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Volumn 96, Issue , 2016, Pages 1-11

Oxidative stress is increased in C. elegans models of Huntington's disease but does not contribute to polyglutamine toxicity phenotypes

Author keywords

aggregation; animal model; C. elegans; genetics; Huntington's disease; oxidative stress; polyglutamine toxicity disorder; reactive oxygen species (ROS); superoxide dismutase

Indexed keywords

ANTIOXIDANT; POLYGLUTAMINE; SUPEROXIDE DISMUTASE; BACTERIAL PROTEIN; CAENORHABDITIS ELEGANS PROTEIN; GLUCOSE; MESSENGER RNA; PEPTIDE; PHOTOPROTEIN; YELLOW FLUORESCENT PROTEIN, BACTERIA;

EID: 84982293243     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2016.08.008     Document Type: Article
Times cited : (37)

References (80)
  • 1
    • 84871892028 scopus 로고    scopus 로고
    • Expanded ataxin-7 cause toxicity by inducing ROS production from NADPH oxidase complexes in a stable inducible Spinocerebellar ataxia type 7 (SCA7) model
    • Ajayi, A., et al. Expanded ataxin-7 cause toxicity by inducing ROS production from NADPH oxidase complexes in a stable inducible Spinocerebellar ataxia type 7 (SCA7) model. BMC Neurosci., 13, 2012, 86.
    • (2012) BMC Neurosci. , vol.13 , pp. 86
    • Ajayi, A.1
  • 2
    • 0033914874 scopus 로고    scopus 로고
    • No evidence for increased oxidative damage to lipids, proteins, or DNA in Huntington's disease
    • Alam, Z.I., et al. No evidence for increased oxidative damage to lipids, proteins, or DNA in Huntington's disease. J. Neurochem. 75 (2000), 840–846.
    • (2000) J. Neurochem. , vol.75 , pp. 840-846
    • Alam, Z.I.1
  • 3
    • 84944398520 scopus 로고    scopus 로고
    • Disruption of immune cell function by mutant huntingtin in Huntington's disease pathogenesis
    • Andre, R., et al. Disruption of immune cell function by mutant huntingtin in Huntington's disease pathogenesis. Curr. Opin. Pharmacol. 26 (2016), 33–38.
    • (2016) Curr. Opin. Pharmacol. , vol.26 , pp. 33-38
    • Andre, R.1
  • 4
    • 0035968856 scopus 로고    scopus 로고
    • Lipoic acid improves survival in transgenic mouse models of Huntington's disease
    • Andreassen, O.A., et al. Lipoic acid improves survival in transgenic mouse models of Huntington's disease. Neuroreport 12 (2001), 3371–3373.
    • (2001) Neuroreport , vol.12 , pp. 3371-3373
    • Andreassen, O.A.1
  • 5
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., et al. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 (2004), 805–810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1
  • 6
    • 84970979556 scopus 로고    scopus 로고
    • SKN-1/Nrf, stress responses, and aging in Caenorhabditis elegans
    • Blackwell, T.K., et al. SKN-1/Nrf, stress responses, and aging in Caenorhabditis elegans. Free Radic. Biol. Med., 2015.
    • (2015) Free Radic. Biol. Med.
    • Blackwell, T.K.1
  • 7
    • 0035668684 scopus 로고    scopus 로고
    • Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease
    • Bogdanov, M.B., et al. Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease. J. Neurochem. 79 (2001), 1246–1249.
    • (2001) J. Neurochem. , vol.79 , pp. 1246-1249
    • Bogdanov, M.B.1
  • 8
    • 84935462298 scopus 로고    scopus 로고
    • The Toxic Effects of Pathogenic Ataxin-3 Variants in a Yeast Cellular Model
    • e0129727
    • Bonanomi, M., et al. The Toxic Effects of Pathogenic Ataxin-3 Variants in a Yeast Cellular Model. PLoS One, 10, 2015, e0129727.
