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Volumn 3, Issue 3, 2004, Pages 205-214

Neurodegenerative diseases and oxidatives stress

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TOCOPHEROL; AMANTADINE; AMYLOID PRECURSOR PROTEIN; ANTIOXIDANT; CATALASE; CLIOQUINOL; COPPER; DEFEROXAMINE; DOPAMINE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; MEMANTINE; NEUROTROPHIN; OXYGEN; REACTIVE OXYGEN METABOLITE; RILUZOLE; SUPEROXIDE DISMUTASE; TRIENTINE; METAL;

EID: 1642308134     PISSN: 14741776     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrd1330     Document Type: Review
Times cited : (3057)

References (137)
  • 1
    • 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. & Stern, S. E. 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, 383-388 (2002).
    • (2002) Neurobiol. Aging , vol.23 , pp. 383-388
    • Selley, M.L.1    Close, D.R.2    Stern, S.E.3
  • 2
    • 0036753272 scopus 로고    scopus 로고
    • Evidence that amyloid β-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
    • Butterfield, D. A., Castegna, A., Lauderback, C. M. & Drake, J. Evidence that amyloid β-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death. Neurobiol. Aging 23, 655-664 (2002).
    • (2002) Neurobiol. Aging , vol.23 , pp. 655-664
    • Butterfield, D.A.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 3
    • 0024585155 scopus 로고
    • Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease
    • Dexter, D. T. et al. Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease. J. Neurochem. 52, 381-389 (1989).
    • (1989) J. Neurochem. , vol.52 , pp. 381-389
    • Dexter, D.T.1
  • 4
    • 0031768026 scopus 로고    scopus 로고
    • Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients
    • Pedersen, W. A. et al. Protein modification by the lipid peroxidation product 4-hydroxynonenal in the spinal cords of amyotrophic lateral sclerosis patients. Ann. Neurol. 44, 819-824 (1998).
    • (1998) Ann. Neurol. , vol.44 , pp. 819-824
    • Pedersen, W.A.1
  • 5
    • 0035985698 scopus 로고    scopus 로고
    • Lipid peroxidation in neurodegeneration: New insights into Alzheimer's disease
    • Arlt, S., Beisiegel, U. & Kontush, A. Lipid peroxidation in neurodegeneration: New insights into Alzheimer's disease. Curr. Opin. Lipidol. 13, 289-294 (2002).
    • (2002) Curr. Opin. Lipidol. , vol.13 , pp. 289-294
    • Arlt, S.1    Beisiegel, U.2    Kontush, A.3
  • 6
    • 0035003439 scopus 로고    scopus 로고
    • Chemistry and biochemistry of oxidative stress in neurodegenerative disease
    • Sayre, L. M., Smith, M. A. & Perry, G. Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr. Med. Chem. 8, 721-738 (2001).
    • (2001) Curr. Med. Chem. , vol.8 , pp. 721-738
    • Sayre, L.M.1    Smith, M.A.2    Perry, G.3
  • 7
    • 0031754202 scopus 로고    scopus 로고
    • Increased nuclear DNA oxidation in the brain in Alzheimer's disease
    • Gabbita, S. P., Lovell, M. A. & Markesbery, W. R. Increased nuclear DNA oxidation in the brain in Alzheimer's disease. J. Neurochem. 71, 2034-2040 (1998).
    • (1998) J. Neurochem. , vol.71 , pp. 2034-2040
    • Gabbita, S.P.1    Lovell, M.A.2    Markesbery, W.R.3
  • 8
    • 0030878073 scopus 로고    scopus 로고
    • Oxidative DNA damage in the parkinsonian brain: An apparent selective increase in 8-hydroxyguanine levels in substantia nigra
    • Adam, Z. I. et al. Oxidative DNA damage in the parkinsonian brain: An apparent selective increase in 8-hydroxyguanine levels in substantia nigra. J. Neurochem. 69, 1196-1203 (1997).
    • (1997) J. Neurochem. , vol.69 , pp. 1196-1203
    • Adam, Z.I.1
  • 9
    • 0024490143 scopus 로고
    • Superoxide dismutase activity in Alzheimer's disease: Possible mechanism for paired helical filament formation
    • Zemlan, F. P., Thienhaus, O. J. & Bosmann, H. B. Superoxide dismutase activity in Alzheimer's disease: Possible mechanism for paired helical filament formation. Brain Res. 476, 160-162 (1989).
    • (1989) Brain Res. , vol.476 , pp. 160-162
    • Zemlan, F.P.1    Thienhaus, O.J.2    Bosmann, H.B.3
  • 10
    • 0026823074 scopus 로고
    • Immunohistochemical evidence of oxidative stress in Alzheimer's disease
    • Pappolla, M. A., Omar, R. A., Kim, K. S. & Robakis, N. K. Immunohistochemical evidence of oxidative stress in Alzheimer's disease. Am. J. Pathol. 140, 621-628 (1992).
    • (1992) Am. J. Pathol. , vol.140 , pp. 621-628
    • Pappolla, M.A.1    Omar, R.A.2    Kim, K.S.3    Robakis, N.K.4
  • 11
    • 0042096585 scopus 로고    scopus 로고
    • Free radicals, lipid peroxidation and antioxidents in apoptosis: Implications in cancer, cardiovascular and neurological diseases
    • Ferrari, C. K. B. Free radicals, lipid peroxidation and antioxidents in apoptosis: Implications in cancer, cardiovascular and neurological diseases. Biologia 55, 581-590 (2000).
