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Volumn 44, Issue 3 SUPPL. 1, 1998, Pages

Determinants of neuronal vulnerability in neurodegenerative diseases

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; ASSOCIATION CORTEX; CONFERENCE PAPER; DEGENERATIVE DISEASE; ENTORHINAL CORTEX; HUMAN; NERVE CELL; NEUROFILAMENT; NEUROPATHOLOGY; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; SPINAL CORD NERVE CELL;

EID: 0031668928     PISSN: 03645134     EISSN: None     Source Type: Journal    
DOI: 10.1002/ana.410440706     Document Type: Conference Paper
Times cited : (101)

References (158)
  • 1
    • 0027452912 scopus 로고
    • Differential vulnerability, connectivity, and cell typology
    • Morrison JH. Differential vulnerability, connectivity, and cell typology. Neurobiol Aging 1993;14:51-54
    • (1993) Neurobiol Aging , vol.14 , pp. 51-54
    • Morrison, J.H.1
  • 2
    • 0023278930 scopus 로고
    • A monoclonal antibody to non-phosphorylated neurofilament protein marks the vulnerable cortical neurons in Alzheimer's disease
    • Morrison JH, Lewis DA, Campbell MJ, et al. A monoclonal antibody to non-phosphorylated neurofilament protein marks the vulnerable cortical neurons in Alzheimer's disease. Brain Res 1987;416:331-336
    • (1987) Brain Res , vol.416 , pp. 331-336
    • Morrison, J.H.1    Lewis, D.A.2    Campbell, M.J.3
  • 3
    • 0025163133 scopus 로고
    • Quantitative analysis of a vulnerable subset of pyramidal neurons in Alzheimer's disease: II. Primary and secondary visual cortex
    • Hof PR, Morrison JH. Quantitative analysis of a vulnerable subset of pyramidal neurons in Alzheimer's disease: II. Primary and secondary visual cortex. J Comp Neurol 1990;301:55-64
    • (1990) J Comp Neurol , vol.301 , pp. 55-64
    • Hof, P.R.1    Morrison, J.H.2
  • 4
    • 0025036899 scopus 로고
    • Quantitative analysis of a vulnerable subset of pyramidal neurons in Alzheimer's disease: I. Superior frontal and inferior temporal cortex
    • Hof PR, Cox K, Morrison JH. Quantitative analysis of a vulnerable subset of pyramidal neurons in Alzheimer's disease: I. Superior frontal and inferior temporal cortex. J Comp Neurol 1990;301:44-54
    • (1990) J Comp Neurol , vol.301 , pp. 44-54
    • Hof, P.R.1    Cox, K.2    Morrison, J.H.3
  • 5
    • 0025327731 scopus 로고
    • Unbiased stereological estimation of the number of neurons in the human hippocampus
    • West MJ, Gundersen HJG. Unbiased stereological estimation of the number of neurons in the human hippocampus. J Comp Neurol 1990;296:1-22
    • (1990) J Comp Neurol , vol.296 , pp. 1-22
    • West, M.J.1    Gundersen, H.J.G.2
  • 6
    • 0026564018 scopus 로고
    • Progressive transformation of the cytoskeleton associated with normal aging and Alzheimer's disease
    • Vickers JC, Delacourte A, Morrison JH. Progressive transformation of the cytoskeleton associated with normal aging and Alzheimer's disease. Brain Res 1992;594:273-278
    • (1992) Brain Res , vol.594 , pp. 273-278
    • Vickers, J.C.1    Delacourte, A.2    Morrison, J.H.3
  • 7
    • 0027164617 scopus 로고
    • Regionally specific loss of neurons in the aging human hippocampus
    • West MJ. Regionally specific loss of neurons in the aging human hippocampus. Neurobiol Aging 1993;14:287-293
    • (1993) Neurobiol Aging , vol.14 , pp. 287-293
    • West, M.J.1
  • 8
    • 0002377794 scopus 로고
    • The cellular basis of cortical disconnection in Alzheimer's disease and related dementing conditions
    • Terry R, Katzman R, Bick K, eds. New York: Raven Press
    • Hof PR, Morrison JH. The cellular basis of cortical disconnection in Alzheimer's disease and related dementing conditions. In: Terry R, Katzman R, Bick K, eds. Alzheimer's disease. New York: Raven Press, 1994:197-229
    • (1994) Alzheimer's Disease , pp. 197-229
    • Hof, P.R.1    Morrison, J.H.2
  • 9
    • 0028101798 scopus 로고
    • Alterations in neurofilament protein immunoreactivity in human hippocampal neurons related to normal aging and Alzheimer's disease
    • Vickers JC, Riederer BM, Marugg RA, et al. Alterations in neurofilament protein immunoreactivity in human hippocampal neurons related to normal aging and Alzheimer's disease. Neuroscience 1994;62:1-13
    • (1994) Neuroscience , vol.62 , pp. 1-13
    • Vickers, J.C.1    Riederer, B.M.2    Marugg, R.A.3
  • 10
    • 0028122463 scopus 로고
    • Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease
    • West MJ, Coleman PD, Flood DG, Troncoso JC. Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease. Lancet 1994;344:769-772
    • (1994) Lancet , vol.344 , pp. 769-772
    • West, M.J.1    Coleman, P.D.2    Flood, D.G.3    Troncoso, J.C.4
  • 11
    • 0030249343 scopus 로고    scopus 로고
    • Dystrophic neurite formation associated with age-related β amyloid deposition in the neocortex: Clues to the genesis of neurofibrillary pathology
    • Vickers JC, Chin D, Edwards AM, et al. Dystrophic neurite formation associated with age-related β amyloid deposition in the neocortex: clues to the genesis of neurofibrillary pathology. Exp Neurol 1996;141:1-11
    • (1996) Exp Neurol , vol.141 , pp. 1-11
    • Vickers, J.C.1    Chin, D.2    Edwards, A.M.3
  • 12
    • 0029979798 scopus 로고    scopus 로고
    • Profound loss of layer II entorhinal cortex neurons occurs in very mild Alzheimer's disease
    • Gómez-Isla T, Price JL, McKeel Jr DW, et al. Profound loss of layer II entorhinal cortex neurons occurs in very mild Alzheimer's disease. J Neurosci 1996;16:4491-4500
    • (1996) J Neurosci , vol.16 , pp. 4491-4500
    • Gómez-Isla, T.1    Price, J.L.2    McKeel Jr., D.W.3
  • 13
    • 0344653664 scopus 로고    scopus 로고
    • Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
    • Gómez-Isla T, Hollister R, West H, et al. Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease. Ann Neurol 1997;41:17-24
    • (1997) Ann Neurol , vol.41 , pp. 17-24
    • Gómez-Isla, T.1    Hollister, R.2    West, H.3
  • 14
    • 0030698871 scopus 로고    scopus 로고
    • Life and death of neurons in the aging brain
    • Morrison JH, Hof PR. Life and death of neurons in the aging brain. Science 1997;278:412-419
    • (1997) Science , vol.278 , pp. 412-419
    • Morrison, J.H.1    Hof, P.R.2
  • 15
    • 0031046970 scopus 로고    scopus 로고
    • Volume and number of neurons of the human hippocampal formation in normal aging and Alzheimer's disease
    • Simic G, Kostovic I, Winblad B, Bodganovic N. Volume and number of neurons of the human hippocampal formation in normal aging and Alzheimer's disease. J Comp Neurol 1997; 379:482-494
    • (1997) J Comp Neurol , vol.379 , pp. 482-494
    • Simic, G.1    Kostovic, I.2    Winblad, B.3    Bodganovic, N.4
  • 16
    • 0030966675 scopus 로고    scopus 로고
    • A cellular mechanism for the neuronal changes underlying Alzheimer's disease
    • Vickers JC. A cellular mechanism for the neuronal changes underlying Alzheimer's disease. Neuroscience 1997;78:629-639
    • (1997) Neuroscience , vol.78 , pp. 629-639
    • Vickers, J.C.1
  • 17
    • 0022841816 scopus 로고
    • Ratio of pyramidal cells versus nonpyramidal cells in the human frontal isocortex and changes in ratio with ageing and Alzheimer's disease
    • Swaab DF, Fliers E, Mirmiran M, Van Gool VA, Van Haaren F, eds. Amsterdam: Elsevier
    • Braak H, Brank E. Ratio of pyramidal cells versus nonpyramidal cells in the human frontal isocortex and changes in ratio with ageing and Alzheimer's disease. In: Swaab DF, Fliers E, Mirmiran M, Van Gool VA, Van Haaren F, eds. Aging of the brain and Alzheimer's disease. Amsterdam: Elsevier, 1986:185-212
    • (1986) Aging of the Brain and Alzheimer's Disease , pp. 185-212
    • Braak, H.1    Brank, E.2
  • 18
    • 0029857822 scopus 로고    scopus 로고
    • Distinct patterns of neuronal loss and Alzheimer's disease lesion distribution in elderly individuals older than 90 years