    • (2015) PLoS One , vol.10
    • Bonanomi, M.1
  • 9
    • 33747053662 scopus 로고    scopus 로고
    • Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model
    • Brignull, H.R., et al. Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model. J. Neurosci. 26 (2006), 7597–7606.
    • (2006) J. Neurosci. , vol.26 , pp. 7597-7606
    • Brignull, H.R.1
  • 10
    • 33947675275 scopus 로고    scopus 로고
    • Oxidative damage in Huntington's disease pathogenesis
    • Browne, S.E., Beal, M.F., Oxidative damage in Huntington's disease pathogenesis. Antioxid. Redox Signal. 8 (2006), 2061–2073.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 2061-2073
    • Browne, S.E.1    Beal, M.F.2
  • 11
    • 0030919567 scopus 로고    scopus 로고
    • Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia
    • Browne, S.E., et al. Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia. Ann. Neurol. 41 (1997), 646–653.
    • (1997) Ann. Neurol. , vol.41 , pp. 646-653
    • Browne, S.E.1
  • 12
    • 0032903802 scopus 로고    scopus 로고
    • Oxidative stress in Huntington's disease
    • Browne, S.E., et al. Oxidative stress in Huntington's disease. Brain Pathol. 9 (1999), 147–163.
    • (1999) Brain Pathol. , vol.9 , pp. 147-163
    • Browne, S.E.1
  • 14
    • 0032612322 scopus 로고    scopus 로고
    • Stress-induced activation of the heat-shock response: cell and molecular biology of heat-shock factors
    • Cotto, J.J., Morimoto, R.I., Stress-induced activation of the heat-shock response: cell and molecular biology of heat-shock factors. Biochem. Soc. Symp. 64 (1999), 105–118.
    • (1999) Biochem. Soc. Symp. , vol.64 , pp. 105-118
    • Cotto, J.J.1    Morimoto, R.I.2
  • 15
    • 57749095081 scopus 로고    scopus 로고
    • Against the oxidative damage theory of aging: superoxide dismutases protect against oxidative stress but have little or no effect on life span in Caenorhabditis elegans
    • Doonan, R., et al. Against the oxidative damage theory of aging: superoxide dismutases protect against oxidative stress but have little or no effect on life span in Caenorhabditis elegans. Genes Dev. 22 (2008), 3236–3241.
    • (2008) Genes Dev. , vol.22 , pp. 3236-3241
    • Doonan, R.1
  • 16
    • 85017357011 scopus 로고    scopus 로고
    • Aging causes decreased resistance to multiple stresses and a failure to activate specific stress response pathways
    • Dues, D.J., et al. Aging causes decreased resistance to multiple stresses and a failure to activate specific stress response pathways. Aging (Albany NY) 8 (2016), 777–795.
    • (2016) Aging (Albany NY) , vol.8 , pp. 777-795
    • Dues, D.J.1
  • 17
    • 0033524413 scopus 로고    scopus 로고
    • Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron
    • Faber, P.W., et al. Polyglutamine-mediated dysfunction and apoptotic death of a Caenorhabditis elegans sensory neuron. Proc. Natl. Acad. Sci. U. S. A. 96 (1999), 179–184.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 179-184
    • Faber, P.W.1
  • 18
    • 0030813067 scopus 로고    scopus 로고
    • Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis
    • Ferrante, R.J., et al. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J. Neurochem. 69 (1997), 2064–2074.
    • (1997) J. Neurochem. , vol.69 , pp. 2064-2074
    • Ferrante, R.J.1
  • 19
    • 0034660457 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease
    • Ferrante, R.J., et al. Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease. J. Neurosci. 20 (2000), 4389–4397.
    • (2000) J. Neurosci. , vol.20 , pp. 4389-4397
    • Ferrante, R.J.1
  • 20
    • 0036523110 scopus 로고    scopus 로고
    • Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease
    • Ferrante, R.J., et al. Therapeutic effects of coenzyme Q10 and remacemide in transgenic mouse models of Huntington's disease. J. Neurosci. 22 (2002), 1592–1599.
