메뉴 건너뛰기




Volumn 14, Issue 12, 2013, Pages 24438-24475

Oxidative stress and neurodegenerative disorders

Author keywords

Aging; Chemobrain; Neurodegenerative diseases; Neurotoxicants; Oxidative stress; Peripheral neuropathy; Pharmaceutical; Signal transduction

Indexed keywords

1, 1 DIPHENYL 2 PICRYLHYDRAZYL; ACTIVATING TRANSCRIPTION FACTOR 6; ALTRETAMINE; BORTEZOMIB; CARBOPLATIN; CATALASE; CISPLATIN; CYTARABINE; CYTOCHROME P450; DOCETAXEL; FLUOROURACIL; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; IFOSFAMIDE; IXABEPILONE; LEVAMISOLE; METHOTREXATE; MIRTAZAPINE; NEUROPROTECTIVE AGENT; OXALIPLATIN; PACLITAXEL; PROCARBAZINE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; SUPEROXIDE DISMUTASE; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG; VINCRISTINE;

EID: 84890535338     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms141224438     Document Type: Article
Times cited : (337)

References (237)
  • 1
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens, J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003, 552, 335-344.
    • (2003) J. Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 2
    • 0026564816 scopus 로고
    • Cytochrome P450: Progress and predictions
    • Coon, M.J.; Ding, X.; Pernecky, S.J.; Vaz, A.D.N. Cytochrome P450: Progress and predictions. FASEB J. 1992, 6, 669-673.
    • (1992) FASEB J , vol.6 , pp. 669-673
    • Coon, M.J.1    Ding, X.2    Pernecky, S.J.3    Vaz, A.D.N.4
  • 3
    • 84856488429 scopus 로고    scopus 로고
    • Formation of P450·P450 complexes and their effect on P450 function
    • Reed, J.R.; Backes, W.L. Formation of P450·P450 complexes and their effect on P450 function. Pharmacol. Ther. 2012, 133, 299-310.
    • (2012) Pharmacol. Ther , vol.133 , pp. 299-310
    • Reed, J.R.1    Backes, W.L.2
  • 4
    • 0030453086 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Molecular interaction of oxidase proteins
    • DeLeo, F.R.; Quinn, M.T. Assembly of the phagocyte NADPH oxidase: Molecular interaction of oxidase proteins. J. Leukoc. Biol. 1996, 60, 677-691.
    • (1996) J. Leukoc. Biol , vol.60 , pp. 677-691
    • Deleo, F.R.1    Quinn, M.T.2
  • 5
    • 0034733807 scopus 로고    scopus 로고
    • Redox-dependent signal transduction
    • Finkel, T. Redox-dependent signal transduction. FEBS Lett. 2000, 476, 52-54.
    • (2000) FEBS Lett , vol.476 , pp. 52-54
    • Finkel, T.1
  • 6
    • 84862297475 scopus 로고    scopus 로고
    • Mechanism of oxidative stress in neurodegeneration
    • 2012, 428010
    • Gandhi, S.; Abramov, A.Y. Mechanism of oxidative stress in neurodegeneration. Oxid. Med. Cell. Longev. 2012, 2012, 428010.
    • (2012) Oxid. Med. Cell. Longev
    • Gandhi, S.1    Abramov, A.Y.2
  • 7
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B.; Sies, H.; Boveris, A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 1979, 59, 527-605.
    • (1979) Physiol. Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 8
    • 0029857135 scopus 로고    scopus 로고
    • Superoxide production by mitochondria in the presence of nitric oxide forms peroxynitrite
    • Packer, M.A.; Porteous, C.M.; Murphy, M.P. Superoxide production by mitochondria in the presence of nitric oxide forms peroxynitrite. Biochem. Mol. Biol. Int. 1996, 40, 527-534.
    • (1996) Biochem. Mol. Biol. Int , vol.40 , pp. 527-534
    • Packer, M.A.1    Porteous, C.M.2    Murphy, M.P.3
  • 9
    • 0033805759 scopus 로고    scopus 로고
    • Peroxynitrite formed by mitochondrial NO synthase promotes mitochondrial Ca2+ release
    • Bringold, U.; Ghafourifar, P.; Richter, C. Peroxynitrite formed by mitochondrial NO synthase promotes mitochondrial Ca2+ release. Free Radic. Biol. Med. 2000, 29, 343-348.
    • (2000) Free Radic. Biol. Med , vol.29 , pp. 343-348
    • Bringold, U.1    Ghafourifar, P.2    Richter, C.3
  • 11
    • 80053034441 scopus 로고    scopus 로고
    • Thioredoxin reductase-2 is essential for keeping low levels of H2O2 emission from isolated heart mitochondria
    • Stanley, B.A.; Sivakumaran, V.; Shi, S.; McDonald, I.; Lloyd, D.; Watson, W.H.; Aon, M.A.; Paolocci, N. Thioredoxin reductase-2 is essential for keeping low levels of H2O2 emission from isolated heart mitochondria. J. Biol. Chem. 2011, 286, 33669-33677.
    • (2011) J. Biol. Chem , vol.286 , pp. 33669-33677
    • Stanley, B.A.1    Sivakumaran, V.2    Shi, S.3    McDonald, I.4    Lloyd, D.5    Watson, W.H.6    Aon, M.A.7    Paolocci, N.8
  • 12
    • 84892366219 scopus 로고    scopus 로고
    • The thioredoxin antioxidant system
    • doi:10.1016/j.freeradbiomed.2013.07.036
    • Lu, J.; Holmgren, A. The thioredoxin antioxidant system. Free Radic. Biol. Med. 2013, doi:10.1016/j.freeradbiomed.2013.07.036.
    • (2013) Free Radic. Biol. Med
    • Lu, J.1    Holmgren, A.2
  • 13
    • 79954596666 scopus 로고    scopus 로고
    • Reactive oxygen species in the regulation of synaptic plasticity and memory
    • Massaad, C.A.; Klann, E. Reactive oxygen species in the regulation of synaptic plasticity and memory. Antioxid. Redox Signal. 2011, 14, 2013-2054.
    • (2011) Antioxid. Redox Signal , vol.14 , pp. 2013-2054
    • Massaad, C.A.1    Klann, E.2
  • 14
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation
    • Rao, R.K.; Clayton, L.W. Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation. Biochem. Biophys. Res. Commun. 2002, 293, 610-616.
    • (2002) Biochem. Biophys. Res. Commun , vol.293 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 15
    • 0042163035 scopus 로고    scopus 로고
    • Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide. Potential regulation of eIF2 alpha phosphorylation in differentiated PC12 cells
    • O'Loghlen, A.; Pérez-Morgado, M.I.; Salinas, M.; Martín, M.E. Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide. Potential regulation of eIF2 alpha phosphorylation in differentiated PC12 cells. Arch. Biochem. Biophys. 2003, 417, 194-202.
    • (2003) Arch. Biochem. Biophys , vol.417 , pp. 194-202
    • O'Loghlen, A.1    Pérez-Morgado, M.I.2    Salinas, M.3    Martín, M.E.4
  • 16
    • 73449129394 scopus 로고    scopus 로고
    • Hydrogen peroxide as a cell-survival signaling molecule
    • Groeger, G.; Quiney, C.; Cotter, T.G. Hydrogen peroxide as a cell-survival signaling molecule. Antioxid. Redox Signal. 2009, 11, 2655-2671.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 2655-2671
    • Groeger, G.1    Quiney, C.2    Cotter, T.G.3
  • 17
    • 0028843581 scopus 로고
    • Hydrogen peroxide preferentially enhances the tyrosine phosphorylation of epidermal growth factor receptor
    • Gamou, S.; Shimizu, N. Hydrogen peroxide preferentially enhances the tyrosine phosphorylation of epidermal growth factor receptor. FEBS Lett. 1995, 357, 161-164.
    • (1995) FEBS Lett , vol.357 , pp. 161-164
    • Gamou, S.1    Shimizu, N.2
  • 19
    • 79751532260 scopus 로고    scopus 로고
    • Redox regulation of ERK1/2 activation induced by sphingosine 1-phosphate in fibroblasts: Involvement of NADPH oxidase and platelet-derived growth factor receptor
    • Catarzi, S.; Romagnoli, C.; Marcucci, G.; Favilli, F.; Iantomasi, T.; Vincenzini, M.T. Redox regulation of ERK1/2 activation induced by sphingosine 1-phosphate in fibroblasts: Involvement of NADPH oxidase and platelet-derived growth factor receptor. Biochim. Biophys. Acta 2011, 1810, 446-456.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 446-456
    • Catarzi, S.1    Romagnoli, C.2    Marcucci, G.3    Favilli, F.4    Iantomasi, T.5    Vincenzini, M.T.6
  • 20
    • 33750909999 scopus 로고    scopus 로고
    • Reactive oxygen species-induced activation of the MAP kinase signaling pathways
    • McCubrey, J.A.; LaHair, M.M.; Franklin, R.A. Reactive oxygen species-induced activation of the MAP kinase signaling pathways. Antioxid. Redox Signal. 2006, 8, 1775-1789.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 1775-1789
    • McCubrey, J.A.1    Lahair, M.M.2    Franklin, R.A.3
  • 21
    • 0029074550 scopus 로고
    • Sublethal levels of oxidant stress stimulate multiple serine/threonine kinases and suppress protein phosphatases in Jurkat T cells
    • Whisler, R.L.; Goyette, M.A.; Grants, I.S.; Newhouse, Y.G. Sublethal levels of oxidant stress stimulate multiple serine/threonine kinases and suppress protein phosphatases in Jurkat T cells. Arch. Biochem. Biophys. 1995, 319, 23-25.
    • (1995) Arch. Biochem. Biophys , vol.319 , pp. 23-25
    • Whisler, R.L.1    Goyette, M.A.2    Grants, I.S.3    Newhouse, Y.G.4
  • 22
    • 0031695197 scopus 로고    scopus 로고
    • Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset
    • Brookmeyer, R.; Gray, S.; Kawas, C. Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset. Am. J. Public Health 1998, 88, 1337-1342.
    • (1998) Am. J. Public Health , vol.88 , pp. 1337-1342
    • Brookmeyer, R.1    Gray, S.2    Kawas, C.3
  • 23
    • 79959334421 scopus 로고    scopus 로고
    • Apoptosis signal-regulating kinase 1 is an intracellular inducer of p38 MAPK-mediated myogenic signalling in cardiac myoblasts
    • Choi, T.G.; Lee, J.; Ha, J.; Kim, S.S. Apoptosis signal-regulating kinase 1 is an intracellular inducer of p38 MAPK-mediated myogenic signalling in cardiac myoblasts. Biochim. Biophys. Acta 2011, 1813, 1412-1421.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1412-1421
    • Choi, T.G.1    Lee, J.2    Ha, J.3    Kim, S.S.4
  • 25
    • 0020575250 scopus 로고
    • The oxidative burst and related phenomena in mouse macrophages elicited by different sterile inflammatory stimuli
    • Keisari, Y.; Braun, L.; Flescher, E. The oxidative burst and related phenomena in mouse macrophages elicited by different sterile inflammatory stimuli. Immunobiology 1983, 165, 78-89.
    • (1983) Immunobiology , vol.165 , pp. 78-89
    • Keisari, Y.1    Braun, L.2    Flescher, E.3
  • 26
    • 0028051845 scopus 로고
    • Mediation of hippocampal mossy fiber long-term potentiation by cyclic AMP
    • Weisskopf, M.G.; Castillo, P.E.; Zalutsky, R.A.; Nicoll, R.A. Mediation of hippocampal mossy fiber long-term potentiation by cyclic AMP. Science 1994, 265, 1878-1882.
    • (1994) Science , vol.265 , pp. 1878-1882
    • Weisskopf, M.G.1    Castillo, P.E.2    Zalutsky, R.A.3    Nicoll, R.A.4
  • 27
    • 0024520759 scopus 로고
    • Long term depression
    • Ito, M. Long term depression. Ann. Rev. Neurosci. 1989, 12, 85-102.
    • (1989) Ann. Rev. Neurosci , vol.12 , pp. 85-102
    • Ito, M.1
  • 28
    • 0026458086 scopus 로고
    • Mechanisms underlying induction of homosynaptic long-term depression in area CA1 of the hippocampus
    • Mulkey, R.M.; Malenka, R.C. Mechanisms underlying induction of homosynaptic long-term depression in area CA1 of the hippocampus. Neuron 1992, 9, 967-975.
