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Volumn 4, Issue 2, 2006, Pages 149-163

The role of β-amyloid protein in synaptic function: Implications for Alzheimer's disease therapy

Author keywords

amyloid protein; Alzheimer disease; Cognitive impairment; Synaptic dysfunction; Synaptic plasticity

Indexed keywords

ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; AMYLOID PRECURSOR PROTEIN; ANTILIPEMIC AGENT; BENZOPHENONE DERIVATIVE; BETA SECRETASE; BETA SECRETASE INHIBITOR; CATION CHANNEL; CHOLINESTERASE INHIBITOR; DONEPEZIL; GAMMA SECRETASE INHIBITOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; IBUPROFEN; INDOMETACIN; JLK 1 8; L 405 484; L 682 679; L 685 458; L 852 205; L 852 505; L 852 646; NONSTEROID ANTIINFLAMMATORY AGENT; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 33646570823     PISSN: 1570159X     EISSN: None     Source Type: Journal    
DOI: 10.2174/157015906776359531     Document Type: Review
Times cited : (40)

References (206)
  • 1
    • 0032077682 scopus 로고    scopus 로고
    • Positive and negative regulatory mechanisms that mediate long-term memory storage
    • Abel, T., Kandel, E. (1998) Positive and negative regulatory mechanisms that mediate long-term memory storage. Brain Res. Brain Res. Rev., 26, 360-378.
    • (1998) Brain Res. Brain Res. Rev. , vol.26 , pp. 360-378
    • Abel, T.1    Kandel, E.2
  • 2
    • 0035943464 scopus 로고    scopus 로고
    • Response Dynamics of Entorhinal Cortex in Awake, Anesthetized, and Bulbotomized Rats
    • Ahrens, K.F., Freeman, W.J. (2001) Response Dynamics of Entorhinal Cortex in Awake, Anesthetized, and Bulbotomized Rats. Brain Res., 911, 193-202.
    • (2001) Brain Res. , vol.911 , pp. 193-202
    • Ahrens, K.F.1    Freeman, W.J.2
  • 5
    • 0028980467 scopus 로고
    • β-amyloid peptide fragment 25-35 potentiates the calcium-dependent release of excitatory amino acids from depolarized hippocampal slices
    • Arias, C., Arrieta, I., Tapia, R. (1995) β-amyloid peptide fragment 25-35 potentiates the calcium-dependent release of excitatory amino acids from depolarized hippocampal slices. J. Neurosci. Res., 41, 561-566.
    • (1995) J. Neurosci. Res. , vol.41 , pp. 561-566
    • Arias, C.1    Arrieta, I.2    Tapia, R.3
  • 6
    • 0036315425 scopus 로고    scopus 로고
    • β-amyloid neurotoxicity is exacerbated during glycolysis inhibition and mitochondrial impairment in the rat hippocampus in vivo and in isolated nerve terminals: Implications for Alzheimer's disease
    • Arias, C., Montiel, T., Quiroz-Báez, R., Massieu, L. (2002) β-amyloid neurotoxicity is exacerbated during glycolysis inhibition and mitochondrial impairment in the rat hippocampus in vivo and in isolated nerve terminals: implications for Alzheimer's disease. Exp. Neurol., 176, 163-174.
    • (2002) Exp. Neurol. , vol.176 , pp. 163-174
    • Arias, C.1    Montiel, T.2    Quiroz-Báez, R.3    Massieu, L.4
  • 7
    • 1242269712 scopus 로고    scopus 로고
    • Architecture of the Alzheimer's AβP ion channel pore
    • Arispe, N. (2004) Architecture of the Alzheimer's AβP ion channel pore. J. Membr. Biol., 197, 33-48.
    • (2004) J. Membr. Biol. , vol.197 , pp. 33-48
    • Arispe, N.1
  • 8
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP (1-40)] in bilayer membranes
    • Arispe, N., Pollard, H.B., Rojas, E. (1993b) Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP (1-40)] in bilayer membranes. Proc. Natl. Acad. Sci. U.S.A., 90, 10573-10577.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 10
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe, N., Rojas, E., Pollard, H.B. (1993a) Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci. U.S.A., 90, 567-571.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 12
    • 0035107442 scopus 로고    scopus 로고
    • Neuroprotective effects of non-steroidal anti-inflammatory drugs by direct scavenging of nitric oxide radicals
    • Asanuma, M., Nishibayashi-Asanuma, S., Miyazaki, I., Kohno, M., Ogawa, N. (2001) Neuroprotective effects of non-steroidal anti-inflammatory drugs by direct scavenging of nitric oxide radicals. J. Neurochem., 76, 1895-1904.
    • (2001) J. Neurochem. , vol.76 , pp. 1895-1904
    • Asanuma, M.1    Nishibayashi-Asanuma, S.2    Miyazaki, I.3    Kohno, M.4    Ogawa, N.5
  • 13
    • 11844304055 scopus 로고    scopus 로고
    • β-Amyloid peptide25-35 depresses excitatory synaptic transmission in the rat basolateral amygdala "in vitro"
    • Ashenafi, S., Fuente, A., Criado, J.M., Riolobos, A.S., Heredia, M., Yajeya, J. (2005) β-Amyloid peptide25-35 depresses excitatory synaptic transmission in the rat basolateral amygdala "in vitro". Neurobiol. Aging, 26, 419-428.
    • (2005) Neurobiol. Aging , vol.26 , pp. 419-428
    • Ashenafi, S.1    Fuente, A.2    Criado, J.M.3    Riolobos, A.S.4    Heredia, M.5    Yajeya, J.6
  • 14
    • 1842636826 scopus 로고    scopus 로고
    • 2+ channel modulation in the neuroprotective actions of estrogen in β-amyloid protein and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) cytotoxic models
    • 2+ channel modulation in the neuroprotective actions of estrogen in β-amyloid protein and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) cytotoxic models. Neurochem. Int., 45, 31-38.
    • (2004) Neurochem. Int. , vol.45 , pp. 31-38
    • Ba, F.1    Pang, P.K.2    Benishin, C.G.3
  • 16
    • 0030735176 scopus 로고    scopus 로고
    • The mean Aβ load in the hippocampus correlates with duration and severity of dementia in subgroups of Alzheimer disease
    • Bartoo, G.T., Nochlin, D., Chang, D., Kim, Y., Sumi, S.M. (1997) The mean Aβ load in the hippocampus correlates with duration and severity of dementia in subgroups of Alzheimer disease. J. Neuropathol. Exp. Neurol., 56, 531-540.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 531-540
    • Bartoo, G.T.1    Nochlin, D.2    Chang, D.3    Kim, Y.4    Sumi, S.M.5
  • 17
    • 0343069811 scopus 로고    scopus 로고
    • Are cognitive processes manifested in event-related gamma, alpha, theta and delta oscillations in the EEG?
    • Basar, E., Basar-Eroglu, C., Karakas, S., Schurmann, M. (1999) Are cognitive processes manifested in event-related gamma, alpha, theta and delta oscillations in the EEG? Neurosci. Lett., 259, 165-168.
    • (1999) Neurosci. Lett. , vol.259 , pp. 165-168
    • Basar, E.1    Basar-Eroglu, C.2    Karakas, S.3    Schurmann, M.4
  • 19
    • 0345096618 scopus 로고    scopus 로고
    • Structural involvement of the glutamatergic presynaptic boutons in a transgenic mouse model expressing early onset amyloid pathology
    • Bell, K.F., de Kort, G.J., Steggerda, S., Shigemoto, R., Ribeiro-daSilva, A., Cuello, A.C. (2003) Structural involvement of the glutamatergic presynaptic boutons in a transgenic mouse model expressing early onset amyloid pathology. Neurosci. Lett., 353, 143-147.
    • (2003) Neurosci. Lett. , vol.353 , pp. 143-147
    • Bell, K.F.1    de Kort, G.J.2    Steggerda, S.3    Shigemoto, R.4    Ribeiro-daSilva, A.5    Cuello, A.C.6
  • 20
    • 0024839699 scopus 로고
    • Computer-assisted morphometry of synaptic plasticity during aging and dementia
    • Bertoni-Freddari, C., Fattoretti, P., Meier-Ruge, W., Ulrich, J. (1989) Computer-assisted morphometry of synaptic plasticity during aging and dementia. Pathol. Res. Pract., 185, 799-802.