    • (2000) Biologia , vol.55 , pp. 581-590
    • Ferrari, C.K.B.1
  • 12
    • 0034667741 scopus 로고    scopus 로고
    • Acrolein, a product of lipid paroxidation, inhibits glucose and glutamate uptake in primary neuronal cultures
    • Lovell, M. A., Xie, C. & Markesbery, W. R. Acrolein, a product of lipid paroxidation, inhibits glucose and glutamate uptake in primary neuronal cultures. Free Radic. Biol. Med. 29, 714-720 (2000).
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 714-720
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 13
    • 0030966546 scopus 로고    scopus 로고
    • Impairment of glucose and glutamate transport arid induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid β-peptide: Role of the lipid peroxidation product 4-hydroxynonenal
    • Keller, J. N. et al. Impairment of glucose and glutamate transport arid induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid β-peptide: Role of the lipid peroxidation product 4-hydroxynonenal. J. Neurochem. 69, 273-284 (1997).
    • (1997) J. Neurochem. , vol.69 , pp. 273-284
    • Keller, J.N.1
  • 15
    • 0037382957 scopus 로고    scopus 로고
    • 2 and 4-hydroxynonenal mediate amyloid β-induced neuronal apoptosis by activating JNKs and p38MAPK
    • 2 and 4-hydroxynonenal mediate amyloid β-induced neuronal apoptosis by activating JNKs and p38MAPK. Exp. Neurol. 180, 144-155 (2003).
    • (2003) Exp. Neurol. , vol.180 , pp. 144-155
    • Tamagno, E.1
  • 16
    • 0036182380 scopus 로고    scopus 로고
    • Calcium and oxidative stress: From cell signaling to cell death
    • Ermak, G. & Davies, K. J. Calcium and oxidative stress: From cell signaling to cell death. Mol. Immunol. 38, 713-721 (2002).
    • (2002) Mol. Immunol. , vol.38 , pp. 713-721
    • Ermak, G.1    Davies, K.J.2
  • 17
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla, F. M. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nature Rev. Neurosci. 3, 862-872 (2002).
    • (2002) Nature Rev. Neurosci. , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 18
    • 0036591850 scopus 로고    scopus 로고
    • Interactions of oxidative stress with cellular calcium dynamics and glucose metabolism in Alzheimer's disease
    • Gibson, G. E. Interactions of oxidative stress with cellular calcium dynamics and glucose metabolism in Alzheimer's disease. Free Radic. Biol. Med. 32, 1061-1070 (2002).
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1061-1070
    • Gibson, G.E.1
  • 19
    • 0042536471 scopus 로고    scopus 로고
    • Neuronal and glial calcium signaling in Alzheimer's disease
    • Mattson, M. P. & Chan, S. L. Neuronal and glial calcium signaling in Alzheimer's disease. Cell Calcium 34, 385-397 (2003).
    • (2003) Cell Calcium , vol.34 , pp. 385-397
    • Mattson, M.P.1    Chan, S.L.2
  • 20
    • 0032507591 scopus 로고    scopus 로고
    • The hydroxyl radical scavenger Nicaraven inhibits glutsmate release after spinal injury in rats
    • Yamamoto, K. et al. The hydroxyl radical scavenger Nicaraven inhibits glutsmate release after spinal injury in rats. Neuroreport 9, 1655-1659 (1998).
    • (1998) Neuroreport , vol.9 , pp. 1655-1659
    • Yamamoto, K.1
  • 21
    • 0043180531 scopus 로고    scopus 로고
    • Excitotoxic and excitoprotective mechanisms: Abundant targets for the prevention and treatment of neurodegenerative disorders
    • Mattson, M. P. Excitotoxic and excitoprotective mechanisms: abundant targets for the prevention and treatment of neurodegenerative disorders. Neuromolecular Med. 3, 65-94 (2003).
    • (2003) Neuromolecular Med. , vol.3 , pp. 65-94
    • Mattson, M.P.1
  • 22
    • 0033789565 scopus 로고    scopus 로고
    • Free radical pathways in CNS injury
    • Lewen, A., Matz, P. & Chan, P. H. Free radical pathways in CNS injury. J. Neurotrauma 17, 871-890 (2000).
    • (2000) J. Neurotrauma , vol.17 , pp. 871-890
    • Lewen, A.1    Matz, P.2    Chan, P.H.3
  • 26
    • 0027990784 scopus 로고
    • The effect of aging on to mineral status of female mice
    • Morita, A., Kimura, M. & Itokawa, Y. The effect of aging on to mineral status of female mice. Biol. Trace Elem. Res. 42, 165-177 (1994).
    • (1994) Biol. Trace Elem. Res. , vol.42 , pp. 165-177
    • Morita, A.1    Kimura, M.2    Itokawa, Y.3
  • 27
    • 0034976070 scopus 로고    scopus 로고
    • Age-related changes in the concentrations of major and trace elements in the brain of rats and mice
    • Takahashi, S. et al. Age-related changes in the concentrations of major and trace elements in the brain of rats and mice. Biol. Trace Elem. Res. 80, 145-158 (2001).
    • (2001) Biol. Trace Elem. Res. , vol.80 , pp. 145-158
    • Takahashi, S.1
  • 28
    • 0037160028 scopus 로고    scopus 로고
    • Overexpression of Alzheimer's disease amyloid-β opposes the age-dependent elevations of brain copper and iron
    • Maynard, C. J. et al. Overexpression of Alzheimer's disease amyloid-β opposes the age-dependent elevations of brain copper and iron. J. Biol. Chem. 277, 44670-4476 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44670-44676
    • Maynard, C.J.1
  • 29
    • 0034035616 scopus 로고    scopus 로고
    • Metals and neuroscience
    • Bush, A. I. Metals and neuroscience. Curr. Opin. Chem. Biol. 4, 184-191 (2000).
