메뉴 건너뛰기




Volumn 9, Issue AUGUST, 2015, Pages

Implications of glial nitric oxide in neurodegenerative diseases

Author keywords

Neurodegenerative disorders; Neuroinflammation; Neuronal death; Neuronal nitric oxide; Nitric oxide

Indexed keywords

BRAIN DERIVED NEUROTROPHIC FACTOR; CYCLIC GMP; CYTOKINE; GLIAL FIBRILLARY ACIDIC PROTEIN; GLUTAMIC ACID; GUANYLATE CYCLASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; MONOCARBOXYLATE TRANSPORTER 1; NEUROTRANSMITTER; NICOTINAMIDE ADENINE DINUCLEOTIDE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; NONSTEROID ANTIINFLAMMATORY AGENT; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PHOSPHODIESTERASE; PRESENILIN 1; PROSTAGLANDIN SYNTHASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; STROMAL CELL DERIVED FACTOR 1; SUPEROXIDE DISMUTASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 84940213599     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2015.00322     Document Type: Review
Times cited : (285)

References (160)
  • 1
    • 0028971936 scopus 로고
    • Induction of nitrotyrosine-like immunoreactivity in the lower motor neuron of amyotrophic lateral sclerosis
    • Abe, K., Pan, L. H., Watanabe, M., Kato, T., and Itoyama, Y. (1995). Induction of nitrotyrosine-like immunoreactivity in the lower motor neuron of amyotrophic lateral sclerosis. Neurosci. Lett. 199, 152-154. doi: 10.1016/0304-3940(95)12039-7
    • (1995) Neurosci. Lett , vol.199 , pp. 152-154
    • Abe, K.1    Pan, L.H.2    Watanabe, M.3    Kato, T.4    Itoyama, Y.5
  • 2
    • 0030888919 scopus 로고    scopus 로고
    • Upregulation of protein-tyrosine nitration in the anterior horn cells of amyotrophic lateral sclerosis
    • Abe, K., Pan, L. H., Watanabe, M., Konno, H., Kato, T., and Itoyama, Y. (1997). Upregulation of protein-tyrosine nitration in the anterior horn cells of amyotrophic lateral sclerosis. Neurol. Res. 19, 124-128.
    • (1997) Neurol. Res , vol.19 , pp. 124-128
    • Abe, K.1    Pan, L.H.2    Watanabe, M.3    Konno, H.4    Kato, T.5    Itoyama, Y.6
  • 3
    • 0242643434 scopus 로고    scopus 로고
    • Relevance of oxidative injury in the pathogenesis of motor neuron diseases
    • Agar, J., and Durham, H. (2003). Relevance of oxidative injury in the pathogenesis of motor neuron diseases. Amyotroph. Lateral Scler. Other Motor Neuron Disord. 4, 232-242. doi: 10.1080/14660820310011278
    • (2003) Amyotroph. Lateral Scler. Other Motor Neuron Disord , vol.4 , pp. 232-242
    • Agar, J.1    Durham, H.2
  • 4
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • Alderton, W. K., Cooper, C. E., and Knowles, R. G. (2001). Nitric oxide synthases: structure, function and inhibition. Biochem. J. 357, 593-615. doi: 10.1042/0264-6021:3570593
    • (2001) Biochem. J , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 5
    • 84880217467 scopus 로고    scopus 로고
    • Association analysis of nitric oxide synthases: NOS1, NOS2A and NOS3 genes, with multiple sclerosis
    • AlFadhli, S., Mohammed, E. M., and Al Shubaili, A. (2013). Association analysis of nitric oxide synthases: NOS1, NOS2A and NOS3 genes, with multiple sclerosis. Ann. Hum. Biol. 40, 368-375. doi: 10.3109/03014460.2013.786756
    • (2013) Ann. Hum. Biol , vol.40 , pp. 368-375
    • AlFadhli, S.1    Mohammed, E.M.2    Al Shubaili, A.3
  • 6
    • 0029592005 scopus 로고
    • Activation of the inducible form of nitric oxide synthase in the brains of patients with multiple sclerosis
    • Bagasra, O., Michaels, F. H., Zheng, Y. M., Bobroski, L. E., Spitsin, S. V., Fu, Z. F., et al. (1995). Activation of the inducible form of nitric oxide synthase in the brains of patients with multiple sclerosis. Proc. Natl. Acad. Sci. U S A 92, 12041-12045. doi: 10.1073/pnas.92.26.12041
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 12041-12045
    • Bagasra, O.1    Michaels, F.H.2    Zheng, Y.M.3    Bobroski, L.E.4    Spitsin, S.V.5    Fu, Z.F.6
  • 7
    • 0034611980 scopus 로고    scopus 로고
    • Neuroinflammation and alzheimer's disease: Critical roles for cytokine/Abeta-induced glial activation, NF-kappaB and apolipoprotein E
    • discussion 451-423
    • Bales, K. R., Du, Y., Holtzman, D., Cordell, B., and Paul, S. M. (2000). Neuroinflammation and alzheimer's disease: critical roles for cytokine/Abeta-induced glial activation, NF-kappaB and apolipoprotein E. Neurobiol. Aging 21, 427-432; discussion 451-423. doi: 10.1016/s0197-4580(00)00143-3
    • (2000) Neurobiol. Aging , vol.21 , pp. 427-432
    • Bales, K.R.1    Du, Y.2    Holtzman, D.3    Cordell, B.4    Paul, S.M.5
  • 8
    • 0027398455 scopus 로고
    • Control of cardiac muscle cell function by an endogenous nitric oxide signaling system
    • Balligand, J. L., Kelly, R. A., Marsden, P. A., Smith, T. W., and Michel, T. (1993). Control of cardiac muscle cell function by an endogenous nitric oxide signaling system. Proc. Natl. Acad. Sci. U S A 90, 347-351. doi: 10.1073/pnas.90.1.347
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 347-351
    • Balligand, J.L.1    Kelly, R.A.2    Marsden, P.A.3    Smith, T.W.4    Michel, T.5
  • 9
    • 0035449358 scopus 로고    scopus 로고
    • Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitotoxicity
    • Bal-Price, A., and Brown, G. C. (2001). Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitotoxicity. J. Neurosci. 21, 6480-6491.
    • (2001) J. Neurosci , vol.21 , pp. 6480-6491
    • Bal-Price, A.1    Brown, G.C.2
  • 10
    • 0037387147 scopus 로고    scopus 로고
    • A cell surface receptor complex for fibrillar beta-amyloid mediates microglial activation
    • Bamberger, M. E., Harris, M. E., McDonald, D. R., Husemann, J., and Landreth, G. E. (2003). A cell surface receptor complex for fibrillar beta-amyloid mediates microglial activation. J. Neurosci. 23, 2665-2674.
    • (2003) J. Neurosci , vol.23 , pp. 2665-2674
    • Bamberger, M.E.1    Harris, M.E.2    McDonald, D.R.3    Husemann, J.4    Landreth, G.E.5
  • 11
  • 12
    • 2542455543 scopus 로고    scopus 로고
    • Evidence of active microglia in substantia nigra pars compacta of parkinsonian monkeys 1 year after MPTP exposure
    • Barcia, C., Sánchez Bahillo, A., Fernández-Villalba, E., Bautista, V., Poza, Y. P. M., Fernández-Barreiro, A., et al. (2004). Evidence of active microglia in substantia nigra pars compacta of parkinsonian monkeys 1 year after MPTP exposure. Glia 46, 402-409. doi: 10.1002/glia.20015
    • (2004) Glia , vol.46 , pp. 402-409
    • Barcia, C.1    Sánchez Bahillo, A.2    Fernández-Villalba, E.3    Bautista, V.4    Poza, Y.P.M.5    Fernández-Barreiro, A.6
  • 13
    • 0031711224 scopus 로고    scopus 로고
    • Excitotoxicity and nitric oxide in parkinson's disease pathogenesis
    • Beal, M. F. (1998). Excitotoxicity and nitric oxide in parkinson's disease pathogenesis. Ann. Neurol. 44, S110-S114. doi: 10.1002/ana.410440716
    • (1998) Ann. Neurol , vol.44 , pp. S110-S114
    • Beal, M.F.1
  • 14
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal, M. F. (2002). Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32, 797-803. doi: 10.1016/s0891-5849(02)00780-3
    • (2002) Free Radic. Biol. Med , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 15
    • 0028584148 scopus 로고
    • Reactions of nitric oxide, superoxide and peroxynitrite with superoxide dismutase in neurodegeneration
    • Beckman, J. S., Chen, J., Crow, J. P., and Ye, Y. Z. (1994). Reactions of nitric oxide, superoxide and peroxynitrite with superoxide dismutase in neurodegeneration. Prog. Brain Res. 103, 371-380. doi: 10.1016/s0079-6123(08)61151-6
    • (1994) Prog. Brain Res , vol.103 , pp. 371-380
    • Beckman, J.S.1    Chen, J.2    Crow, J.P.3    Ye, Y.Z.4
  • 16
    • 0027280338 scopus 로고
    • Pathological implications of nitric oxide, superoxide and peroxynitrite formation
    • Beckman, J. S., and Crow, J. P. (1993). Pathological implications of nitric oxide, superoxide and peroxynitrite formation.Biochem. Soc. Trans. 21, 330-334. doi: 10.1042/bst0210330
    • (1993) Biochem. Soc. Trans , vol.21 , pp. 330-334
    • Beckman, J.S.1    Crow, J.P.2
  • 17
    • 47249160585 scopus 로고    scopus 로고
    • Superoxide dismutase, oxidative stress and ALS
    • eds H. Mitsumoto, S. Perzedborski, and P. H. Gordon (New York: Taylor & Francis Group)
    • Beckman, J. S., and Esteves, A. G. (2006). "Superoxide dismutase, oxidative stress and ALS," in Amyotrophic Lateral Sclerosis, eds H. Mitsumoto, S. Perzedborski, and P. H. Gordon (New York: Taylor & Francis Group), 339-354.
