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Volumn 29, Issue 2, 2005, Pages 333-343

Altered intracellular signaling and reduced viability of Alzheimer's disease neuronal cybrids is reproduced by β-amyloid peptide acting through receptor for advanced glycation end products (RAGE)

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; AMYLOID BETA PROTEIN; ANTIBODY; GAMMA SECRETASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; STRESS ACTIVATED PROTEIN KINASE;

EID: 19444381217     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mcn.2005.02.012     Document Type: Article
Times cited : (58)

References (77)
  • 2
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay
    • A.J. Anderson, J.H. Su, and C.W. Cotman DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay J. Neurosci. 16 1996 1710 1719
    • (1996) J. Neurosci. , vol.16 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 3
    • 0028207907 scopus 로고
    • Amyloid beta peptide induces necrosis rather than apoptosis
    • C. Behl, J.B. Davis, F.G. Klier, and D. Schubert Amyloid beta peptide induces necrosis rather than apoptosis Brain Res. 645 1994 253 264
    • (1994) Brain Res. , vol.645 , pp. 253-264
    • Behl, C.1    Davis, J.B.2    Klier, F.G.3    Schubert, D.4
  • 4
    • 0036208563 scopus 로고    scopus 로고
    • Acetominophen protects hippocampal neurons and PC12 cultures from amyloid beta peptides induced oxidative stress and reduces NFkB activation
    • M. Bisaglia, V. Venezia, P. Piccioli, S. Stanzione, C. Porcile, C. Russo, F. Mancini, C. Milanese, and G. Schettini Acetominophen protects hippocampal neurons and PC12 cultures from amyloid beta peptides induced oxidative stress and reduces NFkB activation Neurochem. Int. 41 2002 43 54
    • (2002) Neurochem. Int. , vol.41 , pp. 43-54
    • Bisaglia, M.1    Venezia, V.2    Piccioli, P.3    Stanzione, S.4    Porcile, C.5    Russo, C.6    Mancini, F.7    Milanese, C.8    Schettini, G.9
  • 6
    • 0035369623 scopus 로고    scopus 로고
    • Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway
    • A. Brunet, S.R. Datta, and M.E. Greenberg Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway Curr. Opin. Neurobiol. 11 2001 297 305
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 297-305
    • Brunet, A.1    Datta, S.R.2    Greenberg, M.E.3
  • 7
    • 0036272650 scopus 로고    scopus 로고
    • Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • C.S. Casley, L. Canevari, J.M. Land, J.B. Clark, and M.A. Sharpe Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities J. Neurochem. 80 2002 91 100
    • (2002) J. Neurochem. , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 8
    • 0033080919 scopus 로고    scopus 로고
    • Identification of microglial signal transduction pathways mediating a neurotoxic response to amyloidogenic fragments of beta-amyloid and prion proteins
    • C.K. Combs, D.E. Johnson, S.B. Cannady, T.M. Lehman, and G.E. Landreth Identification of microglial signal transduction pathways mediating a neurotoxic response to amyloidogenic fragments of beta-amyloid and prion proteins J. Neurosci. 19 1999 928 939
    • (1999) J. Neurosci. , vol.19 , pp. 928-939
    • Combs, C.K.1    Johnson, D.E.2    Cannady, S.B.3    Lehman, T.M.4    Landreth, G.E.5
  • 11
    • 0030669036 scopus 로고    scopus 로고
    • The pathogenesis of senile plaques
    • D. Dickson The pathogenesis of senile plaques J. Neuropathol. Exp. Neurol. 56 1997 321 339
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 321-339
    • Dickson, D.1
  • 12
    • 0000920292 scopus 로고    scopus 로고