    • (1992) Neuron , vol.9 , pp. 967-975
    • Mulkey, R.M.1    Malenka, R.C.2
  • 29
    • 84863822091 scopus 로고    scopus 로고
    • Long-lasting LTP requires neither repeated trains for its induction nor protein synthesis for its development
    • Villers, A.; Godaux, E.; Ris, L. Long-lasting LTP requires neither repeated trains for its induction nor protein synthesis for its development. PLoS One 2012, 7, e40823.
    • (2012) PLoS One , vol.7
    • Villers, A.1    Godaux, E.2    Ris, L.3
  • 31
    • 77955655113 scopus 로고    scopus 로고
    • Long-term potentiation of neuronal excitation in the central nucleus of the rat amygdala revealed by imaging with a voltage-sensitive dye
    • Kiritoshi, T.; Ikeda, H.; Murase, K. Long-term potentiation of neuronal excitation in the central nucleus of the rat amygdala revealed by imaging with a voltage-sensitive dye. Brain Res. 2010, 1349, 32-40.
    • (2010) Brain Res , vol.1349 , pp. 32-40
    • Kiritoshi, T.1    Ikeda, H.2    Murase, K.3
  • 32
    • 0026325599 scopus 로고
    • Persistent protein kinase activation in the maintenance phase of long-term potentiation
    • Klann, E.; Chen, S.-J.; Sweatt, J.D. Persistent protein kinase activation in the maintenance phase of long-term potentiation. J. Biol. Chem. 1991, 266, 24253-24256.
    • (1991) J. Biol. Chem , vol.266 , pp. 24253-24256
    • Klann, E.1    Chen, S.-J.2    Sweatt, J.D.3
  • 33
    • 0027170453 scopus 로고
    • Mechanism of protein kinase C activation during the induction and maintenance of long-term potentiation probed using a novel peptide substrate
    • Klann, E.; Chen, S.-J.; Sweatt, J.D. Mechanism of protein kinase C activation during the induction and maintenance of long-term potentiation probed using a novel peptide substrate. Proc. Natl. Acad. Sci. USA 1993, 90, 8337-8341.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8337-8341
    • Klann, E.1    Chen, S.-J.2    Sweatt, J.D.3
  • 34
    • 0027305085 scopus 로고
    • Persistent activation of the ζ isoform of proten kinase C in the maintenance of long-term potentiation
    • Sacktor, T.C.; Osten, P.; Valsamis, H.; Jiang, X.; Naik, M.U.; Sublette, E. Persistent activation of the ζ isoform of proten kinase C in the maintenance of long-term potentiation. Proc. Natl. Acad. Sci. USA 1993, 90, 8342-8346.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8342-8346
    • Sacktor, T.C.1    Osten, P.2    Valsamis, H.3    Jiang, X.4    Naik, M.U.5    Sublette, E.6
  • 35
    • 0027471455 scopus 로고
    • Long-term potentiation is associated with an increased activity of Ca2+/calmodulindependent protein kinase II
    • Fukanaga, K.; Stoppini, L.; Miyamoto, E.; Muller, D. Long-term potentiation is associated with an increased activity of Ca2+/calmodulindependent protein kinase II. J. Biol. Chem. 1993, 268, 7863-7867.
    • (1993) J. Biol. Chem , vol.268 , pp. 7863-7867
    • Fukanaga, K.1    Stoppini, L.2    Miyamoto, E.3    Muller, D.4
  • 36
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
    • Barria, A.; Muller, D.; Derkach, V.; Griffith, L.C.; Soderling, T.R. Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation. Science 1997, 276, 2042-2045.
    • (1997) Science , vol.276 , pp. 2042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 37
    • 16944366067 scopus 로고    scopus 로고
    • Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus
    • Ouyang, Y.; Kantor, D.; Harris, K.M.; Schuman, E.M.; Kennedy, M.B. Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus. J. Neurosci. 1997, 17, 5416-5427.
    • (1997) J. Neurosci , vol.17 , pp. 5416-5427
    • Ouyang, Y.1    Kantor, D.2    Harris, K.M.3    Schuman, E.M.4    Kennedy, M.B.5
  • 39
    • 5344241223 scopus 로고    scopus 로고
    • LTP An embarrassment of riches
    • Malenka, R.C.; Bear, M.F. LTP and LTD: An embarrassment of riches. Neuron 2004, 44, 5-21.
    • (2004) Neuron , vol.44 , pp. 5-21
    • Malenka, R.C.1    Bear, M.F.2
  • 40
    • 14244254168 scopus 로고    scopus 로고
    • Persistent phosphorylation by protein kinase Mzeta maintains late-phase long-term potentiation
    • Serrano, P.; Yao, Y.; Sacktor, T. Persistent phosphorylation by protein kinase Mzeta maintains late-phase long-term potentiation. J. Neurosci. 2005, 25, 1979-1984.
    • (2005) J. Neurosci , vol.25 , pp. 1979-1984
    • Serrano, P.1    Yao, Y.2    Sacktor, T.3
  • 42
    • 60149095737 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor-dependent long-term potentiation
    • Anwyl, R. Metabotropic glutamate receptor-dependent long-term potentiation. Neuropharmacology 2009, 56, 735-740.
    • (2009) Neuropharmacology , vol.56 , pp. 735-740
    • Anwyl, R.1
  • 43
    • 0034985915 scopus 로고    scopus 로고
    • MGluR1-mediated potentiation of NMDA receptors involves a rise in intracellular calcium and activation of protein kinase C
    • Skeberdis, V.A.; Lan, J.; Opitz, T.; Zheng, X.; Bennett, M.V.; Zukin, R.S. mGluR1-mediated potentiation of NMDA receptors involves a rise in intracellular calcium and activation of protein kinase C. Neuropharmacology 2001, 40, 856-865.
    • (2001) Neuropharmacology , vol.40 , pp. 856-865
    • Skeberdis, V.A.1    Lan, J.2    Opitz, T.3    Zheng, X.4    Bennett, M.V.5    Zukin, R.S.6
  • 44
    • 0030008052 scopus 로고    scopus 로고
    • Superoxide production in rat hippocampal neurons: Selective imaging with hydroethidine
    • Bindokas, V.P.; Jordan, J.; Lee, C.C.; Miller, R.J. Superoxide production in rat hippocampal neurons: Selective imaging with hydroethidine. J. Neurosci. 1996, 16, 1324-1336.
    • (1996) J. Neurosci , vol.16 , pp. 1324-1336
    • Bindokas, V.P.1    Jordan, J.2    Lee, C.C.3    Miller, R.J.4
  • 45
    • 0031840847 scopus 로고    scopus 로고
    • Cell-permeable scavengers of superoxide prevent long-term potentiation in hippocampal area CA1
    • Klann, E. Cell-permeable scavengers of superoxide prevent long-term potentiation in hippocampal area CA1. J. Neurophysiol. 1998, 80, 452-457.
    • (1998) J. Neurophysiol , vol.80 , pp. 452-457
    • Klann, E.1
  • 46
    • 33746483283 scopus 로고    scopus 로고
    • Synaptic plasticity deficits and mild memory impairments in mouse models of chronic granulomatous disease
    • Kishida, K.T.; Hoeffer, C.A.; Hu, D.; Pao, M.; Holland, S.M.; Klann, E. Synaptic plasticity deficits and mild memory impairments in mouse models of chronic granulomatous disease. Mol. Cell. Biol. 2006, 26, 5908-5920.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 5908-5920
    • Kishida, K.T.1    Hoeffer, C.A.2    Hu, D.3    Pao, M.4    Holland, S.M.5    Klann, E.6
  • 47
    • 0032548843 scopus 로고    scopus 로고
    • A role for superoxide in protein kinase C activation and the induction of long-term potentiation
    • Klann, E.; Roberson, E.D.; Knapp, L.T.; Sweatt, J.D. A role for superoxide in protein kinase C activation and the induction of long-term potentiation. J. Biol. Chem. 1998, 273, 4516-4522.
    • (1998) J. Biol. Chem , vol.273 , pp. 4516-4522
    • Klann, E.1    Roberson, E.D.2    Knapp, L.T.3    Sweatt, J.D.4
  • 48
    • 0033121096 scopus 로고    scopus 로고
    • Modulation of protein kinases and protein phosphatases by reactive oxygen species: Implications for hippocampal synaptic plasticity
    • Klann, E.; Thiels, E. Modulation of protein kinases and protein phosphatases by reactive oxygen species: Implications for hippocampal synaptic plasticity. Prog. Neuropsychopharmacol. Biol. Psychiatry 1999, 23, 359-376.
    • (1999) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.23 , pp. 359-376
    • Klann, E.1    Thiels, E.2
  • 49
    • 0036470423 scopus 로고    scopus 로고
    • Potentiation of hippocampal synaptic transmission by superoxide requires the oxidative activation of protein kinase C
    • Knapp, L.T.; Klann, E. Potentiation of hippocampal synaptic transmission by superoxide requires the oxidative activation of protein kinase C. J. Neurosci. 2002, 22, 674-683.
    • (2002) J. Neurosci , vol.22 , pp. 674-683
    • Knapp, L.T.1    Klann, E.2
  • 50
    • 40949119810 scopus 로고    scopus 로고
    • Superoxide-induced potentiation in the hippocampus requires activation of ryanodine receptor type 3 and ERK
    • Huddleston, A.T.; Tang, W.; Takeshima, H.; Hamilton, S.L.; Klann, E. Superoxide-induced potentiation in the hippocampus requires activation of ryanodine receptor type 3 and ERK. J. Neurophysiol. 2008, 99, 1565-1571.
    • (2008) J. Neurophysiol , vol.99 , pp. 1565-1571
    • Huddleston, A.T.1    Tang, W.2    Takeshima, H.3    Hamilton, S.L.4    Klann, E.5
  • 51
    • 0020308323 scopus 로고
    • Parkinson's disease: A disorder due to nigral glutathione deficiency
    • Perry, T.L.; Godin, D.V.; Hansen, S. Parkinson's disease: A disorder due to nigral glutathione deficiency? Neurosci. Lett. 1982, 33, 305-310.
    • (1982) Neurosci. Lett , vol.33 , pp. 305-310
    • Perry, T.L.1    Godin, D.V.2    Hansen, S.3
  • 52
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian, J.; Dexter, D.T.; Lees, A.J.; Daniel, S.; Agid, Y.; Javoy-Agid, F.; Jenner, P.; Marsden, C.D. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann. Neurol. 1994, 36, 348-355.
    • (1994) Ann. Neurol , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Agid, Y.5    Javoy-Agid, F.6    Jenner, P.7    Marsden, C.D.8
  • 53
  • 54
    • 77953954538 scopus 로고    scopus 로고
    • Chemical and molecular mechanisms of antioxidants: Experimental approaches and model systems
    • Lü, J.M.; Lin, P.H.; Yao, Q.; Chen, C. Chemical and molecular mechanisms of antioxidants: Experimental approaches and model systems. J. Cell. Mol. Med. 2010, 14, 840-860.
    • (2010) J. Cell. Mol. Med , vol.14 , pp. 840-860
    • Lü, J.M.1    Lin, P.H.2    Yao, Q.3    Chen, C.4
  • 55
    • 0027391867 scopus 로고
    • Quantitative determination of oxidative base damage in DNA by stable isotope-dilution mass spectrometry
    • Dizdaroglu, M. Quantitative determination of oxidative base damage in DNA by stable isotope-dilution mass spectrometry. FEBS Lett. 1993, 315, 1-6.
    • (1993) FEBS Lett , vol.315 , pp. 1-6
    • Dizdaroglu, M.1
  • 56
    • 32044466239 scopus 로고    scopus 로고
    • Does measurement of oxidative damage to DNA have clinical significance?
    • Cooke, M.S.; Olinski, R.; Evans, M.D. Does measurement of oxidative damage to DNA have clinical significance? Clin. Chim. Acta 2006, 365, 30-49.
    • (2006) Clin. Chim. Acta , vol.365 , pp. 30-49
    • Cooke, M.S.1    Olinski, R.2    Evans, M.D.3
  • 59
    • 0022616654 scopus 로고
    • Alzheimer's disease
    • Katzman, R. Alzheimer's disease. N. Engl. J. Med. 1986, 314, 964-973.
