메뉴 건너뛰기




Volumn 3, Issue 3, 2006, Pages 179-183

Fibrillar β-amyloid impairs the late phase of long term potentiation

Author keywords

Alzheimer's disease; Amyloid; Fibrils; Synapse; Synaptic plasticity

Indexed keywords

AMYLOID BETA PROTEIN; OLIGOMER;

EID: 33745613783     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/156720506777632871     Document Type: Article
Times cited : (21)

References (57)
  • 1
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the beta-amyloid precursor protein
    • Selkoe DJ. Normal and abnormal biology of the beta-amyloid precursor protein. Annu Rev Neurosci 17: 489-517 (1994).
    • (1994) Annu Rev Neurosci , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 2
    • 0028898888 scopus 로고
    • Mechanisms of synaptic dysfunction in Alzheimer's disease
    • Masliah E. Mechanisms of synaptic dysfunction in Alzheimer's disease. Histol Histopathol 10: 509-519 (1995).
    • (1995) Histol Histopathol , vol.10 , pp. 509-519
    • Masliah, E.1
  • 3
    • 0030809128 scopus 로고    scopus 로고
    • Block of LTP in rat hippocampus in vivo by beta-amyloid precursor protein fragments
    • Cullen W K, Suh YH, Anwyl R and Rowan MJ. Block of LTP in rat hippocampus in vivo by beta-amyloid precursor protein fragments. Neuroreport 8: 3213-3217 (1997).
    • (1997) Neuroreport , vol.8 , pp. 3213-3217
    • Cullen, W.K.1    Suh, Y.H.2    Anwyl, R.3    Rowan, M.J.4
  • 4
    • 0032754051 scopus 로고    scopus 로고
    • Impairments of long-term potentiation in hippocampal slices of beta-amyloid-infused rats
    • Itoh A, Akaike T, Sokabe M, Nitta A, Iida R, Olariu A, et al. Impairments of long-term potentiation in hippocampal slices of beta-amyloid-infused rats. Eur J Pharmacol 382: 167-175 (1999).
    • (1999) Eur J Pharmacol , vol.382 , pp. 167-175
    • Itoh, A.1    Akaike, T.2    Sokabe, M.3    Nitta, A.4    Iida, R.5    Olariu, A.6
  • 5
    • 0036792096 scopus 로고    scopus 로고
    • Amyloid beta -peptide inhibition of the PKA/CREB pathway and long-term potentiation: Reversibility by drugs that enhance cAMP signaling
    • USA
    • Vitolo OV, Sant'Angelo A, Costanzo V, Battaglia F, Arancio O and Shelanski M. Amyloid beta -peptide inhibition of the PKA/CREB pathway and long-term potentiation: reversibility by drugs that enhance cAMP signaling. Proc Natl Acad Sci USA 99: 13217-21 (2002).
    • (2002) Proc Natl Acad Sci , 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
  • 6
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535-539 (2002).
    • (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
  • 7
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly JW. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 8: 101-106 (1998).
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 8
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson CM. The structural basis of protein folding and its links with human disease. Philos Trans R Soc Lond B Biol Sci 356: 133-145 (2001).
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 9
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • USA
    • Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 95: 6448-6453 (1998).
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 10
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, et al. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 19: 8876-8884 (1999).
    • (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
  • 11
    • 0032845739 scopus 로고    scopus 로고
    • The nonfibrillar amyloid beta-peptide induces apoptotic neuronal cell death: Involvement of its C-terminal fusogenic domain
    • Pillot T, Drouet B, Queille S, Labeur C, Vandekerchkhove J, Rosseneu M, et al. The nonfibrillar amyloid beta-peptide induces apoptotic neuronal cell death: involvement of its C-terminal fusogenic domain. J Neurochem 73: 1626-1634 (1999).