    • (1989) Pathol. Res. Pract. , vol.185 , pp. 799-802
    • Bertoni-Freddari, C.1    Fattoretti, P.2    Meier-Ruge, W.3    Ulrich, J.4
  • 21
    • 0036079324 scopus 로고    scopus 로고
    • Eliminating membrane depolarization caused by the Alzheimer peptide Aβ(1-42)
    • Blanchard, B.J., Stockwell, B.R., Ingram, V.M. (2002b) Eliminating membrane depolarization caused by the Alzheimer peptide Aβ(1-42). Biochem. Biophys. Res. Commun., 293, 1204-1208.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1204-1208
    • Blanchard, B.J.1    Stockwell, B.R.2    Ingram, V.M.3
  • 22
    • 0036075751 scopus 로고    scopus 로고
    • Mechanism of membrane depolarization caused by the Alzheimer Aβ1-42 peptide
    • Blanchard, B.J., Thomas, V.L., Ingram, V.M. (2002a) Mechanism of membrane depolarization caused by the Alzheimer Aβ1-42 peptide. Biochem. Biophys. Res. Commun.,293, 1197-1203.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1197-1203
    • Blanchard, B.J.1    Thomas, V.L.2    Ingram, V.M.3
  • 23
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss, T.V., Collingridge, G.L. (1993) A synaptic model of memory: long-term potentiation in the hippocampus. Nature, 361, 31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.1    Collingridge, G.L.2
  • 24
    • 0031973596 scopus 로고    scopus 로고
    • Seasonal plasticity of the song control system in wild Nuttall's white-crowned sparrows
    • Brenowitz, E.A., Baptista, L.F., Lent, K., Wingfield, J.C. (1998) Seasonal plasticity of the song control system in wild Nuttall's white-crowned sparrows. J. Neurobiol., 34, 69-82.
    • (1998) J. Neurobiol. , vol.34 , pp. 69-82
    • Brenowitz, E.A.1    Baptista, L.F.2    Lent, K.3    Wingfield, J.C.4
  • 25
    • 14844334934 scopus 로고    scopus 로고
    • Synaptic transmission and synchronous activity is disrupted in hippocampal slices taken from aged TAS10 mice
    • Brown, J.T., Richardson, J.C., Collingridge, G.L., Randall, A.D., Davies, C.H. (2005) Synaptic transmission and synchronous activity is disrupted in hippocampal slices taken from aged TAS10 mice. Hippocampus, 15, 110-117.
    • (2005) Hippocampus , vol.15 , pp. 110-117
    • Brown, J.T.1    Richardson, J.C.2    Collingridge, G.L.3    Randall, A.D.4    Davies, C.H.5
  • 26
    • 18044375010 scopus 로고    scopus 로고
    • Presenilin endoproteolysis is an intramolecular cleavage
    • Brunkan, A.L., Goate, A.M. (2005) Presenilin endoproteolysis is an intramolecular cleavage. Mol. Cell Neurosci., 29, 65-73.
    • (2005) Mol. Cell Neurosci. , vol.29 , pp. 65-73
    • Brunkan, A.L.1    Goate, A.M.2
  • 27
    • 0344824654 scopus 로고    scopus 로고
    • 1-42-associated free radical induced oxidative stress and neurodegeneration in Alzheimer's disease brain: Mechanisms and consequences
    • 1-42-associated free radical induced oxidative stress and neurodegeneration in Alzheimer's disease brain: mechanisms and consequences. Curr. Med. Chem., 10, 2651-2659.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 2651-2659
    • Butterfield, D.A.1
  • 29
    • 0027298090 scopus 로고
    • Electrophysiological effects of 25-35 amyloid-β-protein on guinea-pig lateral septal neurons
    • Carette, B., Poulain, P., Delacourte, A. (1993) Electrophysiological effects of 25-35 amyloid-β-protein on guinea-pig lateral septal neurons. Neurosci. Lett., 151, 111-114.
    • (1993) Neurosci. Lett. , vol.151 , pp. 111-114
    • Carette, B.1    Poulain, P.2    Delacourte, A.3
  • 31
    • 0036644989 scopus 로고    scopus 로고
    • Reversal of amyloid beta toxicity in Alzheimer's disease model Tg2576 by intraventricular antiamyloid β antibody
    • Chauhan, N.B., Siegel, G.J. (2002) Reversal of amyloid beta toxicity in Alzheimer's disease model Tg2576 by intraventricular antiamyloid β antibody. J. Neurosci. Res., 69, 10-23.
    • (2002) J. Neurosci. Res. , vol.69 , pp. 10-23
    • Chauhan, N.B.1    Siegel, G.J.2
  • 32
    • 0034069795 scopus 로고    scopus 로고
    • Impairment of hippocampal long-term potentiation by Alzheimer amyloid β-peptides
    • Chen, Q.S., Kagan, B.L., Hirakura, Y., Xie, C.W. (2000) Impairment of hippocampal long-term potentiation by Alzheimer amyloid β-peptides. J. Neurosci. Res., 60, 65-72.
    • (2000) J. Neurosci. Res. , vol.60 , pp. 65-72
    • Chen, Q.S.1    Kagan, B.L.2    Hirakura, Y.3    Xie, C.W.4
  • 33
    • 0036354603 scopus 로고    scopus 로고
    • Alzheimer amyloid β-peptide inhibits the late phase of long-term potentiation through calcineurin-dependent mechanisms in the hippocampal dentate gyrus
    • Chen, Q.S., Wei, W.Z., Shimahara, T., Xie, C.W. (2002) Alzheimer amyloid β-peptide inhibits the late phase of long-term potentiation through calcineurin-dependent mechanisms in the hippocampal dentate gyrus. Neurobiol. Learn. Mem., 77, 354-371.
    • (2002) Neurobiol. Learn. Mem. , vol.77 , pp. 354-371
    • Chen, Q.S.1    Wei, W.Z.2    Shimahara, T.3    Xie, C.W.4
  • 34
    • 2442711560 scopus 로고    scopus 로고
    • Fyn kinase modulates synaptotoxicity, but not aberrant sprouting human, in amyloid precursor protein transgenic mice
    • Chin, J., Palop, J.J., Yu, G.Q., Kojima, N., Masliah, E., Mucke, L. (2004) Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice. J. Neurosci., 24, 4692-4697.
    • (2004) J. Neurosci. , vol.24 , pp. 4692-4697
    • Chin, J.1    Palop, J.J.2    Yu, G.Q.3    Kojima, N.4    Masliah, E.5    Mucke, L.6
  • 38
    • 0001978651 scopus 로고    scopus 로고
    • Caspase activation in dystrophic neurites in Alzheimer's disease and aged HuAPPsw transgenic mice
    • Iqbal, K., Swaab, D.F., Winbland, B., Wisniewski, H.M., Eds., New York: Wiley & Sons
    • Cole, G.M., Yang, F., Chen, P.P., Frautschy, S.A., Hsiao, K. (1999) Caspase activation in dystrophic neurites in Alzheimer's disease and aged HuAPPsw transgenic mice. In: Iqbal, K., Swaab, D.F., Winbland, B., Wisniewski, H.M., Eds., Alzheimer's disease and related disorders: etiology, pathogenesis and therapeutics. New York: Wiley & Sons. pp. 363-369.
    • (1999) Alzheimer's Disease and Related Disorders: Etiology, Pathogenesis and Therapeutics , pp. 363-369
    • Cole, G.M.1    Yang, F.2    Chen, P.P.3    Frautschy, S.A.4    Hsiao, K.5
  • 39
    • 0026713423 scopus 로고
    • β-amyloid neurotoxicity: A discussion on in vitro findings
    • Cotman, C.W., Pike, C.J., Copan, A. (1992) β-amyloid neurotoxicity: A discussion on in vitro findings. Neurobiol. Aging, 13, 587-590.
    • (1992) Neurobiol. Aging , vol.13 , pp. 587-590
    • Cotman, C.W.1    Pike, C.J.2    Copan, A.3
  • 40
    • 0030809128 scopus 로고    scopus 로고
    • Block of LTP in rat hippocampus in vivo by β-amyloid precursor protein fragments
    • Cullen, W.K., Suh, Y.H., Anwyl, R., Rowan, M.J. (1997) Block of LTP in rat hippocampus in vivo by β-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
  • 41
    • 0030942145 scopus 로고    scopus 로고
    • β-Amyloid produces a delayed NMDA receptor-dependent reduction in synaptic transmission in rat hippocampus
    • Cullen, W.K., Wu, J., Anwyl, R., Rowan, M.J. (1996) β-Amyloid produces a delayed NMDA receptor-dependent reduction in synaptic transmission in rat hippocampus. Neuroreport, 20, 87-92.
    • (1996) Neuroreport , vol.20 , pp. 87-92
    • Cullen, W.K.1    Wu, J.2    Anwyl, R.3    Rowan, M.J.4
  • 42
    • 0028972701 scopus 로고
    • Image analysis of β-amyloid load in Alzheimer's disease and relation to dementia severity
    • Cummings, B.J., Cotman, C.W. (1995) Image analysis of β-amyloid load in Alzheimer's disease and relation to dementia severity. Lancet, 346, 1524-1528.
    • (1995) Lancet , vol.346 , pp. 1524-1528
    • Cummings, B.J.1    Cotman, C.W.2
  • 43
    • 0030464914 scopus 로고    scopus 로고
    • β-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease
    • Cummings, B.J., Pike, C.J., Shankle, R., Cotman, C.W. (1996) β-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease. Neurobiol. Aging, 17, 921-933.
    • (1996) Neurobiol. Aging , vol.17 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 44
    • 0023106967 scopus 로고
    • A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease
    • Davies, C.A., Mann, D.M., Sumpter, P.Q., Yates, P.O. (1987) A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease. J. Neurol. Sci., 78, 151-164.
