메뉴 건너뛰기




Volumn 74, Issue 3, 2000, Pages 1112-1121

Peptide fragments of β-amyloid precursor protein: Effects on parallel Fiber-Purkinje cell synaptic transmission in rat cerebellum

Author keywords

Alzheimer's disease; Calcium; Carboxy terminal fragment (CT105); Cerebellum; Purkinje cell; Amyloid precursor protein

Indexed keywords

AMPA RECEPTOR; AMYLOID PRECURSOR PROTEIN; CALCIUM; NITRIC OXIDE SYNTHASE;

EID: 0033962593     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.741112.x     Document Type: Article
Times cited : (16)

References (64)
  • 1
    • 0028323567 scopus 로고
    • Differential distribution of amyloid protein precursor immunoreactivity in the rat brain studied by using 5 different antibodies
    • Beeson J. G., Shelton E. R., Chan H. W., and Gage F. H. (1994) Differential distribution of amyloid protein precursor immunoreactivity in the rat brain studied by using 5 different antibodies. J. Comp. Neurol. 342, 78-96.
    • (1994) J. Comp. Neurol. , vol.342 , pp. 78-96
    • Beeson, J.G.1    Shelton, E.R.2    Chan, H.W.3    Gage, F.H.4
  • 2
    • 0024815331 scopus 로고
    • The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects
    • Benowitz L. I., Rodriguez W., Paskevich P., Mufson E. J., Schenk D., and Neve R. L. (1989) The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects. Exp. Neurol. 106, 237-250.
    • (1989) Exp. Neurol. , vol.106 , pp. 237-250
    • Benowitz, L.I.1    Rodriguez, W.2    Paskevich, P.3    Mufson, E.J.4    Schenk, D.5    Neve, R.L.6
  • 3
    • 0023086182 scopus 로고
    • Damage to mammalian cells by proteins that form transmembrane pores
    • Bhakdi S. and Tranumjensen J. (1987) Damage to mammalian cells by proteins that form transmembrane pores. Rev. Physiol. Biochem. Pharmacol. 107, 147-223.
    • (1987) Rev. Physiol. Biochem. Pharmacol. , vol.107 , pp. 147-223
    • Bhakdi, S.1    Tranumjensen, J.2
  • 4
    • 0030891016 scopus 로고    scopus 로고
    • Presynaptic and postsynaptic effects of nitric oxide donors at synapses between parallel fibres and Purkinje cells: Involvement in cerebellar long-term depression
    • Blond O., Daniel H., Otani S., Jaillard D., and Crepel F. (1997) Presynaptic and postsynaptic effects of nitric oxide donors at synapses between parallel fibres and Purkinje cells: involvement in cerebellar long-term depression. Neuroscience 77, 945-954.
    • (1997) Neuroscience , vol.77 , pp. 945-954
    • Blond, O.1    Daniel, H.2    Otani, S.3    Jaillard, D.4    Crepel, F.5
  • 5
    • 0026703461 scopus 로고
    • Association of the carboxy-terminus of beta-amyloid protein precursor with Alzheimer paired helical filaments
    • Caputo C. B., Sobel I. E., Scott C. W., Brunner W. F., Barth P. T., and Blowers D. P. (1992) Association of the carboxy-terminus of beta-amyloid protein precursor with Alzheimer paired helical filaments. Biochem. Biophys. Res. Commun. 185, 1034-1040.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 1034-1040
    • Caputo, C.B.1    Sobel, I.E.2    Scott, C.W.3    Brunner, W.F.4    Barth, P.T.5    Blowers, D.P.6
  • 6
    • 0029888368 scopus 로고    scopus 로고
    • Colocalization of lysosomal hydrolase and beta-amyloid in diffuse plaques of the cerebellum and striatum in Alzheimer's disease and Down's syndrome
    • Cataldo A. M., Barnett J. L., Mann D. A., and Nixon R. A. (1996) Colocalization of lysosomal hydrolase and beta-amyloid in diffuse plaques of the cerebellum and striatum in Alzheimer's disease and Down's syndrome. J. Neuropathol. Exp. Neurol. 55, 704-715.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 704-715
    • Cataldo, A.M.1    Barnett, J.L.2    Mann, D.A.3    Nixon, R.A.4
  • 7
    • 0029379605 scopus 로고
    • Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease
    • Checler F. (1995) Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease. J. Neurochem. 65, 1431-1444.