    • (2006) Amyotrophic Lateral Sclerosis , pp. 339-354
    • Beckman, J.S.1    Esteves, A.G.2
  • 18
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar, M., Forrester, M. T., Hess, D. T., and Stamler, J. S. (2008). Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320, 1050-1054. doi: 10.1126/science.1158265
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 19
    • 38949151035 scopus 로고    scopus 로고
    • Nitrated alpha-synuclein immunity accelerates degeneration of nigral dopaminergic neurons
    • Benner, E. J., Banerjee, R., Reynolds, A. D., Sherman, S., Pisarev, V. M., Tsiperson, V., et al. (2008). Nitrated alpha-synuclein immunity accelerates degeneration of nigral dopaminergic neurons. PLoS One 3:e1376. doi: 10.1371/journal.pone.0001376
    • (2008) PLoS One , vol.3
    • Benner, E.J.1    Banerjee, R.2    Reynolds, A.D.3    Sherman, S.4    Pisarev, V.M.5    Tsiperson, V.6
  • 20
    • 0021087536 scopus 로고
    • Monoamine levels and monoamine oxidase activity in different regions of rat brain as a function of age
    • Bhaskaran, D., and Radha, E. (1983). Monoamine levels and monoamine oxidase activity in different regions of rat brain as a function of age. Mech. Ageing Dev. 23, 151-160. doi: 10.1016/0047-6374(83)90064-7
    • (1983) Mech. Ageing Dev , vol.23 , pp. 151-160
    • Bhaskaran, D.1    Radha, E.2
  • 21
    • 0037403787 scopus 로고    scopus 로고
    • Raised nitrate concentration and low SOD activity in the CSF of sporadic ALS patients
    • Boll, M. C., Alcaraz-Zubeldia, M., Montes, S., Murillo-Bonilla, L., and Rios, C. (2003). Raised nitrate concentration and low SOD activity in the CSF of sporadic ALS patients. Neurochem. Res. 28, 699-703. doi: 10.1023/A:1022853531855
    • (2003) Neurochem. Res , vol.28 , pp. 699-703
    • Boll, M.C.1    Alcaraz-Zubeldia, M.2    Montes, S.3    Murillo-Bonilla, L.4    Rios, C.5
  • 22
    • 64849094450 scopus 로고    scopus 로고
    • Transgenic inhibition of astroglial NF-kappa B improves functional outcome in experimental autoimmune encephalomyelitis by suppressing chronic central nervous system inflammation
    • Brambilla, R., Persaud, T., Hu, X., Karmally, S., Shestopalov, V. I., Dvoriantchikova, G., et al. (2009). Transgenic inhibition of astroglial NF-kappa B improves functional outcome in experimental autoimmune encephalomyelitis by suppressing chronic central nervous system inflammation. J. Immunol. 182, 2628-2640. doi: 10.4049/jimmunol.0802954
    • (2009) J. Immunol , vol.182 , pp. 2628-2640
    • Brambilla, R.1    Persaud, T.2    Hu, X.3    Karmally, S.4    Shestopalov, V.I.5    Dvoriantchikova, G.6
  • 23
    • 0025011298 scopus 로고
    • Localization of nitric oxide synthase indicating a neural role for nitric oxide
    • Bredt, D. S., Hwang, P. M., and Snyder, S. H. (1990). Localization of nitric oxide synthase indicating a neural role for nitric oxide. Nature 347, 768-770. doi: 10.1038/347768a0
    • (1990) Nature , vol.347 , pp. 768-770
    • Bredt, D.S.1    Hwang, P.M.2    Snyder, S.H.3
  • 25
    • 36749005178 scopus 로고    scopus 로고
    • Mechanisms of inflammatory neurodegeneration: INOS and NADPH oxidase
    • Brown, G. C. (2007). Mechanisms of inflammatory neurodegeneration: iNOS and NADPH oxidase. Biochem. Soc. Trans. 35, 1119-1121. doi: 10.1042/bst0351119
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 1119-1121
    • Brown, G.C.1
  • 26
    • 0030806228 scopus 로고    scopus 로고
    • Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant
    • Bruijn, L. I., Beal, M. F., Becher, M. W., Schulz, J. B., Wong, P. C., Price, D. L., et al. (1997). Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. Proc. Natl. Acad. Sci. U S A 94, 7606-7611. doi: 10.1073/pnas.94.14.7606
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 7606-7611
    • Bruijn, L.I.1    Beal, M.F.2    Becher, M.W.3    Schulz, J.B.4    Wong, P.C.5    Price, D.L.6
  • 28
    • 33746289543 scopus 로고    scopus 로고
    • A role for CXCL12 (SDF-1alpha) in the pathogenesis of multiple sclerosis: Regulation of CXCL12 expression in astrocytes by soluble myelin basic protein
    • Calderon, T. M., Eugenin, E. A., Lopez, L., Kumar, S. S., Hesselgesser, J., Raine, C. S., et al. (2006). A role for CXCL12 (SDF-1alpha) in the pathogenesis of multiple sclerosis: regulation of CXCL12 expression in astrocytes by soluble myelin basic protein. J. Neuroimmunol. 177, 27-39. doi: 10.1016/j.jneuroim.2006.05.003
    • (2006) J. Neuroimmunol , vol.177 , pp. 27-39
    • Calderon, T.M.1    Eugenin, E.A.2    Lopez, L.3    Kumar, S.S.4    Hesselgesser, J.5    Raine, C.S.6
  • 29
    • 12144271690 scopus 로고    scopus 로고
    • The PSD95-nNOS interface: A target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death
    • Cao, J., Viholainen, J. I., Dart, C., Warwick, H. K., Leyland, M. L., and Courtney, M. J. (2005). The PSD95-nNOS interface: a target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death. J. Cell Biol. 168, 117-126. doi: 10.1083/jcb.200407024
    • (2005) J. Cell Biol , vol.168 , pp. 117-126
    • Cao, J.1    Viholainen, J.I.2    Dart, C.3    Warwick, H.K.4    Leyland, M.L.5    Courtney, M.J.6
  • 30
    • 18144398928 scopus 로고    scopus 로고
    • Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: Possible multifunctional role in the pathogenesis
    • Casoni, F., Basso, M., Massignan, T., Gianazza, E., Cheroni, C., Salmona, M., et al. (2005). Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: possible multifunctional role in the pathogenesis. J. Biol. Chem. 280, 16295-16304. doi: 10.1074/jbc.m413111200
    • (2005) J. Biol. Chem , vol.280 , pp. 16295-16304
    • Casoni, F.1    Basso, M.2    Massignan, T.3    Gianazza, E.4    Cheroni, C.5    Salmona, M.6
  • 31
    • 0036144231 scopus 로고    scopus 로고
    • Peroxynitrite triggers a phenotypic transformation in spinal cord astrocytes that induces motor neuron apoptosis
    • Cassina, P., Peluffo, H., Pehar, M., Martinez-Palma, L., Ressia, A., Beckman, J. S., et al. (2002). Peroxynitrite triggers a phenotypic transformation in spinal cord astrocytes that induces motor neuron apoptosis. J. Neurosci. Res. 67, 21-29. doi: 10.1002/jnr.10107
    • (2002) J. Neurosci. Res , vol.67 , pp. 21-29
    • Cassina, P.1    Peluffo, H.2    Pehar, M.3    Martinez-Palma, L.4    Ressia, A.5    Beckman, J.S.6
  • 32
    • 84875869820 scopus 로고    scopus 로고
    • The effect of intracerebroventricular injection of beta amyloid peptide (1-42) on caspase 3 activity, lipid peroxidation and NOS expression in young adult and aged rat brain
    • Cetin, F., Yazihan, N., Dincer, S., and Akbulut, K. G. (2013). The effect of intracerebroventricular injection of beta amyloid peptide (1-42) on caspase 3 activity, lipid peroxidation and NOS expression in young adult and aged rat brain. Turk. Neurosurg. 23, 144-150. doi: 10.5137/1019-5149.JTN.5855-12.1
    • (2013) Turk. Neurosurg , vol.23 , pp. 144-150
    • Cetin, F.1    Yazihan, N.2    Dincer, S.3    Akbulut, K.G.4
  • 33
    • 0032797262 scopus 로고    scopus 로고
    • Nitric oxide synthases: Targets for therapeutic strategies in neurological diseases
    • Chabrier, P. E., Demerlé-Pallardy, C., and Auguet, M. (1999). Nitric oxide synthases: targets for therapeutic strategies in neurological diseases. Cell. Mol. Life Sci. 55, 1029-1035. doi: 10.1007/s000180050353
    • (1999) Cell. Mol. Life Sci , vol.55 , pp. 1029-1035
    • Chabrier, P.E.1    Demerlé-Pallardy, C.2    Auguet, M.3
  • 34
    • 52549111082 scopus 로고    scopus 로고
    • Chronic NMDA administration increases neuroinflammatory markers in rat frontal cortex: Cross-talk between excitotoxicity and neuroinflammation
    • Chang, Y. C., Kim, H. W., Rapoport, S. I., and Rao, J. S. (2008). Chronic NMDA administration increases neuroinflammatory markers in rat frontal cortex: cross-talk between excitotoxicity and neuroinflammation. Neurochem. Res. 33, 2318-2323. doi: 10.1007/s11064-008-9731-8
    • (2008) Neurochem. Res , vol.33 , pp. 2318-2323
    • Chang, Y.C.1    Kim, H.W.2    Rapoport, S.I.3    Rao, J.S.4
  • 35
    • 77957938071 scopus 로고    scopus 로고
    • NO-releasing NSAIDs suppress NF-kappaB signaling in vitro and in vivo through S-nitrosylation
    • Chattopadhyay, M., Goswami, S., Rodes, D. B., Kodela, R., Velazquez, C. A., Boring, D., et al. (2010). NO-releasing NSAIDs suppress NF-kappaB signaling in vitro and in vivo through S-nitrosylation. Cancer Lett. 298, 204-211. doi: 10.1016/j.canlet.2010.07.006
    • (2010) Cancer Lett , vol.298 , pp. 204-211
    • Chattopadhyay, M.1    Goswami, S.2    Rodes, D.B.3    Kodela, R.4    Velazquez, C.A.5    Boring, D.6
  • 36
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho, D. H., Nakamura, T., Fang, J., Cieplak, P., Godzik, A., Gu, Z., et al. (2009). S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 324, 102-105. doi: 10.1126/science.1171091
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6
  • 37
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung, K. K., Thomas, B., Li, X., Pletnikova, O., Troncoso, J. C., Marsh, L., et al. (2004). S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 304, 1328-1331. doi: 10.1126/science.1093891
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6
  • 38
    • 84860359394 scopus 로고    scopus 로고
    • Stimulation of the neurotrophin receptor TrkB on astrocytes drives nitric oxide production and neurodegeneration
    • Colombo, E., Cordiglieri, C., Melli, G., Newcombe, J., Krumbholz, M., Parada, L. F., et al. (2012). Stimulation of the neurotrophin receptor TrkB on astrocytes drives nitric oxide production and neurodegeneration. J. Exp. Med. 209, 521-535. doi: 10.1084/jem.20110698
    • (2012) J. Exp. Med , vol.209 , pp. 521-535
    • Colombo, E.1    Cordiglieri, C.2    Melli, G.3    Newcombe, J.4    Krumbholz, M.5    Parada, L.F.6
  • 39
    • 33751250771 scopus 로고    scopus 로고
    • Preventing familial ALS: A clinical trial may be feasible but is an efficacy trial warranted?
