메뉴 건너뛰기




Volumn 68-69, Issue , 2002, Pages 197-210

Prostaglandins and other lipid mediators in Alzheimer's disease

Author keywords

Alzheimer's disease (AD); AP1; Arachidonic acid (AA) cycle; Brain membranes; Cytosolic phospholipase A2 (cPLA2); Isoprostane; Neuroinflammation, NF B; Platelet activating factor (PAF); Prostaglandin (PG); STAT1

Indexed keywords

AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; ARACHIDONIC ACID; CYCLOOXYGENASE 2; FATTY ACID; ICOSANOID; LYSOPHOSPHOLIPID; NEUROFILAMENT PROTEIN; NONSTEROID ANTIINFLAMMATORY AGENT; PHOSPHOLIPASE A2; PRESENILIN 1; PRESENILIN 2; PROSTAGLANDIN SYNTHASE; REACTIVE OXYGEN METABOLITE; SYNAPSIN; SYNAPTOBREVIN; THROMBOCYTE ACTIVATING FACTOR; CYCLOOXYGENASE 1; ISOENZYME; ISOPROSTANE DERIVATIVE; MEMBRANE PROTEIN; PHOSPHOLIPASE A; PROSTAGLANDIN; PTGS1 PROTEIN, HUMAN; PTGS2 PROTEIN, HUMAN;

EID: 0036669582     PISSN: 00906980     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0090-6980(02)00031-X     Document Type: Article
Times cited : (159)

References (123)
  • 1
    • 0000293742 scopus 로고
    • Über eine eigenartige erkrankung der hirnrinde
    • Alzheimer A. Über eine eigenartige erkrankung der hirnrinde. Allg. Z. Psychiatry. 64:1907;146.
    • (1907) Allg. Z. Psychiatry , vol.64 , pp. 146
    • Alzheimer, A.1
  • 2
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:2001;741.
    • (2001) Physiol. Rev. , vol.81 , pp. 741
    • Selkoe, D.J.1
  • 3
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G.G., Wong C.W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120:1984;885.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885
    • Glenner, G.G.1    Wong, C.W.2
  • 4
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J., Lemaire H.G., Unterbeck A.et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature. 325:1987;733.
    • (1987) Nature , vol.325 , pp. 733
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 5
    • 0022156464 scopus 로고
    • Neuronal origin of a cerebral amyloid: Neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels
    • Masters C.L., Multhaup G., Simms G., Pottgiesser J., Martins R.N., Beyreuther K. Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO J. 4:1985;2757.
    • (1985) EMBO J. , vol.4 , pp. 2757
    • Masters, C.L.1    Multhaup, G.2    Simms, G.3    Pottgiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 6
    • 0023850791 scopus 로고
    • Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease
    • Tanzi R.E., McClatchey A.I., Lamperti E.D., Villa-Komaroff L., Gusella J.F., Neve R.L. Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease. Nature. 331:1988;528.
    • (1988) Nature , vol.331 , pp. 528
    • Tanzi, R.E.1    McClatchey, A.I.2    Lamperti, E.D.3    Villa-Komaroff, L.4    Gusella, J.F.5    Neve, R.L.6
  • 7
    • 0023872043 scopus 로고
    • Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity
    • Kitaguchi N., Takahashi Y., Tokushima Y., Shiojiri S., Ito H. Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity. Nature. 331:1988;530.
    • (1988) Nature , vol.331 , pp. 530
    • Kitaguchi, N.1    Takahashi, Y.2    Tokushima, Y.3    Shiojiri, S.4    Ito, H.5
  • 8
    • 0023870043 scopus 로고
    • A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
    • Ponte P., Gonzalez-DeWhitt P., Schilling J.et al. A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors. Nature. 331:1988;525.
    • (1988) Nature , vol.331 , pp. 525
    • Ponte, P.1    Gonzalez-DeWhitt, P.2    Schilling, J.3
  • 9
    • 0027477463 scopus 로고
    • Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease
    • Roher A.E., Lowenson J.D., Clarke S.et al. Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J. Biol. Chem. 268:1993;3072.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3072
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3
  • 10
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike C.J., Burdick D., Walencewicz A.J., Glabe C.G., Cotman C.W. Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13:1993;1676.
    • (1993) J. Neurosci. , vol.13 , pp. 1676
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 11
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta-amyloid neurotoxicity
    • Busciglio J., Lorenzo A., Yankner B.A. Methodological variables in the assessment of beta-amyloid neurotoxicity. Neurobiol. Aging. 13:1992;609.
    • (1992) Neurobiol. Aging , vol.13 , pp. 609
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 12
    • 0027297138 scopus 로고
    • Calcium-destabilizing and neurodegenerative effects of aggregated beta-amyloid peptide are attenuated by basic FGF
    • Mattson M.P., Tomaselli K.J., Rydel R.E. Calcium-destabilizing and neurodegenerative effects of aggregated beta-amyloid peptide are attenuated by basic FGF. Brain Res. 621:1993;35.
    • (1993) Brain Res. , vol.621 , pp. 35
    • Mattson, M.P.1    Tomaselli, K.J.2    Rydel, R.E.3
  • 13
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A., Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. USA. 91:1994;12243.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243
    • Lorenzo, A.1    Yankner, B.A.2
  • 14
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., Yankner B.A. Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron. 14:1995;879.
    • (1995) Neuron , vol.14 , pp. 879
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 15
    • 0029034927 scopus 로고
    • Aggregation state and neurotoxic properties of Alzheimer beta-amyloid peptide
    • Howlett D.R., Jennings K.H., Lee D.C.et al. Aggregation state and neurotoxic properties of Alzheimer beta-amyloid peptide. Neurodegeneration. 4:1995;23.
