메뉴 건너뛰기




Volumn 97, Issue 6, 2006, Pages 1634-1658

Oxidative stress and neurodegeneration: Where are we now?

Author keywords

Free radical; Hydroxyl radical; Proteasome; Protein aggregation; Reactive oxygen species; Superoxide

Indexed keywords

ANTIOXIDANT; DNA; GLUTATHIONE; HEMOGLOBIN; LIPID; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

EID: 33745013111     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2006.03907.x     Document Type: Review
Times cited : (2254)

References (211)
  • 1
    • 33646380409 scopus 로고    scopus 로고
    • The role of an astrocytic NADPH oxidase in the neurotoxicity of amyloid β peptides
    • Abramov A. Y. Duchen M. R. 2005 The role of an astrocytic NADPH oxidase in the neurotoxicity of amyloid β peptides. Philos. Trans. R. Soc. Lond. B Biol. Sci. 360, 2309 2314.
    • (2005) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.360 , pp. 2309-2314
    • Abramov, A.Y.1    Duchen, M.R.2
  • 3
    • 1242353138 scopus 로고    scopus 로고
    • Oxygen therapeutics: Can we tame haemoglobin?
    • Alayash A. I. 2004 Oxygen therapeutics: can we tame haemoglobin? Nat. Rev. Drug Discov. 3, 152 159.
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 152-159
    • Alayash, A.I.1
  • 4
    • 0346100520 scopus 로고    scopus 로고
    • Peroxynitrite reactivity with amino acids and proteins
    • Alvarez B. Radi R. 2003 Peroxynitrite reactivity with amino acids and proteins. Amino Acids 25, 295 311.
    • (2003) Amino Acids , vol.25 , pp. 295-311
    • Alvarez, B.1    Radi, R.2
  • 5
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Araki T. Sasaki Y. Milbrandt J. 2004 Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305, 1010 1013.
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 6
    • 0024788706 scopus 로고
    • Carnosine, homocarnosine and anserine: Could they act as antioxidants in vivo?
    • Aruoma O. I. Laughton M. J. Halliwell B. 1989 Carnosine, homocarnosine and anserine: could they act as antioxidants in vivo? Biochem. J. 264, 863 869.
    • (1989) Biochem. J. , vol.264 , pp. 863-869
    • Aruoma, O.I.1    Laughton, M.J.2    Halliwell, B.3
  • 7
    • 16644377315 scopus 로고    scopus 로고
    • A non-enzymatic derived arachidonyl peroxide, 8-iso-prostaglandin F2 alpha, in cerebrospinal fluid of patients with aneurysmal subarachnoid hemorrhage participates in the pathogenesis of delayed cerebral vasospasm
    • Asaeda M. Sakamoto M. Kurosaki M. Tabuchi S. Kamitani H. Yokota M. Watanabe T. 2005 A non-enzymatic derived arachidonyl peroxide, 8-iso-prostaglandin F2 alpha, in cerebrospinal fluid of patients with aneurysmal subarachnoid hemorrhage participates in the pathogenesis of delayed cerebral vasospasm. Neurosci. Lett. 373, 222 225.
    • (2005) Neurosci. Lett. , vol.373 , pp. 222-225
    • Asaeda, M.1    Sakamoto, M.2    Kurosaki, M.3    Tabuchi, S.4    Kamitani, H.5    Yokota, M.6    Watanabe, T.7
  • 9
    • 0033539481 scopus 로고    scopus 로고
    • How oxygen is activated and reduced in respiration
    • Babcock G. T. 1999 How oxygen is activated and reduced in respiration. Proc. Natl Acad. Sci. USA 96, 12 971 12 973.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12971-12973
    • Babcock, G.T.1
  • 10
    • 21844469742 scopus 로고    scopus 로고
    • Selective vulnerability of preterm white matter to oxidative damage defined by F2-isoprostanes
    • Back S. A. Luo N. L. Mallinson R. A. et al. 2005 Selective vulnerability of preterm white matter to oxidative damage defined by F2-isoprostanes. Ann. Neurol. 58, 108 120.
    • (2005) Ann. Neurol. , vol.58 , pp. 108-120
    • Back, S.A.1    Luo, N.L.2    Mallinson, R.A.3
  • 12
    • 0347419379 scopus 로고    scopus 로고
    • Effects of Coenzyme Q10 in Huntington's disease and early Parkinson's disease
    • Beal M. F. Shults C. W. 2003 Effects of Coenzyme Q10 in Huntington's disease and early Parkinson's disease. Biofactors 18, 153 161.
    • (2003) Biofactors , vol.18 , pp. 153-161
    • Beal, M.F.1    Shults, C.W.2
  • 13
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N. F. Sampat R. M. Kopito R. R. 2001 Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552 1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 14
    • 20344365107 scopus 로고    scopus 로고
    • Mild cognitive impairment - No benefit from vitamin E, little from donepezil
    • Blacker D. 2005 Mild cognitive impairment - no benefit from vitamin E, little from donepezil. N. Engl. J. Med. 352, 2439 2441.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 2439-2441
    • Blacker, D.1
  • 16
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota D. A. Davies K. J. 2002 Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 4, 674 680.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 17
    • 0032740245 scopus 로고    scopus 로고
    • Endogenous nitric oxide synthesis: Biological functions and pathophysiology
    • Bredt D. S. 1999 Endogenous nitric oxide synthesis: biological functions and pathophysiology. Free Radic. Res. 31, 577 596.
    • (1999) Free Radic. Res. , vol.31 , pp. 577-596
    • Bredt, D.S.1
  • 18
    • 0033230807 scopus 로고    scopus 로고
    • Tissue-specific functions of individual glutathione peroxidases
    • Brigelius-Flohe R. 1999 Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med. 27, 951 965.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 951-965
    • Brigelius-Flohe, R.1
  • 19
    • 0037354170 scopus 로고    scopus 로고
    • Brain iron uptake and homeostatic mechanisms: An overview
    • Burdo J. R. Connor J. R. 2003 Brain iron uptake and homeostatic mechanisms: an overview. Biometals 16, 63 75.
    • (2003) Biometals , vol.16 , pp. 63-75
    • Burdo, J.R.1    Connor, J.R.2
  • 20
    • 3042727978 scopus 로고    scopus 로고
    • Neuroglobin: A respiratory protein of the nervous system
    • Burmester T. Hankeln T. 2004 Neuroglobin: a respiratory protein of the nervous system. News Physiol. Sci. 19, 110 113.
    • (2004) News Physiol. Sci. , vol.19 , pp. 110-113
    • Burmester, T.1    Hankeln, T.2
  • 25
    • 1642301524 scopus 로고    scopus 로고
    • Proteomic analysis of brain proteins in the gracile axonal dystrophy (gad) mouse, a syndrome that emanates from dysfunctional ubiquitin carboxyl-terminal hydrolase L-1, reveals oxidation of key proteins
    • Castegna A. Thongboonkerd V. Klein J. Lynn B. C. Wang Y. L. Osaka H. Wada K. Butterfield D. A. 2004 Proteomic analysis of brain proteins in the gracile axonal dystrophy (gad) mouse, a syndrome that emanates from dysfunctional ubiquitin carboxyl-terminal hydrolase L-1, reveals oxidation of key proteins. J. Neurochem. 88, 1540 1546.
    • (2004) J. Neurochem. , vol.88 , pp. 1540-1546
    • Castegna, A.1    Thongboonkerd, V.2    Klein, J.3    Lynn, B.C.4    Wang, Y.L.5    Osaka, H.6    Wada, K.7    Butterfield, D.A.8
  • 27
    • 0141927134 scopus 로고    scopus 로고
    • Relationship between protein nitration and oxidation and development of hyperoxic seizures
    • Chavko M. Auker C. R. McCarron R. M. 2003 Relationship between protein nitration and oxidation and development of hyperoxic seizures. Nitric Oxide 9, 18 23.
    • (2003) Nitric Oxide , vol.9 , pp. 18-23
    • Chavko, M.1    Auker, C.R.2    McCarron, R.M.3
  • 28
    • 0029947826 scopus 로고    scopus 로고
    • Correlation of membrane lipid peroxidation with oxidation of hemoglobin variants: Possibly related to the rates of hemin release
    • Chiu D. T. van den Berg J. Kuypers F. A. Hung I. J. Wei J. S. Liu T. Z. 1996 Correlation of membrane lipid peroxidation with oxidation of hemoglobin variants: possibly related to the rates of hemin release. Free Radic. Biol. Med. 21, 89 95.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 89-95
    • Chiu, D.T.1    Van Den Berg, J.2    Kuypers, F.A.3    Hung, I.J.4    Wei, J.S.5    Liu, T.Z.6
  • 29
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J. Levey A. I. Weintraub S. T. Rees H. D. Gearing M. Chin L. S. Li L. 2004 Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J. Biol. Chem. 279, 13 256 13 264.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 30
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A. Brundin P. 2003 The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40, 427 446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 31
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • Davies M. J. 2005 The oxidative environment and protein damage. Biochim. Biophys. Acta 1703, 93 109.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 93-109
    • Davies, M.J.1
  • 32
    • 0036583274 scopus 로고    scopus 로고
    • Effects of reactive gamma-ketoaldehydes formed by the isoprostane pathway (isoketals) and cyclooxygenase pathway (levuglandins) on proteasome function
    • Davies S. S. Amarnath V. Montine K. S. Bernoud-Hubac N. Boutaud O. Montine T. J. Roberts L. J. II. 2002 Effects of reactive gamma-ketoaldehydes formed by the isoprostane pathway (isoketals) and cyclooxygenase pathway (levuglandins) on proteasome function. FASEB J. 16, 715 717.
