메뉴 건너뛰기




Volumn 14, Issue 8, 2010, Pages 2045-2054

Kynurenines, neurodegeneration and Alzheimer's disease

Author keywords

Alzheimer; Glutamate excitotoxicity; Kynurenine; Neuroinflammation; Oxidative stress

Indexed keywords

AMYLOID BETA PROTEIN; KYNURENINE; QUINOLINIC ACID; TRYPTOPHAN;

EID: 77957131120     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2010.01123.x     Document Type: Article
Times cited : (61)

References (150)
  • 1
    • 71849109645 scopus 로고    scopus 로고
    • Alzheimer's disease: a global challenge for the 21st century
    • Dartigues JF. Alzheimer's disease: a global challenge for the 21st century. Lancet Neurol 2009, 8:1082-3.
    • (2009) Lancet Neurol , vol.8 , pp. 1082-1083
    • Dartigues, J.F.1
  • 3
    • 0034859054 scopus 로고    scopus 로고
    • Are Alzheimer's disease patients able to learn visual prototypes
    • Keri S, Kalman J, Kelemen O. Are Alzheimer's disease patients able to learn visual prototypes. Neuropsychologia 2001, 39:1218-23.
    • (2001) Neuropsychologia , vol.39 , pp. 1218-1223
    • Keri, S.1    Kalman, J.2    Kelemen, O.3
  • 4
    • 0036190980 scopus 로고    scopus 로고
    • Corticostriatal circuitry mediates fast-track visual categorization
    • Antal A, Keri S, Kincses T. Corticostriatal circuitry mediates fast-track visual categorization. Brain Res Cogn Brain Res 2002, 13:53-9.
    • (2002) Brain Res Cogn Brain Res , vol.13 , pp. 53-59
    • Antal, A.1    Keri, S.2    Kincses, T.3
  • 5
    • 75149190080 scopus 로고    scopus 로고
    • Temporal parameters of spontaneous speech in Alzheimer's disease
    • Hoffmann I, Nemeth D, Dye CD. Temporal parameters of spontaneous speech in Alzheimer's disease. Int J Speech Lang Pathol 2010, 12:29-34.
    • (2010) Int J Speech Lang Pathol , vol.12 , pp. 29-34
    • Hoffmann, I.1    Nemeth, D.2    Dye, C.D.3
  • 6
    • 11144355971 scopus 로고    scopus 로고
    • Relational integration and executive function in Alzheimer's disease
    • Waltz JA, Knowlton BJ, Holyoak KJ. Relational integration and executive function in Alzheimer's disease. Neuropsychology 2004, 18:296-305.
    • (2004) Neuropsychology , vol.18 , pp. 296-305
    • Waltz, J.A.1    Knowlton, B.J.2    Holyoak, K.J.3
  • 7
    • 0033093822 scopus 로고    scopus 로고
    • The deterioration of semantic memory in Alzheimer's disease
    • Salmon DP, Butters N, Chan AS. The deterioration of semantic memory in Alzheimer's disease. Can J Exp Psychol 1999, 53:108-17.
    • (1999) Can J Exp Psychol , vol.53 , pp. 108-117
    • Salmon, D.P.1    Butters, N.2    Chan, A.S.3
  • 8
    • 57749171545 scopus 로고    scopus 로고
    • Anatomically-distinct genetic associations of APOE epsilon4 allele load with regional cortical atrophy in Alzheimer's disease
    • Filippini N, Rao A, Wetten S. Anatomically-distinct genetic associations of APOE epsilon4 allele load with regional cortical atrophy in Alzheimer's disease. Neuroimage 2009, 44:724-8.
    • (2009) Neuroimage , vol.44 , pp. 724-728
    • Filippini, N.1    Rao, A.2    Wetten, S.3
  • 9
    • 70349959901 scopus 로고    scopus 로고
    • Combining shape and connectivity analysis: an MRI study of thalamic degeneration in Alzheimer's disease
    • Zarei M, Patenaude B, Damoiseaux J. Combining shape and connectivity analysis: an MRI study of thalamic degeneration in Alzheimer's disease. Neuroimage 2010, 49:1-8.
    • (2010) Neuroimage , vol.49 , pp. 1-8
    • Zarei, M.1    Patenaude, B.2    Damoiseaux, J.3
  • 10
    • 62449343163 scopus 로고    scopus 로고
    • Regional white matter integrity differentiates between vascular dementia and Alzheimer disease
    • Zarei M, Damoiseaux JS, Morgese C. Regional white matter integrity differentiates between vascular dementia and Alzheimer disease. Stroke 2009, 40:773-9.
    • (2009) Stroke , vol.40 , pp. 773-779
    • Zarei, M.1    Damoiseaux, J.S.2    Morgese, C.3
  • 11
    • 34347228646 scopus 로고    scopus 로고
    • Longitudinal and cross-sectional analysis of atrophy in Alzheimer's disease: cross-validation of BSI, SIENA and SIENAX
    • Smith SM, Rao A, De Stefano N. Longitudinal and cross-sectional analysis of atrophy in Alzheimer's disease: cross-validation of BSI, SIENA and SIENAX. Neuroimage 2007, 36:1200-6.
    • (2007) Neuroimage , vol.36 , pp. 1200-1206
    • Smith, S.M.1    Rao, A.2    De Stefano, N.3
  • 12
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 1984, 122:1131-5.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 13
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984, 120:885-90.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 14
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • Masters CL, Simms G, Weinman NA. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc Natl Acad Sci USA 1985, 82:4245-9.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4245-4249
    • Masters, C.L.1    Simms, G.2    Weinman, N.A.3
  • 15
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire HG, Unterbeck A. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987, 325:733-6.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 16
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D, Lerman MI, McBride OW. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 1987, 235:877-80.
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3
  • 17
    • 0023109592 scopus 로고
    • Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus
    • Tanzi RE, Gusella JF, Watkins PC. Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus. Science 1987, 235:880-4.
    • (1987) Science , vol.235 , pp. 880-884
    • Tanzi, R.E.1    Gusella, J.F.2    Watkins, P.C.3
  • 18
    • 2142777413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides
    • Robakis NK, Ramakrishna N, Wolfe G. Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides. Proc Natl Acad Sci USA 1987, 84:4190-4.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4190-4194
    • Robakis, N.K.1    Ramakrishna, N.2    Wolfe, G.3
  • 19
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D, Eckman C, Jensen M. Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat Med 1996, 2:864-70.
    • (1996) Nat Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 20
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate A, Chartier-Harlin MC, Mullan M. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991, 349:704-6.
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3
  • 21
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid
    • Mullan M, Crawford F, Axelman K. A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid. Nat Genet 1992, 1:345-7.
    • (1992) Nat Genet , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3
  • 22
    • 0026894414 scopus 로고
    • Framing beta-amyloid
    • Hardy J. Framing beta-amyloid. Nat Genet 1992, 1:233-4.