    • (1986) N. Engl. J. Med , vol.314 , pp. 964-973
    • Katzman, R.1
  • 60
    • 0031614624 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Smith, M.A. Alzheimer's disease. Int. Rev. Neurobiol. 1998, 42, 1-54.
    • (1998) Int. Rev. Neurobiol , vol.42 , pp. 1-54
    • Smith, M.A.1
  • 61
    • 84890509773 scopus 로고    scopus 로고
    • The World Health Report 2000-Health systems: Improving performance. Available online, accessed on 8 January 2009
    • The World Health Report 2000-Health systems: Improving performance. Available online: http://www.who.int/whr/2000/en/ (accessed on 8 January 2009).
  • 65
    • 70349751944 scopus 로고    scopus 로고
    • Lenalidomide (Revlimid) administration at symptom onset is neuroprotective in a mouse model of amyotrophic lateral sclerosis
    • Neymotin, A.; Petri, S.; Calingasan, N.Y.; Wille, E.; Schafer, P.; Stewart, C.; Hensley, K.; Beal, M.F.; Kiaei, M. Lenalidomide (Revlimid) administration at symptom onset is neuroprotective in a mouse model of amyotrophic lateral sclerosis. Exp. Neurol. 2009, 220, 191-197.
    • (2009) Exp. Neurol , vol.220 , pp. 191-197
    • Neymotin, A.1    Petri, S.2    Calingasan, N.Y.3    Wille, E.4    Schafer, P.5    Stewart, C.6    Hensley, K.7    Beal, M.F.8    Kiaei, M.9
  • 66
    • 0142200947 scopus 로고    scopus 로고
    • Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases
    • Hashimoto, M.; Rockenstein, E.; Crews, L.; Masliah, E. Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases. Neuromol. Med. 2003, 4, 21-36.
    • (2003) Neuromol. Med , vol.4 , pp. 21-36
    • Hashimoto, M.1    Rockenstein, E.2    Crews, L.3    Masliah, E.4
  • 68
    • 0042634362 scopus 로고    scopus 로고
    • Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory
    • Turner, P.R.; O'Connor, K.; Tate, W.P.; Abraham, W.C. Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory. Prog. Neurobiol. 2003, 70, 1-32.
    • (2003) Prog. Neurobiol , vol.70 , pp. 1-32
    • Turner, P.R.1    O'Connor, K.2    Tate, W.P.3    Abraham, W.C.4
  • 69
    • 18044377435 scopus 로고    scopus 로고
    • Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein
    • Hooper, N.M. Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein. Biochem. Soc. Trans. 2005, 33, 335-338.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 335-338
    • Hooper, N.M.1
  • 70
    • 2942561028 scopus 로고    scopus 로고
    • The importance of neuritic plaques and tangles to the development and evolution of AD
    • Tiraboschi, P.; Hansen, L.A.; Thal, L.J.; Corey-Bloom, J. The importance of neuritic plaques and tangles to the development and evolution of AD. Neurology 2004, 62, 1984-1989.
    • (2004) Neurology , vol.62 , pp. 1984-1989
    • Tiraboschi, P.1    Hansen, L.A.2    Thal, L.J.3    Corey-Bloom, J.4
  • 71
    • 1642417648 scopus 로고    scopus 로고
    • Amyloid fibrils from the viewpoint of protein folding
    • Ohnishi, S.; Takano, K. Amyloid fibrils from the viewpoint of protein folding. Cell. Mol. Life Sci. 2004, 61, 511-524.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 511-524
    • Ohnishi, S.1    Takano, K.2
  • 72
    • 84874372615 scopus 로고    scopus 로고
    • Oxidative stress-induced posttranslational modifications of alpha-synuclein: Specific modification of alpha-synuclein by 4-hydroxy-2-nonenal increases dopaminergic toxicity
    • Xiang, W.; Schlachetzki, J.C.; Helling, S.; Bussmann, J.C.; Berlinghof, M.; Schäffer, T.E.; Marcus, K.; Winkler, J.; Klucken, J.; Becker, C.M. Oxidative stress-induced posttranslational modifications of alpha-synuclein: Specific modification of alpha-synuclein by 4-hydroxy-2-nonenal increases dopaminergic toxicity. Mol. Cell. Neurosci. 2013, 54, 71-83.
    • (2013) Mol. Cell. Neurosci , vol.54 , pp. 71-83
    • Xiang, W.1    Schlachetzki, J.C.2    Helling, S.3    Bussmann, J.C.4    Berlinghof, M.5    Schäffer, T.E.6    Marcus, K.7    Winkler, J.8    Klucken, J.9    Becker, C.M.10
  • 73
    • 84874654676 scopus 로고    scopus 로고
    • Nuclear translocation of alpha-synuclein increases susceptibility of MES23.5 cells to oxidative stress
    • Zhou, M.; Xu, S.; Mi, J.; Uéda, K.; Chan, P. Nuclear translocation of alpha-synuclein increases susceptibility of MES23.5 cells to oxidative stress. Brain Res. 2013, 1500, 19-27.
    • (2013) Brain Res , vol.1500 , pp. 19-27
    • Zhou, M.1    Xu, S.2    Mi, J.3    Uéda, K.4    Chan, P.5
  • 76
    • 72249109630 scopus 로고    scopus 로고
    • Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells
    • Su, B.; Wang, X.; Lee, H.G.; Tabaton, M.; Perry, G.; Smith, M.A.; Zhu, X. Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells. Neurosci. Lett. 2010, 468, 267-271.
    • (2010) Neurosci. Lett , vol.468 , pp. 267-271
    • Su, B.1    Wang, X.2    Lee, H.G.3    Tabaton, M.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 77
    • 0345701340 scopus 로고    scopus 로고
    • Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells
    • Gómez-Ramos, A.; Díaz-Nido, J.; Smith, M.A.; Perry, G.; Avila, J. Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells. J. Neurosci. Res. 2003, 71, 863-870.
    • (2003) J. Neurosci. Res , vol.71 , pp. 863-870
    • Gómez-Ramos, A.1    Díaz-Nido, J.2    Smith, M.A.3    Perry, G.4    Avila, J.5
  • 78
    • 0034672554 scopus 로고    scopus 로고
    • Phosphorylated, but not native, tau protein assembles following reaction with the lipid peroxidation product, 4-hydroxy-2-nonenal
    • Perez, M.; Cuadros, R.; Smith, M.A.; Perry, G.; Avila, J. Phosphorylated, but not native, tau protein assembles following reaction with the lipid peroxidation product, 4-hydroxy-2-nonenal. FEBS Lett. 2000, 486, 270-274.
    • (2000) FEBS Lett , vol.486 , pp. 270-274
    • Perez, M.1    Cuadros, R.2    Smith, M.A.3    Perry, G.4    Avila, J.5
  • 81
    • 0034643895 scopus 로고    scopus 로고
    • Oxidative stress induces intracellular accumulation of amyloid beta-protein (Abeta) in human neuroblastoma cells
    • Misonou, H.; Morishima-Kawashima, M.; Ihara, Y. Oxidative stress induces intracellular accumulation of amyloid beta-protein (Abeta) in human neuroblastoma cells. Biochemistry 2000, 39, 6951-6959.
    • (2000) Biochemistry , vol.39 , pp. 6951-6959
    • Misonou, H.1    Morishima-Kawashima, M.2    Ihara, Y.3
  • 82
    • 0028200649 scopus 로고
    • Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative
    • Gabuzda, D.; Busciglio, J.; Chen, L.B.; Matsudaira, P.; Yankner, B.A. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J. Biol. Chem. 1994, 269, 13623-13628.
    • (1994) J. Biol. Chem , vol.269 , pp. 13623-13628
    • Gabuzda, D.1    Busciglio, J.2    Chen, L.B.3    Matsudaira, P.4    Yankner, B.A.5
  • 83
    • 4744369310 scopus 로고    scopus 로고
    • Agingrelated increase in oxidative stress correlates with developmental pattern of beta-secretase activity and beta-amyloid plaque formation in transgenic Tg2576 mice with Alzheimerlike pathology
    • Apelt, J.; Bigl, M.; Wunderlich, P.; Schliebs, R. Agingrelated increase in oxidative stress correlates with developmental pattern of beta-secretase activity and beta-amyloid plaque formation in transgenic Tg2576 mice with Alzheimerlike pathology. Int. J. Dev. Neurosci. 2004, 22, 475-484.
    • (2004) Int. J. Dev. Neurosci , vol.22 , pp. 475-484
    • Apelt, J.1    Bigl, M.2    Wunderlich, P.3    Schliebs, R.4
  • 84
    • 0035077553 scopus 로고    scopus 로고
    • Cerebral amyloidosis, amyloid angiopathy, and their relationship to stroke and dementia
    • Ghiso, J.; Frangione, B. Cerebral amyloidosis, amyloid angiopathy, and their relationship to stroke and dementia. J. Alzheimers Dis. 2001, 3, 65-73.
    • (2001) J. Alzheimers Dis , vol.3 , pp. 65-73
    • Ghiso, J.1    Frangione, B.2
  • 86
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida, Y.; Kurosawa, M.; Nukina, N.; Ito, K.; Oda, T.; Tanaka, M. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc. Natl. Acad. Sci. USA 2009, 106, 9679-9684.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 87
    • 84867267823 scopus 로고    scopus 로고
    • Post-aggregation oxidation of mutant huntingtin controls the interactions between aggregates
    • Mitomi, Y.; Nomura, T.; Kurosawa, M.; Nukina, N.; Furukawa, Y. Post-aggregation oxidation of mutant huntingtin controls the interactions between aggregates. J. Biol. Chem. 2012, 287, 34764-34775.
    • (2012) J. Biol. Chem , vol.287 , pp. 34764-34775
    • Mitomi, Y.1    Nomura, T.2    Kurosawa, M.3    Nukina, N.4    Furukawa, Y.5
  • 88
    • 32644481227 scopus 로고    scopus 로고
    • Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction
    • Goswami, A.; Dikshit, P.; Mishra, A.; Mulherkar, S.; Nukina, N.; Jana, N.R. Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction. Biochem. Biophys. Res. Commun. 2006, 342, 184-190.
    • (2006) Biochem. Biophys. Res. Commun , vol.342 , pp. 184-190
    • Goswami, A.1    Dikshit, P.2    Mishra, A.3    Mulherkar, S.4    Nukina, N.5    Jana, N.R.6
  • 90
    • 84857997227 scopus 로고    scopus 로고
    • Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking
    • Cohen, T.J.; Hwang, A.W.; Unger, T.; Trojanowski, J.Q.; Lee, V.M. Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking. EMBO J. 2012, 31, 1241-1252.
    • (2012) EMBO J , vol.31 , pp. 1241-1252
    • Cohen, T.J.1    Hwang, A.W.2    Unger, T.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 91
    • 84875228800 scopus 로고    scopus 로고
    • Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function
    • Chang, C.K.; Chiang, M.H.; Toh, E.K.; Chang, C.F.; Huang, T.H. Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function. FEBS Lett. 2013, 587, 575-582.
    • (2013) FEBS Lett , vol.587 , pp. 575-582
    • Chang, C.K.1    Chiang, M.H.2    Toh, E.K.3    Chang, C.F.4    Huang, T.H.5
  • 92
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid protein toxicity
    • Behl, C.; Davies, J.B.; Lesley, R.; Schubert, D. Hydrogen peroxide mediates amyloid protein toxicity. Cell 1994, 77, 817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davies, J.B.2    Lesley, R.3    Schubert, D.4
  • 93
    • 0141594627 scopus 로고    scopus 로고
    • Copper, beta-amyloid, and Alzheimer's disease: Tapping a sensitive connection
    • Bush, A.I.; Masters, C.L.; Tanzi, R.E. Copper, beta-amyloid, and Alzheimer's disease: Tapping a sensitive connection. Proc. Natl. Acad. Sci. USA 2003, 100, 11193-11194.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11193-11194
    • Bush, A.I.1    Masters, C.L.2    Tanzi, R.E.3
  • 94
    • 0036254698 scopus 로고    scopus 로고
    • Oxidative nerve cell death in Alzheimer's disease and stroke: Antioxidants as neuroprotective compounds
    • Behl, C.; Moosmann, B. Oxidative nerve cell death in Alzheimer's disease and stroke: Antioxidants as neuroprotective compounds. Biol. Chem. 2002, 383, 521-536.