    • (2002) J. Neurosci. , vol.22 , pp. 1592-1599
    • Ferrante, R.J.1
  • 21
    • 0032574018 scopus 로고    scopus 로고
    • A novel superoxide dismutase gene encoding membrane-bound and extracellular isoforms by alternative splicing in Caenorhabditis elegans
    • Fujii, M., et al. A novel superoxide dismutase gene encoding membrane-bound and extracellular isoforms by alternative splicing in Caenorhabditis elegans. DNA Res. 5 (1998), 25–30.
    • (1998) DNA Res. , vol.5 , pp. 25-30
    • Fujii, M.1
  • 22
    • 0028301464 scopus 로고
    • The copper/zinc superoxide dismutase gene of Caenorhabditis elegans
    • Giglio, A.M., et al. The copper/zinc superoxide dismutase gene of Caenorhabditis elegans. Biochem. Mol. Biol. Int. 33 (1994), 41–44.
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 41-44
    • Giglio, A.M.1
  • 23
    • 0028245933 scopus 로고
    • The manganese superoxide dismutase gene of Caenorhabditis elegans
    • Giglio, M.P., et al. The manganese superoxide dismutase gene of Caenorhabditis elegans. Biochem. Mol. Biol. Int. 33 (1994), 37–40.
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 37-40
    • Giglio, M.P.1
  • 24
    • 45149107487 scopus 로고    scopus 로고
    • Mechanisms of neurodegeneration in Huntington's disease
    • Gil, J.M., Rego, A.C., Mechanisms of neurodegeneration in Huntington's disease. Eur. J. Neurosci. 27 (2008), 2803–2820.
    • (2008) Eur. J. Neurosci. , vol.27 , pp. 2803-2820
    • Gil, J.M.1    Rego, A.C.2
  • 25
    • 84896356369 scopus 로고    scopus 로고
    • The role of oxidative stress in Huntington's disease: are antioxidants good therapeutic candidates?
    • Gil-Mohapel, J., et al. The role of oxidative stress in Huntington's disease: are antioxidants good therapeutic candidates?. Curr. Drug Targets 15 (2014), 454–468.
    • (2014) Curr. Drug Targets , vol.15 , pp. 454-468
    • Gil-Mohapel, J.1
  • 26
    • 78649728763 scopus 로고    scopus 로고
    • The mitochondrial UPR - protecting organelle protein homeostasis
    • Haynes, C.M., Ron, D., The mitochondrial UPR - protecting organelle protein homeostasis. J. Cell Sci. 123 (2010), 3849–3855.
    • (2010) J. Cell Sci. , vol.123 , pp. 3849-3855
    • Haynes, C.M.1    Ron, D.2
  • 27
    • 80053124673 scopus 로고    scopus 로고
    • Taking a “good” look at free radicals in the aging process
    • Hekimi, S., et al. Taking a “good” look at free radicals in the aging process. Trends Cell Biol. 21 (2011), 569–576.
    • (2011) Trends Cell Biol. , vol.21 , pp. 569-576
    • Hekimi, S.1
  • 28
    • 0035846604 scopus 로고    scopus 로고
    • daf-16 integrates developmental and environmental inputs to mediate aging in the nematode Caenorhabditis elegans
    • Henderson, S.T., Johnson, T.E., daf-16 integrates developmental and environmental inputs to mediate aging in the nematode Caenorhabditis elegans. Curr. Biol. 11 (2001), 1975–1980.
    • (2001) Curr. Biol. , vol.11 , pp. 1975-1980
    • Henderson, S.T.1    Johnson, T.E.2
  • 29
    • 33644927838 scopus 로고    scopus 로고
    • Creatine in Huntington disease is safe, tolerable, bioavailable in brain and reduces serum 8OH2’dG
    • Hersch, S.M., et al. Creatine in Huntington disease is safe, tolerable, bioavailable in brain and reduces serum 8OH2’dG. Neurology 66 (2006), 250–252.