    • (2002) FASEB J. , vol.16 , pp. 715-717
    • Davies, S.S.1    Amarnath, V.2    Montine, K.S.3    Bernoud-Hubac, N.4    Boutaud, O.5    Montine, T.J.6    Roberts, I.I.L.J.7
  • 33
    • 0034223128 scopus 로고    scopus 로고
    • A re-evaluation of the antioxidant activity of purified carnosine
    • Decker E. A. Livisay S. A. Zhou S. 2000 A re-evaluation of the antioxidant activity of purified carnosine. Biochemistry (Mosc.) 65, 766 770.
    • (2000) Biochemistry (Mosc.) , vol.65 , pp. 766-770
    • Decker, E.A.1    Livisay, S.A.2    Zhou, S.3
  • 34
    • 0037728958 scopus 로고    scopus 로고
    • Proteasome inhibitors induce intracellular protein aggregation and cell death by an oxygen-dependent mechanism
    • Demasi M. Davies K. J. 2003 Proteasome inhibitors induce intracellular protein aggregation and cell death by an oxygen-dependent mechanism. FEBS Lett. 542, 89 94.
    • (2003) FEBS Lett. , vol.542 , pp. 89-94
    • Demasi, M.1    Davies, K.J.2
  • 35
    • 9744223523 scopus 로고    scopus 로고
    • Proteasome inhibition increases DNA and RNA oxidation in astrocyte and neuron cultures
    • Ding Q. Dimayuga E. Markesbery W. R. Keller J. N. 2004 Proteasome inhibition increases DNA and RNA oxidation in astrocyte and neuron cultures. J. Neurochem. 91, 1211 1218.
    • (2004) J. Neurochem. , vol.91 , pp. 1211-1218
    • Ding, Q.1    Dimayuga, E.2    Markesbery, W.R.3    Keller, J.N.4
  • 37
    • 13844292636 scopus 로고    scopus 로고
    • Nitric oxide and neurological disorders
    • Duncan A. J. Heales S. J. 2005 Nitric oxide and neurological disorders. Mol. Aspects Med. 26, 67 96.
    • (2005) Mol. Aspects Med. , vol.26 , pp. 67-96
    • Duncan, A.J.1    Heales, S.J.2
  • 40
    • 28244466766 scopus 로고    scopus 로고
    • Differential modulation of base excision repair activities during brain ontogeny: Implications for repair of transcribed DNA
    • Englander E. W. Ma H. 2006 Differential modulation of base excision repair activities during brain ontogeny: implications for repair of transcribed DNA. Mech. Ageing Dev. 127, 64 69.
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 64-69
    • Englander, E.W.1    Ma, H.2
  • 41
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H. Schaur R. J. Zollner H. 1991 Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11, 81 128.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 42
    • 4444339833 scopus 로고    scopus 로고
    • Oxidative DNA damage and disease: Induction, repair and significance
    • Evans M. D. Dizdaroglu M. Cooke M. S. 2004 Oxidative DNA damage and disease: induction, repair and significance. Mutat. Res. 567, 1 61.
    • (2004) Mutat. Res. , vol.567 , pp. 1-61
    • Evans, M.D.1    Dizdaroglu, M.2    Cooke, M.S.3
  • 43
    • 1042288280 scopus 로고    scopus 로고
    • The intracellular location and function of proteins of neuronal ceroid lipofuscinoses
    • Ezaki J. Kominami E. 2004 The intracellular location and function of proteins of neuronal ceroid lipofuscinoses. Brain Pathol. 14, 77 85.
    • (2004) Brain Pathol. , vol.14 , pp. 77-85
    • Ezaki, J.1    Kominami, E.2
  • 44
    • 0041922325 scopus 로고    scopus 로고
    • The isoprostanes: Unique products of arachidonic acid oxidation - A review
    • Fam S. S. Morrow J. D. 2003 The isoprostanes: unique products of arachidonic acid oxidation - a review. Curr. Med. Chem. 10, 1723 1740.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1723-1740
    • Fam, S.S.1    Morrow, J.D.2
  • 45
    • 0035688664 scopus 로고    scopus 로고
    • Neurochemical consequences of kainate-induced toxicity in brain: Involvement of arachidonic acid release and prevention of toxicity by phospholipase A(2) inhibitors
    • Farooqui A. A. Ong W. Y. Lu X. R. Halliwell B. Horrocks L. A. 2001 Neurochemical consequences of kainate-induced toxicity in brain: involvement of arachidonic acid release and prevention of toxicity by phospholipase A(2) inhibitors. Brain Res. Brain Res. Rev. 38, 61 78.
    • (2001) Brain Res. Brain Res. Rev. , vol.38 , pp. 61-78
    • Farooqui, A.A.1    Ong, W.Y.2    Lu, X.R.3    Halliwell, B.4    Horrocks, L.A.5
  • 48
    • 0024308039 scopus 로고
    • Superoxide dismutases. An adaptation to a paramagnetic gas
    • Fridovich I. 1989 Superoxide dismutases. An adaptation to a paramagnetic gas. J. Biol. Chem. 264, 7761 7764.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7761-7764
    • Fridovich, I.1
  • 49
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. 1995 Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64, 97 112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 50
    • 0033396970 scopus 로고    scopus 로고
    • Fundamental aspects of reactive oxygen species, or what's the matter with oxygen?
    • Fridovich I. 1999 Fundamental aspects of reactive oxygen species, or what's the matter with oxygen? Ann. N. Y. Acad. Sci. 893, 13 18.
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 13-18
    • Fridovich, I.1
  • 51
    • 25644452043 scopus 로고    scopus 로고
    • Novel multifunctional neuroprotective iron chelator-monoamine oxidase inhibitor drugs for neurodegenerative diseases. in vivo selective brain monoamine oxidase inhibition and prevention of MPTP-induced striatal dopamine depletion
    • Gal S. Zheng H. Fridkin M. Youdim M. B. 2005 Novel multifunctional neuroprotective iron chelator-monoamine oxidase inhibitor drugs for neurodegenerative diseases. In vivo selective brain monoamine oxidase inhibition and prevention of MPTP-induced striatal dopamine depletion. J. Neurochem. 95, 79 88.
    • (2005) J. Neurochem. , vol.95 , pp. 79-88
    • Gal, S.1    Zheng, H.2    Fridkin, M.3    Youdim, M.B.4
  • 52
    • 0037466621 scopus 로고    scopus 로고
    • Biochemistry. An overoxidation journey with a return ticket
    • Georgiou G. Masip L. 2003 Biochemistry. An overoxidation journey with a return ticket. Science 300, 592 594.
    • (2003) Science , vol.300 , pp. 592-594
    • Georgiou, G.1    Masip, L.2
  • 53
    • 1542514722 scopus 로고    scopus 로고
    • Role of lipid hydroperoxides in photo-oxidative stress signaling
    • Girotti A. W. Kriska T. 2004 Role of lipid hydroperoxides in photo-oxidative stress signaling. Antioxid. Redox Signal. 6, 301 310.
    • (2004) Antioxid. Redox Signal. , vol.6 , pp. 301-310
    • Girotti, A.W.1    Kriska, T.2
  • 54
    • 10444229539 scopus 로고    scopus 로고
    • Role of cytochromes P450 in chemical toxicity and oxidative stress: Studies with CYP2E1
    • Gonzalez F. J. 2005 Role of cytochromes P450 in chemical toxicity and oxidative stress: studies with CYP2E1. Mutat. Res. 569, 101 110.
    • (2005) Mutat. Res. , vol.569 , pp. 101-110
    • Gonzalez, F.J.1
  • 57
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: Localisation, quantification, consequences for protein function and signal transduction
    • Greenacre S. A. Ischiropoulos H. 2001 Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction. Free Radic. Res. 34, 541 581.
    • (2001) Free Radic. Res. , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 58
    • 0041669528 scopus 로고    scopus 로고
    • The proteasomal system and HNE-modified proteins
    • Grune T. Davies K. J. 2003 The proteasomal system and HNE-modified proteins. Mol. Aspects Med. 24, 195 204.
    • (2003) Mol. Aspects Med. , vol.24 , pp. 195-204
    • Grune, T.1    Davies, K.J.2
  • 59
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T. Merker K. Sandig G. Davies K. J. 2003 Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem. Biophys. Res. Commun. 305, 709 718.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 60
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • Grune T. Jung T. Merker K. Davies K. J. 2004 Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36, 2519 2530.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.4
  • 61
    • 22744444561 scopus 로고    scopus 로고
    • Calorie restriction and SIR2 genes - Towards a mechanism
    • Guarente L. 2005 Calorie restriction and SIR2 genes - towards a mechanism. Mech. Ageing Dev. 126, 923 928.