    • (2002) Biol. Chem , vol.383 , pp. 521-536
    • Behl, C.1    Moosmann, B.2
  • 95
    • 0034233474 scopus 로고    scopus 로고
    • Oxidative processes in Alzheimer's disease: The role of abeta-metal interactions
    • Lynch, T.; Cherny, R.A.; Bush, A.I. Oxidative processes in Alzheimer's disease: The role of abeta-metal interactions. Exp. Gerontol. 2000, 35, 445-451.
    • (2000) Exp. Gerontol , vol.35 , pp. 445-451
    • Lynch, T.1    Cherny, R.A.2    Bush, A.I.3
  • 96
    • 0028981159 scopus 로고
    • Amyloid beta-peptide impairs ion-motive ATPase activities: Evidence for a role in loss of neuronal Ca2+ homeostasis and cell death
    • Mark, R.J.; Hensley, K.; Butterfield, D.A.; Mattson, M.P. Amyloid beta-peptide impairs ion-motive ATPase activities: Evidence for a role in loss of neuronal Ca2+ homeostasis and cell death. J. Neurosci. 1995, 15, 6239-6249.
    • (1995) J. Neurosci , vol.15 , pp. 6239-6249
    • Mark, R.J.1    Hensley, K.2    Butterfield, D.A.3    Mattson, M.P.4
  • 97
    • 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 2003, 34, 385-397.
    • (2003) Cell Calcium , vol.34 , pp. 385-397
    • Mattson, M.P.1    Chan, S.L.2
  • 98
    • 0034319190 scopus 로고    scopus 로고
    • Molecular mechanism of neurodegeneration induced by Alzheimer's beta-amyloid protein: Channel formation and disruption of calcium homeostasis
    • Kawahara, M.; Kuroda, Y. Molecular mechanism of neurodegeneration induced by Alzheimer's beta-amyloid protein: Channel formation and disruption of calcium homeostasis. Brain Res. Bull. 2000, 53, 389-397.
    • (2000) Brain Res. Bull , vol.53 , pp. 389-397
    • Kawahara, M.1    Kuroda, Y.2
  • 99
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: Current status
    • Kagan, B.L.; Hirakura, Y.; Azimov, R.; Azimova, R.; Lin, M.C. The channel hypothesis of Alzheimer's disease: Current status. Peptides 2002, 23, 1311-1315.
    • (2002) Peptides , vol.23 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.C.5
  • 100
    • 79955764600 scopus 로고    scopus 로고
    • Amyloid β-induced impairments in hippocampal synaptic plasticity are rescued by decreasing mitochondrial superoxide
    • Ma, T.; Hoeffer, C.A.; Wong, H.; Massaad, C.A.; Zhou, P.; Iadecola, C.; Murphy, M.P.; Pautler, R.G.; Klann, E. Amyloid β-induced impairments in hippocampal synaptic plasticity are rescued by decreasing mitochondrial superoxide. J. Neurosci. 2011, 31, 5589-5595.
    • (2011) J. Neurosci , vol.31 , pp. 5589-5595
    • Ma, T.1    Hoeffer, C.A.2    Wong, H.3    Massaad, C.A.4    Zhou, P.5    Iadecola, C.6    Murphy, M.P.7    Pautler, R.G.8    Klann, E.9
  • 101
    • 68849110235 scopus 로고    scopus 로고
    • Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease
    • Dumont, M.; Wille, E.; Stack, C.; Calingasan, N.Y.; Beal, M.F.; Lin, M.T. Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease. FASEB J. 2009, 23, 2459-2466.
    • (2009) FASEB J , vol.23 , pp. 2459-2466
    • Dumont, M.1    Wille, E.2    Stack, C.3    Calingasan, N.Y.4    Beal, M.F.5    Lin, M.T.6
  • 102
    • 69449096141 scopus 로고    scopus 로고
    • Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory deficits in a mouse model of Alzheimer's disease
    • Massaad, C.A.; Washington, T.M.; Pautler, R.G.; Klann, E. Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory deficits in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 2009, 106, 13576-13581.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13576-13581
    • Massaad, C.A.1    Washington, T.M.2    Pautler, R.G.3    Klann, E.4
  • 103
    • 84863306063 scopus 로고    scopus 로고
    • Dithiol-based compounds maintain expression of antioxidant protein peroxiredoxin 1 that counteracts toxicity of mutant huntingtin
    • Pitts, A.; Dailey, K.; Newington, J.T.; Chien, A.; Arseneault, R.; Cann, T.; Thompson, L.M.; Cumming, R.C. Dithiol-based compounds maintain expression of antioxidant protein peroxiredoxin 1 that counteracts toxicity of mutant huntingtin. J. Biol. Chem. 2012, 287, 22717-22729.
    • (2012) J. Biol. Chem , vol.287 , pp. 22717-22729
    • Pitts, A.1    Dailey, K.2    Newington, J.T.3    Chien, A.4    Arseneault, R.5    Cann, T.6    Thompson, L.M.7    Cumming, R.C.8
  • 104
    • 79957583304 scopus 로고    scopus 로고
    • Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast
    • Braun, R.J.; Sommer, C.; Carmona-Gutierrez, D.; Khoury, C.M.; Ring, J.; Büttner, S.; Madeo, F. Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast. J. Biol. Chem. 2011, 286, 19958-19972.
    • (2011) J. Biol. Chem , vol.286 , pp. 19958-19972
    • Braun, R.J.1    Sommer, C.2    Carmona-Gutierrez, D.3    Khoury, C.M.4    Ring, J.5    Büttner, S.6    Madeo, F.7
  • 105
    • 77955423158 scopus 로고    scopus 로고
    • Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell
    • Duan, W.; Li, X.; Shi, J.; Guo, Y.; Li, Z.; Li, C. Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell. Neuroscience 2010, 169, 1621-1629.
    • (2010) Neuroscience , vol.169 , pp. 1621-1629
    • Duan, W.1    Li, X.2    Shi, J.3    Guo, Y.4    Li, Z.5    Li, C.6
  • 106
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto, M.; Hsu, L.J.; Xia, Y.; Takeda, A.; Sisk, A.; Sundsmo, M.; Masliah, E. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport 1999, 10, 717-721.
    • (1999) Neuroreport , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6    Masliah, E.7
  • 107
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught, K.S.; Jenner, P. Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 2001, 297, 191-194.
    • (2001) Neurosci. Lett , vol.297 , pp. 191-194
    • McNaught, K.S.1    Jenner, P.2
  • 108
    • 84869039156 scopus 로고    scopus 로고
    • Protein clearance mechanisms of alpha-synuclein and amyloid-beta in lewy body disorders
    • 2012
    • Deleidi, M.; Maetzler, W. Protein clearance mechanisms of alpha-synuclein and amyloid-beta in lewy body disorders. Int. J. Alzheimers Dis. 2012, 2012, 391-438.
    • (2012) Int. J. Alzheimers Dis , pp. 391-438
    • Deleidi, M.1    Maetzler, W.2
  • 109
    • 84881251933 scopus 로고    scopus 로고
    • Microglia during development and aging
    • Harry, G.J. Microglia during development and aging. Pharmacol. Ther. 2013, 139, 313-326.
    • (2013) Pharmacol. Ther , vol.139 , pp. 313-326
    • Harry, G.J.1
  • 110
    • 84890455433 scopus 로고    scopus 로고
    • Roles of endoplasmic reticulum stress in neurodegenerative diseases
    • Kanemoto, S.; Wang, H. Roles of endoplasmic reticulum stress in neurodegenerative diseases. Transl. Med. 2012, 2, 1000e108.
    • (2012) Transl. Med , vol.2
    • Kanemoto, S.1    Wang, H.2
  • 111
    • 84872192695 scopus 로고    scopus 로고
    • An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases
    • Bhandary, B.; Marahatta, A.; Kim, H.R.; Chae, H.J. An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases. Int. J. Mol. Sci. 2012, 14, 434-456.
    • (2012) Int. J. Mol. Sci , vol.14 , pp. 434-456
    • Bhandary, B.1    Marahatta, A.2    Kim, H.R.3    Chae, H.J.4
  • 113
    • 80053252011 scopus 로고    scopus 로고
    • Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders
    • Doyle, K.M.; Kennedy, D.; Gorman, A.M.; Gupta, S.; Healy, S.J.; Samali, A. Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders. J. Cell. Mol. Med. 2011, 15, 2025-2039.
    • (2011) J. Cell. Mol. Med , vol.15 , pp. 2025-2039
    • Doyle, K.M.1    Kennedy, D.2    Gorman, A.M.3    Gupta, S.4    Healy, S.J.5    Samali, A.6
  • 114
    • 84855557782 scopus 로고    scopus 로고
    • Neurological complications of chemotherapy to the central nervous system
    • Newton, H.B. Neurological complications of chemotherapy to the central nervous system. Handb. Clin. Neurol. 2012, 105, 903-916.
    • (2012) Handb. Clin. Neurol , vol.105 , pp. 903-916
    • Newton, H.B.1
  • 115
    • 0032481412 scopus 로고    scopus 로고
    • Impairment of cognitive function in women receiving adjuvant treatment for high-risk breast cancer: High-dose versus standarddose chemotherapy
    • Van Dam, F.S.; Schagen, S.B.; Muller, M.J.; Boogerd, W.; Wall, E.; Droogleever Fortuyn, M.E.; Rodenhuis, S. Impairment of cognitive function in women receiving adjuvant treatment for high-risk breast cancer: high-dose versus standarddose chemotherapy. J. Natl. Cancer Inst. 1998, 90, 210-218.
    • (1998) J. Natl. Cancer Inst , vol.90 , pp. 210-218
    • van Dam, F.S.1    Schagen, S.B.2    Muller, M.J.3    Boogerd, W.4    Wall, E.5    Droogleever, F.M.E.6    Rodenhuis, S.7
  • 117
    • 41549111000 scopus 로고    scopus 로고
    • Cancer and cancer therapy related cognitive dysfunction: An international perspective from the Venice cognitive workshop
    • Vardy, J.; Wefel, J.S.; Ahles, T.; Tannock, I.F.; Schagen, S.B. Cancer and cancer therapy related cognitive dysfunction: An international perspective from the Venice cognitive workshop. Ann. Oncol. 2008, 91, 623-629.
    • (2008) Ann. Oncol , vol.91 , pp. 623-629
    • Vardy, J.1    Wefel, J.S.2    Ahles, T.3    Tannock, I.F.4    Schagen, S.B.5
  • 118
    • 34547226593 scopus 로고    scopus 로고
    • Cognitive function after chemotherapy in adults with solid tumours
    • Vardy, J.; Tannock, I. Cognitive function after chemotherapy in adults with solid tumours. Crit. Rev. Oncol. Hematol. 2007, 63, 183-202.
    • (2007) Crit. Rev. Oncol. Hematol , vol.63 , pp. 183-202
    • Vardy, J.1    Tannock, I.2
  • 119
    • 81755188352 scopus 로고    scopus 로고
    • Cognitive dysfunction and cancer: Which consequences in terms of disease management?
    • Joly, F.; Rigal, O.; Noal, S.; Giffard, B. Cognitive dysfunction and cancer: Which consequences in terms of disease management? Psychooncology 2011, 20, 1251-1258.
    • (2011) Psychooncology , vol.20 , pp. 1251-1258
    • Joly, F.1    Rigal, O.2    Noal, S.3    Giffard, B.4
  • 120
    • 33845641831 scopus 로고    scopus 로고
    • Change in cognitive function after chemotherapy: A prospective longitudinal study in breast cancer patients
    • Schagen, S.B.; Muller, M.J.; Boogerd, W.; Mellenbergh, G.J.; van Dam, F.S. Change in cognitive function after chemotherapy: A prospective longitudinal study in breast cancer patients. J. Natl. Cancer Inst. 2006, 98, 1742-1745.
    • (2006) J. Natl. Cancer Inst , vol.98 , pp. 1742-1745
    • Schagen, S.B.1    Muller, M.J.2    Boogerd, W.3    Mellenbergh, G.J.4    van Dam, F.S.5
  • 122
    • 33744967562 scopus 로고    scopus 로고
    • Effects of high-dose and conventional-dose adjuvant chemotherapy on long-term cognitive sequelae in patients with breast cancer: An electrophysiologic study
    • Kreukels, B.P.; Schagen, S.B.; Ridderinkhof, K.R.; Boogerd, W.; Hamburger, H.L.; Muller, M.J.; van Dam, F.S. Effects of high-dose and conventional-dose adjuvant chemotherapy on long-term cognitive sequelae in patients with breast cancer: an electrophysiologic study. Clin. Breast Cancer 2006, 7, 67-78.