    • (1995) Neurodegeneration , vol.4 , pp. 23
    • Howlett, D.R.1    Jennings, K.H.2    Lee, D.C.3
  • 16
    • 0029583316 scopus 로고
    • Making the diagnosis of mixed and non-Alzheimer's dementias
    • Hansen L.A., Crain B.J. Making the diagnosis of mixed and non-Alzheimer's dementias. Arch Pathol. Lab. Med. 119:1995;1023.
    • (1995) Arch Pathol. Lab. Med. , vol.119 , pp. 1023
    • Hansen, L.A.1    Crain, B.J.2
  • 17
    • 0035053038 scopus 로고    scopus 로고
    • COX-2 as a multifunctional neuronal modulator
    • Bazan N.G. COX-2 as a multifunctional neuronal modulator. Nat. Med. 7:2001;414.
    • (2001) Nat. Med. , vol.7 , pp. 414
    • Bazan, N.G.1
  • 18
    • 0033403325 scopus 로고    scopus 로고
    • Apolipoprotein E: A pharmacogenetic target for the treatment of Alzheimer's disease
    • Poirier J. Apolipoprotein E: a pharmacogenetic target for the treatment of Alzheimer's disease. Mol. Diagn. 4:1999;335.
    • (1999) Mol. Diagn. , vol.4 , pp. 335
    • Poirier, J.1
  • 19
    • 0033632219 scopus 로고    scopus 로고
    • Cellular and molecular basis of beta-amyloid precursor protein metabolism
    • Greenfield JP, Gross RS, Gouras GK, Xu H. Cellular and molecular basis of beta-amyloid precursor protein metabolism. Front. Biosci. 2000;5:172.
    • (2000) Front. Biosci. , vol.5 , pp. 172
    • Greenfield, J.P.1    Gross, R.S.2    Gouras, G.K.3    Xu, H.4
  • 21
    • 0033371315 scopus 로고    scopus 로고
    • Molecular genetics of Alzheimer disease
    • St George-Hyslop P.H. Molecular genetics of Alzheimer disease. Semin. Neurol. 19:1999;371.
    • (1999) Semin. Neurol. , vol.19 , pp. 371
    • St George-Hyslop, P.H.1
  • 22
    • 0027407565 scopus 로고
    • Apolipoprotein E: High-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease
    • Strittmatter W.J., Saunders A.M., Schmechel D.et al. Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc. Natl. Acad. Sci. USA. 90:1993;1977.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1977
    • Strittmatter, W.J.1    Saunders, A.M.2    Schmechel, D.3
  • 23
    • 0032461761 scopus 로고    scopus 로고
    • Apolipoprotein E and Alzheimer's disease the tip of the susceptibility iceberg
    • Roses A.D. Apolipoprotein E and Alzheimer's disease the tip of the susceptibility iceberg. Ann. NY Acad. Sci. 855:1998;738.
    • (1998) Ann. NY Acad. Sci. , vol.855 , pp. 738
    • Roses, A.D.1
  • 24
    • 0033253464 scopus 로고    scopus 로고
    • The role of apolipoprotein E in the pathogenesis of Alzheimer disease
    • Okuizumi K. The role of apolipoprotein E in the pathogenesis of Alzheimer disease. Nippon Rinsho. 57:1999;2673.
    • (1999) Nippon Rinsho , vol.57 , pp. 2673
    • Okuizumi, K.1
  • 25
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington R., Rogaev E.I., Liang Y.et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 375:1995;754.
    • (1995) Nature , vol.375 , pp. 754
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 26
    • 0029984784 scopus 로고    scopus 로고
    • Genomic structure and expression of STM2, the chromosome 1 familial Alzheimer disease gene
    • Levy-Lahad E., Poorkaj P., Wang K. Genomic structure and expression of STM2, the chromosome 1 familial Alzheimer disease gene. Genomics. 34:1996;198.
    • (1996) Genomics , vol.34 , pp. 198
    • Levy-Lahad, E.1    Poorkaj, P.2    Wang, K.3
  • 27
    • 0031569390 scopus 로고    scopus 로고
    • Analysis of the 5′ sequence, genomic structure, and alternative splicing of the presenilin-1 gene (PSEN1) associated with early onset Alzheimer disease
    • Rogaev E.I., Sherrington R., Wu C.et al. Analysis of the 5′ sequence, genomic structure, and alternative splicing of the presenilin-1 gene (PSEN1) associated with early onset Alzheimer disease. Genomics. 40:1999;415.
    • (1999) Genomics , vol.40 , pp. 415
    • Rogaev, E.I.1    Sherrington, R.2    Wu, C.3
  • 28
    • 0033220122 scopus 로고    scopus 로고
    • Genetic factors and a polygenic Mof Alzheimer's disease
    • Rogaev E.I. Genetic factors and a polygenic Mof Alzheimer's disease. Genetika. 35:1999;1558.
    • (1999) Genetika , vol.35 , pp. 1558
    • Rogaev, E.I.1
  • 31
    • 0025618685 scopus 로고
    • Cytoskeletal messenger RNA stability in human neocortex: Studies in normal aging and in Alzheimer's disease
    • Lukiw W.J., Wong L., McLachlan D.R.C. Cytoskeletal messenger RNA stability in human neocortex: studies in normal aging and in Alzheimer's disease. Int. J. Neurosci. 55:1990;81.
    • (1990) Int. J. Neurosci. , vol.55 , pp. 81
    • Lukiw, W.J.1    Wong, L.2    McLachlan, D.R.C.3
  • 33
    • 0032821709 scopus 로고    scopus 로고
    • Neurofilament functions in health and disease
    • Julien J.P. Neurofilament functions in health and disease. Curr. Opin. Neurobiol. 9:1999;554.