    • Conwit, R. A. (2006). Preventing familial ALS: a clinical trial may be feasible but is an efficacy trial warranted? J. Neurol. Sci.251, 1-2. doi: 10.1016/j.jns.2006.07.009
    • (2006) J. Neurol. Sci , vol.251 , pp. 1-2
    • Conwit, R.A.1
  • 40
    • 0036391077 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase (SOD1) mutations associated with familial amyotrophic lateral sclerosis (ALS) affect cellular free radical release in the presence of oxidative stress
    • Cookson, M. R., Menzies, F. M., Manning, P., Eggett, C. J., Figlewicz, D. A., McNeil, C. J., et al. (2002). Cu/Zn superoxide dismutase (SOD1) mutations associated with familial amyotrophic lateral sclerosis (ALS) affect cellular free radical release in the presence of oxidative stress. Amyotroph. Lateral Scler. Other Motor Neuron Disord. 3, 75-85. doi: 10.1080/146608202760196048
    • (2002) Amyotroph. Lateral Scler. Other Motor Neuron Disord , vol.3 , pp. 75-85
    • Cookson, M.R.1    Menzies, F.M.2    Manning, P.3    Eggett, C.J.4    Figlewicz, D.A.5    McNeil, C.J.6
  • 41
    • 0032949602 scopus 로고    scopus 로고
    • Oxidative stress and motor neurone disease
    • Cookson, M. R., and Shaw, P. J. (1999). Oxidative stress and motor neurone disease. Brain Pathol. 9, 165-186. doi: 10.1111/j.1750-3639.1999.tb00217.x
    • (1999) Brain Pathol , vol.9 , pp. 165-186
    • Cookson, M.R.1    Shaw, P.J.2
  • 42
    • 70449519412 scopus 로고    scopus 로고
    • Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile parkinson's disease
    • da Costa, C. A., Sunyach, C., Giaime, E., West, A., Corti, O., Brice, A., et al. (2009). Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile parkinson's disease. Nat. Cell Biol. 11, 1370-1375. doi: 10.1038/ncb1981
    • (2009) Nat. Cell Biol , vol.11 , pp. 1370-1375
    • da Costa, C.A.1    Sunyach, C.2    Giaime, E.3    West, A.4    Corti, O.5    Brice, A.6
  • 43
    • 84881532751 scopus 로고    scopus 로고
    • Clinical perspective on oxidative stress in sporadic amyotrophic lateral sclerosis
    • D'Amico, E., Factor-Litvak, P., Santella, R. M., and Mitsumoto, H. (2013). Clinical perspective on oxidative stress in sporadic amyotrophic lateral sclerosis. Free Radic. Biol. Med. 65C, 509-527. doi: 10.1016/j.freeradbiomed.2013.06.029
    • (2013) Free Radic. Biol. Med , vol.65 C , pp. 509-527
    • D'Amico, E.1    Factor-Litvak, P.2    Santella, R.M.3    Mitsumoto, H.4
  • 44
    • 42649144101 scopus 로고    scopus 로고
    • Oxidative and nitrative protein modifications in parkinson's disease
    • Danielson, S. R., and Andersen, J. K. (2008). Oxidative and nitrative protein modifications in parkinson's disease. Free Radic. Biol. Med. 44, 1787-1794. doi: 10.1016/j.freeradbiomed.2008.03.005
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 1787-1794
    • Danielson, S.R.1    Andersen, J.K.2
  • 45
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer, W., and Przedborski, S. (2003). Parkinson's disease: mechanisms and models. Neuron 39, 889-909. doi: 10.1016/S0896-6273(03)00568-3
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 46
    • 19544393559 scopus 로고    scopus 로고
    • Effects of mechanistically distinct NF-kappaB inhibitors on glial inducible nitric-oxide synthase expression
    • Davis, R. L., Sanchez, A. C., Lindley, D. J., Williams, S. C., and Syapin, P. J. (2005). Effects of mechanistically distinct NF-kappaB inhibitors on glial inducible nitric-oxide synthase expression. Nitric Oxide 12, 200-209. doi: 10.1016/j.niox.2005.04.005
    • (2005) Nitric Oxide , vol.12 , pp. 200-209
    • Davis, R.L.1    Sanchez, A.C.2    Lindley, D.J.3    Williams, S.C.4    Syapin, P.J.5
  • 47
    • 76849113421 scopus 로고    scopus 로고
    • Neuroinflammation in alzheimer's disease and major depression
    • Dobos, N., Korf, J., Luiten, P. G., and Eisel, U. L. (2010). Neuroinflammation in alzheimer's disease and major depression. Biol. Psychiatry 67, 503-504. doi: 10.1016/j.biopsych.2010.01.023
    • (2010) Biol. Psychiatry , vol.67 , pp. 503-504
    • Dobos, N.1    Korf, J.2    Luiten, P.G.3    Eisel, U.L.4
  • 49
    • 0033678217 scopus 로고    scopus 로고
    • Widespread nitration of pathological inclusions in neurodegenerative synucleinopathies
    • Duda, J. E., Giasson, B. I., Chen, Q., Gur, T. L., Hurtig, H. I., Stern, M. B., et al. (2000). Widespread nitration of pathological inclusions in neurodegenerative synucleinopathies. Am. J. Pathol. 157, 1439-1445. doi: 10.1016/s0002-9440(10)64781-5
    • (2000) Am. J. Pathol , vol.157 , pp. 1439-1445
    • Duda, J.E.1    Giasson, B.I.2    Chen, Q.3    Gur, T.L.4    Hurtig, H.I.5    Stern, M.B.6
  • 50
    • 13844292636 scopus 로고    scopus 로고
    • Nitric oxide and neurological disorders
    • Duncan, A. J., and Heales, S. J. (2005). Nitric oxide and neurological disorders. Mol. Aspects Med. 26, 67-96. doi: 10.1016/j.mam.2004.09.004
    • (2005) Mol. Aspects Med , vol.26 , pp. 67-96
    • Duncan, A.J.1    Heales, S.J.2
  • 51
    • 0039533148 scopus 로고    scopus 로고
    • Nitric oxide-dependent production of cGMP supports the survival of rat embryonic motor neurons cultured with brain-derived neurotrophic factor
    • Estévez, A. G., Spear, N., Thompson, J. A., Cornwell, T. L., Radi, R., Barbeito, L., et al. (1998). Nitric oxide-dependent production of cGMP supports the survival of rat embryonic motor neurons cultured with brain-derived neurotrophic factor. J. Neurosci. 18, 3708-3714.
    • (1998) J. Neurosci , vol.18 , pp. 3708-3714
    • Estévez, A.G.1    Spear, N.2    Thompson, J.A.3    Cornwell, T.L.4    Radi, R.5    Barbeito, L.6
  • 52
    • 0034682741 scopus 로고    scopus 로고
    • The skeletal muscle calcium release channel: Coupled O2 sensor and NO signaling functions
    • Eu, J. P., Sun, J., Xu, L., Stamler, J. S., and Meissner, G. (2000). The skeletal muscle calcium release channel: coupled O2 sensor and NO signaling functions. Cell 102, 499-509. doi: 10.1016/s0092-8674(00)00054-4
    • (2000) Cell , vol.102 , pp. 499-509
    • Eu, J.P.1    Sun, J.2    Xu, L.3    Stamler, J.S.4    Meissner, G.5
  • 53
    • 76249107349 scopus 로고    scopus 로고
    • The double edge of reactive oxygen species as damaging and signaling molecules in HL60 cell culture
    • Ferrer, M. D., Sureda, A., Mestre, A., Tur, J. A., and Pons, A. (2010). The double edge of reactive oxygen species as damaging and signaling molecules in HL60 cell culture. Cell. Physiol. Biochem. 25, 241-252. doi: 10.1159/000276558
    • (2010) Cell. Physiol. Biochem , vol.25 , pp. 241-252
    • Ferrer, M.D.1    Sureda, A.2    Mestre, A.3    Tur, J.A.4    Pons, A.5
  • 54
    • 72449204160 scopus 로고    scopus 로고
    • Does neuroinflammation fan the flame in neurodegenerative diseases?
    • Frank-Cannon, T. C., Alto, L. T., McAlpine, F. E., and Tansey, M. G. (2009). Does neuroinflammation fan the flame in neurodegenerative diseases? Mol. Neurodegen. 4:47. doi: 10.1186/1750-1326-4-47
    • (2009) Mol. Neurodegen , vol.4 , pp. 47
    • Frank-Cannon, T.C.1    Alto, L.T.2    McAlpine, F.E.3    Tansey, M.G.4
  • 55
    • 77950188666 scopus 로고    scopus 로고
    • Microglial Cx3cr1 knockout prevents neuron loss in a mouse model of alzheimer's disease
    • Fuhrmann, M., Bittner, T., Jung, C. K., Burgold, S., Page, R. M., Mitteregger, G., et al. (2010). Microglial Cx3cr1 knockout prevents neuron loss in a mouse model of alzheimer's disease. Nat. Neurosci. 13, 411-413. doi: 10.1038/nn.2511
    • (2010) Nat. Neurosci , vol.13 , pp. 411-413
    • Fuhrmann, M.1    Bittner, T.2    Jung, C.K.3    Burgold, S.4    Page, R.M.5    Mitteregger, G.6
  • 56
    • 33845628839 scopus 로고    scopus 로고
    • What is immune privilege (not)?