    • (1999) J Neurochem , vol.73 , pp. 1626-1634
    • Pillot, T.1    Drouet, B.2    Queille, S.3    Labeur, C.4    Vandekerchkhove, J.5    Rosseneu, M.6
  • 12
    • 0033986987 scopus 로고    scopus 로고
    • Inhibition of A beta fibril formation and A beta-induced cytotoxicity by senile plaque-associated proteins
    • Monji A, Yoshida I, Tashiro K, Hayashi Y, Matsuda K and Tashiro N. Inhibition of A beta fibril formation and A beta-induced cytotoxicity by senile plaque-associated proteins. Neurosci Lett 278: 81-84 (2000).
    • (2000) Neurosci Lett , vol.278 , pp. 81-84
    • Monji, A.1    Yoshida, I.2    Tashiro, K.3    Hayashi, Y.4    Matsuda, K.5    Tashiro, N.6
  • 13
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • Walsh DM, Hartley DM, Kusumoto Y, Fezoui Y, Condron MM, Lomakin A, et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 274: 25945-25952 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6
  • 14
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg MS and Lansbury PTJr. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat Cell Biol 2: E115-9 (2000).
    • (2000) Nat Cell Biol , vol.2
    • Goldberg, M.S.1    Lansbury Jr., P.T.2
  • 15
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • USA
    • Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE and Lansbury PT Jr. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc Natl Acad Sci USA 97: 571-576 (2000).
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury Jr., P.T.6
  • 16
    • 0034089960 scopus 로고    scopus 로고
    • Fresh and nonfibrillar amyloid beta protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AbetaP-channel-mediated cellular toxicity
    • Zhu YJ, Lin H and Lal R. Fresh and nonfibrillar amyloid beta protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AbetaP-channel-mediated cellular toxicity. FASEB J 14: 1244-1254 (2000).
    • (2000) FASEB J , vol.14 , pp. 1244-1254
    • Zhu, Y.J.1    Lin, H.2    Lal, R.3
  • 17
    • 0025992417 scopus 로고
    • In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG and Cotman CW. In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res 563: 311-314 (1991).
    • (1991) Brain Res , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 18
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • USA
    • Lorenzo A and Yankner BA. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc Natl Acad Sci USA 91: 12243-12247 (1994).
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 19
    • 0036848056 scopus 로고    scopus 로고
    • A novel beta-sheet breaker, RS-0406, reverses amyloid beta-induced cytotoxicity and impairment of long-term potentiation in vitro
    • Nakagami Y, Nishimura S, Murasugi T, Kaneko I, Meguro M, Marumoto S,, et al. A novel beta-sheet breaker, RS-0406, reverses amyloid beta-induced cytotoxicity and impairment of long-term potentiation in vitro. Br J Pharmacol 137: 676-682 (2002).
    • (2002) Br J Pharmacol , vol.137 , pp. 676-682
    • Nakagami, Y.1    Nishimura, S.2    Murasugi, T.3    Kaneko, I.4    Meguro, M.5    Marumoto, S.6
  • 20
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation
    • Walsh DM, Townsend M, Podlisny MB, Shankar GM, Fadeeva JV, Agnaf OE et al. Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation. J Neurosci 25: 2455-2462 (2005).
    • (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
  • 21
    • 3042798841 scopus 로고    scopus 로고
    • Beta-amyloid-mediated inhibition of NMDA receptor-dependent long-term potentiation induction involves activation of microglia and stimulation of inducible nitric oxide synthase and superoxide
    • Wang Q, Rowan MJ and Anwyl R. Beta-amyloid-mediated inhibition of NMDA receptor-dependent long-term potentiation induction involves activation of microglia and stimulation of inducible nitric oxide synthase and superoxide. J Neurosci 24: 6049-6056 (2004).
    • (2004) J Neurosci , vol.24 , pp. 6049-6056
    • Wang, Q.1    Rowan, M.J.2    Anwyl, R.3
  • 23
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • Stine WB Jr, Dahlgren KN, Krafft GA and LaDu MJ. In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J Biol Chem 278: 11612-11622 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    Ladu, M.J.4
  • 24
    • 0036547110 scopus 로고    scopus 로고
    • Peptide inhibitors of beta amyloid aggregation
    • Findeis MA. Peptide inhibitors of beta amyloid aggregation. Curr Top Med Chem 2: 417-423 (2002).