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 554
    • Julien, J.P.1
  • 35
    • 0024308501 scopus 로고
    • Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system
    • Elferink L.A., Trimble W.S., Scheller K. Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J. Biol. Chem. 264:1989;11061.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11061
    • Elferink, L.A.1    Trimble, W.S.2    Scheller, K.3
  • 36
    • 0028272092 scopus 로고
    • Expression of the ssynaptic vesicle proteins vamps/synaptobrevins 1 and 2 in non-neural tissues
    • Ralston E., Beushausen S., Ploug T. Expression of the ssynaptic vesicle proteins vamps/synaptobrevins 1 and 2 in non-neural tissues. J. Biol. Chem. 269:1994;15403.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15403
    • Ralston, E.1    Beushausen, S.2    Ploug, T.3
  • 37
    • 11944258877 scopus 로고
    • (2+) - But not for GTP gamma S-induced insulin secretion
    • (2+) - but not for GTP gamma S-induced insulin secretion. EMBO J. 14:1995;2723.
    • (1995) EMBO J. , vol.14 , pp. 2723
    • Regazzi, R.1    Wollheim, C.B.2    Lang, J.3
  • 38
    • 0030437791 scopus 로고    scopus 로고
    • Synaptic and cytoskeletal RNA message levels in sporadic Alzheimer neocortex
    • Lukiw W.J., Rogaev E.I., Bazan N.G. Synaptic and cytoskeletal RNA message levels in sporadic Alzheimer neocortex. Alzheimer's Res. 2:1996;221.
    • (1996) Alzheimer's Res. , vol.2 , pp. 221
    • Lukiw, W.J.1    Rogaev, E.I.2    Bazan, N.G.3
  • 39
    • 0032949115 scopus 로고    scopus 로고
    • Expression of proteins linked to exocytosis and neurotransmission in patients with Creutzfeldt-Jakob disease
    • Ferrer I., Rivera R., Blanco R., Marti E. Expression of proteins linked to exocytosis and neurotransmission in patients with Creutzfeldt-Jakob disease. Neurobiol. Dis. 6:1999;92.
    • (1999) Neurobiol. Dis. , vol.6 , pp. 92
    • Ferrer, I.1    Rivera, R.2    Blanco, R.3    Marti, E.4
  • 40
    • 0023443257 scopus 로고
    • Synaptophysin: Molecular organization and mRNA expression as determined from cloned cDNA
    • Leube R.E., Kaiser P., Seiter Zimbelmann R.et al. Synaptophysin: molecular organization and mRNA expression as determined from cloned cDNA. EMBO J. 6:1987;3261.
    • (1987) EMBO J. , vol.6 , pp. 3261
    • Leube, R.E.1    Kaiser, P.2    Seiter Zimbelmann, R.3
  • 41
    • 0029132018 scopus 로고
    • Synaptic vesicle proteins and regulated exocytosis
    • Elferink L.A., Scheller R.H. Synaptic vesicle proteins and regulated exocytosis. Prog. Brain Res. 105:1995;79.
    • (1995) Prog. Brain Res. , vol.105 , pp. 79
    • Elferink, L.A.1    Scheller, R.H.2
  • 42
    • 0032051614 scopus 로고    scopus 로고
    • Temporal cortex synaptophysin mRNA is reduced in Alzheimer's disease and is negatively correlated with the severity of dementia
    • Heffernan J.M., Eastwood S.L., Nagy Z., Sanders M.W., McDonald B., Harrison P.J. Temporal cortex synaptophysin mRNA is reduced in Alzheimer's disease and is negatively correlated with the severity of dementia. Exp. Neurol. 150:1998;235.
    • (1998) Exp. Neurol. , vol.150 , pp. 235
    • Heffernan, J.M.1    Eastwood, S.L.2    Nagy, Z.3    Sanders, M.W.4    McDonald, B.5    Harrison, P.J.6
  • 44
    • 0033025080 scopus 로고    scopus 로고
    • Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles
    • Callahan L.M., Vaules W.A., Coleman P.D. Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles. J. Neuropathol. Exp. Neurol. 58:1999;275.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 275
    • Callahan, L.M.1    Vaules, W.A.2    Coleman, P.D.3
  • 45
    • 0025371602 scopus 로고
    • The structure of the human synapsin I gene and protein
    • Sudhof T.C. The structure of the human synapsin I gene and protein. J. Biol. Chem. 265:1990;7849.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7849
    • Sudhof, T.C.1
  • 46
    • 0027488378 scopus 로고
    • Synapsin I gene expression in the adult rat brain with comparative analysis of mRNA and protein in the hippocampus
    • Melloni R.H. Jr., Hemmendinger L.M., Hamos J.E., DeGennaro L.J. Synapsin I gene expression in the adult rat brain with comparative analysis of mRNA and protein in the hippocampus. J. Comp. Neurol. 327:1993;507.
    • (1993) J. Comp. Neurol. , vol.327 , pp. 507
    • Melloni R.H., Jr.1    Hemmendinger, L.M.2    Hamos, J.E.3    DeGennaro, L.J.4
  • 47
    • 0029046477 scopus 로고
    • Suppression of synapsin II inhibits the formation and maintenance of synapses in hippocampal culture
    • Ferreira A., Han H.Q., Greengard P., Kosik K.S. Suppression of synapsin II inhibits the formation and maintenance of synapses in hippocampal culture. Proc. Natl. Acad. Sci. 92:1995;9225.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 9225
    • Ferreira, A.1    Han, H.Q.2    Greengard, P.3    Kosik, K.S.4
  • 48
    • 0029022960 scopus 로고
    • Impairment of axonal development and of synaptogenesis in hippocampal neurons of synapsin I-deficient mice
    • Chin L.S., Li L., Ferreira A., Kosik K.S., Greengard P. Impairment of axonal development and of synaptogenesis in hippocampal neurons of synapsin I-deficient mice. Proc. Natl. Acad. Sci. USA. 92:1995;9230.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9230
    • Chin, L.S.1    Li, L.2    Ferreira, A.3    Kosik, K.S.4    Greengard, P.5
  • 50
    • 0005233134 scopus 로고    scopus 로고
    • COX-2 RNA message abundance, stability, and hypervariability in sporadic Alzheimer neocortex
    • Lukiw W.J., Bazan N.G. COX-2 RNA message abundance, stability, and hypervariability in sporadic Alzheimer neocortex. J. Neurosci. Res. 15:1997;50.