    • (1987) J. Neurol. Sci. , vol.78 , pp. 151-164
    • Davies, C.A.1    Mann, D.M.2    Sumpter, P.Q.3    Yates, P.O.4
  • 45
    • 0030710114 scopus 로고    scopus 로고
    • The 'amyloid cascade hypothesis' of AD: Decoy or real McCoy?
    • Davis, J.N., Chisholm, J.C. (1997) The 'amyloid cascade hypothesis' of AD: decoy or real McCoy? Trends Neurosci., 20, 558-559.
    • (1997) Trends Neurosci. , vol.20 , pp. 558-559
    • Davis, J.N.1    Chisholm, J.C.2
  • 46
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • DeKosky, S.T., Scheff, S.W. (1990) Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann. Neurol., 27, 457-464.
    • (1990) Ann. Neurol. , vol.27 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 47
    • 0030513943 scopus 로고    scopus 로고
    • Structural correlates of cognition in dementia: Quantification and assessment of synapse change
    • DeKosky, S.T., Scheff, S.W., Styren, S.D. (1996) Structural correlates of cognition in dementia: quantification and assessment of synapse change. Neurodegeneration, 5, 417-421.
    • (1996) Neurodegeneration , vol.5 , pp. 417-421
    • DeKosky, S.T.1    Scheff, S.W.2    Styren, S.D.3
  • 48
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease
    • DeMattos, R.B., Bales, K.R., Cummins, D.J., Dodart, J.C., Paul, S.M., Holtzman, D.M. (2001) Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A., 98, 8850-8855.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8850-8855
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Dodart, J.C.4    Paul, S.M.5    Holtzman, D.M.6
  • 51
    • 0035875962 scopus 로고    scopus 로고
    • β-amyloid activates the mitogen-activated protein kinase cascade via hippocampal α-7 nicotinic acetylcholine receptors: In vitro and in vivo mechanisms related to Alzheimer's disease
    • Dineley, K.T., Westerman, M., Bui, D., Bell, K., Ashe, K.H., Sweatt, J.D. (2001) β-amyloid activates the mitogen-activated protein kinase cascade via hippocampal α-7 nicotinic acetylcholine receptors: In vitro and in vivo mechanisms related to Alzheimer's disease. J. Neurosci., 21, 4125-4133.
    • (2001) J. Neurosci. , vol.21 , pp. 4125-4133
    • Dineley, K.T.1    Westerman, M.2    Bui, D.3    Bell, K.4    Ashe, K.H.5    Sweatt, J.D.6
  • 52
    • 0033067110 scopus 로고    scopus 로고
    • Inhibitory effects of indomethacin on interleukin-1 and nitric oxide production in rat microglia in vitro
    • Du, Z.Y., Li, X.Y. (1999) Inhibitory effects of indomethacin on interleukin-1 and nitric oxide production in rat microglia in vitro. Int. J. Immunopharmacol., 21, 219-225.
    • (1999) Int. J. Immunopharmacol. , vol.21 , pp. 219-225
    • Du, Z.Y.1    Li, X.Y.2
  • 53
    • 0036530261 scopus 로고    scopus 로고
    • Molecular bases of long-term memories: A question of persistence
    • Dudai, Y. (2002) Molecular bases of long-term memories: a question of persistence. Curr. Opin. Neurobiol., 12, 211-216.
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 211-216
    • Dudai, Y.1
  • 54
    • 8444233219 scopus 로고    scopus 로고
    • Altered mitogen-activated protein kinase signaling, tau hyperphosphorylation and mild spatial learning dysfunction in transgenic rats expressing the β-amyloid peptide intracellularly in hippocampal and cortical neurons
    • Echeverria, V., Ducatenzeiler, A., Dowd, E., Jaén, J., Grant, S.M., ZIF, M., Wandosell, F., Avila, J., Grimm, H., Dunnett, S.B., Hartmann, T., Alhonen, L., Cuello, A.C. (2004) Altered mitogen-activated protein kinase signaling, tau hyperphosphorylation and mild spatial learning dysfunction in transgenic rats expressing the β-amyloid peptide intracellularly in hippocampal and cortical neurons. Neuroscience, 129, 583-592.
    • (2004) Neuroscience , vol.129 , pp. 583-592
    • Echeverria, V.1    Ducatenzeiler, A.2    Dowd, E.3    Jaén, J.4    Grant, S.M.5    Zif, M.6    Wandosell, F.7    Avila, J.8    Grimm, H.9    Dunnett, S.B.10    Hartmann, T.11    Alhonen, L.12    Cuello, A.C.13
  • 55
    • 0033569760 scopus 로고    scopus 로고
    • Activation of the L voltage-sensitive calcium channel by mitogen-activated protein (MAP) kinase following exposure of neuronal cells to β-amyloid. MAP kinase mediates β-amyloid-induced neurodegeneration
    • Ekinci, F.J., Malik, K.U., Shea, T.B. (1999) Activation of the L voltage-sensitive calcium channel by mitogen-activated protein (MAP) kinase following exposure of neuronal cells to β-amyloid. MAP kinase mediates β-amyloid-induced neurodegeneration. J. Biol. Chem., 274, 30322-30327.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30322-30327
    • Ekinci, F.J.1    Malik, K.U.2    Shea, T.B.3
  • 56
    • 0028662013 scopus 로고
    • Molecular mechanisms of memory and the pathophysiology of Alzheimer's disease
    • Etcheberrigaray, E., Gibson, G.E., Alkon, D.L. (1994) Molecular mechanisms of memory and the pathophysiology of Alzheimer's disease. Ann. N. Y. Acad. Sci., 747, 245-255.
    • (1994) Ann. N. Y. Acad. Sci. , vol.747 , pp. 245-255
    • Etcheberrigaray, E.1    Gibson, G.E.2    Alkon, D.L.3
  • 58
    • 0032459161 scopus 로고    scopus 로고
    • Benzodiazepines may have protective effects against Alzheimer disease
    • Fastbom, J., Forsell, Y., Winblad, B. (1998). Benzodiazepines may have protective effects against Alzheimer disease. Alzheimer Dis. Assoc. Disord., 12, 14-17.
    • (1998) Alzheimer Dis. Assoc. Disord. , vol.12 , pp. 14-17
    • Fastbom, J.1    Forsell, Y.2    Winblad, B.3
  • 59
    • 0035399822 scopus 로고    scopus 로고
    • Age-related impairment of synaptic transmission but normal long-term potentiation in transgenic mice that overexpress the human APP695SWE mutant form of amyloid precursor protein
    • Fitzjohn, S.M., Morton, R.A., Kuenzi, F., Rosahl, T.W., Shearman, M., Lewis, H., Smith, D., Reynolds, D.S., Davies, C.H., Collingridge, G.L., Seabrook, G.R. (2001) Age-related impairment of synaptic transmission but normal long-term potentiation in transgenic mice that overexpress the human APP695SWE mutant form of amyloid precursor protein. J. Neurosci., 21, 4691-4698.
    • (2001) J. Neurosci. , vol.21 , pp. 4691-4698
    • Fitzjohn, S.M.1    Morton, R.A.2    Kuenzi, F.3    Rosahl, T.W.4    Shearman, M.5    Lewis, H.6    Smith, D.7    Reynolds, D.S.8    Davies, C.H.9    Collingridge, G.L.10    Seabrook, G.R.11
  • 62
    • 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., Sub, Y.H., Chong, Y.H., Djamgoz, M.B. (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    Sub, Y.H.2    Chong, Y.H.3    Djamgoz, M.B.4
  • 63
    • 0031014448 scopus 로고    scopus 로고
    • Ionic effects of the Alzheimer's disease β-amyloid precursor protein and its metabolic fragments
    • Fraser, S.P., Suh, Y.H., Djamgoz, M.B. (1997) Ionic effects of the Alzheimer's disease β-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.B.3
  • 64
    • 0035128734 scopus 로고    scopus 로고
    • Blockade of long-term potentiation by β-amyloid peptides in the CA1 region of the rat hippocampus in vivo
    • Freir, D.B., Holscher, C., Herron, C.E. (2001) Blockade of long-term potentiation by β-amyloid peptides in the CA1 region of the rat hippocampus in vivo. J. Neurophysiol., 85, 708-713.
    • (2001) J. Neurophysiol. , vol.85 , pp. 708-713
    • Freir, D.B.1    Holscher, C.2    Herron, C.E.3
  • 65
    • 0031773366 scopus 로고    scopus 로고
    • Catecholamines potentiate amyloid β-peptide neurotoxicity: Involvement of oxidative stress, mitochondrial dysfunction, and perturbed calcium homeostasis
    • Fu, W., Luo, H., Parthasarathy, S., Mattson, M.P. (1998) Catecholamines potentiate amyloid β-peptide neurotoxicity: involvement of oxidative stress, mitochondrial dysfunction, and perturbed calcium homeostasis. Neurobiol. Dis., 5, 229-243.