    • (1992) Nat Genet , vol.1 , pp. 233-234
    • Hardy, J.1
  • 23
    • 0026879650 scopus 로고
    • Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene
    • Hendriks L, van Duijn CM, Cras P. Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene. Nat Genet 1992, 1:218-21.
    • (1992) Nat Genet , vol.1 , pp. 218-221
    • Hendriks, L.1    van Duijn, C.M.2    Cras, P.3
  • 24
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor
    • Haass C, Hung AY, Selkoe DJ. Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor. J Biol Chem 1994, 269:17741-8.
    • (1994) J Biol Chem , vol.269 , pp. 17741-17748
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3
  • 25
    • 67651180986 scopus 로고    scopus 로고
    • The amyloid hypothesis for Alzheimer's disease: a critical reappraisal
    • Hardy J. The amyloid hypothesis for Alzheimer's disease: a critical reappraisal. J Neurochem 2009, 110:1129-34.
    • (2009) J Neurochem , vol.110 , pp. 1129-1134
    • Hardy, J.1
  • 26
    • 67650178847 scopus 로고    scopus 로고
    • The role of kynurenines in disorders of the central nervous system: possibilities for neuroprotection
    • Vamos E, Pardutz A, Klivenyi P. The role of kynurenines in disorders of the central nervous system: possibilities for neuroprotection. J Neurol Sci 2009, 283:21-7.
    • (2009) J Neurol Sci , vol.283 , pp. 21-27
    • Vamos, E.1    Pardutz, A.2    Klivenyi, P.3
  • 27
    • 70449523216 scopus 로고    scopus 로고
    • Kynurenines in chronic neurodegenerative disorders: future therapeutic strategies
    • Zadori D, Klivenyi P, Vamos E. 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    Vamos, E.3
  • 28
    • 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. 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
  • 29
    • 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. 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
  • 30
    • 0023783911 scopus 로고
    • Kynurenic acid antagonises responses to NMDA via an action at the strychnine-insensitive glycine receptor
    • Birch PJ, Grossman CJ, Hayes AG. Kynurenic acid antagonises responses to NMDA via an action at the strychnine-insensitive glycine receptor. Eur J Pharmacol 1988, 154:85-7.
    • (1988) Eur J Pharmacol , vol.154 , pp. 85-87
    • Birch, P.J.1    Grossman, C.J.2    Hayes, A.G.3
  • 31
    • 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
  • 32
    • 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. 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    Alkondon, M.3
  • 34
    • 0020702374 scopus 로고
    • Quinolinic acid: an endogenous metabolite that produces axon-sparing lesions in rat brain
    • Schwarcz R, Whetsell WO, 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, W.O.2    Mangano, R.M.3
  • 35
    • 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
  • 36
    • 0036128148 scopus 로고    scopus 로고
    • Quinolinic acid stimulates synaptosomal glutamate release and inhibits glutamate uptake into astrocytes
    • Tavares RG, Tasca CI, Santos CE. 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
  • 37
    • 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
  • 38
    • 0035953168 scopus 로고    scopus 로고
    • Quinolinic acid induces oxidative stress in rat brain synaptosomes
    • Santamaria A, Galvan-Arzate S, Lisy V. Quinolinic acid induces oxidative stress in rat brain synaptosomes. Neuroreport 2001, 12:871-4.
    • (2001) Neuroreport , vol.12 , pp. 871-874
    • Santamaria, A.1    Galvan-Arzate, S.2    Lisy, V.3
  • 39
    • 0024384702 scopus 로고
    • Cytotoxicity of 3-hydroxykynurenine in a neuronal hybrid cell line
    • Eastman CL, Guilarte TR. Cytotoxicity of 3-hydroxykynurenine in a neuronal hybrid cell line. Brain Res 1989, 495:225-31.
    • (1989) Brain Res , vol.495 , pp. 225-231
    • Eastman, C.L.1    Guilarte, T.R.2
  • 40
    • 0030018558 scopus 로고    scopus 로고
    • 3-Hydroxykynurenine toxicity on the rat striatum in vivo
    • Nakagami Y, Saito H, Katsuki H. 3-Hydroxykynurenine toxicity on the rat striatum in vivo. Jpn J Pharmacol 1996, 71:183-6.
    • (1996) Jpn J Pharmacol , vol.71 , pp. 183-186
    • Nakagami, Y.1    Saito, H.2    Katsuki, H.3
  • 41
    • 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
  • 42
    • 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. 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
  • 43
    • 0034894035 scopus 로고    scopus 로고
    • Kynurenine pathway metabolism in human astrocytes: a paradox for neuronal protection
    • Guillemin GJ, Kerr SJ, Smythe GA. 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.3
  • 44
    • 23044462498 scopus 로고    scopus 로고
    • Indoleamine 2,3 dioxygenase and quinolinic acid immunoreactivity in Alzheimer's disease hippocampus
    • Guillemin GJ, Brew BJ, Noonan CE. Indoleamine 2,3 dioxygenase and quinolinic acid immunoreactivity in Alzheimer's disease hippocampus. Neuropathol Appl Neurobiol 2005, 31:395-404.
    • (2005) Neuropathol Appl Neurobiol , vol.31 , pp. 395-404
    • Guillemin, G.J.1    Brew, B.J.2    Noonan, C.E.3
  • 45
    • 75849150001 scopus 로고    scopus 로고
    • Structure, expression, and function of kynurenine aminotransferases in human and rodent brains
    • Han Q, Cai T, Tagle DA. 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
  • 46
    • 34250156019 scopus 로고    scopus 로고
    • Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain
    • Guidetti P, Amori L, Sapko MT. 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
  • 47
    • 11244258182 scopus 로고    scopus 로고
    • PH dependence, substrate specificity and inhibition of human kynurenine aminotransferase I
    • Han Q, Li J. pH dependence, substrate specificity and inhibition of human kynurenine aminotransferase I. Eur J Biochem 2004, 271:4804-14.
    • (2004) Eur J Biochem , vol.271 , pp. 4804-4814
    • Han, Q.1    Li, J.2
  • 48
    • 65649107268 scopus 로고    scopus 로고
    • Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K
    • Han Q, Robinson H, Cai T. Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K. J Med Chem 2009, 52:2786-93.
    • (2009) J Med Chem , vol.52 , pp. 2786-2793
    • Han, Q.1    Robinson, H.2    Cai, T.3
  • 49
    • 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. 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    Melendez-Ferro, M.3
  • 50
    • 0026476185 scopus 로고
    • Immunocytochemical localization of kynurenine aminotransferase in the rat striatum: a light and electron microscopic study
    • Roberts RC, Du F, McCarthy KE. 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.3
  • 51
    • 0036110361 scopus 로고    scopus 로고
    • Immunogold localization of mitochondrial aspartate aminotransferase in mitochondria and on the cell surface in normal rat tissues
    • Cechetto JD, Sadacharan SK, Berk PD. Immunogold localization of mitochondrial aspartate aminotransferase in mitochondria and on the cell surface in normal rat tissues. Histol Histopathol 2002, 17:353-64.