    • (1995) J. Neurochem. , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 8
    • 0028351412 scopus 로고
    • Bacterial expression, purification of full-length and carboxyl-terminal fragment of Alzheimer amyloid precursor protein and their proteolytic processing by thrombin
    • Chong Y. H., Jung J. M., Choi W., Park C. W., Choi K. S., and Suh Y. H. (1994) Bacterial expression, purification of full-length and carboxyl-terminal fragment of Alzheimer amyloid precursor protein and their proteolytic processing by thrombin. Life Sci. 54, 1259-1268.
    • (1994) Life Sci. , vol.54 , pp. 1259-1268
    • Chong, Y.H.1    Jung, J.M.2    Choi, W.3    Park, C.W.4    Choi, K.S.5    Suh, Y.H.6
  • 9
    • 0026699777 scopus 로고
    • Implants containing beta-amyloid protein are not neurotoxic to young and old rat brain
    • Clemens J. A. and Stephenson D. T. (1992) Implants containing beta-amyloid protein are not neurotoxic to young and old rat brain. Neurobiol. Aging 13, 581-586.
    • (1992) Neurobiol. Aging , vol.13 , pp. 581-586
    • Clemens, J.A.1    Stephenson, D.T.2
  • 10
    • 0030809128 scopus 로고    scopus 로고
    • Block of LTP in rat hippocampus in vivo by beta-amyloid precursor protein fragments
    • Cullen W. K., Suh Y. H., Anwyl R., and Rowan M. J. (1997) Block of LTP in rat hippocampus in vivo by beta-amyloid precursor protein fragments. Neuroreport 8, 3213-3217.
    • (1997) Neuroreport , vol.8 , pp. 3213-3217
    • Cullen, W.K.1    Suh, Y.H.2    Anwyl, R.3    Rowan, M.J.4
  • 11
    • 0029113189 scopus 로고
    • Two types of calcium response limited to single spines in cerebellar Purkinje cells
    • Denk W., Sugimori M., and Llinas R. (1995) Two types of calcium response limited to single spines in cerebellar Purkinje cells. Proc. Natl. Acad. Sci. USA 92, 8279-8282.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8279-8282
    • Denk, W.1    Sugimori, M.2    Llinas, R.3
  • 13
    • 0028977967 scopus 로고
    • 2+ signalling in fine dendrites and spines of cerebellar Purkinje neurons
    • 2+ signalling in fine dendrites and spines of cerebellar Purkinje neurons. Nature 373, 155-158.
    • (1995) Nature , vol.373 , pp. 155-158
    • Eilers, J.1    Augustine, G.J.2    Konnerth, A.3
  • 16
    • 0029923244 scopus 로고    scopus 로고
    • Membrane currents induced in Xenopus oocytes by the C-terminal fragment of the β-amyloid precursor protein
    • Fraser S. P., Suh Y. H., Chong Y. H., and Djamgoz M. B. A. (1996) Membrane currents induced in Xenopus oocytes by the C-terminal fragment of the β-amyloid precursor protein. J. Neurochem. 66, 2034-2040.
    • (1996) J. Neurochem. , vol.66 , pp. 2034-2040
    • Fraser, S.P.1    Suh, Y.H.2    Chong, Y.H.3    Djamgoz, M.B.A.4
  • 17
    • 0031014448 scopus 로고    scopus 로고
    • Ionic effects of the Alzheimer's disease beta-amyloid precursor protein and its metabolic fragments
    • Fraser S. P., Suh Y. H., and Djamgoz M. A. (1997) Ionic effects of the Alzheimer's disease beta-amyloid precursor protein and its metabolic fragments. Trends Neurosci. 20, 67-72.
    • (1997) Trends Neurosci. , vol.20 , pp. 67-72
    • Fraser, S.P.1    Suh, Y.H.2    Djamgoz, M.A.3
  • 18
    • 0026468207 scopus 로고
    • Expression of carboxy-terminal region of the beta-amyloid precursor protein in a heterogeneous culture of neuroblastoma cells - Evidence for altered processing and selective neurotoxicity
    • Fukuchi K., Kamino K., Deeb S. S., Furlong C. E., Sundstrom J. A., Smith A. C., and Martin G. M. (1992a) Expression of carboxy-terminal region of the beta-amyloid precursor protein in a heterogeneous culture of neuroblastoma cells - evidence for altered processing and selective neurotoxicity. Mol. Brain Res. 16, 37-46.
