • 0025180988 scopus 로고
    • Effects of marginal zinc deficiency on microtubule polymerization in the developing rat brain
    • Oteiza, P.I., Hurley, L.S., Lonnerdal, B. and Keen, C.L., 1990b, Effects of marginal zinc deficiency on microtubule polymerization in the developing rat brain. Biol. Trace Elem. Res. 24: 13.
    • (1990) Biol. Trace Elem. Res. , vol.24 , pp. 13
    • Oteiza, P.I.1    Hurley, L.S.2    Lonnerdal, B.3    Keen, C.L.4
  • 174
    • 0026823074 scopus 로고
    • Immunohistochemical evidence of oxidative (corrected) stress in Alzheimer's disease
    • Pappolla, M.A., Omar, R.A., Kim, K.S. and Robakis, N.K., 1992, Immunohistochemical evidence of oxidative (corrected) stress in Alzheimer's disease. Am. J. Pathol. 140: 621.
    • (1992) Am. J. Pathol. , vol.140 , pp. 621
    • Pappolla, M.A.1    Omar, R.A.2    Kim, K.S.3    Robakis, N.K.4
  • 175
    • 0034811346 scopus 로고    scopus 로고
    • Zinc enhances synthesis of presenilin 1 in mouse primary cortical culture
    • Park, I.H., Jung, M.W., Mori, H. and Mook-Jung, I., 2001, Zinc enhances synthesis of presenilin 1 in mouse primary cortical culture. Biochem. Biophys Res. Commun. 285: 680.
    • (2001) Biochem. Biophys Res. Commun. , vol.285 , pp. 680
    • Park, I.H.1    Jung, M.W.2    Mori, H.3    Mook-Jung, I.4
  • 178
    • 4544335597 scopus 로고    scopus 로고
    • Mild cognitive impairment as a diagnostic entity
    • Petersen, R.C., 2004, Mild cognitive impairment as a diagnostic entity. J. Intern. Med. 256: 183.
    • (2004) J. Intern. Med. , vol.256 , pp. 183
    • Petersen, R.C.1
  • 182
    • 51249175720 scopus 로고
    • Trace elements in the human central nervous system studied with neutron activation analysis
    • Plantin, L.-O., Lysing-Tunnell, U. and Kristensson, K., 1987, Trace elements in the human central nervous system studied with neutron activation analysis. Biol. Trace Elem. Res. 13: 69.
    • (1987) Biol. Trace Elem. Res. , vol.13 , pp. 69
    • Plantin, L.-O.1    Lysing-Tunnell, U.2    Kristensson, K.3
  • 184
    • 2442471606 scopus 로고    scopus 로고
    • Intracellular copper transport in mammals
    • Prohaska, J.R. and Gybina, A.A., 2004, Intracellular copper transport in mammals. J. Nutr. 134: 1003.
    • (2004) J. Nutr. , vol.134 , pp. 1003
    • Prohaska, J.R.1    Gybina, A.A.2
  • 186
    • 20444401173 scopus 로고    scopus 로고
    • Tetanically released zinc inhibits hippocampal mossy fiber calcium, zinc, and synaptic responses
    • Quinta-Ferreira, M.E. and Matias, C.M., 2005, Tetanically released zinc inhibits hippocampal mossy fiber calcium, zinc, and synaptic responses. Brain Res. 1047: 1.
    • (2005) Brain Res. , vol.1047 , pp. 1
    • Quinta-Ferreira, M.E.1    Matias, C.M.2
  • 187
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • Rae, T.D., Schmidt, P.J., Pufahl, R.A., Culotta, V.C. and O'Halloran, T.V., 1999, Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284: 805.