    • (2002) Histol Histopathol , vol.17 , pp. 353-364
    • Cechetto, J.D.1    Sadacharan, S.K.2    Berk, P.D.3
  • 52
    • 0035165356 scopus 로고    scopus 로고
    • Immunohistochemical visualization of newly formed quinolinate in the normal and excitotoxically lesioned rat striatum
    • Lehrmann E, Molinari A, Speciale C. Immunohistochemical visualization of newly formed quinolinate in the normal and excitotoxically lesioned rat striatum. Exp Brain Res 2001, 141:389-97.
    • (2001) Exp Brain Res , vol.141 , pp. 389-397
    • Lehrmann, E.1    Molinari, A.2    Speciale, C.3
  • 53
    • 0023860251 scopus 로고
    • Quinolinic acid metabolism in the rat brain. Immunohistochemical identification of 3-hydroxyanthranilic acid oxygenase and quinolinic acid phosphoribosyltransferase in the hippocampal region
    • Kohler C, Eriksson LG, Flood PR. Quinolinic acid metabolism in the rat brain. Immunohistochemical identification of 3-hydroxyanthranilic acid oxygenase and quinolinic acid phosphoribosyltransferase in the hippocampal region. J Neurosci 1988, 8:975-87.
    • (1988) J Neurosci , vol.8 , pp. 975-987
    • Kohler, C.1    Eriksson, L.G.2    Flood, P.R.3
  • 54
    • 0028931873 scopus 로고
    • 3-Hydroxyanthranilic acid oxygenase-containing astrocytic processes surround glutamate-containing axon terminals in the rat striatum
    • Roberts RC, McCarthy KE, Du F. 3-Hydroxyanthranilic acid oxygenase-containing astrocytic processes surround glutamate-containing axon terminals in the rat striatum. J Neurosci 1995, 15:1150-61.
    • (1995) J Neurosci , vol.15 , pp. 1150-1161
    • Roberts, R.C.1    McCarthy, K.E.2    Du, F.3
  • 55
  • 56
    • 22144432194 scopus 로고    scopus 로고
    • Role of kynurenines in the central and peripheral nervous systems
    • Nemeth H, Toldi J, Vecsei L. Role of kynurenines in the central and peripheral nervous systems. Curr Neurovasc Res 2005, 2:249-60.
    • (2005) Curr Neurovasc Res , vol.2 , pp. 249-260
    • Nemeth, H.1    Toldi, J.2    Vecsei, L.3
  • 57
    • 0027123158 scopus 로고
    • Kynurenine and its metabolites in nervous system diseases
    • Vecsei L, Schwab F. Kynurenine and its metabolites in nervous system diseases. Orv Hetil 1992, 133:1803-7.
    • (1992) Orv Hetil , vol.133 , pp. 1803-1807
    • Vecsei, L.1    Schwab, F.2
  • 58
    • 0342592253 scopus 로고    scopus 로고
    • Huntington's disease, behavioral disturbances, and kynurenines: preclinical findings and therapeutic perspectives
    • Vecsei L, Beal MF. Huntington's disease, behavioral disturbances, and kynurenines: preclinical findings and therapeutic perspectives. Biol Psychiatry 1996, 39:1061-3.
    • (1996) Biol Psychiatry , vol.39 , pp. 1061-1063
    • Vecsei, L.1    Beal, M.F.2
  • 59
    • 33750347713 scopus 로고    scopus 로고
    • Kynurenines, Parkinson's disease and other neurodegenerative disorders: preclinical and clinical studies
    • Nemeth H, Toldi J, Vecsei L. Kynurenines, Parkinson's disease and other neurodegenerative disorders: preclinical and clinical studies. J Neural Transm Suppl 2006, 285-304.
    • (2006) J Neural Transm Suppl , pp. 285-304
    • Nemeth, H.1    Toldi, J.2    Vecsei, L.3
  • 60
    • 27744509130 scopus 로고    scopus 로고
    • Kynurenine metabolism in plasma and in red blood cells in Parkinson's disease
    • Hartai Z, Klivenyi P, Janaky T. Kynurenine metabolism in plasma and in red blood cells in Parkinson's disease. J Neurol Sci 2005, 239:31-5.
    • (2005) J Neurol Sci , vol.239 , pp. 31-35
    • Hartai, Z.1    Klivenyi, P.2    Janaky, T.3
  • 61
    • 63349083606 scopus 로고    scopus 로고
    • Neuroprotection in Parkinson's disease and other neurodegenerative disorders: preclinical and clinical findings
    • Rakoczi K, Klivenyi P, Vecsei L. Neuroprotection in Parkinson's disease and other neurodegenerative disorders: preclinical and clinical findings. Ideggyogy Sz 2009, 62:25-34.
    • (2009) Ideggyogy Sz , vol.62 , pp. 25-34
    • Rakoczi, K.1    Klivenyi, P.2    Vecsei, L.3
  • 62
    • 80053213044 scopus 로고    scopus 로고
    • Pharmacological therapy in Parkinson's disease: focus on neuroprotection
    • DOI: 10.1111/j.1755-5949.2010.00150.x
    • Kincses ZT, Vecsei L. Pharmacological therapy in Parkinson's disease: focus on neuroprotection. CNS Neurosci Ther 2010, 10.1111/j.1755-5949.2010.00150.x, DOI
    • (2010) CNS Neurosci Ther
    • Kincses, Z.T.1    Vecsei, L.2
  • 63
  • 64
    • 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
  • 65
    • 34248645158 scopus 로고    scopus 로고
    • Peripheral kynurenine metabolism in focal dystonia
    • Hartai Z, Klivenyi P, Janaky T. Peripheral kynurenine metabolism in focal dystonia. Med Chem 2007, 3:285-8.
    • (2007) Med Chem , vol.3 , pp. 285-288
    • Hartai, Z.1    Klivenyi, P.2    Janaky, T.3
  • 66
    • 1542512479 scopus 로고    scopus 로고
    • Kynurenine aminotransferase in the supratentorial dura mater of the rat: effect of stimulation of the trigeminal ganglion
    • Knyihar-Csillik E, Chadaide Z, Okuno E. Kynurenine aminotransferase in the supratentorial dura mater of the rat: effect of stimulation of the trigeminal ganglion. Exp Neurol 2004, 186:242-7.
    • (2004) Exp Neurol , vol.186 , pp. 242-247
    • Knyihar-Csillik, E.1    Chadaide, Z.2    Okuno, E.3
  • 67
    • 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. 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
  • 68
    • 68749117393 scopus 로고    scopus 로고
    • L-kynurenine combined with probenecid and the novel synthetic kynurenic acid derivative attenuate nitroglycerin-induced nNOS in the rat caudal trigeminal nucleus
    • Vamos E, Pardutz A, Varga H. l-kynurenine combined with probenecid and the novel synthetic kynurenic acid derivative attenuate nitroglycerin-induced nNOS in the rat caudal trigeminal nucleus. Neuropharmacology 2009, 57:425-9.