    • Giannakopoulos P, Hof PR, Kövari E, et al. Distinct patterns of neuronal loss and Alzheimer's disease lesion distribution in elderly individuals older than 90 years. J Neuropathol Exp Neurol 1996;55:1110-1120
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1110-1120
    • Giannakopoulos, P.1    Hof, P.R.2    Kövari, E.3
  • 19
    • 0002918293 scopus 로고
    • Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ
    • Sternberger LA, Sternberger NH. Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ. Proc Natl Acad Sci USA 1983;80:6126-6130
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 6126-6130
    • Sternberger, L.A.1    Sternberger, N.H.2
  • 20
    • 0023520075 scopus 로고
    • Monoclonal antibodies distinguish several differentially phosphorylated states of the two largest rat neurofilament subunits (NF-H and NF-M) and demonstrate their existence in the normal nervous system of adult rats
    • Lee VM, Carden MJ, Schlaepfer WW, Trojanowski JQ. Monoclonal antibodies distinguish several differentially phosphorylated states of the two largest rat neurofilament subunits (NF-H and NF-M) and demonstrate their existence in the normal nervous system of adult rats. J Neurosci 1987;7:3474-3488
    • (1987) J Neurosci , vol.7 , pp. 3474-3488
    • Lee, V.M.1    Carden, M.J.2    Schlaepfer, W.W.3    Trojanowski, J.Q.4
  • 21
    • 0023942881 scopus 로고
    • Neurofilament phosphorylation in axons and perikarya: Immunofluorescence study of the rat spinal cord and dorsal root ganglia with monoclonal antibodies
    • Dahl D, Labkovsky B, Bignami A. Neurofilament phosphorylation in axons and perikarya: immunofluorescence study of the rat spinal cord and dorsal root ganglia with monoclonal antibodies. J Comp Neurol 1988;271:445-450
    • (1988) J Comp Neurol , vol.271 , pp. 445-450
    • Dahl, D.1    Labkovsky, B.2    Bignami, A.3
  • 22
    • 0024550350 scopus 로고
    • Monoclonal antibody to neurofilament protein (SMI-32) labels a subpopulation of pyramidal neurons in the human and monkey neocortex
    • Campbell MJ, Morrison JH. Monoclonal antibody to neurofilament protein (SMI-32) labels a subpopulation of pyramidal neurons in the human and monkey neocortex. J Comp Neurol 1989;282:191-205
    • (1989) J Comp Neurol , vol.282 , pp. 191-205
    • Campbell, M.J.1    Morrison, J.H.2
  • 23
    • 0342519699 scopus 로고
    • Recognition of tau epitopes by anti-neurofilament antibodies that bind to Alzheimer neurofibrillary tangles
    • Ksiezak-Reding H, Dickson DW, Davies P, Yen SH. Recognition of tau epitopes by anti-neurofilament antibodies that bind to Alzheimer neurofibrillary tangles. Proc Natl Acad Sci USA 1987;84:3410-3414
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3410-3414
    • Ksiezak-Reding, H.1    Dickson, D.W.2    Davies, P.3    Yen, S.H.4
  • 24
  • 25
    • 0027479150 scopus 로고
    • Altered tau and neurofilament proteins in neurodegenerative diseases: Diagnostic implications for Alzheimer's disease and Lewy body dementias
    • Trojanowski JQ, Schmidt ML, Shin R-W, et al. Altered tau and neurofilament proteins in neurodegenerative diseases: diagnostic implications for Alzheimer's disease and Lewy body dementias. Brain Pathol 1993;3:45-54
    • (1993) Brain Pathol , vol.3 , pp. 45-54
    • Trojanowski, J.Q.1    Schmidt, M.L.2    Shin, R.-W.3
  • 26
    • 0028957486 scopus 로고
    • Neurofilament protein defines regional patterns of cortical organization in the macaque monkey visual system: A quantitative immunohistochemical analysis
    • Hof PR, Morrison JH. Neurofilament protein defines regional patterns of cortical organization in the macaque monkey visual system: a quantitative immunohistochemical analysis. J Comp Neurol 1995;352:161-186
    • (1995) J Comp Neurol , vol.352 , pp. 161-186
    • Hof, P.R.1    Morrison, J.H.2
  • 27
    • 0026949496 scopus 로고
    • Regional distribution of neurofilament and calcium-binding proteins in the cingulate cortex of the macaque monkey
    • Hof PR, Nimchinsky EA. Regional distribution of neurofilament and calcium-binding proteins in the cingulate cortex of the macaque monkey. Cereb Cortex 1992;2:456-467
    • (1992) Cereb Cortex , vol.2 , pp. 456-467
    • Hof, P.R.1    Nimchinsky, E.A.2
  • 28
    • 0028868528 scopus 로고
    • Neurochemical phenorype of corticocortical connections in the macaque monkey: Quantitative analysis of a subset of neurofilament protein-immunoreactive projection neurons in frontal, parietal, temporal, and cingulate cortices
    • Hof PR, Nimchinsky EA, Morrison JH. Neurochemical phenorype of corticocortical connections in the macaque monkey: quantitative analysis of a subset of neurofilament protein-immunoreactive projection neurons in frontal, parietal, temporal, and cingulate cortices. J Comp Neurol 1995;362:109-133
    • (1995) J Comp Neurol , vol.362 , pp. 109-133
    • Hof, P.R.1    Nimchinsky, E.A.2    Morrison, J.H.3
  • 30
    • 0030792364 scopus 로고    scopus 로고
    • Neurofilament and calcium-binding proteins in the human cingulate cortex
    • Nimchinsky EA, Vogt BA, Morrison JH, Hof PR. Neurofilament and calcium-binding proteins in the human cingulate cortex. J Comp Neurol 1997;384:597-620
    • (1997) J Comp Neurol , vol.384 , pp. 597-620
    • Nimchinsky, E.A.1    Vogt, B.A.2    Morrison, J.H.3    Hof, P.R.4
  • 31
    • 0026029966 scopus 로고
    • A subpopulation of primate corticocortical neurons is distinguished by somatodendritic distribution of neurofilament protein
    • Campbell MJ, Hof PR, Morrison JH. A subpopulation of primate corticocortical neurons is distinguished by somatodendritic distribution of neurofilament protein. Brain Res 1991; 539:133-136
    • (1991) Brain Res , vol.539 , pp. 133-136
    • Campbell, M.J.1    Hof, P.R.2    Morrison, J.H.3
  • 32
    • 0029849966 scopus 로고    scopus 로고
    • Neurofilament protein is differentially distributed in subpopulations of corticocortical projection neurons in the macaque monkey visual pathways
    • Hof PR, Ungerleider LG, Webster MJ, et al. Neurofilament protein is differentially distributed in subpopulations of corticocortical projection neurons in the macaque monkey visual pathways. J Comp Neurol 1996;376:112-127
    • (1996) J Comp Neurol , vol.376 , pp. 112-127
    • Hof, P.R.1    Ungerleider, L.G.2    Webster, M.J.3
  • 33
    • 0008474992 scopus 로고    scopus 로고
    • Morphologic and neurochemical characteristics of corticocortical projections: Emergence of circuit-specific features and relationships to degenerative changes in Alzheimer's disease
    • Hyman BT, Duyckaerts C, Christen Y, eds. Berlin: Springer-Verlag
    • Hof PR, Nimchinsky EA, Ungerleider LG, Morrison JH. Morphologic and neurochemical characteristics of corticocortical projections: emergence of circuit-specific features and relationships to degenerative changes in Alzheimer's disease. In: Hyman BT, Duyckaerts C, Christen Y, eds. Connections, cognition, and Alzheimer's disease. Berlin: Springer-Verlag, 1997: 59-82
    • (1997) Connections, Cognition, and Alzheimer's Disease , pp. 59-82
    • Hof, P.R.1    Nimchinsky, E.A.2    Ungerleider, L.G.3    Morrison, J.H.4
  • 34
    • 0031240016 scopus 로고    scopus 로고
    • Callosally-projecting neurons in the macaque monkey V1/V2 border are enriched in nonphosphorylated neurofilament protein
    • Hof PR, Ungerleider LG, Adams MM, et al. Callosally-projecting neurons in the macaque monkey V1/V2 border are enriched in nonphosphorylated neurofilament protein. Vis Neurosci 1997;14:981-987
    • (1997) Vis Neurosci , vol.14 , pp. 981-987
    • Hof, P.R.1    Ungerleider, L.G.2    Adams, M.M.3
  • 35
    • 0029795679 scopus 로고    scopus 로고
    • Neurochemical, morphologic and laminar characterization of cortical projection neurons in the cingulate motor areas of the macaque monkey
    • Nimchinsky EA, Hof PR, Young WG, Morrison JH. Neurochemical, morphologic and laminar characterization of cortical projection neurons in the cingulate motor areas of the macaque monkey. J Comp Neurol 1996;374:136-160