    • (2002) Curr Top Med Chem , vol.2 , pp. 417-423
    • Findeis, M.A.1
  • 25
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG and Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120: 885-890 (1984).
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 26
    • 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 CL, Multhaup G, Simms G, Pottgiesser J, Martins RN and Beyreuther K. Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO J 4: 2757-2763 (1985).
    • (1985) EMBO 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
  • 27
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire HG, Unterbeck A, Salbaum JM, Masters CL, Grzeschik KH, et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325: 733-736 (1987).
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3    Salbaum, J.M.4    Masters, C.L.5    Grzeschik, K.H.6
  • 29
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids
    • Seubert P, Vigo-Pelfrey C, Esch F, Lee M, Dovey H, Davis D, et al. Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids. Nature 359: 325-327 (1992).
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Esch, F.3    Lee, M.4    Dovey, H.5    Davis, D.6
  • 30
    • 0026760261 scopus 로고
    • Production of the Alzheimer amyloid beta protein by normal proteolytic processing
    • Shoji M, Golde TE, Ghiso J, Cheung TT, Estus S, Shaffer LM, et al. Production of the Alzheimer amyloid beta protein by normal proteolytic processing. Science 258: 126-129 (1992).
    • (1992) Science , vol.258 , pp. 126-129
    • Shoji, M.1    Golde, T.E.2    Ghiso, J.3    Cheung, T.T.4    Estus, S.5    Shaffer, L.M.6
  • 31
    • 0027407570 scopus 로고
    • Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • USA
    • Busciglio J, Gabuzda DH, Matsudaira P and Yankner BA. Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc Natl Acad Sci USA 90: 2092-2096 (1993).
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 32
    • 0034516988 scopus 로고    scopus 로고
    • Toward a comprehensive theory for Alzheimer's disease. Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of amyloid beta-protein
    • Selkoe DJ. Toward a comprehensive theory for Alzheimer's disease. Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of amyloid beta-protein. Ann N Y Acad Sci 924: 17-25 (2000).
    • (2000) Ann N Y Acad Sci , vol.924 , pp. 17-25
    • Selkoe, D.J.1
  • 33
  • 34
    • 0028913471 scopus 로고
    • Trafficking of cell surface beta-amyloid precursor protein: Retrograde and transcytotic transport in cultured neurons
    • Yamazaki T, Selkoe DJ and Koo EH. Trafficking of cell surface beta-amyloid precursor protein: retrograde and transcytotic transport in cultured neurons. J Cell Biol 129: 431-442 (1995).
    • (1995) J Cell Biol , vol.129 , pp. 431-442
    • Yamazaki, T.1    Selkoe, D.J.2    Koo, E.H.3
  • 35
    • 0026432318 scopus 로고
    • Seminars in medicine of the Beth Israel Hospital, Boston. beta-Amyloid and the pathogenesis of Alzheimer's disease
    • Yankner BA and Mesulam MM. Seminars in medicine of the Beth Israel Hospital, Boston. beta-Amyloid and the pathogenesis of Alzheimer's disease. N Engl J Med 325: 1849-1857 (1991).
    • (1991) N Engl J Med , vol.325 , pp. 1849-1857
    • Yankner, B.A.1    Mesulam, M.M.2
  • 36
  • 37
    • 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 and Seubert P. Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice. Brain Res 840: 23-35 (1999).
    • (1999) Brain Res , vol.840 , pp. 23-35
    • Larson, J.1    Lynch, G.2    Games, D.3    Seubert, P.4
  • 38
    • 13044287361 scopus 로고    scopus 로고
    • Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models
    • USA
    • Hsia AY, Masliah E, McConlogue L, Yu GQ, Tatsuno G, Hu K, et al. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc Natl Acad Sci USA 96: 3228-3233 (1999).
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 3228-3233
    • Hsia, A.Y.1    Masliah, E.2    McConlogue, L.3    Yu, G.Q.4    Tatsuno, G.5    Hu, K.6
  • 39
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Abeta and synaptic dysfunction
    • Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, Kayed R, et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron 39: 409-421 (2003).