    • (2009) Neuropharmacology , vol.57 , pp. 425-429
    • Vamos, E.1    Pardutz, A.2    Varga, H.3
  • 69
    • 34247343347 scopus 로고    scopus 로고
    • Prevention of electrical stimulation-induced increase of c-fos immunoreaction in the caudal trigeminal nucleus by kynurenine combined with probenecid
    • Knyihar-Csillik E, Toldi J, Krisztin-Peva B. Prevention of electrical stimulation-induced increase of c-fos immunoreaction in the caudal trigeminal nucleus by kynurenine combined with probenecid. Neurosci Lett 2007, 418:122-6.
    • (2007) Neurosci Lett , vol.418 , pp. 122-126
    • Knyihar-Csillik, E.1    Toldi, J.2    Krisztin-Peva, B.3
  • 70
    • 0034106148 scopus 로고    scopus 로고
    • Tryptophan degradation and immune activation in Alzheimer's disease
    • Widner B, Leblhuber F, Walli J. Tryptophan degradation and immune activation in Alzheimer's disease. J Neural Transm 2000, 107:343-53.
    • (2000) J Neural Transm , vol.107 , pp. 343-353
    • Widner, B.1    Leblhuber, F.2    Walli, J.3
  • 71
    • 0033058001 scopus 로고    scopus 로고
    • Kynurenine metabolism in Alzheimer's disease
    • Baran H, Jellinger K, Deecke L. Kynurenine metabolism in Alzheimer's disease. J Neural Transm 1999, 106:165-81.
    • (1999) J Neural Transm , vol.106 , pp. 165-181
    • Baran, H.1    Jellinger, K.2    Deecke, L.3
  • 72
    • 0032566190 scopus 로고    scopus 로고
    • Increased aspartate aminotransferase activity in cerebrospinal fluid and Alzheimer's disease
    • Tapiola T, Lehtovirta M, Pirttila T. Increased aspartate aminotransferase activity in cerebrospinal fluid and Alzheimer's disease. Lancet 1998, 352:287.
    • (1998) Lancet , vol.352 , pp. 287
    • Tapiola, T.1    Lehtovirta, M.2    Pirttila, T.3
  • 73
    • 33846228447 scopus 로고    scopus 로고
    • Decreased serum and red blood cell kynurenic acid levels in Alzheimer's disease
    • Hartai Z, Juhasz A, Rimanoczy A. Decreased serum and red blood cell kynurenic acid levels in Alzheimer's disease. Neurochem Int 2007, 50:308-13.
    • (2007) Neurochem Int , vol.50 , pp. 308-313
    • Hartai, Z.1    Juhasz, A.2    Rimanoczy, A.3
  • 74
    • 0026539659 scopus 로고
    • Quinolinic acid and kynurenine pathway metabolism in inflammatory and non-inflammatory neurological disease
    • Heyes MP, Saito K, Crowley JS. 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
  • 76
    • 1042291136 scopus 로고    scopus 로고
    • Quinolinic acid in the pathogenesis of Alzheimer's disease
    • Guillemin GJ, Williams KR, Smith DG. Quinolinic acid in the pathogenesis of Alzheimer's disease. Adv Exp Med Biol 2003, 527:167-76.
    • (2003) Adv Exp Med Biol , vol.527 , pp. 167-176
    • Guillemin, G.J.1    Williams, K.R.2    Smith, D.G.3
  • 77
    • 2342507918 scopus 로고    scopus 로고
    • A beta 1-42 induces production of quinolinic acid by human macrophages and microglia
    • Guillemin GJ, Smythe GA, Veas LA. A beta 1-42 induces production of quinolinic acid by human macrophages and microglia. Neuroreport 2003, 14:2311-5.
    • (2003) Neuroreport , vol.14 , pp. 2311-2315
    • Guillemin, G.J.1    Smythe, G.A.2    Veas, L.A.3
  • 78
    • 0035341254 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in Alzheimer's disease
    • Hirai K, Aliev G, Nunomura A. Mitochondrial abnormalities in Alzheimer's disease. J Neurosci 2001, 21:3017-23.
    • (2001) J Neurosci , vol.21 , pp. 3017-3023
    • Hirai, K.1    Aliev, G.2    Nunomura, A.3
  • 79
    • 33644845279 scopus 로고    scopus 로고
    • Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease
    • Reddy PH. Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease. J Neurochem 2006, 96:1-13.
    • (2006) J Neurochem , vol.96 , pp. 1-13
    • Reddy, P.H.1
  • 80
    • 24644511602 scopus 로고    scopus 로고
    • Oxidative imbalance in Alzheimer's disease
    • Zhu X, Lee HG, Casadesus G. Oxidative imbalance in Alzheimer's disease. Mol Neurobiol 2005, 31:205-17.
    • (2005) Mol Neurobiol , vol.31 , pp. 205-217
    • Zhu, X.1    Lee, H.G.2    Casadesus, G.3
  • 81
    • 0028180518 scopus 로고
    • A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease
    • Hensley K, Carney JM, Mattson MP. A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc Natl Acad Sci USA 1994, 91:3270-4.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3270-3274
    • Hensley, K.1    Carney, J.M.2    Mattson, M.P.3
  • 82
    • 0034613438 scopus 로고    scopus 로고
    • Reduced antioxidant enzyme activity in brains of mice transgenic for human presenilin-1 with single or multiple mutations
    • Leutner S, Czech C, Schindowski K. Reduced antioxidant enzyme activity in brains of mice transgenic for human presenilin-1 with single or multiple mutations. Neurosci Lett 2000, 292:87-90.
    • (2000) Neurosci Lett , vol.292 , pp. 87-90
    • Leutner, S.1    Czech, C.2    Schindowski, K.3
  • 83
    • 0030989545 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease
    • Sayre LM, Zelasko DA, Harris PL. 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. J Neurochem 1997, 68:2092-7.
    • (1997) J Neurochem , vol.68 , pp. 2092-2097
    • Sayre, L.M.1    Zelasko, D.A.2    Harris, P.L.3
  • 84
    • 0029902166 scopus 로고    scopus 로고
    • Evidence of neuronal oxidative damage in Alzheimer's disease
    • Good PF, Werner P, Hsu A. Evidence of neuronal oxidative damage in Alzheimer's disease. Am J Pathol 1996, 149:21-8.
    • (1996) Am J Pathol , vol.149 , pp. 21-28
    • Good, P.F.1    Werner, P.2    Hsu, A.3
  • 85
    • 0037444553 scopus 로고    scopus 로고
    • In vivo imaging of reactive oxygen species specifically associated with thioflavine S-positive amyloid plaques by multiphoton microscopy
    • McLellan ME, Kajdasz ST, Hyman BT. In vivo imaging of reactive oxygen species specifically associated with thioflavine S-positive amyloid plaques by multiphoton microscopy. J Neurosci 2003, 23:2212-7.