    • (2006) Clin. Breast Cancer , vol.7 , pp. 67-78
    • Kreukels, B.P.1    Schagen, S.B.2    Ridderinkhof, K.R.3    Boogerd, W.4    Hamburger, H.L.5    Muller, M.J.6    van Dam, F.S.7
  • 125
    • 77954898295 scopus 로고    scopus 로고
    • Acute and late onset cognitive dysfunction associated with chemotherapy in women with breast cancer
    • Wefel, J.S.; Saleeba, A.K.; Buzdar, A.U.; Meyers, C.A. Acute and late onset cognitive dysfunction associated with chemotherapy in women with breast cancer. Cancer 2010,116, 3348-3356.
    • (2010) Cancer , vol.116 , pp. 3348-3356
    • Wefel, J.S.1    Saleeba, A.K.2    Buzdar, A.U.3    Meyers, C.A.4
  • 127
    • 33847307470 scopus 로고    scopus 로고
    • Glutathione elevation by gamma-glutamyl cysteine ethyl ester as a potential therapeutic strategy for preventing oxidative stress in brain mediated by in vivo administration of adriamycin: Implication for chemobrain
    • Joshi, G.; Hardas, S.; Sultana, R.; St Clair, D.K.; Vore, M.; Butterfield, D.A. Glutathione elevation by gamma-glutamyl cysteine ethyl ester as a potential therapeutic strategy for preventing oxidative stress in brain mediated by in vivo administration of adriamycin: Implication for chemobrain. J. Neurosci. Res. 2007, 85, 497-503.
    • (2007) J. Neurosci. Res , vol.85 , pp. 497-503
    • Joshi, G.1    Hardas, S.2    Sultana, R.3    St Clair, D.K.4    Vore, M.5    Butterfield, D.A.6
  • 130
    • 48249126198 scopus 로고    scopus 로고
    • 5-Fluorouracil chemotherapy affects spatial working memory and newborn neurons in the adult rat hippocampus
    • Mustafa, S.; Walker, A.; Bennett, G.; Wigmore, P.M. 5-Fluorouracil chemotherapy affects spatial working memory and newborn neurons in the adult rat hippocampus. Eur. J. Neurosci. 2008, 28, 323-330.
    • (2008) Eur. J. Neurosci , vol.28 , pp. 323-330
    • Mustafa, S.1    Walker, A.2    Bennett, G.3    Wigmore, P.M.4
  • 132
    • 78649903193 scopus 로고    scopus 로고
    • Neurobiological basis of chemotherapy-induced cognitive impairment: A review of rodent research
    • Seigers, R.; Fardell, J.E. Neurobiological basis of chemotherapy-induced cognitive impairment: A review of rodent research. Neurosci. Biobehav. Rev. 2011, 35, 729-741.
    • (2011) Neurosci. Biobehav. Rev , vol.35 , pp. 729-741
    • Seigers, R.1    Fardell, J.E.2
  • 133
    • 84890473791 scopus 로고    scopus 로고
    • Antioxidant Supplementation in Cancer: Potential Interactions with Conventional Chemotherapy and Radiation Therapy. Available online, accessed on 1 May 2001
    • Antioxidant Supplementation in Cancer: Potential Interactions with Conventional Chemotherapy and Radiation Therapy. Available online: http://jdc.jefferson.edu/jmbcim/12/ (accessed on 1 May 2001).
  • 135
    • 42549123787 scopus 로고    scopus 로고
    • Systemic 5-fluorouracil treatment causes a syndrome of delayed myelin destruction in the central nervous system
    • Han, R.; Yang, Y.M.; Dietrich, J.; Luebke, A.; Mayer-Pröschel, M.; Noble, M. Systemic 5-fluorouracil treatment causes a syndrome of delayed myelin destruction in the central nervous system. J. Biol. 2008, 7, 12.
    • (2008) J. Biol , vol.7 , pp. 12
    • Han, R.1    Yang, Y.M.2    Dietrich, J.3    Luebke, A.4    Mayer-Pröschel, M.5    Noble, M.6
  • 137
    • 84863976493 scopus 로고    scopus 로고
    • Reduction of oxidative stress in liver cancer patients by oral green tea polyphenol tablets during hepatic arterial infusion chemotherapy
    • Baba, Y.; Sonoda, J.I.; Hayashi, S.; Tosuji, N.; Sonoda, S.; Makisumi, K.; Nakajo, M. Reduction of oxidative stress in liver cancer patients by oral green tea polyphenol tablets during hepatic arterial infusion chemotherapy. Exp. Ther. Med. 2012, 4, 452-458.
    • (2012) Exp. Ther. Med , vol.4 , pp. 452-458
    • Baba, Y.1    Sonoda, J.I.2    Hayashi, S.3    Tosuji, N.4    Sonoda, S.5    Makisumi, K.6    Nakajo, M.7
  • 139
    • 16644366977 scopus 로고    scopus 로고
    • Oxidative changes in cerebral spinal fluid phosphatidylcholine during treatment for acute lymphoblastic leukemia
    • Miketova, P.; Kaemingk, K.; Hockenberry, M.; Pasvogel, A.; Hutter, J.; Krull, K.; Moore, I.M. Oxidative changes in cerebral spinal fluid phosphatidylcholine during treatment for acute lymphoblastic leukemia. Biol. Res. Nurs. 2005, 6, 187-195.
    • (2005) Biol. Res. Nurs , vol.6 , pp. 187-195
    • Miketova, P.1    Kaemingk, K.2    Hockenberry, M.3    Pasvogel, A.4    Hutter, J.5    Krull, K.6    Moore, I.M.7
  • 140
    • 69849108260 scopus 로고    scopus 로고
    • Oxidative stress and executive function in children receiving chemotherapy for acute lymphoblastic leukemia
    • Caron, J.E.; Krull, K.R.; Hockenberry, M.; Jain, N.; Kaemingk, K.; Moore, I.M. Oxidative stress and executive function in children receiving chemotherapy for acute lymphoblastic leukemia. Pediatr. Blood Cancer 2009, 53, 551-556.
    • (2009) Pediatr. Blood Cancer , vol.53 , pp. 551-556
    • Caron, J.E.1    Krull, K.R.2    Hockenberry, M.3    Jain, N.4    Kaemingk, K.5    Moore, I.M.6
  • 141
    • 33748090583 scopus 로고    scopus 로고
    • Neurological complications of cancer chemotherapy
    • Hildebrand, J. Neurological complications of cancer chemotherapy. Curr. Opin. Oncol. 2006, 18, 321-324.
    • (2006) Curr. Opin. Oncol , vol.18 , pp. 321-324
    • Hildebrand, J.1
  • 142
    • 84890444639 scopus 로고    scopus 로고
    • NCI Report. Available online, accessed on 30 September
    • NCI Report. Available online: http://www.cancer.gov/aboutnci/ncicancerbulletin/archive/2010/022310/page6 (accessed on 30 September 2013).
    • (2013)
  • 144
    • 77956223765 scopus 로고    scopus 로고
    • Patient perceptions associated with chemotherapy-induced peripheral neuropathy
    • Tofthagen, C. Patient perceptions associated with chemotherapy-induced peripheral neuropathy. Clin. J. Oncol. Nurs. 2010, 14, E22-E28.
    • (2010) Clin. J. Oncol. Nurs , vol.14
    • Tofthagen, C.1
  • 145
    • 77952217466 scopus 로고    scopus 로고
    • Effects on the visual system might contribute to some of the cognitive deficits of cancer chemotherapy-induced chemo-fog
    • Raffa, R.B.; Tallarida, R.J. Effects on the visual system might contribute to some of the cognitive deficits of cancer chemotherapy-induced "chemo-fog". J. Clin. Pharm. Ther. 2010, 35, 249-255.
    • (2010) J. Clin. Pharm. Ther , vol.35 , pp. 249-255
    • Raffa, R.B.1    Tallarida, R.J.2
  • 147
    • 84857786335 scopus 로고    scopus 로고
    • Oxaliplatin-induced neuropathy: Oxidative stress as pathological mechanism. Protective effect of silibinin
    • Di Cesare Mannelli, L.; Zanardelli, M.; Failli, P.; Ghelardini, C. Oxaliplatin-induced neuropathy: Oxidative stress as pathological mechanism. Protective effect of silibinin. J. Pain 2012, 13, 276-284.
    • (2012) J. Pain , vol.13 , pp. 276-284
    • Di Cesare, M.L.1    Zanardelli, M.2    Failli, P.3    Ghelardini, C.4
  • 149
    • 51049100621 scopus 로고    scopus 로고
    • Implications of apurinic/apyrimidinic endonuclease in reactive oxygen signaling response after cisplatin treatment of dorsal root ganglion neurons
    • Jiang, Y.; Guo, C.; Vasko, M.R.; Kelley, M.R. Implications of apurinic/apyrimidinic endonuclease in reactive oxygen signaling response after cisplatin treatment of dorsal root ganglion neurons. Cancer Res. 2008, 68, 6425-6434.
    • (2008) Cancer Res , vol.68 , pp. 6425-6434
    • Jiang, Y.1    Guo, C.2    Vasko, M.R.3    Kelley, M.R.4
  • 150
    • 8844251566 scopus 로고    scopus 로고
    • Antioxidant protection in a new animal model of cisplatin-induced ototoxicity
    • Minami, S.B.; Sha, S.H.; Schacht, J. Antioxidant protection in a new animal model of cisplatin-induced ototoxicity. Hear. Res. 2004, 198, 137-143.
    • (2004) Hear. Res , vol.198 , pp. 137-143
    • Minami, S.B.1    Sha, S.H.2    Schacht, J.3
  • 151
    • 84875271492 scopus 로고    scopus 로고
    • Cisplatin-induced ototoxicity: Transporters playing a role in cisplatin toxicity
    • Waissbluth, S.; Daniel, S.J. Cisplatin-induced ototoxicity: Transporters playing a role in cisplatin toxicity. Hear. Res. 2013, 299, 37-45.
    • (2013) Hear. Res , vol.299 , pp. 37-45
    • Waissbluth, S.1    Daniel, S.J.2
  • 152
    • 38449121513 scopus 로고    scopus 로고
    • Studies on free radicals, antioxidants, and co-factors
    • Rahman, K. Studies on free radicals, antioxidants, and co-factors. Clin. Interv. Aging 2007, 2, 219-236.
    • (2007) Clin. Interv. Aging , vol.2 , pp. 219-236
    • Rahman, K.1
  • 154
    • 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.; Praticò, D. 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. 2004, 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    Praticò, D.7
  • 155
    • 0030875330 scopus 로고    scopus 로고
    • Mechanisms and dynamics of antioxidant action of ubiquinol
    • Niki, E. Mechanisms and dynamics of antioxidant action of ubiquinol. Mol. Aspects Med. 1997, 18, S63-S70.
    • (1997) Mol. Aspects Med , vol.18
    • Niki, E.1
  • 156
    • 65549091910 scopus 로고    scopus 로고
    • Combination therapy with coenzyme Q10 and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases
    • Yang, L.; Calingasan, N.Y.; Wille, E.J.; Cormier, K.; Smith, K.; Ferrante, R.J.; Beal, M.F. Combination therapy with coenzyme Q10 and creatine produces additive neuroprotective effects in models of Parkinson's and Huntington's diseases. J. Neurochem. 2009, 109, 1427-1439.
    • (2009) J. Neurochem , vol.109 , pp. 1427-1439
    • Yang, L.1    Calingasan, N.Y.2    Wille, E.J.3    Cormier, K.4    Smith, K.5    Ferrante, R.J.6    Beal, M.F.7
  • 157
    • 84889887220 scopus 로고    scopus 로고
    • Therapeutic neuroprotective agents for amyotrophic lateral sclerosis
    • doi:10.1007/s00018-013-1415-0
    • Pandya, R.S.; Zhu, H.; Li, W.; Bowser, R.; Friedlander, R.M.; Wang, X. Therapeutic neuroprotective agents for amyotrophic lateral sclerosis. Cell. Mol. Life Sci. 2013, doi:10.1007/s00018-013-1415-0.