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 184-191
    • Bush, A.I.1
  • 30
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush, A. I. The metallobiology of Alzheimer's disease. Trends Neurosci. 26, 207-214 (2003).
    • (2003) Trends Neurosci. , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 31
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy, J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20, 154-159 (1997).
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 32
  • 33
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • Masters, C. L. et al. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc. Natl Acad. Sci. USA 82, 4245-4249 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4245-4249
    • Masters, C.L.1
  • 34
    • 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, 885-890 (1984).
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 35
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang, J. et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325, 733-736 (1987).
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1
  • 36
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee, J. Y., Cole, T. B., Palmiter, R. D., Suh, S. W. & Koh, J. Y. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl Acad. Sci. USA 99, 7705-7710 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7705-7710
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Suh, S.W.4    Koh, J.Y.5
  • 38
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith, M. A., Harris, P. L., Sayre, L. M. & Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc. Natl Acad. Sci. USA 94, 9866-9868 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.2    Sayre, L.M.3    Perry, G.4
  • 39
    • 0030704680 scopus 로고    scopus 로고
    • Zinc-induced Alzheimer's Aβ 1-40 aggregation is mediated by conformational factors
    • Huang, X. et al. Zinc-induced Alzheimer's Aβ 1-40 aggregation is mediated by conformational factors. J. Biol. Chem. 272, 26464-26470 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26464-26470
    • Huang, X.1
  • 40
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood, C. S. et al. Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273, 12817-12826 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 12817-12826
    • Atwood, C.S.1
  • 41
    • 0029795197 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimer disease: An alternative to the amyloid hypothesis
    • Terry, R. D. The pathogenesis of Alzheimer disease: An alternative to the amyloid hypothesis. J. Neuropathol. Exp. Neurol. 55, 1023-1025 (1996).
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 1023-1025
    • Terry, R.D.1
  • 42
    • 0022480081 scopus 로고
    • Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress
    • Martins, R. N., Harper, C. G., Stokes, G. B. & Masters, C. L. Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress. J. Neurochem. 46, 1042-1045 (1986).
    • (1986) J. Neurochem. , vol.46 , pp. 1042-1045
    • Martins, R.N.1    Harper, C.G.2    Stokes, G.B.3    Masters, C.L.4
  • 43
    • 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. et al. In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals. J. Neurochem. 74, 270-279 (2000).
    • (2000) J. Neurochem. , vol.74 , pp. 270-279
    • Sayre, L.M.1
  • 44
    • 0032613038 scopus 로고    scopus 로고
    • Role of free radicals and metal ions in the pathogenesis of Alzheimer's disease
    • Atwood, C. S., Huang, X., Moir, R. D., Tanzi, R. E. & Bush, A. I. Role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Met. Ions Biol. Syst. 36, 309-364 (1999).
    • (1999) Met. Ions Biol. Syst. , vol.36 , pp. 309-364
    • Atwood, C.S.1    Huang, X.2    Moir, R.D.3    Tanzi, R.E.4    Bush, A.I.5
  • 45
    • 0026041595 scopus 로고
    • Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease
    • 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, 231-258 (1991).
    • (1991) J. Neural Transm. Park. Dis. Dement. Sect. , vol.3 , pp. 231-258
    • Basun, H.1    Forssell, L.G.2    Wetterberg, L.3    Winblad, B.4
  • 46
    • 0037159210 scopus 로고    scopus 로고
    • Elevation of serum copper levels in Alzheimer's disease
    • Squitti, R. et al. Elevation of serum copper levels in Alzheimer's disease. Neurology 59, 1153-1161 (2002).
    • (2002) Neurology , vol.59 , pp. 1153-1161
    • Squitti, R.1
  • 47
    • 0036970184 scopus 로고    scopus 로고
    • Iron: A pathological mediator of Alzheimer disease?
    • Bishop, G. M. et al. Iron: A pathological mediator of Alzheimer disease? Dev. Neurosci. 24, 184-187 (2002).
    • (2002) Dev. Neurosci. , vol.24 , pp. 184-187
    • Bishop, G.M.1
  • 48
    • 0031776586 scopus 로고    scopus 로고
    • Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4-dinitrophenylhydrazine
    • Smith, M. A. et al. Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4-dinitrophenylhydrazine. J. Histochem. Cytochem. 46, 731-735 (1998).
    • (1998) J. Histochem. Cytochem. , vol.46 , pp. 731-735
    • Smith, M.A.1
  • 49
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • Dong, J. et al. Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42, 2768-2773 (2003).
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1
  • 50
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl, C., Davis, J. B., Lesley, R. & Schubert, D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77, 817-827 (1994).
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 52
    • 0033601338 scopus 로고    scopus 로고
    • Cu(II) potentiation of alzheimer Aβ neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction
    • Huang, X. et al. Cu(II) potentiation of alzheimer Aβ neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction. J. Biol. Chem. 274, 37111-37116 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 37111-37116
    • Huang, X.1
  • 53
    • 18344414746 scopus 로고    scopus 로고
    • The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction
    • Huang, X. et al. The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 38, 7609-7616 (1999).
