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Volumn 15, Issue 4, 2011, Pages 701-717

Endogenous neuroprotection in chronic neurodegenerative disorders: With particular regard to the kynurenines

Author keywords

Glutamate excitotoxicity; Huntington's disease; Kynurenic acid; Kynurenine pathway; Neurodegeneration; Neuroprotection; Oxidative stress; Parkinson's disease; Quinolinic acid

Indexed keywords

KYNURENINE;

EID: 79955675748     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2010.01237.x     Document Type: Review
Times cited : (51)

References (256)
  • 2
    • 33645677966 scopus 로고    scopus 로고
    • The prevalence of Parkinson's disease in an area of North Tyneside in the North-East of England
    • Porter B, Macfarlane R, Unwin N, et al The prevalence of Parkinson's disease in an area of North Tyneside in the North-East of England. Neuroepidemiology. 2006; 26: 156-61.
    • (2006) Neuroepidemiology. , vol.26 , pp. 156-161
    • Porter, B.1    Macfarlane, R.2    Unwin, N.3
  • 3
    • 77958150541 scopus 로고    scopus 로고
    • The prevalence of Parkinson's disease in a rural area of North-East England
    • Walker RW, Hand A, Jones C, et al The prevalence of Parkinson's disease in a rural area of North-East England. Parkinsonism Relat Disord. 2010; DOI: .
    • (2010) Parkinsonism Relat Disord
    • Walker, R.W.1    Hand, A.2    Jones, C.3
  • 4
    • 33646480477 scopus 로고    scopus 로고
    • Prevalence of Parkinson's disease in metropolitan and rural Queensland: a general practice survey
    • Peters CM, Gartner CE, Silburn PA, et al Prevalence of Parkinson's disease in metropolitan and rural Queensland: a general practice survey. J Clin Neurosci. 2006; 13: 343-8.
    • (2006) J Clin Neurosci. , vol.13 , pp. 343-348
    • Peters, C.M.1    Gartner, C.E.2    Silburn, P.A.3
  • 5
    • 33745919520 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • de Lau LM, Breteler MM. Epidemiology of Parkinson's disease. Lancet Neurol. 2006; 5: 525-35.
    • (2006) Lancet Neurol. , vol.5 , pp. 525-535
    • de Lau, L.M.1    Breteler, M.M.2
  • 6
    • 72149101615 scopus 로고    scopus 로고
    • Initial clinical manifestations of Parkinson's disease: features and pathophysiological mechanisms
    • Rodriguez-Oroz MC, Jahanshahi M, Krack P, et al. Initial clinical manifestations of Parkinson's disease: features and pathophysiological mechanisms. Lancet Neurol. 2009; 8: 1128-39.
    • (2009) Lancet Neurol. , vol.8 , pp. 1128-1139
    • Rodriguez-Oroz, M.C.1    Jahanshahi, M.2    Krack, P.3
  • 7
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson's disease
    • Braak H, Del Tredici K, Rub U, et al. Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol Aging. 2003; 24: 197-211.
    • (2003) Neurobiol Aging. , vol.24 , pp. 197-211
    • Braak, H.1    Del Tredici, K.2    Rub, U.3
  • 9
    • 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. Cell. 1993; 72: 971-83.
    • (1993) Cell. , vol.72 , pp. 971-983
  • 10
    • 0023232953 scopus 로고
    • Huntington disease in Maryland: clinical aspects of racial variation
    • Folstein SE, Chase GA, Wahl WE, et al. Huntington disease in Maryland: clinical aspects of racial variation. Am J Hum Genet. 1987; 41: 168-79.
    • (1987) Am J Hum Genet. , vol.41 , pp. 168-179
    • Folstein, S.E.1    Chase, G.A.2    Wahl, W.E.3
  • 11
    • 0024598812 scopus 로고
    • Epidemiology of Huntington's disease in Rijeka district, Yugoslavia
    • Sepcic J, Antonelli L, Sepic-Grahovac D, et al Epidemiology of Huntington's disease in Rijeka district, Yugoslavia. Neuroepidemiology. 1989; 8: 105-8.
    • (1989) Neuroepidemiology. , vol.8 , pp. 105-108
    • Sepcic, J.1    Antonelli, L.2    Sepic-Grahovac, D.3
  • 12
    • 85047696356 scopus 로고    scopus 로고
    • Predictive DNA-testing for Huntington's disease and reproductive decision making: a European collaborative study
    • Evers-Kiebooms G, Nys K, Harper P, et al. Predictive DNA-testing for Huntington's disease and reproductive decision making: a European collaborative study. Eur J Hum Genet. 2002; 10: 167-76.
    • (2002) Eur J Hum Genet. , vol.10 , pp. 167-176
    • Evers-Kiebooms, G.1    Nys, K.2    Harper, P.3
  • 13
    • 65649125624 scopus 로고    scopus 로고
    • Epidemiology of Huntington's disease in Slovenia
    • Peterlin B, Kobal J, Teran N, et al. Epidemiology of Huntington's disease in Slovenia. Acta Neurol Scand. 2009; 119: 371-5.
    • (2009) Acta Neurol Scand. , vol.119 , pp. 371-375
    • Peterlin, B.1    Kobal, J.2    Teran, N.3
  • 14
    • 7944224718 scopus 로고    scopus 로고
    • Huntington's disease: pathomechanism and therapeutic perspectives
    • Gardian G, Vecsei L. Huntington's disease: pathomechanism and therapeutic perspectives. J Neural Transm. 2004; 111: 1485-94.
    • (2004) J Neural Transm. , vol.111 , pp. 1485-1494
    • Gardian, G.1    Vecsei, L.2
  • 15
    • 33846225133 scopus 로고    scopus 로고
    • Huntington's disease
    • Walker FO. Huntington's disease. Lancet. 2007; 369: 218-28.
    • (2007) Lancet. , vol.369 , pp. 218-228
    • Walker, F.O.1
  • 16
    • 0023880409 scopus 로고
    • The coexistence of bradykinesia and chorea in Huntington's disease and its implications for theories of basal ganglia control of movement
    • Thompson PD, Berardelli A, Rothwell JC, et al. The coexistence of bradykinesia and chorea in Huntington's disease and its implications for theories of basal ganglia control of movement. Brain. 1988; 111: 223-44.
    • (1988) Brain. , vol.111 , pp. 223-244
    • Thompson, P.D.1    Berardelli, A.2    Rothwell, J.C.3
  • 19
    • 0022343684 scopus 로고
    • Selective sparing of a class of striatal neurons in Huntington's disease
    • Ferrante RJ, Kowall NW, Beal MF, et al. Selective sparing of a class of striatal neurons in Huntington's disease. Science. 1985; 230: 561-3.
    • (1985) Science. , vol.230 , pp. 561-563
    • Ferrante, R.J.1    Kowall, N.W.2    Beal, M.F.3
  • 20
    • 0022978557 scopus 로고
    • Topography of enkephalin, substance P and acetylcholinesterase staining in Huntington's disease striatum
    • Ferrante RJ, Kowall NW, Richardson EP Jr, et al. Topography of enkephalin, substance P and acetylcholinesterase staining in Huntington's disease striatum. Neurosci Lett. 1986; 71: 283-8.
    • (1986) Neurosci Lett. , vol.71 , pp. 283-288
    • Ferrante, R.J.1    Kowall, N.W.2    Richardson Jr, E.P.3
  • 21
    • 0001589776 scopus 로고
    • Differential loss of striatal projection neurons in Huntington disease
    • Reiner A, Albin RL, Anderson KD, et al. Differential loss of striatal projection neurons in Huntington disease. Proc Natl Acad Sci USA. 1988; 85: 5733-7.
    • (1988) Proc Natl Acad Sci USA. , vol.85 , pp. 5733-5737
    • Reiner, A.1    Albin, R.L.2    Anderson, K.D.3
  • 22
    • 34948830669 scopus 로고    scopus 로고
    • Mechanisms of disease: basic-research-driven investigations in humans - the case of hyperkinetic disorders
    • Centonze D, Bernardi G, Koch G. Mechanisms of disease: basic-research-driven investigations in humans - the case of hyperkinetic disorders. Nat Clin Pract Neurol. 2007; 3: 572-80.
    • (2007) Nat Clin Pract Neurol. , vol.3 , pp. 572-580
    • Centonze, D.1    Bernardi, G.2    Koch, G.3
  • 23
    • 34249788738 scopus 로고    scopus 로고
    • Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders
    • Sas K, Robotka H, Toldi J, et al Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. J Neurol Sci. 2007; 257: 221-39.
    • (2007) J Neurol Sci. , vol.257 , pp. 221-239
    • Sas, K.1    Robotka, H.2    Toldi, J.3
  • 24
    • 78649510476 scopus 로고    scopus 로고
    • Dementia, stroke and migraine - some common pathological mechanisms
    • Sas K, Pardutz A, Toldi J, et al. Dementia, stroke and migraine - some common pathological mechanisms. J Neurol Sci. 2010: DOI: .
    • (2010) J Neurol Sci
    • Sas, K.1    Pardutz, A.2    Toldi, J.3
  • 25
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide
    • Beckman JS, Beckman TW, Chen J, et al. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA. 1990; 87: 1620-4.
    • (1990) Proc Natl Acad Sci USA. , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    J, C.3
  • 26
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle JT, Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science. 1993; 262: 689-95.
    • (1993) Science. , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 27
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science. 1998; 281: 1309-12.
    • (1998) Science. , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 28
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Beal MF. Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci. 2000; 23: 298-304.
    • (2000) Trends Neurosci. , vol.23 , pp. 298-304
    • Beal, M.F.1
  • 29
    • 0028793257 scopus 로고
    • Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function
    • Ankarcrona M, Dypbukt JM, Bonfoco E, et al. Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function. Neuron. 1995; 15: 961-73.
    • (1995) Neuron. , vol.15 , pp. 961-973
    • Ankarcrona, M.1    Dypbukt, J.M.2    E, B.3
  • 30
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis
    • Leist M, Single B, Castoldi AF, et al. Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J Exp Med. 1997; 185: 1481-6.
    • (1997) J Exp Med. , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi A.F.et, al.3
  • 31
    • 35848932091 scopus 로고    scopus 로고
    • Mechanisms of impaired mitochondrial energy metabolism in acute and chronic neurodegenerative disorders
    • Soane L, Kahraman S, Kristian T, et al Mechanisms of impaired mitochondrial energy metabolism in acute and chronic neurodegenerative disorders. J Neurosci Res. 2007; 85: 3407-15.
    • (2007) J Neurosci Res. , vol.85 , pp. 3407-3415
    • Soane, L.1    Kahraman, S.2    Kristian, T.3
  • 32
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 1997; 91: 479-89.
    • (1997) Cell. , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    I, B.3
  • 33
    • 77951911493 scopus 로고    scopus 로고
    • Non-caspase proteases: triggers or amplifiers of apoptosis
    • Schrader K, Huai J, Jockel L, et al. Non-caspase proteases: triggers or amplifiers of apoptosis Cell Mol Life Sci. 2010; 67: 1607-18.
    • (2010) Cell Mol Life Sci. , vol.67 , pp. 1607-1618
    • Schrader, K.1    Huai, J.2    L, J.3
  • 34
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston JW, Ballard P, Tetrud JW, et al Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science. 1983; 219: 979-80.
    • (1983) Science. , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3
  • 35
    • 0005444118 scopus 로고
    • Parkinson's disease in a chemist working with 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
    • Langston JW, Ballard PA Jr. Parkinson's disease in a chemist working with 1-methyl-4-phenyl-1, 2, 5, 6-tetrahydropyridine. N Engl J Med. 1983; 309: 310.
    • (1983) N Engl J Med , vol.309 , pp. 310
    • Langston, J.W.1    Ballard Jr, P.A.2
  • 36
    • 0021276089 scopus 로고
    • Metabolism of the neurotoxic tertiary amine, MPTP, by brain monoamine oxidase
    • Chiba K, Trevor A, Castagnoli N Jr. Metabolism of the neurotoxic tertiary amine, MPTP, by brain monoamine oxidase. Biochem Biophys Res Commun. 1984; 120: 574-8.
    • (1984) Biochem Biophys Res Commun. , vol.120 , pp. 574-578
    • Chiba, K.1    Trevor, A.2    Castagnoli Jr, N.3
  • 37
    • 0021263249 scopus 로고
    • 1-Methyl-4-phenylpyridinium ion (MPP+): identification of a metabolite of MPTP, a toxin selective to the substantia nigra
    • Langston JW, Irwin I, Langston EB, et al 1-Methyl-4-phenylpyridinium ion (MPP+): identification of a metabolite of MPTP, a toxin selective to the substantia nigra. Neurosci Lett. 1984; 48: 87-92.
    • (1984) Neurosci Lett. , vol.48 , pp. 87-92
    • Langston, J.W.1    Irwin, I.2    Langston, E.B.3
  • 38
    • 0021810979 scopus 로고
    • Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
    • Nicklas WJ, Vyas I, Heikkila RE. Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1, 2, 5, 6-tetrahydropyridine. Life Sci. 1985; 36: 2503-8.
    • (1985) Life Sci. , vol.36 , pp. 2503-2508
    • Nicklas, W.J.1    Vyas, I.2    Heikkila, R.E.3
  • 39
    • 0023186383 scopus 로고
    • Effects of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and 1-methyl-4-phenylpyridinium ion on activities of the enzymes in the electron transport system in mouse brain
    • Mizuno Y, Sone N, Saitoh T. Effects of 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine and 1-methyl-4-phenylpyridinium ion on activities of the enzymes in the electron transport system in mouse brain. J Neurochem. 1987; 48: 1787-93.
    • (1987) J Neurochem. , vol.48 , pp. 1787-1793
    • Mizuno, Y.1    Sone, N.2    Saitoh, T.3
  • 40
    • 0002149818 scopus 로고
    • Biochemical analyses of respiratory chain enzymes in different brain regions of patients with Parkinson's disease
    • Bad Kissingen; (abstract).
    • Reichmann H, Riederer P. Biochemical analyses of respiratory chain enzymes in different brain regions of patients with Parkinson's disease. BMFT Symposium "Morbus Parkinson und andere Basalganglienerkrankungen". Bad Kissingen; 1989. p. 44 (abstract).