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 923-928
    • Guarente, L.1
  • 62
    • 0020529963 scopus 로고
    • Antioxidant properties of caeruloplasmin towards iron- and copper-dependent oxygen radical formation
    • Gutteridge J. M. 1983 Antioxidant properties of caeruloplasmin towards iron- and copper-dependent oxygen radical formation. FEBS Lett. 157, 37 40.
    • (1983) FEBS Lett. , vol.157 , pp. 37-40
    • Gutteridge, J.M.1
  • 63
    • 0022469346 scopus 로고
    • Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides
    • Gutteridge J. M. 1986 Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides. FEBS Lett. 201, 291 295.
    • (1986) FEBS Lett. , vol.201 , pp. 291-295
    • Gutteridge, J.M.1
  • 64
    • 0026635456 scopus 로고
    • Iron and oxygen radicals in brain
    • Gutteridge J. M. 1992 Iron and oxygen radicals in brain. Ann. Neurol. 32, S16 S21.
    • (1992) Ann. Neurol. , vol.32
    • Gutteridge, J.M.1
  • 65
    • 0024241523 scopus 로고
    • Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation
    • Gutteridge J. M. Smith A. 1988 Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation. Biochem. J. 256, 861 865.
    • (1988) Biochem. J. , vol.256 , pp. 861-865
    • Gutteridge, J.M.1    Smith, A.2
  • 66
    • 0021207254 scopus 로고
    • Manganese ions, oxidation reactions and the superoxide radical
    • Halliwell B. 1984 Manganese ions, oxidation reactions and the superoxide radical. Neurotoxicology 5, 113 117.
    • (1984) Neurotoxicology , vol.5 , pp. 113-117
    • Halliwell, B.1
  • 67
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. 1992 Reactive oxygen species and the central nervous system. J. Neurochem. 59, 1609 1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 68
    • 0034796353 scopus 로고    scopus 로고
    • Role of free radicals in the neurodegenerative diseases: Therapeutic implications for antioxidant treatment
    • Halliwell B. 2001 Role of free radicals in the neurodegenerative diseases: therapeutic implications for antioxidant treatment. Drugs Aging 18, 685 716.
    • (2001) Drugs Aging , vol.18 , pp. 685-716
    • Halliwell, B.1
  • 69
    • 0036268224 scopus 로고    scopus 로고
    • Hypothesis: Proteasomal dysfunction: A primary event in neurodegeneration that leads to nitrative and oxidative stress and subsequent cell death
    • Halliwell B. 2002 Hypothesis: proteasomal dysfunction: a primary event in neurodegeneration that leads to nitrative and oxidative stress and subsequent cell death. Ann. N. Y. Acad. Sci. 962, 182 194.
    • (2002) Ann. N. Y. Acad. Sci. , vol.962 , pp. 182-194
    • Halliwell, B.1
  • 70
    • 0037430971 scopus 로고    scopus 로고
    • Oxidative stress in cell culture: An under-appreciated problem?
    • Halliwell B. 2003 Oxidative stress in cell culture: an under-appreciated problem? FEBS Lett. 540, 3 6.
    • (2003) FEBS Lett. , vol.540 , pp. 3-6
    • Halliwell, B.1
  • 71
    • 33846313981 scopus 로고    scopus 로고
    • Proteasomal dysfunction: A common feature of all neurodegenerative diseases? Implications for the environmental origins of neurodegeneration
    • in press:.
    • Halliwell B. 2006 Proteasomal dysfunction: a common feature of all neurodegenerative diseases? Implications for the environmental origins of neurodegeneration. Antiox. Redox Signal in press :.
    • (2006) Antiox. Redox Signal
    • Halliwell, B.1
  • 72
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B. Gutteridge J. M. 1984 Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219, 1 14.
    • (1984) Biochem. J. , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 73
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B. Gutteridge J. M. 1990 Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol. 186, 1 85.
    • (1990) Methods Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 74
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation. An update
    • Halliwell B. Gutteridge J. M. 1992 Biologically relevant metal ion-dependent hydroxyl radical generation. An update. FEBS Lett. 307, 108 112.
    • (1992) FEBS Lett. , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.2
  • 75
    • 0030809468 scopus 로고    scopus 로고
    • Lipid peroxidation in brain homogenates: The role of iron and hydroxyl radicals
    • Halliwell B. Gutteridge J. M. 1997 Lipid peroxidation in brain homogenates: the role of iron and hydroxyl radicals. J. Neurochem. 69, 1330 1331.
    • (1997) J. Neurochem. , vol.69 , pp. 1330-1331
    • Halliwell, B.1    Gutteridge, J.M.2
  • 77
    • 2942572700 scopus 로고    scopus 로고
    • Measuring reactive species and oxidative damage in vivo and in cell culture: How should you do it and what do the results mean?
    • Halliwell B. Whiteman M. 2004 Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean? Br. J. Pharmacol. 142, 231 255.
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 78
    • 0032715834 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite. the ugly, the uglier and the not so good: A personal view of recent controversies
    • Halliwell B. Zhao K. Whiteman M. 1999 Nitric oxide and peroxynitrite. The ugly, the uglier and the not so good: a personal view of recent controversies. Free Radic. Res. 31, 651 669.
    • (1999) Free Radic. Res. , vol.31 , pp. 651-669
    • Halliwell, B.1    Zhao, K.2    Whiteman, M.3
  • 79
    • 13844298231 scopus 로고    scopus 로고
    • Health promotion by flavonoids, tocopherols, tocotrienols, and other phenols: Direct or indirect effects? Antioxidant or not?
    • Halliwell B. Rafter J. Jenner A. 2005 Health promotion by flavonoids, tocopherols, tocotrienols, and other phenols: direct or indirect effects? Antioxidant or not? Am. J. Clin. Nutr. 81, 268S 276S.
    • (2005) Am. J. Clin. Nutr. , vol.81
    • Halliwell, B.1    Rafter, J.2    Jenner, A.3
  • 80
    • 20144389286 scopus 로고    scopus 로고
    • Antioxidant treatment of patients with Friedreich ataxia: Four-year follow-up
    • Hart P. E. Lodi R. Rajagopalan B. et al. 2005 Antioxidant treatment of patients with Friedreich ataxia: four-year follow-up. Arch. Neurol. 62, 621 626.
    • (2005) Arch. Neurol. , vol.62 , pp. 621-626
    • Hart, P.E.1    Lodi, R.2    Rajagopalan, B.3
  • 81
    • 14944341253 scopus 로고    scopus 로고
    • Vitamin e in neural and visual function
    • Hayton S. M. Muller D. P. 2004 Vitamin E in neural and visual function. Ann. N. Y. Acad. Sci. 1031, 263 270.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1031 , pp. 263-270
    • Hayton, S.M.1    Muller, D.P.2
  • 82
    • 2542447171 scopus 로고    scopus 로고
    • Reactivity studies of the Fe(III) and Fe(II) NO forms of human neuroglobin reveal a potential role against oxidative stress
    • Herold S. Fago A. Weber R. E. Dewilde S. Moens L. 2004 Reactivity studies of the Fe(III) and Fe(II) NO forms of human neuroglobin reveal a potential role against oxidative stress. J. Biol. Chem. 279, 22 841 22 847.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22841-22847
    • Herold, S.1    Fago, A.2    Weber, R.E.3    Dewilde, S.4    Moens, L.5
  • 83
    • 8844245412 scopus 로고    scopus 로고
    • A mutation in a novel ATP-dependent Lon protease gene in a kindred with mild mental retardation
    • Higgins J. J. Pucilowska J. Lombardi R. Q. Rooney J. P. 2004 A mutation in a novel ATP-dependent Lon protease gene in a kindred with mild mental retardation. Neurology 63, 1927 1931.
    • (2004) Neurology , vol.63 , pp. 1927-1931
    • Higgins, J.J.1    Pucilowska, J.2    Lombardi, R.Q.3    Rooney, J.P.4
  • 84
    • 0942298545 scopus 로고    scopus 로고
    • Endogenous mitochondrial oxidative stress: Neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice
    • Hinerfeld D. Traini M. D. Weinberger R. P. Cochran B. Doctrow S. R. Harry J. Melov S. 2004 Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice. J. Neurochem. 88, 657 667.
    • (2004) J. Neurochem. , vol.88 , pp. 657-667
    • Hinerfeld, D.1    Traini, M.D.2    Weinberger, R.P.3    Cochran, B.4    Doctrow, S.R.5    Harry, J.6    Melov, S.7
  • 85
    • 1642464743 scopus 로고    scopus 로고
    • Isomer-specific contractile effects of a series of synthetic F2-isoprostanes on retinal and cerebral microvasculature
    • Hou X. Roberts L. J. II., Gobeil F. Jr. et al. 2004 Isomer-specific contractile effects of a series of synthetic F2-isoprostanes on retinal and cerebral microvasculature. Free Radic. Biol. Med. 36, 163 172.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 163-172
    • Hou, X.1    Roberts, I.I.L.J.2    Gobeil Jr., F.3
  • 86
    • 28444445972 scopus 로고    scopus 로고
    • Glyoxalase 1 and glutathione reductase 1 regulate anxiety in mice
    • Hovatta I. Tennant R. S. Helton R. et al. 2005 Glyoxalase 1 and glutathione reductase 1 regulate anxiety in mice. Nature 438, 662 666.