    • (1999) Biochemistry , vol.38 , pp. 7609-7616
    • Huang, X.1
  • 54
    • 0034733705 scopus 로고    scopus 로고
    • Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Aβ by zinc
    • Cuajungco, M. P. et al. Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Aβ by zinc. J. Biol. Chem. 275, 19439-19442 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 19439-19442
    • Cuajungco, M.P.1
  • 55
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain, C. C. et al. Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276, 20466-20473 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1
  • 56
    • 0037474240 scopus 로고    scopus 로고
    • Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-β peptide with membrane lipid
    • Curtain, C. C. et al. Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-β peptide with membrane lipid. J. Biol. Chem. 278, 2977-2982 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 2977-2982
    • Curtain, C.C.1
  • 57
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β 1-42
    • Atwood, C. S. et al. Characterization of copper interactions with alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β 1-42. J. Neurochem. 75, 1219-1233 (2000).
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1
  • 58
    • 0242290357 scopus 로고    scopus 로고
    • Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation
    • Barnham, K. J. et al. Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation. J. Biol. Chem. 278, 42959-42965 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 42959-42965
    • Barnham, K.J.1
  • 59
    • 0001052504 scopus 로고    scopus 로고
    • Copper catalyzed oxidation of Alzheimer Aβ
    • Atwood, C. S. et al. Copper catalyzed oxidation of Alzheimer Aβ. Cell. Mol. Biol. (Noisy-Le-Grand) 46, 777-783 (2000).
    • (2000) Cell Mol. Biol. (Noisy-Le-Grand) , vol.46 , pp. 777-783
    • Atwood, C.S.1
  • 60
    • 0034746895 scopus 로고    scopus 로고
    • Oxidation of Aβ and plaque biogenesis in Alzheimer's disease and Down syndrome
    • Head, E. et al. Oxidation of Aβ and plaque biogenesis in Alzheimer's disease and Down syndrome. Neurobiol. Dis. 8, 792-806 (2001).
    • (2001) Neurobiol. Dis. , vol.8 , pp. 792-806
    • Head, E.1
  • 61
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean, C. A. et al. Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 46, 860-866 (1999).
    • (1999) Ann. Neurol. , vol.46 , pp. 860-866
    • McLean, C.A.1
  • 62
    • 0033551782 scopus 로고    scopus 로고
    • Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion
    • Cherny, R. A. et al. Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion. J. Biol. Chem. 274, 23223-23228 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 23223-23228
    • Cherny, R.A.1
  • 64
    • 0141853765 scopus 로고    scopus 로고
    • Amyloid-β: A chameleon walking in two worlds: A review of the trophic and toxic properties of amyloid-β
    • Atwood, C. S. et al. Amyloid-β: A chameleon walking in two worlds: A review of the trophic and toxic properties of amyloid-β. Brain Res. Brain Res. Rev. 43, 1-16 (2003).
    • (2003) Brain Res. Brain Res. Rev. , vol.43 , pp. 1-16
    • Atwood, C.S.1
  • 65
    • 0030882856 scopus 로고    scopus 로고
    • α-synuclein in Lewy bodies
    • Spillantini, M. G. et al. α-synuclein in Lewy bodies. Nature 388, 839-840 (1997).
    • (1997) Nature , vol.388 , pp. 839-840
    • Spillantini, M.G.1
  • 66
    • 0034798193 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease
    • Gasser, T. Genetics of Parkinson's disease. J. Neurol. 248, 833-840 (2001).
    • (2001) J. Neurol. , vol.248 , pp. 833-840
    • Gasser, T.1
  • 67
    • 0020996094 scopus 로고
    • Neuromelanin and Parkinson's disease
    • Marsden, C. D. Neuromelanin and Parkinson's disease. J. Neural. Transm. Suppl. 19, 121-141 (1983).
    • (1983) J. Neural. Transm. Suppl. , vol.19 , pp. 121-141
    • Marsden, C.D.1
  • 68
    • 0023740954 scopus 로고
    • Melanized dopaminergic neurons are differentially susceptible to degeneration in Parkinson's disease
    • Hirsch, E., Graybiel, A. M. & Agid, Y. A. Melanized dopaminergic neurons are differentially susceptible to degeneration in Parkinson's disease. Nature 334, 345-348 (1988).
    • (1988) Nature , vol.334 , pp. 345-348
    • Hirsch, E.1    Graybiel, A.M.2    Agid, Y.A.3
  • 69
    • 0042731682 scopus 로고    scopus 로고
    • The structure of neuromelanin as studied by chemical degradative methods
    • Wakamatsu, K., Fujikawa, K., Zucca, F. A., Zecca, L. & Ito, S. The structure of neuromelanin as studied by chemical degradative methods. J. Neurochem. 86, 1015-1023 (2003).
    • (2003) J. Neurochem. , vol.86 , pp. 1015-1023
    • Wakamatsu, K.1    Fujikawa, K.2    Zucca, F.A.3    Zecca, L.4    Ito, S.5
  • 70
    • 0141975261 scopus 로고    scopus 로고
    • The neuromelanin of human substantia nigra: Structure, synthesis and molecular behaviour
    • Zecca, L. et al. The neuromelanin of human substantia nigra: structure, synthesis and molecular behaviour. J. Neural. Transm. Suppl. 145-155 (2003).
    • (2003) J. Neural. Transm. Suppl. , pp. 145-155
    • Zecca, L.1
  • 71
    • 43949155367 scopus 로고
    • Complexes of iron(III) with ligands of biological interest: Dopamine and 8-hydroxyquinoline-5-sulfonic acid
    • Gerard, C., Chehhal, H. & Hugel, R. P. Complexes of iron(III) with ligands of biological interest: Dopamine and 8-hydroxyquinoline-5-sulfonic acid. Polyhedron 13, 591-597 (1994).