    • (2013) Cell. Mol. Life Sci
    • Pandya, R.S.1    Zhu, H.2    Li, W.3    Bowser, R.4    Friedlander, R.M.5    Wang, X.6
  • 159
    • 0034482931 scopus 로고    scopus 로고
    • Evaluation of D-methionine as a cytoprotectant in cisplatin treatment of an animal model for ovarian cancer
    • Cloven, N.G.; Re, A.; McHale, M.T.; Burger, R.A.; DiSaia, P.J.; Rose, G.S.; Campbell, K.C.; Fan, H. Evaluation of D-methionine as a cytoprotectant in cisplatin treatment of an animal model for ovarian cancer. Anticancer Res. 2000, 20, 4205-4209.
    • (2000) Anticancer Res , vol.20 , pp. 4205-4209
    • Cloven, N.G.1    Re, A.2    McHale, M.T.3    Burger, R.A.4    Disaia, P.J.5    Rose, G.S.6    Campbell, K.C.7    Fan, H.8
  • 160
  • 163
    • 84890485350 scopus 로고    scopus 로고
    • CIPN: Treatment preservation and prevention are the goals. Available online, accessed on 1 September 2011
    • CIPN: Treatment preservation and prevention are the goals. Available online: http://www.oncologynurseadvisor.com/cipn-treatment-preservation-and-prevention-are-the-goals/article/212533/ (accessed on 1 September 2011).
  • 164
    • 0033134010 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of photoreceptor apoptosis in vitro
    • Carmody, R.J.; McGowan, A.J.; Cotter, T.G. Reactive oxygen species as mediators of photoreceptor apoptosis in vitro. Exp. Cell. Res. 1999, 248, 520-530.
    • (1999) Exp. Cell. Res , vol.248 , pp. 520-530
    • Carmody, R.J.1    McGowan, A.J.2    Cotter, T.G.3
  • 165
    • 0033062872 scopus 로고    scopus 로고
    • Induction of CD95 ligand and apoptosis by doxorubicin is modulated by the redox state in chemosensitive- and drug-resistant tumor cells
    • Friesen, C.; Fulda, S.; Debatin, K.M. Induction of CD95 ligand and apoptosis by doxorubicin is modulated by the redox state in chemosensitive- and drug-resistant tumor cells. Cell Death Differ. 1999, 6, 471-480.
    • (1999) Cell Death Differ , vol.6 , pp. 471-480
    • Friesen, C.1    Fulda, S.2    Debatin, K.M.3
  • 166
    • 0035869341 scopus 로고    scopus 로고
    • Evidence for redox regulation of cytochrome C release during programmed neuronal death: Antioxidant effects of protein synthesis and caspase inhibition
    • Kirkland, R.A.; Franklin, J.L. Evidence for redox regulation of cytochrome C release during programmed neuronal death: Antioxidant effects of protein synthesis and caspase inhibition. J. Neurosci. 2001, 21, 1949-1963.
    • (2001) J. Neurosci , vol.21 , pp. 1949-1963
    • Kirkland, R.A.1    Franklin, J.L.2
  • 168
    • 0034979803 scopus 로고    scopus 로고
    • Contribution of reactive oxygen species to 3-hydroxyglutarate neurotoxicity in primary neuronal cultures from chick embryo telencephalons
    • Kölker, S.; Ahlemeyer, B.; Krieglstein, J.; Hoffmann, G.F. Contribution of reactive oxygen species to 3-hydroxyglutarate neurotoxicity in primary neuronal cultures from chick embryo telencephalons. Pediatr. Res. 2001, 50, 76-82.
    • (2001) Pediatr. Res , vol.50 , pp. 76-82
    • Kölker, S.1    Ahlemeyer, B.2    Krieglstein, J.3    Hoffmann, G.F.4
  • 169
    • 80054874386 scopus 로고    scopus 로고
    • Melatonin abrogates cadmium induced oxidative stress related neurotoxicity in rats
    • Shagirtha, K.; Muthumani, M.; Prabu, S.M. Melatonin abrogates cadmium induced oxidative stress related neurotoxicity in rats. Eur. Rev. Med. Pharmacol. Sci. 2011, 15, 1039-1050.
    • (2011) Eur. Rev. Med. Pharmacol. Sci , vol.15 , pp. 1039-1050
    • Shagirtha, K.1    Muthumani, M.2    Prabu, S.M.3
  • 170
    • 0033042355 scopus 로고    scopus 로고
    • Synergism of nitric oxide and iron in killing the transformed murine oligodendrocyte cell line N20.1
    • Boullerne, A.I.; Nedelkoska, L.; Benjamins, J.A. Synergism of nitric oxide and iron in killing the transformed murine oligodendrocyte cell line N20.1. J. Neurochem. 1999, 72, 1050-1060.
    • (1999) J. Neurochem , vol.72 , pp. 1050-1060
    • Boullerne, A.I.1    Nedelkoska, L.2    Benjamins, J.A.3
  • 172
    • 78751698755 scopus 로고    scopus 로고
    • Quercetin exerts a neuroprotective effect through inhibition of the iNOS/NO system and pro-inflammation gene expression in PC12 cells and in zebrafish
    • Zhang, Z.J.; Cheang, L.C.; Wang, M.W.; Lee, S.M. Quercetin exerts a neuroprotective effect through inhibition of the iNOS/NO system and pro-inflammation gene expression in PC12 cells and in zebrafish. Int. J. Mol. Med. 2011, 27, 195-203.
    • (2011) Int. J. Mol. Med , vol.27 , pp. 195-203
    • Zhang, Z.J.1    Cheang, L.C.2    Wang, M.W.3    Lee, S.M.4
  • 173
    • 0034038044 scopus 로고    scopus 로고
    • Uric acid, a peroxynitrite scavenger, inhibits CNS inflammation, blood-CNS barrier permeability changes, and tissue damage in a mouse model of multiple sclerosis
    • Hooper, D.C.; Scott, G.S.; Zborek, A.; Mikheeva, T.; Kean, R.B.; Koprowski, H.; Spitsin, S.V. Uric acid, a peroxynitrite scavenger, inhibits CNS inflammation, blood-CNS barrier permeability changes, and tissue damage in a mouse model of multiple sclerosis. FASEB J. 2000, 14, 691-698.
    • (2000) FASEB J , vol.14 , pp. 691-698
    • Hooper, D.C.1    Scott, G.S.2    Zborek, A.3    Mikheeva, T.4    Kean, R.B.5    Koprowski, H.6    Spitsin, S.V.7
  • 174
    • 3042625013 scopus 로고    scopus 로고
    • Hesperetin: A potent antioxidant against peroxynitrite
    • Kim, J.Y.; Jung, K.J.; Choi, J.S.; Chung, H.Y. Hesperetin: A potent antioxidant against peroxynitrite. Free Radic. Res. 2004, 38, 761-769.
    • (2004) Free Radic. Res , vol.38 , pp. 761-769
    • Kim, J.Y.1    Jung, K.J.2    Choi, J.S.3    Chung, H.Y.4
  • 175
    • 0020625894 scopus 로고
    • Flow cytometric studies of oxidative product formation by neutrophils: A graded response to membrane stimulation
    • Bass, D.A.; Parce, J.W.; Dechatelet, L.R.; Szejda, P.; Seeds, M.C.; Thomas, M. Flow cytometric studies of oxidative product formation by neutrophils: A graded response to membrane stimulation. J. Immunol. 1983, 130, 1910-1917.
    • (1983) J. Immunol , vol.130 , pp. 1910-1917
    • Bass, D.A.1    Parce, J.W.2    Dechatelet, L.R.3    Szejda, P.4    Seeds, M.C.5    Thomas, M.6
  • 176
    • 0027249757 scopus 로고
    • Evaluation of 2',7'-dichlorofluorescin and dihydrorhodamine 123 as fluorescent probes for intracellular H2O2 in cultured endothelial cells
    • Royall, J.A.; Ischiropoulos, H. Evaluation of 2',7'-dichlorofluorescin and dihydrorhodamine 123 as fluorescent probes for intracellular H2O2 in cultured endothelial cells. Arch. Biochem. Biophys. 1993, 302, 348-355.
    • (1993) Arch. Biochem. Biophys , vol.302 , pp. 348-355
    • Royall, J.A.1    Ischiropoulos, H.2
  • 177
    • 0026643574 scopus 로고
    • Flow cytometric analysis of nitric oxide production in human neutrophils using dichlorofluorescein diacetate in the presence of a calmodulin inhibitor
    • Rao, K.M.; Padmanabhan, J.; Kilby, D.L.; Cohen, H.J.; Currie, M.S.; Weinberg, J.B. Flow cytometric analysis of nitric oxide production in human neutrophils using dichlorofluorescein diacetate in the presence of a calmodulin inhibitor. J. Leukoc. Biol. 1992, 51, 496-500.
    • (1992) J. Leukoc. Biol , vol.51 , pp. 496-500
    • Rao, K.M.1    Padmanabhan, J.2    Kilby, D.L.3    Cohen, H.J.4    Currie, M.S.5    Weinberg, J.B.6
  • 178
    • 0037718255 scopus 로고    scopus 로고
    • Evaluation of the probes 2',7'-dichlorofluorescin diacetate, luminol, and lucigenin as indicators of reactive species formation
    • Myhre, O.; Andersen, J.M.; Aarnes, H.; Fonnum, F. Evaluation of the probes 2',7'-dichlorofluorescin diacetate, luminol, and lucigenin as indicators of reactive species formation. Biochem. Pharmacol. 2003, 65, 1575-1582.
    • (2003) Biochem. Pharmacol , vol.65 , pp. 1575-1582
    • Myhre, O.1    Andersen, J.M.2    Aarnes, H.3    Fonnum, F.4
  • 179
    • 11044223897 scopus 로고    scopus 로고
    • Analysis of dichlorodihydrofluorescein and dihydrocalcein as probes for the detection of intracellular reactive oxygen species
    • Keller, A.; Mohamed, A.; Dröse, S.; Brandt, U.; Fleming, I.; Brandes, R.P. Analysis of dichlorodihydrofluorescein and dihydrocalcein as probes for the detection of intracellular reactive oxygen species. Free Radic. Res. 2004, 38, 1257-1267.
    • (2004) Free Radic. Res , vol.38 , pp. 1257-1267
    • Keller, A.1    Mohamed, A.2    Dröse, S.3    Brandt, U.4    Fleming, I.5    Brandes, R.P.6
  • 180
    • 0031796255 scopus 로고    scopus 로고
    • Analytical and numerical techniques for evaluation of free radical damage in cultured cells using imaging cytometry and fluorescent indicators
    • Buxser, S.E.; Sawada, G.; Raub, T.J. Analytical and numerical techniques for evaluation of free radical damage in cultured cells using imaging cytometry and fluorescent indicators. Methods Enzymol. 1999, 300, 256-275.
    • (1999) Methods Enzymol , vol.300 , pp. 256-275
    • Buxser, S.E.1    Sawada, G.2    Raub, T.J.3
  • 181
    • 0032211437 scopus 로고    scopus 로고
    • Critical evaluation of the use of hydroethidine as a measure of superoxide anion radical
    • Benov, L.; Sztejnberg, L.; Fridovich, I. Critical evaluation of the use of hydroethidine as a measure of superoxide anion radical. Free Radic. Biol. Med. 1998, 25, 826-831.
    • (1998) Free Radic. Biol. Med , vol.25 , pp. 826-831
    • Benov, L.1    Sztejnberg, L.2    Fridovich, I.3
  • 182
    • 34547123848 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species signal hepatocyte steatosis by regulating the phosphatidylinositol 3-kinase cell survival pathway
    • Kohli, R.; Pan, X.; Malladi, P.; Wainwright, M.S.; Whitington, P.F. Mitochondrial reactive oxygen species signal hepatocyte steatosis by regulating the phosphatidylinositol 3-kinase cell survival pathway. J. Biol. Chem. 2007, 282, 21327-21336.
    • (2007) J. Biol. Chem , vol.282 , pp. 21327-21336
    • Kohli, R.1    Pan, X.2    Malladi, P.3    Wainwright, M.S.4    Whitington, P.F.5
  • 183
    • 80053371451 scopus 로고    scopus 로고
    • Oxidative chemistry of fluorescent dyes: Implications in the detection of reactive oxygen and nitrogen species
    • Kalyanaraman, B. Oxidative chemistry of fluorescent dyes: Implications in the detection of reactive oxygen and nitrogen species. Biochem. Soc. Trans. 2011, 39, 1221-1225.