    • (1989) BMFT Symposium "Morbus Parkinson und andere Basalganglienerkrankungen" , pp. 44
    • Reichmann, H.1    Riederer, P.2
  • 41
    • 0024390719 scopus 로고
    • Mitochondrial complex I deficiency in Parkinson's disease
    • Schapira AH, Cooper JM, Dexter D, et al. Mitochondrial complex I deficiency in Parkinson's disease. Lancet. 1989; 1: 1269.
    • (1989) Lancet , vol.1 , pp. 1269
    • Schapira, A.H.1    Cooper, J.M.2    D, D.3
  • 42
    • 68649108355 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis
    • Banerjee R, Starkov AA, Beal MF, et al Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis. Biochim Biophys Acta. 2009; 1792: 651-63.
    • (2009) Biochim Biophys Acta. , vol.1792 , pp. 651-663
    • Banerjee, R.1    Starkov, A.A.2    Beal, M.F.3
  • 43
    • 44549088952 scopus 로고    scopus 로고
    • Parkinson's disease and pesticides: a toxicological perspective
    • Hatcher JM, Pennell KD, Miller GW. Parkinson's disease and pesticides: a toxicological perspective. Trends Pharmacol Sci. 2008; 29: 322-9.
    • (2008) Trends Pharmacol Sci. , vol.29 , pp. 322-329
    • Hatcher, J.M.1    Pennell, K.D.2    Miller, G.W.3
  • 44
    • 11144353557 scopus 로고    scopus 로고
    • The relevance of iron in the pathogenesis of Parkinson's disease
    • Gotz ME, Double K, Gerlach M, et al. The relevance of iron in the pathogenesis of Parkinson's disease. Ann NY Acad Sci. 2004; 1012: 193-208.
    • (2004) Ann NY Acad Sci. , vol.1012 , pp. 193-208
    • Gotz, M.E.1    Double, K.2    M, G.3
  • 45
    • 72849119992 scopus 로고    scopus 로고
    • Iron elevations in the aging Parkinsonian brain: a consequence of impaired iron homeostasis
    • Lee DW, Andersen JK. Iron elevations in the aging Parkinsonian brain: a consequence of impaired iron homeostasis J Neurochem. 2010; 112: 332-9.
    • (2010) J Neurochem. , vol.112 , pp. 332-339
    • Lee, D.W.1    Andersen, J.K.2
  • 46
    • 77953541514 scopus 로고    scopus 로고
    • The transition metals copper and iron in neurodegenerative diseases
    • Rivera-Mancia S, Perez-Neri I, Rios C, et al. The transition metals copper and iron in neurodegenerative diseases. Chem Biol Interact. 2010; 186: 184-99.
    • (2010) Chem Biol Interact. , vol.186 , pp. 184-199
    • Rivera-Mancia, S.1    Perez-Neri, I.2    C, R.3
  • 47
    • 37049004489 scopus 로고    scopus 로고
    • Mitochondria in the aetiology and pathogenesis of Parkinson's disease
    • Schapira AH. Mitochondria in the aetiology and pathogenesis of Parkinson's disease. Lancet Neurol. 2008; 7: 97-109.
    • (2008) Lancet Neurol. , vol.7 , pp. 97-109
    • Schapira, A.H.1
  • 48
    • 51649115600 scopus 로고    scopus 로고
    • Genes associated with Parkinson syndrome
    • Biskup S, Gerlach M, Kupsch A, et al. Genes associated with Parkinson syndrome. J Neurol. 2008; 255: 8-17.
    • (2008) J Neurol. , vol.255 , pp. 8-17
    • Biskup, S.1    Gerlach, M.2    A, K.3
  • 49
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • Devi L, Raghavendran V, Prabhu BM, et al. Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J Biol Chem. 2008; 283: 9089-100.
    • (2008) J Biol Chem. , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3
  • 50
    • 34547676083 scopus 로고    scopus 로고
    • Downregulation of parkin damages antioxidant defenses and enhances proteasome inhibition-induced toxicity in PC12 cells
    • Yang H, Zhou HY, Li B, et al. Downregulation of parkin damages antioxidant defenses and enhances proteasome inhibition-induced toxicity in PC12 cells. J Neuroimmune Pharmacol. 2007; 2: 276-83.
    • (2007) J Neuroimmune Pharmacol. , vol.2 , pp. 276-283
    • Yang, H.1    Zhou, H.Y.2    B, L.3
  • 51
    • 56049091236 scopus 로고    scopus 로고
    • PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
    • Kim Y, Park J, Kim S, et al. PINK1 controls mitochondrial localization of Parkin through direct phosphorylation. Biochem Biophys Res Commun. 2008; 377: 975-80.
    • (2008) Biochem Biophys Res Commun. , vol.377 , pp. 975-980
    • Kim, Y.1    Park, J.2    S, K.3
  • 52
    • 35748935851 scopus 로고    scopus 로고
    • The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1
    • Plun-Favreau H, Klupsch K, Moisoi N, et al. The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1. Nat Cell Biol. 2007; 9: 1243-52.
    • (2007) Nat Cell Biol. , vol.9 , pp. 1243-1252
    • Plun-Favreau, H.1    Klupsch, K.2    N, M.3
  • 53
    • 35548972027 scopus 로고    scopus 로고
    • DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidase
    • Andres-Mateos E, Perier C, Zhang L, et al. DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidase. Proc Natl Acad Sci USA. 2007; 104: 14807-12.
    • (2007) Proc Natl Acad Sci USA. , vol.104 , pp. 14807-14812
    • Andres-Mateos, E.1    Perier, C.2    L, Z.3
  • 54
    • 33845298032 scopus 로고    scopus 로고
    • Localization of LRRK2 to membranous and vesicular structures in mammalian brain
    • Biskup S, Moore DJ, Celsi F, et al. Localization of LRRK2 to membranous and vesicular structures in mammalian brain. Ann Neurol. 2006; 60: 557-69.
    • (2006) Ann Neurol. , vol.60 , pp. 557-569
    • Biskup, S.1    Moore, D.J.2    F, C.3
  • 55
    • 33646358693 scopus 로고    scopus 로고
    • Early-onset familial parkinsonism due to POLG mutations
    • Davidzon G, Greene P, Mancuso M, et al. Early-onset familial parkinsonism due to POLG mutations. Ann Neurol. 2006; 59: 859-62.
    • (2006) Ann Neurol. , vol.59 , pp. 859-862
    • Davidzon, G.1    Greene, P.2    M, M.3
  • 56
    • 0016259560 scopus 로고
    • Biochemical abnormalities in Huntington's chorea brains
    • Stahl WL, Swanson PD. Biochemical abnormalities in Huntington's chorea brains. Neurology. 1974; 24: 813-9.
    • (1974) Neurology. , vol.24 , pp. 813-819
    • Stahl, W.L.1    Swanson, P.D.2
  • 57
    • 0343983913 scopus 로고
    • 3-Nitropropionate, the toxic substance of Indigofera, is a suicide inactivator of succinate dehydrogenase
    • Alston TA, Mela L, Bright HJ. 3-Nitropropionate, the toxic substance of Indigofera, is a suicide inactivator of succinate dehydrogenase. Proc Natl Acad Sci USA. 1977; 74: 3767-71.
    • (1977) Proc Natl Acad Sci USA. , vol.74 , pp. 3767-3771
    • Alston, T.A.1    Mela, L.2    Bright, H.J.3
  • 58
    • 0023376444 scopus 로고
    • Extrapyramidal lesions induced by mildewed sugarcane poisoning, three case reports
    • He FS, Zhang SL, Liu LH, et al. Extrapyramidal lesions induced by mildewed sugarcane poisoning, three case reports. Chinese J Med. 1987; 67: 395-7.
    • (1987) Chinese J Med. , vol.67 , pp. 395-397
    • He, F.S.1    Zhang, S.L.2    Liu L.H.et, al.3
  • 59
    • 0043252906 scopus 로고
    • LXXXIV. Some properties of the dehydrogenating enzymes of bacteria
    • Quastel JH, Wooldridge WR. LXXXIV. Some properties of the dehydrogenating enzymes of bacteria. Biochem J. 1928; 22: 689-702.
    • (1928) Biochem J. , vol.22 , pp. 689-702
    • Quastel, J.H.1    Wooldridge, W.R.2
  • 60
    • 0020465435 scopus 로고
    • Basal ganglia degeneration, myelin alterations, and enzyme inhibition induced in mice by the plant toxin 3-nitropropanoic acid
    • Gould DH, Gustine DL. Basal ganglia degeneration, myelin alterations, and enzyme inhibition induced in mice by the plant toxin 3-nitropropanoic acid. Neuropathol Appl Neurobiol. 1982; 8: 377-93.
    • (1982) Neuropathol Appl Neurobiol. , vol.8 , pp. 377-393
    • Gould, D.H.1    Gustine, D.L.2
  • 61
    • 0027204154 scopus 로고
    • Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate
    • Beal MF, Brouillet E, Jenkins B, et al. Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate. J Neurochem. 1993; 61: 1147-50.
    • (1993) J Neurochem. , vol.61 , pp. 1147-1150
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.3
  • 62
    • 0027433553 scopus 로고
    • Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid
    • Beal MF, Brouillet E, Jenkins BG, et al. Neurochemical and histologic characterization of striatal excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid. J Neurosci. 1993; 13: 4181-92.
    • (1993) J Neurosci. , vol.13 , pp. 4181-4192
    • Beal, M.F.1    Brouillet, E.2    Jenkins, B.G.3
  • 63
    • 40849147435 scopus 로고    scopus 로고
    • N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking
    • Orr AL, Li S, Wang CE, et al. N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking. J Neurosci. 2008; 28: 2783-92.
    • (2008) J Neurosci. , vol.28 , pp. 2783-2792
    • Orr, A.L.1    Li, S.2    Wang, C.E.3
  • 64
    • 0036327065 scopus 로고    scopus 로고
    • Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
    • Panov AV, Gutekunst CA, Leavitt BR, et al. Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines. Nat Neurosci. 2002; 5: 731-6.
    • (2002) Nat Neurosci. , vol.5 , pp. 731-736
    • Panov, A.V.1    Gutekunst, C.A.2    Leavitt, B.R.3
  • 65
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • Cui L, Jeong H, Borovecki F, et al. Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell. 2006; 127: 59-69.
    • (2006) Cell. , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3
  • 66
    • 84948011844 scopus 로고
    • The toxic effect of sodium L-glutamate on the inner layers of the retina
    • Lucas DR, Newhouse JP. The toxic effect of sodium L-glutamate on the inner layers of the retina. AMA Arch Ophthalmol. 1957; 58: 193-201.
    • (1957) AMA Arch Ophthalmol. , vol.58 , pp. 193-201
    • Lucas, D.R.1    Newhouse, J.P.2
  • 67
    • 0014668762 scopus 로고
    • Brain lesions, obesity, and other disturbances in mice treated with monosodium glutamate
    • Olney JW. Brain lesions, obesity, and other disturbances in mice treated with monosodium glutamate. Science. 1969; 164: 719-21.
    • (1969) Science. , vol.164 , pp. 719-721
    • Olney, J.W.1
  • 68
    • 77955570062 scopus 로고    scopus 로고
    • Glutamate receptors, neurotoxicity and neurodegeneration
    • Lau A, Tymianski M. Glutamate receptors, neurotoxicity and neurodegeneration. Pflugers Arch. 2010; 460: 525-42.
    • (2010) Pflugers Arch. , vol.460 , pp. 525-542
    • Lau, A.1    Tymianski, M.2
  • 69
    • 0036241207 scopus 로고    scopus 로고
    • Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
    • Hardingham GE, Fukunaga Y, Bading H. Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways. Nat Neurosci. 2002; 5: 405-14.
    • (2002) Nat Neurosci. , vol.5 , pp. 405-414
    • Hardingham, G.E.1    Fukunaga, Y.2    Bading, H.3
  • 70
    • 0033562610 scopus 로고    scopus 로고
    • The incorporation of NMDA receptors with a distinct subunit composition at nascent hippocampal synapses in vitro
    • Tovar KR, Westbrook GL. The incorporation of NMDA receptors with a distinct subunit composition at nascent hippocampal synapses in vitro. J Neurosci. 1999; 19: 4180-8.
    • (1999) J Neurosci. , vol.19 , pp. 4180-4188
    • Tovar, K.R.1    Westbrook, G.L.2
  • 71
    • 33947331063 scopus 로고    scopus 로고
    • NMDA receptor subunits have differential roles in mediating excitotoxic neuronal death both in vitro and in vivo
    • Liu Y, Wong TP, Aarts M, et al. NMDA receptor subunits have differential roles in mediating excitotoxic neuronal death both in vitro and in vivo. J Neurosci. 2007; 27: 2846-57.
    • (2007) J Neurosci. , vol.27 , pp. 2846-2857
    • Liu, Y.1    Wong, T.P.2    M, A.3
  • 72
    • 0026596597 scopus 로고
    • Signal transduction and pharmacological characteristics of a metabotropic glutamate receptor, mGluR1, in transfected CHO cells
    • Aramori I, Nakanishi S. Signal transduction and pharmacological characteristics of a metabotropic glutamate receptor, mGluR1, in transfected CHO cells. Neuron. 1992; 8: 757-65.
    • (1992) Neuron. , vol.8 , pp. 757-765
    • Aramori, I.1    Nakanishi, S.2
  • 73
    • 0026681594 scopus 로고
    • Molecular characterization of a novel metabotropic glutamate receptor mGluR5 coupled to inositol phosphate/Ca2+ signal transduction
    • Abe T, Sugihara H, Nawa H, et al. Molecular characterization of a novel metabotropic glutamate receptor mGluR5 coupled to inositol phosphate/Ca2+ signal transduction. J Biol Chem. 1992; 267: 13361-8.
    • (1992) J Biol Chem. , vol.267 , pp. 13361-13368
    • Abe, T.1    Sugihara, H.2    H, N.3
  • 74
    • 0027410488 scopus 로고
    • Signal transduction, pharmacological properties, and expression patterns of two rat metabotropic glutamate receptors, mGluR3 and mGluR4
    • Tanabe Y, Nomura A, Masu M, et al. Signal transduction, pharmacological properties, and expression patterns of two rat metabotropic glutamate receptors, mGluR3 and mGluR4. J Neurosci. 1993; 13: 1372-8.
    • (1993) J Neurosci. , vol.13 , pp. 1372-1378
    • Tanabe, Y.1    Nomura, A.2    M, M.3
  • 75
    • 33645899316 scopus 로고    scopus 로고
    • Role of astrocytes in glutamate homeostasis: implications for excitotoxicity
    • Schousboe A, Waagepetersen HS. Role of astrocytes in glutamate homeostasis: implications for excitotoxicity. Neurotox Res. 2005; 8: 221-5.