    • (1997) J. Neurosci. Res. , vol.15 , pp. 50
    • Lukiw, W.J.1    Bazan, N.G.2
  • 51
    • 0032551633 scopus 로고    scopus 로고
    • COX-2 expression is increased in frontal cortex of Alzheimer's disease brain
    • Pasinetti G.M., Aisen P.S. COX-2 expression is increased in frontal cortex of Alzheimer's disease brain. Neuroscience. 87:1998;319.
    • (1998) Neuroscience , vol.87 , pp. 319
    • Pasinetti, G.M.1    Aisen, P.S.2
  • 52
    • 0033608169 scopus 로고    scopus 로고
    • Increased expression of COXs and peroxisome proliferator-activated receptor-gamma in Alzheimer's disease brains
    • Kitamura Y., Shimohama S., Koik e H.et al. Increased expression of COXs and peroxisome proliferator-activated receptor-gamma in Alzheimer's disease brains. Biochem. Biophys. Res. Commun. 254:1999;582.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 582
    • Kitamura, Y.1    Shimohama, S.2    Koik e, H.3
  • 53
  • 54
    • 12644314071 scopus 로고    scopus 로고
    • 2 and glutamate on inducing cell death and sustained arachidonic acid metabolic changes in primary cortical neuronal cultures
    • 2 and glutamate on inducing cell death and sustained arachidonic acid metabolic changes in primary cortical neuronal cultures. J. Biol. Chem. 271:1996;32722.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32722
    • Kolko, M.1    DeCoster, M.A.2    De Turco, E.B.3    Bazan, N.G.4
  • 56
    • 0032990757 scopus 로고    scopus 로고
    • Phospholipases and phagocytosis: The role of phospholipid-derived second messengers in phagocytosis
    • Lennartz M.R. Phospholipases and phagocytosis: the role of phospholipid-derived second messengers in phagocytosis. Int. J. Biochem. Cell Biol. 31:1999;415.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 415
    • Lennartz, M.R.1
  • 59
    • 0025358788 scopus 로고
    • Arachidonic acid cascade and signal transduction
    • Shimizu T., Wolfe L.S. Arachidonic acid cascade and signal transduction. J. Neurochem. 55:1990;1.
    • (1990) J. Neurochem. , vol.55 , pp. 1
    • Shimizu, T.1    Wolfe, L.S.2
  • 61
    • 0028802503 scopus 로고
    • Mediators of injury in neurotrauma: Intracellular signal transduction and gene expression
    • Bazan N.G., Rodriguez de Turco E.B., Allan G. Mediators of injury in neurotrauma: intracellular signal transduction and gene expression. J. Neurotrauma. 12:1995;791.
    • (1995) J. Neurotrauma , vol.12 , pp. 791
    • Bazan, N.G.1    Rodriguez de Turco, E.B.2    Allan, G.3
  • 62
    • 0031740532 scopus 로고    scopus 로고
    • The neuromessenger platelet-activating factor in plasticity and neurodegeneration
    • Bazan N.G. The neuromessenger platelet-activating factor in plasticity and neurodegeneration. Prog. Brain Res. 118:1998;281.
    • (1998) Prog. Brain Res. , vol.118 , pp. 281
    • Bazan, N.G.1
  • 63
    • 0032829605 scopus 로고    scopus 로고
    • 2 inhibitors, PAF acetylhydrolases, PAF receptor antagonists and free radical scavengers PGs leukot
    • 2 inhibitors, PAF acetylhydrolases, PAF receptor antagonists and free radical scavengers PGs leukot. Essent. Fatty Acids. 61:1999;65.
    • (1999) Essent. Fatty Acids , vol.61 , pp. 65
    • Peplow, P.V.1
  • 64
    • 0032944604 scopus 로고    scopus 로고
    • Inflammation of the brain in Alzheimer's disease: Implications for therapy
    • McGeer P.L., McGeer E.G. Inflammation of the brain in Alzheimer's disease: implications for therapy. J. Leukoc. Biol. 65:1999;409.
    • (1999) J. Leukoc. Biol. , vol.65 , pp. 409
    • McGeer, P.L.1    McGeer, E.G.2
  • 65
    • 0028289083 scopus 로고
    • Inverse association of anti-inflammatory treatments and Alzheimer's disease: Initial results of a co-twin control study
    • Breitner J.C., Gau B.A., Welsh K.A.et al. Inverse association of anti-inflammatory treatments and Alzheimer's disease: initial results of a co-twin control study. Neurology. 44:1994;227.
    • (1994) Neurology , vol.44 , pp. 227
    • Breitner, J.C.1    Gau, B.A.2    Welsh, K.A.3
  • 66
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • McGeer P.L., Schulzer M., McGeer E.G. Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies. Neurology. 47:1996;425.
    • (1996) Neurology , vol.47 , pp. 425
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 67
    • 0027268393 scopus 로고
    • Clinical trial of indomethacin in Alzheimer's disease
    • Rogers J., Kirby L.C., Hempelman S.R.et al. Clinical trial of indomethacin in Alzheimer's disease. Neurology. 43:1993;1609.