    • Galea, I., Bechmann, I., and Perry, V. H. (2007). What is immune privilege (not)? Trends Immunol. 28, 12-18. doi: 10.1016/j.it.2006.11.004
    • (2007) Trends Immunol , vol.28 , pp. 12-18
    • Galea, I.1    Bechmann, I.2    Perry, V.H.3
  • 57
    • 0033792866 scopus 로고    scopus 로고
    • Overexpression of neutrophil neuronal nitric oxide synthase in parkinson's disease
    • Gatto, E. M., Riobó, N. A., Carreras, M. C., Cherñavsky, A., Rubio, A., Satz, M. L., et al. (2000). Overexpression of neutrophil neuronal nitric oxide synthase in parkinson's disease. Nitric Oxide 4, 534-539. doi: 10.1006/niox.2000.0288
    • (2000) Nitric Oxide , vol.4 , pp. 534-539
    • Gatto, E.M.1    Riobó, N.A.2    Carreras, M.C.3    Cherñavsky, A.4    Rubio, A.5    Satz, M.L.6
  • 58
    • 1842367972 scopus 로고    scopus 로고
    • The application of multifactorial cluster analysis in the staging of plaques in early multiple sclerosis. Identification and characterization of the primary demyelinating lesion
    • Gay, F. W., Drye, T. J., Dick, G. W., and Esiri, M. M. (1997). The application of multifactorial cluster analysis in the staging of plaques in early multiple sclerosis. Identification and characterization of the primary demyelinating lesion. Brain 120(Pt. 8), 1461-1483. doi: 10.1093/brain/120.8.1461
    • (1997) Brain , vol.120 , pp. 1461-1483
    • Gay, F.W.1    Drye, T.J.2    Dick, G.W.3    Esiri, M.M.4
  • 59
    • 0034986361 scopus 로고    scopus 로고
    • Oxidative stress induced-neurodegenerative diseases: The need for antioxidants that penetrate the blood brain barrier
    • Gilgun-Sherki, Y., Melamed, E., and Offen, D. (2001). Oxidative stress induced-neurodegenerative diseases: the need for antioxidants that penetrate the blood brain barrier. Neuropharmacology 40, 959-975. doi: 10.1016/s0028-3908(01)00019-3
    • (2001) Neuropharmacology , vol.40 , pp. 959-975
    • Gilgun-Sherki, Y.1    Melamed, E.2    Offen, D.3
  • 60
    • 84921373282 scopus 로고    scopus 로고
    • Quantitative neuropathology associated with chronic manganese exposure in south african mine workers
    • Gonzalez-Cuyar, L. F., Nelson, G., Criswell, S. R., Ho, P., Lonzanida, J. A., Checkoway, H., et al. (2014). Quantitative neuropathology associated with chronic manganese exposure in south african mine workers. Neurotoxicology 45, 260-266. doi: 10.1016/j.neuro.2013.12.008
    • (2014) Neurotoxicology , vol.45 , pp. 260-266
    • Gonzalez-Cuyar, L.F.1    Nelson, G.2    Criswell, S.R.3    Ho, P.4    Lonzanida, J.A.5    Checkoway, H.6
  • 62
    • 77955085868 scopus 로고    scopus 로고
    • Redox reactions induced by nitrosative stress mediate protein misfolding and mitochondrial dysfunction in neurodegenerative diseases
    • Gu, Z., Nakamura, T., and Lipton, S. A. (2010). Redox reactions induced by nitrosative stress mediate protein misfolding and mitochondrial dysfunction in neurodegenerative diseases. Mol. Neurobiol. 41, 55-72. doi: 10.1007/s12035-010-8113-9
    • (2010) Mol. Neurobiol , vol.41 , pp. 55-72
    • Gu, Z.1    Nakamura, T.2    Lipton, S.A.3
  • 63
    • 24144494527 scopus 로고    scopus 로고
    • The physiology and pathophysiology of nitric oxide in the brain
    • Guix, F. X., Uribesalgo, I., Coma, M., and Muñoz, F. J. (2005). The physiology and pathophysiology of nitric oxide in the brain.Prog. Neurobiol. 76, 126-152. doi: 10.1016/j.pneurobio.2005.06.001
    • (2005) Prog. Neurobiol , vol.76 , pp. 126-152
    • Guix, F.X.1    Uribesalgo, I.2    Coma, M.3    Muñoz, F.J.4
  • 64
    • 84862307062 scopus 로고    scopus 로고
    • Modification of gamma-secretase by nitrosative stress links neuronal ageing to sporadic Alzheimer's disease
    • Guix, F. X., Wahle, T., Vennekens, K., Snellinx, A., Chávez-Gutiérrez, L., Ill-Raga, G., et al. (2012). Modification of gamma-secretase by nitrosative stress links neuronal ageing to sporadic Alzheimer's disease. EMBO Mol. Med. 4, 660-673. doi: 10.1002/emmm.201200243
    • (2012) EMBO Mol. Med , vol.4 , pp. 660-673
    • Guix, F.X.1    Wahle, T.2    Vennekens, K.3    Snellinx, A.4    Chávez-Gutiérrez, L.5    Ill-Raga, G.6
  • 65
    • 2942574528 scopus 로고    scopus 로고
    • NO suppresses while peroxynitrite sustains NF-kappaB: A paradigm to rationalize cytoprotective and cytotoxic actions attributed to NO
    • Hattori, Y., Kasai, K., and Gross, S. S. (2004). NO suppresses while peroxynitrite sustains NF-kappaB: a paradigm to rationalize cytoprotective and cytotoxic actions attributed to NO. Cardiovasc. Res. 63, 31-40. doi: 10.1016/j.cardiores.2004.03.014
    • (2004) Cardiovasc. Res , vol.63 , pp. 31-40
    • Hattori, Y.1    Kasai, K.2    Gross, S.S.3
  • 66
    • 0141767129 scopus 로고    scopus 로고
    • Role of nitric oxide in rotenone-induced nigro-striatal injury
    • He, Y., Imam, S. Z., Dong, Z., Jankovic, J., Ali, S. F., Appel, S. H., et al. (2003). Role of nitric oxide in rotenone-induced nigro-striatal injury. J. Neurochem. 86, 1338-1345. doi: 10.1046/j.1471-4159.2003.01938.x
    • (2003) J. Neurochem , vol.86 , pp. 1338-1345
    • He, Y.1    Imam, S.Z.2    Dong, Z.3    Jankovic, J.4    Ali, S.F.5    Appel, S.H.6
  • 67
    • 0042926482 scopus 로고    scopus 로고
    • Nitration of tau protein is linked to neurodegeneration in tauopathies
    • Horiguchi, T., Uryu, K., Giasson, B. I., Ischiropoulos, H., Lightfoot, R., Bellmann, C., et al. (2003). Nitration of tau protein is linked to neurodegeneration in tauopathies. Am. J. Pathol. 163, 1021-1031. doi: 10.1016/s0002-9440(10)63462-1
    • (2003) Am. J. Pathol , vol.163 , pp. 1021-1031
    • Horiguchi, T.1    Uryu, K.2    Giasson, B.I.3    Ischiropoulos, H.4    Lightfoot, R.5    Bellmann, C.6
  • 68
    • 84856227885 scopus 로고    scopus 로고
    • Phagocytosis of neuronal debris by microglia is associated with neuronal damage in multiple sclerosis
    • Huizinga, R., Van Der Star, B. J., Kipp, M., Jong, R., Gerritsen, W., Clarner, T., et al. (2012). Phagocytosis of neuronal debris by microglia is associated with neuronal damage in multiple sclerosis. Glia 60, 422-431. doi: 10.1002/glia.22276
    • (2012) Glia , vol.60 , pp. 422-431
    • Huizinga, R.1    Van Der Star, B.J.2    Kipp, M.3    Jong, R.4    Gerritsen, W.5    Clarner, T.6
  • 69
    • 0037378023 scopus 로고    scopus 로고
    • Neuroinflammatory processes in parkinson's disease
    • discussion S58-S49
    • Hunot, S., and Hirsch, E. C. (2003). Neuroinflammatory processes in parkinson's disease. Ann. Neurol. 53(Suppl. 3), S49-S58; discussion S58-S60. doi: 10.1002/ana.10481
    • (2003) Ann. Neurol , vol.53 , pp. S58-S60
    • Hunot, S.1    Hirsch, E.C.2
  • 70
    • 0029933293 scopus 로고    scopus 로고
    • Nitric oxide-induced perturbations in a cell culture model of the blood-brain barrier
    • Hurst, R. D., and Fritz, I. B. (1996). Nitric oxide-induced perturbations in a cell culture model of the blood-brain barrier. J. Cell. Physiol. 167, 89-94. doi: 10.1002/(sici)1097-4652(199604)167:1<89::aid-jcp10>3.0.co;2-k
    • (1996) J. Cell. Physiol , vol.167 , pp. 89-94
    • Hurst, R.D.1    Fritz, I.B.2
  • 71
    • 0038155130 scopus 로고    scopus 로고
    • Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins
    • Hyun, D. H., Lee, M., Halliwell, B., and Jenner, P. (2003). Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins. J. Neurochem. 86, 363-373. doi: 10.1046/j.1471-4159.2003.01841.x
    • (2003) J. Neurochem , vol.86 , pp. 363-373
    • Hyun, D.H.1    Lee, M.2    Halliwell, B.3    Jenner, P.4
  • 72
    • 0037237927 scopus 로고    scopus 로고
    • Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?
    • Ischiropoulos, H., and Beckman, J. S. (2003). Oxidative stress and nitration in neurodegeneration: cause, effect, or association?. J. Clin. Invest. 111, 163-169. doi: 10.1172/jci17638
    • (2003) J. Clin. Invest , vol.111 , pp. 163-169
    • Ischiropoulos, H.1    Beckman, J.S.2
  • 73
    • 0027934277 scopus 로고
    • Regulation of blood-brain barrier endothelial cells by nitric oxide
    • Janigro, D., West, G. A., Nguyen, T. S., and Winn, H. R. (1994). Regulation of blood-brain barrier endothelial cells by nitric oxide. Circ. Res. 75, 528-538. doi: 10.1161/01.res.75.3.528
    • (1994) Circ. Res , vol.75 , pp. 528-538
    • Janigro, D.1    West, G.A.2    Nguyen, T.S.3    Winn, H.R.4
  • 74
    • 33749050855 scopus 로고    scopus 로고
    • Fibrillar beta-amyloid peptide Abeta1-40 activates microglial proliferation via stimulating TNF-alpha release and H2O2 derived from NADPH oxidase: A cell culture study
    • Jekabsone, A., Mander, P. K., Tickler, A., Sharpe, M., and Brown, G. C. (2006). Fibrillar beta-amyloid peptide Abeta1-40 activates microglial proliferation via stimulating TNF-alpha release and H2O2 derived from NADPH oxidase: a cell culture study. J. Neuroinflammation 3:24. doi: 10.1186/1742-2094-3-24
    • (2006) J. Neuroinflammation , vol.3 , pp. 24
    • Jekabsone, A.1    Mander, P.K.2    Tickler, A.3    Sharpe, M.4    Brown, G.C.5
  • 75
    • 34548645927 scopus 로고    scopus 로고
    • Nitric oxide from neuronal nitric oxide synthase sensitises neurons to hypoxia-induced death via competitive inhibition of cytochrome oxidase
    • Jekabsone, A., Neher, J. J., Borutaite, V., and Brown, G. C. (2007). Nitric oxide from neuronal nitric oxide synthase sensitises neurons to hypoxia-induced death via competitive inhibition of cytochrome oxidase. J. Neurochem. 103, 346-356. doi: 10.1111/j.1471-4159.2007.04765.x
    • (2007) J. Neurochem , vol.103 , pp. 346-356
    • Jekabsone, A.1    Neher, J.J.2    Borutaite, V.3    Brown, G.C.4
  • 76
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in parkinson's disease
    • discussion S36
    • Jenner, P. (2003). Oxidative stress in parkinson's disease. Ann. Neurol. 53(Suppl. 3), S26-S36; discussion S36-S28. doi: 10.1002/ana.10483
    • (2003) Ann. Neurol , vol.53 , pp. S26-S28
    • Jenner, P.1
  • 77
    • 58149216131 scopus 로고    scopus 로고
    • Inflammatory response in the hippocampus of PS1M146L/APP751SL mouse model of Alzheimer's disease: Age-dependent switch in the microglial phenotype from alternative to classic
    • Jimenez, S., Baglietto-Vargas, D., Caballero, C., Moreno-Gonzalez, I., Torres, M., Sanchez-Varo, R., et al. (2008). Inflammatory response in the hippocampus of PS1M146L/APP751SL mouse model of Alzheimer's disease: age-dependent switch in the microglial phenotype from alternative to classic. J. Neurosci. 28, 11650-11661. doi: 10.1523/jneurosci.3024-08.2008
    • (2008) J. Neurosci , vol.28 , pp. 11650-11661