    • Amyloid-b peptide-receptor for advanced glycation endproduct interaction elicits neuronal expression of macrophage-colony stimulating factor: A proinflammatory pathway in Alzheimer disease
    • Y.S. Du, H. Zhu, J. Fu, S.F. Yan, A. Roher, W.W. Tourtellotte, T. Rajavashisth, X. Chen, G.C. Godman, D. Stern, and A.M. Schmidt Amyloid-b peptide-receptor for advanced glycation endproduct interaction elicits neuronal expression of macrophage-colony stimulating factor: a proinflammatory pathway in Alzheimer disease Proc. Natl. Acad. Sci. U. S. A. 94 1997 5296 5301
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5296-5301
    • Du, Y.S.1    Zhu, H.2    Fu, J.3    Yan, S.F.4    Roher, A.5    Tourtellotte, W.W.6    Rajavashisth, T.7    Chen, X.8    Godman, G.C.9    Stern, D.10    Schmidt, A.M.11
  • 15
    • 0027076090 scopus 로고
    • Normal processing of the Alzheimer's disease amyloid beta protein precursor generates potentially amyloidogenic carboxyl-terminal derivatives
    • S. Estus, T.E. Golde, and S.G. Younkin Normal processing of the Alzheimer's disease amyloid beta protein precursor generates potentially amyloidogenic carboxyl-terminal derivatives Ann. N. Y. Acad. Sci. 674 1992 138 148
    • (1992) Ann. N. Y. Acad. Sci. , vol.674 , pp. 138-148
    • Estus, S.1    Golde, T.E.2    Younkin, S.G.3
  • 17
    • 0027973061 scopus 로고
    • CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 β-converting enzyme
    • T. Fernandes-Alnemri, G. Litwack, and E.S. Alnemri CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 β-converting enzyme J. Biol. Chem. 269 1994 30761 30764
    • (1994) J. Biol. Chem. , vol.269 , pp. 30761-30764
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 19
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • T.E. Golde, S. Estus, L.H. Younkin, D.J. Selkoe, and S.G. Younkin Processing of the amyloid protein precursor to potentially amyloidogenic derivatives Science 255 1992 728 730
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 20
    • 0036312008 scopus 로고    scopus 로고
    • Divergent pathways account for two distinct effects of amyloid beta peptides on exocytosis and Ca2+ currents: Involvement of ROS and NFkB
    • K.N. Green, and C. Peers Divergent pathways account for two distinct effects of amyloid beta peptides on exocytosis and Ca2+ currents: involvement of ROS and NFkB J. Neurochem. 81 2002 1043 1051
    • (2002) J. Neurochem. , vol.81 , pp. 1043-1051
    • Green, K.N.1    Peers, C.2
  • 21
    • 0033830186 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 in the nervous system
    • H.C. Ha, and S.H Snyder Poly(ADP-ribose) polymerase-1 in the nervous system Neurobiol. Dis. 7 2000 225 239
    • (2000) Neurobiol. Dis. , vol.7 , pp. 225-239
    • Ha, H.C.1    Snyder, S.H.2
  • 23
    • 0036861112 scopus 로고    scopus 로고
    • Testing times for the 'amyloid cascade hypothesis'
    • J. Hardy Testing times for the 'amyloid cascade hypothesis' Neurobiol. Aging 23 2002 1073 1074
    • (2002) Neurobiol. Aging , vol.23 , pp. 1073-1074
    • Hardy, J.1
  • 24
    • 0033458064 scopus 로고    scopus 로고
    • Intracellular biology of Alzheimer's disease amyloid beta peptide
    • T. Hartmann Intracellular biology of Alzheimer's disease amyloid beta peptide Eur. Arch. Psychiatry Clin. Neurosci. 249 1999 291 298
    • (1999) Eur. Arch. Psychiatry Clin. Neurosci. , vol.249 , pp. 291-298
    • Hartmann, T.1
  • 26
    • 0030983079 scopus 로고    scopus 로고
    • Transcription factor NF-kappaB is activated in primary neurons by amyloid beta peptides and in neurons surrounding early plaques from patients with Alzheimer disease