    • (2005) Neurotox Res. , vol.8 , pp. 221-225
    • Schousboe, A.1    Waagepetersen, H.S.2
  • 76
    • 0023895734 scopus 로고
    • Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced
    • Novelli A, Reilly JA, Lysko PG, et al Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced. Brain Res. 1988; 451: 205-12.
    • (1988) Brain Res. , vol.451 , pp. 205-212
    • Novelli, A.1    Reilly, J.A.2    Lysko, P.G.3
  • 78
    • 68749114987 scopus 로고    scopus 로고
    • Impaired glutamate homeostasis and programmed cell death in a chronic MPTP mouse model of Parkinson's disease
    • Meredith GE, Totterdell S, Beales M, et al Impaired glutamate homeostasis and programmed cell death in a chronic MPTP mouse model of Parkinson's disease. Exp Neurol. 2009; 219: 334-40.
    • (2009) Exp Neurol. , vol.219 , pp. 334-340
    • Meredith, G.E.1    Totterdell, S.2    Beales, M.3
  • 79
    • 71549151931 scopus 로고    scopus 로고
    • Glutamate, excitotoxicity, and programmed cell death in Parkinson disease
    • Caudle WM, Zhang J. Glutamate, excitotoxicity, and programmed cell death in Parkinson disease. Exp Neurol. 2009; 220: 230-3.
    • (2009) Exp Neurol. , vol.220 , pp. 230-233
    • Caudle, W.M.1    Zhang, J.2
  • 80
    • 5444258474 scopus 로고    scopus 로고
    • Innervation of the substantia nigra
    • Misgeld U. Innervation of the substantia nigra. Cell Tissue Res. 2004; 318: 107-14.
    • (2004) Cell Tissue Res. , vol.318 , pp. 107-114
    • Misgeld, U.1
  • 81
    • 0031696407 scopus 로고    scopus 로고
    • Subthalamic nucleus-mediated excitotoxicity in Parkinson's disease: a target for neuroprotection
    • Rodriguez MC, Obeso JA, Olanow CW. Subthalamic nucleus-mediated excitotoxicity in Parkinson's disease: a target for neuroprotection. Ann Neurol. 1998; 44: S175-88.
    • (1998) Ann Neurol , vol.44
    • Rodriguez, M.C.1    Obeso, J.A.2    Olanow, C.W.3
  • 82
    • 0017167057 scopus 로고
    • Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea
    • Coyle JT, Schwarcz R. Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea. Nature. 1976; 263: 244-6.
    • (1976) Nature. , vol.263 , pp. 244-246
    • Coyle, J.T.1    Schwarcz, R.2
  • 83
    • 0017090806 scopus 로고
    • Duplication of biochemical changes of Huntington's chorea by intrastriatal injections of glutamic and kainic acids
    • McGeer EG, McGeer PL. Duplication of biochemical changes of Huntington's chorea by intrastriatal injections of glutamic and kainic acids. Nature. 1976; 263: 517-9.
    • (1976) Nature. , vol.263 , pp. 517-519
    • McGeer, E.G.1    McGeer, P.L.2
  • 84
    • 0018695450 scopus 로고
    • Ibotenic acid-induced neuronal degeneration: a morphological and neurochemical study
    • Schwarcz R, Hokfelt T, Fuxe K, et al. Ibotenic acid-induced neuronal degeneration: a morphological and neurochemical study. Exp Brain Res. 1979; 37: 199-216.
    • (1979) Exp Brain Res. , vol.37 , pp. 199-216
    • Schwarcz, R.1    Hokfelt, T.2    K, F.3
  • 85
    • 0020702374 scopus 로고
    • Quinolinic acid: an endogenous metabolite that produces axon-sparing lesions in rat brain
    • Schwarcz R, Whetsell WO Jr, Mangano RM. Quinolinic acid: an endogenous metabolite that produces axon-sparing lesions in rat brain. Science. 1983; 219: 316-8.
    • (1983) Science. , vol.219 , pp. 316-318
    • Schwarcz, R.1    Whetsell Jr, W.O.2    Mangano, R.M.3
  • 86
    • 0022446150 scopus 로고
    • Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid
    • Beal MF, Kowall NW, Ellison DW, et al. Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid. Nature. 1986; 321: 168-71.
    • (1986) Nature. , vol.321 , pp. 168-171
    • Beal, M.F.1    Kowall, N.W.2    Ellison, D.W.3
  • 87
    • 0019434631 scopus 로고
    • Biochemical evidence for glutamate as neurotransmitter in corticostriatal and corticothalamic fibres in rat brain
    • Fonnum F, Storm-Mathisen J, Divac I. Biochemical evidence for glutamate as neurotransmitter in corticostriatal and corticothalamic fibres in rat brain. Neuroscience. 1981; 6: 863-73.
    • (1981) Neuroscience. , vol.6 , pp. 863-873
    • Fonnum, F.1    Storm-Mathisen, J.2    Divac, I.3
  • 88
    • 4344658072 scopus 로고    scopus 로고
    • The thalamostriatal system: a highly specific network of the basal ganglia circuitry
    • Smith Y, Raju DV, Pare JF, et al The thalamostriatal system: a highly specific network of the basal ganglia circuitry. Trends Neurosci. 2004; 27: 520-7.
    • (2004) Trends Neurosci. , vol.27 , pp. 520-527
    • Smith, Y.1    Raju, D.V.2    Pare, J.F.3
  • 89
    • 0029068332 scopus 로고
    • NMDA receptor subunit mRNA expression by projection neurons and interneurons in rat striatum
    • Landwehrmeyer GB, Standaert DG, Testa CM, et al. NMDA receptor subunit mRNA expression by projection neurons and interneurons in rat striatum. J Neurosci. 1995; 15: 5297-307.
    • (1995) J Neurosci. , vol.15 , pp. 5297-5307
    • Landwehrmeyer, G.B.1    Standaert, D.G.2    Testa, C.M.3
  • 90
    • 0037075624 scopus 로고    scopus 로고
    • Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease
    • Zeron MM, Hansson O, Chen N, et al. Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron. 2002; 33: 849-60.
    • (2002) Neuron. , vol.33 , pp. 849-860
    • Zeron, M.M.1    Hansson, O.2    N, C.3
  • 91
    • 30744437894 scopus 로고    scopus 로고
    • Striatal neuronal apoptosis is preferentially enhanced by NMDA receptor activation in YAC transgenic mouse model of Huntington disease
    • Shehadeh J, Fernandes HB, Zeron Mullins MM, et al. Striatal neuronal apoptosis is preferentially enhanced by NMDA receptor activation in YAC transgenic mouse model of Huntington disease. Neurobiol Dis. 2006; 21: 392-403.
    • (2006) Neurobiol Dis. , vol.21 , pp. 392-403
    • Shehadeh, J.1    Fernandes, H.B.2    Zeron Mullins, M.M.3
  • 92
    • 0023690166 scopus 로고
    • NMDA receptor losses in putamen from patients with Huntington's disease
    • Young AB, Greenamyre JT, Hollingsworth Z, et al. NMDA receptor losses in putamen from patients with Huntington's disease. Science. 1988; 241: 981-3.
    • (1988) Science. , vol.241 , pp. 981-983
    • Young, A.B.1    Greenamyre, J.T.2    Z, H.3
  • 93
    • 2542508397 scopus 로고    scopus 로고
    • Expression of NMDA receptor subunit mRNAs in neurochemically identified projection and interneurons in the human striatum
    • Kuppenbender KD, Standaert DG, Feuerstein TJ, et al. Expression of NMDA receptor subunit mRNAs in neurochemically identified projection and interneurons in the human striatum. J Comp Neurol. 2000; 419: 407-21.
    • (2000) J Comp Neurol. , vol.419 , pp. 407-421
    • Kuppenbender, K.D.1    Standaert, D.G.2    Feuerstein, T.J.3
  • 94
    • 74549181538 scopus 로고    scopus 로고
    • Early increase in extrasynaptic NMDA receptor signaling and expression contributes to phenotype onset in Huntington's disease mice
    • Milnerwood AJ, Gladding CM, Pouladi MA, et al. Early increase in extrasynaptic NMDA receptor signaling and expression contributes to phenotype onset in Huntington's disease mice. Neuron. 2010; 65: 178-90.
    • (2010) Neuron. , vol.65 , pp. 178-190
    • Milnerwood, A.J.1    Gladding, C.M.2    Pouladi, M.A.3
  • 95
    • 71549143207 scopus 로고    scopus 로고
    • Balance between synaptic versus extrasynaptic NMDA receptor activity influences inclusions and neurotoxicity of mutant huntingtin
    • Okamoto S, Pouladi MA, Talantova M, et al. Balance between synaptic versus extrasynaptic NMDA receptor activity influences inclusions and neurotoxicity of mutant huntingtin. Nat Med. 2009; 15: 1407-13.
    • (2009) Nat Med. , vol.15 , pp. 1407-1413
    • Okamoto, S.1    Pouladi, M.A.2    M, T.3
  • 96
    • 0032971311 scopus 로고    scopus 로고
    • Subtype-specific enhancement of NMDA receptor currents by mutant huntingtin
    • Chen N, Luo T, Wellington C, et al. Subtype-specific enhancement of NMDA receptor currents by mutant huntingtin. J Neurochem. 1999; 72: 1890-8.
    • (1999) J Neurochem. , vol.72 , pp. 1890-1898
    • Chen, N.1    Luo, T.2    C, W.3
  • 97
    • 0042357138 scopus 로고    scopus 로고
    • Expression of polyglutamine-expanded huntingtin induces tyrosine phosphorylation of N-methyl-D-aspartate receptors
    • Song C, Zhang Y, Parsons CG, et al Expression of polyglutamine-expanded huntingtin induces tyrosine phosphorylation of N-methyl-D-aspartate receptors. J Biol Chem. 2003; 278: 33364-9.
    • (2003) J Biol Chem. , vol.278 , pp. 33364-33369
    • Song, C.1    Zhang, Y.2    Parsons, C.G.3
  • 98
    • 63849154126 scopus 로고    scopus 로고
    • In vivo evidence for NMDA receptor-mediated excitotoxicity in a murine genetic model of Huntington disease
    • Heng MY, Detloff PJ, Wang PL, et al. In vivo evidence for NMDA receptor-mediated excitotoxicity in a murine genetic model of Huntington disease. J Neurosci. 2009; 29: 3200-5.
    • (2009) J Neurosci. , vol.29 , pp. 3200-3205
    • Heng, M.Y.1    Detloff, P.J.2    Wang, P.L.3
  • 99
    • 0035816627 scopus 로고    scopus 로고
    • Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95
    • Sun Y, Savanenin A, Reddy PH, et al Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-D-aspartate receptors via post-synaptic density 95. J Biol Chem. 2001; 276: 24713-8.
    • (2001) J Biol Chem. , vol.276 , pp. 24713-24718
    • Sun, Y.1    Savanenin, A.2    Reddy, P.H.3
  • 100
    • 0033546347 scopus 로고    scopus 로고
    • Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein
    • Sattler R, Xiong Z, Lu WY, et al. Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein. Science. 1999; 284: 1845-8.
    • (1999) Science. , vol.284 , pp. 1845-1848
    • Sattler, R.1    Xiong, Z.2    Lu, W.Y.3
  • 101
    • 38349101590 scopus 로고    scopus 로고
    • Glutamate uptake is reduced in prefrontal cortex in Huntington's disease
    • Hassel B, Tessler S, Faull RL, et al Glutamate uptake is reduced in prefrontal cortex in Huntington's disease. Neurochem Res. 2008; 33: 232-7.
    • (2008) Neurochem Res. , vol.33 , pp. 232-237
    • Hassel, B.1    Tessler, S.2    Faull, R.L.3
  • 102
    • 0032568517 scopus 로고    scopus 로고
    • Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human huntington disease gene
    • Cha JH, Kosinski CM, Kerner JA, et al. Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human huntington disease gene. Proc Natl Acad Sci USA. 1998; 95: 6480-5.
    • (1998) Proc Natl Acad Sci USA. , vol.95 , pp. 6480-6485
    • Cha, J.H.1    Kosinski, C.M.2    Kerner, J.A.3
  • 103
    • 0041963057 scopus 로고    scopus 로고
    • Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1
    • Tang TS, Tu H, Chan EY, et al. Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1, 4, 5) triphosphate receptor type 1. Neuron. 2003; 39: 227-39.
    • (2003) Neuron. , vol.39 , pp. 227-239
    • Tang, T.S.1    Tu, H.2    Chan, E.Y.3
  • 104
    • 84913107940 scopus 로고
    • Über das Kynurenin, ein intermediäres Stoffwechselprodukt des Tryptophans
    • Kotake Y, Iwao J. Über das Kynurenin, ein intermediäres Stoffwechselprodukt des Tryptophans. Z Physiol Chem. 1931; 195: 139-47.
    • (1931) Z Physiol Chem. , vol.195 , pp. 139-147
    • Kotake, Y.1    Iwao, J.2
  • 105
    • 2642607157 scopus 로고
    • Über eine neue Substanz, die aus Tryptophan im Tierkörper gebildet wird
    • Matsuoka Z, Yoshimatsu N. Über eine neue Substanz, die aus Tryptophan im Tierkörper gebildet wird. Z Physiol Chem. 1925; 143: 206-10.
    • (1925) Z Physiol Chem. , vol.143 , pp. 206-210
    • Matsuoka, Z.1    Yoshimatsu, N.2
  • 106
    • 0016007501 scopus 로고
    • The effect of hormones and vitamin B6 on urinary excretion of metabolites of the kynurenine pathway
    • Wolf H. The effect of hormones and vitamin B6 on urinary excretion of metabolites of the kynurenine pathway. Scand J Clin Lab Invest Suppl. 1974; 136: 1-186.
    • (1974) Scand J Clin Lab Invest Suppl. , vol.136 , pp. 1-186
    • Wolf, H.1
  • 107
    • 4143105239 scopus 로고
    • Kynurenine as an Intermediate in the Formation of Nicotinic Acid from Tryptophane by Neurospora
    • Beadle GW, Mitchell HK, Nyc JF. Kynurenine as an Intermediate in the Formation of Nicotinic Acid from Tryptophane by Neurospora. Proc Natl Acad Sci USA. 1947; 33: 155-8.