    • (2006) Neurology , vol.66 , pp. 250-252
    • Hersch, S.M.1
  • 30
    • 0030667197 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of two manganese superoxide dismutases from Caenorhabditis elegans
    • Hunter, T., et al. Cloning, expression, and characterization of two manganese superoxide dismutases from Caenorhabditis elegans. J. Biol. Chem. 272 (1997), 28652–28659.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28652-28659
    • Hunter, T.1
  • 31
    • 29244480623 scopus 로고    scopus 로고
    • Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS
    • Jensen, L.T., Culotta, V.C., Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS. J. Biol. Chem. 280 (2005), 41373–41379.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41373-41379
    • Jensen, L.T.1    Culotta, V.C.2
  • 32
    • 84896499806 scopus 로고    scopus 로고
    • The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease
    • Jovaisaite, V., et al. The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease. J. Exp. Biol. 217 (2014), 137–143.
    • (2014) J. Exp. Biol. , vol.217 , pp. 137-143
    • Jovaisaite, V.1
  • 33
    • 0042671525 scopus 로고    scopus 로고
    • Polyglutamine-expanded ataxin-1 recruits Cu/Zn-superoxide dismutase into the nucleus of HeLa cells
    • Kim, S.J., et al. Polyglutamine-expanded ataxin-1 recruits Cu/Zn-superoxide dismutase into the nucleus of HeLa cells. Biochem. Biophys. Res. Commun. 307 (2003), 660–665.
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 660-665
    • Kim, S.J.1
  • 34
    • 37749000434 scopus 로고    scopus 로고
    • Oxidative stress parameters in plasma of Huntington's disease patients, asymptomatic Huntington's disease gene carriers and healthy subjects : a cross-sectional study
    • Klepac, N., et al. Oxidative stress parameters in plasma of Huntington's disease patients, asymptomatic Huntington's disease gene carriers and healthy subjects : a cross-sectional study. J. Neurol. 254 (2007), 1676–1683.
    • (2007) J. Neurol. , vol.254 , pp. 1676-1683
    • Klepac, N.1
  • 35
    • 0035127907 scopus 로고    scopus 로고
    • Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo
    • Leavitt, B.R., et al. Wild-type huntingtin reduces the cellular toxicity of mutant huntingtin in vivo. Am. J. Hum. Genet. 68 (2001), 313–324.
    • (2001) Am. J. Hum. Genet. , vol.68 , pp. 313-324
    • Leavitt, B.R.1
  • 36
    • 78650177082 scopus 로고    scopus 로고
    • Inhibition of respiration extends C. elegans life span via reactive oxygen species that increase HIF-1 activity
    • Lee, S.J., et al. Inhibition of respiration extends C. elegans life span via reactive oxygen species that increase HIF-1 activity. Curr. Biol. 20 (2010), 2131–2136.
    • (2010) Curr. Biol. , vol.20 , pp. 2131-2136
    • Lee, S.J.1
  • 37
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini, L., et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87 (1996), 493–506.
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1
  • 38
    • 84889031644 scopus 로고    scopus 로고
    • HDAC4 Reduction: A Novel Therapeutic Strategy to Target Cytoplasmic Huntingtin and Ameliorate Neurodegeneration
    • e1001717
    • Mielcarek, M., et al. HDAC4 Reduction: A Novel Therapeutic Strategy to Target Cytoplasmic Huntingtin and Ameliorate Neurodegeneration. PLoS Biol., 11, 2013, e1001717.
    • (2013) PLoS Biol. , vol.11
    • Mielcarek, M.1
  • 39
    • 36549083344 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration in dentatorubral-pallidoluysian atrophy
    • Miyata, R., et al. Oxidative stress in neurodegeneration in dentatorubral-pallidoluysian atrophy. J. Neurol. Sci. 264 (2008), 133–139.