    • B. Kaltschmidt, M. Uherek, B. Volk, P.A. Baeuerle, and C. Kaltschmidt Transcription factor NF-kappaB is activated in primary neurons by amyloid beta peptides and in neurons surrounding early plaques from patients with Alzheimer disease Proc. Natl. Acad. Sci. U. S. A. 94 1997 2642 2647
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2642-2647
    • Kaltschmidt, B.1    Uherek, M.2    Volk, B.3    Baeuerle, P.A.4    Kaltschmidt, C.5
  • 27
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis
    • S.H. Kaufmann, S. Desnoyers, Y. Ottaviano, N.E. Davidson, and G.G. Poirier Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis Cancer Res. 53 1993 3976 3985
    • (1993) Cancer Res. , vol.53 , pp. 3976-3985
    • Kaufmann, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 29
    • 0035997221 scopus 로고    scopus 로고
    • Correlation between beta-amyloid peptide production and human APP-induced neuronal death
    • P. Kienlen-Campard, and J.N. Octave Correlation between beta-amyloid peptide production and human APP-induced neuronal death Peptides 23 2002 1199 1204
    • (2002) Peptides , vol.23 , pp. 1199-1204
    • Kienlen-Campard, P.1    Octave, J.N.2
  • 30
    • 0035957946 scopus 로고    scopus 로고
    • Alpha 7 nicotinic receptor transduces signals to phosphatidylinositol 3-kinase to block a beta-amyloid-induced neurotoxicity
    • T. Kihara, S. Shimohama, H. Sawada, K. Honda, T. Nakamizo, H. Shibasaki, T. Kume, and A. Akaike Alpha 7 nicotinic receptor transduces signals to phosphatidylinositol 3-kinase to block A beta-amyloid-induced neurotoxicity J. Biol. Chem. 276 2001 13541 13546
    • (2001) J. Biol. Chem. , vol.276 , pp. 13541-13546
    • Kihara, T.1    Shimohama, S.2    Sawada, H.3    Honda, K.4    Nakamizo, T.5    Shibasaki, H.6    Kume, T.7    Akaike, A.8
  • 31
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • M. King, and G. Attardi Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation Science 246 1989 500 503
    • (1989) Science , vol.246 , pp. 500-503
    • King, M.1    Attardi, G.2
  • 32
    • 0032430882 scopus 로고    scopus 로고
    • Induction of apoptosis in Hep-2 cells by infection with herpes simplex virus type 2
    • A.H. Koyama, H. Akari, A. Adachi, F. Goshima, and Y. Nishiyama Induction of apoptosis in Hep-2 cells by infection with herpes simplex virus type 2 Arch. Virol. 143 1998 2435 2441
    • (1998) Arch. Virol. , vol.143 , pp. 2435-2441
    • Koyama, A.H.1    Akari, H.2    Adachi, A.3    Goshima, F.4    Nishiyama, Y.5
  • 33
    • 0030859290 scopus 로고    scopus 로고
    • Activation of the receptor for advanced glycation end products triggers a p21(ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress
    • H.M. Lander, J.M. Tauras, J.S. Ogiste, O. Hori, R.A. Moss, and A.M. Schmidt Activation of the receptor for advanced glycation end products triggers a p21(ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress J. Biol. Chem. 272 1997 17810 17814
    • (1997) J. Biol. Chem. , vol.272 , pp. 17810-17814
    • Lander, H.M.1    Tauras, J.M.2    Ogiste, J.S.3    Hori, O.4    Moss, R.A.5    Schmidt, A.M.6
  • 34
    • 0031918250 scopus 로고    scopus 로고
    • Receptors for advanced glycosylation endproducts in human brain: Role in brain homeostasis
    • J.J. Li, D. Dickson, P.R. Hof, and H. Vlassara Receptors for advanced glycosylation endproducts in human brain: role in brain homeostasis Mol. Med. 4 1998 46 60
    • (1998) Mol. Med. , vol.4 , pp. 46-60
    • Li, J.J.1    Dickson, D.2    Hof, P.R.3    Vlassara, H.4
  • 35
    • 0034840664 scopus 로고    scopus 로고