    • (1993) Neurology , vol.43 , pp. 1609
    • Rogers, J.1    Kirby, L.C.2    Hempelman, S.R.3
  • 68
    • 33746673176 scopus 로고    scopus 로고
    • Analysis of 1184 gene transcript levels in Alzheimer CA1 hippocampus: Synaptic signaling and transcription factor deficits and upregulation of proinlammatory pathways
    • Lukiw W.J., Carver L.A., LeBlanc H.J., Bazan N.G. Analysis of 1184 gene transcript levels in Alzheimer CA1 hippocampus: synaptic signaling and transcription factor deficits and upregulation of proinlammatory pathways. Alzheimer's Reports. 3:2000;161.
    • (2000) Alzheimer's Reports , vol.3 , pp. 161
    • Lukiw, W.J.1    Carver, L.A.2    LeBlanc, H.J.3    Bazan, N.G.4
  • 69
    • 0026588059 scopus 로고
    • PG Endoperoxide synthase gene structure: Identification of the transcriptional start site and 5′-flanking regulatory sequences
    • Kraemer S.A., Meade E.A., DeWitt D.L. PG Endoperoxide synthase gene structure: identification of the transcriptional start site and 5′-flanking regulatory sequences. Arch. Biochem. Biophys. 293:1992;391.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 391
    • Kraemer, S.A.1    Meade, E.A.2    DeWitt, D.L.3
  • 70
    • 0026702494 scopus 로고
    • Structure of the mitogen-inducible TIS10 gene and demonstration that the TIS10-encoded protein is a functional PG G/H synthase
    • Fletcher B.S., Kujubu D.A., Perrin D.M., Herschman H.R. Structure of the mitogen-inducible TIS10 gene and demonstration that the TIS10-encoded protein is a functional PG G/H synthase. J. Biol. Chem. 267:1992;4338.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4338
    • Fletcher, B.S.1    Kujubu, D.A.2    Perrin, D.M.3    Herschman, H.R.4
  • 71
    • 0029040041 scopus 로고
    • Biochemistry of PG endoperoxide H synthase-1 and synthase-2 and their differential susceptibility to nonsteroidal anti-inflammatory drugs
    • Smith W.L., De Witt D.L. Biochemistry of PG endoperoxide H synthase-1 and synthase-2 and their differential susceptibility to nonsteroidal anti-inflammatory drugs. Semin. Nephrol. 15:1995;179.
    • (1995) Semin. Nephrol. , vol.15 , pp. 179
    • Smith, W.L.1    De Witt, D.L.2
  • 72
    • 0033558187 scopus 로고    scopus 로고
    • Regulation of COX-2 expression in human mesangial cells - Transcriptional inhibition by IL-13
    • Diaz-Cazorla M., Perez-Sala D., Ros J., Jimenez W., Fresno M., Lamas S. Regulation of COX-2 expression in human mesangial cells - transcriptional inhibition by IL-13. Eur. J. Biochem. 260:1999;268.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 268
    • Diaz-Cazorla, M.1    Perez-Sala, D.2    Ros, J.3    Jimenez, W.4    Fresno, M.5    Lamas, S.6
  • 73
    • 0033923351 scopus 로고    scopus 로고
    • Interferon-gamma and interleukin 4 inhibit interleukin 1 beta-induced delayed PG E(2) generation through suppression of COX-2 expression in human fibroblasts
    • Hayashi Y., Kobayashi M., Kuwata H.et al. Interferon-gamma and interleukin 4 inhibit interleukin 1 beta-induced delayed PG E(2) generation through suppression of COX-2 expression in human fibroblasts. Cytokine. 12:2000;603.
    • (2000) Cytokine , vol.12 , pp. 603
    • Hayashi, Y.1    Kobayashi, M.2    Kuwata, H.3
  • 75
    • 0032896588 scopus 로고    scopus 로고
    • COX-2: Molecular biology, pharmacology, and neurobiology
    • O'Banion M.K. COX-2: molecular biology, pharmacology, and neurobiology. Crit. Rev. Neurobiol. 13:1999;45.
    • (1999) Crit. Rev. Neurobiol. , vol.13 , pp. 45
    • O'Banion, M.K.1
  • 76
    • 0030033449 scopus 로고    scopus 로고
    • IL-13 and IL-4 inhibit bone resorption by suppressing COX-2-dependent PG synthesis in osteoblasts
    • Onoe Y., Miyaura C., Kaminakayashiki T. IL-13 and IL-4 inhibit bone resorption by suppressing COX-2-dependent PG synthesis in osteoblasts. J. Immunol. 156:1996;758.
    • (1996) J. Immunol. , vol.156 , pp. 758
    • Onoe, Y.1    Miyaura, C.2    Kaminakayashiki, T.3
  • 79
    • 0034302872 scopus 로고    scopus 로고
    • Neuroinflammatory signaling upregulation in Alzheimer's disease
    • Lukiw W.J., Bazan N.G. Neuroinflammatory signaling upregulation in Alzheimer's disease. Neurochem. Res. 25:2000;1173.
    • (2000) Neurochem. Res. , vol.25 , pp. 1173
    • Lukiw, W.J.1    Bazan, N.G.2
  • 80
    • 0032190264 scopus 로고    scopus 로고
    • COX and inflammation in Alzheimer's disease: Experimental approaches and clinical interventions
    • Pasinetti G.M. COX and inflammation in Alzheimer's disease: experimental approaches and clinical interventions. J. Neurosci. Res. 54:1998;1.
    • (1998) J. Neurosci. Res. , vol.54 , pp. 1
    • Pasinetti, G.M.1
  • 81
    • 0034924557 scopus 로고    scopus 로고
    • COX and Alzheimer's disease: Implications for preventive initiatives to slow the progression of clinical dementia
    • Pasinetti G.M. COX and Alzheimer's disease: implications for preventive initiatives to slow the progression of clinical dementia. Arch. Gerontol. Geriatr. 33:2001;13.