    • (1998) Neurobiol. Dis. , vol.5 , pp. 229-243
    • Fu, W.1    Luo, H.2    Parthasarathy, S.3    Mattson, M.P.4
  • 66
    • 0034623106 scopus 로고    scopus 로고
    • In vivo synaptic transmission in young and aged amyloid precursor protein transgenic mice
    • Giacchino, J., Criado, J.R., Games, D., Henriksen, S. (2000) In vivo synaptic transmission in young and aged amyloid precursor protein transgenic mice. Brain Res., 876, 185-190.
    • (2000) Brain Res. , vol.876 , pp. 185-190
    • Giacchino, J.1    Criado, J.R.2    Games, D.3    Henriksen, S.4
  • 67
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner, G.G., Wong C.W. (1984) Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun., 122, 1131-1135.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 68
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber, D., Lerman, M.I., McBridge, O.W., Saffiotti, V., Gadusek, D.C. (1987) Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science, 235, 877-880.
    • (1987) Science , vol.235 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBridge, O.W.3    Saffiotti, V.4    Gadusek, D.C.5
  • 70
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric A ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong, Y., Chang, L., Viola, K.L., Lacor, P.N., Lambert, M.P., Finch, C.E., Krafft, G.A., Klein, W.L. (2003) Alzheimer's disease-affected brain: presence of oligomeric A ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. U.S.A., 100, 10417-10422.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6    Krafft, G.A.7    Klein, W.L.8
  • 71
    • 0037440717 scopus 로고    scopus 로고
    • Amyloid β1-42 peptide alters the gating of human and mouse α-bungarotoxin-sensitive nicotinic receptors
    • Grassi, F., Palma, E., Tonini, R., Amici, M., Ballivet, M., Eusebi, F. (2003) Amyloid β1-42 peptide alters the gating of human and mouse α-bungarotoxin-sensitive nicotinic receptors. J. Physiol., 547, 147-157.
    • (2003) J. Physiol. , vol.547 , pp. 147-157
    • Grassi, F.1    Palma, E.2    Tonini, R.3    Amici, M.4    Ballivet, M.5    Eusebi, F.6
  • 72
    • 0037098737 scopus 로고    scopus 로고
    • 2+ channels in PC12 cells via increased amyloid β peptide formation and reactive oxygen species generation
    • 2+ channels in PC12 cells via increased amyloid β peptide formation and reactive oxygen species generation. J. Physiol., 541, 1013-1023.
    • (2002) J. Physiol. , vol.541 , pp. 1013-1023
    • Green, K.N.1    Boyle, J.P.2    Peers, C.3
  • 74
    • 0036200702 scopus 로고    scopus 로고
    • Insights into immediate-early gene function in hippocampal memory consolidation using antisense oligonucleotide and fluorescent imaging approaches
    • Guzowski, J.F., Lyford, G.L., Stevenson, G.D., Houston, F.P., McGaugh, J.L. (2002) Insights into immediate-early gene function in hippocampal memory consolidation using antisense oligonucleotide and fluorescent imaging approaches. Hippocampus, 12, 86-104.
    • (2002) Hippocampus , vol.12 , pp. 86-104
    • Guzowski, J.F.1    Lyford, G.L.2    Stevenson, G.D.3    Houston, F.P.4    McGaugh, J.L.5
  • 75
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy, J., Allsop, D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci., 12, 383-388.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 76
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J.D., Lansbury, P.T. Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem., 66, 385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 77
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley, D.M., Walsh, D.M., Ye, C.P., Diehl, T., Vasquez, S., Vassilev, P.M., Teplow, D.B., Selkoe, D.J. (1999) Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci., 19, 8876-8884.
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 78
    • 0042023711 scopus 로고    scopus 로고
    • Alzheimer disease in the US population: Prevalence estimates using the 2000 census
    • Hebert, L.E., Scherr, P.A., Bienias, J.L., Bennett, D.A., Evans, D.A. (2003) Alzheimer disease in the US population: prevalence estimates using the 2000 census. Arch. Neurol., 60, 1119-1122.
    • (2003) Arch. Neurol. , vol.60 , pp. 1119-1122
    • Hebert, L.E.1    Scherr, P.A.2    Bienias, J.L.3    Bennett, D.A.4    Evans, D.A.5
  • 80
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (-secretase) complexed with inhibitor
    • Hong, L., Koelsch, G., Lin, X., Wu, S., Terzyan, S., Ghosh, A.K., Zhang, X.C., Tang, J. (2000) Structure of the protease domain of memapsin 2 (-secretase) complexed with inhibitor. Science, 290, 150-153.
    • (2000) Science , vol.290 , pp. 150-153
    • Hong, L.1    Koelsch, G.2    Lin, X.3    Wu, S.4    Terzyan, S.5    Ghosh, A.K.6    Zhang, X.C.7    Tang, J.8
  • 84
    • 0027258525 scopus 로고
    • The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J.T., Berger, E.P., Lansbury, P.T. Jr. (1993) The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry, 32, 4693-7.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 85
    • 0034843660 scopus 로고    scopus 로고
    • Cellular mechanisms for amyloid β-protein activation of rat cholinergic basal forebrain neurons
    • Jhamandas, J.H., Cho, C., Jassar, B., Harris, K., MacTavish, D., Easaw, J. (2001) Cellular mechanisms for amyloid β-protein activation of rat cholinergic basal forebrain neurons. J. Neurophysiol., 86, 1312-1320.
    • (2001) J. Neurophysiol. , vol.86 , pp. 1312-1320
    • Jhamandas, J.H.1    Cho, C.2    Jassar, B.3    Harris, K.4    MacTavish, D.5    Easaw, J.6
  • 87
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: Current status
    • Kagan, B.L., Hirakura, Y., Azimov, R., Azimova, R., Lin, M.C. (2002) The channel hypothesis of Alzheimer's disease: current status. Peptides, 23, 1311-1315.
    • (2002) Peptides , vol.23 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.C.5
  • 88
    • 0034603512 scopus 로고    scopus 로고
    • The role of cerebral ischemia in Alzheimer's disease
    • Kalaria, R.N. (2000) The role of cerebral ischemia in Alzheimer's disease. Neurobiol. Aging, 21, 321-330.
    • (2000) Neurobiol. Aging , vol.21 , pp. 321-330
    • Kalaria, R.N.1
  • 90
    • 0345826094 scopus 로고    scopus 로고
    • BACE1 suppression by RNA interference in primary cortical neurons
    • Kao, S.C., Krichevsky, A.M., Kosik, K.S., Tsai, L.H. (2004) BACE1 suppression by RNA interference in primary cortical neurons. J. Biol. Chem., 279, 1942-9.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1942-1949
    • Kao, S.C.1    Krichevsky, A.M.2    Kosik, K.S.3    Tsai, L.H.4
  • 91
    • 0031969880 scopus 로고    scopus 로고
    • Amyloid β-peptide inhibits high-affinity choline uptake and acetylcholine release in rat hippocampal slices
    • Kar, S., Issa, A.M., Seto, D., Auld, D.S., Collier, B., Quirino, R.J., (1998) Amyloid β-peptide inhibits high-affinity choline uptake and acetylcholine release in rat hippocampal slices. J Neurochem., 70, 2179-2187.
    • (1998) J Neurochem. , vol.70 , pp. 2179-2187
    • Kar, S.1    Issa, A.M.2    Seto, D.3    Auld, D.S.4    Collier, B.5    Quirino, R.J.6
  • 92
    • 11344265672 scopus 로고    scopus 로고
    • Interactions between β-amyloid and central cholinergic neurons: Implications for Alzheimer's disease
    • Kar, S., Slowikowski, S.P., Westaway, D., Mount, H.T. (2004) Interactions between β-amyloid and central cholinergic neurons: implications for Alzheimer's disease. J. Psychiatry Neurosci., 29, 427-441.
    • (2004) J. Psychiatry Neurosci. , vol.29 , pp. 427-441
    • Kar, S.1    Slowikowski, S.P.2    Westaway, D.3    Mount, H.T.4
  • 93
    • 0030966536 scopus 로고    scopus 로고
    • 2+-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons
    • 2+-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons. Biophys. J., 73, 67-75.
    • (1997) Biophys. J. , vol.73 , pp. 67-75
    • Kawahara, M.1    Arispe, N.2    Kuroda, Y.3    Rojas, E.4
  • 94
    • 0030966546 scopus 로고    scopus 로고
    • Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid β-peptide: Role of the lipid peroxidation product 4-hydroxynonenal
    • Keller, J.N., Pang, Z., Geddes, J.W., Begley, J.G., Germeyer, A., Waeg, G., Mattson, M.P. (1997) Impairment of glucose and glutamate transport and induction of mitochondrial oxidative stress and dysfunction in synaptosomes by amyloid β-peptide: role of the lipid peroxidation product 4-hydroxynonenal. J. Neurochem., 69, 273-284.