    • (1999) Science , vol.284 , pp. 805
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'halloran, T.V.5
  • 189
    • 18144374793 scopus 로고    scopus 로고
    • Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid-beta peptide
    • Raman, B., Ban, T., Yamaguchi, K., Sakai, M., Kawai, T., Naiki, H. and Goto, Y., 2005, Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid-beta peptide. J. Biol. Chem. 280: 16157.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16157
    • Raman, B.1    Ban, T.2    Yamaguchi, K.3    Sakai, M.4    Kawai, T.5    Naiki, H.6    Goto, Y.7
  • 192
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid-beta precursor protein: Integrating structure with biological function
    • Reinhard, C., Hebert, S.S. and De Strooper, B., 2005, The amyloid-beta precursor protein: integrating structure with biological function. EMBO J. 24: 3996.
    • (2005) EMBO J. , vol.24 , pp. 3996
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3
  • 195
    • 30644479192 scopus 로고    scopus 로고
    • Clinical aspects of inflammation in Alzheimer's disease
    • Rosenberg, P.B., 2005, Clinical aspects of inflammation in Alzheimer's disease. Int. Rev. Psychiatry 17: 503.
    • (2005) Int. Rev. Psychiatry , vol.17 , pp. 503
    • Rosenberg, P.B.1
  • 197
    • 0345035452 scopus 로고    scopus 로고
    • Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein
    • Ruiz, F.H., Gonzalez, M., Bodini, M., Opazo, C. and Inestrosa, N.C., 1999, Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein. J. Neurochem. 73: 1288.
    • (1999) J. Neurochem. , vol.73 , pp. 1288
    • Ruiz, F.H.1    Gonzalez, M.2    Bodini, M.3    Opazo, C.4    Inestrosa, N.C.5
  • 198
    • 0030030030 scopus 로고    scopus 로고
    • Increased antioxidant enzyme activity in amyloid beta protein-resistant cells
    • Sagara, Y., Dargusch, R., Klier, F.G., Schubert, D. and Behl, C., 1996, Increased antioxidant enzyme activity in amyloid beta protein-resistant cells. J. Neurosci. 16: 497.
    • (1996) J. Neurosci. , vol.16 , pp. 497
    • Sagara, Y.1    Dargusch, R.2    Klier, F.G.3    Schubert, D.4    Behl, C.5
  • 199
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • Sayre, L.M., Perry, G., Harris, P.L., Liu, Y., Schubert, K.A. and Smith, M.A., 2000, In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals. J. Neurochem. 74: 270.
    • (2000) J. Neurochem. , vol.74 , pp. 270
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 201
    • 12144257164 scopus 로고    scopus 로고
    • NMDA receptor activation mediates copper homeostasis in hippocampal neurons
    • Schlief, M.L., Craig, A.M. and Gitlin, J.D., 2005, NMDA receptor activation mediates copper homeostasis in hippocampal neurons. J. Neurosci. 25: 239.
    • (2005) J. Neurosci. , vol.25 , pp. 239
    • Schlief, M.L.1    Craig, A.M.2    Gitlin, J.D.3
  • 202
    • 2542558147 scopus 로고    scopus 로고
    • Spatial and temporal relationships between plaques and tangles in Alzheimer-pathology
    • Schonheit, B., Zarski, R. and Ohm, T.G., 2004, Spatial and temporal relationships between plaques and tangles in Alzheimer-pathology. Neurobiol. Aging 25: 697.
    • (2004) Neurobiol. Aging , vol.25 , pp. 697
    • Schonheit, B.1    Zarski, R.2    Ohm, T.G.3
  • 205
    • 0036224435 scopus 로고    scopus 로고
    • The effect of increased concentrations of homocysteine on the concentration of (E)-4-hydroxy-2-nonenal in the plasma and cerebrospinal fluid of patients with Alzheimer's disease
    • Selley, M.L., Close, D.R. and Stern, S.E., 2002, The effect of increased concentrations of homocysteine on the concentration of (E)-4-hydroxy-2-nonenal in the plasma and cerebrospinal fluid of patients with Alzheimer's disease. Neurobiol. Aging 23: 383.
    • (2002) Neurobiol. Aging , vol.23 , pp. 383
    • Selley, M.L.1    Close, D.R.2    Stern, S.E.3
  • 206
    • 0023682156 scopus 로고
    • Identification of zinc-binding sites of proteins: Zinc binds to the amino-terminal region of tubulin
    • Serrano, L., Dominguez, J.E. and Avila, J., 1988, Identification of zinc-binding sites of proteins: zinc binds to the amino-terminal region of tubulin. Anal. Biochem. 172: 210.