    • (1994) Polyhedron , vol.13 , pp. 591-597
    • Gerard, C.1    Chehhal, H.2    Hugel, R.P.3
  • 72
    • 0041695547 scopus 로고    scopus 로고
    • Iron-binding characteristics of neuromelanin of the human substantia nigra
    • Double, K. L. et al. Iron-binding characteristics of neuromelanin of the human substantia nigra. Biochem. Pharmacol. 66, 489-494 (2003).
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 489-494
    • Double, K.L.1
  • 74
    • 12944305793 scopus 로고    scopus 로고
    • Neuromelanin biosynthesis is driven by excess cytosolic catecholamines not accumulated by synaptic vesicles
    • Sulzer, D. et al. Neuromelanin biosynthesis is driven by excess cytosolic catecholamines not accumulated by synaptic vesicles. Proc. Natl Acad. Sci. USA 97, 11869-11874 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11869-11874
    • Sulzer, D.1
  • 75
    • 0026040282 scopus 로고
    • Iron-melanin interaction and lipid peroxidation: Implications for Parkinson's disease
    • Ben-Shachar, D., Riederer, P. & Youdim, M. B. Iron-melanin interaction and lipid peroxidation: Implications for Parkinson's disease. J. Neurochem. 57, 1609-1614 (1991).
    • (1991) J. Neurochem. , vol.57 , pp. 1609-1614
    • Ben-Shachar, D.1    Riederer, P.2    Youdim, M.B.3
  • 76
    • 0042433192 scopus 로고    scopus 로고
    • Neuromelanin associated redox-active iron is increased in the substantia nigra of patients with Parkinson's disease
    • Faucheux, B.A. et al. Neuromelanin associated redox-active iron is increased in the substantia nigra of patients with Parkinson's disease. J. Neurochem. 86, 1142-1148 (2003).
    • (2003) J. Neurochem. , vol.86 , pp. 1142-1148
    • Faucheux, B.A.1
  • 77
    • 0037064078 scopus 로고    scopus 로고
    • Effect of mutant α-synuclein on dopamine homeostasis in a new human mesencephalic cell line
    • Lotharius, J. et al. Effect of mutant α-synuclein on dopamine homeostasis in a new human mesencephalic cell line. J. Biol. Chem. 277, 38884-38894 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 38884-38894
    • Lotharius, J.1
  • 78
    • 0036797552 scopus 로고    scopus 로고
    • Impaired dopamine storage resulting from α-synuclein mutations may contribute to the pathogenesis of Parkinson's disease
    • Lotharius, J. & Brundin, P. Impaired dopamine storage resulting from α-synuclein mutations may contribute to the pathogenesis of Parkinson's disease. Hum. Mol. Genet. 11, 2395-2407 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2395-2407
    • Lotharius, J.1    Brundin, P.2
  • 79
    • 0038701729 scopus 로고    scopus 로고
    • Co-ordinate transcriptional regulation of dopamine synthesis genes by α-synuclein in human neuroblastoma cell lines
    • Baptista, M. J. et al. Co-ordinate transcriptional regulation of dopamine synthesis genes by α-synuclein in human neuroblastoma cell lines. J. Neurochem. 85, 957-968 (2003).
    • (2003) J. Neurochem. , vol.85 , pp. 957-968
    • Baptista, M.J.1
  • 80
    • 0642364992 scopus 로고    scopus 로고
    • Modulation of dopamine transporter function by α-synuclein is altered by impairment of cell adhesion and by induction of oxidative stress
    • Wersinger, C., Prou, D., Vernier, P & Sidhu, A. Modulation of dopamine transporter function by α-synuclein is altered by impairment of cell adhesion and by induction of oxidative stress. FASEB. J. (2003).
    • (2003) FASEB. J.
    • Wersinger, C.1    Prou, D.2    Vernier, P.3    Sidhu, A.4
  • 81
    • 0037092442 scopus 로고    scopus 로고
    • A role for α-synuclein in the regulation of dopamine biosynthesis
    • Perez, R. G. et al. A role for α-synuclein in the regulation of dopamine biosynthesis. J. Neurosci. 22, 3090-3099 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 3090-3099
    • Perez, R.G.1
  • 82
    • 0035104181 scopus 로고    scopus 로고
    • α-synuclein immunopositive Parkinson's disease-related inclusion bodies in lower brain stem nuclei
    • Braak, E. et al. α-synuclein immunopositive Parkinson's disease-related inclusion bodies in lower brain stem nuclei. Acta Neuropathol. (Berl) 101, 195-201 (2001).
    • (2001) Acta Neuropathol. (Berl) , vol.101 , pp. 195-201
    • Braak, E.1
  • 83
    • 0037410207 scopus 로고    scopus 로고
    • Residual substantia nigra neuromelanin in Parkinson's disease is cross-linked to α-synuclein
    • Fasano, M., Giraudo, S., Coha, S., Bergamasco, B. & Lopiano, L Residual substantia nigra neuromelanin in Parkinson's disease is cross-linked to α-synuclein. Neurochem. Int. 42, 603-606 (2003).
    • (2003) Neurochem. Int. , vol.42 , pp. 603-606
    • Fasano, M.1    Giraudo, S.2    Coha, S.3    Bergamasco, B.4    Lopiano, L.5
  • 84
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson disease
    • Xu, J. et al. Dopamine-dependent neurotoxicity of α-synuclein: A mechanism for selective neurodegeneration in Parkinson disease. Nature Med. 8, 600-606 (2002).