    • (1997) J. Neurochem. , vol.69 , pp. 273-284
    • Keller, J.N.1    Pang, Z.2    Geddes, J.W.3    Begley, J.G.4    Germeyer, A.5    Waeg, G.6    Mattson, M.P.7
  • 95
    • 0033553326 scopus 로고    scopus 로고
    • Cation selective channels formed by a C-terminal fragment of β-amyloid precursor protein
    • Kim, H.J., Suh, Y.H., Lee, M.H., Ryu, P.D. (1999) Cation selective channels formed by a C-terminal fragment of β-amyloid precursor protein. Neuroreport, 10, 1427-1431.
    • (1999) Neuroreport , vol.10 , pp. 1427-1431
    • Kim, H.J.1    Suh, Y.H.2    Lee, M.H.3    Ryu, P.D.4
  • 96
    • 0035866076 scopus 로고    scopus 로고
    • Use-dependent effects of amyloidogenic fragments of β-amyloid precursor protein on synaptic plasticity in rat hippocampus in vivo
    • Kim, J.H., Anwyl, R., Suh, Y.H., Djamgoz, M.B., Rowan, M.J. (2001) Use-dependent effects of amyloidogenic fragments of β-amyloid precursor protein on synaptic plasticity in rat hippocampus in vivo. J. Neurosci., 21, 1327-1333.
    • (2001) J. Neurosci. , vol.21 , pp. 1327-1333
    • Kim, J.H.1    Anwyl, R.2    Suh, Y.H.3    Djamgoz, M.B.4    Rowan, M.J.5
  • 97
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation
    • Kirschner, D.A., Abraham, C., Selkoe, D.J. (1986) X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation. Proc. Natl. Acad. Sci. U.S.A., 83, 503-507.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 99
    • 0242424155 scopus 로고    scopus 로고
    • 1-42 into globular neurotoxins
    • 1-42 into globular neurotoxins. Biochemistry, 42, 12749-12760.
    • (2003) Biochemistry , vol.42 , pp. 12749-12760
    • Klein, W.L.1
  • 101
    • 19444371852 scopus 로고    scopus 로고
    • Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain
    • Kokubo, H., Kayed, R., Glabe, C.G., Saido, T.C., Iwata, N., Helms, J.B., Yamaguchi, H. (2005) Oligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain. Brain Res., 1045, 224-228.
    • (2005) Brain Res. , vol.1045 , pp. 224-228
    • Kokubo, H.1    Kayed, R.2    Glabe, C.G.3    Saido, T.C.4    Iwata, N.5    Helms, J.B.6    Yamaguchi, H.7
  • 102
    • 11844300395 scopus 로고    scopus 로고
    • Soluble Aβ oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain
    • Kokubo, H., Kayed, R., Glabe, C.G., Yamaguchi, H. (2005) Soluble Aβ oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain. Brain Res., 1031, 222-228.
    • (2005) Brain Res. , vol.1031 , pp. 222-228
    • Kokubo, H.1    Kayed, R.2    Glabe, C.G.3    Yamaguchi, H.4
  • 103
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
    • Kojro, E., Gimpl, G., Lammich, S., Marz, W., Fahrenholz, F. (2001) Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10. Proc. Natl. Acad. Sci. U.S.A., 98, 5815-5820.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 104
    • 0030920771 scopus 로고    scopus 로고
    • A kinase to remember: Dual roles for MAP kinase in long-term memory
    • Kornhauser, J.M., Greenberg, M.E. (1997) A kinase to remember: dual roles for MAP kinase in long-term memory. Neuron, 18, 839-842.
    • (1997) Neuron , vol.18 , pp. 839-842
    • Kornhauser, J.M.1    Greenberg, M.E.2
  • 105
    • 1842555337 scopus 로고    scopus 로고
    • Alzheimer's amyloid-β (A beta) is an essential synaptic protein, not neurotoxic junk
    • Koudinov, A.R., Berezov, T.T. (2004) Alzheimer's amyloid-β (A beta) is an essential synaptic protein, not neurotoxic junk. Acta Neurobiol. Exp., 64, 71-79.
    • (2004) Acta Neurobiol. Exp. , vol.64 , pp. 71-79
    • Koudinov, A.R.1    Berezov, T.T.2
  • 110
    • 0033523480 scopus 로고    scopus 로고
    • Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice
    • Larson, J., Lynch, G., Games, D., Seubert, P. (1999) Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice. Brain Res., 840, 23-35.
    • (1999) Brain Res. , vol.840 , pp. 23-35
    • Larson, J.1    Lynch, G.2    Games, D.3    Seubert, P.4
  • 112
    • 7444247272 scopus 로고    scopus 로고
    • Alzheimer's β-peptide oligomer formation at physiologic concentrations
    • LeVine, H. 3rd. (2004) Alzheimer's β-peptide oligomer formation at physiologic concentrations. Anal. Biochem., 335, 81-90.
    • (2004) Anal. Biochem. , vol.335 , pp. 81-90
    • LeVine III, H.1
  • 114
    • 0032704781 scopus 로고    scopus 로고
    • Suppression of an amyloid β peptide-mediated calcium channel response by a secreted beta-amyloid precursor protein
    • Li, W.Y., Butler, J.P., Hale, J.E., McClure, D.B., Little, S.P., Czilli, D.L., Simmons, L.K. (2000) Suppression of an amyloid β peptide-mediated calcium channel response by a secreted beta-amyloid precursor protein. Neuroscience, 95, 1-4.
    • (2000) Neuroscience , vol.95 , pp. 1-4
    • Li, W.Y.1    Butler, J.P.2    Hale, J.E.3    McClure, D.B.4    Little, S.P.5    Czilli, D.L.6    Simmons, L.K.7
  • 115
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin, H., Bhatia, R., Lal, R. (2001) Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J., 15, 2433-2444.
    • (2001) FASEB J. , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 117
    • 0028172886 scopus 로고
    • β-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo, A., Yankner, B.A. (1994) β-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. U.S.A., 91, 12243-12247.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 119
    • 0038360763 scopus 로고    scopus 로고
    • Degeneration of beta-amyloid-associated cholinergic structures in transgenic APP SW mice
    • Luth, H.J., Apelt, J., Ihunwo, A.O., Arendt, T., Schliebs, R. (2003) Degeneration of beta-amyloid-associated cholinergic structures in transgenic APP SW mice. Brain Res., 977, 16-22.
    • (2003) Brain Res. , vol.977 , pp. 16-22
    • Luth, H.J.1    Apelt, J.2    Ihunwo, A.O.3    Arendt, T.4    Schliebs, R.5
  • 121
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark, R.J., Pang, Z., Geddes, J.W., Uchida, K., Mattson, M.P. (1997) Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J. Neurosci., 17, 1046-1054.
    • (1997) J. Neurosci. , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 123
    • 0026032039 scopus 로고
    • Cortical and subcortical patterns of synaptophysin-like immunoreactivity in Alzheimer's disease
    • Masliah, E., Terry, R.D., Alford, M., De Teresa, R., Hansen, L.A. (1991) Cortical and subcortical patterns of synaptophysin-like immunoreactivity in Alzheimer's disease. Am. J. Pathol., 138, 235-246.
    • (1991) Am. J. Pathol. , vol.138 , pp. 235-246
    • Masliah, E.1    Terry, R.D.2    Alford, M.3    De Teresa, R.4    Hansen, L.A.5
  • 124
    • 0025600931 scopus 로고
    • Diffuse plaques do not accentuate synapse loss in Alzheimer's disease
    • Masliah, E., Terry, R.D., Mallory, M., Alford, M., Hansen, L.A. (1990) Diffuse plaques do not accentuate synapse loss in Alzheimer's disease. Am. J. Pathol., 137, 1293-1297.
    • (1990) Am. J. Pathol. , vol.137 , pp. 1293-1297
    • Masliah, E.1    Terry, R.D.2    Mallory, M.3    Alford, M.4    Hansen, L.A.5
  • 125
    • 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. (1985) 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. EMO J., 4, 2757-2763.
    • (1985) EMO J. , vol.4 , pp. 2757-2763
    • Masters, C.L.1    Multhaup, G.2    Simms, G.3    Pottgiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 126
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson, M.P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I., Rydel, R.E. (1992) β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci., 12, 376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 128
    • 1942455221 scopus 로고    scopus 로고
    • Effect of sterols on β-amyloid peptide (AβP1-40) channel formation and their properties in planar lipid membranes
    • Micelli, S., Meleleo, D., Picciarelli V., Gallucci, E. (2004) Effect of sterols on β-amyloid peptide (AβP1-40) channel formation and their properties in planar lipid membranes. Biophys. J., 86, 2231-2237.
    • (2004) Biophys. J. , vol.86 , pp. 2231-2237
    • Micelli, S.1    Meleleo, D.2    Picciarelli, V.3    Gallucci, E.4
  • 130
    • 4043052478 scopus 로고    scopus 로고
    • Preserved fronto-striatal plasticity and enhanced procedural learning in a transgenic mouse model of Alzheimer's disease overexpressing mutant hAPPswe
    • Middei, S., Geracitano, R., Caprioli, A., Mercuri, N., Ammassari-Teule, M. (2004) Preserved fronto-striatal plasticity and enhanced procedural learning in a transgenic mouse model of Alzheimer's disease overexpressing mutant hAPPswe. Learn. Mem., 11, 447-452.