    • (2005) Nature , vol.438 , pp. 662-666
    • Hovatta, I.1    Tennant, R.S.2    Helton, R.3
  • 87
    • 0037739660 scopus 로고    scopus 로고
    • Brain CYP2E1 is induced by nicotine and ethanol in rat and is higher in smokers and alcoholics
    • Howard L. A. Miksys S. Hoffmann E. Mash D. Tyndale R. F. 2003 Brain CYP2E1 is induced by nicotine and ethanol in rat and is higher in smokers and alcoholics. Br. J. Pharmacol. 138, 1376 1386.
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 1376-1386
    • Howard, L.A.1    Miksys, S.2    Hoffmann, E.3    Mash, D.4    Tyndale, R.F.5
  • 88
    • 0035949516 scopus 로고    scopus 로고
    • Dehydroascorbic acid, a blood-brain barrier transportable form of vitamin C, mediates potent cerebroprotection in experimental stroke
    • Huang J. Agus D. B. Winfree C. J. et al. 2001 Dehydroascorbic acid, a blood-brain barrier transportable form of vitamin C, mediates potent cerebroprotection in experimental stroke. Proc. Natl Acad. Sci. USA 98, 11 720 11 724.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11720-11724
    • Huang, J.1    Agus, D.B.2    Winfree, C.J.3
  • 89
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay J. A. 2003 Pathways of oxidative damage. Annu. Rev. Microbiol. 57, 395 418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 90
    • 0037237927 scopus 로고    scopus 로고
    • Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?
    • Ischiropoulos H. Beckman J. S. 2003 Oxidative stress and nitration in neurodegeneration: cause, effect, or association? J. Clin. Invest. 111, 163 169.
    • (2003) J. Clin. Invest. , vol.111 , pp. 163-169
    • Ischiropoulos, H.1    Beckman, J.S.2
  • 91
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • Jenner P. 2003 Oxidative stress in Parkinson's disease. Ann. Neurol. 53, S26 S36.
    • (2003) Ann. Neurol. , vol.53
    • Jenner, P.1
  • 92
    • 0038711587 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system
    • Jeong S. Y. David S. 2003 Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system. J. Biol. Chem. 278, 27 144 27 148.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27144-27148
    • Jeong, S.Y.1    David, S.2
  • 94
    • 0037101878 scopus 로고    scopus 로고
    • Chemistry-based studies on oxidative DNA damage: Formation, repair, and mutagenesis
    • Kasai H. 2002 Chemistry-based studies on oxidative DNA damage: formation, repair, and mutagenesis. Free Radic. Biol. Med. 33, 450 456.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 450-456
    • Kasai, H.1
  • 98
    • 0141869839 scopus 로고    scopus 로고
    • Neurodegeneration in striatum induced by the mitochondrial toxin 3-nitropropionic acid: Role of matrix metalloproteinase-9 in early blood-brain barrier disruption?
    • Kim G. W. Gasche Y. Grzeschik S. Copin J. C. Maier C. M. Chan P. H. 2003 Neurodegeneration in striatum induced by the mitochondrial toxin 3-nitropropionic acid: role of matrix metalloproteinase-9 in early blood-brain barrier disruption? J. Neurosci. 23, 8733 8742.
    • (2003) J. Neurosci. , vol.23 , pp. 8733-8742
    • Kim, G.W.1    Gasche, Y.2    Grzeschik, S.3    Copin, J.C.4    Maier, C.M.5    Chan, P.H.6
  • 99
    • 13944262937 scopus 로고    scopus 로고
    • Understanding the odd science of aging
    • Kirkwood T. B. 2005 Understanding the odd science of aging. Cell 120, 437 447.
    • (2005) Cell , vol.120 , pp. 437-447
    • Kirkwood, T.B.1
  • 100
    • 18244415707 scopus 로고    scopus 로고
    • Defenses against peroxynitrite: Selenocompounds and flavonoids
    • Klotz L. O. Sies H. 2003 Defenses against peroxynitrite: selenocompounds and flavonoids. Toxicol. Lett. 140-141, 125 132.
    • (2003) Toxicol. Lett. , vol.140-141 , pp. 125-132
    • Klotz, L.O.1    Sies, H.2
  • 101
    • 19444374556 scopus 로고    scopus 로고
    • Mediation of cell death by poly(ADP-ribose) polymerase-1
    • Koh D. W. Dawson T. M. Dawson V. L. 2005 Mediation of cell death by poly(ADP-ribose) polymerase-1. Pharmacol. Res. 52, 5 14.
    • (2005) Pharmacol. Res. , vol.52 , pp. 5-14
    • Koh, D.W.1    Dawson, T.M.2    Dawson, V.L.3
  • 103
    • 9144257277 scopus 로고    scopus 로고
    • Tissue distribution and putative physiological function of NOX family NADPH oxidases
    • Krause K. H. 2004 Tissue distribution and putative physiological function of NOX family NADPH oxidases. Jpn J. Infect. Dis. 57, S28 S29.
    • (2004) Jpn J. Infect. Dis. , vol.57
    • Krause, K.H.1
  • 105
    • 13244249527 scopus 로고    scopus 로고
    • Why do neurons enter the cell cycle?
    • Kruman I. I. 2004 Why do neurons enter the cell cycle? Cell Cycle 3, 769 773.
    • (2004) Cell Cycle , vol.3 , pp. 769-773
    • Kruman, I.I.1
  • 107
    • 18044391656 scopus 로고    scopus 로고
    • Characterization of superoxide production sites in isolated rat brain and skeletal muscle mitochondria
    • Kudin A. P. Debska-Vielhaber G. Kunz W. S. 2005 Characterization of superoxide production sites in isolated rat brain and skeletal muscle mitochondria. Biomed. Pharmacother. 59, 163 168.
    • (2005) Biomed. Pharmacother. , vol.59 , pp. 163-168
    • Kudin, A.P.1    Debska-Vielhaber, G.2    Kunz, W.S.3
  • 109
    • 0034946830 scopus 로고    scopus 로고
    • Effect of proteasome inhibition on cellular oxidative damage, antioxidant defences and nitric oxide production
    • Lee M. H. Hyun D. H. Jenner P. Halliwell B. 2001 Effect of proteasome inhibition on cellular oxidative damage, antioxidant defences and nitric oxide production. J. Neurochem. 78, 32 41.
    • (2001) J. Neurochem. , vol.78 , pp. 32-41
    • Lee, M.H.1    Hyun, D.H.2    Jenner, P.3    Halliwell, B.4
  • 110
    • 0035142573 scopus 로고    scopus 로고
    • Absorption and tissue distribution of zeaxanthin and lutein in rhesus monkeys after taking Fructus lycii (Gou Qi Zi) extract
    • Leung I. Tso M. Li W. Lam T. 2001 Absorption and tissue distribution of zeaxanthin and lutein in rhesus monkeys after taking Fructus lycii (Gou Qi Zi) extract. Invest. Ophthalmol. Vis. Sci. 42, 466 471.
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 466-471
    • Leung, I.1    Tso, M.2    Li, W.3    Lam, T.4
  • 111
    • 4444360218 scopus 로고    scopus 로고
    • Iron-sulfur enzyme mediated mitochondrial superoxide toxicity in experimental Parkinson's disease
    • Liang L. P. Patel M. 2004 Iron-sulfur enzyme mediated mitochondrial superoxide toxicity in experimental Parkinson's disease. J. Neurochem. 90, 1076 1084.
    • (2004) J. Neurochem. , vol.90 , pp. 1076-1084
    • Liang, L.P.1    Patel, M.2
  • 112
    • 23044460297 scopus 로고    scopus 로고
    • Minocycline blocks bilirubin neurotoxicity and prevents hyperbilirubinemia-induced cerebellar hypoplasia in the Gunn rat
    • Lin S. Wei X. Bales K. R. Paul A. B. Ma Z. Yan G. Paul S. M. Du Y. 2005 Minocycline blocks bilirubin neurotoxicity and prevents hyperbilirubinemia- induced cerebellar hypoplasia in the Gunn rat. Eur. J. Neurosci. 22, 21 27.
    • (2005) Eur. J. Neurosci. , vol.22 , pp. 21-27
    • Lin, S.1    Wei, X.2    Bales, K.R.3    Paul, A.B.4    Ma, Z.5    Yan, G.6    Paul, S.M.7    Du, Y.8
  • 113
    • 0032785355 scopus 로고    scopus 로고
    • Cellular expression of xanthine oxidoreductase protein in normal human tissues
    • Linder N. Rapola J. Raivio K. O. 1999 Cellular expression of xanthine oxidoreductase protein in normal human tissues. Lab. Invest. 79, 967 974.