    • (1996) J Comp Neurol , vol.374 , pp. 136-160
    • Nimchinsky, E.A.1    Hof, P.R.2    Young, W.G.3    Morrison, J.H.4
  • 36
    • 0023870521 scopus 로고
    • Pharmacology of glutamate neurotoxicity in cortical cell culture: Attenuation by NMDA antagonists
    • Choi DW, Koh J, Peters S. Pharmacology of glutamate neurotoxicity in cortical cell culture: attenuation by NMDA antagonists. J Neurosci 1988;8:185-196
    • (1988) J Neurosci , vol.8 , pp. 185-196
    • Choi, D.W.1    Koh, J.2    Peters, S.3
  • 37
    • 0025265926 scopus 로고
    • The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death
    • Choi DW, Rothman SM. The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death. Annu Rev Neurosci 1990;13:171-182
    • (1990) Annu Rev Neurosci , vol.13 , pp. 171-182
    • Choi, D.W.1    Rothman, S.M.2
  • 38
    • 0025470262 scopus 로고
    • Cerebral hypoxia: Some new approaches and unanswered questions
    • Choi DW. Cerebral hypoxia: some new approaches and unanswered questions. J Neurosci 1990;10:2493-2501
    • (1990) J Neurosci , vol.10 , pp. 2493-2501
    • Choi, D.W.1
  • 39
    • 0025063609 scopus 로고
    • Excitatory amino acid neurotoxicity and neurodegenerative disease
    • Meldrum B, Garthwaite J. Excitatory amino acid neurotoxicity and neurodegenerative disease. Trends Pharmacol Sci 1990;11:379-387
    • (1990) Trends Pharmacol Sci , vol.11 , pp. 379-387
    • Meldrum, B.1    Garthwaite, J.2
  • 41
    • 0025883589 scopus 로고
    • Excitatory amino acid receptors, neural membrane phospholipid metabolism and neurological disorders
    • Farooqui AA, Horrocks LA. Excitatory amino acid receptors, neural membrane phospholipid metabolism and neurological disorders. Brain Res Rev 1991;16:171-191
    • (1991) Brain Res Rev , vol.16 , pp. 171-191
    • Farooqui, A.A.1    Horrocks, L.A.2
  • 42
    • 0002858344 scopus 로고
    • Excitatory amino acid neurotoxicity and neurodegenerative diseases
    • Meldrum B, Garthwaite J. Excitatory amino acid neurotoxicity and neurodegenerative diseases. Trends Pharmacol Sci 1991;11:54-61
    • (1991) Trends Pharmacol Sci , vol.11 , pp. 54-61
    • Meldrum, B.1    Garthwaite, J.2
  • 43
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle JT, Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science 1993;262:689-695
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 44
    • 0027269660 scopus 로고
    • Cortical pyramidal neurone loss may cause glutamatergic hypoactivity and cognitive impairment in Alzheimer's disease: Investigative and therapeutic perspectives
    • Francis PT, Sims NR, Procter AW, Bowen DM. Cortical pyramidal neurone loss may cause glutamatergic hypoactivity and cognitive impairment in Alzheimer's disease: investigative and therapeutic perspectives. J Neurochem 1993;61:1589-1594
    • (1993) J Neurochem , vol.61 , pp. 1589-1594
    • Francis, P.T.1    Sims, N.R.2    Procter, A.W.3    Bowen, D.M.4
  • 45
    • 0028069874 scopus 로고
    • Microzonal decreases in the immunostaining for non-NMDA ionotropic excitatory amino acid receptor subunits GluR2/3 and GluR5/6/7 in the human epileptogenic neocortex
    • DeFelipe J, Huntley GW, del Rio MR, et al. Microzonal decreases in the immunostaining for non-NMDA ionotropic excitatory amino acid receptor subunits GluR2/3 and GluR5/6/7 in the human epileptogenic neocortex. Brain Res 1994; 657:150-158
    • (1994) Brain Res , vol.657 , pp. 150-158
    • DeFelipe, J.1    Huntley, G.W.2    Del Rio, M.R.3
  • 46
    • 0028934737 scopus 로고
    • The N-methyl-D-aspartate antagonists phencyclidine, ketamine and dizocilpine as both behavioral and anatomical models of the dementias
    • Ellison G. The N-methyl-D-aspartate antagonists phencyclidine, ketamine and dizocilpine as both behavioral and anatomical models of the dementias. Brain Res Rev 1995;20:250-267
    • (1995) Brain Res Rev , vol.20 , pp. 250-267
    • Ellison, G.1
  • 47
    • 0028762647 scopus 로고
    • Excitatory amino acids as a final common pathway for neurologic disorders
    • Lipton SA, Rosenberg PA. Excitatory amino acids as a final common pathway for neurologic disorders. N Engl J Med 1995;330:613-622
    • (1995) N Engl J Med , vol.330 , pp. 613-622
    • Lipton, S.A.1    Rosenberg, P.A.2
  • 48
    • 0029806084 scopus 로고    scopus 로고
    • Altered distribution of α-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit GluR2(4) and N-methyl-D-aspartate receptor subunit NMDAR1 in the hippocampus of patients with temporal lobe epilepsy
    • Blümcke I, Beck H, Scheffler B, et al. Altered distribution of α-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit GluR2(4) and N-methyl-D-aspartate receptor subunit NMDAR1 in the hippocampus of patients with temporal lobe epilepsy. Acta Neuropathol (Berl) 1996;92:576-587
    • (1996) Acta Neuropathol (Berl) , vol.92 , pp. 576-587
    • Blümcke, I.1    Beck, H.2    Scheffler, B.3
  • 49
    • 0011746121 scopus 로고    scopus 로고
    • Glutamate receptors: Emerging links between subunit proteins and specific excitatory circuits in primate hippocampus and neocortex
    • Morrison JH, Siegel SJ, Gazzaley AH, Huntley GW. Glutamate receptors: emerging links between subunit proteins and specific excitatory circuits in primate hippocampus and neocortex. Neuroscientist 1996;2:272-283
    • (1996) Neuroscientist , vol.2 , pp. 272-283
    • Morrison, J.H.1    Siegel, S.J.2    Gazzaley, A.H.3    Huntley, G.W.4
  • 50
    • 0030293629 scopus 로고    scopus 로고
    • Ischemic disruption of glutamate homeostasis in brain: Quantitative immunocytochemical analyses
    • Ottersen OP, Laake JH, Reichelt W, et al. Ischemic disruption of glutamate homeostasis in brain: quantitative immunocytochemical analyses. J Chem Neuroanat 1996;12:1-14
    • (1996) J Chem Neuroanat , vol.12 , pp. 1-14
    • Ottersen, O.P.1    Laake, J.H.2    Reichelt, W.3
  • 51
    • 0026041623 scopus 로고
    • Slow non-NMDA receptor mediated neurotoxicity and amyotrophic lateral sclerosis
    • Rowland LP, ed. New York: Raven Press
    • Weiss JH, Choi DW. Slow non-NMDA receptor mediated neurotoxicity and amyotrophic lateral sclerosis. In: Rowland LP, ed. Amyotrophic lateral sclerosis and other motor neuron diseases. New York: Raven Press, 1991:311-318
    • (1991) Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases , pp. 311-318
    • Weiss, J.H.1    Choi, D.W.2
  • 52
    • 0023137252 scopus 로고
    • Ionic dependence of glutamate neurotoxicity
    • Choi DW. Ionic dependence of glutamate neurotoxicity. J Neurosci 1987;7:369-379
    • (1987) J Neurosci , vol.7 , pp. 369-379
    • Choi, D.W.1
  • 53
    • 0027337920 scopus 로고
    • 2+ chelators reduce early excitotoxic and ischemic neuronal injury in vitro and in vivo
    • 2+ chelators reduce early excitotoxic and ischemic neuronal injury in vitro and in vivo. Neuron 1993;11:221-235
    • (1993) Neuron , vol.11 , pp. 221-235
    • Tymianski, M.1    Wallace, M.C.2    Spigelman, I.3
  • 54
    • 0028024908 scopus 로고
    • Triggering and execution of neuronal death in brain ischemia: Two phases of glutamate release by different mechanisms
    • Szatkowski M, Atwell D. Triggering and execution of neuronal death in brain ischemia: two phases of glutamate release by different mechanisms. Trends Neurosci 1994;17:359-365
    • (1994) Trends Neurosci , vol.17 , pp. 359-365
    • Szatkowski, M.1    Atwell, D.2
  • 56
    • 0025995296 scopus 로고
    • RNa editing in brain controls a determinant of ion flow in glutamate-gated channels
    • Sommer B, Kohler M, Sprengel R, Seeburg PH. RNA editing in brain controls a determinant of ion flow in glutamate-gated channels. Cell 1991;67:11-19
    • (1991) Cell , vol.67 , pp. 11-19
    • Sommer, B.1    Kohler, M.2    Sprengel, R.3    Seeburg, P.H.4
  • 57
    • 0025879427 scopus 로고
    • Structural determinants of ion flow through recombinant glutamate receptor channels