    • (2003) J Neurosci , vol.23 , pp. 2212-2217
    • McLellan, M.E.1    Kajdasz, S.T.2    Hyman, B.T.3
  • 86
    • 0026486606 scopus 로고
    • Ultrastructural localization of Alzheimer amyloid beta/A4 protein precursor in the cytoplasm of neurons and senile plaque-associated astrocytes
    • Yamaguchi H, Yamazaki T, Ishiguro K. Ultrastructural localization of Alzheimer amyloid beta/A4 protein precursor in the cytoplasm of neurons and senile plaque-associated astrocytes. Acta Neuropathol 1992, 85:15-22.
    • (1992) Acta Neuropathol , vol.85 , pp. 15-22
    • Yamaguchi, H.1    Yamazaki, T.2    Ishiguro, K.3
  • 87
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E. Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 2006, 15:1437-49.
    • (2006) Hum Mol Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3
  • 88
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C. ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 2004, 304:448-52.
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 89
    • 33748684352 scopus 로고    scopus 로고
    • Copper-dependent inhibition of cytochrome c oxidase by Abeta(1-42) requires reduced methionine at residue 35 of the Abeta peptide
    • Crouch PJ, Barnham KJ, Duce JA. Copper-dependent inhibition of cytochrome c oxidase by Abeta(1-42) requires reduced methionine at residue 35 of the Abeta peptide. J Neurochem 2006, 99:226-36.
    • (2006) J Neurochem , vol.99 , pp. 226-236
    • Crouch, P.J.1    Barnham, K.J.2    Duce, J.A.3
  • 90
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L, Prabhu BM, Galati DF. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J Neurosci 2006, 26:9057-68.
    • (2006) J Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3
  • 91
    • 36248991348 scopus 로고    scopus 로고
    • Chronic exposure to sub-lethal beta-amyloid (Abeta) inhibits the import of nuclear-encoded proteins to mitochondria in differentiated PC12 cells
    • Sirk D, Zhu Z, Wadia JS. Chronic exposure to sub-lethal beta-amyloid (Abeta) inhibits the import of nuclear-encoded proteins to mitochondria in differentiated PC12 cells. J Neurochem 2007, 103:1989-2003.
    • (2007) J Neurochem , vol.103 , pp. 1989-2003
    • Sirk, D.1    Zhu, Z.2    Wadia, J.S.3
  • 92
    • 0035780141 scopus 로고    scopus 로고
    • Amyloid beta-peptide promotes permeability transition pore in brain mitochondria
    • Moreira PI, Santos MS, Moreno A. Amyloid beta-peptide promotes permeability transition pore in brain mitochondria. Biosci Rep 2001, 21:789-800.
    • (2001) Biosci Rep , vol.21 , pp. 789-800
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3
  • 93
    • 53549129483 scopus 로고    scopus 로고
    • Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
    • Du H, Guo L, Fang F. Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease. Nat Med 2008, 14:1097-105.
    • (2008) Nat Med , vol.14 , pp. 1097-1105
    • Du, H.1    Guo, L.2    Fang, F.3
  • 94
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp 2) as beta-secretase
    • Hussain I, Powell D, Howlett DR. Identification of a novel aspartic protease (Asp 2) as beta-secretase. Mol Cell Neurosci 1999, 14:419-27.
    • (1999) Mol Cell Neurosci , vol.14 , pp. 419-427
    • Hussain, I.1    Powell, D.2    Howlett, D.R.3
  • 95
    • 0034533808 scopus 로고    scopus 로고
    • ASP1 (BACE2) cleaves the amyloid precursor protein at the beta-secretase site
    • Hussain I, Powell DJ, Howlett DR. ASP1 (BACE2) cleaves the amyloid precursor protein at the beta-secretase site. Mol Cell Neurosci 2000, 16:609-19.
    • (2000) Mol Cell Neurosci , vol.16 , pp. 609-619
    • Hussain, I.1    Powell, D.J.2    Howlett, D.R.3
  • 96
    • 0036403838 scopus 로고    scopus 로고
    • Oxidative stress increases expression and activity of BACE in NT2 neurons
    • Tamagno E, Bardini P, Obbili A. Oxidative stress increases expression and activity of BACE in NT2 neurons. Neurobiol Dis 2002, 10:279-88.
    • (2002) Neurobiol Dis , vol.10 , pp. 279-288
    • Tamagno, E.1    Bardini, P.2    Obbili, A.3
  • 97
    • 0027180115 scopus 로고
    • MK-801, an N-methyl-D-aspartate receptor antagonist, blocks quinolinic acid-induced lipid peroxidation in rat corpus striatum
    • Santamaria A, Rios C. MK-801, an N-methyl-D-aspartate receptor antagonist, blocks quinolinic acid-induced lipid peroxidation in rat corpus striatum. Neurosci Lett 1993, 159:51-4.
    • (1993) Neurosci Lett , vol.159 , pp. 51-54
    • Santamaria, A.1    Rios, C.2
  • 98
    • 0031024185 scopus 로고    scopus 로고
    • The effect of quinolinate on rat brain lipid peroxidation is dependent on iron
    • Stipek S, Stastny F, Platenik J. The effect of quinolinate on rat brain lipid peroxidation is dependent on iron. Neurochem Int 1997, 30:233-7.
    • (1997) Neurochem Int , vol.30 , pp. 233-237
    • Stipek, S.1    Stastny, F.2    Platenik, J.3
  • 99
    • 0343114486 scopus 로고    scopus 로고
    • Effect of quinolinic acid on endogenous antioxidants in rat corpus striatum
    • Rodriguez-Martinez E, Camacho A, Maldonado PD. Effect of quinolinic acid on endogenous antioxidants in rat corpus striatum. Brain Res 2000, 858:436-9.
    • (2000) Brain Res , vol.858 , pp. 436-439
    • Rodriguez-Martinez, E.1    Camacho, A.2    Maldonado, P.D.3
  • 100
    • 0032587828 scopus 로고    scopus 로고
    • Nomega-nitro-L-arginine, a nitric oxide synthase inhibitor, antagonizes quinolinic acid-induced neurotoxicity and oxidative stress in rat striatal slices
    • Santamaria D, Espinoza-Gonzalez V, Rios C. Nomega-nitro-L-arginine, a nitric oxide synthase inhibitor, antagonizes quinolinic acid-induced neurotoxicity and oxidative stress in rat striatal slices. Neurochem Res 1999, 24:843-8.
    • (1999) Neurochem Res , vol.24 , pp. 843-848
    • Santamaria, D.1    Espinoza-Gonzalez, V.2    Rios, C.3
  • 101
    • 0035689922 scopus 로고    scopus 로고
    • N(G)-nitro-L-arginine and its methyl ester inhibit brain synthesis of kynurenic acid possibly via nitric oxide-independent mechanism
    • Luchowski P, Kocki T, Urbanska EM. N(G)-nitro-L-arginine and its methyl ester inhibit brain synthesis of kynurenic acid possibly via nitric oxide-independent mechanism. Pol J Pharmacol 2001, 53:597-604.