    • Involvement of microglial receptor for advanced glycation endproducts (RAGE) in Alzheimer's disease: Identification of a cellular activation mechanism
    • L.F. Lue, D.G. Walker, L. Brachova, T.G. Beach, J. Rogers, A.M. Schmidt, D.M. Stern, and S.D. Yan Involvement of microglial receptor for advanced glycation endproducts (RAGE) in Alzheimer's disease: identification of a cellular activation mechanism Exp. Neurol. 171 2001 29 45
    • (2001) Exp. Neurol. , vol.171 , pp. 29-45
    • Lue, L.F.1    Walker, D.G.2    Brachova, L.3    Beach, T.G.4    Rogers, J.5    Schmidt, A.M.6    Stern, D.M.7    Yan, S.D.8
  • 38
    • 0034839145 scopus 로고    scopus 로고
    • Effect of the Alzheimer amyloid fragment Abeta (25-35) on Akt/PKB kinase and survival of PC12 cells
    • D. Martin, M. Salinas, R. Lopez-Valdaliso, E. Serrano, M. Recuero, and A. Cuadrado Effect of the Alzheimer amyloid fragment Abeta (25-35) on Akt/PKB kinase and survival of PC12 cells J. Neurochem. 78 2001 1000 1008
    • (2001) J. Neurochem. , vol.78 , pp. 1000-1008
    • Martin, D.1    Salinas, M.2    Lopez-Valdaliso, R.3    Serrano, E.4    Recuero, M.5    Cuadrado, A.6
  • 39
    • 0034665698 scopus 로고    scopus 로고
    • Caspase-3 activation and inflammatory responses in rat hippocampus inoculated with a recombinant adenovirus expressing the Alzheimer amyloid precursor protein
    • M. Masumura, R. Hata, I. Nishimura, T. Uetsuki, T. Sawada, and K. Yoshikawa Caspase-3 activation and inflammatory responses in rat hippocampus inoculated with a recombinant adenovirus expressing the Alzheimer amyloid precursor protein Brain Res., Mol. Brain Res. 80 2000 219 227
    • (2000) Brain Res., Mol. Brain Res. , vol.80 , pp. 219-227
    • Masumura, M.1    Hata, R.2    Nishimura, I.3    Uetsuki, T.4    Sawada, T.5    Yoshikawa, K.6
  • 41
    • 0036826903 scopus 로고    scopus 로고
    • Selective inhibition of Abeta 42 production by NSAID R-enantiomers
    • T. Morihara, T. Chu, O. Ubeda, W. Beech, and G.M. Cole Selective inhibition of Abeta 42 production by NSAID R-enantiomers J. Neurochem. 83 2002 1009 1012
    • (2002) J. Neurochem. , vol.83 , pp. 1009-1012
    • Morihara, T.1    Chu, T.2    Ubeda, O.3    Beech, W.4    Cole, G.M.5
  • 42
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • T. Mosmann Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays J. Immunol. Methods 65 1983 55 63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 43
    • 0033597105 scopus 로고    scopus 로고
    • Gamma-secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid beta peptides of varying length
    • M.P. Murphy, L.J. Hickman, C.B. Eckman, S.N. Uljon, R. Wang, and T.E. Golde Gamma-secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid beta peptides of varying length J. Biol. Chem. 274 1999 11914 11923
    • (1999) J. Biol. Chem. , vol.274 , pp. 11914-11923
    • Murphy, M.P.1    Hickman, L.J.2    Eckman, C.B.3    Uljon, S.N.4    Wang, R.5    Golde, T.E.6
  • 44
    • 17544378704 scopus 로고    scopus 로고
    • Endogenous oxidative stress in sporadic Alzheimer's disease neuronal cybrids reduces viability by increasing apoptosis through pro-death signaling pathways and is mimicked by oxidant exposure of control cybrids
    • in press. (available online 19th March 2005; doi:10.1016/j.nbd.2005.01. 026).
    • Onyango, I.G., Bennett Jr., J.P., Tuttle, J.B., in press. Endogenous oxidative stress in sporadic Alzheimer's disease neuronal cybrids reduces viability by increasing apoptosis through pro-death signaling pathways and is mimicked by oxidant exposure of control cybrids. Neurobiol. Dis. (available online 19th March 2005; doi:10.1016/j.nbd.2005.01.026).
    • Neurobiol. Dis.