    • Verdoorn TA, Burnashev N, Monyer H, et al. Structural determinants of ion flow through recombinant glutamate receptor channels. Science 1991;252:1715-1718
    • (1991) Science , vol.252 , pp. 1715-1718
    • Verdoorn, T.A.1    Burnashev, N.2    Monyer, H.3
  • 58
    • 0026910417 scopus 로고
    • Determinants of the calcium permeation of ligand-gated cation channels
    • Gasic GP, Heinemann S. Determinants of the calcium permeation of ligand-gated cation channels. Curr Opin Cell Biol 1992;4:670-677
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 670-677
    • Gasic, G.P.1    Heinemann, S.2
  • 59
    • 0028075810 scopus 로고
    • Cellular and synaptic localization of NMDA and non-NMDA receptor subunits in neocortex: Organizational features related to cortical circuitry, function, and disease
    • Huntley GW, Vickers JC, Morrison JH. Cellular and synaptic localization of NMDA and non-NMDA receptor subunits in neocortex: organizational features related to cortical circuitry, function, and disease. Trends Neurosci 1994;17:536-543
    • (1994) Trends Neurosci , vol.17 , pp. 536-543
    • Huntley, G.W.1    Vickers, J.C.2    Morrison, J.H.3
  • 60
    • 0025785213 scopus 로고
    • Glutamate metabotropic and AMPA binding sites are reduced in Alzheimer's disease: An autoradiographic study of the hippocampus
    • Dewar D, Chalmers DT, Graham DI, McCulloch J. Glutamate metabotropic and AMPA binding sites are reduced in Alzheimer's disease: an autoradiographic study of the hippocampus. Brain Res 1991;553:58-64
    • (1991) Brain Res , vol.553 , pp. 58-64
    • Dewar, D.1    Chalmers, D.T.2    Graham, D.I.3    McCulloch, J.4
  • 61
    • 0027291657 scopus 로고
    • NMDA, AMPA, and benzodiazepine binding site changes in Alzheimer's disease visual cortex
    • Carlson MD, Penney JB Jr., Young AB. NMDA, AMPA, and benzodiazepine binding site changes in Alzheimer's disease visual cortex. Neurobiol Aging 1993;14:343-352
    • (1993) Neurobiol Aging , vol.14 , pp. 343-352
    • Carlson, M.D.1    Penney Jr., J.B.2    Young, A.B.3
  • 62
    • 0028040087 scopus 로고
    • Excitatory amino acid AMPA receptor mRNA localization in several regions of normal and neurological disease affected human brain. An in situ hybridization histochemistry study
    • García-Ladona FJ, Palacios JM, Probst A, et al. Excitatory amino acid AMPA receptor mRNA localization in several regions of normal and neurological disease affected human brain. An in situ hybridization histochemistry study. Mol Brain Res 1994;21:75-84
    • (1994) Mol Brain Res , vol.21 , pp. 75-84
    • García-Ladona, F.J.1    Palacios, J.M.2    Probst, A.3
  • 64
    • 0030930206 scopus 로고    scopus 로고
    • The loss of GluR2(3) immunoreactivity precedes neurofibrillary tangle formation in the entorhinal cortex and hippocampus of Alzheimer brains
    • Ikonomovic MD, Mizukami K, Davies P, et al. The loss of GluR2(3) immunoreactivity precedes neurofibrillary tangle formation in the entorhinal cortex and hippocampus of Alzheimer brains. J Neuropathol Exp Neurol 1997;56:1018-1027
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 1018-1027
    • Ikonomovic, M.D.1    Mizukami, K.2    Davies, P.3
  • 65
    • 0028350662 scopus 로고
    • AMPA-selective glutamate receptor subtype immunoreactivity in the entorhinal cortex of non-demented elderly and patients with Alzheimer's disease
    • Armstrong DM, Ikonomovic MD, Sheffield R, Wenthold RJ. AMPA-selective glutamate receptor subtype immunoreactivity in the entorhinal cortex of non-demented elderly and patients with Alzheimer's disease. Brain Res 1994;639:207-216
    • (1994) Brain Res , vol.639 , pp. 207-216
    • Armstrong, D.M.1    Ikonomovic, M.D.2    Sheffield, R.3    Wenthold, R.J.4
  • 66
    • 0028952094 scopus 로고
    • Reduction of AMPA-selective glutamate receptor subunits in the entorhinal cortex of patients with Alzheimer's disease pathology: A biochemical study
    • Yasuda RP, Ikonomovic MD, Sheffield R, et al. Reduction of AMPA-selective glutamate receptor subunits in the entorhinal cortex of patients with Alzheimer's disease pathology: a biochemical study. Brain Res 1995;678:161-167
    • (1995) Brain Res , vol.678 , pp. 161-167
    • Yasuda, R.P.1    Ikonomovic, M.D.2    Sheffield, R.3
  • 67
    • 0029843713 scopus 로고    scopus 로고
    • AMPA-selective glutamate receptor subtype immunoreactivity in the hippocampal dentate gyrus of patients with Alzheimer's disease - Evidence for hippocampal plasticity
    • Armstrong DM, Ikonomovic MD. AMPA-selective glutamate receptor subtype immunoreactivity in the hippocampal dentate gyrus of patients with Alzheimer's disease - evidence for hippocampal plasticity. Mol Chem Neuropathol 1996;28: 59-64
    • (1996) Mol Chem Neuropathol , vol.28 , pp. 59-64
    • Armstrong, D.M.1    Ikonomovic, M.D.2
  • 68
    • 0021848540 scopus 로고
    • Controlled induction of paired helical filaments of the Alzheimer type in cultured human neurons by glutamate and aspartate
    • De Boni U, Crapper McLachlan DR. Controlled induction of paired helical filaments of the Alzheimer type in cultured human neurons by glutamate and aspartate. J Neurol Sci 1985; 68:105-118
    • (1985) J Neurol Sci , vol.68 , pp. 105-118
    • De Boni, U.1    Crapper McLachlan, D.R.2
  • 69
    • 0026636164 scopus 로고
    • Tau antigenic changes induced by glutamate in rat primary culture model: A biochemical approach
    • Sautière PE, Sindou P, Couratier P, et al. Tau antigenic changes induced by glutamate in rat primary culture model: a biochemical approach. Neurosci Lett 1992;140:206-210
    • (1992) Neurosci Lett , vol.140 , pp. 206-210
    • Sautière, P.E.1    Sindou, P.2    Couratier, P.3
  • 70
    • 0026570528 scopus 로고
    • β-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson MP, Cheng B, Davis D, et al. β-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J Neurosci 1992;12:376-389
    • (1992) J Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3
  • 71
    • 0028868345 scopus 로고
    • Phosphorylated and nonphosphorylated neurofilament proteins: Distribution in the rat hippocampus and early changes after kainic acid induced seizures
    • Yang Q, Wang S, Karlsson JE, et al. Phosphorylated and nonphosphorylated neurofilament proteins: distribution in the rat hippocampus and early changes after kainic acid induced seizures. J Chem Neuroanat 1995;9:217-228
    • (1995) J Chem Neuroanat , vol.9 , pp. 217-228
    • Yang, Q.1    Wang, S.2    Karlsson, J.E.3
  • 72
    • 0028173843 scopus 로고
    • Glutamate increases tau phosphorylation in primary neuronal cultures from fetal rat cerebral cortex
    • Sindou P, Lesort M, Couratier P, et al. Glutamate increases tau phosphorylation in primary neuronal cultures from fetal rat cerebral cortex. Brain Res 1994;646:124-128
    • (1994) Brain Res , vol.646 , pp. 124-128
    • Sindou, P.1    Lesort, M.2    Couratier, P.3
  • 73
    • 0028950572 scopus 로고
    • Vulnerability of the hippocampus to kainate excitotoxicity
    • Kesslak JP, Yuan D, Neeper S, Cotman CW. Vulnerability of the hippocampus to kainate excitotoxicity. Neurosci Lett 1995;188:117-120
    • (1995) Neurosci Lett , vol.188 , pp. 117-120
    • Kesslak, J.P.1    Yuan, D.2    Neeper, S.3    Cotman, C.W.4
  • 74
    • 0029991888 scopus 로고    scopus 로고
    • Modifications of neuronal phosphorylated τ immunoreactivity induced by NMDA toxicity
    • Couratier P, Lesort M, Sindou P, et al. Modifications of neuronal phosphorylated τ immunoreactivity induced by NMDA toxicity. Mol Chem Neuropathol 1996;27:259-264
    • (1996) Mol Chem Neuropathol , vol.27 , pp. 259-264
    • Couratier, P.1    Lesort, M.2    Sindou, P.3
  • 75
    • 0029032499 scopus 로고
    • SMI-32 antibody against non-phosphorylated neurofilaments identifies a subpopulation of cultured cortical neurons hypersensitive to kainate toxicity