    • (1947) Proc Natl Acad Sci USA. , vol.33 , pp. 155-158
    • Beadle, G.W.1    Mitchell, H.K.2    Nyc, J.F.3
  • 109
    • 79955673383 scopus 로고
    • The metabolism of tryptophan III. The availability of kynurenine in supplementing a diet deficient in tryptophane
    • Jackson RW, Jackson WT. The metabolism of tryptophan III. The availability of kynurenine in supplementing a diet deficient in tryptophane. J Biol Chem. 1932; 96: 697-701.
    • (1932) J Biol Chem. , vol.96 , pp. 697-701
    • Jackson, R.W.1    Jackson, W.T.2
  • 110
    • 0004402825 scopus 로고
    • Studien über den intermediären Stoffwechsel des Tryptophans. XXXIV. Über die Anthranilsäurebildung aus Kynurenin durch Organsaft
    • Kotake Y, Nakayama Y. Studien über den intermediären Stoffwechsel des Tryptophans. XXXIV. Über die Anthranilsäurebildung aus Kynurenin durch Organsaft. Z Physiol Chem. 1941; 270: 76-82.
    • (1941) Z Physiol Chem. , vol.270 , pp. 76-82
    • Kotake, Y.1    Nakayama, Y.2
  • 111
    • 2642704374 scopus 로고
    • +-Gen-abhängiges Glied im intermediären Tryptophan-Stoffwechsel
    • +-Gen-abhängiges Glied im intermediären Tryptophan-Stoffwechsel. Z Naturf. 1949; 4b: 242-4.
    • (1949) Z Naturf , vol.4 , pp. 242-244
    • Butenandt, A.1    Weidel, W.2    Schlossberger, H.3
  • 112
    • 0012050994 scopus 로고
    • Quinolinic acid excretion by the rat receiving tryptophan
    • Henderson LM. Quinolinic acid excretion by the rat receiving tryptophan. J Biol Chem. 1949; 178: 1005-6.
    • (1949) J Biol Chem. , vol.178 , pp. 1005-1006
    • Henderson, L.M.1
  • 113
    • 36649021140 scopus 로고
    • Quinolinic acid metabolism; urinary excretion by the rat following tryptophan and 3-hydroxyanthranilic acid administration
    • Henderson LM, Hirsch HM. Quinolinic acid metabolism; urinary excretion by the rat following tryptophan and 3-hydroxyanthranilic acid administration. J Biol Chem. 1949; 181: 667-75.
    • (1949) J Biol Chem. , vol.181 , pp. 667-675
    • Henderson, L.M.1    Hirsch, H.M.2
  • 114
    • 0017597639 scopus 로고
    • The determination of kynurenine by gas-liquid chromatography; evidence for its presence in rat brain [proceedings]
    • Joseph MH. The determination of kynurenine by gas-liquid chromatography; evidence for its presence in rat brain [proceedings]. Br J Pharmacol. 1977; 59: 525P.
    • (1977) Br J Pharmacol , vol.59
    • Joseph, M.H.1
  • 115
    • 0017883532 scopus 로고
    • Synthesis and metabolism of L-kynurenine in rat brain
    • Gal EM, Sherman AD. Synthesis and metabolism of L-kynurenine in rat brain. J Neurochem. 1978; 30: 607-13.
    • (1978) J Neurochem. , vol.30 , pp. 607-613
    • Gal, E.M.1    Sherman, A.D.2
  • 116
    • 0018421069 scopus 로고
    • Kynurenine: penetration to the brain, effect on brain tryptophan and 5-hydroxytryptamine metabolism and binding to plasma albumin [proceedings]
    • Joseph MH, Kadam BV. Kynurenine: penetration to the brain, effect on brain tryptophan and 5-hydroxytryptamine metabolism and binding to plasma albumin [proceedings]. Br J Pharmacol. 1979; 66: 483P-4P.
    • (1979) Br J Pharmacol , vol.66
    • Joseph, M.H.1    Kadam, B.V.2
  • 117
    • 0018360268 scopus 로고
    • The uptake of kynurenine, a tryptophan metabolite, into mouse brain [proceedings]
    • Gould SE. The uptake of kynurenine, a tryptophan metabolite, into mouse brain [proceedings]. Br J Pharmacol. 1979; 66: 484P-5P.
    • (1979) Br J Pharmacol , vol.66
    • Gould, S.E.1
  • 118
    • 0026076136 scopus 로고
    • Blood-brain barrier transport of kynurenines: implications for brain synthesis and metabolism
    • Fukui S, Schwarcz R, Rapoport SI, et al. Blood-brain barrier transport of kynurenines: implications for brain synthesis and metabolism. J Neurochem. 1991; 56: 2007-17.
    • (1991) J Neurochem. , vol.56 , pp. 2007-2017
    • Fukui, S.1    Schwarcz, R.2    Rapoport, S.I.3
  • 119
    • 79955674100 scopus 로고
    • Mass-fragmentographic identification and measurement of the excitotoxin quinolinic acid in the mammalian brain
    • Lombardi G, Moneti G, Moroni F. Mass-fragmentographic identification and measurement of the excitotoxin quinolinic acid in the mammalian brain. Acta Pharmacol Toxicol. 1983; 53: 145.
    • (1983) Acta Pharmacol Toxicol , vol.53 , pp. 145
    • Lombardi, G.1    Moneti, G.2    Moroni, F.3
  • 120
    • 70449523216 scopus 로고    scopus 로고
    • Kynurenines in chronic neurodegenerative disorders: future therapeutic strategies
    • Zadori D, Klivenyi P, Vamos E, et al. Kynurenines in chronic neurodegenerative disorders: future therapeutic strategies. J Neural Transm. 2009; 116: 1403-9.
    • (2009) J Neural Transm. , vol.116 , pp. 1403-1409
    • Zadori, D.1    Klivenyi, P.2    E, V.3
  • 121
    • 77957131120 scopus 로고    scopus 로고
    • Kynurenines, neurodegeneration and Alzheimer's disease
    • Kincses ZT, Toldi J, Vecsei L. Kynurenines, neurodegeneration and Alzheimer's disease. J Cell Mol Med. 2010; DOI: .
    • (2010) J Cell Mol Med
    • Kincses, Z.T.1    Toldi, J.2    Vecsei, L.3
  • 122
    • 38449098312 scopus 로고    scopus 로고
    • Kynurenines, redox disturbances and neurodegeneration in multiple sclerosis
    • Rajda C, Bergquist J, Vecsei L. Kynurenines, redox disturbances and neurodegeneration in multiple sclerosis. J Neural Transm Suppl. 2007; 72: 323-9.
    • (2007) J Neural Transm Suppl. , vol.72 , pp. 323-329
    • Rajda, C.1    Bergquist, J.2    Vecsei, L.3
  • 123
    • 0015734617 scopus 로고
    • Kynurenines as probable participants of depression
    • Lapin IP. Kynurenines as probable participants of depression. Pharmakopsychiatr Neuropsychopharmakol. 1973; 6: 273-9.
    • (1973) Pharmakopsychiatr Neuropsychopharmakol. , vol.6 , pp. 273-279
    • Lapin, I.P.1
  • 124
    • 0017887867 scopus 로고
    • Stimulant and convulsive effects of kynurenines injected into brain ventricles in mice
    • Lapin IP. Stimulant and convulsive effects of kynurenines injected into brain ventricles in mice. J Neural Transm. 1978; 42: 37-43.
    • (1978) J Neural Transm. , vol.42 , pp. 37-43
    • Lapin, I.P.1
  • 125
    • 75849150001 scopus 로고    scopus 로고
    • Structure, expression, and function of kynurenine aminotransferases in human and rodent brains
    • Han Q, Cai T, Tagle DA, et al Structure, expression, and function of kynurenine aminotransferases in human and rodent brains. Cell Mol Life Sci. 2010; 67: 353-68.
    • (2010) Cell Mol Life Sci. , vol.67 , pp. 353-368
    • Han, Q.1    Cai, T.2    Tagle, D.A.3
  • 126
    • 0025972897 scopus 로고
    • Two kynurenine aminotransferases in human brain
    • Okuno E, Nakamura M, Schwarcz R. Two kynurenine aminotransferases in human brain. Brain Res. 1991; 542: 307-12.
    • (1991) Brain Res. , vol.542 , pp. 307-312
    • Okuno, E.1    Nakamura, M.2    Schwarcz, R.3
  • 127
    • 31844438501 scopus 로고    scopus 로고
    • Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family
    • Yu P, Li Z, Zhang L, et al. Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family. Gene. 2006; 365: 111-8.
    • (2006) Gene. , vol.365 , pp. 111-118
    • Yu, P.1    Li, Z.2    L, Z.3
  • 128
    • 34250156019 scopus 로고    scopus 로고
    • Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain
    • Guidetti P, Amori L, Sapko MT, et al. Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain. J Neurochem. 2007; 102: 103-11.
    • (2007) J Neurochem. , vol.102 , pp. 103-111
    • Guidetti, P.1    Amori, L.2    Sapko, M.T.3
  • 129
    • 0034894035 scopus 로고    scopus 로고
    • Kynurenine pathway metabolism in human astrocytes: a paradox for neuronal protection
    • Guillemin GJ, Kerr SJ, Smythe GA, et al. Kynurenine pathway metabolism in human astrocytes: a paradox for neuronal protection. J Neurochem. 2001; 78: 842-53.
    • (2001) J Neurochem. , vol.78 , pp. 842-853
    • Guillemin, G.J.1    Kerr, S.J.2    Smythe G.A.et, al.3
  • 130
    • 0026476185 scopus 로고
    • Immunocytochemical localization of kynurenine aminotransferase in the rat striatum: a light and electron microscopic study
    • Roberts RC, Du F, McCarthy KE, et al. Immunocytochemical localization of kynurenine aminotransferase in the rat striatum: a light and electron microscopic study. J Comp Neurol. 1992; 326: 82-90.
    • (1992) J Comp Neurol. , vol.326 , pp. 82-90
    • Roberts, R.C.1    Du, F.2    McCarthy, K.E.M.3
  • 131
    • 33751558659 scopus 로고    scopus 로고
    • Astrocytic localization of kynurenine aminotransferase II in the rat brain visualized by immunocytochemistry
    • Guidetti P, Hoffman GE, Melendez-Ferro M, et al. Astrocytic localization of kynurenine aminotransferase II in the rat brain visualized by immunocytochemistry. Glia. 2007; 55: 78-92.
    • (2007) Glia. , vol.55 , pp. 78-92
    • Guidetti, P.1    Hoffman, G.E.2    M, M.-F.3
  • 132
    • 0019861419 scopus 로고
    • Presence of kynurenine hydroxylase in developing rat brain
    • Battie C, Verity MA. Presence of kynurenine hydroxylase in developing rat brain. J Neurochem. 1981; 36: 1308-10.
    • (1981) J Neurochem. , vol.36 , pp. 1308-1310
    • Battie, C.1    Verity, M.A.2
  • 133
    • 0022471686 scopus 로고
    • Synthesis of quinolinic acid by 3-hydroxyanthranilic acid oxygenase in rat brain tissue in vitro
    • Foster AC, White RJ, Schwarcz R. Synthesis of quinolinic acid by 3-hydroxyanthranilic acid oxygenase in rat brain tissue in vitro. J Neurochem. 1986; 47: 23-30.
    • (1986) J Neurochem. , vol.47 , pp. 23-30
    • Foster, A.C.1    White, R.J.2    Schwarcz, R.3
  • 134
    • 0030887550 scopus 로고    scopus 로고
    • Activated human microglia produce the excitotoxin quinolinic acid
    • Espey MG, Chernyshev ON, Reinhard JF Jr, et al. Activated human microglia produce the excitotoxin quinolinic acid. Neuroreport. 1997; 8: 431-4.
    • (1997) Neuroreport. , vol.8 , pp. 431-434
    • Espey, M.G.1    Chernyshev, O.N.2    Reinhard Jr, J.F.3
  • 135
    • 0019967973 scopus 로고
    • An iontophoretic investigation of the actions of convulsant kynurenines and their interaction with the endogenous excitant quinolinic acid
    • Perkins MN, Stone TW. An iontophoretic investigation of the actions of convulsant kynurenines and their interaction with the endogenous excitant quinolinic acid. Brain Res. 1982; 247: 184-7.
    • (1982) Brain Res. , vol.247 , pp. 184-187
    • Perkins, M.N.1    Stone, T.W.2
  • 136
    • 0024564076 scopus 로고
    • A glycine site associated with N-methyl-D-aspartic acid receptors: characterization and identification of a new class of antagonists
    • Kessler M, Terramani T, Lynch G, et al A glycine site associated with N-methyl-D-aspartic acid receptors: characterization and identification of a new class of antagonists. J Neurochem. 1989; 52: 1319-28.
    • (1989) J Neurochem. , vol.52 , pp. 1319-1328
    • Kessler, M.1    Terramani, T.2    Lynch, G.3
  • 137
    • 0023809607 scopus 로고
    • Kynurenate and FG9041 have both competitive and non-competitive antagonist actions at excitatory amino acid receptors
    • Birch PJ, Grossman CJ, Hayes AG. Kynurenate and FG9041 have both competitive and non-competitive antagonist actions at excitatory amino acid receptors. Eur J Pharmacol. 1988; 151: 313-5.
    • (1988) Eur J Pharmacol. , vol.151 , pp. 313-315
    • Birch, P.J.1    Grossman, C.J.2    Hayes, A.G.3
  • 138
    • 33646780229 scopus 로고    scopus 로고
    • Kynurenic acid has a dual action on AMPA receptor responses
    • Prescott C, Weeks AM, Staley KJ, et al Kynurenic acid has a dual action on AMPA receptor responses. Neurosci Lett. 2006; 402: 108-12.
    • (2006) Neurosci Lett. , vol.402 , pp. 108-112
    • Prescott, C.1    Weeks, A.M.2    Staley, K.J.3
  • 140
    • 0035478066 scopus 로고    scopus 로고
    • The brain metabolite kynurenic acid inhibits alpha7 nicotinic receptor activity and increases non-alpha7 nicotinic receptor expression: physiopathological implications
    • Hilmas C, Pereira EF, Alkondon M, et al. The brain metabolite kynurenic acid inhibits alpha7 nicotinic receptor activity and increases non-alpha7 nicotinic receptor expression: physiopathological implications. J Neurosci. 2001; 21: 7463-73.