    • (1988) Anal. Biochem. , vol.172 , pp. 210
    • Serrano, L.1    Dominguez, J.E.2    Avila, J.3
  • 207
    • 27944440133 scopus 로고    scopus 로고
    • Susceptibility of amyloid β peptide degrading enzymes to oxidative damage: A potential Alzheimer's disease spiral
    • Shinall, H., Song, E.S. and Hersh, L.B., 2005, Susceptibility of amyloid β peptide degrading enzymes to oxidative damage: a potential Alzheimer's disease spiral. Biochemistry 44: 15345.
    • (2005) Biochemistry , vol.44 , pp. 15345
    • Shinall, H.1    Song, E.S.2    Hersh, L.B.3
  • 208
    • 0024005801 scopus 로고
    • Alzheimer's disease amyloidogenic glycoprotein: Expression pattern in rat brain suggests a role in cell contact
    • Shivers, B.D., Hilbich, C., Multhaup, G., Salbaum, M., Beyreuther, K. and Seeburg, P.H., 1988, Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact. EMBO J. 7: 1365.
    • (1988) EMBO J. , vol.7 , pp. 1365
    • Shivers, B.D.1    Hilbich, C.2    Multhaup, G.3    Salbaum, M.4    Beyreuther, K.5    Seeburg, P.H.6
  • 212
    • 0141702360 scopus 로고    scopus 로고
    • Trace amounts of copper in water induce beta-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease
    • Sparks, D.L. and Schreurs, B.G., 2003, Trace amounts of copper in water induce beta-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 100: 11065.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11065
    • Sparks, D.L.1    Schreurs, B.G.2
  • 213
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier, T.C., 2001, Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. 36: 1539.
    • (2001) Exp. Gerontol. , vol.36 , pp. 1539
    • Squier, T.C.1
  • 216
    • 3042845492 scopus 로고    scopus 로고
    • Microglia and Alzheimer's disease pathogenesis
    • Streit, W.J., 2004, Microglia and Alzheimer's disease pathogenesis. J. Neurosci. Res. 77: 1.
    • (2004) J. Neurosci. Res. , vol.77 , pp. 1
    • Streit, W.J.1
  • 217
    • 0033986037 scopus 로고    scopus 로고
    • Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains
    • Suh, S.W., Jensen, K.B., Jensen, M.S., Silva, D.S., Kesslak, P.J., Danscher, G. and Frederickson, C.J., 2000, Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains. Brain Res. 852: 274.
    • (2000) Brain Res. , vol.852 , pp. 274
    • Suh, S.W.1    Jensen, K.B.2    Jensen, M.S.3    Silva, D.S.4    Kesslak, P.J.5    Danscher, G.6    Frederickson, C.J.7
  • 218
    • 0036736218 scopus 로고    scopus 로고
    • Amyloid precursor protein, presenilins, and alpha-synuclein: Molecular pathogenesis and pharmacological applications in Alzheimer's disease
    • Suh, Y.H. and Checler, F., 2002, Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease. Pharmacol. Rev. 54: 469.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 469
    • Suh, Y.H.1    Checler, F.2
  • 220
    • 2442461177 scopus 로고    scopus 로고
    • Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: Folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): Insights from a range of complementary spectroscopic techniques
    • Syme, C.D., Nadal, R.C., Rigby, S.E. and Viles, J.H., 2004, Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques. J. Biol. Chem. 279: 18169.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18169
    • Syme, C.D.1    Nadal, R.C.2    Rigby, S.E.3    Viles, J.H.4
  • 221
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypo thesis: A genetic perspective
    • Tanzi, R.E. and Bertram, L., 2005, Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120: 545.