    • Gottron F, Turetsky D, Choi D. SMI-32 antibody against non-phosphorylated neurofilaments identifies a subpopulation of cultured cortical neurons hypersensitive to kainate toxicity. Neurosci Lett 1995;194:1-4
    • (1995) Neurosci Lett , vol.194 , pp. 1-4
    • Gottron, F.1    Turetsky, D.2    Choi, D.3
  • 76
    • 0030015076 scopus 로고    scopus 로고
    • Motor neurons are selectively vulnerable to AMPA/kainate receptor-mediated injury in vitro
    • Carriedo SG, Yin HZ, Weiss JH. Motor neurons are selectively vulnerable to AMPA/kainate receptor-mediated injury in vitro. J Neurosci 1996;16:4069-4079
    • (1996) J Neurosci , vol.16 , pp. 4069-4079
    • Carriedo, S.G.1    Yin, H.Z.2    Weiss, J.H.3
  • 77
    • 0031056622 scopus 로고    scopus 로고
    • Quantitative localization of NMDAR1 receptor subunit immunoreactivity in inferotemporal and prefrontal association cortices of monkey and human
    • Huntley GW, Vickers JC, Morrison JH. Quantitative localization of NMDAR1 receptor subunit immunoreactivity in inferotemporal and prefrontal association cortices of monkey and human. Brain Res 1997;749:245-262
    • (1997) Brain Res , vol.749 , pp. 245-262
    • Huntley, G.W.1    Vickers, J.C.2    Morrison, J.H.3
  • 78
    • 0027223325 scopus 로고
    • Quantitative localization of AMPA/kainate and kainate glutamate receptor subunit immunoreactivity in neurochemically identified subpopulations of neurons in the prefrontal cortex of the macaque monkey
    • Vickers JC, Huntley GW, Edwards AM, et al. Quantitative localization of AMPA/kainate and kainate glutamate receptor subunit immunoreactivity in neurochemically identified subpopulations of neurons in the prefrontal cortex of the macaque monkey. J Neurosci 1993;13:2982-2992
    • (1993) J Neurosci , vol.13 , pp. 2982-2992
    • Vickers, J.C.1    Huntley, G.W.2    Edwards, A.M.3
  • 79
    • 0031972719 scopus 로고    scopus 로고
    • Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments
    • Ehlers MD, Fung ET, O'Brien RJ, Huganir RL. Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments. J Neurosci 1998; 18:720-730
    • (1998) J Neurosci , vol.18 , pp. 720-730
    • Ehlers, M.D.1    Fung, E.T.2    O'Brien, R.J.3    Huganir, R.L.4
  • 81
    • 0026530110 scopus 로고
    • 2+-binding proteins in human neurodegenerative disorders
    • 2+-binding proteins in human neurodegenerative disorders. Trends Neurosci 1992; 15:259-264
    • (1992) Trends Neurosci , vol.15 , pp. 259-264
    • Heizmann, C.W.1    Braun, K.2
  • 82
    • 0027447304 scopus 로고
    • Calcium-binding proteins: Selective markers of nerve cells
    • Andressen C, Blümcke I, Celio MR. Calcium-binding proteins: selective markers of nerve cells. Cell Tissue Res 1993; 271:181-208
    • (1993) Cell Tissue Res , vol.271 , pp. 181-208
    • Andressen, C.1    Blümcke, I.2    Celio, M.R.3
  • 83
    • 0027946813 scopus 로고
    • The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis
    • Alexianu ME, Ho B-K, Mohamed AH, et al. The role of calcium-binding proteins in selective motoneuron vulnerability in amyotrophic lateral sclerosis. Aim Neurol 1994;36:846-858
    • (1994) Aim Neurol , vol.36 , pp. 846-858
    • Alexianu, M.E.1    Ho, B.-K.2    Mohamed, A.H.3
  • 85
    • 0031149760 scopus 로고    scopus 로고
    • The cellular basis for the relative resistance of parvalbumin and calretinin immunoreactive neocortical neurons to the pathology of Alzheimer's disease
    • Sampson VL, Morrison JH, Vickers JC. The cellular basis for the relative resistance of parvalbumin and calretinin immunoreactive neocortical neurons to the pathology of Alzheimer's disease. Exp Neurol 1997;154:295-302
    • (1997) Exp Neurol , vol.154 , pp. 295-302
    • Sampson, V.L.1    Morrison, J.H.2    Vickers, J.C.3
  • 86
    • 0026318759 scopus 로고
    • Parvalbumin immunoreactive neurons in normal human temporal neocortex and in patients with Alzheimer's disease
    • Ferrer I, Soriano E, Tuñon T, et al. Parvalbumin immunoreactive neurons in normal human temporal neocortex and in patients with Alzheimer's disease. J Neurol Sci 1991;106:135-141
    • (1991) J Neurol Sci , vol.106 , pp. 135-141
    • Ferrer, I.1    Soriano, E.2    Tuñon, T.3
  • 87
    • 0027417571 scopus 로고
    • Calbindin D-28k and parvalbumin immunoreactivity in the frontal cortex in patients with frontal lobe dementia of non-Alzheimer type associated with amyotrophic lateral sclerosis
    • Ferrer I, Tuñon T, Serrano MT, et al. Calbindin D-28k and parvalbumin immunoreactivity in the frontal cortex in patients with frontal lobe dementia of non-Alzheimer type associated with amyotrophic lateral sclerosis. J Neurol Neurosurg Psychiatry 1993;56:257-261
    • (1993) J Neurol Neurosurg Psychiatry , vol.56 , pp. 257-261
    • Ferrer, I.1    Tuñon, T.2    Serrano, M.T.3
  • 88
    • 0025807752 scopus 로고
    • Parvalbumin-immunoreactive neurons in the neocortex are resistant to degeneration in Alzheimer's disease
    • Hof PR, Cox K, Young WG, et al. Parvalbumin-immunoreactive neurons in the neocortex are resistant to degeneration in Alzheimer's disease. J Neuropathol Exp Neurol 1991;50: 451-462
    • (1991) J Neuropathol Exp Neurol , vol.50 , pp. 451-462
    • Hof, P.R.1    Cox, K.2    Young, W.G.3
  • 89
    • 0027328789 scopus 로고
    • Chandelier cell axons identified by parvalbumin-immunoreactivity in the normal human temporal cortex and in Alzheimer's disease
    • Fonseca M, Soriano E, Ferrer I, et al. Chandelier cell axons identified by parvalbumin-immunoreactivity in the normal human temporal cortex and in Alzheimer's disease. Neuroscience 1993;55:1107-1116
    • (1993) Neuroscience , vol.55 , pp. 1107-1116
    • Fonseca, M.1    Soriano, E.2    Ferrer, I.3
  • 90
    • 0026349261 scopus 로고
    • Parvalbumin neurons in the hippocampus in senile dementia of the Alzheimer type, Parkinson's disease and multi-infarct dementia
    • Chan-Palay V, Zetzsche T, Höchli M. Parvalbumin neurons in the hippocampus in senile dementia of the Alzheimer type, Parkinson's disease and multi-infarct dementia. Dementia 1991;2:297-313
    • (1991) Dementia , vol.2 , pp. 297-313
    • Chan-Palay, V.1    Zetzsche, T.2    Höchli, M.3
  • 91
    • 0029930270 scopus 로고    scopus 로고
    • Contingent vulnerability of entorhinal parvalbumin-containing neurons in Alzheimer's disease
    • Solodkin A, Veldhuizen SD, Van Hoesen GW. Contingent vulnerability of entorhinal parvalbumin-containing neurons in Alzheimer's disease. J Neurosci 1996;16:3311-3321
    • (1996) J Neurosci , vol.16 , pp. 3311-3321
    • Solodkin, A.1    Veldhuizen, S.D.2    Van Hoesen, G.W.3
  • 92
    • 0027231535 scopus 로고
    • Calretinin-immunoreactive neocortical interneurons are unaffected in Alzheimer's disease
    • Hof PR, Nimchinsky EA, Celio MR, et al. Calretinin-immunoreactive neocortical interneurons are unaffected in Alzheimer's disease. Neurosci Lett 1993;152:145-149
    • (1993) Neurosci Lett , vol.152 , pp. 145-149
    • Hof, P.R.1    Nimchinsky, E.A.2    Celio, M.R.3
  • 93
    • 0028981481 scopus 로고
    • Calretinin-immunoreactive neurons in the normal human temporal cortex and in Alzheimer's disease
    • Fonseca M, Soriano E. Calretinin-immunoreactive neurons in the normal human temporal cortex and in Alzheimer's disease. Brain Res 1995;691:83-91
    • (1995) Brain Res , vol.691 , pp. 83-91
    • Fonseca, M.1    Soriano, E.2
  • 94
    • 0028287326 scopus 로고
    • A subset of calretinin-positive neurons are abnormal in Alzheimer's disease
    • Brion JP, Résibois A. A subset of calretinin-positive neurons are abnormal in Alzheimer's disease. Acta Neuropathol (Berl) 1994;88:33-43
    • (1994) Acta Neuropathol (Berl) , vol.88 , pp. 33-43
    • Brion, J.P.1    Résibois, A.2
  • 95
    • 0023684906 scopus 로고
    • Loss of calbindin-28k immunoreactive neurones from the cortex in Alzheimer-type dementia
    • Ichimiya Y, Emson PC, Mountjoy CQ, et al. Loss of calbindin-28k immunoreactive neurones from the cortex in Alzheimer-type dementia. Brain Res 1988;475:156-159