    • (1992) Mol. Brain Res. , vol.16 , pp. 37-46
    • Fukuchi, K.1    Kamino, K.2    Deeb, S.S.3    Furlong, C.E.4    Sundstrom, J.A.5    Smith, A.C.6    Martin, G.M.7
  • 19
    • 0026542758 scopus 로고
    • Overexpression of amyloid precursor protein alters its normal processing and is associated with neurotoxicity
    • Fukuchi K., Kamino K., Deeb S. S., Smith A. C., Dang T., and Martin G. M. (1992b) Overexpression of amyloid precursor protein alters its normal processing and is associated with neurotoxicity. Biochem. Biophys. Res. Commun. 182, 165-173.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 165-173
    • Fukuchi, K.1    Kamino, K.2    Deeb, S.S.3    Smith, A.C.4    Dang, T.5    Martin, G.M.6
  • 20
    • 0030590225 scopus 로고    scopus 로고
    • Purkinje cell loss and astrocytosis in the cerebellum in familial and sporadic Alzheimer's disease
    • Fukutani Y., Cairns N. J., Rossor M. N., and Lantos P. L. (1996) Purkinje cell loss and astrocytosis in the cerebellum in familial and sporadic Alzheimer's disease. Neurosci. Lett. 214, 33-36.
    • (1996) Neurosci. Lett. , vol.214 , pp. 33-36
    • Fukutani, Y.1    Cairns, N.J.2    Rossor, M.N.3    Lantos, P.L.4
  • 21
    • 0030068094 scopus 로고    scopus 로고
    • + channels and suppression of neuronal activity by secreted beta-amyloid precursor protein
    • + channels and suppression of neuronal activity by secreted beta-amyloid precursor protein. Nature 379, 74-78.
    • (1996) Nature , vol.379 , pp. 74-78
    • Furukawa, K.1    Narger, S.W.2    Blalock, E.M.3    Mattson, M.P.4
  • 24
    • 0021256895 scopus 로고
    • Alzheimer's disease - Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (1984) Alzheimer's disease - initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 25
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde T. E., Estus S., Younkin L. H., Selkoe D. J., and Younkin S. G. (1992) Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 255, 728-730.
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 26
    • 0026735070 scopus 로고
    • Targeting of cell-surface beta-amyloid precursor protein to lysosomes - Alternative processing into amyloid-bearing fragments
    • Haass C., Koo E. H., Mellon A., Hung A. Y., and Selkoe D. J. (1992a) Targeting of cell-surface beta-amyloid precursor protein to lysosomes - alternative processing into amyloid-bearing fragments. Nature 357, 500-503.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 28
    • 0029971424 scopus 로고    scopus 로고
    • Strong activation of parallel fibers produces localized calcium transients and a form of LTD that spreads to distant synapses
    • Hartell N. A. (1996a) Strong activation of parallel fibers produces localized calcium transients and a form of LTD that spreads to distant synapses. Neuron 16, 601-610.
    • (1996) Neuron , vol.16 , pp. 601-610
    • Hartell, N.A.1
  • 29
    • 0003521191 scopus 로고    scopus 로고
    • Two separate pathways for cerebellar LTD: NO-dependent and NO-independent
    • Hartell N. A. (1996b) Two separate pathways for cerebellar LTD: NO-dependent and NO-independent. Behav. Brain Sci. 19, 453.
    • (1996) Behav. Brain Sci. , vol.19 , pp. 453
    • Hartell, N.A.1
  • 30
    • 0026699985 scopus 로고
    • Protease inhibitors generate cytotoxic fragments from Alzheimer amyloid protein precursor in cDNA-transfected glioma cells
    • Hayashi Y., Kashiwagi K., and Yoshikawa K. (1992) Protease inhibitors generate cytotoxic fragments from Alzheimer amyloid protein precursor in cDNA-transfected glioma cells. Biochem. Biophys. Res. Commun. 187, 1249-1255.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1249-1255
    • Hayashi, Y.1    Kashiwagi, K.2    Yoshikawa, K.3
  • 31
    • 0028316742 scopus 로고
    • Properties of glutamate receptors are modified during long-term depression in rat cerebellar Purkinje cells
    • Hemart N., Daniel H., Jaillard D., and Crepel F. (1994) Properties of glutamate receptors are modified during long-term depression in rat cerebellar Purkinje cells. Neurosci. Res. 19, 213-221.