    • (1999) Lab. Invest. , vol.79 , pp. 967-974
    • Linder, N.1    Rapola, J.2    Raivio, K.O.3
  • 115
    • 0032819067 scopus 로고    scopus 로고
    • Increase in external glutamate and NMDA receptor activation contribute to H2O2-induced neuronal apoptosis
    • Mailly F. Marin P. Israel M. Glowinski J. Premont J. 1999 Increase in external glutamate and NMDA receptor activation contribute to H2O2-induced neuronal apoptosis. J. Neurochem. 73, 1181 1188.
    • (1999) J. Neurochem. , vol.73 , pp. 1181-1188
    • Mailly, F.1    Marin, P.2    Israel, M.3    Glowinski, J.4    Premont, J.5
  • 116
    • 20944444111 scopus 로고    scopus 로고
    • Multifunctional activities of green tea catechins in neuroprotection. Modulation of cell survival genes, iron-dependent oxidative stress and PKC signaling pathway
    • Mandel S. A. Avramovich-Tirosh Y. Reznichenko L. Zheng H. Weinreb O. Amit T. Youdim M. B. 2005 Multifunctional activities of green tea catechins in neuroprotection. Modulation of cell survival genes, iron-dependent oxidative stress and PKC signaling pathway. Neurosignals 14, 46 60.
    • (2005) Neurosignals , vol.14 , pp. 46-60
    • Mandel, S.A.1    Avramovich-Tirosh, Y.2    Reznichenko, L.3    Zheng, H.4    Weinreb, O.5    Amit, T.6    Youdim, M.B.7
  • 117
    • 0035054659 scopus 로고    scopus 로고
    • Comparison of the radical trapping ability of PBN, S-PPBN and NXY-059
    • Maples K. R. Ma F. Zhang Y. K. 2001 Comparison of the radical trapping ability of PBN, S-PPBN and NXY-059. Free Radic. Res. 34, 417 426.
    • (2001) Free Radic. Res. , vol.34 , pp. 417-426
    • Maples, K.R.1    Ma, F.2    Zhang, Y.K.3
  • 118
    • 10844282711 scopus 로고    scopus 로고
    • Nitrone-related therapeutics: Potential of NXY-059 for the treatment of acute ischaemic stroke
    • Maples K. R. Green A. R. Floyd R. A. 2004 Nitrone-related therapeutics: potential of NXY-059 for the treatment of acute ischaemic stroke. CNS Drugs 18, 1071 1084.
    • (2004) CNS Drugs , vol.18 , pp. 1071-1084
    • Maples, K.R.1    Green, A.R.2    Floyd, R.A.3
  • 121
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide
    • Mark R. J. Lovell M. A. Markesbery W. R. Uchida K. Mattson M. P. 1997 A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β-peptide. J. Neurochem. 68, 255 264.
    • (1997) J. Neurochem. , vol.68 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 122
    • 27644446857 scopus 로고    scopus 로고
    • Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment
    • Markesbery W. R. Kryscio R. J. Lovell M. A. Morrow J. D. 2005 Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment. Ann. Neurol. 58, 730 735.
    • (2005) Ann. Neurol. , vol.58 , pp. 730-735
    • Markesbery, W.R.1    Kryscio, R.J.2    Lovell, M.A.3    Morrow, J.D.4
  • 123
    • 33646493798 scopus 로고    scopus 로고
    • Manganese neurotoxicity: Connecting the dots along the continuum of dysfunction
    • in press:.
    • Martin C. J. 2006 Manganese neurotoxicity: Connecting the dots along the continuum of dysfunction. Neurotoxicology in press :.
    • (2006) Neurotoxicology
    • Martin, C.J.1
  • 124
    • 0036790835 scopus 로고    scopus 로고
    • Roles of vitamins e and C on neurodegenerative diseases and cognitive performance
    • Martin A. Youdim K. Szprengiel A. Shukitt-Hale B. Joseph J. 2002 Roles of vitamins E and C on neurodegenerative diseases and cognitive performance. Nutr. Rev. 60, 308 326.
    • (2002) Nutr. Rev. , vol.60 , pp. 308-326
    • Martin, A.1    Youdim, K.2    Szprengiel, A.3    Shukitt-Hale, B.4    Joseph, J.5
  • 125
    • 23244450626 scopus 로고    scopus 로고
    • Neuroscience. Preventing Alzheimer's: A lifelong commitment?
    • Marx J. 2005 Neuroscience. Preventing Alzheimer's: a lifelong commitment? Science 309, 864 866.
    • (2005) Science , vol.309 , pp. 864-866
    • Marx, J.1
  • 126
    • 0042536471 scopus 로고    scopus 로고
    • Neuronal and glial calcium signaling in Alzheimer's disease
    • Mattson M. P. Chan S. L. 2003 Neuronal and glial calcium signaling in Alzheimer's disease. Cell Calcium 34, 385 397.
    • (2003) Cell Calcium , vol.34 , pp. 385-397
    • Mattson, M.P.1    Chan, S.L.2
  • 127
    • 23844455290 scopus 로고    scopus 로고
    • Prophylactic activation of neuroprotective stress response pathways by dietary and behavioral manipulations
    • Mattson M. P. Duan W. Wan R. Guo Z. 2004 Prophylactic activation of neuroprotective stress response pathways by dietary and behavioral manipulations. Neurorx 1, 111 116.
    • (2004) Neurorx , vol.1 , pp. 111-116
    • Mattson, M.P.1    Duan, W.2    Wan, R.3    Guo, Z.4
  • 128
    • 13844298846 scopus 로고    scopus 로고
    • Concurrent administration of coenzyme Q10 and alpha-tocopherol improves learning in aged mice
    • McDonald S. R. Sohal R. S. Forster M. J. 2005 Concurrent administration of coenzyme Q10 and alpha-tocopherol improves learning in aged mice. Free Radic. Biol. Med. 38, 729 736.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 729-736
    • McDonald, S.R.1    Sohal, R.S.2    Forster, M.J.3
  • 131
    • 3042519581 scopus 로고    scopus 로고
    • The unique regulation of brain cytochrome P450 2 (CYP2) family enzymes by drugs and genetics
    • Miksys S. Tyndale R. F. 2004 The unique regulation of brain cytochrome P450 2 (CYP2) family enzymes by drugs and genetics. Drug Metab. Rev. 36, 313 333.
    • (2004) Drug Metab. Rev. , vol.36 , pp. 313-333
    • Miksys, S.1    Tyndale, R.F.2
  • 132
    • 0036736195 scopus 로고    scopus 로고
    • Regional and cellular expression of CYP2D6 in human brain: Higher levels in alcoholics
    • Miksys S. Rao Y. Hoffmann E. Mash D. C. Tyndale R. F. 2002 Regional and cellular expression of CYP2D6 in human brain: higher levels in alcoholics. J. Neurochem. 82, 1376 1387.
    • (2002) J. Neurochem. , vol.82 , pp. 1376-1387
    • Miksys, S.1    Rao, Y.2    Hoffmann, E.3    Mash, D.C.4    Tyndale, R.F.5
  • 134
    • 0346847502 scopus 로고    scopus 로고
    • Aceruloplasminemia, an iron metabolic disorder
    • Miyajima H. 2003 Aceruloplasminemia, an iron metabolic disorder. Neuropathology 23, 345 350.
    • (2003) Neuropathology , vol.23 , pp. 345-350
    • Miyajima, H.1
  • 135
    • 0038288716 scopus 로고    scopus 로고
    • Singlet molecular oxygen generated from lipid hydroperoxides by the Russell mechanism: Studies using 18(O)-labeled linoleic acid hydroperoxide and monomol light emission measurements
    • Miyamoto S. Martinez G. R. Medeiros M. H. Di Mascio P. 2003 Singlet molecular oxygen generated from lipid hydroperoxides by the Russell mechanism: studies using 18(O)-labeled linoleic acid hydroperoxide and monomol light emission measurements. J. Am. Chem. Soc. 125, 6172 6179.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6172-6179
    • Miyamoto, S.1    Martinez, G.R.2    Medeiros, M.H.3    Di Mascio, P.4
  • 137
    • 0036799799 scopus 로고    scopus 로고
    • Antioxidants as treatment for neurodegenerative disorders
    • Moosmann B. Behl C. 2002 Antioxidants as treatment for neurodegenerative disorders. Expert Opin. Invest. Drugs 11, 1407 1435.
    • (2002) Expert Opin. Invest. Drugs , vol.11 , pp. 1407-1435
    • Moosmann, B.1    Behl, C.2
  • 139
    • 13244279737 scopus 로고    scopus 로고
    • Quantification of isoprostanes as indices of oxidant stress and the risk of atherosclerosis in humans
    • Morrow J. D. 2005 Quantification of isoprostanes as indices of oxidant stress and the risk of atherosclerosis in humans. Arterioscler. Thromb. Vasc. Biol. 25, 279 286.