    • (1988) Brain Res , vol.475 , pp. 156-159
    • Ichimiya, Y.1    Emson, P.C.2    Mountjoy, C.Q.3
  • 96
    • 0025969656 scopus 로고
    • Neocortical neuronal subpopulations labeled by a monoclonal antibody to calbindin exhibit differential vulnerability in Alzheimer's disease
    • Hof PR, Morrison JH. Neocortical neuronal subpopulations labeled by a monoclonal antibody to calbindin exhibit differential vulnerability in Alzheimer's disease. Exp Neurol 1991; 111:293-301
    • (1991) Exp Neurol , vol.111 , pp. 293-301
    • Hof, P.R.1    Morrison, J.H.2
  • 97
    • 0027131842 scopus 로고
    • Selective loss of calbindin D28k-immunoreactive neurons in the cortical layer II in brains of Alzheimer's disease: A morphometric study
    • Nishiyama E, Ohwada J, Iwamoto N, Arai H. Selective loss of calbindin D28k-immunoreactive neurons in the cortical layer II in brains of Alzheimer's disease: a morphometric study. Neurosci Lett 1993;163:223-226
    • (1993) Neurosci Lett , vol.163 , pp. 223-226
    • Nishiyama, E.1    Ohwada, J.2    Iwamoto, N.3    Arai, H.4
  • 98
    • 0026449691 scopus 로고
    • Nonphosphorylated neurofilament protein and calbindin immunoreactivity in layer III pyramidal neurons of human neocortex
    • Hayes TL, Lewis DA. Nonphosphorylated neurofilament protein and calbindin immunoreactivity in layer III pyramidal neurons of human neocortex. Cereb Cortex 1992;2:56-67
    • (1992) Cereb Cortex , vol.2 , pp. 56-67
    • Hayes, T.L.1    Lewis, D.A.2
  • 100
    • 0002634911 scopus 로고
    • Clinical features and differential diagnosis of classical motor neuron disease
    • Williams AC, ed. London: Chapman and Hall
    • Tandan R. Clinical features and differential diagnosis of classical motor neuron disease. In: Williams AC, ed. Motor neuron disease. London: Chapman and Hall, 1994:3-28
    • (1994) Motor Neuron Disease , pp. 3-28
    • Tandan, R.1
  • 101
  • 102
    • 0026042995 scopus 로고
    • Cytopathology of amyotrophic lateral sclerosis
    • Rowland LP, ed. New York: Raven Press
    • Hirano A. Cytopathology of amyotrophic lateral sclerosis. In: Rowland LP, ed. Amyotrophic lateral sclerosis and other motor neuron diseases. New York: Raven Press, 1991:91-101
    • (1991) Amyotrophic Lateral Sclerosis and Other Motor Neuron Diseases , pp. 91-101
    • Hirano, A.1
  • 104
    • 0029812020 scopus 로고    scopus 로고
    • Reactive astrogliosis of the spinal cord in amyotrophic lateral sclerosis
    • Schiffer D, Cordera S, Cavalla P, Migheli A. Reactive astrogliosis of the spinal cord in amyotrophic lateral sclerosis. J Neurol Sci 1996;139(Suppl):S27-33
    • (1996) J Neurol Sci , vol.139 , Issue.SUPPL.
    • Schiffer, D.1    Cordera, S.2    Cavalla, P.3    Migheli, A.4
  • 105
    • 0024560042 scopus 로고
    • Evidence for sequential degeneration of the neurons in the intermediate zone of the spinal cord in amyotrophic lateral sclerosis: A topographic and quantitative investigation
    • Oyanagi K, Ikuta F, Horikawa Y. Evidence for sequential degeneration of the neurons in the intermediate zone of the spinal cord in amyotrophic lateral sclerosis: a topographic and quantitative investigation. Acta Neuropathol (Berl) 1989;77: 343-349
    • (1989) Acta Neuropathol (Berl) , vol.77 , pp. 343-349
    • Oyanagi, K.1    Ikuta, F.2    Horikawa, Y.3
  • 106
    • 0028325407 scopus 로고
    • Disease-specific patterns of neuronal loss in the spinal ventral horn in amyotrophic lateral sclerosis, multiple system atrophy and X-linked recessive bulbospinal neuronopathy, with special reference to the loss of small neurons in the intermediate zone
    • Terao S, Sobue G, Hashizume Y, et al. Disease-specific patterns of neuronal loss in the spinal ventral horn in amyotrophic lateral sclerosis, multiple system atrophy and X-linked recessive bulbospinal neuronopathy, with special reference to the loss of small neurons in the intermediate zone. J Neurol 1994; 241:196-203
    • (1994) J Neurol , vol.241 , pp. 196-203
    • Terao, S.1    Sobue, G.2    Hashizume, Y.3
  • 107
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation
    • Gurney ME, Pu H, Chiu AY, et al. Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 1994;264:1772-1775
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1    Pu, H.2    Chiu, A.Y.3
  • 108
    • 0029096114 scopus 로고
    • Age-dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Chiu AY, Zhai P, Dal Canto MC, et al. Age-dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis. Mol Cell Neurosci 1995;6:349-362
    • (1995) Mol Cell Neurosci , vol.6 , pp. 349-362
    • Chiu, A.Y.1    Zhai, P.2    Dal Canto, M.C.3
  • 109
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • Ripps ME, Huntley GW, Hof PR, et al. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 1995;92:689-693
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 689-693
    • Ripps, M.E.1    Huntley, G.W.2    Hof, P.R.3
  • 110
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong PC, Pardo CA, Borchelt DR, et al. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 1995;14:1105-1116
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3
  • 111
    • 0029793872 scopus 로고    scopus 로고
    • Quantitative immunocytochemical analysis of the spinal cord in G86R superoxide dismutase transgenic mice: Neurochemical correlates of selective vulnerability
    • Morrison BM, Gordon JW, Ripps ME, Morrison JH. Quantitative immunocytochemical analysis of the spinal cord in G86R superoxide dismutase transgenic mice: neurochemical correlates of selective vulnerability. J Comp Neurol 1996;373: 619-631
    • (1996) J Comp Neurol , vol.373 , pp. 619-631
    • Morrison, B.M.1    Gordon, J.W.2    Ripps, M.E.3    Morrison, J.H.4
  • 112
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn LI, Becher MW, Lee MK, et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 1997;18:327-338
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1    Becher, M.W.2    Lee, M.K.3
  • 113
    • 0030887622 scopus 로고    scopus 로고
    • Midbrain dopaminergic neuronal degeneration in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Kostic V, Gurney ME, Deng H-X, et al. Midbrain dopaminergic neuronal degeneration in a transgenic mouse model of familial amyotrophic lateral sclerosis. Ann Neurol 1997;41: 497-504
    • (1997) Ann Neurol , vol.41 , pp. 497-504
    • Kostic, V.1    Gurney, M.E.2    Deng, H.-X.3
  • 114
    • 0032472831 scopus 로고    scopus 로고
    • Time course of neuropathology in the spinal cord of G86R superoxide dismutase transgenic mice
    • Morrison BM, Janssen WG, Gordon JW, Morrison JH. Time course of neuropathology in the spinal cord of G86R superoxide dismutase transgenic mice. J Comp Neurol 1998;391: 64-77
    • (1998) J Comp Neurol , vol.391 , pp. 64-77
    • Morrison, B.M.1    Janssen, W.G.2    Gordon, J.W.3    Morrison, J.H.4
  • 115
    • 0026344258 scopus 로고
    • Degeneration of the substantia nigra in familial amyotrophic lateral sclerosis
    • Wolf HK, Crain BJ, Siddique T. Degeneration of the substantia nigra in familial amyotrophic lateral sclerosis. Clin Neuropathol 1991;6:291-296
    • (1991) Clin Neuropathol , vol.6 , pp. 291-296
    • Wolf, H.K.1    Crain, B.J.2    Siddique, T.3
  • 116
    • 0028815433 scopus 로고
    • Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons
    • Pardo CA, Xu Z, Borchelt DR, et al. Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc Natl Acad Sci USA 1995;92:954-958
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 954-958
    • Pardo, C.A.1    Xu, Z.2    Borchelt, D.R.3
  • 117
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase are associated with familial amyotrophic lateral sclerosis
    • Rosen DR, Siddique T, Patterson D, et al. Mutations in Cu/Zn superoxide dismutase are associated with familial amyotrophic lateral sclerosis. Nature 1993;362:59-62