    • Onyango, I.G.1    Bennett Jr., J.P.2    Tuttle, J.B.3
  • 45
    • 0034745636 scopus 로고    scopus 로고
    • Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro
    • J.K. Parks, T.S. Smith, P.A. Trimmer, J.P. Bennett Jr., and W.D. Parker Jr. Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro J. Neurochem. 76 2001 1050 1056
    • (2001) J. Neurochem. , vol.76 , pp. 1050-1056
    • Parks, J.K.1    Smith, T.S.2    Trimmer, P.A.3    Bennett Jr., J.P.4    Parker Jr., W.D.5
  • 46
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures
    • C.J. Pike, A.J. Walencewicz, C.G. Glabe, and C.W. Cotman Aggregation-related toxicity of synthetic beta-amyloid protein in hippocampal cultures Eur. J. Pharmacol. 207 1991 367 368
    • (1991) Eur. J. Pharmacol. , vol.207 , pp. 367-368
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 47
    • 0035141757 scopus 로고    scopus 로고
    • Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease
    • T.T. Rohn, E. Head, J.H. Su, A.J. Anderson, B.A. Bahr, C.W. Cotman, and D.H. Cribbs Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer's disease Am. J. Pathol. 158 2001 189 198
    • (2001) Am. J. Pathol. , vol.158 , pp. 189-198
    • Rohn, T.T.1    Head, E.2    Su, J.H.3    Anderson, A.J.4    Bahr, B.A.5    Cotman, C.W.6    Cribbs, D.H.7
  • 48
    • 0035847269 scopus 로고    scopus 로고
    • Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease
    • N. Sasaki, S. Toki, H. Chowei, T. Saito, N. Nakano, Y. Hayashi, M. Takeuchi, and Z. Makita Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease Brain Res. 888 2001 256 262
    • (2001) Brain Res. , vol.888 , pp. 256-262
    • Sasaki, N.1    Toki, S.2    Chowei, H.3    Saito, T.4    Nakano, N.5    Hayashi, Y.6    Takeuchi, M.7    Makita, Z.8
  • 49
    • 0031587787 scopus 로고    scopus 로고
    • Elevated amyloid beta protein (1-40) level induces CREB phosphorylation at serine-133 via p44/42 MAP kinase (ERK1/2)-dependent pathway in rat pheochromocytoma PC12 cells
    • N. Sato, K. Kamino, K. Tateishi, T. Satoh, Y. Nishiwaki, A. Yoshiiwa, T. Miki, and T. Ogihara Elevated amyloid beta protein (1-40) level induces CREB phosphorylation at serine-133 via p44/42 MAP kinase (ERK1/2)-dependent pathway in rat pheochromocytoma PC12 cells Biochem. Biophys. Res. 232 1997
    • (1997) Biochem. Biophys. Res. , vol.232
    • Sato, N.1    Kamino, K.2    Tateishi, K.3    Satoh, T.4    Nishiwaki, Y.5    Yoshiiwa, A.6    Miki, T.7    Ogihara, T.8
  • 50
    • 0034795140 scopus 로고    scopus 로고
    • The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
    • A.M. Schmidt, S.D. Yan, S.F. Yan, and D.M. Stern The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses J. Clin. Invest. 108 2001 949 955
    • (2001) J. Clin. Invest. , vol.108 , pp. 949-955
    • Schmidt, A.M.1    Yan, S.D.2    Yan, S.F.3    Stern, D.M.4
  • 52
    • 0031017696 scopus 로고    scopus 로고
    • Altered calcium homeostasis in cells transformed by mitochondria from individuals with Parkinson's disease
    • J.P. Sheehan, R.H. Swerdlow, W.D. Parker, S.W. Miller, R.E. Davis, and J.B. Tuttle Altered calcium homeostasis in cells transformed by mitochondria from individuals with Parkinson's disease J. Neurochem. 68 1997 1221 1233
    • (1997) J. Neurochem. , vol.68 , pp. 1221-1233
    • Sheehan, J.P.1    Swerdlow, R.H.2    Parker, W.D.3    Miller, S.W.4    Davis, R.E.5    Tuttle, J.B.6
  • 53
    • 0030923869 scopus 로고    scopus 로고
    • Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease