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 279-286
    • Morrow, J.D.1
  • 140
    • 0038611016 scopus 로고    scopus 로고
    • Selenium-deficient diet enhances protein oxidation and affects methionine sulfoxide reductase (MsrB) protein level in certain mouse tissues
    • Moskovitz J. Stadtman E. R. 2003 Selenium-deficient diet enhances protein oxidation and affects methionine sulfoxide reductase (MsrB) protein level in certain mouse tissues. Proc. Natl Acad. Sci. USA 100, 7486 7490.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 7486-7490
    • Moskovitz, J.1    Stadtman, E.R.2
  • 141
    • 0025265411 scopus 로고
    • Neurochemical, neurophysiological, and neuropathological studies in vitamin e deficiency
    • Muller D. P. Goss-Sampson M. A. 1990 Neurochemical, neurophysiological, and neuropathological studies in vitamin E deficiency. Crit. Rev. Neurobiol. 5, 239 263.
    • (1990) Crit. Rev. Neurobiol. , vol.5 , pp. 239-263
    • Muller, D.P.1    Goss-Sampson, M.A.2
  • 142
    • 17444386729 scopus 로고    scopus 로고
    • Cyclopentenone eicosanoids as mediators of neurodegeneration: A pathogenic mechanism of oxidative stress-mediated and cyclooxygenase-mediated neurotoxicity
    • Musiek E. S. Milne G. L. McLaughlin B. Morrow J. D. 2005 Cyclopentenone eicosanoids as mediators of neurodegeneration: a pathogenic mechanism of oxidative stress-mediated and cyclooxygenase-mediated neurotoxicity. Brain Pathol. 15, 149 158.
    • (2005) Brain Pathol. , vol.15 , pp. 149-158
    • Musiek, E.S.1    Milne, G.L.2    McLaughlin, B.3    Morrow, J.D.4
  • 143
    • 0034739448 scopus 로고    scopus 로고
    • Phospholipase A(2)s and lipid peroxidation
    • Nigam S. Schewe T. 2000 Phospholipase A(2)s and lipid peroxidation. Biochim. Biophys. Acta 1488, 167 181.
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 167-181
    • Nigam, S.1    Schewe, T.2
  • 144
    • 19744380563 scopus 로고    scopus 로고
    • Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo
    • Nimmerjahn A. Kirchhoff F. Helmchen F. 2005 Resting microglial cells are highly dynamic surveillants of brain parenchyma in vivo. Science 308, 1314 1318.
    • (2005) Science , vol.308 , pp. 1314-1318
    • Nimmerjahn, A.1    Kirchhoff, F.2    Helmchen, F.3
  • 145
    • 1542269162 scopus 로고    scopus 로고
    • The scientific basis for the current treatment of Parkinson's disease
    • Olanow C. W. 2004 The scientific basis for the current treatment of Parkinson's disease. Annu. Rev. Med. 55, 41 60.
    • (2004) Annu. Rev. Med. , vol.55 , pp. 41-60
    • Olanow, C.W.1
  • 146
    • 1842608817 scopus 로고    scopus 로고
    • Iron, atherosclerosis, and neurodegeneration: A key role for cholesterol in promoting iron-dependent oxidative damage?
    • Ong W. Y. Halliwell B. 2004 Iron, atherosclerosis, and neurodegeneration: a key role for cholesterol in promoting iron-dependent oxidative damage? Ann. N. Y. Acad. Sci. 1012, 51 64.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 51-64
    • Ong, W.Y.1    Halliwell, B.2
  • 147
    • 0034038541 scopus 로고    scopus 로고
    • Changes in glutathione in the hippocampus of rats injected with kainate: Depletion in neurons and upregulation in glia
    • Ong W. Y. Hu C. Y. Hjelle O. P. Ottersen O. P. Halliwell B. 2000a Changes in glutathione in the hippocampus of rats injected with kainate: depletion in neurons and upregulation in glia. Exp. Brain Res. 132, 510 516.
    • (2000) Exp. Brain Res. , vol.132 , pp. 510-516
    • Ong, W.Y.1    Hu, C.Y.2    Hjelle, O.P.3    Ottersen, O.P.4    Halliwell, B.5
  • 148
    • 0034656016 scopus 로고    scopus 로고
    • Distribution of hydroxynonenal-modified proteins in the kainate-lesioned rat hippocampus: Evidence that hydroxynonenal formation precedes neuronal cell death
    • Ong W. Y. Lu X. R. Hu C. Y. Halliwell B. 2000b Distribution of hydroxynonenal-modified proteins in the kainate-lesioned rat hippocampus: evidence that hydroxynonenal formation precedes neuronal cell death. Free Radic. Biol. Med. 28, 1214 1221.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1214-1221
    • Ong, W.Y.1    Lu, X.R.2    Hu, C.Y.3    Halliwell, B.4
  • 149
    • 16544394210 scopus 로고    scopus 로고
    • Neurodegenerative disease: Neuron protection agency
    • Orr H. T. 2004 Neurodegenerative disease: neuron protection agency. Nature 431, 747 748.
    • (2004) Nature , vol.431 , pp. 747-748
    • Orr, H.T.1
  • 151
    • 0033744466 scopus 로고    scopus 로고
    • Mechanisms of vitamin e regulation: Research over the past decade and focus on the future
    • Parks E. Traber M. G. 2000 Mechanisms of vitamin E regulation: research over the past decade and focus on the future. Antioxid. Redox Signal. 2, 405 412.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 405-412
    • Parks, E.1    Traber, M.G.2
  • 153
    • 20944435890 scopus 로고    scopus 로고
    • Emerging roles of thioredoxin cycle enzymes in the central nervous system
    • Patenaude A. Murthy M. R. Mirault M. E. 2005 Emerging roles of thioredoxin cycle enzymes in the central nervous system. Cell. Mol. Life Sci. 62, 1063 1080.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1063-1080
    • Patenaude, A.1    Murthy, M.R.2    Mirault, M.E.3
  • 154
    • 0034667888 scopus 로고    scopus 로고
    • Effect of a prolonged superoxide flux on transferrin and ferritin
    • Paul T. 2000 Effect of a prolonged superoxide flux on transferrin and ferritin. Arch. Biochem. Biophys. 382, 253 261.
    • (2000) Arch. Biochem. Biophys. , vol.382 , pp. 253-261
    • Paul, T.1
  • 155
    • 1642534405 scopus 로고    scopus 로고
    • A potentially critical role of phospholipases in central nervous system ischemic, traumatic, and neurodegenerative disorders
    • Phillis J. W. O'Regan M. H. 2004 A potentially critical role of phospholipases in central nervous system ischemic, traumatic, and neurodegenerative disorders. Brain Res. Brain Res. Rev. 44, 13 47.
    • (2004) Brain Res. Brain Res. Rev. , vol.44 , pp. 13-47
    • Phillis, J.W.1    O'Regan, M.H.2
  • 157
    • 84984565443 scopus 로고    scopus 로고
    • Neuroprotective effect of ebselen on rat hippocampal slices submitted to oxygen-glucose deprivation: Correlation with immunocontent of inducible nitric oxide synthase
    • Porciuncula L. O. Rocha J. B. Cimarosti H. Vinade L. Ghisleni G. Salbego C. G. Souza D. O. 2003 Neuroprotective effect of ebselen on rat hippocampal slices submitted to oxygen-glucose deprivation: correlation with immunocontent of inducible nitric oxide synthase. Neurosci. Lett. 346, 101 104.
    • (2003) Neurosci. Lett. , vol.346 , pp. 101-104
    • Porciuncula, L.O.1    Rocha, J.B.2    Cimarosti, H.3    Vinade, L.4    Ghisleni, G.5    Salbego, C.G.6    Souza, D.O.7
  • 158
    • 0035875690 scopus 로고    scopus 로고
    • Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis
    • Pratico D. Uryu K. Leight S. Trojanoswki J. Q. Lee V. M. 2001 Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis. J. Neurosci. 21, 4183 4187.
    • (2001) J. Neurosci. , vol.21 , pp. 4183-4187
    • Pratico, D.1    Uryu, K.2    Leight, S.3    Trojanoswki, J.Q.4    Lee, V.M.5
  • 159
    • 17644413217 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species: Weapons of neuronal destruction in models of Parkinson's disease
    • Przedborski S. Ischiropoulos H. 2005 Reactive oxygen and nitrogen species: weapons of neuronal destruction in models of Parkinson's disease. Antioxid. Redox Signal. 7, 685 693.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 685-693
    • Przedborski, S.1    Ischiropoulos, H.2
  • 160
    • 0023779695 scopus 로고
    • Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is haemoglobin a biological Fenton reagent?
    • Puppo A. Halliwell B. 1988 Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is haemoglobin a biological Fenton reagent? Biochem. J. 249, 185 190.
    • (1988) Biochem. J. , vol.249 , pp. 185-190
    • Puppo, A.1    Halliwell, B.2
  • 162
    • 33645141178 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell-death program: A novel HSP90-independent role for the small chaperone protein p23
    • Rao R. V. Niazi K. Mollahan P. Mao X. Crippen D. Poksay K. S. Chen S. Bredesen D. E. 2006 Coupling endoplasmic reticulum stress to the cell-death program: a novel HSP90-independent role for the small chaperone protein p23. Cell Death Differ. 13, 415 425.