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 118
    • 0029810307 scopus 로고    scopus 로고
    • Genetics of amyotrophic lateral sclerosis
    • Siddique T, Deng H-X. Genetics of amyotrophic lateral sclerosis. Hum Mol Genet 1996;5:1465-1470
    • (1996) Hum Mol Genet , vol.5 , pp. 1465-1470
    • Siddique, T.1    Deng, H.-X.2
  • 119
    • 0027965073 scopus 로고
    • Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity
    • Borchelt DR, Lee MK, Slunt HS, et al. Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc Natl Acad Sci USA 1994;91:8292-8296
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8292-8296
    • Borchelt, D.R.1    Lee, M.K.2    Slunt, H.S.3
  • 120
    • 0027997236 scopus 로고
    • Analysis of the functional effects of a mutation in SOD1 associated with familial amyotrophic lateral sclerosis
    • Tsuda T, Munthasser S, Fraser PE, et al. Analysis of the functional effects of a mutation in SOD1 associated with familial amyotrophic lateral sclerosis. Neuron 1994;13:727-736
    • (1994) Neuron , vol.13 , pp. 727-736
    • Tsuda, T.1    Munthasser, S.2    Fraser, P.E.3
  • 121
    • 0028955472 scopus 로고
    • Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells
    • Fujii J, Myint T, Seo HG, et al. Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells. J Neurochem 1995;64:1456-1461
    • (1995) J Neurochem , vol.64 , pp. 1456-1461
    • Fujii, J.1    Myint, T.2    Seo, H.G.3
  • 122
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
    • Reaume AG, Elliott JL, Hoffman EK, et al. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nature Genet 1996;13:43-47
    • (1996) Nature Genet , vol.13 , pp. 43-47
    • Reaume, A.G.1    Elliott, J.L.2    Hoffman, E.K.3
  • 123
    • 0023607666 scopus 로고
    • Brain glutamate deficiency in amyotrophic lateral sclerosis
    • Perry TL, Hansen S, Jones K. Brain glutamate deficiency in amyotrophic lateral sclerosis. Neurology 1987;37:1845-1848
    • (1987) Neurology , vol.37 , pp. 1845-1848
    • Perry, T.L.1    Hansen, S.2    Jones, K.3
  • 124
    • 0023617392 scopus 로고
    • Abnormal glutamate metabolism in amyotrophic lateral sclerosis
    • Plaitakis A, Caroscio JT. Abnormal glutamate metabolism in amyotrophic lateral sclerosis. Ann Neurol 1987;22:575-579
    • (1987) Ann Neurol , vol.22 , pp. 575-579
    • Plaitakis, A.1    Caroscio, J.T.2
  • 125
    • 0023804850 scopus 로고
    • The neuroexcitotoxic amino acids glutamate and aspartate are altered in the spinal cord and brain in amyotrophic lateral sclerosis
    • Plaitakis A, Constantakakis E, Smith J. The neuroexcitotoxic amino acids glutamate and aspartate are altered in the spinal cord and brain in amyotrophic lateral sclerosis. Ann Neurol 1988;24:446-449
    • (1988) Ann Neurol , vol.24 , pp. 446-449
    • Plaitakis, A.1    Constantakakis, E.2    Smith, J.3
  • 126
    • 0025299819 scopus 로고
    • Abnormal excitatory amino acid metabolism in amyotrophic lateral sclerosis
    • Rothstein JD, Tsai G, Kuncl RW, et al. Abnormal excitatory amino acid metabolism in amyotrophic lateral sclerosis. Ann Neurol 1990;28:18-25
    • (1990) Ann Neurol , vol.28 , pp. 18-25
    • Rothstein, J.D.1    Tsai, G.2    Kuncl, R.W.3
  • 127
    • 0026597010 scopus 로고
    • Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis
    • Rothstein JD, Martin LJ, Kuncl RW. Decreased glutamate transport by the brain and spinal cord in amyotrophic lateral sclerosis. N Engl J Med 1992;326:1464-1468
    • (1992) N Engl J Med , vol.326 , pp. 1464-1468
    • Rothstein, J.D.1    Martin, L.J.2    Kuncl, R.W.3
  • 128
    • 0029030610 scopus 로고
    • Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis
    • Rothstein JD, Van Kammen M, Levey AI, et al. Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis. Ann Neurol 1995;38:73-84
    • (1995) Ann Neurol , vol.38 , pp. 73-84
    • Rothstein, J.D.1    Van Kammen, M.2    Levey, A.I.3
  • 129
    • 0027274623 scopus 로고
    • Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity
    • Rothstein JD, Jin L, Dykes-Hoberg M, Kuncl RW. Chronic inhibition of glutamate uptake produces a model of slow neurotoxicity. Proc Natl Acad Sci USA 1993;90:6591-6595
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6591-6595
    • Rothstein, J.D.1    Jin, L.2    Dykes-Hoberg, M.3    Kuncl, R.W.4
  • 130
    • 13344286293 scopus 로고    scopus 로고
    • Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate
    • Rothstein JD, Dykes-Hoberg M, Pardo CA, et al. Knockout of glutamate transporters reveals a major role for astroglial transport in excitotoxicity and clearance of glutamate. Neuron 1996;16:675-686
    • (1996) Neuron , vol.16 , pp. 675-686
    • Rothstein, J.D.1    Dykes-Hoberg, M.2    Pardo, C.A.3
  • 131
    • 0026486270 scopus 로고
    • Stable transfection of calbindin-D28k into the GH3 cell line alters calcium currents and intracellular calcium homeostasis
    • Lledo P-M, Somasundaram B, Morton AJ, et al. Stable transfection of calbindin-D28k into the GH3 cell line alters calcium currents and intracellular calcium homeostasis. Neuron 1992;9:943-954
    • (1992) Neuron , vol.9 , pp. 943-954
    • Lledo, P.-M.1    Somasundaram, B.2    Morton, A.J.3
  • 132
    • 0027730919 scopus 로고
    • Calcium buffering properties of calbindin D-28k and parvalbumin in rat sensory neurones
    • Chard PS, Bleakman D, Christakos S, et al. Calcium buffering properties of calbindin D-28k and parvalbumin in rat sensory neurones. J Physiol 1993;472:341-357
    • (1993) J Physiol , vol.472 , pp. 341-357
    • Chard, P.S.1    Bleakman, D.2    Christakos, S.3
  • 133
    • 13344261949 scopus 로고    scopus 로고
    • Motor neuron degeneration induced by excitotoxin agonists has features in common with those seen in the SOD-1 transgenic mouse model of amyotrophic lateral sclerosis
    • Ikonomidou C, Qin Qin Y, Labruyere J, Olney JW. Motor neuron degeneration induced by excitotoxin agonists has features in common with those seen in the SOD-1 transgenic mouse model of amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 1996;55:211-224
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 211-224
    • Ikonomidou, C.1    Qin Qin, Y.2    Labruyere, J.3    Olney, J.W.4
  • 134
    • 0024367836 scopus 로고
    • Cloning by functional expression of a member of the glutamate receptor family
    • Hollmann M, O'Shea-Greenfield A, Rogers SW, Heinemann S. Cloning by functional expression of a member of the glutamate receptor family. Nature 1989;342:643-648
    • (1989) Nature , vol.342 , pp. 643-648
    • Hollmann, M.1    O'Shea-Greenfield, A.2    Rogers, S.W.3    Heinemann, S.4
  • 135
    • 0025088156 scopus 로고
    • Molecular cloning and functional expression of glutamate receptor subunit genes
    • Boulter J, Hollmann M, O'Shea-Greenfield A, et al. Molecular cloning and functional expression of glutamate receptor subunit genes. Science 1990;249:1033-1037
    • (1990) Science , vol.249 , pp. 1033-1037
    • Boulter, J.1    Hollmann, M.2    O'Shea-Greenfield, A.3
  • 136
    • 0025150414 scopus 로고
    • A family of AMPA-selective glutamate receptors
    • Keinanen K, Wisden W, Sommer B, et al. A family of AMPA-selective glutamate receptors. Science 1990;249:556-560
    • (1990) Science , vol.249 , pp. 556-560
    • Keinanen, K.1    Wisden, W.2    Sommer, B.3
  • 137
    • 0028341877 scopus 로고
    • Differential assembly of coexpressed glutamate receptor subunits in neurons of rat cerebral cortex
    • Brose N, Huntley GW, Stern-Bach Y, et al. Differential assembly of coexpressed glutamate receptor subunits in neurons of rat cerebral cortex. J Biol Chem 1994;269:16780-16784
    • (1994) J Biol Chem , vol.269 , pp. 16780-16784
    • Brose, N.1    Huntley, G.W.2    Stern-Bach, Y.3
  • 138
    • 0027941193 scopus 로고
    • Selective RNA editing and subunit assembly of native glutamate receptors
    • Puchalski RB, Louis J-C, Brose N, et al. Selective RNA editing and subunit assembly of native glutamate receptors. Neuron 1994;13:131-147