    • (1994) Neurosci. Res. , vol.19 , pp. 213-221
    • Hemart, N.1    Daniel, H.2    Jaillard, D.3    Crepel, F.4
  • 33
    • 0024447098 scopus 로고
    • Diffuse senile plaques occur commonly in the cerebellum in Alzheimer's disease
    • Joachim C. L., Morris J. H., and Selkoe D. J. (1989) Diffuse senile plaques occur commonly in the cerebellum in Alzheimer's disease. Am. J. Pathol. 135, 309-319.
    • (1989) Am. J. Pathol. , vol.135 , pp. 309-319
    • Joachim, C.L.1    Morris, J.H.2    Selkoe, D.J.3
  • 34
    • 0027934516 scopus 로고
    • Secretory cleavage site of Alzheimer amyloid precursor protein is heterogeneous in Down's syndrome brain
    • Kametani F., Tanaka K., Tokuda T., and Ikeda S. (1994) Secretory cleavage site of Alzheimer amyloid precursor protein is heterogeneous in Down's syndrome brain. FEBS Lett. 351, 165-167.
    • (1994) FEBS Lett. , vol.351 , pp. 165-167
    • Kametani, F.1    Tanaka, K.2    Tokuda, T.3    Ikeda, S.4
  • 35
    • 0026443727 scopus 로고
    • Deposition of beta/a4 immunoreactivity and neuronal pathology in transgenic mice expressing the carboxyl-terminal fragment of the Alzheimer amyloid precursor in the brain
    • Kammesheidt A., Boyce F. M., Spanoyannis A. F., Cummings B. J., Ortegon M., Cotman C., Vaught J. L., and Neve R. L. (1992) Deposition of beta/a4 immunoreactivity and neuronal pathology in transgenic mice expressing the carboxyl-terminal fragment of the Alzheimer amyloid precursor in the brain. Proc. Natl. Acad. Sci. USA 89, 10857-10861.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10857-10861
    • Kammesheidt, A.1    Boyce, F.M.2    Spanoyannis, A.F.3    Cummings, B.J.4    Ortegon, M.5    Cotman, C.6    Vaught, J.L.7    Neve, R.L.8
  • 37
    • 0029799609 scopus 로고    scopus 로고
    • Neurotoxicity of a carboxyl-terminal fragment of the Alzheimer's amyloid precursor protein
    • Kim S.-H. and Suh Y.-H. (1996) Neurotoxicity of a carboxyl-terminal fragment of the Alzheimer's amyloid precursor protein. J. Neurochem. 67, 1172-1182.
    • (1996) J. Neurochem. , vol.67 , pp. 1172-1182
    • Kim, S.-H.1    Suh, Y.-H.2
  • 38
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involve the endocytic pathway
    • Koo E. H. and Squazzo S. L. (1994) Evidence that production and release of amyloid beta-protein involve the endocytic pathway. J. Biol. Chem. 269, 17386-17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 39
    • 0027288860 scopus 로고
    • Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth
    • Koo E. H., Park L., and Selkoe D. J. (1993) Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth. Proc. Natl. Acad. Sci. USA 90, 4748-4752.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4748-4752
    • Koo, E.H.1    Park, L.2    Selkoe, D.J.3
  • 42
    • 0028281506 scopus 로고
    • Amyloid plaques in cerebellar cortex and the integrity of Purkinje cell dendrites
    • Li Y. T., Woodruffpak D. S., and Trojanowski J. Q. (1994) Amyloid plaques in cerebellar cortex and the integrity of Purkinje cell dendrites. Neurobiol. Aging 15, 1-9.
    • (1994) Neurobiol. Aging , vol.15 , pp. 1-9
    • Li, Y.T.1    Woodruffpak, D.S.2    Trojanowski, J.Q.3
  • 43
    • 0028014381 scopus 로고
    • Altered processing characteristics of beta-amyloid-containing peptides in cytosol and in media of familial Alzheimer's disease cells
    • Matsumoto A. (1994) Altered processing characteristics of beta-amyloid-containing peptides in cytosol and in media of familial Alzheimer's disease cells. Biochim. Biophys. Acta 1225, 304-310.
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 304-310
    • Matsumoto, A.1
  • 44
    • 0031022255 scopus 로고    scopus 로고
    • Increased expression of cathepsins E and D in neurons of the aged rat brain and their colocalization with lipofuscin and carboxy-terminal fragments of Alzheimer amyloid precursor protein
    • Nakanishi H., Amano T., Sastradipura D. F., Yoshimine Y., Tsukuba T., Tanabe K., Hirotsu I., Ohono T., and Yamamoto K. (1997) Increased expression of cathepsins E and D in neurons of the aged rat brain and their colocalization with lipofuscin and carboxy-terminal fragments of Alzheimer amyloid precursor protein. J. Neurochem. 68, 739-749.