    • (2008) J. Neurol. Sci. , vol.264 , pp. 133-139
    • Miyata, R.1
  • 40
    • 40549129694 scopus 로고    scopus 로고
    • Glyoxalase-1 prevents mitochondrial protein modification and enhances lifespan in Caenorhabditis elegans
    • Morcos, M., et al. Glyoxalase-1 prevents mitochondrial protein modification and enhances lifespan in Caenorhabditis elegans. Aging Cell 7 (2008), 260–269.
    • (2008) Aging Cell , vol.7 , pp. 260-269
    • Morcos, M.1
  • 41
    • 71949098172 scopus 로고    scopus 로고
    • Signalling pathways in the unfolded protein response: development from yeast to mammals
    • Mori, K., Signalling pathways in the unfolded protein response: development from yeast to mammals. J. Biochem. 146 (2009), 743–750.
    • (2009) J. Biochem. , vol.146 , pp. 743-750
    • Mori, K.1
  • 42
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley, J.F., et al. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 10417–10422.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10417-10422
    • Morley, J.F.1
  • 43
    • 0035818590 scopus 로고    scopus 로고
    • Expanded polyglutamines in Caenorhabditis elegans cause axonal abnormalities and severe dysfunction of PLM mechanosensory neurons without cell death
    • Parker, J.A., et al. Expanded polyglutamines in Caenorhabditis elegans cause axonal abnormalities and severe dysfunction of PLM mechanosensory neurons without cell death. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 13318–13323.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13318-13323
    • Parker, J.A.1
  • 44
    • 69949091182 scopus 로고    scopus 로고
    • Is the oxidative stress theory of aging dead?
    • Perez, V.I., et al. Is the oxidative stress theory of aging dead?. Biochim. Biophys. Acta 1790 (2009), 1005–1014.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1005-1014
    • Perez, V.I.1
  • 45
    • 0342635463 scopus 로고    scopus 로고
    • Striatal oxidative damage parallels the expression of a neurological phenotype in mice transgenic for the mutation of Huntington's disease
    • Perez-Severiano, F., et al. Striatal oxidative damage parallels the expression of a neurological phenotype in mice transgenic for the mutation of Huntington's disease. Brain Res. 862 (2000), 234–237.
    • (2000) Brain Res. , vol.862 , pp. 234-237
    • Perez-Severiano, F.1
  • 46
    • 0033520166 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex
    • Polidori, M.C., et al. Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex. Neurosci. Lett. 272 (1999), 53–56.
    • (1999) Neurosci. Lett. , vol.272 , pp. 53-56
    • Polidori, M.C.1
  • 47
    • 77954310408 scopus 로고    scopus 로고
    • Hypoxia signaling and resistance in C. elegans
    • Powell-Coffman, J.A., Hypoxia signaling and resistance in C. elegans. Trends Endocrinol. Metab. 21 (2010), 435–440.
    • (2010) Trends Endocrinol. Metab. , vol.21 , pp. 435-440
    • Powell-Coffman, J.A.1
  • 48
    • 57649221161 scopus 로고    scopus 로고
    • Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows
    • Pratico, D., Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows. Ann. N. Y. Acad. Sci. 1147 (2008), 70–78.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 70-78
    • Pratico, D.1
  • 49
    • 84929380037 scopus 로고    scopus 로고
    • Distinct Etiological Roles for Myocytes and Motor Neurons in a Mouse Model of Kennedy's Disease/Spinobulbar Muscular Atrophy
    • Ramzan, F., et al. Distinct Etiological Roles for Myocytes and Motor Neurons in a Mouse Model of Kennedy's Disease/Spinobulbar Muscular Atrophy. J. Neurosci. 35 (2015), 6444–6451.