    • (2004) Learn. Mem. , vol.11 , pp. 447-452
    • Middei, S.1    Geracitano, R.2    Caprioli, A.3    Mercuri, N.4    Ammassari-Teule, M.5
  • 134
    • 0036215321 scopus 로고    scopus 로고
    • β-amyloid peptide induces ultrastructural changes in synaptosomes and potentiates mitochondrial dysfunction in the presence of ryanodine
    • Mungarro-Menchaca, X., Ferrera, P., Morán, J., Arias, C. (2002) β-amyloid peptide induces ultrastructural changes in synaptosomes and potentiates mitochondrial dysfunction in the presence of ryanodine. J. Neurosci. Res., 68, 89-96.
    • (2002) J. Neurosci. Res. , vol.68 , pp. 89-96
    • Mungarro-Menchaca, X.1    Ferrera, P.2    Morán, J.3    Arias, C.4
  • 135
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline
    • Naslund, J., Haroutunian, V., Mohs, R., Davis, K.L., Davies, P., Greengard, P., Buxbaum, J.D. (2000) Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. JAAM, 283, 1571-1577.
    • (2000) JAAM , vol.283 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greengard, P.6    Buxbaum, J.D.7
  • 136
    • 0027209083 scopus 로고
    • Release of amyloid β-protein precursor derivatives by electrical depolarization of rat hippocampal slices
    • Nitsch, R.M., Farber, S.A., Growdon, J.H., Wurtman, R.J. (1993) Release of amyloid β-protein precursor derivatives by electrical depolarization of rat hippocampal slices. Proc. Natl. Acad. Sci. U.S.A., 90, 5191-5193.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5191-5193
    • Nitsch, R.M.1    Farber, S.A.2    Growdon, J.H.3    Wurtman, R.J.4
  • 137
    • 0032945724 scopus 로고    scopus 로고
    • Synaptic transmission and hippocampal long-term potentiation in transgenic mice expressing FAD-linked presenilin 1
    • Parent, A., Linden, D.J., Sisodia, S.S., Borchelt, D.R. (1999) Synaptic transmission and hippocampal long-term potentiation in transgenic mice expressing FAD-linked presenilin 1. Neurobiol. Dis., 6, 56-62.
    • (1999) Neurobiol. Dis. , vol.6 , pp. 56-62
    • Parent, A.1    Linden, D.J.2    Sisodia, S.S.3    Borchelt, D.R.4
  • 138
    • 0032502033 scopus 로고    scopus 로고
    • Alzheimer's amyloid precursor protein β-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: Similarities to the angiotensin converting enzyme secretase
    • Parvathy, S., Hussain, I., Karran, E.H., Turner, A.J., Hooper, N.M. (1998) Alzheimer's amyloid precursor protein β-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: similarities to the angiotensin converting enzyme secretase. Biochemistry, 37, 1680-1685.
    • (1998) Biochemistry , vol.37 , pp. 1680-1685
    • Parvathy, S.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 140
    • 0035005101 scopus 로고    scopus 로고
    • New protease inhibitors prevent γ-secretase-mediated production of Aβ40/42 without affecting Notch cleavage
    • Petit, A., Bihel, F., Alves, da Costa, C., Pourquie, O., Checler, F., Kraus, J.L. (2001) New protease inhibitors prevent γ-secretase-mediated production of Aβ40/42 without affecting Notch cleavage. Nat. Cell Biol., 3, 507-511.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 507-511
    • Petit, A.1    Bihel, F.2    da Costa Alves, C.3    Pourquie, O.4    Checler, F.5    Kraus, J.L.6
  • 141
    • 0035219699 scopus 로고    scopus 로고
    • β-Amyloid(1-42) peptide directly modulates nicotinic receptors in the rat hippocampal slice
    • Pettit, D.L., Shao, Z., Yakel, J.L. (2001) β-Amyloid(1-42) peptide directly modulates nicotinic receptors in the rat hippocampal slice. J. Neurosci., 21, RC120.
    • (2001) J. Neurosci. , vol.21
    • Pettit, D.L.1    Shao, Z.2    Yakel, J.L.3
  • 142
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike, C.J., Walencewicz, A.J., Glabe, C.G., Cotman, C.W. (1991) In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res., 563, 311-314.
    • (1991) Brain Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 143
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C.J., Burdick, D., Walencewicz, A.J., Glabe, C.G., Cotman, C.W. (1993) Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci., 13, 1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 145
    • 0031921466 scopus 로고    scopus 로고
    • Mutant genes in familial Alzheimer's disease and transgenic models
    • Price, D.L., Sisodia, S.S. (1998) Mutant genes in familial Alzheimer's disease and transgenic models. Annu. Rev. Neurosci., 21, 479-505.
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.S.2
  • 146
    • 11444251445 scopus 로고    scopus 로고
    • Apolipoprotein E, cholesterol transport and synthesis in sporadic Alzheimer's disease
    • Poirier, J. (2005) Apolipoprotein E, cholesterol transport and synthesis in sporadic Alzheimer's disease. Neurobiol. Aging, 26, 355-361.
    • (2005) Neurobiol. Aging , vol.26 , pp. 355-361
    • Poirier, J.1
  • 147
    • 22544485048 scopus 로고    scopus 로고
    • Amyloid-β peptide inhibits activation of the nitric oxide/cGMP/ cAMP-responsive element-binding protein pathway during hippocampal synaptic plasticity
    • Puzzo, D., Vitolo, O., Trinchese, F., Jacob, J.P., Palmeri, A., Arancio, O. (2005) Amyloid-β peptide inhibits activation of the nitric oxide/ cGMP/cAMP-responsive element-binding protein pathway during hippocampal synaptic plasticity. J. Neurosci., 25, 6887-6897.
    • (2005) J. Neurosci. , vol.25 , pp. 6887-6897
    • Puzzo, D.1    Vitolo, O.2    Trinchese, F.3    Jacob, J.P.4    Palmeri, A.5    Arancio, O.6
  • 148
    • 9644294519 scopus 로고    scopus 로고
    • Pacemaker neurons and neuronal networks: An integrative view
    • Ramirez, J.M., Tryba, A.K., Pena, F. (2004) Pacemaker neurons and neuronal networks: an integrative view. Curr. Opin. Neurobiol., 14, 665-674.
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 665-674
    • Ramirez, J.M.1    Tryba, A.K.2    Pena, F.3
  • 149
    • 0037195424 scopus 로고    scopus 로고
    • 2+ channel currents in primary cultures of rat cortical neurones by amyloid β protein (1-40) is dependent on solubility status
    • 2+ channel currents in primary cultures of rat cortical neurones by amyloid β protein (1-40) is dependent on solubility status. Brain Res., 956, 254-261.
    • (2002) Brain Res. , vol.956 , pp. 254-261
    • Ramsden, M.1    Henderson, Z.2    Pearson, H.A.3
  • 151
    • 0037432559 scopus 로고    scopus 로고
    • NMDA receptor regulation by amyloid-β does not account for its inhibition of LTP in rat hippocampus
    • Raymond, C.R., Ireland, D.R., Abraham, W.C. (2003) NMDA receptor regulation by amyloid-β does not account for its inhibition of LTP in rat hippocampus. Brain Res., 968, 263-272.
    • (2003) Brain Res. , vol.968 , pp. 263-272
    • Raymond, C.R.1    Ireland, D.R.2    Abraham, W.C.3
  • 152
    • 0042266332 scopus 로고    scopus 로고
    • Electrophysiological studies on the hippocampus and prefrontal cortex assessing the effects of amyloidosis in amyloid precursor protein 23 transgenic mice
    • Roder, S., Danober, L., Pozza, M.F., Lingenhoehl, K., Wiederhold, K.H., Olpe, H.R. (2003) Electrophysiological studies on the hippocampus and prefrontal cortex assessing the effects of amyloidosis in amyloid precursor protein 23 transgenic mice. Neuroscience, 120, 705-720.
    • (2003) Neuroscience , vol.120 , pp. 705-720
    • Roder, S.1    Danober, L.2    Pozza, M.F.3    Lingenhoehl, K.4    Wiederhold, K.H.5    Olpe, H.R.6
  • 154
    • 0035984337 scopus 로고    scopus 로고
    • Aβ(25-35) and Aβ(1-40) act on different calcium channels in CA1 hippocampal neurons
    • Rovira, C., Arbez, N., Mariani, J. (2002) Aβ(25-35) and Aβ(1-40) act on different calcium channels in CA1 hippocampal neurons. Biochem. Biophys. Res. Commun., 296, 1317-1321.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 1317-1321
    • Rovira, C.1    Arbez, N.2    Mariani, J.3
  • 155
    • 0034648038 scopus 로고    scopus 로고
    • SB203580, the p38 mitogen-activated protein kinase inhibitor blocks the inhibitory effect of β-amyloid on long-term potentiation in the rat hippocampus
    • Saleshando, G., O'Connor, J.J. (2000) SB203580, the p38 mitogen-activated protein kinase inhibitor blocks the inhibitory effect of β-amyloid on long-term potentiation in the rat hippocampus. Neurosci. Lett., 288, 119-122.