    • (1997) J. Neurochem. , vol.68 , pp. 739-749
    • Nakanishi, H.1    Amano, T.2    Sastradipura, D.F.3    Yoshimine, Y.4    Tsukuba, T.5    Tanabe, K.6    Hirotsu, I.7    Ohono, T.8    Yamamoto, K.9
  • 46
    • 0026568638 scopus 로고
    • Brain transplants of cells expressing the carboxyl-terminal fragment of the Alzheimer amyloid protein precursor cause specific neuropathology in vivo
    • Neve R. L., Kammesheidt A., and Hohmann C. F. (1992) Brain transplants of cells expressing the carboxyl-terminal fragment of the Alzheimer amyloid protein precursor cause specific neuropathology in vivo. Proc. Natl. Acad. Sci. USA 89, 3448-3452.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3448-3452
    • Neve, R.L.1    Kammesheidt, A.2    Hohmann, C.F.3
  • 47
    • 0029862137 scopus 로고    scopus 로고
    • Age-dependent neuronal and synaplic degeneration in mice transgenic for the c-terminus of the amyloid precursor protein
    • Ostergranite M. L., McPhie D. L., Greenan J., and Neve R. L. (1996) Age-dependent neuronal and synaplic degeneration in mice transgenic for the c-terminus of the amyloid precursor protein. J. Neurosci. 16, 6732-6741.
    • (1996) J. Neurosci. , vol.16 , pp. 6732-6741
    • Ostergranite, M.L.1    McPhie, D.L.2    Greenan, J.3    Neve, R.L.4
  • 49
    • 0028171885 scopus 로고
    • Amyloid β-protein precursors; new clues to the genesis of Alzheimer's disease
    • Selkoe D. J. (1994) Amyloid β-protein precursors; new clues to the genesis of Alzheimer's disease. Curr. Opin. Neurobiol. 4, 708-716.
    • (1994) Curr. Opin. Neurobiol. , vol.4 , pp. 708-716
    • Selkoe, D.J.1
  • 50
    • 0001067847 scopus 로고
    • Beta-amyloid precursor protein of Alzheimer disease occurs as 110-kilodalton to 135-kilodalton membrane-associated proteins in neural and nonneural tissues
    • Selkoe D. J., Podlisny M. B., Joachim C. L., Vickers E. A., Lee G., Fritz L. C., and Oltersdorf T. (1988) Beta-amyloid precursor protein of Alzheimer disease occurs as 110-kilodalton to 135-kilodalton membrane-associated proteins in neural and nonneural tissues. Proc. Natl. Acad. Sci. USA 85, 7341-7345.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7341-7345
    • Selkoe, D.J.1    Podlisny, M.B.2    Joachim, C.L.3    Vickers, E.A.4    Lee, G.5    Fritz, L.C.6    Oltersdorf, T.7
  • 52
    • 0025373508 scopus 로고
    • Evidence that beta-amyloid protein in Alzheimer's disease is not derived by normal processing
    • Sisodia S. S., Koo E. H., Beyreuther K., Unterbeck A., and Price D. L. (1990) Evidence that beta-amyloid protein in Alzheimer's disease is not derived by normal processing. Science 248, 492-495.
    • (1990) Science , vol.248 , pp. 492-495
    • Sisodia, S.S.1    Koo, E.H.2    Beyreuther, K.3    Unterbeck, A.4    Price, D.L.5
  • 54
    • 0027971254 scopus 로고
    • Cytotoxicity mediated by conditional expression of a carboxyl-terminal derivative of the beta-amyloid precursor protein
    • Sopher B. L., Fukuchi K., Smith A. C., Leppig K. A., Furlong C. E., and Martin G. M. (1994) Cytotoxicity mediated by conditional expression of a carboxyl-terminal derivative of the beta-amyloid precursor protein. Mol. Brain Res. 26, 207-217.
    • (1994) Mol. Brain Res. , vol.26 , pp. 207-217
    • Sopher, B.L.1    Fukuchi, K.2    Smith, A.C.3    Leppig, K.A.4    Furlong, C.E.5    Martin, G.M.6
  • 55
    • 0026657287 scopus 로고
    • Failure of beta-amyloid protein fragment 25-35 to cause hippocampal damage in the rat
    • Steinbehrens B., Adams K., Yeh M., and Sapolsky R. (1992) Failure of beta-amyloid protein fragment 25-35 to cause hippocampal damage in the rat. Neurobiol. Aging 13, 577-579.