    • Jimenez, S.1    Baglietto-Vargas, D.2    Caballero, C.3    Moreno-Gonzalez, I.4    Torres, M.5    Sanchez-Varo, R.6
  • 78
    • 0035153513 scopus 로고    scopus 로고
    • Inhibition of nerve growth factor signaling by peroxynitrite
    • Jonnala, R. R., and Buccafusco, J. J. (2001). Inhibition of nerve growth factor signaling by peroxynitrite. J. Neurosci. Res. 63, 27-34. doi: 10.1002/1097-4547(20010101)63:1<27::aid-jnr4>3.3.co;2-r
    • (2001) J. Neurosci. Res , vol.63 , pp. 27-34
    • Jonnala, R.R.1    Buccafusco, J.J.2
  • 80
    • 23844484923 scopus 로고    scopus 로고
    • Molecular targets of nitric-oxide-donating aspirin in cancer
    • Kashfi, K., and Rigas, B. (2005). Molecular targets of nitric-oxide-donating aspirin in cancer. Biochem. Soc. Trans. 33, 701-704. doi: 10.1042/bst0330701
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 701-704
    • Kashfi, K.1    Rigas, B.2
  • 81
    • 33644629020 scopus 로고    scopus 로고
    • Redox system expression in the motor neurons in amyotrophic lateral sclerosis (ALS): Immunohistochemical studies on sporadic ALS, superoxide dismutase 1 (SOD1)-mutated familial ALS and SOD1-mutated ALS animal models
    • Kato, S., Kato, M., Abe, Y., Matsumura, T., Nishino, T., Aoki, M., et al. (2005). Redox system expression in the motor neurons in amyotrophic lateral sclerosis (ALS): immunohistochemical studies on sporadic ALS, superoxide dismutase 1 (SOD1)-mutated familial ALS and SOD1-mutated ALS animal models. Acta Neuropathol. 110, 101-112. doi: 10.1007/s00401-005-1019-3
    • (2005) Acta Neuropathol , vol.110 , pp. 101-112
    • Kato, S.1    Kato, M.2    Abe, Y.3    Matsumura, T.4    Nishino, T.5    Aoki, M.6
  • 82
    • 0034548047 scopus 로고    scopus 로고
    • The peroxynitrite scavenger uric acid prevents inflammatory cell invasion into the central nervous system in experimental allergic encephalomyelitis through maintenance of blood-central nervous system barrier integrity
    • Kean, R. B., Spitsin, S. V., Mikheeva, T., Scott, G. S., and Hooper, D. C. (2000). The peroxynitrite scavenger uric acid prevents inflammatory cell invasion into the central nervous system in experimental allergic encephalomyelitis through maintenance of blood-central nervous system barrier integrity. J. Immunol. 165, 6511-6518. doi: 10.4049/jimmunol.165.11.6511
    • (2000) J. Immunol , vol.165 , pp. 6511-6518
    • Kean, R.B.1    Spitsin, S.V.2    Mikheeva, T.3    Scott, G.S.4    Hooper, D.C.5
  • 83
    • 70449503705 scopus 로고    scopus 로고
    • Chronic NMDA administration to rats increases brain pro-apoptotic factors while decreasing anti-Apoptotic factors and causes cell death
    • Kim, H. W., Chang, Y. C., Chen, M., Rapoport, S. I., and Rao, J. S. (2009). Chronic NMDA administration to rats increases brain pro-apoptotic factors while decreasing anti-Apoptotic factors and causes cell death. BMC Neurosci. 10:123. doi: 10.1186/1471-2202-10-123
    • (2009) BMC Neurosci , vol.10 , pp. 123
    • Kim, H.W.1    Chang, Y.C.2    Chen, M.3    Rapoport, S.I.4    Rao, J.S.5
  • 84
    • 0034520395 scopus 로고    scopus 로고
    • Inflammatory regulators in parkinson's disease: INOS, lipocortin-1 and cyclooxygenases-1 and -2
    • Knott, C., Stern, G., and Wilkin, G. P. (2000). Inflammatory regulators in parkinson's disease: iNOS, lipocortin-1 and cyclooxygenases-1 and -2. Mol. Cell. Neurosci. 16, 724-739. doi: 10.1006/mcne.2000.0914
    • (2000) Mol. Cell. Neurosci , vol.16 , pp. 724-739
    • Knott, C.1    Stern, G.2    Wilkin, G.P.3
  • 85
    • 0028349156 scopus 로고
    • Nitric oxide synthases in mammals
    • Knowles, R. G., and Moncada, S. (1994). Nitric oxide synthases in mammals. Biochem. J. 298(Pt. 2), 249-258.
    • (1994) Biochem. J , vol.298 , pp. 249-258
    • Knowles, R.G.1    Moncada, S.2
  • 86
    • 0028046502 scopus 로고
    • Nitric oxide in skeletal muscle
    • Kobzik, L., Reid, M. B., Bredt, D. S., and Stamler, J. S. (1994). Nitric oxide in skeletal muscle. Nature 372, 546-548. doi: 10.1038/372546a0
    • (1994) Nature , vol.372 , pp. 546-548
    • Kobzik, L.1    Reid, M.B.2    Bredt, D.S.3    Stamler, J.S.4
  • 87
    • 0037066408 scopus 로고    scopus 로고
    • Reduced nicotinamide nucleotides prevent nitration of tyrosine hydroxylase by peroxynitrite
    • Kuhn, D. M., and Geddes, T. J. (2002). Reduced nicotinamide nucleotides prevent nitration of tyrosine hydroxylase by peroxynitrite. Brain Res. 933, 85-89. doi: 10.1016/s0006-8993(02)02307-7
    • (2002) Brain Res , vol.933 , pp. 85-89
    • Kuhn, D.M.1    Geddes, T.J.2
  • 88
    • 80052410564 scopus 로고    scopus 로고
    • Nitration of tyrosine 10 critically enhances amyloid beta aggregation and plaque formation
    • Kummer, M. P., Hermes, M., Delekarte, A., Hammerschmidt, T., Kumar, S., Terwel, D., et al. (2011). Nitration of tyrosine 10 critically enhances amyloid beta aggregation and plaque formation. Neuron 71, 833-844. doi: 10.1016/j.neuron.2011.07.001
    • (2011) Neuron , vol.71 , pp. 833-844
    • Kummer, M.P.1    Hermes, M.2    Delekarte, A.3    Hammerschmidt, T.4    Kumar, S.5    Terwel, D.6
  • 89
    • 78549264026 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease
    • Lambert, J. C., Heath, S., Even, G., Campion, D., Sleegers, K., Hiltunen, M., et al. (2009). Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease. Nat. Genet. 41, 1094-1099. doi: 10.1038/ng.439
    • (2009) Nat. Genet , vol.41 , pp. 1094-1099
    • Lambert, J.C.1    Heath, S.2    Even, G.3    Campion, D.4    Sleegers, K.5    Hiltunen, M.6
  • 90
    • 70449517404 scopus 로고    scopus 로고
    • Neuroinflammation in parkinson's disease
    • Lee, J. K., Tran, T., and Tansey, M. G. (2009). Neuroinflammation in parkinson's disease. J. Neuroimmune Pharmacol. 4, 419-429. doi: 10.1007/s11481-009-9176-0
    • (2009) J. Neuroimmune Pharmacol , vol.4 , pp. 419-429
    • Lee, J.K.1    Tran, T.2    Tansey, M.G.3
  • 91
    • 84863260868 scopus 로고    scopus 로고
    • Gastrodin inhibits neuroinflammation in rotenone-induced parkinson's disease model rats
    • Li, C., Chen, X., Zhang, N., Song, Y., and Mu, Y. (2012). Gastrodin inhibits neuroinflammation in rotenone-induced parkinson's disease model rats. Neural Regen. Res. 7, 325-331. doi: 10.3969/j.issn.1673-5374.2012.05.001
    • (2012) Neural Regen. Res , vol.7 , pp. 325-331
    • Li, C.1    Chen, X.2    Zhang, N.3    Song, Y.4    Mu, Y.5
  • 92
    • 34648843243 scopus 로고    scopus 로고
    • Pathologically activated therapeutics for neuroprotection
    • Lipton, S. A. (2007a). Pathologically activated therapeutics for neuroprotection. Nat. Rev. Neurosci. 8, 803-808. doi: 10.1038/nrn2260
    • (2007) Nat. Rev. Neurosci , vol.8 , pp. 803-808
    • Lipton, S.A.1
  • 93
    • 34249093924 scopus 로고    scopus 로고
    • Pathologically-activated therapeutics for neuroprotection: Mechanism of NMDA receptor block by memantine and S-nitrosylation
    • Lipton, S. A. (2007b). Pathologically-activated therapeutics for neuroprotection: mechanism of NMDA receptor block by memantine and S-nitrosylation. Curr. Drug Targets 8, 621-632. doi: 10.2174/138945007780618472
    • (2007) Curr. Drug Targets , vol.8 , pp. 621-632
    • Lipton, S.A.1
  • 94
    • 0027194540 scopus 로고
    • A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds
    • Lipton, S. A., Choi, Y. B., Pan, Z. H., Lei, S. Z., Chen, H. S., Sucher, N. J., et al. (1993). A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds. Nature 364, 626-632. doi: 10.1038/364626a0
    • (1993) Nature , vol.364 , pp. 626-632
    • Lipton, S.A.1    Choi, Y.B.2    Pan, Z.H.3    Lei, S.Z.4    Chen, H.S.5    Sucher, N.J.6
  • 95
    • 0034965383 scopus 로고    scopus 로고
    • Expression of inducible nitric oxide synthase and nitrotyrosine in multiple sclerosis lesions
    • Liu, J. S., Zhao, M. L., Brosnan, C. F., and Lee, S. C. (2001). Expression of inducible nitric oxide synthase and nitrotyrosine in multiple sclerosis lesions. Am. J. Pathol. 158, 2057-2066. doi: 10.1016/s0002-9440(10)64677-9
    • (2001) Am. J. Pathol , vol.158 , pp. 2057-2066
    • Liu, J.S.1    Zhao, M.L.2    Brosnan, C.F.3    Lee, S.C.4
  • 96
    • 0031795877 scopus 로고    scopus 로고
    • Expression of nitric oxide synthase-2 in glia associated with CNS pathology
    • Loihl, A. K., and Murphy, S. (1998). Expression of nitric oxide synthase-2 in glia associated with CNS pathology. Prog. Brain Res. 118, 253-267. doi: 10.1016/s0079-6123(08)63213-6
    • (1998) Prog. Brain Res , vol.118 , pp. 253-267
    • Loihl, A.K.1    Murphy, S.2
  • 97
    • 84875901499 scopus 로고    scopus 로고
    • Roles of vitamin D in amyotrophic lateral sclerosis: Possible genetic and cellular signaling mechanisms
    • Long, K., and Nguyen, L. T. (2013). Roles of vitamin D in amyotrophic lateral sclerosis: possible genetic and cellular signaling mechanisms. Mol. Brain 6:16. doi: 10.1186/1756-6606-6-16
    • (2013) Mol. Brain , vol.6 , pp. 16
    • Long, K.1    Nguyen, L.T.2
  • 98
    • 0034662806 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA and activity of mitochondrial enzymes in chronic active lesions of multiple sclerosis
    • Lu, F., Selak, M., O'connor, J., Croul, S., Lorenzana, C., Butunoi, C., et al. (2000). Oxidative damage to mitochondrial DNA and activity of mitochondrial enzymes in chronic active lesions of multiple sclerosis. J. Neurol. Sci. 177, 95-103. doi: 10.1016/s0022-510x(00)00343-9
    • (2000) J. Neurol. Sci , vol.177 , pp. 95-103
    • Lu, F.1    Selak, M.2    O'connor, J.3    Croul, S.4    Lorenzana, C.5    Butunoi, C.6
  • 99
    • 34248187134 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, free radical generation and cellular stress response in neurodegenerative disorders
    • Mancuso, C., Scapagini, G., Curro, D., Giuffrida Stella, A. M., De Marco, C., Butterfield, D. A., et al. (2007). Mitochondrial dysfunction, free radical generation and cellular stress response in neurodegenerative disorders. Front. Biosci. 12, 1107-1123. doi: 10.2741/2130
    • (2007) Front. Biosci , vol.12 , pp. 1107-1123
    • Mancuso, C.1    Scapagini, G.2    Curro, D.3    Giuffrida Stella, A.M.4    De Marco, C.5    Butterfield, D.A.6
  • 100
    • 0033028795 scopus 로고    scopus 로고
    • VEGF increases permeability of the blood-brain barrier via a nitric oxide synthase/cGMP-dependent pathway
    • Mayhan, W. G. (1999). VEGF increases permeability of the blood-brain barrier via a nitric oxide synthase/cGMP-dependent pathway. Am. J. Physiol. 276, C1148-C1153.