    • (2001) Pol J Pharmacol , vol.53 , pp. 597-604
    • Luchowski, P.1    Kocki, T.2    Urbanska, E.M.3
  • 102
    • 44549088278 scopus 로고    scopus 로고
    • The pentylenetetrazole-induced activity in the hippocampus can be inhibited by the conversion of L-kynurenine to kynurenic acid: an in vitro study
    • Rozsa E, Robotka H, Nagy D. The pentylenetetrazole-induced activity in the hippocampus can be inhibited by the conversion of L-kynurenine to kynurenic acid: an in vitro study. Brain Res Bull 2008, 76:474-9.
    • (2008) Brain Res Bull , vol.76 , pp. 474-479
    • Rozsa, E.1    Robotka, H.2    Nagy, D.3
  • 103
    • 0033593608 scopus 로고    scopus 로고
    • Free radical scavenger OPC-14117 attenuates quinolinic acid-induced NF-kappaB activation and apoptosis in rat striatum
    • Nakai M, Qin ZH, Wang Y. Free radical scavenger OPC-14117 attenuates quinolinic acid-induced NF-kappaB activation and apoptosis in rat striatum. Brain Res Mol Brain Res 1999, 64:59-68.
    • (1999) Brain Res Mol Brain Res , vol.64 , pp. 59-68
    • Nakai, M.1    Qin, Z.H.2    Wang, Y.3
  • 104
    • 0030580581 scopus 로고    scopus 로고
    • Effects of alpha-phenyl-tert-butyl nitrone on neuronal survival and motor function following intrastriatal injections of quinolinate or 3-nitropropionic acid
    • Nakao N, Brundin P. Effects of alpha-phenyl-tert-butyl nitrone on neuronal survival and motor function following intrastriatal injections of quinolinate or 3-nitropropionic acid. Neuroscience 1997, 76:749-61.
    • (1997) Neuroscience , vol.76 , pp. 749-761
    • Nakao, N.1    Brundin, P.2
  • 105
    • 0026497926 scopus 로고
    • Excitotoxic cell death
    • Choi DW. Excitotoxic cell death. J Neurobiol 1992, 23:1261-76.
    • (1992) J Neurobiol , vol.23 , pp. 1261-1276
    • Choi, D.W.1
  • 106
    • 0025831357 scopus 로고
    • Selective blockade of non-NMDA receptors does not block rapidly triggered glutamate-induced neuronal death
    • Koh JY, Choi DW. Selective blockade of non-NMDA receptors does not block rapidly triggered glutamate-induced neuronal death. Brain Res 1991, 548:318-21.
    • (1991) Brain Res , vol.548 , pp. 318-321
    • Koh, J.Y.1    Choi, D.W.2
  • 107
    • 0024020782 scopus 로고
    • Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo
    • Siman R, Noszek JC. Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo. Neuron 1988, 1:279-87.
    • (1988) Neuron , vol.1 , pp. 279-287
    • Siman, R.1    Noszek, J.C.2
  • 108
    • 0025674468 scopus 로고
    • N-methyl-D-aspartate-sensitive glutamate receptors induce calcium-mediated arachidonic acid release in primary cultures of cerebellar granule cells
    • Lazarewicz JW, Wroblewski JT, Costa E. N-methyl-D-aspartate-sensitive glutamate receptors induce calcium-mediated arachidonic acid release in primary cultures of cerebellar granule cells. J Neurochem 1990, 55:1875-81.
    • (1990) J Neurochem , vol.55 , pp. 1875-1881
    • Lazarewicz, J.W.1    Wroblewski, J.T.2    Costa, E.3
  • 109
    • 67651039313 scopus 로고    scopus 로고
    • Arachidonic acid-induced apoptosis of human neuroblastoma SK-N-SH cells is mediated through mitochondrial alteration elicited by ROS and Ca(2+)-evoked activation of p38alpha MAPK and JNK1
    • Chen KC, Chang LS. Arachidonic acid-induced apoptosis of human neuroblastoma SK-N-SH cells is mediated through mitochondrial alteration elicited by ROS and Ca(2+)-evoked activation of p38alpha MAPK and JNK1. Toxicology 2009, 262:199-206.
    • (2009) Toxicology , vol.262 , pp. 199-206
    • Chen, K.C.1    Chang, L.S.2
  • 110
    • 0035887601 scopus 로고    scopus 로고
    • An NMDA receptor signaling complex with protein phosphatase 2A
    • Chan SF, Sucher NJ. An NMDA receptor signaling complex with protein phosphatase 2A. J Neurosci 2001, 21:7985-92.
    • (2001) J Neurosci , vol.21 , pp. 7985-7992
    • Chan, S.F.1    Sucher, N.J.2
  • 111
    • 67651243648 scopus 로고    scopus 로고
    • The excitotoxin quinolinic acid induces tau phosphorylation in human neurons
    • Rahman A, Ting K, Cullen KM. The excitotoxin quinolinic acid induces tau phosphorylation in human neurons. PLoS One 2009, 4:e6344.
    • (2009) PLoS One , vol.4
    • Rahman, A.1    Ting, K.2    Cullen, K.M.3
  • 112
    • 70349754448 scopus 로고    scopus 로고
    • Mechanism for quinolinic acid cytotoxicity in human astrocytes and neurons
    • Braidy N, Grant R, Adams S. Mechanism for quinolinic acid cytotoxicity in human astrocytes and neurons. Neurotox Res 2009, 16:77-86.
    • (2009) Neurotox Res , vol.16 , pp. 77-86
    • Braidy, N.1    Grant, R.2    Adams, S.3
  • 113
    • 2442465965 scopus 로고    scopus 로고
    • Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration
    • Li L, Sengupta A, Haque N. Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration. FEBS Lett 2004, 566:261-9.
    • (2004) FEBS Lett , vol.566 , pp. 261-269
    • Li, L.1    Sengupta, A.2    Haque, N.3
  • 114
    • 21644447108 scopus 로고    scopus 로고
    • In vivo quinolinic acid increases synaptosomal glutamate release in rats: reversal by guanosine
    • Tavares RG, Schmidt AP, Abud J. In vivo quinolinic acid increases synaptosomal glutamate release in rats: reversal by guanosine. Neurochem Res 2005, 30:439-44.
    • (2005) Neurochem Res , vol.30 , pp. 439-444
    • Tavares, R.G.1    Schmidt, A.P.2    Abud, J.3
  • 115
    • 77953543635 scopus 로고    scopus 로고
    • In vivo neuroprotective effects of peripheral kynurenine on acute neurotoxicity induced by glutamate in rat cerebral cortex
    • Kumar A, Babu GN. In vivo neuroprotective effects of peripheral kynurenine on acute neurotoxicity induced by glutamate in rat cerebral cortex. Neurochem Res 2010, 35:636-44.
    • (2010) Neurochem Res , vol.35 , pp. 636-644
    • Kumar, A.1    Babu, G.N.2
  • 116
    • 0025077080 scopus 로고
    • Molecular, cellular, and pathologic characterization of HLA-DR immunoreactivity in normal elderly and Alzheimer's disease brain
    • Styren SD, Civin WH, Rogers J. Molecular, cellular, and pathologic characterization of HLA-DR immunoreactivity in normal elderly and Alzheimer's disease brain. Exp Neurol 1990, 110:93-104.