    • (2006) Cell Death Differ. , vol.13 , pp. 415-425
    • Rao, R.V.1    Niazi, K.2    Mollahan, P.3    Mao, X.4    Crippen, D.5    Poksay, K.S.6    Chen, S.7    Bredesen, D.E.8
  • 163
    • 27544484846 scopus 로고    scopus 로고
    • Are mitochondria critical in the pathogenesis of Alzheimer's disease?
    • Reddy P. H. Beal M. F. 2005 Are mitochondria critical in the pathogenesis of Alzheimer's disease? Brain. Res. Rev. 49, 618 632.
    • (2005) Brain. Res. Rev. , vol.49 , pp. 618-632
    • Reddy, P.H.1    Beal, M.F.2
  • 164
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee S. G. Chae H. Z. Kim K. 2005 Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 38, 1543 1552.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 165
    • 0034194081 scopus 로고    scopus 로고
    • Ascorbate regulation and its neuroprotective role in the brain
    • Rice M. E. 2000 Ascorbate regulation and its neuroprotective role in the brain. Trends Neurosci. 23, 209 216.
    • (2000) Trends Neurosci. , vol.23 , pp. 209-216
    • Rice, M.E.1
  • 166
    • 0024431857 scopus 로고
    • The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine
    • Rice-Evans C. Okunade G. Khan R. 1989 The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine. Free Radic. Res. Commun. 7, 45 54.
    • (1989) Free Radic. Res. Commun. , vol.7 , pp. 45-54
    • Rice-Evans, C.1    Okunade, G.2    Khan, R.3
  • 167
    • 0037163887 scopus 로고    scopus 로고
    • Vitamin e sensitive genes in the developing rat fetal brain: A high-density oligonucleotide microarray analysis
    • Roy S. Lado B. H. Khanna S. Sen C. K. 2002 Vitamin E sensitive genes in the developing rat fetal brain: a high-density oligonucleotide microarray analysis. FEBS Lett. 530, 17 23.
    • (2002) FEBS Lett. , vol.530 , pp. 17-23
    • Roy, S.1    Lado, B.H.2    Khanna, S.3    Sen, C.K.4
  • 168
    • 85026171376 scopus 로고    scopus 로고
    • Idebenone treatment in Friedreich patients: One-year-long randomized placebo-controlled trial
    • Rustin P. Bonnet D. Rotig A. Munnich A. Sidi D. 2004 Idebenone treatment in Friedreich patients: one-year-long randomized placebo-controlled trial. Neurology 62, 524 525.
    • (2004) Neurology , vol.62 , pp. 524-525
    • Rustin, P.1    Bonnet, D.2    Rotig, A.3    Munnich, A.4    Sidi, D.5
  • 169
    • 18344363918 scopus 로고    scopus 로고
    • Relationship between dementia and nutrition-related factors and disorders: An overview
    • Salerno-Kennedy R. Cashman K. D. 2005 Relationship between dementia and nutrition-related factors and disorders: an overview. Int. J. Vitam. Nutr. Res. 75, 83 95.
    • (2005) Int. J. Vitam. Nutr. Res. , vol.75 , pp. 83-95
    • Salerno-Kennedy, R.1    Cashman, K.D.2
  • 170
    • 14744271216 scopus 로고    scopus 로고
    • Distinguishing levuglandins produced through the cyclooxygenase and isoprostane pathways
    • Salomon R. G. 2005 Distinguishing levuglandins produced through the cyclooxygenase and isoprostane pathways. Chem. Phys. Lipids 134, 1 20.
    • (2005) Chem. Phys. Lipids , vol.134 , pp. 1-20
    • Salomon, R.G.1
  • 173
    • 9244231109 scopus 로고    scopus 로고
    • High-field magnetic resonance imaging of brain iron: Birth of a biomarker?
    • Schenck J. F. Zimmerman E. A. 2004 High-field magnetic resonance imaging of brain iron: birth of a biomarker? NMR Biomed. 17, 433 445.
    • (2004) NMR Biomed. , vol.17 , pp. 433-445
    • Schenck, J.F.1    Zimmerman, E.A.2
  • 174
    • 0034642203 scopus 로고    scopus 로고
    • Oxidative stress in patients with Friedreich ataxia
    • Schulz J. B. Dehmer T. Schols L. et al. 2000 Oxidative stress in patients with Friedreich ataxia. Neurology 55, 1719 1721.
    • (2000) Neurology , vol.55 , pp. 1719-1721
    • Schulz, J.B.1    Dehmer, T.2    Schols, L.3
  • 175
    • 0027097615 scopus 로고
    • Distribution and antioxidant activity of a palm oil carotene fraction in rats
    • Serbinova E. Choo M. Packer L. 1992 Distribution and antioxidant activity of a palm oil carotene fraction in rats. Biochem. Int. 28, 881 886.
    • (1992) Biochem. Int. , vol.28 , pp. 881-886
    • Serbinova, E.1    Choo, M.2    Packer, L.3
  • 176
    • 0033387202 scopus 로고    scopus 로고
    • The alpha-ketoglutarate dehydrogenase complex
    • Sheu K. F. Blass J. P. 1999 The alpha-ketoglutarate dehydrogenase complex. Ann. N. Y. Acad. Sci. 893, 61 78.
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 61-78
    • Sheu, K.F.1    Blass, J.P.2
  • 177
    • 0018853019 scopus 로고
    • Hydrogen peroxide production by rat brain in vivo
    • Sinet P. M. Heikkila R. E. Cohen G. 1980 Hydrogen peroxide production by rat brain in vivo. J. Neurochem. 34, 1421 1428.
    • (1980) J. Neurochem. , vol.34 , pp. 1421-1428
    • Sinet, P.M.1    Heikkila, R.E.2    Cohen, G.3
  • 179
    • 15044339422 scopus 로고    scopus 로고
    • Cyclooxygenases, peroxide tone and the allure of fish oil
    • Smith W. L. 2005 Cyclooxygenases, peroxide tone and the allure of fish oil. Curr. Opin. Cell Biol. 17, 174 182.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 174-182
    • Smith, W.L.1
  • 180
    • 85047699109 scopus 로고    scopus 로고
    • Ascorbic-acid transporter Slc23a1 is essential for vitamin C transport into the brain and for perinatal survival
    • Sotiriou S. Gispert S. Cheng J. et al. 2002 Ascorbic-acid transporter Slc23a1 is essential for vitamin C transport into the brain and for perinatal survival. Nat. Med. 8, 514 517.
    • (2002) Nat. Med. , vol.8 , pp. 514-517
    • Sotiriou, S.1    Gispert, S.2    Cheng, J.3
  • 181
    • 0031722906 scopus 로고    scopus 로고
    • Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: Possible mechanisms of formation involving reactive oxygen species
    • Spencer J. P. Jenner P. Daniel S. E. Lees A. J. Marsden D. C. Halliwell B. 1998 Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species. J. Neurochem. 71, 2112 2122.
    • (1998) J. Neurochem. , vol.71 , pp. 2112-2122
    • Spencer, J.P.1    Jenner, P.2    Daniel, S.E.3    Lees, A.J.4    Marsden, D.C.5    Halliwell, B.6
  • 182
    • 1042290475 scopus 로고    scopus 로고
    • Cellular uptake and metabolism of flavonoids and their metabolites: Implications for their bioactivity
    • Spencer J. P. Abd-el-Mohsen M. M. Rice-Evans C. 2004 Cellular uptake and metabolism of flavonoids and their metabolites: implications for their bioactivity. Arch. Biochem. Biophys. 423, 148 161.
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 148-161
    • Spencer, J.P.1    Abd-El-Mohsen, M.M.2    Rice-Evans, C.3
  • 183
    • 0026503414 scopus 로고
    • Cis-trans isomers of lycopene and beta-carotene in human serum and tissues
    • Stahl W. Schwarz W. Sundquist A. R. Sies H. 1992 Cis-trans isomers of lycopene and beta-carotene in human serum and tissues. Arch. Biochem. Biophys. 294, 173 177.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 173-177
    • Stahl, W.1    Schwarz, W.2    Sundquist, A.R.3    Sies, H.4
  • 186
    • 33644913675 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Abeta (1-42)
    • Sultana R. Perluigi M. Butterfield D. A. 2006 Redox proteomics identification of oxidatively modified proteins in Alzheimer's disease brain and in vivo and in vitro models of AD centered around Abeta (1-42). J. Chromatogr. B. 833, 3 11.
    • (2006) J. Chromatogr. B. , vol.833 , pp. 3-11
    • Sultana, R.1    Perluigi, M.2    Butterfield, D.A.3
  • 187
    • 1442314722 scopus 로고    scopus 로고
    • Early vitamin e supplementation in young but not aged mice reduces Abeta levels and amyloid deposition in a transgenic model of Alzheimer's disease
    • Sung S. Yao Y. Uryu K. Yang H. Lee V. M. Trojanowski J. Q. Pratico D. 2004 Early vitamin E supplementation in young but not aged mice reduces Abeta levels and amyloid deposition in a transgenic model of Alzheimer's disease. FASEB J. 18, 323 325.