    • (1999) Am. J. Physiol , vol.276 , pp. C1148-C1153
    • Mayhan, W.G.1
  • 101
    • 0023740773 scopus 로고
    • Rate of cell death in parkinsonism indicates active neuropathological process
    • McGeer, P. L., Itagaki, S., Akiyama, H., and McGeer, E. G. (1988). Rate of cell death in parkinsonism indicates active neuropathological process. Ann. Neurol. 24, 574-576. doi: 10.1002/ana.410240415
    • (1988) Ann. Neurol , vol.24 , pp. 574-576
    • McGeer, P.L.1    Itagaki, S.2    Akiyama, H.3    McGeer, E.G.4
  • 102
    • 33847339301 scopus 로고    scopus 로고
    • NSAIDs and alzheimer disease: Epidemiological, animal model and clinical studies
    • McGeer, P. L., and McGeer, E. G. (2007). NSAIDs and alzheimer disease: epidemiological, animal model and clinical studies.Neurobiol. Aging 28, 639-647. doi: 10.1016/j.neurobiolaging.2006.03.013
    • (2007) Neurobiol. Aging , vol.28 , pp. 639-647
    • McGeer, P.L.1    McGeer, E.G.2
  • 103
    • 0242384667 scopus 로고    scopus 로고
    • Presence of reactive microglia in monkey substantia nigra years after 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine administration
    • McGeer, P. L., Schwab, C., Parent, A., and Doudet, D. (2003). Presence of reactive microglia in monkey substantia nigra years after 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine administration. Ann. Neurol. 54, 599-604. doi: 10.1002/ana.10728
    • (2003) Ann. Neurol , vol.54 , pp. 599-604
    • McGeer, P.L.1    Schwab, C.2    Parent, A.3    Doudet, D.4
  • 104
    • 0029968144 scopus 로고    scopus 로고
    • Myocardial contractile response to nitric oxide and cGMP
    • Mohan, P., Brutsaert, D. L., Paulus, W. J., and Sys, S. U. (1996). Myocardial contractile response to nitric oxide and cGMP.Circulation 93, 1223-1229. doi: 10.1161/01.cir.93.6.1223
    • (1996) Circulation , vol.93 , pp. 1223-1229
    • Mohan, P.1    Brutsaert, D.L.2    Paulus, W.J.3    Sys, S.U.4
  • 105
    • 22944434894 scopus 로고    scopus 로고
    • Modulation of prostaglandin biosynthesis by nitric oxide and nitric oxide donors
    • Mollace, V., Muscoli, C., Masini, E., Cuzzocrea, S., and Salvemini, D. (2005). Modulation of prostaglandin biosynthesis by nitric oxide and nitric oxide donors. Pharmacol. Rev. 57, 217-252. doi: 10.1124/pr.57.2.1
    • (2005) Pharmacol. Rev , vol.57 , pp. 217-252
    • Mollace, V.1    Muscoli, C.2    Masini, E.3    Cuzzocrea, S.4    Salvemini, D.5
  • 106
    • 0034607613 scopus 로고    scopus 로고
    • Developmental changes in expression of the three ryanodine receptor mRNAs in the mouse brain
    • Mori, F., Fukaya, M., Abe, H., Wakabayashi, K., and Watanabe, M. (2000). Developmental changes in expression of the three ryanodine receptor mRNAs in the mouse brain. Neurosci. Lett. 285, 57-60. doi: 10.1016/s0304-3940(00)01046-6
    • (2000) Neurosci. Lett , vol.285 , pp. 57-60
    • Mori, F.1    Fukaya, M.2    Abe, H.3    Wakabayashi, K.4    Watanabe, M.5
  • 107
    • 84897954445 scopus 로고    scopus 로고
    • Microglial dysfunction in brain aging and Alzheimer's disease
    • Mosher, K. I., and Wyss-Coray, T. (2014). Microglial dysfunction in brain aging and Alzheimer's disease. Biochem. Pharmacol.88, 594-604. doi: 10.1016/j.bcp.2014.01.008
    • (2014) Biochem. Pharmacol , vol.88 , pp. 594-604
    • Mosher, K.I.1    Wyss-Coray, T.2
  • 108
    • 33845211714 scopus 로고    scopus 로고
    • Neuroinflammation, oxidative stress and the pathogenesis of parkinson's disease
    • Mosley, R. L., Benner, E. J., Kadiu, I., Thomas, M., Boska, M. D., Hasan, K., et al. (2006). Neuroinflammation, oxidative stress and the pathogenesis of parkinson's disease. Clin. Neurosci. Res. 6, 261-281. doi: 10.1016/j.cnr.2006.09.006
    • (2006) Clin. Neurosci. Res , vol.6 , pp. 261-281
    • Mosley, R.L.1    Benner, E.J.2    Kadiu, I.3    Thomas, M.4    Boska, M.D.5    Hasan, K.6
  • 109
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex I due to peroxynitrite: Identification of reactive tyrosines by mass spectrometry
    • Murray, J., Taylor, S. W., Zhang, B., Ghosh, S. S., and Capaldi, R. A. (2003). Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry. J. Biol. Chem. 278, 37223-37230. doi: 10.1074/jbc.m305694200
    • (2003) J. Biol. Chem , vol.278 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3    Ghosh, S.S.4    Capaldi, R.A.5
  • 110
    • 0036888239 scopus 로고    scopus 로고
    • Direct scavenging of nitric oxide and superoxide by green tea
    • Nakagawa, T., and Yokozawa, T. (2002). Direct scavenging of nitric oxide and superoxide by green tea. Food Chem. Toxicol.40, 1745-1750. doi: 10.1016/s0278-6915(02)00169-2
    • (2002) Food Chem. Toxicol , vol.40 , pp. 1745-1750
    • Nakagawa, T.1    Yokozawa, T.2
  • 111
    • 79952860820 scopus 로고    scopus 로고
    • S-nitrosylation of critical protein thiols mediates protein misfolding and mitochondrial dysfunction in neurodegenerative diseases
    • Nakamura, T., and Lipton, S. A. (2011). S-nitrosylation of critical protein thiols mediates protein misfolding and mitochondrial dysfunction in neurodegenerative diseases. Antioxid. Redox Signal. 14, 1479-1492. doi: 10.1089/ars.2010.3570
    • (2011) Antioxid. Redox Signal , vol.14 , pp. 1479-1492
    • Nakamura, T.1    Lipton, S.A.2
  • 112
    • 79953761792 scopus 로고    scopus 로고
    • A reversible form of axon damage in experimental autoimmune encephalomyelitis and multiple sclerosis
    • Nikić, I., Merkler, D., Sorbara, C., Brinkoetter, M., Kreutzfeldt, M., Bareyre, F. M., et al. (2011). A reversible form of axon damage in experimental autoimmune encephalomyelitis and multiple sclerosis. Nat. Med. 17, 495-499. doi: 10.1038/nm.2324
    • (2011) Nat. Med , vol.17 , pp. 495-499
    • Nikić, I.1    Merkler, D.2    Sorbara, C.3    Brinkoetter, M.4    Kreutzfeldt, M.5    Bareyre, F.M.6
  • 114
    • 48349131772 scopus 로고    scopus 로고
    • S-nitrosylation of beta-arrestin regulates beta-adrenergic receptor trafficking
    • Ozawa, K., Whalen, E. J., Nelson, C. D., Mu, Y., Hess, D. T., Lefkowitz, R. J., et al. (2008). S-nitrosylation of beta-arrestin regulates beta-adrenergic receptor trafficking. Mol. Cell 31, 395-405. doi: 10.1016/j.molcel.2008.05.024
    • (2008) Mol. Cell , vol.31 , pp. 395-405
    • Ozawa, K.1    Whalen, E.J.2    Nelson, C.D.3    Mu, Y.4    Hess, D.T.5    Lefkowitz, R.J.6
  • 115
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher, P., Beckman, J. S., and Liaudet, L. (2007). Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 87, 315-424. doi: 10.1152/physrev.00029.2006
    • (2007) Physiol. Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 116
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer, R. M., Ferrige, A. G., and Moncada, S. (1987). Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature 327, 524-526. doi: 10.1038/327524a0
    • (1987) Nature , vol.327 , pp. 524-526
    • Palmer, R.M.1    Ferrige, A.G.2    Moncada, S.3
  • 117
    • 33750361150 scopus 로고    scopus 로고
    • Peroxynitrite transforms nerve growth factor into an apoptotic factor for motor neurons
    • Pehar, M., Vargas, M. R., Robinson, K. M., Cassina, P., England, P., Beckman, J. S., et al. (2006). Peroxynitrite transforms nerve growth factor into an apoptotic factor for motor neurons. Free Radic. Biol. Med. 41, 1632-1644. doi: 10.1016/j.freeradbiomed.2006.08.010
    • (2006) Free Radic. Biol. Med , vol.41 , pp. 1632-1644
    • Pehar, M.1    Vargas, M.R.2    Robinson, K.M.3    Cassina, P.4    England, P.5    Beckman, J.S.6
  • 118
  • 120
    • 3142619404 scopus 로고    scopus 로고
    • Therapeutic doses of L-dopa reverse hypersensitivity of corticostriatal D2-dopamine receptors and glutamatergic overactivity in experimental parkinsonism
    • Picconi, B., Centonze, D., Rossi, S., Bernardi, G., and Calabresi, P. (2004). Therapeutic doses of L-dopa reverse hypersensitivity of corticostriatal D2-dopamine receptors and glutamatergic overactivity in experimental parkinsonism. Brain127, 1661-1669. doi: 10.1093/brain/awh190
    • (2004) Brain , vol.127 , pp. 1661-1669
    • Picconi, B.1    Centonze, D.2    Rossi, S.3    Bernardi, G.4    Calabresi, P.5
  • 121
    • 34548214550 scopus 로고    scopus 로고
    • Chronic NMDA administration to rats up-regulates frontal cortex cytosolic phospholipase A2 and its transcription factor, activator protein-2
    • Rao, J. S., Ertley, R. N., Rapoport, S. I., Bazinet, R. P., and Lee, H. J. (2007). Chronic NMDA administration to rats up-regulates frontal cortex cytosolic phospholipase A2 and its transcription factor, activator protein-2. J. Neurochem. 102, 1918-1927. doi: 10.1111/j.1471-4159.2007.04648.x
    • (2007) J. Neurochem , vol.102 , pp. 1918-1927
    • Rao, J.S.1    Ertley, R.N.2    Rapoport, S.I.3    Bazinet, R.P.4    Lee, H.J.5
  • 122
    • 77950022786 scopus 로고    scopus 로고
    • Increased excitotoxicity and neuroinflammatory markers in postmortem frontal cortex from bipolar disorder patients
    • Rao, J. S., Harry, G. J., Rapoport, S. I., and Kim, H. W. (2010). Increased excitotoxicity and neuroinflammatory markers in postmortem frontal cortex from bipolar disorder patients. Mol. Psychiatry 15, 384-392. doi: 10.1038/mp.2009.47