    • (2015) J. Neurosci. , vol.35 , pp. 6444-6451
    • Ramzan, F.1
  • 50
    • 0042243499 scopus 로고    scopus 로고
    • Ascorbate treatment attenuates the Huntington behavioral phenotype in mice
    • Rebec, G.V., et al. Ascorbate treatment attenuates the Huntington behavioral phenotype in mice. Neuroreport 14 (2003), 1263–1265.
    • (2003) Neuroreport , vol.14 , pp. 1263-1265
    • Rebec, G.V.1
  • 51
    • 0034705224 scopus 로고    scopus 로고
    • Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans
    • Satyal, S.H., et al. Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U. S. A. 97 (2000), 5750–5755.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5750-5755
    • Satyal, S.H.1
  • 52
    • 84924362186 scopus 로고    scopus 로고
    • Mitochondrial and cytoplasmic ROS have opposing effects on lifespan
    • e1004972
    • Schaar, C.E., et al. Mitochondrial and cytoplasmic ROS have opposing effects on lifespan. PLoS Genet., 11, 2015, e1004972.
    • (2015) PLoS Genet. , vol.11
    • Schaar, C.E.1
  • 53
    • 10744227174 scopus 로고    scopus 로고
    • Selective striatal neuronal loss in a YAC128 mouse model of Huntington disease
    • Slow, E.J., et al. Selective striatal neuronal loss in a YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 12 (2003), 1555–1567.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1555-1567
    • Slow, E.J.1
  • 54
    • 84975138044 scopus 로고    scopus 로고
    • Overexpression of cystathionine gamma-lyase suppresses detrimental effects of spinocerebellar ataxia type 3
    • Snijder, P.M., et al. Overexpression of cystathionine gamma-lyase suppresses detrimental effects of spinocerebellar ataxia type 3. Mol. Med., 2015.
    • (2015) Mol. Med.
    • Snijder, P.M.1
  • 55
    • 48449091060 scopus 로고    scopus 로고
    • Proteomic and oxidative stress analysis in human brain samples of Huntington disease
    • Sorolla, M.A., et al. Proteomic and oxidative stress analysis in human brain samples of Huntington disease. Free Radic. Biol. Med. 45 (2008), 667–678.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 667-678
    • Sorolla, M.A.1
  • 56
    • 84862248517 scopus 로고    scopus 로고
    • Protein oxidation in Huntington disease
    • Sorolla, M.A., et al. Protein oxidation in Huntington disease. Biofactors 38 (2012), 173–185.
    • (2012) Biofactors , vol.38 , pp. 173-185
    • Sorolla, M.A.1
  • 57
    • 57649171133 scopus 로고    scopus 로고
    • Evidence of oxidant damage in Huntington's disease: translational strategies using antioxidants
    • Stack, E.C., et al. Evidence of oxidant damage in Huntington's disease: translational strategies using antioxidants. Ann. N. Y. Acad. Sci. 1147 (2008), 79–92.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 79-92
    • Stack, E.C.1
  • 58
    • 18144386929 scopus 로고    scopus 로고
    • Tryptophan metabolism and oxidative stress in patients with Huntington's disease
    • Stoy, N., et al. Tryptophan metabolism and oxidative stress in patients with Huntington's disease. J. Neurochem. 93 (2005), 611–623.
    • (2005) J. Neurochem. , vol.93 , pp. 611-623
    • Stoy, N.1
  • 59
    • 0030606605 scopus 로고    scopus 로고
    • Cloning, sequencing and mapping of a manganese superoxide dismutase gene of the nematode Caenorhabditis elegans
    • Suzuki, N., et al. Cloning, sequencing and mapping of a manganese superoxide dismutase gene of the nematode Caenorhabditis elegans. DNA Res. 3 (1996), 171–174.