    • (1990) Exp Neurol , vol.110 , pp. 93-104
    • Styren, S.D.1    Civin, W.H.2    Rogers, J.3
  • 117
    • 0023633015 scopus 로고
    • Reactive microglia in patients with senile dementia of the Alzheimer type are positive for the histocompatibility glycoprotein HLA-DR
    • McGeer PL, Itagaki S, Tago H. Reactive microglia in patients with senile dementia of the Alzheimer type are positive for the histocompatibility glycoprotein HLA-DR. Neurosci Lett 1987, 79:195-200.
    • (1987) Neurosci Lett , vol.79 , pp. 195-200
    • McGeer, P.L.1    Itagaki, S.2    Tago, H.3
  • 118
    • 0028787874 scopus 로고
    • Role of microglia in senile plaque formation
    • Mackenzie IR, Hao C, Munoz DG. Role of microglia in senile plaque formation. Neurobiol Aging 1995, 16:797-804.
    • (1995) Neurobiol Aging , vol.16 , pp. 797-804
    • Mackenzie, I.R.1    Hao, C.2    Munoz, D.G.3
  • 119
    • 0026969190 scopus 로고
    • Localization of smg p25A/rab3A p25, a small GTP-binding protein, at the active zone of the rat neuromuscular junction
    • Mizoguchi A, Arakawa M, Masutani M. Localization of smg p25A/rab3A p25, a small GTP-binding protein, at the active zone of the rat neuromuscular junction. Biochem Biophys Res Commun 1992, 186:1345-52.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 1345-1352
    • Mizoguchi, A.1    Arakawa, M.2    Masutani, M.3
  • 120
    • 0026685656 scopus 로고
    • Ultrastructural studies of the cells forming amyloid in the cortical vessel wall in Alzheimer's disease
    • Wisniewski HM, Wegiel J, Wang KC. Ultrastructural studies of the cells forming amyloid in the cortical vessel wall in Alzheimer's disease. Acta Neuropathol 1992, 84:117-27.
    • (1992) Acta Neuropathol , vol.84 , pp. 117-127
    • Wisniewski, H.M.1    Wegiel, J.2    Wang, K.C.3
  • 121
    • 0035845283 scopus 로고    scopus 로고
    • In-vivo measurement of activated microglia in dementia
    • Cagnin A, Brooks DJ, Kennedy AM. In-vivo measurement of activated microglia in dementia. Lancet 2001, 358:461-7.
    • (2001) Lancet , vol.358 , pp. 461-467
    • Cagnin, A.1    Brooks, D.J.2    Kennedy, A.M.3
  • 122
    • 56349144614 scopus 로고    scopus 로고
    • Microglia, amyloid, and cognition in Alzheimer's disease: an [11C](R)PK11195-PET and [11C]PIB-PET study
    • Edison P, Archer HA, Gerhard A. Microglia, amyloid, and cognition in Alzheimer's disease: an [11C](R)PK11195-PET and [11C]PIB-PET study. Neurobiol Dis 2008, 32:412-9.
    • (2008) Neurobiol Dis , vol.32 , pp. 412-419
    • Edison, P.1    Archer, H.A.2    Gerhard, A.3
  • 123
    • 2542431100 scopus 로고    scopus 로고
    • The microglial phagocytic role with specific plaque types in the Alzheimer disease brain
    • D'Andrea MR, Cole GM, Ard MD. The microglial phagocytic role with specific plaque types in the Alzheimer disease brain. Neurobiol Aging 2004, 25:675-83.
    • (2004) Neurobiol Aging , vol.25 , pp. 675-683
    • D'Andrea, M.R.1    Cole, G.M.2    Ard, M.D.3
  • 124
  • 125
    • 0036685522 scopus 로고    scopus 로고
    • Inflammation in neurodegenerative disease-a double-edged sword
    • Wyss-Coray T, Mucke L. Inflammation in neurodegenerative disease-a double-edged sword. Neuron 2002, 35:419-32.
    • (2002) Neuron , vol.35 , pp. 419-432
    • Wyss-Coray, T.1    Mucke, L.2
  • 126
    • 70449535530 scopus 로고    scopus 로고
    • Inflammation and microglia actions in Alzheimer's disease
    • Combs CK. Inflammation and microglia actions in Alzheimer's disease. J Neuroimmune Pharmacol 2009, 4:380-8.
    • (2009) J Neuroimmune Pharmacol , vol.4 , pp. 380-388
    • Combs, C.K.1
  • 127
    • 0027716965 scopus 로고
    • A mechanism of quinolinic acid formation by brain in inflammatory neurological disease. Attenuation of synthesis from L-tryptophan by 6-chlorotryptophan and 4-chloro-3-hydroxyanthranilate
    • Heyes MP, Saito K, Major EO. A mechanism of quinolinic acid formation by brain in inflammatory neurological disease. Attenuation of synthesis from L-tryptophan by 6-chlorotryptophan and 4-chloro-3-hydroxyanthranilate. Brain 1993, 116:1425-50.
    • (1993) Brain , vol.116 , pp. 1425-1450
    • Heyes, M.P.1    Saito, K.2    Major, E.O.3
  • 128
    • 0028971636 scopus 로고
    • Metabolism of L-tryptophan to kynurenate and quinolinate in the central nervous system: effects of 6-chlorotryptophan and 4-chloro-3-hydroxyanthranilate
    • Naritsin DB, Saito K, Markey SP. Metabolism of L-tryptophan to kynurenate and quinolinate in the central nervous system: effects of 6-chlorotryptophan and 4-chloro-3-hydroxyanthranilate. J Neurochem 1995, 65:2217-26.
    • (1995) J Neurochem , vol.65 , pp. 2217-2226
    • Naritsin, D.B.1    Saito, K.2    Markey, S.P.3
  • 129
    • 0029960647 scopus 로고    scopus 로고
    • Human microglia convert l-tryptophan into the neurotoxin quinolinic acid
    • Heyes MP, Achim CL, Wiley CA. Human microglia convert l-tryptophan into the neurotoxin quinolinic acid. Biochem J 1996, 320:595-7.
    • (1996) Biochem J , vol.320 , pp. 595-597
    • Heyes, M.P.1    Achim, C.L.2    Wiley, C.A.3
  • 130
    • 0030887550 scopus 로고    scopus 로고
    • Activated human microglia produce the excitotoxin quinolinic acid
    • Espey MG, Chernyshev ON, Reinhard JF. 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, J.F.3
  • 131
    • 1042302739 scopus 로고    scopus 로고
    • Expression of the kynurenine pathway enzymes in human microglia and macrophages
    • Guillemin GJ, Smith DG, Smythe GA. Expression of the kynurenine pathway enzymes in human microglia and macrophages. Adv Exp Med Biol 2003, 527:105-12.