    • (2001) Arch. Gerontol. Geriatr. , vol.33 , pp. 13
    • Pasinetti, G.M.1
  • 82
    • 0027290813 scopus 로고
    • Expression of a mitogen-inducible COX in brain neurons
    • Yamagata K., Andreasson K.I., Kaufmann W.E.et al. Expression of a mitogen-inducible COX in brain neurons. Neuron. 11:1993;371.
    • (1993) Neuron , vol.11 , pp. 371
    • Yamagata, K.1    Andreasson, K.I.2    Kaufmann, W.E.3
  • 83
    • 0005233137 scopus 로고    scopus 로고
    • COX systems in the mammalian brain
    • Breder C.D. COX systems in the mammalian brain. Ann. NY Acad. Sci. 15:1997;813.
    • (1997) Ann. NY Acad. Sci. , vol.15 , pp. 813
    • Breder, C.D.1
  • 85
    • 0029995029 scopus 로고    scopus 로고
    • COX-2, a synaptically induced enzyme, is expressed by excitatory neurons at postsynaptic sites in rat cerebral cortex
    • Kaufmann W.E., Worley P.F., Pegg J., Bremer M., Isakson P. COX-2, a synaptically induced enzyme, is expressed by excitatory neurons at postsynaptic sites in rat cerebral cortex. Proc. Natl. Acad. Sci. USA. 93:1996;2317.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2317
    • Kaufmann, W.E.1    Worley, P.F.2    Pegg, J.3    Bremer, M.4    Isakson, P.5
  • 86
    • 0030000385 scopus 로고    scopus 로고
    • The role of anti-inflammatory drugs in the prevention and treatment of Alzheimer's disease
    • Breitner J.C. The role of anti-inflammatory drugs in the prevention and treatment of Alzheimer's disease. Annu. Rev. Med. 47:1996;401.
    • (1996) Annu. Rev. Med. , vol.47 , pp. 401
    • Breitner, J.C.1
  • 88
    • 0030897133 scopus 로고    scopus 로고
    • Risk of Alzheimer's disease and duration of NSAID use
    • Stewart W.F., Kawas C., Corrada M., Metter E.J. Risk of Alzheimer's disease and duration of NSAID use. Neurology. 48:1997;626.
    • (1997) Neurology , vol.48 , pp. 626
    • Stewart, W.F.1    Kawas, C.2    Corrada, M.3    Metter, E.J.4
  • 91
    • 0032725481 scopus 로고    scopus 로고
    • COX-1 in human Alzheimer and control brain: Quantitative analysis of expression by microglia and CA3 hippocampal neurons
    • Yermakova A.V., Rollins J., Callahan L.M., Rogers J., O'Banion M.K. COX-1 in human Alzheimer and control brain: quantitative analysis of expression by microglia and CA3 hippocampal neurons. J. Neuropathol. Exp. Neurol. 58:1999;1135.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 1135
    • Yermakova, A.V.1    Rollins, J.2    Callahan, L.M.3    Rogers, J.4    O'Banion, M.K.5
  • 92
    • 0031900411 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drug use and Alzheimer-type pathology in aging
    • Mackenzie I.R., Munoz D.G. Nonsteroidal anti-inflammatory drug use and Alzheimer-type pathology in aging. Neurology. 50:1998;986.
    • (1998) Neurology , vol.50 , pp. 986
    • Mackenzie, I.R.1    Munoz, D.G.2
  • 93
    • 0344863161 scopus 로고    scopus 로고
    • Regional distribution of PG H synthase-2 and neuronal nitric oxide synthase in piglet brain
    • Degi R., Bari F., Beasley T.C.et al. Regional distribution of PG H synthase-2 and neuronal nitric oxide synthase in piglet brain. Pediatr. Res. 43:1998;683.
    • (1998) Pediatr. Res. , vol.43 , pp. 683
    • Degi, R.1    Bari, F.2    Beasley, T.C.3
  • 94
    • 0030250598 scopus 로고    scopus 로고
    • PG G/H synthase-2 (COX-2) mRNA expression is decreased in Alzheimer's disease
    • Chang J.W., Coleman P.D., O'Banion M.K. PG G/H synthase-2 (COX-2) mRNA expression is decreased in Alzheimer's disease. Neurobiol. Aging. 17:1996;801.
    • (1996) Neurobiol. Aging , vol.17 , pp. 801
    • Chang, J.W.1    Coleman, P.D.2    O'Banion, M.K.3
  • 95
    • 0029953089 scopus 로고    scopus 로고
    • Interleukin-1 beta induces PG G/H synthase-2 (COX-2) in primary murine astrocyte cultures
    • O'Banion M.K., Miller J.C., Chang J.W., Kaplan M.D., Coleman P.D. Interleukin-1 beta induces PG G/H synthase-2 (COX-2) in primary murine astrocyte cultures. J. Neurochem. 66:1996;2532.
    • (1996) J. Neurochem. , vol.66 , pp. 2532
    • O'Banion, M.K.1    Miller, J.C.2    Chang, J.W.3    Kaplan, M.D.4    Coleman, P.D.5
  • 96
    • 0029915326 scopus 로고    scopus 로고
    • Effects of protein kinase c activation on PG production and COX mRNA levels in ovine astroglia
    • Nam M.J., Thore C., Busija D. Effects of protein kinase c activation on PG production and COX mRNA levels in ovine astroglia. Prostglandins. 51:1996;203.
    • (1996) Prostglandins , vol.51 , pp. 203
    • Nam, M.J.1    Thore, C.2    Busija, D.3
  • 97
    • 0031724850 scopus 로고    scopus 로고
    • Transforming growth factor beta 1 regulates the expression of COX in cultured cortical astrocytes and neurons
    • Luo J., Lang J.A., Miller M.W. Transforming growth factor beta 1 regulates the expression of COX in cultured cortical astrocytes and neurons. J. Neurochem. 71:1998;526.