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6
  • 40
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice
    • Hsiao K, Chapman P, Nilsen S, Eckman C, Harigaya Y, Younkin S, et al. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 274: 99-102 (1996).
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6
  • 41
    • 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 SM, Morton RA, Kuenzi F, Rosahl TW, Shearman M, Lewis H, et al. 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).
    • (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
  • 42
    • 0033525520 scopus 로고    scopus 로고
    • Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain
    • Moechars D, Dewachter I, Lorent K, Reverse D, Baekelandt V, Naidu A, et al. Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain. J Biol Chem 274: 6483-6492 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 6483-6492
    • Moechars, D.1    Dewachter, I.2    Lorent, K.3    Reverse, D.4    Baekelandt, V.5    Naidu, A.6
  • 43
    • 0030978998 scopus 로고    scopus 로고
    • Impaired learning and LTP in mice expressing the carboxy terminus of the Alzheimer amyloid precursor protein
    • Nalbantoglu J, Tirado-Santiago G, Lahsaini A, Poirier J, Goncalves O, Verge G, et al. Impaired learning and LTP in mice expressing the carboxy terminus of the Alzheimer amyloid precursor protein. Nature 387: 500-505 (1997).
    • (1997) Nature , vol.387 , pp. 500-505
    • Nalbantoglu, J.1    Tirado-Santiago, G.2    Lahsaini, A.3    Poirier, J.4    Goncalves, O.5    Verge, G.6
  • 44
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, Wang N, et al. ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 304: 448-452 (2004).
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3    Xu, H.W.4    Takuma, K.5    Wang, N.6
  • 45
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction
    • Takuma K, Yao J, Huang J, Xu H, Chen X, Luddy J, et al. ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction. FASEB J 19: 597-598 (2005).
    • (2005) FASEB J , vol.19 , pp. 597-598
    • Takuma, K.1    Yao, J.2    Huang, J.3    Xu, H.4    Chen, X.5    Luddy, J.6
  • 46
    • 8144223671 scopus 로고    scopus 로고
    • RAGE potentiates Abeta-induced perturbation of neuronal function in transgenic mice
    • Arancio O, Zhang HP, Chen X, Lin C, Trinchese F, Puzzo D, et al. RAGE potentiates Abeta-induced perturbation of neuronal function in transgenic mice. EMBO J 23: 4096-4105 (2004).
    • (2004) EMBO J , vol.23 , pp. 4096-4105
    • Arancio, O.1    Zhang, H.P.2    Chen, X.3    Lin, C.4    Trinchese, F.5    Puzzo, D.6
  • 47
    • 0035875962 scopus 로고    scopus 로고
    • Beta-amyloid activates the mitogen-activated protein kinase cascade via hippocampal alpha7 nicotinic acetylcholine receptors: In vitro and in vivo mechanisms related to Alzheimer's disease
    • Dineley KT, Westerman M, Bui D, Bell K, Ashe KH and Sweatt JD. Beta-amyloid activates the mitogen-activated protein kinase cascade via hippocampal alpha7 nicotinic acetylcholine receptors: In vitro and in vivo mechanisms related to Alzheimer's disease. J Neurosci 21: 4125-4133 (2001).
    • (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
  • 48
    • 0034648038 scopus 로고    scopus 로고
    • SB203580, the p38 mitogena-ctivated protein kinase inhibitor blocks the inhibitory effect of beta-amyloid on long-term potentiation in the rat hippocampus
    • Saleshando G and O'Connor JJ. SB203580, the p38 mitogena-ctivated protein kinase inhibitor blocks the inhibitory effect of beta-amyloid on long-term potentiation in the rat hippocampus. Neurosci Lett 288: 119-22 (2000).
    • (2000) Neurosci Lett , vol.288 , pp. 119-122
    • Saleshando, G.1    O'Connor, J.J.2
  • 49
    • 22544485048 scopus 로고    scopus 로고
    • Amyloid-beta 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 JP, Palmeri A and Arancio O. Amyloid-beta peptide inhibits activation of the nitric oxide/cGMP/cAMP- responsive element-binding protein pathway during hippocampal synaptic plasticity. J Neurosci 25: 6887-97 (2005).