    • (2000) Neurosci. Lett. , vol.288 , pp. 119-122
    • Saleshando, G.1    O'Connor, J.J.2
  • 157
    • 11244317067 scopus 로고    scopus 로고
    • Alzheimer's amyloid peptides mediate hypoxic up-regulation of L-type Ca2+ channels
    • Scragg, J.L., Fearon, I.M., Boyle, J.P., Ball, S.G., Varadi, G., Peers, C. (2005) Alzheimer's amyloid peptides mediate hypoxic up-regulation of L-type Ca2+ channels. FASEB J., 19, 150-152.
    • (2005) FASEB J. , vol.19 , pp. 150-152
    • Scragg, J.L.1    Fearon, I.M.2    Boyle, J.P.3    Ball, S.G.4    Varadi, G.5    Peers, C.6
  • 158
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe, D.J. (1991) The molecular pathology of Alzheimer's disease. Neuron, 6, 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 159
    • 0142021035 scopus 로고    scopus 로고
    • Aging, Amyloid, and Alzheimer's Disease: A Perspective in Honor of Carl Cotman
    • Selkoe, D.J. (2003) Aging, Amyloid, and Alzheimer's Disease: A Perspective in Honor of Carl Cotman. Neurochem. Res., 28, 1705-1713.
    • (2003) Neurochem. Res. , vol.28 , pp. 1705-1713
    • Selkoe, D.J.1
  • 160
    • 0034716942 scopus 로고    scopus 로고
    • Direct visualisation of the β-sheet structure of synthetic Alzheimer's amyloid
    • Serpell, L.C., Smith, J.M. (2000) Direct visualisation of the β-sheet structure of synthetic Alzheimer's amyloid. J. Mol. Biol., 299, 225-231.
    • (2000) J. Mol. Biol. , vol.299 , pp. 225-231
    • Serpell, L.C.1    Smith, J.M.2
  • 162
    • 0033528286 scopus 로고    scopus 로고
    • Activation of microglial cells by PrP and β-amyloid fragments raises intracellular calcium through L-type voltage sensitive calcium channels
    • Silei, V., Fabrizi, C., Venturini, G., Salmona, M., Bugiani, O., Tagliavini, F., Lauro, G.M. (1999) Activation of microglial cells by PrP and β-amyloid fragments raises intracellular calcium through L-type voltage sensitive calcium channels. Brain Res., 818, 168-170.
    • (1999) Brain Res. , vol.818 , pp. 168-170
    • Silei, V.1    Fabrizi, C.2    Venturini, G.3    Salmona, M.4    Bugiani, O.5    Tagliavini, F.6    Lauro, G.M.7
  • 163
    • 0035433962 scopus 로고    scopus 로고
    • Alzheimer's disease and Aβ toxicity: From top to bottom
    • Small, D.H., Mok, S.S., Bornstein, J.C. (2001) Alzheimer's disease and Aβ toxicity: From top to bottom. Nat. Rev. Neurosci., 2, 595-598.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 595-598
    • Small, D.H.1    Mok, S.S.2    Bornstein, J.C.3
  • 165
    • 23444448170 scopus 로고    scopus 로고
    • Dendritic spine abnormalities in amyloid precursor protein transgenic mice demonstrated by gene transfer and intravital multiphoton microscopy
    • Spires T.L., Meyer-Luehmann M., Stern E.A., McLean P.J., Skoch J., Nguyen P.T., Bacskai B.J., Hyman B.T. (2005) Dendritic spine abnormalities in amyloid precursor protein transgenic mice demonstrated by gene transfer and intravital multiphoton microscopy. J. Neurosci., 25, 7278-7287.
    • (2005) J. Neurosci. , vol.25 , pp. 7278-7287
    • Spires, T.L.1    Meyer-Luehmann, M.2    Stern, E.A.3    McLean, P.J.4    Skoch, J.5    Nguyen, P.T.6    Bacskai, B.J.7    Hyman, B.T.8
  • 166
    • 0035425615 scopus 로고    scopus 로고
    • Generation of aggregated β-amyloid in the rat hippocampus impairs synaptic transmission and plasticity and causes memory deficits
    • Stephan, A., Laroche, S., Davis, S. (2001) Generation of aggregated β-amyloid in the rat hippocampus impairs synaptic transmission and plasticity and causes memory deficits. J. Neurosci., 21, 5703-5714.
    • (2001) J. Neurosci. , vol.21 , pp. 5703-5714
    • Stephan, A.1    Laroche, S.2    Davis, S.3
  • 168
    • 0036082750 scopus 로고    scopus 로고
    • Impairment of hippocampal CA1 heterosynaptic transformation and spatial memory by β-amyloid(25-35)
    • Sun, M.K., Alkon, D.L. (2002) Impairment of hippocampal CA1 heterosynaptic transformation and spatial memory by β-amyloid(25-35). J. Neurophysiol., 87, 2441-2449.
    • (2002) J. Neurophysiol. , vol.87 , pp. 2441-2449
    • Sun, M.K.1    Alkon, D.L.2
  • 169
    • 0035166616 scopus 로고    scopus 로고
    • The neuronal MAP kinase cascade: A biochemical signal integration system subserving synaptic plasticity and memory
    • Sweatt, J.D. (2001) The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory. J. Neurochem., 6, 1-10.
    • (2001) J. Neurochem. , vol.6 , pp. 1-10
    • Sweatt, J.D.1
  • 170
    • 0030872413 scopus 로고    scopus 로고
    • Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease
    • Sze, C.I., Troncoso, J.C., Kawas, C., Mouton, P., Price, D.L., Martin, L.J. (1997) Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease. J. Neuropathol. Exp. Neurol., 56, 933-944.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 933-944
    • Sze, C.I.1    Troncoso, J.C.2    Kawas, C.3    Mouton, P.4    Price, D.L.5    Martin, L.J.6
  • 171
    • 27744527103 scopus 로고    scopus 로고
    • Divergent effects of Aβ1-42 on ionotropic glutamate receptor-mediated responses in CA1 neurons in vivo
    • Szegedi, V., Juhasz, G., Budai, D., Penke, B. (2005) Divergent effects of Aβ1-42 on ionotropic glutamate receptor-mediated responses in CA1 neurons in vivo. Brain Res., 1062, 120-126.
    • (2005) Brain Res. , vol.1062 , pp. 120-126
    • Szegedi, V.1    Juhasz, G.2    Budai, D.3    Penke, B.4
  • 172
    • 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. (1988) Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease. Nature, 331, 528-530.
    • (1988) Nature , vol.331 , pp. 528-530
    • Tanzi, R.E.1    McClatchey, A.I.2    Lamperti, E.D.3    Villa-Komaroff, L.4    Gusella, J.F.5    Neve, R.L.6
  • 174
    • 0029795197 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimer disease: An alternative to the amyloid hypothesis
    • Terry, R.D. (1996) The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis. J. Neuropathol. Exp. Neurol., 55, 1023-1025.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 1023-1025
    • Terry, R.D.1
  • 175
    • 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., Butters, N., DeTeresa, R., Hill, R., Hansen, L.A., Katzman, R. (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol., 30, 572-580.
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 176
    • 0034681159 scopus 로고    scopus 로고
    • Theta oscillations index human hippocampal activation during a working memory task
    • Tesche, C.D., Karhu, J. (2000) Theta oscillations index human hippocampal activation during a working memory task. Proc. Natl. Acad. Sci. U.S.A., 97, 919-924.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 919-924
    • Tesche, C.D.1    Karhu, J.2
  • 177
    • 0035907325 scopus 로고    scopus 로고
    • 1-42 impairs activity-dependent cAMP-response element-binding protein signaling in neurons at concentrations in which cell survival is not compromised
    • 1-42 impairs activity-dependent cAMP-response element-binding protein signaling in neurons at concentrations in which cell survival is not compromised. J. Biol. Chem., 276, 17301-17306.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17301-17306
    • Tong, L.1    Thornton, P.L.2    Balazs, R.3    Cotman, C.W.4
  • 178
    • 7044220336 scopus 로고    scopus 로고
    • Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches
    • Tsai, J., Grutzendler, J., Duff, K., Gan, W.B. (2004) Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches. Nat. Neurosci., 7, 1181-1183.
    • (2004) Nat. Neurosci. , vol.7 , pp. 1181-1183
    • Tsai, J.1    Grutzendler, J.2    Duff, K.3    Gan, W.B.4
  • 179
    • 0031035954 scopus 로고    scopus 로고
    • Amyloid β protein potentiates Ca2+ influx through L-type voltage-sensitive Ca2+ channels: A possible involvement of free radicals
    • Ueda, K., Shinohara, S., Yagami, T., Asakura, K., Kawasaki, K. (1997) Amyloid β protein potentiates Ca2+ influx through L-type voltage-sensitive Ca2+ channels: a possible involvement of free radicals. J. Neurochem., 68, 265-271.