    • (2002) Nature Med. , vol.8 , pp. 600-606
    • Xu, J.1
  • 85
    • 0033564726 scopus 로고    scopus 로고
    • Copper(II)-induced self-oligomerization of α-synuclein
    • Paik, S. R., Shin, H. J., Lee, J. H., Chang, O. S. & Kim, J. Copper(II)-induced self-oligomerization of α-synuclein. Biochem. J. 340, 821-828 (1999).
    • (1999) Biochem. J. , vol.340 , pp. 821-828
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3    Chang, O.S.4    Kim, J.5
  • 86
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation at human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure
    • Uversky, V. N., Li, J. & Fink, A. L. Metal-triggered structural transformations, aggregation, and fibrillation at human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 276, 44284-44296 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 88
    • 0041845349 scopus 로고    scopus 로고
    • Certain metals trigger fibrillation of methionine-oxidized α-synuclein
    • Yamin, G., Glaser, C. B., Uversky, V. N. & Fink, A. L. Certain metals trigger fibrillation of methionine-oxidized α-synuclein. J. Biol. Chem. 278, 27630-27635 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 27630-27635
    • Yamin, G.1    Glaser, C.B.2    Uversky, V.N.3    Fink, A.L.4
  • 89
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn, L. I. et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281, 1851-1854 (1998).
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1
  • 90
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation
    • Gurney, M. E. et al. Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264, 1772-1775 (1994).
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1
  • 91
    • 0037388067 scopus 로고    scopus 로고
    • Misfolded CuZnSOD and amyotrophic lateral sclerosis
    • Valentine, J. S. & Hart, P. J. Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc. Natl Acad. Sci. USA 100, 3617-3622 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3617-3622
    • Valentine, J.S.1    Hart, P.J.2
  • 92
    • 0029671220 scopus 로고    scopus 로고
    • Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis
    • Wiedau-Pazos, M. et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 271, 515-518 (1996).
    • (1996) Science , vol.271 , pp. 515-518
    • Wiedau-Pazos, M.1
  • 93
    • 0030831352 scopus 로고    scopus 로고
    • Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: Molecular mechanisms of neuronal death and protection
    • Ghadge, G. D. et al. Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis: Molecular mechanisms of neuronal death and protection. J. Neurosci. 17, 8756-8766 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 8756-8766
    • Ghadge, G.D.1
  • 94
    • 0030862630 scopus 로고    scopus 로고
    • The copper chelator D-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Hottinger, A. F., Fine, E. G., Gurney, M. E., Zurn, A. D. & Aebischer, P. The copper chelator D-penicillamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis. Eur. J. Neurosci. 9, 1548-1551 (1997).
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 1548-1551
    • Hottinger, A.F.1    Fine, E.G.2    Gurney, M.E.3    Zurn, A.D.4    Aebischer, P.5
  • 95
    • 0033970574 scopus 로고    scopus 로고
    • Prevention of mutant SOD1 motoneuron degeneration by copper chelators in vitro
    • Azzouz, M. et al. Prevention of mutant SOD1 motoneuron degeneration by copper chelators in vitro. J. Neurobiol. 42, 49-55 (2000).
    • (2000) J. Neurobiol. , vol.42 , pp. 49-55
    • Azzouz, M.1
  • 96
    • 0039251419 scopus 로고    scopus 로고
    • Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase
    • Estevez, A. G. et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 286, 2498-600 (1999).
    • (1999) Science , vol.286 , pp. 2498-2600
    • Estevez, A.G.1
  • 97
    • 0036212119 scopus 로고    scopus 로고
    • Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading
    • Subramaniam, J. R. et al. Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading. Nature Neurosci. 5, 301-307 (2002).
    • (2002) Nature Neurosci. , vol.5 , pp. 301-307
    • Subramaniam, J.R.1
  • 98
    • 0033977325 scopus 로고    scopus 로고
    • Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • Goto, J. J. et al. Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 275, 1007-1014 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 1007-1014
    • Goto, J.J.1
  • 99
    • 0034682615 scopus 로고    scopus 로고
    • 2+ binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant
    • 2+ binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant. Biochemistry 39, 8125-8132 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8125-8132
    • Liu, H.1
  • 100
    • 33845333122 scopus 로고    scopus 로고
    • Is ALS caused by an altered oxidative activity of mutant superoxide dismutase?
    • author reply 919-920
    • Bush, A. I. Is ALS caused by an altered oxidative activity of mutant superoxide dismutase? Nature Neurosci. 5, 919; author reply 919-920 (2002).
    • (2002) Nature Neurosci. , vol.5 , pp. 919
    • Bush, A.I.1
  • 101
    • 0036799799 scopus 로고    scopus 로고
    • Antioxidants as treatment for neurodegenerative disorders
    • Moosmann, M. & Behl, C. Antioxidants as treatment for neurodegenerative disorders. Exp. Opin. Invest. Drugs 11, 1407-1435 (2002).
    • (2002) Exp. Opin. Invest. Drugs , vol.11 , pp. 1407-1435
    • Moosmann, M.1    Behl, C.2
  • 102
    • 0027530638 scopus 로고
    • Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease
    • The Parkinson Study Group
    • Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease. The Parkinson Study Group. N. Engl. J. Med. 328, 176-183 (1993).
    • (1993) N. Engl. J. Med. , vol.328 , pp. 176-183
  • 103
    • 0030967165 scopus 로고    scopus 로고
    • A controlled trial of selegiline, α-tocopherol, or both as treatment for Alzheimer's disease. The Alzheimer's Disease Cooperative Study
    • Sano, M. et al. A controlled trial of selegiline, α-tocopherol, or both as treatment for Alzheimer's disease. The Alzheimer's Disease Cooperative Study. N. Engl. J. Med. 336, 1216-1222 (1997).