    • (2010) Mol. Psychiatry , vol.15 , pp. 384-392
    • Rao, J.S.1    Harry, G.J.2    Rapoport, S.I.3    Kim, H.W.4
  • 124
    • 80051692194 scopus 로고    scopus 로고
    • Brain creatine elevation and N-acetylaspartate reduction indicates neuronal dysfunction in the setting of enhanced glial energy metabolism in a macaque model of neuroAIDS
    • Ratai, E. M., Annamalai, L., Burdo, T., Joo, C. G., Bombardier, J. P., Fell, R., et al. (2011). Brain creatine elevation and N-acetylaspartate reduction indicates neuronal dysfunction in the setting of enhanced glial energy metabolism in a macaque model of neuroAIDS. Magn. Reson. Med. 66, 625-634. doi: 10.1002/mrm.22821
    • (2011) Magn. Reson. Med , vol.66 , pp. 625-634
    • Ratai, E.M.1    Annamalai, L.2    Burdo, T.3    Joo, C.G.4    Bombardier, J.P.5    Fell, R.6
  • 125
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
    • Reaume, A. G., Elliott, J. L., Hoffman, E. K., Kowall, N. W., Ferrante, R. J., Siwek, D. F., et al. (1996). Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet. 13, 43-47. doi: 10.1038/ng0596-43
    • (1996) Nat. Genet , vol.13 , pp. 43-47
    • Reaume, A.G.1    Elliott, J.L.2    Hoffman, E.K.3    Kowall, N.W.4    Ferrante, R.J.5    Siwek, D.F.6
  • 126
    • 0031439343 scopus 로고    scopus 로고
    • Nitric oxide donors reversibly block axonal conduction: Demyelinated axons are especially susceptible
    • Redford, E. J., Kapoor, R., and Smith, K. J. (1997). Nitric oxide donors reversibly block axonal conduction: demyelinated axons are especially susceptible. Brain 120, 2149-2157. doi: 10.1093/brain/120.12.2149
    • (1997) Brain , vol.120 , pp. 2149-2157
    • Redford, E.J.1    Kapoor, R.2    Smith, K.J.3
  • 127
    • 33750940057 scopus 로고    scopus 로고
    • Tau nitration occurs at tyrosine 29 in the fibrillar lesions of Alzheimer's disease and other tauopathies
    • Reynolds, M. R., Reyes, J. F., Fu, Y., Bigio, E. H., Guillozet-Bongaarts, A. L., Berry, R. W., et al. (2006). Tau nitration occurs at tyrosine 29 in the fibrillar lesions of Alzheimer's disease and other tauopathies. J. Neurosci. 26, 10636-10645. doi: 10.1523/jneurosci.2143-06.2006
    • (2006) J. Neurosci , vol.26 , pp. 10636-10645
    • Reynolds, M.R.1    Reyes, J.F.2    Fu, Y.3    Bigio, E.H.4    Guillozet-Bongaarts, A.L.5    Berry, R.W.6
  • 128
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein, J. D. (2009). Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann. Neurol. 65, (Suppl. 1), S3-S9. doi: 10.1002/ana.21543
    • (2009) Ann. Neurol , vol.65 , pp. S3-S9
    • Rothstein, J.D.1
  • 129
    • 33745807628 scopus 로고    scopus 로고
    • Regulation of inducible nitric oxide synthase gene in glial cells
    • Saha, R. N., and Pahan, K. (2006). Regulation of inducible nitric oxide synthase gene in glial cells. Antioxid. Redox Signal. 8, 929-947. doi: 10.1089/ars.2006.8.929
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 929-947
    • Saha, R.N.1    Pahan, K.2
  • 130
    • 80053168133 scopus 로고    scopus 로고
    • Hydrogen peroxide differentially modulates cardiac myocyte nitric oxide synthesis
    • Sartoretto, J. L., Kalwa, H., Pluth, M. D., Lippard, S. J., and Michel, T. (2011). Hydrogen peroxide differentially modulates cardiac myocyte nitric oxide synthesis. Proc. Natl. Acad. Sci. U S A 108, 15792-15797. doi: 10.1073/pnas.1111331108
    • (2011) Proc. Natl. Acad. Sci. U S A , vol.108 , pp. 15792-15797
    • Sartoretto, J.L.1    Kalwa, H.2    Pluth, M.D.3    Lippard, S.J.4    Michel, T.5
  • 131
    • 44849143064 scopus 로고    scopus 로고
    • Augmentation of vascular remodeling by uncoupled endothelial nitric oxide synthase in a mouse model of diabetes mellitus
    • Sasaki, N., Yamashita, T., Takaya, T., Shinohara, M., Shiraki, R., Takeda, M., et al. (2008). Augmentation of vascular remodeling by uncoupled endothelial nitric oxide synthase in a mouse model of diabetes mellitus. Arterioscler. Thromb. Vasc. Biol. 28, 1068-1076. doi: 10.1161/atvbaha.107.160754
    • (2008) Arterioscler. Thromb. Vasc. Biol , vol.28 , pp. 1068-1076
    • Sasaki, N.1    Yamashita, T.2    Takaya, T.3    Shinohara, M.4    Shiraki, R.5    Takeda, M.6
  • 132
    • 68249112361 scopus 로고    scopus 로고
    • Distinct neuroinflammatory profile in post-mortem human huntington's disease
    • Silvestroni, A., Faull, R. L., Strand, A. D., and Möller, T. (2009). Distinct neuroinflammatory profile in post-mortem human huntington's disease. Neuroreport 20, 1098-1103. doi: 10.1097/wnr.0b013e32832e34ee
    • (2009) Neuroreport , vol.20 , pp. 1098-1103
    • Silvestroni, A.1    Faull, R.L.2    Strand, A.D.3    Möller, T.4
  • 133
    • 9344248393 scopus 로고    scopus 로고
    • The neurobiology of glia in the context of water and ion homeostasis
    • Simard, M., and Nedergaard, M. (2004). The neurobiology of glia in the context of water and ion homeostasis. Neuroscience129, 877-896. doi: 10.1016/j.neuroscience.2004.09.053
    • (2004) Neuroscience , vol.129 , pp. 877-896
    • Simard, M.1    Nedergaard, M.2
  • 134
    • 11244316895 scopus 로고    scopus 로고
    • Chemical physiology of blood flow regulation by red blood cells: The role of nitric oxide and S-nitrosohemoglobin
    • Singel, D. J., and Stamler, J. S. (2005). Chemical physiology of blood flow regulation by red blood cells: the role of nitric oxide and S-nitrosohemoglobin. Annu. Rev. Physiol. 67, 99-145. doi: 10.1146/annurev.physiol.67.060603.090918
    • (2005) Annu. Rev. Physiol , vol.67 , pp. 99-145
    • Singel, D.J.1    Stamler, J.S.2
  • 135
    • 33746342757 scopus 로고    scopus 로고
    • Involvement of nitric oxide in neurodegeneration: A study on the experimental models of parkinson's disease
    • Singh, S., Das, T., Ravindran, A., Chaturvedi, R. K., Shukla, Y., Agarwal, A. K., et al. (2005). Involvement of nitric oxide in neurodegeneration: a study on the experimental models of parkinson's disease. Redox Rep. 10, 103-109. doi: 10.1179/135100005x38842
    • (2005) Redox Rep , vol.10 , pp. 103-109
    • Singh, S.1    Das, T.2    Ravindran, A.3    Chaturvedi, R.K.4    Shukla, Y.5    Agarwal, A.K.6
  • 136
    • 0013292906 scopus 로고    scopus 로고
    • The role of nitric oxide in multiple sclerosis
    • Smith, K. J., and Lassmann, H. (2002). The role of nitric oxide in multiple sclerosis. Lancet Neurol. 1, 232-241. doi: 10.1016/s1474-4422(02)00102-3
    • (2002) Lancet Neurol , vol.1 , pp. 232-241
    • Smith, K.J.1    Lassmann, H.2
  • 137
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alpha -synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies
    • Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M., and Ischiropoulos, H. (2000). Dityrosine cross-linking promotes formation of stable alpha -synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 275, 18344-18349. doi: 10.1074/jbc.m000206200
    • (2000) J. Biol. Chem , vol.275 , pp. 18344-18349
    • Souza, J.M.1    Giasson, B.I.2    Chen, Q.3    Lee, V.M.4    Ischiropoulos, H.5
  • 138
    • 79957610938 scopus 로고    scopus 로고
    • The outs and the ins of sphingosine-1-phosphate in immunity
    • Spiegel, S., and Milstien, S. (2011). The outs and the ins of sphingosine-1-phosphate in immunity. Nat. Rev. Immunol. 11, 403-415. doi: 10.1038/nri2974
    • (2011) Nat. Rev. Immunol , vol.11 , pp. 403-415
    • Spiegel, S.1    Milstien, S.2
  • 139
    • 0034613447 scopus 로고    scopus 로고
    • Protection of myelin basic protein immunized mice from free-radical mediated inflammatory cell invasion of the central nervous system by the natural peroxynitrite scavenger uric acid
    • Spitsin, S. V., Scott, G. S., Kean, R. B., Mikheeva, T., and Hooper, D. C. (2000). Protection of myelin basic protein immunized mice from free-radical mediated inflammatory cell invasion of the central nervous system by the natural peroxynitrite scavenger uric acid. Neurosci. Lett. 292, 137-141. doi: 10.1016/s0304-3940(00)01446-4
    • (2000) Neurosci. Lett , vol.292 , pp. 137-141
    • Spitsin, S.V.1    Scott, G.S.2    Kean, R.B.3    Mikheeva, T.4    Hooper, D.C.5
  • 140
    • 84868286870 scopus 로고    scopus 로고
    • New insights in the amyloid-beta interaction with mitochondria
    • Spuch, C., Ortolano, S., and Navarro, C. (2012). New insights in the amyloid-beta interaction with mitochondria. J. Aging Res.2012:324968. doi: 10.1155/2012/324968
    • (2012) J. Aging Res , vol.2012
    • Spuch, C.1    Ortolano, S.2    Navarro, C.3
  • 141
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. the prototypic redox-based signaling mechanism
    • Stamler, J. S., Lamas, S., and Fang, F. C. (2001). Nitrosylation. the prototypic redox-based signaling mechanism. Cell 106, 675-683. doi: 10.1016/S0092-8674(01)00495-0
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 142
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: Translocation, regulation and a consensus motif
    • Stamler, J. S., Toone, E. J., Lipton, S. A., and Sucher, N. J. (1997). (S)NO signals: translocation, regulation and a consensus motif. Neuron 18, 691-696. doi: 10.1016/s0896-6273(00)80310-4