    • (2003) Adv Exp Med Biol , vol.527 , pp. 105-112
    • Guillemin, G.J.1    Smith, D.G.2    Smythe, G.A.3
  • 132
    • 33646089457 scopus 로고    scopus 로고
    • Gene expression changes by amyloid beta peptide-stimulated human postmortem brain microglia identify activation of multiple inflammatory processes
    • Walker DG, Link J, Lue LF. Gene expression changes by amyloid beta peptide-stimulated human postmortem brain microglia identify activation of multiple inflammatory processes. J Leukoc Biol 2006, 79:596-610.
    • (2006) J Leukoc Biol , vol.79 , pp. 596-610
    • Walker, D.G.1    Link, J.2    Lue, L.F.3
  • 133
    • 10744228559 scopus 로고    scopus 로고
    • Identification of cathepsin B as a mediator of neuronal death induced by Abeta-activated microglial cells using a functional genomics approach
    • Gan L, Ye S, Chu A. Identification of cathepsin B as a mediator of neuronal death induced by Abeta-activated microglial cells using a functional genomics approach. J Biol Chem 2004, 279:5565-72.
    • (2004) J Biol Chem , vol.279 , pp. 5565-5572
    • Gan, L.1    Ye, S.2    Chu, A.3
  • 134
    • 67650472723 scopus 로고    scopus 로고
    • Proinflammatory cytokine interferon-gamma increases induction of indoleamine 2,3-dioxygenase in monocytic cells primed with amyloid beta peptide 1-42: implications for the pathogenesis of Alzheimer's disease
    • Yamada A, Akimoto H, Kagawa S. Proinflammatory cytokine interferon-gamma increases induction of indoleamine 2,3-dioxygenase in monocytic cells primed with amyloid beta peptide 1-42: implications for the pathogenesis of Alzheimer's disease. J Neurochem 2009, 110:791-800.
    • (2009) J Neurochem , vol.110 , pp. 791-800
    • Yamada, A.1    Akimoto, H.2    Kagawa, S.3
  • 135
    • 11144314849 scopus 로고    scopus 로고
    • Expression of indoleamine 2,3-dioxygenase and production of quinolinic acid by human microglia, astrocytes, and neurons
    • Guillemin GJ, Smythe G, Takikawa O. Expression of indoleamine 2,3-dioxygenase and production of quinolinic acid by human microglia, astrocytes, and neurons. Glia 2005, 49:15-23.
    • (2005) Glia , vol.49 , pp. 15-23
    • Guillemin, G.J.1    Smythe, G.2    Takikawa, O.3
  • 136
    • 73249145672 scopus 로고    scopus 로고
    • Effect of quinolinic acid on human astrocytes morphology and functions: implications in Alzheimer's disease
    • Ting KK, Brew BJ, Guillemin GJ. Effect of quinolinic acid on human astrocytes morphology and functions: implications in Alzheimer's disease. J Neuroinflammation 2009, 6:36-49.
    • (2009) J Neuroinflammation , vol.6 , pp. 36-49
    • Ting, K.K.1    Brew, B.J.2    Guillemin, G.J.3
  • 137
    • 0035368649 scopus 로고    scopus 로고
    • Time course of glial proliferation and glial apoptosis following excitotoxic CNS injury
    • Dihne M, Block F, Korr H. Time course of glial proliferation and glial apoptosis following excitotoxic CNS injury. Brain Res 2001, 902:178-89.
    • (2001) Brain Res , vol.902 , pp. 178-189
    • Dihne, M.1    Block, F.2    Korr, H.3
  • 138
    • 0037128509 scopus 로고    scopus 로고
    • Excitotoxic and metabolic damage to the rodent striatum: role of the P75 neurotrophin receptor and glial progenitors
    • Hanbury R, Charles V, Chen EY. Excitotoxic and metabolic damage to the rodent striatum: role of the P75 neurotrophin receptor and glial progenitors. J Comp Neurol 2002, 444:291-305.
    • (2002) J Comp Neurol , vol.444 , pp. 291-305
    • Hanbury, R.1    Charles, V.2    Chen, E.Y.3
  • 139
    • 0037337196 scopus 로고    scopus 로고
    • Quinolinic acid upregulates chemokine production and chemokine receptor expression in astrocytes
    • Guillemin GJ, Croitoru-Lamoury J, Dormont D. Quinolinic acid upregulates chemokine production and chemokine receptor expression in astrocytes. Glia 2003, 41:371-81.
    • (2003) Glia , vol.41 , pp. 371-381
    • Guillemin, G.J.1    Croitoru-Lamoury, J.2    Dormont, D.3
  • 140
    • 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
  • 141
    • 0026076136 scopus 로고
    • Blood-brain barrier transport of kynurenines: implications for brain synthesis and metabolism
    • Fukui S, Schwarcz R, Rapoport SI. 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
  • 142
    • 0036435647 scopus 로고    scopus 로고
    • L-4-chlorokynurenine attenuates kainate-induced seizures and lesions in the rat
    • Wu HQ, Lee SC, Scharfman HE. L-4-chlorokynurenine attenuates kainate-induced seizures and lesions in the rat. Exp Neurol 2002, 177:222-32.
    • (2002) Exp Neurol , vol.177 , pp. 222-232
    • Wu, H.Q.1    Lee, S.C.2    Scharfman, H.E.3
  • 143
    • 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
  • 144
    • 0031566868 scopus 로고    scopus 로고
    • Enzyme-catalyzed production of the neuroprotective NMDA receptor antagonist 7-chlorokynurenic acid in the rat brain in vivo
    • Wu HQ, Salituro FG, Schwarcz R. Enzyme-catalyzed production of the neuroprotective NMDA receptor antagonist 7-chlorokynurenic acid in the rat brain in vivo. Eur J Pharmacol 1997, 319:13-20.
    • (1997) Eur J Pharmacol , vol.319 , pp. 13-20
    • Wu, H.Q.1    Salituro, F.G.2    Schwarcz, R.3
  • 145
    • 71949108894 scopus 로고    scopus 로고
    • Syntheses, transformations and pharmaceutical applications of kynurenic acid derivatives
    • Fulop F, Szatmari I, Vamos E. 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
  • 146
    • 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. 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
  • 147
    • 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. 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
  • 148
    • 0031836667 scopus 로고    scopus 로고
    • Modulation of striatal quinolinate neurotoxicity by elevation of endogenous brain kynurenic acid
    • Harris CA, Miranda AF, Tanguay JJ. 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
  • 149
    • 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. 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    Nguyen, Q.3
  • 150
    • 62649121884 scopus 로고    scopus 로고
    • On the relationship between the two branches of the kynurenine pathway in the rat brain in vivo
    • Amori L, Guidetti P, Pellicciari R. On the relationship between the two branches of the kynurenine pathway in the rat brain in vivo. J Neurochem 2009, 109:316-25.
    • (2009) J Neurochem , vol.109 , pp. 316-325
    • Amori, L.1    Guidetti, P.2    Pellicciari, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.