    • (1992) Neurobiol. Aging , vol.13 , pp. 577-579
    • Steinbehrens, B.1    Adams, K.2    Yeh, M.3    Sapolsky, R.4
  • 56
    • 0029088203 scopus 로고
    • Pre- and postsynaptic determinants of epsc waveform at cerebellar climbing fiber and parallel fiber to Purkinje cell synapses
    • Takahashi M., Kovalchuk Y., and Attwell D. (1995) Pre- and postsynaptic determinants of epsc waveform at cerebellar climbing fiber and parallel fiber to Purkinje cell synapses. J. Neurosci. 15, 5693-5702.
    • (1995) J. Neurosci. , vol.15 , pp. 5693-5702
    • Takahashi, M.1    Kovalchuk, Y.2    Attwell, D.3
  • 57
    • 0026558595 scopus 로고
    • Identification of a stable fragment of the Alzheimer amyloid precursor containing the beta-protein in brain microvessels
    • Tamaoka A., Kalaria R. N., Lieberburg I., and Selkoe D. J. (1992) Identification of a stable fragment of the Alzheimer amyloid precursor containing the beta-protein in brain microvessels. Proc. Natl. Acad. Sci. USA 89, 1345-1349.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1345-1349
    • Tamaoka, A.1    Kalaria, R.N.2    Lieberburg, I.3    Selkoe, D.J.4
  • 58
    • 0028985583 scopus 로고
    • Secretory cleavage of beta-amyloid precursor protein in the cerebral white matter produces amyloidogenic carboxyl-terminal fragments
    • Tokuda T., Tanaka K., Kametani F., Ikeda S., and Yanagisawa N. (1995) Secretory cleavage of beta-amyloid precursor protein in the cerebral white matter produces amyloidogenic carboxyl-terminal fragments. Neurosci. Lett. 186, 149-152.
    • (1995) Neurosci. Lett. , vol.186 , pp. 149-152
    • Tokuda, T.1    Tanaka, K.2    Kametani, F.3    Ikeda, S.4    Yanagisawa, N.5
  • 59
    • 0027043303 scopus 로고
    • P-type calcium channels in the somata and dendrites of adult cerebellar Purkinje cells
    • Usowicz M. M., Sugimori M., Chersky B., and Llinas R. (1992) P-type calcium channels in the somata and dendrites of adult cerebellar Purkinje cells. Neuron 9, 1185-1199.
    • (1992) Neuron , vol.9 , pp. 1185-1199
    • Usowicz, M.M.1    Sugimori, M.2    Chersky, B.3    Llinas, R.4
  • 61
    • 0024472693 scopus 로고
    • Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease
    • Yankner B. A., Dawes L. R., Fisher S., Villakomaroff L., Ostergranite M. L., and Neve R. L. (1989) Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease. Science 245, 417-420.
    • (1989) Science , vol.245 , pp. 417-420
    • Yankner, B.A.1    Dawes, L.R.2    Fisher, S.3    Villakomaroff, L.4    Ostergranite, M.L.5    Neve, R.L.6
  • 62
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta-protein - Reversal by tachykinin neuropeptides
    • Yankner B. A., Duffy L. K., and Kirschner D. A. (1990) Neurotrophic and neurotoxic effects of amyloid beta-protein - reversal by tachykinin neuropeptides. Science 250, 279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 63
    • 0026779680 scopus 로고
    • Degeneration in vitro of postmitotic neurons overexpressing the Alzheimer amyloid protein precursor
    • Yoshikawa K., Aizawa T., and Hayashi Y. (1992) Degeneration in vitro of postmitotic neurons overexpressing the Alzheimer amyloid protein precursor. Nature 359, 64-67.
    • (1992) Nature , vol.359 , pp. 64-67
    • Yoshikawa, K.1    Aizawa, T.2    Hayashi, Y.3
  • 64
    • 0022558797 scopus 로고
    • Mechanism of membrane damage mediated by human eosinophil cationic protein
    • Young J. D., Peterson C. B., Venge P., and Cohn Z. A. (1986) Mechanism of membrane damage mediated by human eosinophil cationic protein. Nature 321, 613-616.
    • (1986) Nature , vol.321 , pp. 613-616
    • Young, J.D.1    Peterson, C.B.2    Venge, P.3    Cohn, Z.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.