    • (1996) DNA Res. , vol.3 , pp. 171-174
    • Suzuki, N.1
  • 60
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 72 (1993), 971–983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 61
    • 79952577733 scopus 로고    scopus 로고
    • Protein folding in the cytoplasm and the heat shock response
    • Vabulas, R.M., et al. Protein folding in the cytoplasm and the heat shock response. Cold Spring Harb. Perspect. Biol., 2, 2010, a004390.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2 , pp. a004390
    • Vabulas, R.M.1
  • 62
    • 84982254913 scopus 로고    scopus 로고
    • Levels and location are crucial in determining the effect of ROS on lifespan
    • e1094607
    • Van Raamsdonk, J.M., Levels and location are crucial in determining the effect of ROS on lifespan. WormBook, 4, 2015, e1094607.
    • (2015) WormBook , vol.4
    • Van Raamsdonk, J.M.1
  • 63
    • 61449184625 scopus 로고    scopus 로고
    • Deletion of the mitochondrial superoxide dismutase sod-2 extends lifespan in Caenorhabditis elegans
    • e1000361
    • Van Raamsdonk, J.M., Hekimi, S., Deletion of the mitochondrial superoxide dismutase sod-2 extends lifespan in Caenorhabditis elegans. PLoS Genet., 5, 2009, e1000361.
    • (2009) PLoS Genet. , vol.5
    • Van Raamsdonk, J.M.1    Hekimi, S.2
  • 64
    • 78149343508 scopus 로고    scopus 로고
    • Reactive Oxygen Species and Aging in Caenorhabditis elegans: Causal or Casual Relationship?
    • Van Raamsdonk, J.M., Hekimi, S., Reactive Oxygen Species and Aging in Caenorhabditis elegans: Causal or Casual Relationship?. Antioxid. Redox Signal. 13 (2010), 1911–1953.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1911-1953
    • Van Raamsdonk, J.M.1    Hekimi, S.2
  • 65
    • 84859575436 scopus 로고    scopus 로고
    • Superoxide dismutase is dispensable for normal animal lifespan
    • Van Raamsdonk, J.M., Hekimi, S., Superoxide dismutase is dispensable for normal animal lifespan. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 5785–5790.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 5785-5790
    • Van Raamsdonk, J.M.1    Hekimi, S.2
  • 66
    • 19744380273 scopus 로고    scopus 로고
    • Loss of wild-type huntingtin influences motor dysfunction and survival in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk, J.M., et al. Loss of wild-type huntingtin influences motor dysfunction and survival in the YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 14 (2005), 1379–1392.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1379-1392
    • Van Raamsdonk, J.M.1
  • 67
    • 27744478499 scopus 로고    scopus 로고
    • Ethyl-EPA treatment improves motor dysfunction, but not neurodegeneration in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk, J.M., et al. Ethyl-EPA treatment improves motor dysfunction, but not neurodegeneration in the YAC128 mouse model of Huntington disease. Exp. Neurol. 196 (2005), 266–272.
    • (2005) Exp. Neurol. , vol.196 , pp. 266-272
    • Van Raamsdonk, J.M.1
  • 68
    • 33846576161 scopus 로고    scopus 로고
    • Wild-type huntingtin ameliorates striatal neuronal atrophy but does not prevent other abnormalities in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk, J.M., et al. Wild-type huntingtin ameliorates striatal neuronal atrophy but does not prevent other abnormalities in the YAC128 mouse model of Huntington disease. BMC Neurosci., 7, 2006, 80.
    • (2006) BMC Neurosci. , vol.7 , pp. 80
    • Van Raamsdonk, J.M.1
  • 69
    • 34248531227 scopus 로고    scopus 로고
    • Testicular degeneration in Huntington disease
    • Van Raamsdonk, J.M., et al. Testicular degeneration in Huntington disease. Neurobiol. Dis. 26 (2007), 512–520.