    • (1998) J. Neurochem. , vol.71 , pp. 526
    • Luo, J.1    Lang, J.A.2    Miller, M.W.3
  • 98
    • 0031862558 scopus 로고    scopus 로고
    • The effect of nitric oxide on cytokine-induced release of PGE2 by human cultured astroglial cells
    • Mollace V., Colasanti M., Muscoli C.et al. The effect of nitric oxide on cytokine-induced release of PGE2 by human cultured astroglial cells. Br. J. Pharmacol. 124:1998;742.
    • (1998) Br. J. Pharmacol. , vol.124 , pp. 742
    • Mollace, V.1    Colasanti, M.2    Muscoli, C.3
  • 99
    • 0034745370 scopus 로고    scopus 로고
    • Interleukin-1 beta induced COX 2 expression and PG E2 secretion by human neuroblastoma cells: Implications for Alzheimer's disease
    • Hoozemans J.J., Veerhuis R., Janssen I., Rozemuller A.J., Eikelenboom P. Interleukin-1 beta induced COX 2 expression and PG E2 secretion by human neuroblastoma cells: implications for Alzheimer's disease. Exp. Gerontol. 36:2001;559.
    • (2001) Exp. Gerontol. , vol.36 , pp. 559
    • Hoozemans, J.J.1    Veerhuis, R.2    Janssen, I.3    Rozemuller, A.J.4    Eikelenboom, P.5
  • 101
    • 0033526660 scopus 로고    scopus 로고
    • Distribution of COX-1 and COX-2 mRNAs and proteins in human brain and peripheral organs
    • Yasojima K., Schwab C., McGeer E.G., McGeer P.L. Distribution of COX-1 and COX-2 mRNAs and proteins in human brain and peripheral organs. Brain Res. 830:1999;226.
    • (1999) Brain Res. , vol.830 , pp. 226
    • Yasojima, K.1    Schwab, C.2    McGeer, E.G.3    McGeer, P.L.4
  • 102
    • 0033876817 scopus 로고    scopus 로고
    • Cytokine gene expression as a function of the clinical progression of Alzheimer disease Dementia
    • Luterman J.D., Haroutunian V., Yemul S.et al. Cytokine gene expression as a function of the clinical progression of Alzheimer disease Dementia. Arch. Neurol. 57:2000;1153.
    • (2000) Arch. Neurol. , vol.57 , pp. 1153
    • Luterman, J.D.1    Haroutunian, V.2    Yemul, S.3
  • 103
    • 0028926976 scopus 로고
    • Interleukin-1 expression in different plaque types in Alzheimer's disease: Significance in plaque evolution
    • Griffin W.S., Sheng J.G., Roberts G.W., Mrak R.E. Interleukin-1 expression in different plaque types in Alzheimer's disease: significance in plaque evolution. J. Neuropathol. Exp. Neurol. 54:1995;276.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 276
    • Griffin, W.S.1    Sheng, J.G.2    Roberts, G.W.3    Mrak, R.E.4
  • 104
    • 0029051259 scopus 로고
    • Interleukin-6 is present in early stages of plaque formation and is restricted to the brains of Alzheimer's disease patients
    • Huell M., Strauss S., Volk B., Berger M., Bauer J. Interleukin-6 is present in early stages of plaque formation and is restricted to the brains of Alzheimer's disease patients. Acta Neuropathol. (Berl.). 89:1995;544.
    • (1995) Acta Neuropathol. (Berl.) , vol.89 , pp. 544
    • Huell, M.1    Strauss, S.2    Volk, B.3    Berger, M.4    Bauer, J.5
  • 105
    • 0026553710 scopus 로고
    • Detection of interleukin-6 and alpha 2-macroglobulin immunoreactivity in cortex and hippocampus of Alzheimer's disease patients
    • Strauss S., Bauer J., Ganter U., Jonas U., Berger M., Volk B. Detection of interleukin-6 and alpha 2-macroglobulin immunoreactivity in cortex and hippocampus of Alzheimer's disease patients. Lab. Invest. 66:1992;223.
    • (1992) Lab. Invest. , vol.66 , pp. 223
    • Strauss, S.1    Bauer, J.2    Ganter, U.3    Jonas, U.4    Berger, M.5    Volk, B.6
  • 106
    • 0028937265 scopus 로고
    • Enhanced processing of APP Induced by IL-1 beta can be reduced by indomethacin and nordihydroguaiaretic acid
    • Dash P.K., Moore A.N. Enhanced processing of APP Induced by IL-1 beta can be reduced by indomethacin and nordihydroguaiaretic acid. Biochem. Biophys. Res. Commun. 208:1995;542.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 542
    • Dash, P.K.1    Moore, A.N.2
  • 107
    • 0030614598 scopus 로고    scopus 로고
    • Prostaglandin E2 induces interleukin-6 synthesis in human astrocytoma cells
    • Fiebich B.L., Hull M., Lieb K., Gyufko K., Berger M., Bauer J. Prostaglandin E2 induces interleukin-6 synthesis in human astrocytoma cells. J. Neurochem. 68:1997;704.
    • (1997) J. Neurochem. , vol.68 , pp. 704
    • Fiebich, B.L.1    Hull, M.2    Lieb, K.3    Gyufko, K.4    Berger, M.5    Bauer, J.6
  • 108
    • 0030951257 scopus 로고    scopus 로고
    • Induction of cyclooxygenase 2 in brains of patients with down's syndrome and dementia of Alzheimer type: Specific localization in affected neurones and axons
    • Oka A., Takashima S. Induction of cyclooxygenase 2 in brains of patients with down's syndrome and dementia of Alzheimer type: specific localization in affected neurones and axons. Neuroreport. 8:1997;1161.