    • (2011) Biochem. Soc. Trans , vol.39 , pp. 1221-1225
    • Kalyanaraman, B.1
  • 184
    • 84890117297 scopus 로고    scopus 로고
    • HPLC-based monitoring of products formed from hydroethidine-based fluorogenic probes-The ultimate approach for intra- and extracellular superoxide detection
    • doi:10.1016/j.bbagen.2013.05.008
    • Kalyanaraman, B.; Dranka, B.P.; Hardy, M.; Michalski, R.; Zielonka, J. HPLC-based monitoring of products formed from hydroethidine-based fluorogenic probes-The ultimate approach for intra- and extracellular superoxide detection. Biochim. Biophys. Acta 2013, doi:10.1016/j.bbagen.2013.05.008.
    • (2013) Biochim. Biophys. Acta
    • Kalyanaraman, B.1    Dranka, B.P.2    Hardy, M.3    Michalski, R.4    Zielonka, J.5
  • 185
    • 1342284088 scopus 로고    scopus 로고
    • Detection of superoxide and peroxynitrite in model systems and mitochondria by the luminol analogue L-012
    • Daiber, A.; Oelze, M.; August, M.; Wendt, M.; Sydow, K.; Wieboldt, H.; Kleschyov, A.L.; Munzel, T. Detection of superoxide and peroxynitrite in model systems and mitochondria by the luminol analogue L-012. Free Radic. Res. 2004, 38, 259-269.
    • (2004) Free Radic. Res , vol.38 , pp. 259-269
    • Daiber, A.1    Oelze, M.2    August, M.3    Wendt, M.4    Sydow, K.5    Wieboldt, H.6    Kleschyov, A.L.7    Munzel, T.8
  • 186
    • 0027489601 scopus 로고
    • Luminol and lucigenin as detectors for O2
    • Faulkner, K.; Fridovich, I. Luminol and lucigenin as detectors for O2. Free Radic. Biol. Med. 1993, 15, 447-451.
    • (1993) Free Radic. Biol. Med , vol.15 , pp. 447-451
    • Faulkner, K.1    Fridovich, I.2
  • 187
    • 0034650766 scopus 로고    scopus 로고
    • Lucigenin: Redox potential in aqueous media and redox cycling with O2 production
    • Spasojevic, I.; Liochev, S.I.; Fridovich, I. Lucigenin: Redox potential in aqueous media and redox cycling with O2 production. Arch. Biochem. Biophys. 2000, 373, 447-450.
    • (2000) Arch. Biochem. Biophys , vol.373 , pp. 447-450
    • Spasojevic, I.1    Liochev, S.I.2    Fridovich, I.3
  • 188
    • 0032533982 scopus 로고    scopus 로고
    • Lucigenin as mediator of superoxide production: Revisited
    • Liochev, S.I.; Fridovich, I. Lucigenin as mediator of superoxide production: Revisited. Free Radic. Biol. Med. 1998, 25, 926-928.
    • (1998) Free Radic. Biol. Med , vol.25 , pp. 926-928
    • Liochev, S.I.1    Fridovich, I.2
  • 189
    • 0031941373 scopus 로고    scopus 로고
    • Validation of lucigenin (bis-N-methylacridinium) as a chemilumigenic probe for detecting superoxide anion radical production by enzymatic and cellular systems
    • Li, Y.; Zhu, H.; Kuppusamy, P.; Roubaud, V.; Zweier, J.L.; Trush, M.A. Validation of lucigenin (bis-N-methylacridinium) as a chemilumigenic probe for detecting superoxide anion radical production by enzymatic and cellular systems. J. Biol. Chem. 1998, 273, 2015-2023.
    • (1998) J. Biol. Chem , vol.273 , pp. 2015-2023
    • Li, Y.1    Zhu, H.2    Kuppusamy, P.3    Roubaud, V.4    Zweier, J.L.5    Trush, M.A.6
  • 190
    • 17644394600 scopus 로고    scopus 로고
    • Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescence
    • Zhao, H.; Joseph, J.; Fales, H.M.; Sokoloski, E.A.; Levine, R.L.; Vasquez-Vivar, J.; Kalyanaraman, B. Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescence. Proc. Natl. Acad. Sci. USA 2005, 102, 5727-5732.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5727-5732
    • Zhao, H.1    Joseph, J.2    Fales, H.M.3    Sokoloski, E.A.4    Levine, R.L.5    Vasquez-Vivar, J.6    Kalyanaraman, B.7
  • 191
    • 67649421395 scopus 로고    scopus 로고
    • Hydroxyl and superoxide radical scavenging abilities of chromonyl-thiazolidine-2,4-dione compounds
    • Kruk, I.; Bozdaǧ-Dündar, O.; Ertan, R.; Aboul-Enein, H.Y.; Michalska, T. Hydroxyl and superoxide radical scavenging abilities of chromonyl-thiazolidine-2,4-dione compounds. Luminescence 2009, 24, 96-101.
    • (2009) Luminescence , vol.24 , pp. 96-101
    • Kruk, I.1    Bozdaǧ-Dündar, O.2    Ertan, R.3    Aboul-Enein, H.Y.4    Michalska, T.5
  • 192
    • 84886771321 scopus 로고    scopus 로고
    • Antioxidant activities of some new chromonyl-2,4-thiazolidinediones and chromonyl-2,4-imidazolidinediones having chromone cores
    • Berczyński, P.; Kładna, A.; Kruk, I.; Piechowska, T.; Aboul-Enein, H.Y.; Bozdaǧ-Dündar, O.; Ceylan-Unlusoy, M. Antioxidant activities of some new chromonyl-2,4-thiazolidinediones and chromonyl-2,4-imidazolidinediones having chromone cores. J. Fluoresc. 2013, 23, 1319-1327.
    • (2013) J. Fluoresc , vol.23 , pp. 1319-1327
    • Berczyński, P.1    Kładna, A.2    Kruk, I.3    Piechowska, T.4    Aboul-Enein, H.Y.5    Bozdaǧ-Dündar, O.6    Ceylan-Unlusoy, M.7
  • 193
    • 0035282339 scopus 로고    scopus 로고
    • Noninvasive detection of hydroxyl radical generation in lung by diesel exhaust particles
    • Han, J.Y.; Takeshita, K.; Utsumi, H. Noninvasive detection of hydroxyl radical generation in lung by diesel exhaust particles. Free Radic. Biol. Med. 2001, 30, 516-525.
    • (2001) Free Radic. Biol. Med , vol.30 , pp. 516-525
    • Han, J.Y.1    Takeshita, K.2    Utsumi, H.3
  • 194
    • 0037677089 scopus 로고    scopus 로고
    • In vivo electron spin resonance-computed tomography/nitroxyl probe technique for non-invasive analysis of oxidative injuries
    • Utsumi, H.; Yamada, K. In vivo electron spin resonance-computed tomography/nitroxyl probe technique for non-invasive analysis of oxidative injuries. Arch. Biochem. Biophys. 2003, 416, 1-8.
    • (2003) Arch. Biochem. Biophys , vol.416 , pp. 1-8
    • Utsumi, H.1    Yamada, K.2
  • 195
    • 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. 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. 2004, 142, 231-255.
    • (2004) Br. J. Pharmacol , vol.142 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 197
    • 0032496404 scopus 로고    scopus 로고
    • Direct evidence of nitric oxide production from bovine aortic endothelial cells using new fluorescence indicators: Diaminofluoresceins
    • Nakatsubo, N.; Kojima, H.; Kikuchi, K.; Nagoshi, H.; Hirata, Y.; Maeda, D.; Imai, Y.; Irimura, T.; Nagano, T. Direct evidence of nitric oxide production from bovine aortic endothelial cells using new fluorescence indicators: diaminofluoresceins. FEBS Lett. 1998, 427, 263-266.
    • (1998) FEBS Lett , vol.427 , pp. 263-266
    • Nakatsubo, N.1    Kojima, H.2    Kikuchi, K.3    Nagoshi, H.4    Hirata, Y.5    Maeda, D.6    Imai, Y.7    Irimura, T.8    Nagano, T.9
  • 198
    • 0036644215 scopus 로고    scopus 로고
    • Regulation and measurement of oxidative stress in apoptosis
    • Curtin, J.F.; Donovan, M.; Cotter, T.G. Regulation and measurement of oxidative stress in apoptosis. J. Immunol. Methods 2002, 265, 49-72.
    • (2002) J. Immunol. Methods , vol.265 , pp. 49-72
    • Curtin, J.F.1    Donovan, M.2    Cotter, T.G.3
  • 199
    • 33747807950 scopus 로고    scopus 로고
    • Mechanism-based molecular design of highly selective fluorescence probes for nitrative stress
    • Ueno, T.; Urano, Y.; Kojima, H.; Nagano, T. Mechanism-based molecular design of highly selective fluorescence probes for nitrative stress. J. Am. Chem. Soc. 2006, 128, 10640-10641.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10640-10641
    • Ueno, T.1    Urano, Y.2    Kojima, H.3    Nagano, T.4
  • 200
    • 77951988104 scopus 로고    scopus 로고
    • Peroxynitrite is the major species formed from different flux ratios of co-generated nitric oxide and superoxide: Direct reaction with boronate-based fluorescent probe
    • Zielonka, J.; Sikora, A.; Joseph, J.; Kalyanaraman, B. Peroxynitrite is the major species formed from different flux ratios of co-generated nitric oxide and superoxide: Direct reaction with boronate-based fluorescent probe. J. Biol. Chem. 2010, 285, 14210-14216.
    • (2010) J. Biol. Chem , vol.285 , pp. 14210-14216
    • Zielonka, J.1    Sikora, A.2    Joseph, J.3    Kalyanaraman, B.4
  • 201
    • 0025191219 scopus 로고
    • Isolation of nitric oxide synthetase, a calmodulinrequiring enzyme
    • Bredt, D.S.; Snyder, S.H. Isolation of nitric oxide synthetase, a calmodulinrequiring enzyme. Proc. Natl. Acad. Sci. USA 1990, 87, 682-685.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 682-685
    • Bredt, D.S.1    Snyder, S.H.2
  • 202
    • 0028034105 scopus 로고
    • Molecular mechanisms of inhibition of porcine brain nitric oxide synthase by the antinociceptive drug 7-nitroindazole
    • Mayer, B.; Klatt, P.; Werner, E.R.; Schmidt, K. Molecular mechanisms of inhibition of porcine brain nitric oxide synthase by the antinociceptive drug 7-nitroindazole. Neuropharmacology 1994, 33, 1253-1259.
    • (1994) Neuropharmacology , vol.33 , pp. 1253-1259
    • Mayer, B.1    Klatt, P.2    Werner, E.R.3    Schmidt, K.4
  • 203
    • 0030697859 scopus 로고    scopus 로고
    • Nitric oxide synthase activity in mitochondria
    • Ghafourifar, P.; Richter, C. Nitric oxide synthase activity in mitochondria. FEBS Lett. 1997, 418, 291-296.
    • (1997) FEBS Lett , vol.418 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 204
    • 0032755519 scopus 로고    scopus 로고
    • Specific efflux of glutathione from the basolateral membrane domain in polarized MDCK cells during ricin-induced apoptosis
    • Oda, T.; Sadakata, N.; Komatsu, N.; Muramatsu, T. Specific efflux of glutathione from the basolateral membrane domain in polarized MDCK cells during ricin-induced apoptosis. J. Biochem. 1999, 126, 715-721.
    • (1999) J. Biochem , vol.126 , pp. 715-721
    • Oda, T.1    Sadakata, N.2    Komatsu, N.3    Muramatsu, T.4
  • 206
    • 0029061415 scopus 로고
    • Bromobimane probes for thiols
    • Kosower, E.M.; Kosower, N.S. Bromobimane probes for thiols. Methods Enzymol. 1995, 251, 133-148.
    • (1995) Methods Enzymol , vol.251 , pp. 133-148
    • Kosower, E.M.1    Kosower, N.S.2
  • 207
    • 0031974066 scopus 로고    scopus 로고
    • Transmembrane redox signaling activates NF-kappaB in macrophages
    • Kaul, N.; Choi, J.; Forman, H.J. Transmembrane redox signaling activates NF-kappaB in macrophages. Free Radic. Biol. Med. 1998, 24, 202-207.
    • (1998) Free Radic. Biol. Med , vol.24 , pp. 202-207
    • Kaul, N.1    Choi, J.2    Forman, H.J.3
  • 208
    • 0014481378 scopus 로고
    • Enzymatic method for quantification of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze, F. Enzymatic method for quantification of total and oxidized glutathione: Applications to mammalian blood and other tissues. Anal. Biochem. 1969, 27, 502-522.