    • (1994) Neuron , vol.13 , pp. 131-147
    • Puchalski, R.B.1    Louis, J.-C.2    Brose, N.3
  • 139
    • 0029089601 scopus 로고
    • 2+ permeability of AMPA receptots in principal neurons and interneurons in rat CNS
    • 2+ permeability of AMPA receptots in principal neurons and interneurons in rat CNS. Neuron 1995;15:193-204
    • (1995) Neuron , vol.15 , pp. 193-204
    • Geiger, J.R.P.1    Melcher, T.2    Koh, D.-S.3
  • 141
    • 0027510535 scopus 로고
    • The differential expression patterns of messenger RNAs encoding non-N-methyl-D-aspartate glutamate receptor subunits (GluR1-4) in the rat brain
    • Sato K, Kiyama H, Tohyama M. The differential expression patterns of messenger RNAs encoding non-N-methyl-D-aspartate glutamate receptor subunits (GluR1-4) in the rat brain. Neuroscience 1993;52:515-539
    • (1993) Neuroscience , vol.52 , pp. 515-539
    • Sato, K.1    Kiyama, H.2    Tohyama, M.3
  • 142
    • 0027141312 scopus 로고
    • The differential expression of 16 NMDA and non-NMDA receptor subunits in the rat spinal cord and in periaqueductal gray
    • Tolle TR, Berthele A, Zieglgansberger W, et al. The differential expression of 16 NMDA and non-NMDA receptor subunits in the rat spinal cord and in periaqueductal gray. J Neurosci 1993;13:5009-5028
    • (1993) J Neurosci , vol.13 , pp. 5009-5028
    • Tolle, T.R.1    Berthele, A.2    Zieglgansberger, W.3
  • 143
    • 0029025131 scopus 로고
    • Quantitative and qualitative changes in AMPA receptor expression during spinal cord development
    • Jakowec MW, Fox AJ, Martin LJ, Kalb RG. Quantitative and qualitative changes in AMPA receptor expression during spinal cord development. Neuroscience 1995;67:893-907
    • (1995) Neuroscience , vol.67 , pp. 893-907
    • Jakowec, M.W.1    Fox, A.J.2    Martin, L.J.3    Kalb, R.G.4
  • 144
    • 0029044061 scopus 로고
    • In situ hybridization analysis of AMPA receptor subunit gene expression in the developing rat spinal cord
    • Jakowec MW, Yen L, Kalb RG. In situ hybridization analysis of AMPA receptor subunit gene expression in the developing rat spinal cord. Neuroscience 1995;67:909-920
    • (1995) Neuroscience , vol.67 , pp. 909-920
    • Jakowec, M.W.1    Yen, L.2    Kalb, R.G.3
  • 145
    • 0029075824 scopus 로고
    • Flip and flop variants of AMPA receptors in the rat lumbar spinal cord
    • Tolle TR, Berthele A, Zieglgansberger W, et al. Flip and flop variants of AMPA receptors in the rat lumbar spinal cord. Eur J Neurosci 1995;7:1414-1419
    • (1995) Eur J Neurosci , vol.7 , pp. 1414-1419
    • Tolle, T.R.1    Berthele, A.2    Zieglgansberger, W.3
  • 146
    • 0030731215 scopus 로고    scopus 로고
    • Expression of glutamate receptor subunits in alpha-motoneurons
    • Temkin R, Lowe D, Jensen P, et al. Expression of glutamate receptor subunits in alpha-motoneurons. Mol Brain Res 1997; 52:38-45
    • (1997) Mol Brain Res , vol.52 , pp. 38-45
    • Temkin, R.1    Lowe, D.2    Jensen, P.3
  • 147
    • 0032527065 scopus 로고    scopus 로고
    • Light and electron microscopic distribution of the AMPA receptor subunit, GluR2, in the spinal cord of control and G86R mutant superoxide dismutase transgenic mice
    • Morrison BM, Janssen WGM, Gordon JW, Morrison JH. Light and electron microscopic distribution of the AMPA receptor subunit, GluR2, in the spinal cord of control and G86R mutant superoxide dismutase transgenic mice. J Comp Neurol 1998:395:523-534
    • (1998) J Comp Neurol , vol.395 , pp. 523-534
    • Morrison, B.M.1    Janssen, W.G.M.2    Gordon, J.W.3    Morrison, J.H.4
  • 148
    • 0029671398 scopus 로고    scopus 로고
    • Regional analysis of developmental changes in the extent of GluR6 mRNA editing in rat brain
    • Schmitt J, Dux E, Gissel C, Paschen W. Regional analysis of developmental changes in the extent of GluR6 mRNA editing in rat brain. Dev Brain Res 1996;91:153-157
    • (1996) Dev Brain Res , vol.91 , pp. 153-157
    • Schmitt, J.1    Dux, E.2    Gissel, C.3    Paschen, W.4
  • 149
    • 0031579422 scopus 로고    scopus 로고
    • Developmental changes of RNA editing of glutamate receptor subunits GluR5 and GluR6: In vivo versus in vitro
    • Paschen W, Schmitt J, Gissel C, Dux E. Developmental changes of RNA editing of glutamate receptor subunits GluR5 and GluR6: in vivo versus in vitro. Dev Brain Res 1997;98: 271-280
    • (1997) Dev Brain Res , vol.98 , pp. 271-280
    • Paschen, W.1    Schmitt, J.2    Gissel, C.3    Dux, E.4
  • 150
    • 0023707216 scopus 로고
    • Phosphorylation of neurofilaments is altered in amyotrophic lateral sclerosis
    • Manetto V, Sternberger NH, Perry G, et al. Phosphorylation of neurofilaments is altered in amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 1988;47:642-653
    • (1988) J Neuropathol Exp Neurol , vol.47 , pp. 642-653
    • Manetto, V.1    Sternberger, N.H.2    Perry, G.3
  • 151
    • 0023738527 scopus 로고
    • Accumulation of phosphorylated neurofilaments in anterior horn motoneurons of amyotrophic lateral sclerosis patients
    • Munoz DG, Greene C, Perl DP, Selkoe DJ. Accumulation of phosphorylated neurofilaments in anterior horn motoneurons of amyotrophic lateral sclerosis patients. J Neuropathol Exp Neurol 1988;47:9-18
    • (1988) J Neuropathol Exp Neurol , vol.47 , pp. 9-18
    • Munoz, D.G.1    Greene, C.2    Perl, D.P.3    Selkoe, D.J.4
  • 152
    • 0024428392 scopus 로고
    • Focal accumulation of phosphorylated neurofilaments within anterior horn cell in familial amyotrophic lateral sclerosis
    • Mizusawa H, Matsumoto S, Yen S-H, et al. Focal accumulation of phosphorylated neurofilaments within anterior horn cell in familial amyotrophic lateral sclerosis. Acta Neuropathol (Berl) 1989;79:37-43
    • (1989) Acta Neuropathol (Berl) , vol.79 , pp. 37-43
    • Mizusawa, H.1    Matsumoto, S.2    Yen, S.-H.3
  • 154
    • 0027465098 scopus 로고
    • Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis
    • Côté F, Collard J-F, Julien J-P. Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis. Cell 1993;73:35-46
    • (1993) Cell , vol.73 , pp. 35-46
    • Côté, F.1    Collard, J.-F.2    Julien, J.-P.3
  • 155
    • 0027410516 scopus 로고
    • Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease
    • Xu Z, Cork LC, Griffin JW, Cleveland DW. Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell 1993;73:23-33
    • (1993) Cell , vol.73 , pp. 23-33
    • Xu, Z.1    Cork, L.C.2    Griffin, J.W.3    Cleveland, D.W.4
  • 156
    • 0028116467 scopus 로고
    • A mutant neurofilament subunit causes massive, selective motor neuron death: Implication for the pathogenesis of human motor neuron disease
    • Lee MK, Marszalek JR, Cleveland DW. A mutant neurofilament subunit causes massive, selective motor neuron death: implication for the pathogenesis of human motor neuron disease. Neuron 1994;13:975-988
    • (1994) Neuron , vol.13 , pp. 975-988
    • Lee, M.K.1    Marszalek, J.R.2    Cleveland, D.W.3
  • 157
    • 0025169140 scopus 로고
    • Abnormal distribution of phosphorylated neurofilaments in neuronal degeneration induced by kainic acid
    • Hugon J, Vallat JM. Abnormal distribution of phosphorylated neurofilaments in neuronal degeneration induced by kainic acid. Neurosci Lett 1990;119:45-48
    • (1990) Neurosci Lett , vol.119 , pp. 45-48
    • Hugon, J.1    Vallat, J.M.2
  • 158
    • 0028111812 scopus 로고
    • Age-associated and cell-type-specific neurofibrillary pathology in transgenic mice expressing the human mid-sized neurofilament subunit
    • Vickers JC, Morrison JH, Friedrich Jr VL, et al. Age-associated and cell-type-specific neurofibrillary pathology in transgenic mice expressing the human mid-sized neurofilament subunit. J Neurosci 1994;14:5603-5612
    • (1994) J Neurosci , vol.14 , pp. 5603-5612
    • Vickers, J.C.1    Morrison, J.H.2    Friedrich Jr., V.L.3


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