    • (1997) J. Neurochem. , vol.68 , pp. 265-271
    • Ueda, K.1    Shinohara, S.2    Yagami, T.3    Asakura, K.4    Kawasaki, K.5
  • 181
    • 0027379395 scopus 로고
    • Characterization of b-amyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey, C., Lee, D., Keim, P., Leiberburg, I., Schenk, D.B. (1993) Characterization of b-amyloid peptide from human cerebrospinal fluid. J. Neurochem., 61, 1965-1968.
    • (1993) J. Neurochem. , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Leiberburg, I.4    Schenk, D.B.5
  • 182
    • 0036792096 scopus 로고    scopus 로고
    • Amyloid β-peptide inhibition of the PKA/CREB pathway and long-term potentiation: Reversibility by drugs that enhance cAMP signaling
    • Vitolo, O.V., Sant'Angelo, A., Costanzo, V., Battaglia, F., Arancio, O., Shelanski, M. (2002) Amyloid β-peptide inhibition of the PKA/CREB pathway and long-term potentiation: reversibility by drugs that enhance cAMP signaling. Proc. Natl. Acad. Sci. U.S.A., 99, 13217-13221.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13217-13221
    • Vitolo, O.V.1    Sant'Angelo, A.2    Costanzo, V.3    Battaglia, F.4    Arancio, O.5    Shelanski, M.6
  • 184
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D.M., Klyubin, I., Fadeeva, J.V., Cullen, W.K., Anwyl, R., Wolfe, M.S., Rowan, M.J., Selkoe, D.J. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature, 416, 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 185
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh, D.M., Selkoe, D.J. (2004) Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron, 44, 181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 186
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation
    • Walsh, D.M., Townsend, M., Podlisny, M.B., Shankar, G.M., Fadeeva, J.V., Agnaf, O.E., Hartley, D.M., Selkoe, D.J. (2005) Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation. J. Neurosci., 25, 2455-2462.
    • (2005) J. Neurosci. , vol.25 , pp. 2455-2462
    • Walsh, D.M.1    Townsend, M.2    Podlisny, M.B.3    Shankar, G.M.4    Fadeeva, J.V.5    Agnaf, O.E.6    Hartley, D.M.7    Selkoe, D.J.8
  • 188
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid β-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang, Q., Walsh, D.M., Rowan, M.J., Selkoe, D.J., Anwyl, R. (2004) Block of long-term potentiation by naturally secreted and synthetic amyloid β-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J. Neurosci., 24, 3370-3378.
    • (2004) J. Neurosci. , vol.24 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 189
    • 26944437967 scopus 로고    scopus 로고
    • Small nonfibrillar assemblies of amyloid β-protein bearing the Arctic mutation induce rapid neuritic degeneration
    • Whalen, B.M., Selkoe, D.J., Hartley, D.M. (2005) Small nonfibrillar assemblies of amyloid β-protein bearing the Arctic mutation induce rapid neuritic degeneration. Neurobiol. Dis., 20, 254-266.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 254-266
    • Whalen, B.M.1    Selkoe, D.J.2    Hartley, D.M.3
  • 191
    • 0031470904 scopus 로고    scopus 로고
    • SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling
    • Wen, C., Metzstein, M.M., Greenwald, I. (1997) SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling. Development, 124, 4759-4767.
    • (1997) Development , vol.124 , pp. 4759-4767
    • Wen, C.1    Metzstein, M.M.2    Greenwald, I.3
  • 192
    • 0032983786 scopus 로고    scopus 로고
    • Memantine in severe dementia: Results of the 9M-Best Study (Benefit and efficacy in severely demented patients during treatment with memantine)
    • Winblad, B., Poritis, N. (1999) Memantine in severe dementia: results of the 9M-Best Study (Benefit and efficacy in severely demented patients during treatment with memantine). Int. J. Geriatr. Psychiatry, 14, 135-146.
    • (1999) Int. J. Geriatr. Psychiatry , vol.14 , pp. 135-146
    • Winblad, B.1    Poritis, N.2
  • 194
    • 0029417021 scopus 로고
    • β-Amyloid selectively augments NMDA receptor-mediated synaptic transmission in rat hippocampus
    • Wu, J., Anwyl, R., Rowan, M.J. (1995a) β-Amyloid selectively augments NMDA receptor-mediated synaptic transmission in rat hippocampus. Neuroreport, 6, 2409-2413.
    • (1995) Neuroreport , vol.6 , pp. 2409-2413
    • Wu, J.1    Anwyl, R.2    Rowan, M.J.3
  • 195
    • 0029652085 scopus 로고
    • β-Amyloid-(1-40) increases long-term potentiation in rat hippocampus in vitro
    • Wu, J., Anwyl, R., Rowan, M.J. (1995b) β-Amyloid-(1-40) increases long-term potentiation in rat hippocampus in vitro. Eur. J. Pharmacol., 284, R1-3.
    • (1995) Eur. J. Pharmacol. , vol.284
    • Wu, J.1    Anwyl, R.2    Rowan, M.J.3
  • 197
    • 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
  • 198
    • 0037343844 scopus 로고    scopus 로고
    • Defects in expression of genes related to synaptic vesicle trafficking in frontal cortex of Alzheimer's disease
    • Yao, P.J., Zhu, M., Pyun, E.I., Brooks, A.I., Therianos, S., Meyers, V.E., Coleman, P.D. (2003) Defects in expression of genes related to synaptic vesicle trafficking in frontal cortex of Alzheimer's disease. Neurobiol. Dis., 12, 97-109.
    • (2003) Neurobiol. Dis. , vol.12 , pp. 97-109
    • Yao, P.J.1    Zhu, M.2    Pyun, E.I.3    Brooks, A.I.4    Therianos, S.5    Meyers, V.E.6    Coleman, P.D.7
  • 199
    • 0042405095 scopus 로고    scopus 로고
    • Protofibrils of amyloid β-protein inhibit specific K+ currents in neocortical cultures
    • Ye, C.P., Selkoe, D.J., Hartley, D.M. (2003) Protofibrils of amyloid β-protein inhibit specific K+ currents in neocortical cultures. Neurobiol. Dis., 13, 177-190.
    • (2003) Neurobiol. Dis. , vol.13 , pp. 177-190
    • Ye, C.P.1    Selkoe, D.J.2    Hartley, D.M.3
  • 200
    • 0032754141 scopus 로고    scopus 로고
    • Suppressive action produced by β-amyloid peptide fragment 31-35 on long-term potentiation in rat hippocampus is N-methyl-D-aspartate receptor-independent: It's offset by (-)huperzine A
    • Ye, L., Qiao, J.T. (1999) Suppressive action produced by β-amyloid peptide fragment 31-35 on long-term potentiation in rat hippocampus is N-methyl-D-aspartate receptor-independent: it's offset by (-)huperzine A. Neurosci. Lett., 275, 187-190.
    • (1999) Neurosci. Lett. , vol.275 , pp. 187-190
    • Ye, L.1    Qiao, J.T.2
  • 201
    • 3543060658 scopus 로고    scopus 로고
    • Amyloid β-protein induced electrophysiological changes are dependent on aggregation state: N-methyl-D-aspartate (NMDA) versus non-NMDA receptor/channel activation
    • Ye, C., Walsh, D.M., Selkoe, D.J., Hartley, D.M. (2004) Amyloid β-protein induced electrophysiological changes are dependent on aggregation state: N-methyl-D-aspartate (NMDA) versus non-NMDA receptor/ channel activation. Neurosci. Lett., 366, 320-325.
    • (2004) Neurosci. Lett. , vol.366 , pp. 320-325
    • Ye, C.1    Walsh, D.M.2    Selkoe, D.J.3    Hartley, D.M.4
  • 203
    • 0004491134 scopus 로고    scopus 로고
    • Enhancement of outward potassium current may participate in β-amyloid peptide-induced cortical neuronal death
    • Yu, S.P., Farhangrazi, Z.S., Ying, H.S., Yeh, C.H., Choi, D.W. (1998) Enhancement of outward potassium current may participate in β-amyloid peptide-induced cortical neuronal death. Neurobiol. Dis., 5, 81-88.
    • (1998) Neurobiol. Dis. , vol.5 , pp. 81-88
    • Yu, S.P.1    Farhangrazi, Z.S.2    Ying, H.S.3    Yeh, C.H.4    Choi, D.W.5
  • 205
    • 0442293848 scopus 로고    scopus 로고
    • Effects of presenilins and β-amyloid precursor protein on delayed rectifier potassium channels in cultured rat hippocampal neurons
    • Zhang, W., Jin, H.W., Wang, X.L. (2004) Effects of presenilins and β-amyloid precursor protein on delayed rectifier potassium channels in cultured rat hippocampal neurons. Acta Pharmacol. Sin., 25, 181-185.
    • (2004) Acta Pharmacol. Sin. , vol.25 , pp. 181-185
    • Zhang, W.1    Jin, H.W.2    Wang, X.L.3


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