    • (1997) N. Engl. J. Med. , vol.336 , pp. 1216-1222
    • Sano, M.1
  • 104
    • 0033958696 scopus 로고    scopus 로고
    • Vitamin E and Alzheimer's disease: The basis for additional clinical trials
    • Grundman, M. Vitamin E and Alzheimer's disease: The basis for additional clinical trials. Am. J. Clin. Nutr. 71, S630-S636 (2000).
    • (2000) Am. J. Clin. Nutr. , vol.71
    • Grundman, M.1
  • 105
    • 0037417238 scopus 로고    scopus 로고
    • Memantine in moderate-to-severe Alzheimer's disease
    • Reisberg, B. et al. Memantine in moderate-to-severe Alzheimer's disease. N. Engl. J. Med. 348, 1333-1341 (2003).
    • (2003) N. Engl. J. Med. , vol.348 , pp. 1333-1341
    • Reisberg, B.1
  • 106
    • 0141483720 scopus 로고    scopus 로고
    • Memantine: Update on the current evidence
    • Mobius, H. J. Memantine: Update on the current evidence. Int. J. Geriatr. Psychiatry 18, S47-S54 (2003).
    • (2003) Int. J. Geriatr. Psychiatry , vol.18
    • Mobius, H.J.1
  • 107
    • 0141595258 scopus 로고    scopus 로고
    • Treating the full spectrum of dementia with memantine
    • Winblad, B. & Jelic, V. Treating the full spectrum of dementia with memantine. Int. J. Geriatr. Psychiatry 18, S41-S46 (2003).
    • (2003) Int. J. Geriatr. Psychiatry , vol.18
    • Winblad, B.1    Jelic, V.2
  • 109
    • 0028097839 scopus 로고
    • A controlled trial of riluzole in amyotrophic lateral sclerosis
    • ALS/Riluzole Study Group
    • Bensimon, G., Lacomblez, L. & Meininger, V. A controlled trial of riluzole in amyotrophic lateral sclerosis. ALS/Riluzole Study Group. N. Engl. J. Med. 330, 585-591 (1994).
    • (1994) N. Engl. J. Med. , vol.330 , pp. 585-591
    • Bensimon, G.1    Lacomblez, L.2    Meininger, V.3
  • 110
    • 0036451888 scopus 로고    scopus 로고
    • Non-cholinergic strategies for treating and preventing Alzheimer's disease
    • Doraiswamy, P. M. Non-cholinergic strategies for treating and preventing Alzheimer's disease. CNS Drugs 16, 811-824 (2002).
    • (2002) CNS Drugs , vol.16 , pp. 811-824
    • Doraiswamy, P.M.1
  • 111
    • 0037465541 scopus 로고    scopus 로고
    • Will caloric restriction and folate protect against AD and PD?
    • Mattson, M. P. Will caloric restriction and folate protect against AD and PD? Neurology 80, 690-695 (2003).
    • (2003) Neurology , vol.80 , pp. 690-695
    • Mattson, M.P.1
  • 112
    • 0025726462 scopus 로고
    • Intramuscular desferrioxamine in patients with Alzheimer's disease
    • Crapper McLachlan, D. R. et al. Intramuscular desferrioxamine in patients with Alzheimer's disease. Lancet 337, 1304-1308 (1991).
    • (1991) Lancet , vol.337 , pp. 1304-1308
    • Crapper McLachlan, D.R.1
  • 113
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny, R. A. et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30, 665-676 (2001).
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1
  • 114
    • 10744224267 scopus 로고    scopus 로고
    • Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Aβ amyloid deposition and toxicity in Alzheimer's disease: Biochemical and clinical responses in a pilot phase 2 clinical trial
    • Ritchie, C. W. et al. Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Aβ amyloid deposition and toxicity in Alzheimer's disease: Biochemical and clinical responses in a pilot phase 2 clinical trial. Arch. Neurol. 60, 1685-1691 (2003).
    • (2003) Arch. Neurol. , vol.60 , pp. 1685-1691
    • Ritchie, C.W.1
  • 115
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer, W. & Przedborski, S. Parkinson's disease: Mechanisms and models. Neuron 39, 889-909 (2003).
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 116
    • 0242684415 scopus 로고    scopus 로고
    • Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: A novel therapy for Parkinson's disease
    • Kaur, D. et al. Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: A novel therapy for Parkinson's disease. Neuron 37, 899-909 (2003).
    • (2003) Neuron , vol.37 , pp. 899-909
    • Kaur, D.1
  • 117
    • 0036660458 scopus 로고    scopus 로고
    • Metal ion chelation in neurodegenerative disorders
    • Angel, I. et al. Metal ion chelation in neurodegenerative disorders. Drug Dev. Res. 56, 300-309 (2002).
    • (2002) Drug Dev. Res. , vol.56 , pp. 300-309
    • Angel, I.1
  • 118
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano, V. et al. Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 271, 1423-1427 (1996).
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1
  • 119
    • 0033957174 scopus 로고    scopus 로고
    • Clinical, biochemical and molecular genetic correlations in Friedreich's ataxia
    • Bradley, J. L. et al. Clinical, biochemical and molecular genetic correlations in Friedreich's ataxia. Hum. Mol. Genet. 9, 275-282 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 275-282
    • Bradley, J.L.1
  • 120
    • 0033533071 scopus 로고    scopus 로고
    • Effect of idebenone on cardiomyopathy in Friedreich's ataxia: A preliminary study
    • Rustin, P. et al. Effect of idebenone on cardiomyopathy in Friedreich's ataxia: A preliminary study. Lancet 354, 477-479 (1999).