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 143
    • 84883072266 scopus 로고    scopus 로고
    • S-Nitrosylation of parkin as a novel regulator of p53-mediated neuronal cell death in sporadic parkinson's disease
    • Sunico, C. R., Nakamura, T., Rockenstein, E., Mante, M., Adame, A., Chan, S. F., et al. (2013). S-Nitrosylation of parkin as a novel regulator of p53-mediated neuronal cell death in sporadic parkinson's disease. Mol. Neurodegener. 8:29. doi: 10.1186/1750-1326-8-29
    • (2013) Mol. Neurodegener , vol.8 , pp. 29
    • Sunico, C.R.1    Nakamura, T.2    Rockenstein, E.3    Mante, M.4    Adame, A.5    Chan, S.F.6
  • 144
    • 80053892506 scopus 로고    scopus 로고
    • Brain aging, Alzheimer's disease and mitochondria
    • Swerdlow, R. H. (2011). Brain aging, Alzheimer's disease and mitochondria. Biochim. Biophys. Acta 1812, 1630-1639. doi: 10.1016/j.bbadis.2011.08.012
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 1630-1639
    • Swerdlow, R.H.1
  • 145
    • 84880823246 scopus 로고    scopus 로고
    • Heme binding induces dimerization and nitration of truncated beta-amyloid peptide Abeta16 under oxidative stress
    • Thiabaud, G., Pizzocaro, S., Garcia-Serres, R., Latour, J. M., Monzani, E., and Casella, L. (2013). Heme binding induces dimerization and nitration of truncated beta-amyloid peptide Abeta16 under oxidative stress. Angew. Chem. Int. Ed. Engl. 52, 8041-8044. doi: 10.1002/anie.201302989
    • (2013) Angew. Chem. Int. Ed. Engl , vol.52 , pp. 8041-8044
    • Thiabaud, G.1    Pizzocaro, S.2    Garcia-Serres, R.3    Latour, J.M.4    Monzani, E.5    Casella, L.6
  • 146
    • 0014170957 scopus 로고
    • The sub-mitochondrial localization of monoamine oxidase in rat liver and brain
    • Tipton, K. F. (1967). The sub-mitochondrial localization of monoamine oxidase in rat liver and brain. Biochim. Biophys. Acta135, 910-920. doi: 10.1016/0005-2736(67)90060-0
    • (1967) Biochim. Biophys. Acta , vol.135 , pp. 910-920
    • Tipton, K.F.1
  • 147
    • 35948985533 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs may protect against parkinson disease
    • Wahner, A. D., Bronstein, J. M., Bordelon, Y. M., and Ritz, B. (2007). Nonsteroidal anti-inflammatory drugs may protect against parkinson disease. Neurology 69, 1836-1842. doi: 10.1212/01.wnl.0000279519.99344.ad
    • (2007) Neurology , vol.69 , pp. 1836-1842
    • Wahner, A.D.1    Bronstein, J.M.2    Bordelon, Y.M.3    Ritz, B.4
  • 148
    • 0037147758 scopus 로고    scopus 로고
    • Dopamine D2 receptors are present in prefrontal cortical afferents and their targets in patches of the rat caudate-putamen nucleus
    • Wang, H., and Pickel, V. M. (2002). Dopamine D2 receptors are present in prefrontal cortical afferents and their targets in patches of the rat caudate-putamen nucleus. J. Comp. Neurol. 442, 392-404. doi: 10.1002/cne.10086
    • (2002) J. Comp. Neurol , vol.442 , pp. 392-404
    • Wang, H.1    Pickel, V.M.2
  • 149
    • 33751192706 scopus 로고    scopus 로고
    • The microglial NADPH oxidase complex as a source of oxidative stress in Alzheimer's disease
    • Wilkinson, B. L., and Landreth, G. E. (2006). The microglial NADPH oxidase complex as a source of oxidative stress in Alzheimer's disease. J. Neuroinflammation 3:30. doi: 10.1186/1742-2094-3-30
    • (2006) J. Neuroinflammation , vol.3 , pp. 30
    • Wilkinson, B.L.1    Landreth, G.E.2
  • 150
    • 34347357758 scopus 로고    scopus 로고
    • Inflammation in parkinson's diseases and other neurodegenerative diseases: Cause and therapeutic implications
    • Wilms, H., Zecca, L., Rosenstiel, P., Sievers, J., Deuschl, G., and Lucius, R. (2007). Inflammation in parkinson's diseases and other neurodegenerative diseases: cause and therapeutic implications. Curr. Pharm. Des. 13, 1925-1928. doi: 10.2174/138161207780858429
    • (2007) Curr. Pharm. Des , vol.13 , pp. 1925-1928
    • Wilms, H.1    Zecca, L.2    Rosenstiel, P.3    Sievers, J.4    Deuschl, G.5    Lucius, R.6
  • 151
    • 0035877050 scopus 로고    scopus 로고
    • Differential expression of nitric oxide synthases in bacterial meningitis: Role of the inducible isoform for blood-brain barrier breakdown
    • Winkler, F., Koedel, U., Kastenbauer, S., and Pfister, H. W. (2001). Differential expression of nitric oxide synthases in bacterial meningitis: role of the inducible isoform for blood-brain barrier breakdown. J. Infect. Dis. 183, 1749-1759. doi: 10.1086/320730
    • (2001) J. Infect. Dis , vol.183 , pp. 1749-1759
    • Winkler, F.1    Koedel, U.2    Kastenbauer, S.3    Pfister, H.W.4
  • 152
    • 69649105401 scopus 로고    scopus 로고
    • Endothelial NOS-deficient mice reveal dual roles for nitric oxide during experimental autoimmune encephalomyelitis
    • Wu, M., and Tsirka, S. E. (2009). Endothelial NOS-deficient mice reveal dual roles for nitric oxide during experimental autoimmune encephalomyelitis. Glia 57, 1204-1215. doi: 10.1002/glia.20842
    • (2009) Glia , vol.57 , pp. 1204-1215
    • Wu, M.1    Tsirka, S.E.2
  • 153
    • 0032475865 scopus 로고    scopus 로고
    • Superoxide generation from endothelial nitric-oxide synthase. A Ca2+/calmodulin-dependent and tetrahydrobiopterin regulatory process
    • Xia, Y., Tsai, A. L., Berka, V., and Zweier, J. L. (1998). Superoxide generation from endothelial nitric-oxide synthase. A Ca2+/calmodulin-dependent and tetrahydrobiopterin regulatory process. J. Biol. Chem. 273, 25804-25808. doi: 10.1074/jbc.273.40.25804
    • (1998) J. Biol. Chem , vol.273 , pp. 25804-25808
    • Xia, Y.1    Tsai, A.L.2    Berka, V.3    Zweier, J.L.4
  • 154
    • 77956678062 scopus 로고    scopus 로고
    • Ginsenoside Rb1 protects PC12 cells against β-amyloid-induced cell injury
    • Xie, X., Wang, H.-T., Li, H.-L., Gao, X.-H., Ding, J., Zhao, H.-H., et al. (2010). Ginsenoside Rb1 protects PC12 cells against β-amyloid-induced cell injury. Mol. Med. Rep. 3, 635-639. doi: 10.3892/mmr_00000308
    • (2010) Mol. Med. Rep , vol.3 , pp. 635-639
    • Xie, X.1    Wang, H.-T.2    Li, H.-L.3    Gao, X.-H.4    Ding, J.5    Zhao, H.-H.6
  • 155
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation
    • Xu, L., Eu, J. P., Meissner, G., and Stamler, J. S. (1998). Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation. Science 279, 234-237. doi: 10.1126/science.279.5348.234
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 156
    • 33847119443 scopus 로고    scopus 로고
    • Investigation of the therapeutic effects of edaravone, a free radical scavenger, on amyotrophic lateral sclerosis (Phase II study)
    • Yoshino, H., and Kimura, A. (2006). Investigation of the therapeutic effects of edaravone, a free radical scavenger, on amyotrophic lateral sclerosis (Phase II study). Amyotroph. Lateral Scler. 7, 241-245. doi: 10.1080/17482960600881870
    • (2006) Amyotroph. Lateral Scler , vol.7 , pp. 241-245
    • Yoshino, H.1    Kimura, A.2
  • 157
    • 47749110631 scopus 로고    scopus 로고
    • Human neuromelanin induces neuroinflammation and neurodegeneration in the rat substantia nigra: Implications for parkinson's disease
    • Zecca, L., Wilms, H., Geick, S., Claasen, J. H., Brandenburg, L. O., Holzknecht, C., et al. (2008). Human neuromelanin induces neuroinflammation and neurodegeneration in the rat substantia nigra: implications for parkinson's disease. Acta Neuropathol.116, 47-55. doi: 10.1007/s00401-008-0361-7
    • (2008) Acta Neuropathol , vol.116 , pp. 47-55
    • Zecca, L.1    Wilms, H.2    Geick, S.3    Claasen, J.H.4    Brandenburg, L.O.5    Holzknecht, C.6
  • 158
    • 28444498107 scopus 로고    scopus 로고
    • Role of nitric oxide in parkinson's disease
    • Zhang, L., Dawson, V. L., and Dawson, T. M. (2006). Role of nitric oxide in parkinson's disease. Pharmacol. Ther. 109, 33-41. doi: 10.1016/j.pharmthera.2005.05.007
    • (2006) Pharmacol. Ther , vol.109 , pp. 33-41
    • Zhang, L.1    Dawson, V.L.2    Dawson, T.M.3
  • 159
    • 84876907931 scopus 로고    scopus 로고
    • Integrated systems approach identifies genetic nodes and networks in late-onset Alzheimer's disease
    • Zhang, B., Gaiteri, C., Bodea, L. G., Wang, Z., McElwee, J., Podtelezhnikov, A. A., et al. (2013). Integrated systems approach identifies genetic nodes and networks in late-onset Alzheimer's disease. Cell 153, 707-720. doi: 10.1016/j.cell.2013.03.030
    • (2013) Cell , vol.153 , pp. 707-720
    • Zhang, B.1    Gaiteri, C.2    Bodea, L.G.3    Wang, Z.4    McElwee, J.5    Podtelezhnikov, A.A.6
  • 160
    • 0028874051 scopus 로고
    • Inhibition of brain macrophage/microglial respiratory chain enzyme activity in experimental autoimmune encephalomyelitis of the lewis rat
    • Zielasek, J., Reichmann, H., Künzig, H., Jung, S., Hartung, H. P., and Toyka, K. V. (1995). Inhibition of brain macrophage/microglial respiratory chain enzyme activity in experimental autoimmune encephalomyelitis of the lewis rat.Neurosci. Lett. 184, 129-132. doi: 10.1016/0304-3940(94)11187-n
    • (1995) Neurosci. Lett , vol.184 , pp. 129-132
    • Zielasek, J.1    Reichmann, H.2    Künzig, H.3    Jung, S.4    Hartung, H.P.5    Toyka, K.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.