    • (2001) J Neurosci. , vol.21 , pp. 7463-7473
    • Hilmas, C.1    Pereira, E.F.2    M, A.3
  • 141
    • 0036325889 scopus 로고    scopus 로고
    • Direct evidence that release-stimulating alpha7* nicotinic cholinergic receptors are localized on human and rat brain glutamatergic axon terminals
    • Marchi M, Risso F, Viola C, et al. Direct evidence that release-stimulating alpha7* nicotinic cholinergic receptors are localized on human and rat brain glutamatergic axon terminals. J Neurochem. 2002; 80: 1071-8.
    • (2002) J Neurochem. , vol.80 , pp. 1071-1078
    • Marchi, M.1    Risso, F.2    C, V.3
  • 142
    • 33746823331 scopus 로고    scopus 로고
    • Kynurenic acid as a ligand for orphan G protein-coupled receptor GPR35
    • Wang J, Simonavicius N, Wu X, et al. Kynurenic acid as a ligand for orphan G protein-coupled receptor GPR35. J Biol Chem. 2006; 281: 22021-8.
    • (2006) J Biol Chem. , vol.281 , pp. 22021-22028
    • Wang, J.1    Simonavicius, N.2    X, W.3
  • 143
    • 0036839337 scopus 로고    scopus 로고
    • Expression of kynurenine aminotransferase in the subplate of the rat and its possible role in the regulation of programmed cell death
    • Csillik AE, Okuno E, Csillik B, et al. Expression of kynurenine aminotransferase in the subplate of the rat and its possible role in the regulation of programmed cell death. Cereb Cortex. 2002; 12: 1193-201.
    • (2002) Cereb Cortex. , vol.12 , pp. 1193-1201
    • Csillik, A.E.1    Okuno, E.2    B, C.3
  • 144
    • 0342468278 scopus 로고    scopus 로고
    • The endogenous agonist quinolinic acid and the non endogenous homoquinolinic acid discriminate between NMDAR2 receptor subunits
    • de Carvalho LP, Bochet P, Rossier J. The endogenous agonist quinolinic acid and the non endogenous homoquinolinic acid discriminate between NMDAR2 receptor subunits. Neurochem Int. 1996; 28: 445-52.
    • (1996) Neurochem Int. , vol.28 , pp. 445-452
    • de Carvalho, L.P.1    Bochet, P.2    Rossier, J.3
  • 145
    • 0019440926 scopus 로고
    • Quinolinic acid: a potent endogenous excitant at amino acid receptors in CNS
    • Stone TW, Perkins MN. Quinolinic acid: a potent endogenous excitant at amino acid receptors in CNS. Eur J Pharmacol. 1981; 72: 411-2.
    • (1981) Eur J Pharmacol. , vol.72 , pp. 411-412
    • Stone, T.W.1    Perkins, M.N.2
  • 146
    • 0023876882 scopus 로고
    • Quinolinic acid effects on amino acid release from the rat cerebral cortex in vitro and in vivo
    • Connick JH, Stone TW. Quinolinic acid effects on amino acid release from the rat cerebral cortex in vitro and in vivo. Br J Pharmacol. 1988; 93: 868-76.
    • (1988) Br J Pharmacol. , vol.93 , pp. 868-876
    • Connick, J.H.1    Stone, T.W.2
  • 147
    • 0036128148 scopus 로고    scopus 로고
    • Quinolinic acid stimulates synaptosomal glutamate release and inhibits glutamate uptake into astrocytes
    • Tavares RG, Tasca CI, Santos CE, et al. Quinolinic acid stimulates synaptosomal glutamate release and inhibits glutamate uptake into astrocytes. Neurochem Int. 2002; 40: 621-7.
    • (2002) Neurochem Int. , vol.40 , pp. 621-627
    • Tavares, R.G.1    Tasca, C.I.2    Santos, C.E.3
  • 148
    • 0033406026 scopus 로고    scopus 로고
    • Oxidative stress as a mechanism for quinolinic acid-induced hippocampal damage: protection by melatonin and deprenyl
    • Behan WM, McDonald M, Darlington LG, et al Oxidative stress as a mechanism for quinolinic acid-induced hippocampal damage: protection by melatonin and deprenyl. Br J Pharmacol. 1999; 128: 1754-60.
    • (1999) Br J Pharmacol. , vol.128 , pp. 1754-1760
    • Behan, W.M.1    McDonald, M.2    Darlington, L.G.3
  • 149
    • 0025936872 scopus 로고
    • Quinolinic acid is a potent lipid peroxidant in rat brain homogenates
    • Rios C, Santamaria A. Quinolinic acid is a potent lipid peroxidant in rat brain homogenates. Neurochem Res. 1991; 16: 1139-43.
    • (1991) Neurochem Res. , vol.16 , pp. 1139-1143
    • Rios, C.1    Santamaria, A.2
  • 150
    • 0025672787 scopus 로고
    • The role of hydrogen peroxide in the in vitro cytotoxicity of 3-hydroxykynurenine
    • Eastman CL, Guilarte TR. The role of hydrogen peroxide in the in vitro cytotoxicity of 3-hydroxykynurenine. Neurochem Res. 1990; 15: 1101-7.
    • (1990) Neurochem Res. , vol.15 , pp. 1101-1107
    • Eastman, C.L.1    Guilarte, T.R.2
  • 151
    • 0031972945 scopus 로고    scopus 로고
    • 3-Hydroxykynurenine, an endogenous oxidative stress generator, causes neuronal cell death with apoptotic features and region selectivity
    • Okuda S, Nishiyama N, Saito H, et al 3-Hydroxykynurenine, an endogenous oxidative stress generator, causes neuronal cell death with apoptotic features and region selectivity. J Neurochem. 1998; 70: 299-307.
    • (1998) J Neurochem. , vol.70 , pp. 299-307
    • Okuda, S.1    Nishiyama, N.2    Saito, H.3
  • 152
    • 0023095424 scopus 로고
    • Oxidative reactivity of the tryptophan metabolites 3-hydroxyanthranilate, cinnabarinate, quinolinate and picolinate
    • Dykens JA, Sullivan SG, Stern A. Oxidative reactivity of the tryptophan metabolites 3-hydroxyanthranilate, cinnabarinate, quinolinate and picolinate. Biochem Pharmacol. 1987; 36: 211-7.
    • (1987) Biochem Pharmacol. , vol.36 , pp. 211-217
    • Dykens, J.A.1    Sullivan, S.G.2    Stern, A.3
  • 153
    • 0025149531 scopus 로고
    • Quinolinate-induced cortical cholinergic damage: modulation by tryptophan metabolites
    • Jhamandas K, Boegman RJ, Beninger RJ, et al Quinolinate-induced cortical cholinergic damage: modulation by tryptophan metabolites. Brain Res. 1990; 529: 185-91.
    • (1990) Brain Res. , vol.529 , pp. 185-191
    • Jhamandas, K.1    Boegman, R.J.2    Beninger, R.J.3
  • 154
    • 0026671306 scopus 로고
    • Kynurenine pathway abnormalities in Parkinson's disease
    • Ogawa T, Matson WR, Beal MF, et al. Kynurenine pathway abnormalities in Parkinson's disease. Neurology. 1992; 42: 1702-6.
    • (1992) Neurology. , vol.42 , pp. 1702-1706
    • Ogawa, T.1    Matson, W.R.2    Beal, M.F.3
  • 155
    • 17944399946 scopus 로고    scopus 로고
    • Decreased expression of kynurenine aminotransferase-I (KAT-I) in the substantia nigra of mice after 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) treatment
    • Knyihar-Csillik E, Csillik B, Pakaski M, et al. Decreased expression of kynurenine aminotransferase-I (KAT-I) in the substantia nigra of mice after 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) treatment. Neuroscience. 2004; 126: 899-914.
    • (2004) Neuroscience. , vol.126 , pp. 899-914
    • Knyihar-Csillik, E.1    Csillik, B.2    M, P.3
  • 156
    • 39049186145 scopus 로고    scopus 로고
    • Effect of 6-hydroxydopamine treatment on kynurenine aminotransferase-I (KAT-I) immunoreactivity of neurons and glial cells in the rat substantia nigra
    • Knyihar-Csillik E, Chadaide Z, Mihaly A, et al. Effect of 6-hydroxydopamine treatment on kynurenine aminotransferase-I (KAT-I) immunoreactivity of neurons and glial cells in the rat substantia nigra. Acta Neuropathol. 2006; 112: 127-37.
    • (2006) Acta Neuropathol. , vol.112 , pp. 127-137
    • Knyihar-Csillik, E.1    Chadaide, Z.2    A, M.3
  • 157
    • 0037072547 scopus 로고    scopus 로고
    • 1-Methyl-4-phenylpyridinium and 3-nitropropionic acid diminish cortical synthesis of kynurenic acid via interference with kynurenine aminotransferases in rats
    • Luchowski P, Luchowska E, Turski WA, et al 1-Methyl-4-phenylpyridinium and 3-nitropropionic acid diminish cortical synthesis of kynurenic acid via interference with kynurenine aminotransferases in rats. Neurosci Lett. 2002; 330: 49-52.
    • (2002) Neurosci Lett. , vol.330 , pp. 49-52
    • Luchowski, P.1    Luchowska, E.2    Turski, W.A.3
  • 158
    • 0025161567 scopus 로고
    • Kynurenine pathway measurements in Huntington's disease striatum: evidence for reduced formation of kynurenic acid
    • Beal MF, Matson WR, Swartz KJ, et al. Kynurenine pathway measurements in Huntington's disease striatum: evidence for reduced formation of kynurenic acid. J Neurochem. 1990; 55: 1327-39.
    • (1990) J Neurochem. , vol.55 , pp. 1327-1339
    • Beal, M.F.1    Matson, W.R.2    Swartz, K.J.3
  • 159
    • 0028903541 scopus 로고
    • Dysfunction of brain kynurenic acid metabolism in Huntington's disease: focus on kynurenine aminotransferases
    • Jauch D, Urbanska EM, Guidetti P, et al. Dysfunction of brain kynurenic acid metabolism in Huntington's disease: focus on kynurenine aminotransferases. J Neurol Sci. 1995; 130: 39-47.
    • (1995) J Neurol Sci. , vol.130 , pp. 39-47
    • Jauch, D.1    Urbanska, E.M.2    P, G.3
  • 160
    • 9644270316 scopus 로고    scopus 로고
    • Neostriatal and cortical quinolinate levels are increased in early grade Huntington's disease
    • Guidetti P, Luthi-Carter RE, Augood SJ, et al Neostriatal and cortical quinolinate levels are increased in early grade Huntington's disease. Neurobiol Dis. 2004; 17: 455-61.
    • (2004) Neurobiol Dis. , vol.17 , pp. 455-461
    • Guidetti, P.1    Luthi-Carter, R.E.2    Augood, S.J.3
  • 161
    • 0026539659 scopus 로고
    • Quinolinic acid and kynurenine pathway metabolism in inflammatory and non-inflammatory neurological disease
    • Heyes MP, Saito K, Crowley JS, et al. Quinolinic acid and kynurenine pathway metabolism in inflammatory and non-inflammatory neurological disease. Brain. 1992; 115: 1249-73.
    • (1992) Brain. , vol.115 , pp. 1249-1273
    • Heyes, M.P.1    Saito, K.2    Crowley, J.S.3
  • 162
    • 0024024251 scopus 로고
    • 3-Hydroxyanthranilate oxygenase activity is increased in the brains of Huntington disease victims
    • Schwarcz R, Okuno E, White RJ, et al. 3-Hydroxyanthranilate oxygenase activity is increased in the brains of Huntington disease victims. Proc Natl Acad Sci USA. 1988; 85: 4079-81.
    • (1988) Proc Natl Acad Sci USA. , vol.85 , pp. 4079-4081
    • Schwarcz, R.1    Okuno, E.2    White, R.J.3
  • 163
    • 0025776094 scopus 로고
    • Comparative behavioral and neurochemical studies with striatal kainic acid- or quinolinic acid-lesioned rats
    • Vecsei L, Beal MF. Comparative behavioral and neurochemical studies with striatal kainic acid- or quinolinic acid-lesioned rats. Pharmacol Biochem Behav. 1991; 39: 473-8.
    • (1991) Pharmacol Biochem Behav. , vol.39 , pp. 473-478
    • Vecsei, L.1    Beal, M.F.2
  • 164
    • 76849100874 scopus 로고    scopus 로고
    • Of mice, rats and men: Revisiting the quinolinic acid hypothesis of Huntington's disease
    • Schwarcz R, Guidetti P, Sathyasaikumar KV, et al Of mice, rats and men: Revisiting the quinolinic acid hypothesis of Huntington's disease. Prog Neurobiol. 2010; 90: 230-45.
    • (2010) Prog Neurobiol. , vol.90 , pp. 230-245
    • Schwarcz, R.1    Guidetti, P.2    Sathyasaikumar, K.V.3
  • 165
    • 29144485791 scopus 로고    scopus 로고
    • Endogenous kynurenate controls the vulnerability of striatal neurons to quinolinate: Implications for Huntington's disease
    • Sapko MT, Guidetti P, Yu P, et al. Endogenous kynurenate controls the vulnerability of striatal neurons to quinolinate: Implications for Huntington's disease. Exp Neurol. 2006; 197: 31-40.
    • (2006) Exp Neurol. , vol.197 , pp. 31-40
    • Sapko, M.T.1    Guidetti, P.2    P, Y.3
  • 166
    • 0026783169 scopus 로고
    • Increased brain concentrations of a neurotoxin, 3-hydroxykynurenine, in Huntington's disease
    • Pearson SJ, Reynolds GP. Increased brain concentrations of a neurotoxin, 3-hydroxykynurenine, in Huntington's disease. Neurosci Lett. 1992; 144: 199-201.
    • (1992) Neurosci Lett. , vol.144 , pp. 199-201
    • Pearson, S.J.1    Reynolds, G.P.2
  • 167
    • 0032698232 scopus 로고    scopus 로고
    • 3-Hydroxykynurenine potentiates quinolinate but not NMDA toxicity in the rat striatum
    • Guidetti P, Schwarcz R. 3-Hydroxykynurenine potentiates quinolinate but not NMDA toxicity in the rat striatum. Eur J Neurosci. 1999; 11: 3857-63.