    • (2005) Cell , vol.120 , pp. 545
    • Tanzi, R.E.1    Bertram, L.2
  • 222
    • 16544372917 scopus 로고    scopus 로고
    • Regional distribution of manganese, iron, copper, and zinc in the rat brain during development
    • Tarohda, T., Yamamoto, M. and Amamo, R., 2004, Regional distribution of manganese, iron, copper, and zinc in the rat brain during development. Anal. Bioanal. Chem. 380: 240.
    • (2004) Anal. Bioanal. Chem. , vol.380 , pp. 240
    • Tarohda, T.1    Yamamoto, M.2    Amamo, R.3
  • 223
    • 0029795197 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimer's disease: An alternative to the amyloid hypothesis
    • Terry, R.D., 1996, The pathogenesis of Alzheimer's disease: an alternative to the amyloid hypothesis. J. Neuropathol. Exp. Neurol. 55: 1023.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 1023
    • Terry, R.D.1
  • 224
    • 0016561975 scopus 로고
    • Structural and chemical changes of the aged human brain
    • Terry, R.D. and Wisniewski, H.M., 1975, Structural and chemical changes of the aged human brain. Psychopharmacol. Bull. 11: 46.
    • (1975) Psychopharmacol. Bull. , vol.11 , pp. 46
    • Terry, R.D.1    Wisniewski, H.M.2
  • 225
    • 10644280708 scopus 로고    scopus 로고
    • Clioquinol mediates copper uptake and counteracts copper efflux activities of the amyloid precursor protein of Alzheimer's disease
    • Treiber, C., Simons, A., Strauss, M., Hafner, M., Cappai, R., Bayer, T.A. and Multhaup, G., 2004, Clioquinol mediates copper uptake and counteracts copper efflux activities of the amyloid precursor protein of Alzheimer's disease. J. Biol. Chem. 279: 51958.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51958
    • Treiber, C.1    Simons, A.2    Strauss, M.3    Hafner, M.4    Cappai, R.5    Bayer, T.A.6    Multhaup, G.7
  • 226
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
    • Uchida, Y., Takio, K., Titani, K., Ihara, Y. and Tomonaga, M., 1991, The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein. Neuron 7: 337.
    • (1991) Neuron , vol.7 , pp. 337
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 228
    • 18544371009 scopus 로고    scopus 로고
    • Metals, toxicity, and oxidative stress
    • Valko, M., Morris, H. and Cronin, M.T., 2005, Metals, toxicity, and oxidative stress. Curr. Med. Chem. 12: 1161.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1161
    • Valko, M.1    Morris, H.2    Cronin, M.T.3
  • 230
    • 14944344156 scopus 로고    scopus 로고
    • The integrated role of desferrioxamine and phenserine targeted to an iron-responsive element in the APP-mRNA 5?-untranslated region
    • Venti, A., Giordano, T., Eder, P., Bush, A.I., Lahiri, D.K., Greig, N.H. and Rogers, J.T., 2004, The integrated role of desferrioxamine and phenserine targeted to an iron-responsive element in the APP-mRNA 5?-untranslated region. Ann. NY Acad. Sci. 1035: 34.
    • (2004) Ann. NY Acad. Sci. , vol.1035 , pp. 34
    • Venti, A.1    Giordano, T.2    Eder, P.3    Bush, A.I.4    Lahiri, D.K.5    Greig, N.H.6    Rogers, J.T.7
  • 232
    • 0025175970 scopus 로고
    • Survival of outpatients with Alzheimer-type dementia
    • Walsh, J.S., Welch, H.G. and Larson, E.B., 1990, Survival of outpatients with Alzheimer-type dementia. Ann. Intern. Med. 113: 429.
    • (1990) Ann. Intern. Med. , vol.113 , pp. 429
    • Walsh, J.S.1    Welch, H.G.2    Larson, E.B.3
  • 233
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D.M., Klyubin, I., Fadeeva, J.V., Cullen, W.K., Anwyl, R., Wolfe, M.S., Rowan, M.J. and Selkoe, D.J., 2002a, Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535.
    • (2002) Nature , vol.416 , pp. 535
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 235
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging
    • Wang, J., Dickson, D.W., Trojanowski, J.Q. and Lee, V.M., 1999, The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging. Exp. Neurol. 158: 328.