    • (1969) Anal. Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 209
    • 0030782430 scopus 로고    scopus 로고
    • Requirement for cGMP in nerve cell death caused by glutathione depletion
    • Li, Y.; Maher, P.; Schubert, D. Requirement for cGMP in nerve cell death caused by glutathione depletion. J. Cell Biol. 1997, 139, 1317-1324.
    • (1997) J. Cell Biol , vol.139 , pp. 1317-1324
    • Li, Y.1    Maher, P.2    Schubert, D.3
  • 210
    • 0033950664 scopus 로고    scopus 로고
    • A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1)
    • Peskin, A.V.; Winterbourn, C.C. A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1). Clin. Chim. Acta 2000, 293, 157-166.
    • (2000) Clin. Chim. Acta , vol.293 , pp. 157-166
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 211
    • 33646922865 scopus 로고    scopus 로고
    • Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice
    • Esposito, L.; Raber, J.; Kekonius, L.; Yan, F.; Yu, G.Q.; Bien-Ly, N.; Puoliväli, J.; Scearce-Levie, K.; Masliah, E.; Mucke, L. Reduction in mitochondrial superoxide dismutase modulates Alzheimer's disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice. J. Neurosci. 2006, 26, 5167-5179.
    • (2006) J. Neurosci , vol.26 , pp. 5167-5179
    • Esposito, L.1    Raber, J.2    Kekonius, L.3    Yan, F.4    Yu, G.Q.5    Bien-Ly, N.6    Puoliväli, J.7    Scearce-Levie, K.8    Masliah, E.9    Mucke, L.10
  • 214
    • 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. 1989, 476, 160-162.
    • (1989) Brain Res , vol.476 , pp. 160-162
    • Zemlan, F.P.1    Thienhaus, O.J.2    Bosmann, H.B.3
  • 215
    • 0026823074 scopus 로고
    • Immunohistochemical evidence of oxidative [corrected] stress in Alzheimer's disease
    • Pappolla, M.A.; Omar, R.A.; Kim, K.S.; Robakis, N.K. Immunohistochemical evidence of oxidative [corrected] stress in Alzheimer's disease. Am. J. Pathol. 1992, 140, 621-628.
    • (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
  • 216
  • 217
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • Paglia, D.E.; Valentine, W.N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med. 1967, 70, 158-69.
    • (1967) J. Lab. Clin. Med , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 219
    • 0023692586 scopus 로고
    • A spectrophotometric method for determination of catalase activity in small tissue samples
    • Johansson, L.H.; Borg, L.A. A spectrophotometric method for determination of catalase activity in small tissue samples. Anal. Biochem. 1988, 174, 331-336.
    • (1988) Anal. Biochem , vol.174 , pp. 331-336
    • Johansson, L.H.1    Borg, L.A.2
  • 220
    • 0032826921 scopus 로고    scopus 로고
    • Plasma pharmacokinetics, nervous system biodistribution and biostability, and spinal cord permeability at the blood-brain barrier of putrescine-modified catalase in the adult rat
    • Reinholz, M.M.; Haggard, J.J.; Curran, G.L.; Poduslo, J.F. Plasma pharmacokinetics, nervous system biodistribution and biostability, and spinal cord permeability at the blood-brain barrier of putrescine-modified catalase in the adult rat. Exp. Neurol. 1999, 159, 191-203.
    • (1999) Exp. Neurol , vol.159 , pp. 191-203
    • Reinholz, M.M.1    Haggard, J.J.2    Curran, G.L.3    Poduslo, J.F.4
  • 221
    • 23244453399 scopus 로고    scopus 로고
    • Antioxidant properties of minocycline: Neuroprotection in an oxidative stress assay and direct radical-scavenging activity
    • Kraus, R.L.; Pasieczny, R.; Lariosa-Willingham, K.; Turner, M.S.; Jiang, A.; Trauger, J.W. Antioxidant properties of minocycline: neuroprotection in an oxidative stress assay and direct radical-scavenging activity. J. Neurochem. 2005, 94, 819-827.
    • (2005) J. Neurochem , vol.94 , pp. 819-827
    • Kraus, R.L.1    Pasieczny, R.2    Lariosa-Willingham, K.3    Turner, M.S.4    Jiang, A.5    Trauger, J.W.6
  • 222
    • 84871485772 scopus 로고    scopus 로고
    • Nitric Oxide scavenging activity study of ethanolic extracts of Ixora coccinea from two different areas of kolkata
    • Banerjee, S.; Chanda, A.; Ghoshal, A.; Debnath, R.; Chakraborty, S.; Saha, R.; Das, A. Nitric Oxide scavenging activity study of ethanolic extracts of Ixora coccinea from two different areas of kolkata. Asian J. Exp. Biol. Sci. 2011, 2, 595-599.
    • (2011) Asian J. Exp. Biol. Sci , vol.2 , pp. 595-599
    • Banerjee, S.1    Chanda, A.2    Ghoshal, A.3    Debnath, R.4    Chakraborty, S.5    Saha, R.6    Das, A.7
  • 223
    • 0032831961 scopus 로고    scopus 로고
    • Melatonin and its precursors scavenge nitric oxide
    • Noda, Y.; Mori, A.; Liburdy, R.; Packer, L. Melatonin and its precursors scavenge nitric oxide. J. Pineal Res. 1999, 27, 159-163.
    • (1999) J. Pineal Res , vol.27 , pp. 159-163
    • Noda, Y.1    Mori, A.2    Liburdy, R.3    Packer, L.4
  • 225
    • 0022342973 scopus 로고
    • Quantitative determination of the lipid peroxidation product 4-hydroxynonenal by high-performance liquid chromatography
    • Lang, J.; Celotto, C.; Esterbauer, H. Quantitative determination of the lipid peroxidation product 4-hydroxynonenal by high-performance liquid chromatography. Anal. Biochem. 1985, 150, 369-378.
    • (1985) Anal. Biochem , vol.150 , pp. 369-378
    • Lang, J.1    Celotto, C.2    Esterbauer, H.3
  • 226
    • 0027462210 scopus 로고
    • Determination of 4-hydroxynonenal by high-performance liquid chromatography with electrochemical detection
    • Goldring, C.; Casini, A.F.; Maellaro, E.; Del Bello, B.; Comporti, M. Determination of 4-hydroxynonenal by high-performance liquid chromatography with electrochemical detection. Lipids 1993, 8, 141-145.
    • (1993) Lipids , vol.8 , pp. 141-145
    • Goldring, C.1    Casini, A.F.2    Maellaro, E.3    Del Bello, B.4    Comporti, M.5
  • 227
    • 84883210033 scopus 로고    scopus 로고
    • HPLC determination of malondialdehyde as biomarker for oxidative stress: Application in patients with alcohol dependence
    • Fucile, C.; Marini, V.; Zuccoli, M.L.; Leone, S.; Robbiano, L.; Martelli, A.; Mattioli, F. HPLC determination of malondialdehyde as biomarker for oxidative stress: application in patients with alcohol dependence. Clin. Lab. 2013, 59, 837-841.
    • (2013) Clin. Lab , vol.59 , pp. 837-841
    • Fucile, C.1    Marini, V.2    Zuccoli, M.L.3    Leone, S.4    Robbiano, L.5    Martelli, A.6    Mattioli, F.7
  • 229
    • 67849119170 scopus 로고    scopus 로고
    • PAN-811 inhibits oxidative stress-induced cell death of human Alzheimer's disease-derived and age-matched olfactory neuroepithelial cells via suppression of intracellular reactive oxygen species
    • Nelson, V.M.; Dancik, C.M.; Pan, W.; Jiang, Z.G.; Lebowitz, M.S.; Ghanbari, H.A. PAN-811 inhibits oxidative stress-induced cell death of human Alzheimer's disease-derived and age-matched olfactory neuroepithelial cells via suppression of intracellular reactive oxygen species. J. Alzheimers Dis. 2009, 17, 611-619.
    • (2009) J. Alzheimers Dis , vol.17 , pp. 611-619
    • Nelson, V.M.1    Dancik, C.M.2    Pan, W.3    Jiang, Z.G.4    Lebowitz, M.S.5    Ghanbari, H.A.6
  • 231
    • 77951225062 scopus 로고    scopus 로고
    • Quantification of nitrotyrosine in nitrated proteins
    • Yang, H.; Zhang, Y.; Pöschl, U. Quantification of nitrotyrosine in nitrated proteins. Anal. Bioanal. Chem. 2010, 397, 879-886.
    • (2010) Anal. Bioanal. Chem , vol.397 , pp. 879-886
    • Yang, H.1    Zhang, Y.2    Pöschl, U.3
  • 232
    • 66149088854 scopus 로고    scopus 로고
    • 8-hydroxy-2'-deoxyguanosine (8-OHdG): A critical biomarker of oxidative stress and carcinogenesis
    • Valavanidis, A.; Vlachogianni, T.; Fiotakis, C. 8-hydroxy-2'-deoxyguanosine (8-OHdG): A critical biomarker of oxidative stress and carcinogenesis. J. Environ. Sci. Health C 2009, 27, 120-139.
    • (2009) J. Environ. Sci. Health C , vol.27 , pp. 120-139
    • Valavanidis, A.1    Vlachogianni, T.2    Fiotakis, C.3
  • 233
    • 30644474179 scopus 로고    scopus 로고
    • A method to determine RNA and DNA oxidation simultaneously by HPLC-ECD: Greater RNA than DNA oxidation in rat liver after doxorubicin administration
    • Hofer, T.; Seo, A.Y.; Prudencio, M.; Leeuwenburgh, C. A method to determine RNA and DNA oxidation simultaneously by HPLC-ECD: Greater RNA than DNA oxidation in rat liver after doxorubicin administration. Biol. Chem. 2006, 387, 103-111.
    • (2006) Biol. Chem , vol.387 , pp. 103-111
    • Hofer, T.1    Seo, A.Y.2    Prudencio, M.3    Leeuwenburgh, C.4
  • 234
    • 33745853157 scopus 로고    scopus 로고
    • 8-nitroguanine, a product of nitrative DNA damage caused by reactive nitrogen species: Formation, occurrence, and implications in inflammation and carcinogenesis
    • Ohshima, H.; Sawa, T.; Akaike, T. 8-nitroguanine, a product of nitrative DNA damage caused by reactive nitrogen species: formation, occurrence, and implications in inflammation and carcinogenesis. Antioxid. Redox Signal. 2006, 8, 1033-1045.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 1033-1045
    • Ohshima, H.1    Sawa, T.2    Akaike, T.3
  • 235
    • 31644447230 scopus 로고    scopus 로고
    • Analysis of urinary 8-nitroguanine, a marker of nitrative nucleic acid damage, by high-performance liquid chromatography-electrochemical detection coupled with immunoaffinity purification: Association with cigarette smoking
    • Sawa, T.; Tatemichi, M.; Akaike, T.; Barbin, A.; Ohshima, H. Analysis of urinary 8-nitroguanine, a marker of nitrative nucleic acid damage, by high-performance liquid chromatography-electrochemical detection coupled with immunoaffinity purification: Association with cigarette smoking. Free Radic. Biol. Med. 2006, 40, 711-720.
    • (2006) Free Radic. Biol. Med , vol.40 , pp. 711-720
    • Sawa, T.1    Tatemichi, M.2    Akaike, T.3    Barbin, A.4    Ohshima, H.5
  • 236
    • 0031567576 scopus 로고    scopus 로고
    • What nitrates tyrosine? Is nitrotyrosine specific as a biomarker of peroxynitrite formation in vivo?
    • Halliwell, B. What nitrates tyrosine? Is nitrotyrosine specific as a biomarker of peroxynitrite formation in vivo? FEBS Lett. 1997, 411, 157-160.
    • (1997) FEBS Lett , vol.411 , pp. 157-160
    • Halliwell, B.1
  • 237
    • 10944234930 scopus 로고    scopus 로고
    • Recent methodological advances in the mass spectrometric analysis of free and protein-associated 3-nitrotyrosine in human plasma
    • Tsikas, D.; Caidahl, K. Recent methodological advances in the mass spectrometric analysis of free and protein-associated 3-nitrotyrosine in human plasma. J. Chromatogr. B 2005, 814, 1-9.
    • (2005) J. Chromatogr. B , vol.814 , pp. 1-9
    • Tsikas, D.1    Caidahl, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.