    • (1999) Eur J Neurosci. , vol.11 , pp. 3857-3863
    • Guidetti, P.1    Schwarcz, R.2
  • 168
    • 0036435648 scopus 로고    scopus 로고
    • Effect of 3-nitropropionic acid on kynurenine aminotransferase in the rat brain
    • Csillik A, Knyihar E, Okuno E, et al. Effect of 3-nitropropionic acid on kynurenine aminotransferase in the rat brain. Exp Neurol. 2002; 177: 233-41.
    • (2002) Exp Neurol. , vol.177 , pp. 233-241
    • Csillik, A.1    Knyihar, E.2    E, O.3
  • 169
    • 18144406846 scopus 로고    scopus 로고
    • A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease
    • Giorgini F, Guidetti P, Nguyen Q, et al. A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease. Nat Genet. 2005; 37: 526-31.
    • (2005) Nat Genet. , vol.37 , pp. 526-531
    • Giorgini, F.1    Guidetti, P.2    Q, N.3
  • 170
    • 41249101172 scopus 로고    scopus 로고
    • Neuroprotection for Huntington's disease: ready, set, slow
    • Hersch SM, Rosas HD. Neuroprotection for Huntington's disease: ready, set, slow. Neurotherapeutics. 2008; 5: 226-36.
    • (2008) Neurotherapeutics. , vol.5 , pp. 226-236
    • Hersch, S.M.1    Rosas, H.D.2
  • 171
    • 76949084998 scopus 로고    scopus 로고
    • Novel therapeutic strategies in Parkinson's disease
    • Klivenyi P, Vecsei L. Novel therapeutic strategies in Parkinson's disease. Eur J Clin Pharmacol. 2010; 66: 119-25.
    • (2010) Eur J Clin Pharmacol. , vol.66 , pp. 119-125
    • Klivenyi, P.1    Vecsei, L.2
  • 172
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • Zuccato C, Valenza M, Cattaneo E. Molecular mechanisms and potential therapeutical targets in Huntington's disease. Physiol Rev. 2010; 90: 905-81.
    • (2010) Physiol Rev. , vol.90 , pp. 905-981
    • Zuccato, C.1    Valenza, M.2    Cattaneo, E.3
  • 173
    • 77957113336 scopus 로고    scopus 로고
    • Pharmacological therapy in Parkinson's disease: focus on neuroprotection
    • Kincses ZT, Vecsei L. Pharmacological therapy in Parkinson's disease: focus on neuroprotection. CNS Neurosci Ther. 2010; DOI: .
    • (2010) CNS Neurosci Ther
    • Kincses, Z.T.1    Vecsei, L.2
  • 174
    • 0036240776 scopus 로고    scopus 로고
    • Delaying brain mitochondrial decay and aging with mitochondrial antioxidants and metabolites
    • Liu J, Atamna H, Kuratsune H, et al Delaying brain mitochondrial decay and aging with mitochondrial antioxidants and metabolites. Ann NY Acad Sci. 2002; 959: 133-66.
    • (2002) Ann NY Acad Sci. , vol.959 , pp. 133-166
    • Liu, J.1    Atamna, H.2    Kuratsune, H.3
  • 175
    • 33845186388 scopus 로고    scopus 로고
    • L-carnitine protects neurons from 1-methyl-4-phenylpyridinium-induced neuronal apoptosis in rat forebrain culture
    • Wang C, Sadovova N, Ali HK, et al. L-carnitine protects neurons from 1-methyl-4-phenylpyridinium-induced neuronal apoptosis in rat forebrain culture. Neuroscience. 2007; 144: 46-55.
    • (2007) Neuroscience. , vol.144 , pp. 46-55
    • Wang, C.1    Sadovova, N.2    Ali, H.K.3
  • 177
    • 77951950272 scopus 로고    scopus 로고
    • Combined R-alpha-lipoic acid and acetyl-L-carnitine exerts efficient preventative effects in a cellular model of Parkinson's disease
    • Zhang H, Jia H, Liu J, et al. Combined R-alpha-lipoic acid and acetyl-L-carnitine exerts efficient preventative effects in a cellular model of Parkinson's disease. J Cell Mol Med. 2010; 14: 215-25.
    • (2010) J Cell Mol Med. , vol.14 , pp. 215-225
    • Zhang, H.1    Jia, H.2    Liu, J.3
  • 178
    • 58749093249 scopus 로고    scopus 로고
    • Mechanism of 3-nitropropionic acid-induced membrane permeability transition of isolated mitochondria and its suppression by L-carnitine
    • Nishimura M, Okimura Y, Fujita H, et al. Mechanism of 3-nitropropionic acid-induced membrane permeability transition of isolated mitochondria and its suppression by L-carnitine. Cell Biochem Funct. 2008; 26: 881-91.
    • (2008) Cell Biochem Funct. , vol.26 , pp. 881-891
    • Nishimura, M.1    Okimura, Y.2    Fujita, H.3
  • 179
    • 77952322688 scopus 로고    scopus 로고
    • Neuroprotective effects of L-carnitine in a transgenic animal model of Huntington's disease
    • Vamos E, Voros K, Vecsei L, et al Neuroprotective effects of L-carnitine in a transgenic animal model of Huntington's disease. Biomed Pharmacother. 2010; 64: 282-6.
    • (2010) Biomed Pharmacother. , vol.64 , pp. 282-286
    • Vamos, E.1    Voros, K.2    Vecsei, L.3
  • 180
    • 0025050646 scopus 로고
    • L-acetyl-carnitine in Huntington's disease: double-blind placebo controlled crossover study of drug effects on movement disorder and dementia
    • Goetz CG, Tanner CM, Cohen JA, et al. L-acetyl-carnitine in Huntington's disease: double-blind placebo controlled crossover study of drug effects on movement disorder and dementia. Mov Disord. 1990; 5: 263-5.
    • (1990) Mov Disord. , vol.5 , pp. 263-265
    • Goetz, C.G.1    Tanner, C.M.2    Cohen, J.A.3
  • 181
    • 77952395404 scopus 로고    scopus 로고
    • Carnosine as a natural antioxidant and geroprotector: from molecular mechanisms to clinical trials
    • Boldyrev AA, Stvolinsky SL, Fedorova TN, et al Carnosine as a natural antioxidant and geroprotector: from molecular mechanisms to clinical trials. Rejuvenation Res. 2010; 13: 156-8.
    • (2010) Rejuvenation Res. , vol.13 , pp. 156-158
    • Boldyrev, A.A.1    Stvolinsky, S.L.2    Fedorova, T.N.3
  • 182
    • 50449098572 scopus 로고    scopus 로고
    • Carnosine increases efficiency of DOPA therapy of Parkinson's disease: a pilot study
    • Boldyrev A, Fedorova T, Stepanova M, et al. Carnosine increases efficiency of DOPA therapy of Parkinson's disease: a pilot study. Rejuvenation Res. 2008; 11: 821-7.
    • (2008) Rejuvenation Res. , vol.11 , pp. 821-827
    • Boldyrev, A.1    Fedorova, T.2    Stepanova, M.3
  • 183
    • 0031594295 scopus 로고    scopus 로고
    • 10 attenuates the 1-methyl-4-phenyl-1,2,3,tetrahydropyridine (MPTP) induced loss of striatal dopamine and dopaminergic axons in aged mice
    • 10 attenuates the 1-methyl-4-phenyl-1, 2, 3, tetrahydropyridine (MPTP) induced loss of striatal dopamine and dopaminergic axons in aged mice. Brain Res. 1998; 783: 109-14.
    • (1998) Brain Res. , vol.783 , pp. 109-114
    • Beal, M.F.1    Matthews, R.T.2    Tieleman, A.3
  • 184
    • 0035960544 scopus 로고    scopus 로고
    • 10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model
    • 10 and remacemide hydrochloride ameliorate motor deficits in a Huntington's disease transgenic mouse model. Neurosci Lett. 2001; 315: 149-53.
    • (2001) Neurosci Lett. , vol.315 , pp. 149-153
    • Schilling, G.1    Coonfield, M.L.2    Ross, C.A.3
  • 185
  • 186
    • 0030626791 scopus 로고    scopus 로고
    • Q10 therapy in patients with idiopathic Parkinson's disease
    • Strijks E, Kremer HP, Horstink MW. Q10 therapy in patients with idiopathic Parkinson's disease. Mol Aspects Med. 1997; 18: S237-40.
    • (1997) Mol Aspects Med , vol.18
    • Strijks, E.1    Kremer, H.P.2    Horstink, M.W.3
  • 187
    • 0036771852 scopus 로고    scopus 로고
    • Effects of coenzyme Q10 in early Parkinson disease: evidence of slowing of the functional decline
    • Shults CW, Oakes D, Kieburtz K, et al. Effects of coenzyme Q10 in early Parkinson disease: evidence of slowing of the functional decline. Arch Neurol. 2002; 59: 1541-50.
    • (2002) Arch Neurol. , vol.59 , pp. 1541-1550
    • Shults, C.W.1    Oakes, D.2    Kieburtz, K.3
  • 188
    • 0037426566 scopus 로고    scopus 로고
    • Coenzyme Q10 supplementation provides mild symptomatic benefit in patients with Parkinson's disease
    • Muller T, Buttner T, Gholipour AF, et al Coenzyme Q10 supplementation provides mild symptomatic benefit in patients with Parkinson's disease. Neurosci Lett. 2003; 341: 201-4.
    • (2003) Neurosci Lett. , vol.341 , pp. 201-204
    • Muller, T.1    Buttner, T.2    Gholipour, A.F.3
  • 189
    • 34447252358 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled trial on symptomatic effects of coenzyme Q(10) in Parkinson disease
    • Storch A, Jost WH, Vieregge P, et al. Randomized, double-blind, placebo-controlled trial on symptomatic effects of coenzyme Q(10) in Parkinson disease. Arch Neurol. 2007; 64: 938-44.
    • (2007) Arch Neurol. , vol.64 , pp. 938-944
    • Storch, A.1    Jost, W.H.2    Vieregge, P.3
  • 190
    • 85009226418 scopus 로고    scopus 로고
    • A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease
    • Huntington Study Group
    • Huntington Study Group. A randomized, placebo-controlled trial of coenzyme Q10 and remacemide in Huntington's disease. Neurology. 2001; 57: 397-404.
    • (2001) Neurology. , vol.57 , pp. 397-404
  • 191
    • 77956802394 scopus 로고    scopus 로고
    • Safety and tolerability of high-dosage coenzyme Q(10) in Huntington's disease and healthy subjects
    • The Huntington Study Group Pre2CARE Investigators
    • The Huntington Study Group Pre2CARE Investigators. Safety and tolerability of high-dosage coenzyme Q(10) in Huntington's disease and healthy subjects. Mov Disord. 2010; 25: 1924-8.
    • (2010) Mov Disord. , vol.25 , pp. 1924-1928
  • 192
    • 0027724925 scopus 로고
    • Functional aspects of creatine kinase in brain
    • Hemmer W, Wallimann T. Functional aspects of creatine kinase in brain. Dev Neurosci. 1993; 15: 249-60.
    • (1993) Dev Neurosci. , vol.15 , pp. 249-260
    • Hemmer, W.1    Wallimann, T.2
  • 193
    • 0031559949 scopus 로고    scopus 로고
    • The role of creatine kinase in inhibition of mitochondrial permeability transition
    • O'Gorman E, Beutner G, Dolder M, et al. The role of creatine kinase in inhibition of mitochondrial permeability transition. FEBS Lett. 1997; 414: 253-7.
    • (1997) FEBS Lett. , vol.414 , pp. 253-257
    • O'Gorman, E.1    Beutner, G.2    Dolder, M.3
  • 194
    • 0032914740 scopus 로고    scopus 로고
    • Creatine and cyclocreatine attenuate MPTP neurotoxicity
    • Matthews RT, Ferrante RJ, Klivenyi P, et al. Creatine and cyclocreatine attenuate MPTP neurotoxicity. Exp Neurol. 1999; 157: 142-9.
    • (1999) Exp Neurol. , vol.157 , pp. 142-149
    • Matthews, R.T.1    Ferrante, R.J.2    Klivenyi, P.3
  • 195
    • 0031964359 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine and cyclocreatine in animal models of Huntington's disease
    • Matthews RT, Yang L, Jenkins BG, et al. Neuroprotective effects of creatine and cyclocreatine in animal models of Huntington's disease. J Neurosci. 1998; 18: 156-63.
    • (1998) J Neurosci. , vol.18 , pp. 156-163
    • Matthews, R.T.1    Yang, L.2    Jenkins, B.G.3
  • 196
    • 0034660457 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease
    • Ferrante RJ, Andreassen OA, Jenkins BG, et al. Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease. J Neurosci. 2000; 20: 4389-97.
    • (2000) J Neurosci. , vol.20 , pp. 4389-4397
    • Ferrante, R.J.1    Andreassen, O.A.2    Jenkins, B.G.3
  • 197
    • 0034743672 scopus 로고    scopus 로고
    • Creatine increase survival and delays motor symptoms in a transgenic animal model of Huntington's disease
    • Andreassen OA, Dedeoglu A, Ferrante RJ, et al. Creatine increase survival and delays motor symptoms in a transgenic animal model of Huntington's disease. Neurobiol Dis. 2001; 8: 479-91.
    • (2001) Neurobiol Dis. , vol.8 , pp. 479-491
    • Andreassen, O.A.1    Dedeoglu, A.2    Ferrante, R.J.3
  • 198
    • 33645894705 scopus 로고    scopus 로고
    • A randomized, double-blind, futility clinical trial of creatine and minocycline in early Parkinson disease
    • NINDS NET-PD Investigators
    • NINDS NET-PD Investigators. A randomized, double-blind, futility clinical trial of creatine and minocycline in early Parkinson disease. Neurology. 2006; 66: 664-71.
    • (2006) Neurology. , vol.66 , pp. 664-671
  • 199
    • 44649153832 scopus 로고    scopus 로고
    • A pilot clinical trial of creatine and minocycline in early Parkinson disease: 18-month results
    • NINDS NET-PD Investigators
    • NINDS NET-PD Investigators. A pilot clinical trial of creatine and minocycline in early Parkinson disease: 18-month results. Clin Neuropharmacol. 2008; 31: 141-50.
    • (2008) Clin Neuropharmacol. , vol.31 , pp. 141-150
  • 200
    • 33749835508 scopus 로고    scopus 로고
    • Creatine supplementation in Parkinson disease: a placebo-controlled randomized pilot trial
    • Bender A, Koch W, Elstner M, et al. Creatine supplementation in Parkinson disease: a placebo-controlled randomized pilot trial. Neurology. 2006; 67: 1262-4.