    • (1999) Exp. Neurol. , vol.158 , pp. 328
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 237
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer's disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • Wang, Q., Woltjer, R.L., Cimino, P.J., Pan, C., Montine, K.S., Zhang, J. and Montine, T.J., 2005, Proteomic analysis of neurofibrillary tangles in Alzheimer's disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J. 19: 869.
    • (2005) FASEB J. , vol.19 , pp. 869
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4    Montine, K.S.5    Zhang, J.6    Montine, T.J.7
  • 238
    • 0015520152 scopus 로고
    • Microtubule formation in vitro in solutions containing low calcium concentrations
    • Weisenberg, R.C., 1972, Microtubule formation in vitro in solutions containing low calcium concentrations. Science 177: 1104.
    • (1972) Science , vol.177 , pp. 1104
    • Weisenberg, R.C.1
  • 239
    • 10344245544 scopus 로고    scopus 로고
    • Cumulative lead exposure and prospective change in cognition among elderly men: The VA normative aging study
    • Weisskopf, M.G., Wright, R.O., Schwartz, J., Spiro, A. 3rd, Sparrow, D., Aro, A. and Hu, H., 2004, Cumulative lead exposure and prospective change in cognition among elderly men: the VA normative aging study. Am. J. Epidemiol. 160: 1184.
    • (2004) Am. J. Epidemiol. , vol.160 , pp. 1184
    • Weisskopf, M.G.1    Wright, R.O.2    Schwartz, J.3    Spiro III, A.4    Sparrow, D.5    Aro, A.6    Hu, H.7
  • 240
    • 0027022662 scopus 로고
    • Electron paramagnetic resonance analysis of heavy metals in the aging human brain
    • Wender, M., Szczech, J., Hoffmann, S. and Hilczer, W., 1992, Electron paramagnetic resonance analysis of heavy metals in the aging human brain. Neuropatol. Pol. 30: 65.
    • (1992) Neuropatol. Pol. , vol.30 , pp. 65
    • Wender, M.1    Szczech, J.2    Hoffmann, S.3    Hilczer, W.4
  • 242
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille, H., Drewes, G., Biernat, J., Mandelkow, E.M. and Mandelkow, E., 1992, Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J. Cell Biol. 118: 573.
    • (1992) J. Cell Biol. , vol.118 , pp. 573
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 244
    • 0036724204 scopus 로고    scopus 로고
    • Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: Implications in the formation of neurofibrillary tangles of Alzheimer's disease
    • Yamamoto, A., Shin, R.W., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F. and Kitamoto, T., 2002, Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease. J. Neurochem. 82: 1137.
    • (2002) J. Neurochem. , vol.82 , pp. 1137
    • Yamamoto, A.1    Shin, R.W.2    Hasegawa, K.3    Naiki, H.4    Sato, H.5    Yoshimasu, F.6    Kitamoto, T.7
  • 250
    • 0024490143 scopus 로고
    • Superoxide dismutase activity in Alzheimer's disease: Possible mechanism for paired helical filament formation
    • Zemlan, F.P., Thienhaus, O.J. and Bosmann, H.B., 1989, Superoxide dismutase activity in Alzheimer's disease: possible mechanism for paired helical filament formation. Brain Res. 476: 160.
    • (1989) Brain Res. , vol.476 , pp. 160
    • Zemlan, F.P.1    Thienhaus, O.J.2    Bosmann, H.B.3
  • 251
    • 27844441278 scopus 로고    scopus 로고
    • Gamma-cleavage is dependent on zetacleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain
    • Zhao, G., Cui, M.Z., Mao, G., Dong, Y., Tan, J., Sun, L. and Xu, X., 2005, Gamma-cleavage is dependent on zetacleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain. J. Biol. Chem. 280: 37689.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37689
    • Zhao, G.1    Cui, M.Z.2    Mao, G.3    Dong, Y.4    Tan, J.5    Sun, L.6    Xu, X.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.