    • (1997) Neuroreport , vol.8 , pp. 1161
    • Oka, A.1    Takashima, S.2
  • 110
    • 0030031692 scopus 로고    scopus 로고
    • COX-2 induction in cerebral cortex: An intracellular response to synaptic excitation
    • Adams J., Collaço-Moraes Y., de Belleroche J. COX-2 induction in cerebral cortex: an intracellular response to synaptic excitation. J. Neurochem. 66:1996;6.
    • (1996) J. Neurochem. , vol.66 , pp. 6
    • Adams, J.1    Collaço-Moraes, Y.2    De Belleroche, J.3
  • 111
    • 0030782939 scopus 로고    scopus 로고
    • Excitotoxic neurodegeneration in Alzheimer disease. new hypothesis and new therapeutic strategies
    • Olney J.W., Wozniak D.F., Farber N.B. Excitotoxic neurodegeneration in Alzheimer disease. new hypothesis and new therapeutic strategies. Arch. Neurol. 54:1997;1234.
    • (1997) Arch. Neurol. , vol.54 , pp. 1234
    • Olney, J.W.1    Wozniak, D.F.2    Farber, N.B.3
  • 112
    • 0030906889 scopus 로고    scopus 로고
    • Lesioning of deep prepiriform cortex protects against ischemic neuronal necrosis by attenuating extracellular glutamate concentrations
    • Kawaguchi K., Huerbin M., Simon R.P. Lesioning of deep prepiriform cortex protects against ischemic neuronal necrosis by attenuating extracellular glutamate concentrations. J. Neurochem. 69:1997;412.
    • (1997) J. Neurochem. , vol.69 , pp. 412
    • Kawaguchi, K.1    Huerbin, M.2    Simon, R.P.3
  • 113
    • 0032887341 scopus 로고    scopus 로고
    • Potentiation of excitotoxicity in transgenic mice overexpressing neuronal COX-2
    • Kelley K.A., Ho L., Winger D.et al. Potentiation of excitotoxicity in transgenic mice overexpressing neuronal COX-2. Am. J. Pathol. 155:1999;995.
    • (1999) Am. J. Pathol. , vol.155 , pp. 995
    • Kelley, K.A.1    Ho, L.2    Winger, D.3
  • 114
    • 0035013564 scopus 로고    scopus 로고
    • Brain oxidative stress in animal models of accelerated aging and the age-related neurodegenerative disorders, Alzheimer's disease and Huntington's disease
    • Butterfield D.A., Howard B.J., LaFontaine M.A. Brain oxidative stress in animal models of accelerated aging and the age-related neurodegenerative disorders, Alzheimer's disease and Huntington's disease. Curr. Med. Chem. 8:2001;815.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 815
    • Butterfield, D.A.1    Howard, B.J.2    LaFontaine, M.A.3
  • 115
    • 0024435515 scopus 로고
    • Arachidonic acid and its metabolites in cerebral ischemia
    • Hsu C.Y., Liu T.H., Xu J.et al. Arachidonic acid and its metabolites in cerebral ischemia. Ann. NY Acad. Sci. 559:1989;282.
    • (1989) Ann. NY Acad. Sci. , vol.559 , pp. 282
    • Hsu, C.Y.1    Liu, T.H.2    Xu, J.3
  • 116
    • 0030475604 scopus 로고    scopus 로고
    • Peroxynitrite, the coupling product of nitric oxide and superoxide, activates prostaglandin biosynthesis
    • Landino L.M., Crews B.C., Timmons M.D., Morrow J.D., Marnett L.J. Peroxynitrite, the coupling product of nitric oxide and superoxide, activates prostaglandin biosynthesis. Proc. Natl. Acad. Sci. USA. 93:1996;15069.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15069
    • Landino, L.M.1    Crews, B.C.2    Timmons, M.D.3    Morrow, J.D.4    Marnett, L.J.5
  • 118
    • 0034302893 scopus 로고    scopus 로고
    • Isoprostanes, novel markers of oxidative injury, help understanding the pathogenesis of neurodegenerative diseases
    • Greco A., Minghetti L., Levi G. Isoprostanes, novel markers of oxidative injury, help understanding the pathogenesis of neurodegenerative diseases. Neurochem. Res. 25:2000;1357.
    • (2000) Neurochem. Res. , vol.25 , pp. 1357
    • Greco, A.1    Minghetti, L.2    Levi, G.3
  • 119
    • 0035875690 scopus 로고    scopus 로고
    • Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis
    • Pratico D., Uryu K., Leight S., Trojanoswki J.Q., Lee V.M. Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis. J. Neurosci. 21:2001;4183.
    • (2001) J. Neurosci. , vol.21 , pp. 4183
    • Pratico, D.1    Uryu, K.2    Leight, S.3    Trojanoswki, J.Q.4    Lee, V.M.5
  • 120
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry R.D., Masliah E., Salmon D.P. Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol. 30:1991;572.
    • (1991) Ann. Neurol. , vol.30 , pp. 572
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3
  • 122
    • 0023128721 scopus 로고
    • Dementia of the Alzheimer type: Clinical and familial study of 22 twin pairs
    • Nee L.E., Eldridge R., Sunderland T. Dementia of the Alzheimer type: clinical and familial study of 22 twin pairs. Neurology. 37:1987;359.
    • (1987) Neurology , vol.37 , pp. 359
    • Nee, L.E.1    Eldridge, R.2    Sunderland, T.3
  • 123
    • 0025994384 scopus 로고
    • Discordance and concordance of dementia of the Alzheimer type (DAT) in monozygotic twins indicate heritable and sporadic forms of Alzheimer's disease
    • Rapoport S.I., Pettigrew K.D., Schapiro M.B. Discordance and concordance of dementia of the Alzheimer type (DAT) in monozygotic twins indicate heritable and sporadic forms of Alzheimer's disease. Neurology. 41:1991;1549.
    • (1991) Neurology , vol.41 , pp. 1549
    • Rapoport, S.I.1    Pettigrew, K.D.2    Schapiro, M.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.