    • (2006) Neurology. , vol.67 , pp. 1262-1264
    • Bender, A.1    Koch, W.2    Elstner, M.3
  • 201
    • 0037677341 scopus 로고    scopus 로고
    • Creatine therapy for Huntington's disease: clinical and MRS findings in a 1-year pilot study
    • Tabrizi SJ, Blamire AM, Manners DN, et al. Creatine therapy for Huntington's disease: clinical and MRS findings in a 1-year pilot study. Neurology. 2003; 61: 141-2.
    • (2003) Neurology. , vol.61 , pp. 141-142
    • Tabrizi, S.J.1    Blamire, A.M.2    Manners, D.N.3
  • 202
    • 18144370445 scopus 로고    scopus 로고
    • High-dose creatine therapy for Huntington disease: a 2-year clinical and MRS study
    • Tabrizi SJ, Blamire AM, Manners DN, et al. High-dose creatine therapy for Huntington disease: a 2-year clinical and MRS study. Neurology. 2005; 64: 1655-6.
    • (2005) Neurology. , vol.64 , pp. 1655-1656
    • Tabrizi, S.J.1    Blamire, A.M.2    Manners D.N.et, al.3
  • 203
    • 0141959170 scopus 로고    scopus 로고
    • Creatine supplementation in Huntington's disease: a placebo-controlled pilot trial
    • Verbessem P, Lemiere J, Eijnde BO, et al. Creatine supplementation in Huntington's disease: a placebo-controlled pilot trial. Neurology. 2003; 61: 925-30.
    • (2003) Neurology. , vol.61 , pp. 925-930
    • Verbessem, P.1    Lemiere, J.2    Eijnde, B.O.3
  • 204
    • 41049099937 scopus 로고    scopus 로고
    • Antioxidant effect of cysteamine in brain cortex of young rats
    • Kessler A, Biasibetti M, da Silva Melo DA, et al. Antioxidant effect of cysteamine in brain cortex of young rats. Neurochem Res. 2008; 33: 737-44.
    • (2008) Neurochem Res. , vol.33 , pp. 737-744
    • Kessler, A.1    Biasibetti, M.2    da Silva Melo, D.A.3
  • 205
    • 44449148186 scopus 로고    scopus 로고
    • Cysteamine prevents inhibition of thiol-containing enzymes caused by cystine or cystine dimethylester loading in rat brain cortex
    • Rech VC, Feksa LR, Fleck RM, et al. Cysteamine prevents inhibition of thiol-containing enzymes caused by cystine or cystine dimethylester loading in rat brain cortex. Metab Brain Dis. 2008; 23: 133-45.
    • (2008) Metab Brain Dis. , vol.23 , pp. 133-145
    • Rech, V.C.1    Feksa, L.R.2    Fleck, R.M.3
  • 206
    • 0036134819 scopus 로고    scopus 로고
    • Evidence for a role for transglutaminase in Huntington's disease and the potential therapeutic implications
    • Karpuj MV, Becher MW, Steinman L. Evidence for a role for transglutaminase in Huntington's disease and the potential therapeutic implications. Neurochem Int. 2002; 40: 31-6.
    • (2002) Neurochem Int. , vol.40 , pp. 31-36
    • Karpuj, M.V.1    Becher, M.W.2    Steinman, L.3
  • 207
    • 0022548599 scopus 로고
    • Systemic administration of antioxidants does not protect mice against the dopaminergic neurotoxicity of 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine (MPTP)
    • Martinovits G, Melamed E, Cohen O, et al. Systemic administration of antioxidants does not protect mice against the dopaminergic neurotoxicity of 1-methyl-4-phenyl-1, 2, 5, 6-tetrahydropyridine (MPTP). Neurosci Lett. 1986; 69: 192-7.
    • (1986) Neurosci Lett. , vol.69 , pp. 192-197
    • Martinovits, G.1    Melamed, E.2    Cohen, O.3
  • 208
    • 77952322840 scopus 로고    scopus 로고
    • Effects of cysteamine on MPTP-induced dopaminergic neurodegeneration in mice
    • Sun L, Xu S, Zhou M, et al. Effects of cysteamine on MPTP-induced dopaminergic neurodegeneration in mice. Brain Res. 2010; 1335: 74-82.
    • (2010) Brain Res. , vol.1335 , pp. 74-82
    • Sun, L.1    Xu, S.2    Zhou, M.3
  • 209
    • 33646469999 scopus 로고    scopus 로고
    • Neuroprotective effects of cystamine in aged parkinsonian mice
    • Tremblay ME, Saint-Pierre M, Bourhis E, et al. Neuroprotective effects of cystamine in aged parkinsonian mice. Neurobiol Aging. 2006; 27: 862-70.
    • (2006) Neurobiol Aging. , vol.27 , pp. 862-870
    • Tremblay, M.E.1    Saint-Pierre, M.2    Bourhis, E.3
  • 210
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • Karpuj MV, Becher MW, Springer JE, et al. Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat Med. 2002; 8: 143-9.
    • (2002) Nat Med. , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3
  • 211
    • 0037109665 scopus 로고    scopus 로고
    • Therapeutic effects of cystamine in a murine model of Huntington's disease
    • Dedeoglu A, Kubilus JK, Jeitner TM, et al. Therapeutic effects of cystamine in a murine model of Huntington's disease. J Neurosci. 2002; 22: 8942-50.
    • (2002) J Neurosci. , vol.22 , pp. 8942-8950
    • Dedeoglu, A.1    Kubilus, J.K.2    Jeitner, T.M.3
  • 212
    • 25644445315 scopus 로고    scopus 로고
    • Cystamine treatment is neuroprotective in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk JM, Pearson J, Bailey CD, et al. Cystamine treatment is neuroprotective in the YAC128 mouse model of Huntington disease. J Neurochem. 2005; 95: 210-20.
    • (2005) J Neurochem. , vol.95 , pp. 210-220
    • Van Raamsdonk, J.M.1    Pearson, J.2    Bailey, C.D.3
  • 213
    • 33646248382 scopus 로고    scopus 로고
    • CYTE-I-HD: phase I dose finding and tolerability study of cysteamine (Cystagon) in Huntington's disease
    • Dubinsky R, Gray C. CYTE-I-HD: phase I dose finding and tolerability study of cysteamine (Cystagon) in Huntington's disease. Mov Disord. 2006; 21: 530-3.
    • (2006) Mov Disord. , vol.21 , pp. 530-533
    • Dubinsky, R.1    Gray, C.2
  • 214
    • 0037088677 scopus 로고    scopus 로고
    • The biochemistry of n-3 polyunsaturated fatty acids
    • Jump DB. The biochemistry of n-3 polyunsaturated fatty acids. J Biol Chem. 2002; 277: 8755-8.
    • (2002) J Biol Chem. , vol.277 , pp. 8755-8758
    • Jump, D.B.1
  • 216
    • 0037126988 scopus 로고    scopus 로고
    • Essential fatty acids given from conception prevent topographies of motor deficit in a transgenic model of Huntington's disease
    • Clifford JJ, Drago J, Natoli AL, et al. Essential fatty acids given from conception prevent topographies of motor deficit in a transgenic model of Huntington's disease. Neuroscience. 2002; 109: 81-8.
    • (2002) Neuroscience. , vol.109 , pp. 81-88
    • Clifford, J.J.1    Drago, J.2    Natoli, A.L.3
  • 217
    • 0037148140 scopus 로고    scopus 로고
    • A randomised, placebo-controlled, double blind study of treatment of Huntington's disease with unsaturated fatty acids
    • Vaddadi KS, Soosai E, Chiu E, et al A randomised, placebo-controlled, double blind study of treatment of Huntington's disease with unsaturated fatty acids. Neuroreport. 2002; 13: 29-33.
    • (2002) Neuroreport. , vol.13 , pp. 29-33
    • Vaddadi, K.S.1    Soosai, E.2    Chiu, E.3
  • 218
    • 27744478499 scopus 로고    scopus 로고
    • Ethyl-EPA treatment improves motor dysfunction, but not neurodegeneration in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk JM, Pearson J, Rogers DA, et al. Ethyl-EPA treatment improves motor dysfunction, but not neurodegeneration in the YAC128 mouse model of Huntington disease. Exp Neurol. 2005; 196: 266-72.
    • (2005) Exp Neurol. , vol.196 , pp. 266-272
    • Van Raamsdonk, J.M.1    Pearson, J.2    Rogers, D.A.3
  • 219
    • 0037148131 scopus 로고    scopus 로고
    • MRI and neuropsychological improvement in Huntington disease following ethyl-EPA treatment
    • Puri BK, Bydder GM, Counsell SJ, et al. MRI and neuropsychological improvement in Huntington disease following ethyl-EPA treatment. Neuroreport. 2002; 13: 123-6.
    • (2002) Neuroreport. , vol.13 , pp. 123-126
    • Puri, B.K.1    Bydder, G.M.2    Counsell, S.J.3
  • 220
    • 54449085055 scopus 로고    scopus 로고
    • Reduction in cerebral atrophy associated with ethyl-eicosapentaenoic acid treatment in patients with Huntington's disease
    • Puri BK, Bydder GM, Manku MS, et al. Reduction in cerebral atrophy associated with ethyl-eicosapentaenoic acid treatment in patients with Huntington's disease. J Int Med Res. 2008; 36: 896-905.
    • (2008) J Int Med Res. , vol.36 , pp. 896-905
    • Puri, B.K.1    Bydder, G.M.2    Manku, M.S.3
  • 221
    • 22544452137 scopus 로고    scopus 로고
    • Ethyl-EPA in Huntington disease: a double-blind, randomized, placebo-controlled trial
    • Puri BK, Leavitt BR, Hayden MR, et al. Ethyl-EPA in Huntington disease: a double-blind, randomized, placebo-controlled trial. Neurology. 2005; 65: 286-92.
    • (2005) Neurology. , vol.65 , pp. 286-292
    • Puri, B.K.1    Leavitt, B.R.2    Hayden, M.R.3
  • 222
    • 61449249687 scopus 로고    scopus 로고
    • Randomized controlled trial of ethyl-eicosapentaenoic acid in Huntington disease: the TREND-HD study
    • Huntington Study Group TREND-HD Investigators
    • Huntington Study Group TREND-HD Investigators. Randomized controlled trial of ethyl-eicosapentaenoic acid in Huntington disease: the TREND-HD study. Arch Neurol. 2008; 65: 1582-9.
    • (2008) Arch Neurol. , vol.65 , pp. 1582-1589
  • 223
    • 0035968856 scopus 로고    scopus 로고
    • Lipoic acid improves survival in transgenic mouse models of Huntington's disease
    • Andreassen OA, Ferrante RJ, Dedeoglu A, et al Lipoic acid improves survival in transgenic mouse models of Huntington's disease. Neuroreport. 2001; 12: 3371-3.
    • (2001) Neuroreport. , vol.12 , pp. 3371-3373
    • Andreassen, O.A.1    Ferrante, R.J.2    Dedeoglu, A.3
  • 224
    • 0037421494 scopus 로고    scopus 로고
    • Pyruvic acid cytoprotection against 1-methyl-4-phenylpyridinium, 6-hydroxydopamine and hydrogen peroxide toxicities in vitro
    • Mazzio E, Soliman KF. Pyruvic acid cytoprotection against 1-methyl-4-phenylpyridinium, 6-hydroxydopamine and hydrogen peroxide toxicities in vitro. Neurosci Lett. 2003; 337: 77-80.
    • (2003) Neurosci Lett. , vol.337 , pp. 77-80
    • Mazzio, E.1    Soliman, K.F.2
  • 225
    • 77950515496 scopus 로고    scopus 로고
    • Ethyl pyruvate has a neuroprotective effect through activation of extracellular signal-regulated kinase in Parkinson's disease model
    • Choi JS, Lee MS, Jeong JW. Ethyl pyruvate has a neuroprotective effect through activation of extracellular signal-regulated kinase in Parkinson's disease model. Biochem Biophys Res Commun. 2010; 394: 854-8.
    • (2010) Biochem Biophys Res Commun. , vol.394 , pp. 854-858
    • Choi, J.S.1    Lee, M.S.2    Jeong, J.W.3
  • 226
    • 0141560478 scopus 로고    scopus 로고
    • Neuroprotective effects of pyruvate in the quinolinic acid rat model of Huntington's disease
    • Ryu JK, Kim SU, McLarnon JG. Neuroprotective effects of pyruvate in the quinolinic acid rat model of Huntington's disease. Exp Neurol. 2003; 183: 700-4.
    • (2003) Exp Neurol. , vol.183 , pp. 700-704
    • Ryu, J.K.1    Kim, S.U.2    McLarnon, J.G.3
  • 227
    • 63649111659 scopus 로고    scopus 로고
    • Amino acids: metabolism, functions, and nutrition
    • Wu G. Amino acids: metabolism, functions, and nutrition. Amino Acids. 2009; 37: 1-17.
    • (2009) Amino Acids. , vol.37 , pp. 1-17
    • Wu, G.1
  • 228
    • 29244433508 scopus 로고    scopus 로고
    • Neuroprotective effect of taurine in 3-nitropropionic acid-induced experimental animal model of Huntington's disease phenotype
    • Tadros MG, Khalifa AE, Abdel-Naim AB, et al Neuroprotective effect of taurine in 3-nitropropionic acid-induced experimental animal model of Huntington's disease phenotype. Pharmacol Biochem Behav. 2005; 82: 574-82.
    • (2005) Pharmacol Biochem Behav. , vol.82 , pp. 574-582
    • Tadros, M.G.1    Khalifa, A.E.2    Abdel-Naim, A.B.3
  • 229
    • 0023638144 scopus 로고
    • Alpha-tocopherol and beta-carotene do not protect marmosets against the dopaminergic neurotoxicity of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
    • Perry TL, Yong VW, Hansen S, et al. Alpha-tocopherol and beta-carotene do not protect marmosets against the dopaminergic neurotoxicity of N-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine. J Neurol Sci. 1987; 81: 321-31.
    • (1987) J Neurol Sci. , vol.81 , pp. 321-331
    • Perry, T.L.1    Yong, V.W.2    Hansen, S.3
  • 230
    • 0027530638 scopus 로고
    • Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease
    • The Parkinson Study Group
    • The Parkinson Study Group. Effects of tocopherol and deprenyl on the progression of disability in early Parkinson's disease. N Engl J Med. 1993; 328: 176-83.