    • (1999) Lancet , vol.354 , pp. 477-479
    • Rustin, P.1
  • 121
    • 0036221156 scopus 로고    scopus 로고
    • Idebenone and reduced cardiac hypertrophy in Friedreich's ataxia
    • Hausse, A. O. et al. Idebenone and reduced cardiac hypertrophy in Friedreich's ataxia. Heart 87, 346-349 (2002).
    • (2002) Heart , vol.87 , pp. 346-349
    • Hausse, A.O.1
  • 122
    • 0038187688 scopus 로고    scopus 로고
    • Idebenone treatment in Friedreich's ataxia: Neurological, cardiac, and biochemical monitoring
    • Buyse, G. et al. Idebenone treatment in Friedreich's ataxia: neurological, cardiac, and biochemical monitoring. Neurology 60, 1679-1681 (2003).
    • (2003) Neurology , vol.60 , pp. 1679-1681
    • Buyse, G.1
  • 123
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong, A. et al. The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet. 8, 425-430 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 425-430
    • Wong, A.1
  • 124
    • 0035978474 scopus 로고    scopus 로고
    • Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilize mitochondrial iron
    • Richardson, D. R., Mouralian, C., Ponka, P. & Becker, E. Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilize mitochondrial iron. Biochim. Biophys. Acta 1536, 133-40 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 133-140
    • Richardson, D.R.1    Mouralian, C.2    Ponka, P.3    Becker, E.4
  • 125
    • 0030802648 scopus 로고    scopus 로고
    • The copper chaperone for superoxide dismutase
    • Culotta, V. C. et al. The copper chaperone for superoxide dismutase. J. Biol. Chem. 272, 23469-23472 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23469-23472
    • Culotta, V.C.1
  • 126
  • 127
    • 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. & O'Halloran, T. V. Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase. Science 284, 805-808 (1999).
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 128
    • 0035811030 scopus 로고    scopus 로고
    • Mining copper transport genes
    • Andrews, N. C. Mining copper transport genes. Proc. Natl Acad. Sci. USA 96, 6543-6545 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6543-6545
    • Andrews, N.C.1
  • 129
    • 0032830357 scopus 로고    scopus 로고
    • Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice
    • White, A. R. et al. Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice. Brain Res. 842, 439-444 (1999).
    • (1999) Brain Res. , vol.842 , pp. 439-444
    • White, A.R.1
  • 130
    • 10744226316 scopus 로고    scopus 로고
    • Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Aβ production in APP23 transgenic mice
    • Bayer, T. A. et al. Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Aβ production in APP23 transgenic mice. Proc. Natl Acad. Sci. USA 100, 14187-14192 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14187-14192
    • Bayer, T.A.1
  • 131
    • 10744228112 scopus 로고    scopus 로고
    • In vivo reduction of amyloid-β by a mutant copper transporter
    • Phinney, A. L. et al. In vivo reduction of amyloid-β by a mutant copper transporter. Proc. Natl Acad. Sci. USA 100, 14193-14198 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14193-14198
    • Phinney, A.L.1
  • 132
    • 0033430087 scopus 로고    scopus 로고
    • Copper inhibits β-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion
    • Borchardt, T. et al. Copper inhibits β-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion. Biochem. J. 344 Pt 2, 461-467 (1999).
    • (1999) Biochem. J. , vol.344 , Issue.PART 2 , pp. 461-467
    • Borchardt, T.1
  • 133
    • 0037931743 scopus 로고    scopus 로고
    • Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis
    • Barnham, K. J. et al. Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis. J. Biol. Chem. 278, 17401-17407 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 17401-17407
    • Barnham, K.J.1
  • 134
    • 0347928847 scopus 로고    scopus 로고
    • An iron-responsive element type II in the 5′-untranslated region of the Alzheimer's amyloid precursor protein transcript
    • Rogers, J. T. et al. An iron-responsive element type II in the 5′-untranslated region of the Alzheimer's amyloid precursor protein transcript. J. Biol. Chem. 277, 45518-45528 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 45518-45528
    • Rogers, J.T.1
  • 135
    • 0019124032 scopus 로고
    • Relationship of octanol/water partition coefficient and molecular weight to rat brain capillary permeability
    • Levin, V. A. Relationship of octanol/water partition coefficient and molecular weight to rat brain capillary permeability. J. Med Chem. 23, 682-684 (1980).
    • (1980) J. Med Chem. , vol.23 , pp. 682-684
    • Levin, V.A.1
  • 136
    • 0033152287 scopus 로고    scopus 로고
    • Investigation into the correlation between the structure of hydroxypyridinones and blood-brain barrier permeability
    • Habgood, M. D. et al. Investigation into the correlation between the structure of hydroxypyridinones and blood-brain barrier permeability. Biochem. Pharmacol. 57, 1305-1310 (1999).
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 1305-1310
    • Habgood, M.D.1
  • 137
    • 0036844787 scopus 로고    scopus 로고
    • Predicting blood-brain barrier partitioning of organic molecules using membrane-interaction QSAR analysis
    • Iyer, M., Mishru, R., Han, Y. & Hopfinger, A. J. Predicting blood-brain barrier partitioning of organic molecules using membrane-interaction QSAR analysis. Pharm Res 19, 1611-1621 (2002).
    • (2002) Pharm. Res. , vol.19 , pp. 1611-1621
    • Iyer, M.1    Mishru, R.2    Han, Y.3    Hopfinger, A.J.4


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