    • (2007) Neurobiol. Dis. , vol.26 , pp. 512-520
    • Van Raamsdonk, J.M.1
  • 70
    • 77955503270 scopus 로고    scopus 로고
    • Decreased energy metabolism extends life span in Caenorhabditis elegans without reducing oxidative damage
    • Van Raamsdonk, J.M., et al. Decreased energy metabolism extends life span in Caenorhabditis elegans without reducing oxidative damage. Genetics 185 (2010), 559–571.
    • (2010) Genetics , vol.185 , pp. 559-571
    • Van Raamsdonk, J.M.1
  • 71
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter, P., Ron, D., The unfolded protein response: from stress pathway to homeostatic regulation. Science 334 (2011), 1081–1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 72
    • 84969780661 scopus 로고    scopus 로고
    • Roles for ROS and hydrogen sulfide in the longevity response to germline loss in Caenorhabditis elegans
    • Wei, Y., Kenyon, C., Roles for ROS and hydrogen sulfide in the longevity response to germline loss in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U. S. A. 113 (2016), E2832–E2841.
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. E2832-E2841
    • Wei, Y.1    Kenyon, C.2
  • 73
    • 65549169003 scopus 로고    scopus 로고
    • SOD-1 deletions in Caenorhabditis elegans alter the localization of intracellular reactive oxygen species and show molecular compensation
    • Yanase, S., et al. SOD-1 deletions in Caenorhabditis elegans alter the localization of intracellular reactive oxygen species and show molecular compensation. J. Gerontol. A Biol. Sci. Med. Sci. 64 (2009), 530–539.
    • (2009) J. Gerontol. A Biol. Sci. Med. Sci. , vol.64 , pp. 530-539
    • Yanase, S.1
  • 74
    • 78650455712 scopus 로고    scopus 로고
    • A mitochondrial superoxide signal triggers increased longevity in Caenorhabditis elegans
    • e1000556
    • Yang, W., Hekimi, S., A mitochondrial superoxide signal triggers increased longevity in Caenorhabditis elegans. PLoS Biol., 8, 2010, e1000556.
    • (2010) PLoS Biol. , vol.8
    • Yang, W.1    Hekimi, S.2
  • 75
    • 37249016870 scopus 로고    scopus 로고
    • A Measurable increase in oxidative damage due to reduction in superoxide detoxification fails to shorten the life span of long-lived mitochondrial mutants of Caenorhabditis elegans
    • Yang, W., et al. A Measurable increase in oxidative damage due to reduction in superoxide detoxification fails to shorten the life span of long-lived mitochondrial mutants of Caenorhabditis elegans. Genetics 177 (2007), 2063–2074.
    • (2007) Genetics , vol.177 , pp. 2063-2074
    • Yang, W.1
  • 76
    • 66049150300 scopus 로고    scopus 로고
    • Decreased antioxidant enzyme activity and increased mitochondrial DNA damage in cellular models of Machado-Joseph disease
    • Yu, Y.C., et al. Decreased antioxidant enzyme activity and increased mitochondrial DNA damage in cellular models of Machado-Joseph disease. J. Neurosci. Res. 87 (2009), 1884–1891.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 1884-1891
    • Yu, Y.C.1
  • 77
    • 33845720388 scopus 로고    scopus 로고
    • Huntingtin inhibits caspase-3 activation
    • Zhang, Y., et al. Huntingtin inhibits caspase-3 activation. EMBO J. 25 (2006), 5896–5906.
    • (2006) EMBO J. , vol.25 , pp. 5896-5906
    • Zhang, Y.1
  • 78
    • 57649155208 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance
    • Zhou, C., et al. Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance. Ann. N. Y. Acad. Sci. 1147 (2008), 93–104.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 93-104
    • Zhou, C.1
  • 79
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H.Y., Orr, H.T., Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23 (2000), 217–247.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 80
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • Zuccato, C., et al. Molecular mechanisms and potential therapeutical targets in Huntington's disease. Physiol. Rev. 90 (2010), 905–981.
    • (2010) Physiol. Rev. , vol.90 , pp. 905-981
    • Zuccato, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.