    • (1993) N Engl J Med. , vol.328 , pp. 176-183
  • 231
    • 0024500857 scopus 로고
    • Vitamin E attenuates the toxic effects of intrastriatal injection of 6-hydroxydopamine (6-OHDA) in rats: behavioral and biochemical evidence
    • Cadet JL, Katz M, Jackson-Lewis V, et al Vitamin E attenuates the toxic effects of intrastriatal injection of 6-hydroxydopamine (6-OHDA) in rats: behavioral and biochemical evidence. Brain Res. 1989; 476: 10-5.
    • (1989) Brain Res. , vol.476 , pp. 10-15
    • Cadet, J.L.1    Katz, M.2    Jackson-Lewis, V.3
  • 232
    • 77952099517 scopus 로고    scopus 로고
    • Alpha-tocopherol decreases iron-induced hippocampal and nigral neuron loss
    • Bostanci MO, Bas O, Bagirici F. Alpha-tocopherol decreases iron-induced hippocampal and nigral neuron loss. Cell Mol Neurobiol. 2010; 30: 389-94.
    • (2010) Cell Mol Neurobiol. , vol.30 , pp. 389-394
    • Bostanci, M.O.1    Bas, O.2    Bagirici, F.3
  • 233
    • 0026636491 scopus 로고
    • A pilot trial of high-dose alpha-tocopherol and ascorbate in early Parkinson's disease
    • Fahn S. A pilot trial of high-dose alpha-tocopherol and ascorbate in early Parkinson's disease. Ann Neurol. 1992; 32: S128-32.
    • (1992) Ann Neurol , vol.32
    • Fahn, S.1
  • 234
    • 0028856571 scopus 로고
    • Trial of d-alpha-tocopherol in Huntington's disease
    • Peyser CE, Folstein M, Chase GA, et al. Trial of d-alpha-tocopherol in Huntington's disease. Am J Psychiatry. 1995; 152: 1771-5.
    • (1995) Am J Psychiatry. , vol.152 , pp. 1771-1775
    • Peyser, C.E.1    Folstein, M.2    Chase, G.A.3
  • 235
    • 33745512853 scopus 로고    scopus 로고
    • gamma-Tocopherol attenuates MPTP-induced dopamine loss more efficiently than alpha-tocopherol in mouse brain
    • Itoh N, Masuo Y, Yoshida Y, et al. gamma-Tocopherol attenuates MPTP-induced dopamine loss more efficiently than alpha-tocopherol in mouse brain. Neurosci Lett. 2006; 403: 136-40.
    • (2006) Neurosci Lett. , vol.403 , pp. 136-140
    • Itoh, N.1    Masuo, Y.2    Yoshida, Y.3
  • 236
    • 0030956088 scopus 로고    scopus 로고
    • Protection against quinolinic acid-mediated excitotoxicity in nigrostriatal dopaminergic neurons by endogenous kynurenic acid
    • Miranda AF, Boegman RJ, Beninger RJ, et al Protection against quinolinic acid-mediated excitotoxicity in nigrostriatal dopaminergic neurons by endogenous kynurenic acid. Neuroscience. 1997; 78: 967-75.
    • (1997) Neuroscience. , vol.78 , pp. 967-975
    • Miranda, A.F.1    Boegman, R.J.2    Beninger, R.J.3
  • 237
    • 0031836667 scopus 로고    scopus 로고
    • Modulation of striatal quinolinate neurotoxicity by elevation of endogenous brain kynurenic acid
    • Harris CA, Miranda AF, Tanguay JJ, et al. Modulation of striatal quinolinate neurotoxicity by elevation of endogenous brain kynurenic acid. Br J Pharmacol. 1998; 124: 391-9.
    • (1998) Br J Pharmacol. , vol.124 , pp. 391-399
    • Harris, C.A.1    Miranda, A.F.2    Tanguay, J.J.3
  • 238
    • 0026535226 scopus 로고
    • Neuroprotective effects of L-kynurenine on hypoxia-ischemia and NMDA lesions in neonatal rats
    • Nozaki K, Beal MF. Neuroprotective effects of L-kynurenine on hypoxia-ischemia and NMDA lesions in neonatal rats. J Cereb Blood Flow Metab. 1992; 12: 400-7.
    • (1992) J Cereb Blood Flow Metab. , vol.12 , pp. 400-407
    • Nozaki, K.1    Beal, M.F.2
  • 239
    • 34250625265 scopus 로고    scopus 로고
    • Neuroprotective effect of L-kynurenine sulfate administered before focal cerebral ischemia in mice and global cerebral ischemia in gerbils
    • Gigler G, Szenasi G, Simo A, et al. Neuroprotective effect of L-kynurenine sulfate administered before focal cerebral ischemia in mice and global cerebral ischemia in gerbils. Eur J Pharmacol. 2007; 564: 116-22.
    • (2007) Eur J Pharmacol. , vol.564 , pp. 116-122
    • Gigler, G.1    Szenasi, G.2    Simo, A.3
  • 240
    • 33947546552 scopus 로고    scopus 로고
    • Kynurenine in combination with probenecid mitigates the stimulation-induced increase of c-fos immunoreactivity of the rat caudal trigeminal nucleus in an experimental migraine model
    • Knyihar-Csillik E, Toldi J, Mihaly A, et al. Kynurenine in combination with probenecid mitigates the stimulation-induced increase of c-fos immunoreactivity of the rat caudal trigeminal nucleus in an experimental migraine model. J Neural Transm. 2007; 114: 417-21.
    • (2007) J Neural Transm. , vol.114 , pp. 417-421
    • Knyihar-Csillik, E.1    Toldi, J.2    Mihaly, A.3
  • 241
    • 70349481060 scopus 로고    scopus 로고
    • Modulatory effects of probenecid on the nitroglycerin-induced changes in the rat caudal trigeminal nucleus
    • Vamos E, Pardutz A, Fejes A, et al. Modulatory effects of probenecid on the nitroglycerin-induced changes in the rat caudal trigeminal nucleus. Eur J Pharmacol. 2009; 621: 33-7.
    • (2009) Eur J Pharmacol. , vol.621 , pp. 33-37
    • Vamos, E.1    Pardutz, A.2    Fejes, A.3
  • 242
    • 69549114430 scopus 로고    scopus 로고
    • Neuroprotective effects of probenecid in a transgenic animal model of Huntington's disease
    • Vamos E, Voros K, Zadori D, et al. Neuroprotective effects of probenecid in a transgenic animal model of Huntington's disease. J Neural Transm. 2009; 116: 1079-86.
    • (2009) J Neural Transm. , vol.116 , pp. 1079-1086
    • Vamos, E.1    Voros, K.2    Zadori, D.3
  • 243
    • 17144446935 scopus 로고
    • Injection of excitatory amino acid antagonists into the medial pallidal segment of a 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) treated primate reverses motor symptoms of parkinsonism
    • Graham WC, Robertson RG, Sambrook MA, et al Injection of excitatory amino acid antagonists into the medial pallidal segment of a 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) treated primate reverses motor symptoms of parkinsonism. Life Sci. 1990; 47: PL91-7.
    • (1990) Life Sci , vol.47
    • Graham, W.C.1    Robertson, R.G.2    Sambrook, M.A.3
  • 244
    • 0002051255 scopus 로고    scopus 로고
    • The effects of reversible inactivation of the subthalamo-pallidal pathway on the behaviour of naive and hemiparkinsonian monkeys
    • Butler EG, Bourke DW, Finkelstein DI, et al The effects of reversible inactivation of the subthalamo-pallidal pathway on the behaviour of naive and hemiparkinsonian monkeys. J Clin Neurosci. 1997; 4: 218-27.
    • (1997) J Clin Neurosci. , vol.4 , pp. 218-227
    • Butler, E.G.1    Bourke, D.W.2    Finkelstein, D.I.3
  • 245
    • 26844476662 scopus 로고    scopus 로고
    • Murine renal organic anion transporters mOAT1 and mOAT3 facilitate the transport of neuroactive tryptophan metabolites
    • Bahn A, Ljubojevic M, Lorenz H, et al. Murine renal organic anion transporters mOAT1 and mOAT3 facilitate the transport of neuroactive tryptophan metabolites. Am J Physiol Cell Physiol. 2005; 289: C1075-84.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Bahn, A.1    Ljubojevic, M.2    Lorenz, H.3
  • 246
    • 0034176154 scopus 로고    scopus 로고
    • Development and therapeutic potential of kynurenic acid and kynurenine derivatives for neuroprotection
    • Stone TW. Development and therapeutic potential of kynurenic acid and kynurenine derivatives for neuroprotection. Trends Pharmacol Sci. 2000; 21: 149-54.
    • (2000) Trends Pharmacol Sci. , vol.21 , pp. 149-154
    • Stone, T.W.1
  • 247
    • 0742323784 scopus 로고    scopus 로고
    • The kynurenine pathway of tryptophan degradation as a drug target
    • Schwarcz R. The kynurenine pathway of tryptophan degradation as a drug target. Curr Opin Pharmacol. 2004; 4: 12-7.
    • (2004) Curr Opin Pharmacol. , vol.4 , pp. 12-17
    • Schwarcz, R.1
  • 248
    • 71949108894 scopus 로고    scopus 로고
    • Syntheses, transformations and pharmaceutical applications of kynurenic acid derivatives
    • Fulop F, Szatmari I, Vamos E, et al. Syntheses, transformations and pharmaceutical applications of kynurenic acid derivatives. Curr Med Chem. 2009; 16: 4828-42.
    • (2009) Curr Med Chem. , vol.16 , pp. 4828-4842
    • Fulop, F.1    Szatmari, I.2    Vamos, E.3
  • 249
    • 0032778037 scopus 로고    scopus 로고
    • The non-NMDA glutamate receptor antagonists 6-cyano-7-nitroquinoxaline-2,3-dione and 2,3-dihydroxy-6-nitro-7-sulfamoylbenzo(f)quinoxaline, but not NMDA antagonists, block the intrastriatal neurotoxic effect of MPP+
    • Merino M, Vizuete ML, Cano J, et al The non-NMDA glutamate receptor antagonists 6-cyano-7-nitroquinoxaline-2, 3-dione and 2, 3-dihydroxy-6-nitro-7-sulfamoylbenzo(f)quinoxaline, but not NMDA antagonists, block the intrastriatal neurotoxic effect of MPP+. J Neurochem. 1999; 73: 750-7.
    • (1999) J Neurochem. , vol.73 , pp. 750-757
    • Merino, M.1    Vizuete, M.L.2    Cano, J.3
  • 250
    • 0034024706 scopus 로고    scopus 로고
    • In situ produced 7-chlorokynurenate provides protection against quinolinate-and malonate-induced neurotoxicity in the rat striatum
    • Guidetti P, Wu HQ, Schwarcz R. In situ produced 7-chlorokynurenate provides protection against quinolinate-and malonate-induced neurotoxicity in the rat striatum. Exp Neurol. 2000; 163: 123-30.
    • (2000) Exp Neurol. , vol.163 , pp. 123-130
    • Guidetti, P.1    Wu, H.Q.2    Schwarcz, R.3
  • 251
    • 0019294951 scopus 로고
    • Metabolism of 6-chlorotryptophan to 4-chloro-3-hydroxyanthranilic acid: a potent inhibitor of 3-hydroxyanthranilic acid oxidase
    • Parli CJ, Krieter P, Schmidt B. Metabolism of 6-chlorotryptophan to 4-chloro-3-hydroxyanthranilic acid: a potent inhibitor of 3-hydroxyanthranilic acid oxidase. Arch Biochem Biophys. 1980; 203: 161-6.
    • (1980) Arch Biochem Biophys. , vol.203 , pp. 161-166
    • Parli, C.J.1    Krieter, P.2    Schmidt, B.3
  • 252
    • 0025740632 scopus 로고
    • Kynurenic acid derivatives. Structure-activity relationships for excitatory amino acid antagonism and identification of potent and selective antagonists at the glycine site on the N-methyl-D-aspartate receptor
    • Leeson PD, Baker R, Carling RW, et al. Kynurenic acid derivatives. Structure-activity relationships for excitatory amino acid antagonism and identification of potent and selective antagonists at the glycine site on the N-methyl-D-aspartate receptor. J Med Chem. 1991; 34: 1243-52.
    • (1991) J Med Chem. , vol.34 , pp. 1243-1252
    • Leeson, P.D.1    Baker, R.2    Carling, R.W.3
  • 253
    • 33846089855 scopus 로고    scopus 로고
    • Kynurenic acid amides as novel NR2B selective NMDA receptor antagonists
    • Borza I, Kolok S, Galgoczy K, et al. Kynurenic acid amides as novel NR2B selective NMDA receptor antagonists. Bioorg Med Chem Lett. 2007; 17: 406-9.
    • (2007) Bioorg Med Chem Lett. , vol.17 , pp. 406-409
    • Borza, I.1    Kolok, S.2    Galgoczy, K.3
  • 254
    • 77951836040 scopus 로고    scopus 로고
    • Kynurenate derivative attenuates the nitroglycerin-induced CamKIIalpha and CGRP expression changes
    • Vamos E, Fejes A, Koch J, et al. Kynurenate derivative attenuates the nitroglycerin-induced CamKIIalpha and CGRP expression changes. Headache. 2010; 50: 834-43.
    • (2010) Headache. , vol.50 , pp. 834-843
    • Vamos, E.1    Fejes, A.2    Koch, J.3
  • 255
    • 77249133018 scopus 로고    scopus 로고
    • A novel kynurenic acid analogue: a comparison with kynurenic acid. An in vitro electrophysiological study
    • Marosi M, Nagy D, Farkas T, et al. A novel kynurenic acid analogue: a comparison with kynurenic acid. An in vitro electrophysiological study. J Neural Transm. 2010; 117: 183-8.
    • (2010) J Neural Transm. , vol.117 , pp. 183-188
    • Marosi, M.1    Nagy, D.2    Farkas, T.3
  • 256
    • 79955661135 scopus 로고    scopus 로고
    • Neuroprotective effects of a novel kynurenic acid analogue in a transgenic mouse model of Huntington's disease
    • Zadori D, Nyiri G, Szonyi A, et al. Neuroprotective effects of a novel kynurenic acid analogue in a transgenic mouse model of Huntington's disease. J Neural Transm. 2011; DOI: .
    • (2011) J Neural Transm
    • Zadori, D.1    Nyiri, G.2    Szonyi, A.3


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