    • (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
  • 50
    • 14844315768 scopus 로고    scopus 로고
    • Amyloid beta prevents activation of calcium/calmodulin-dependent protein kinase II and AMPA receptor phosphorylation during hippocampal long-term potentiation
    • Zhao D, Watson JB and Xie CW. Amyloid beta prevents activation of calcium/calmodulin-dependent protein kinase II and AMPA receptor phosphorylation during hippocampal long-term potentiation. J Neurophysiol 92: 2853-2858 (2004).
    • (2004) J Neurophysiol , vol.92 , pp. 2853-2858
    • Zhao, D.1    Watson, J.B.2    Xie, C.W.3
  • 51
    • 0028170035 scopus 로고
    • cAMP contributes to mossy fiber LTP by initiating both a covalently mediated early phase and macromolecular synthesis-dependent late phase
    • Huang YY, Li XC and Kandel ER. cAMP contributes to mossy fiber LTP by initiating both a covalently mediated early phase and macromolecular synthesis-dependent late phase. Cell 79: 69-79 (1994).
    • (1994) Cell , vol.79 , pp. 69-79
    • Huang, Y.Y.1    Li, X.C.2    Kandel, E.R.3
  • 52
    • 0028051845 scopus 로고
    • Mediation of hippocampal mossy fiber long-term potentiation by cyclic AMP
    • Weisskopf MG, Castillo PE, Zalutsky RA and Nicoll RA. Mediation of hippocampal mossy fiber long-term potentiation by cyclic AMP. Science 265: 1878-1882 (1994).
    • (1994) Science , vol.265 , pp. 1878-1882
    • Weisskopf, M.G.1    Castillo, P.E.2    Zalutsky, R.A.3    Nicoll, R.A.4
  • 53
    • 17444438298 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase cascade is required for NMDA receptor-independent LTP in area CA1 but not area CA3 of the hippocampus
    • Kanterewicz BI, Urban NN, McMahon DB, Norman ED, Giffen LJ, Favata MF, et al. The extracellular signal-regulated kinase cascade is required for NMDA receptor-independent LTP in area CA1 but not area CA3 of the hippocampus. J Neurosci 20: 3057-3066 (2000).
    • (2000) J Neurosci , vol.20 , pp. 3057-3066
    • Kanterewicz, B.I.1    Urban, N.N.2    McMahon, D.B.3    Norman, E.D.4    Giffen, L.J.5    Favata, M.F.6
  • 54
    • 0027203084 scopus 로고
    • Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons
    • Frey U, Huang YY and Kandel ER. Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons. Science 260: 1661-1664 (1993).
    • (1993) Science , vol.260 , pp. 1661-1664
    • Frey, U.1    Huang, Y.Y.2    Kandel, E.R.3
  • 55
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416: 507-511 (2002).
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 56
    • 0037073604 scopus 로고    scopus 로고
    • A novel compound RS-0466 reverses beta-amyloid-induced cytotoxicity through the Akt signaling pathway in vitro
    • Nakagami Y, Nishimura S, Murasugi T, Kubo T, Kaneko I, Meguro M, et al. A novel compound RS-0466 reverses beta-amyloid-induced cytotoxicity through the Akt signaling pathway in vitro. Eur J Pharmacol 457: 11-17 (2002).
    • (2002) Eur J Pharmacol , vol.457 , pp. 11-17
    • Nakagami, Y.1    Nishimura, S.2    Murasugi, T.3    Kubo, T.4    Kaneko, I.5    Meguro, M.6
  • 57
    • 21044453723 scopus 로고    scopus 로고
    • Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo
    • Klyubin I, Walsh DM, Lemere CA, Cullen WK, Shankar GM, Betts V, et al. Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo. Nat Med 11: 556-561 (2005).
    • (2005) Nat Med , vol.11 , pp. 556-561
    • Klyubin, I.1    Walsh, D.M.2    Lemere, C.A.3    Cullen, W.K.4    Shankar, G.M.5    Betts, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.