    • (2004) FASEB J. , vol.18 , pp. 323-325
    • Sung, S.1    Yao, Y.2    Uryu, K.3    Yang, H.4    Lee, V.M.5    Trojanowski, J.Q.6    Pratico, D.7
  • 188
    • 0028346793 scopus 로고
    • Peroxynitrite releases copper from caeruloplasmin: Implications for atherosclerosis
    • Swain J. A. Darley-Usmar V. Gutteridge J. M. 1994 Peroxynitrite releases copper from caeruloplasmin: implications for atherosclerosis. FEBS Lett. 342, 49 52.
    • (1994) FEBS Lett. , vol.342 , pp. 49-52
    • Swain, J.A.1    Darley-Usmar, V.2    Gutteridge, J.M.3
  • 189
    • 1842587600 scopus 로고    scopus 로고
    • Astrocyte influences on ischemic neuronal death
    • Swanson R. A. Ying W. Kauppinen T. M. 2004 Astrocyte influences on ischemic neuronal death. Curr. Mol. Med. 4, 193 205.
    • (2004) Curr. Mol. Med. , vol.4 , pp. 193-205
    • Swanson, R.A.1    Ying, W.2    Kauppinen, T.M.3
  • 191
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens J. F. 2003 Mitochondrial formation of reactive oxygen species. J. Physiol. 552, 335 344.
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 193
    • 0032738907 scopus 로고    scopus 로고
    • Hemoglobin and iron-evoked oxidative stress in the brain: Protection by bile pigments, manganese and S-nitrosoglutathione
    • Van Bergen P. Rauhala P. Spooner C. M. Chiueh C. C. 1999 Hemoglobin and iron-evoked oxidative stress in the brain: protection by bile pigments, manganese and S-nitrosoglutathione. Free Radic. Res. 31, 631 640.
    • (1999) Free Radic. Res. , vol.31 , pp. 631-640
    • Van Bergen, P.1    Rauhala, P.2    Spooner, C.M.3    Chiueh, C.C.4
  • 195
    • 12144288373 scopus 로고    scopus 로고
    • Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging
    • Van Remmen H. Ikeno Y. Hamilton M. et al. 2003 Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging. Physiol. Genomics 16, 29 37.
    • (2003) Physiol. Genomics , vol.16 , pp. 29-37
    • Van Remmen, H.1    Ikeno, Y.2    Hamilton, M.3
  • 197
    • 28044458281 scopus 로고    scopus 로고
    • Energy inhibition elevates β-secretase levels and activity and is potentially amyloidogenic in APP transgenic mice: Possible early events in Alzheimer's disease pathogenesis
    • Velliquette R. A. O'Connor T. Vassar R. 2005 Energy inhibition elevates β-secretase levels and activity and is potentially amyloidogenic in APP transgenic mice: possible early events in Alzheimer's disease pathogenesis. J. Neurosci. 25, 10874 10883.
    • (2005) J. Neurosci. , vol.25 , pp. 10874-10883
    • Velliquette, R.A.1    O'Connor, T.2    Vassar, R.3
  • 198
    • 0344142491 scopus 로고    scopus 로고
    • The inhibition of mammalian 15-lipoxygenases by the anti-inflammatory drug ebselen: Dual-type mechanism involving covalent linkage and alteration of the iron ligand sphere
    • Walther M. Holzhutter H. G. Kuban R. J. Wiesner R. Rathmann J. Kuhn H. 1999 The inhibition of mammalian 15-lipoxygenases by the anti-inflammatory drug ebselen: dual-type mechanism involving covalent linkage and alteration of the iron ligand sphere. Mol. Pharmacol. 56, 196 203.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 196-203
    • Walther, M.1    Holzhutter, H.G.2    Kuban, R.J.3    Wiesner, R.4    Rathmann, J.5    Kuhn, H.6
  • 200
    • 0242662455 scopus 로고    scopus 로고
    • Evidence for ozone formation in human atherosclerotic arteries
    • Wentworth P. Jr., Nieva J. Takeuchi C. et al. 2003 Evidence for ozone formation in human atherosclerotic arteries. Science 302, 1053 1056.
    • (2003) Science , vol.302 , pp. 1053-1056
    • Wentworth Jr., P.1    Nieva, J.2    Takeuchi, C.3
  • 201
    • 8544273285 scopus 로고    scopus 로고
    • Hsp90 enhances degradation of oxidized calmodulin by the 20 S proteasome
    • Whittier J. E. Xiong Y. Rechsteiner M. C. Squier T. C. 2004 Hsp90 enhances degradation of oxidized calmodulin by the 20 S proteasome. J. Biol. Chem. 279, 46 135 46 142.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46135-46142
    • Whittier, J.E.1    Xiong, Y.2    Rechsteiner, M.C.3    Squier, T.C.4
  • 202
    • 0031802887 scopus 로고    scopus 로고
    • Oxidation of serotonin by superoxide radical: Implications to neurodegenerative brain disorders
    • Wrona M. Z. Dryhurst G. 1998 Oxidation of serotonin by superoxide radical: implications to neurodegenerative brain disorders. Chem. Res. Toxicol. 11, 639 650.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 639-650
    • Wrona, M.Z.1    Dryhurst, G.2
  • 203
    • 20444441575 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Alzheimer's disease: Role of amyloid-β peptide alcohol dehydrogenase (ABAD)
    • Yan S. D. Stern D. M. 2005 Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-β peptide alcohol dehydrogenase (ABAD). Int. J. Exp. Pathol. 86, 161 171.
    • (2005) Int. J. Exp. Pathol. , vol.86 , pp. 161-171
    • Yan, S.D.1    Stern, D.M.2
  • 204
    • 23844516979 scopus 로고    scopus 로고
    • Proteasome inhibition by lactacystin in primary neuronal cells induces both potentially neuroprotective and pro-apoptotic transcriptional responses: A microarray analysis
    • Yew E. H. Cheung N. S. Choy M. S. et al. 2005 Proteasome inhibition by lactacystin in primary neuronal cells induces both potentially neuroprotective and pro-apoptotic transcriptional responses: a microarray analysis. J. Neurochem. 94, 943 956.
    • (2005) J. Neurochem. , vol.94 , pp. 943-956
    • Yew, E.H.1    Cheung, N.S.2    Choy, M.S.3
  • 205
    • 25444508963 scopus 로고    scopus 로고
    • Neuroprotective properties of the natural phenolic antioxidants curcumin and naringenin but not quercetin and fisetin in a 6-OHDA model of Parkinson's disease
    • Zbarsky V. Datla K. P. Parkar S. Rai D. K. Aruoma O. I. Dexter D. T. 2005 Neuroprotective properties of the natural phenolic antioxidants curcumin and naringenin but not quercetin and fisetin in a 6-OHDA model of Parkinson's disease. Free Radic. Res. 39, 1119 1125.
    • (2005) Free Radic. Res. , vol.39 , pp. 1119-1125
    • Zbarsky, V.1    Datla, K.P.2    Parkar, S.3    Rai, D.K.4    Aruoma, O.I.5    Dexter, D.T.6
  • 207
    • 24144450324 scopus 로고    scopus 로고
    • Mitochondrial inhibition and oxidative stress: Reciprocating players in neurodegeneration
    • Zeevalk G. D. Bernard L. P. Song C. Gluck M. Ehrhart J. 2005 Mitochondrial inhibition and oxidative stress: reciprocating players in neurodegeneration. Antioxid. Redox Signal. 7, 1117 1139.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1117-1139
    • Zeevalk, G.D.1    Bernard, L.P.2    Song, C.3    Gluck, M.4    Ehrhart, J.5
  • 208
    • 20544465100 scopus 로고    scopus 로고
    • Neuroprotection by iron chelator against proteasome inhibitor-induced nigral degeneration
    • Zhang X. Xie W. Qu S. Pan T. Wang X. Le W. 2005 Neuroprotection by iron chelator against proteasome inhibitor-induced nigral degeneration. Biochem. Biophys. Res. Commun. 333, 544 549.
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 544-549
    • Zhang, X.1    Xie, W.2    Qu, S.3    Pan, T.4    Wang, X.5    Le, W.6
  • 210
    • 2342502657 scopus 로고    scopus 로고
    • Non-antioxidant activities of vitamin e
    • Zingg J. M. Azzi A. 2004 Non-antioxidant activities of vitamin E. Curr. Med. Chem. 11, 1113 1133.
    • (2004) Curr. Med. Chem. , vol.11 , pp. 1113-1133
    • Zingg, J.M.1    Azzi, A.2
  • 211
    • 32144461723 scopus 로고    scopus 로고
    • Stroke and neurovascular protection
    • del Zoppo G. P. 2006 Stroke and neurovascular protection. N. Engl. J. Med. 354, 553 555.
    • (2006) N. Engl. J. Med. , vol.354 , pp. 553-555
    • Del Zoppo, G.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.