    • J.P. Sheehan, R.H. Swerdlow, S.W. Miller, R.E. Davis, J.K. Parks, W.D. Parker, and J.B. Tuttle Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease J. Neurosci. 17 1997 4612 4622
    • (1997) J. Neurosci. , vol.17 , pp. 4612-4622
    • Sheehan, J.P.1    Swerdlow, R.H.2    Miller, S.W.3    Davis, R.E.4    Parks, J.K.5    Parker, W.D.6    Tuttle, J.B.7
  • 56
    • 0034073966 scopus 로고    scopus 로고
    • DNA damage and activated caspase-3 expression in neurons and astrocytes: Evidence for apoptosis in frontotemporal dementia
    • J.H. Su, K.E. Nichol, and T. Sitch DNA damage and activated caspase-3 expression in neurons and astrocytes: evidence for apoptosis in frontotemporal dementia Exp. Neurol. 163 2000 9 19
    • (2000) Exp. Neurol. , vol.163 , pp. 9-19
    • Su, J.H.1    Nichol, K.E.2    Sitch, T.3
  • 60
    • 0037200036 scopus 로고    scopus 로고
    • Linear non-competitive inhibition of solubilized human-secretase by pepstatin a methylester, L685458, sulfonamides, and benzodiazepines
    • G.T. Tian, C.D. Sobotka-Briner, J. Zysk, X. Liu, C. Birr, M.A. Sylvester, P.D. Edwards, C.D. Scott, and B.D. Greenberg Linear non-competitive inhibition of solubilized human-secretase by pepstatin a methylester, L685458, sulfonamides, and benzodiazepines J. Biol. Chem. 277 2002 31499 31505
    • (2002) J. Biol. Chem. , vol.277 , pp. 31499-31505
    • Tian, G.T.1    Sobotka-Briner, C.D.2    Zysk, J.3    Liu, X.4    Birr, C.5    Sylvester, M.A.6    Edwards, P.D.7    Scott, C.D.8    Greenberg, B.D.9
  • 64
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • Y. Verdier, M. Zarandi, and B. Penke Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease J. Pept. Sci. 10 2004 229 248
    • (2004) J. Pept. Sci. , vol.10 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 65
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • D.M. Walsh, I. Klyubin, J.V. Fadeeva, W.K. Cullen, R. Anwyl, M.S. Wolfe, M.J. Rowan, and D.J. Selkoe Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo Nature 416 2002 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
  • 66
    • 0036138048 scopus 로고    scopus 로고
    • Rapid tyrosine phosphorylation of neuronal proteins including tau and focal adhesion kinase in response to amyloid-beta peptide exposure: Involvement of Src family protein kinases
    • R. Williamson, T. Scales, B.R. Clark, G. Gibb, C.H. Reynolds, S. Kellie, I.N. Bird, I.M. Varndell, P.W. Sheppard, I. Everall, and B.H. Anderton Rapid tyrosine phosphorylation of neuronal proteins including tau and focal adhesion kinase in response to amyloid-beta peptide exposure: involvement of Src family protein kinases J. Neurosci. 22 2002 10 20
    • (2002) J. Neurosci. , vol.22 , pp. 10-20
    • Williamson, R.1    Scales, T.2    Clark, B.R.3    Gibb, G.4    Reynolds, C.H.5    Kellie, S.6    Bird, I.N.7    Varndell, I.M.8    Sheppard, P.W.9    Everall, I.10    Anderton, B.H.11
  • 67
    • 0035933279 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice
    • O. Wirths, G. Multhaup, and C. Czech Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice Neurosci. Lett. 306 2001 116 120
    • (2001) Neurosci. Lett. , vol.306 , pp. 116-120
    • Wirths, O.1    Multhaup, G.2    Czech, C.3
  • 68
    • 7244236841 scopus 로고    scopus 로고
    • A modified b-amyloid hypothesis: Intraneuronal accumulation of the b-amyloid peptide-The first step of a fatal cascade
    • O. Wirths, G. Multhaup, and T.A. Bayer A modified b-amyloid hypothesis: intraneuronal accumulation of the b-amyloid peptide-The first step of a fatal cascade J. Neurochem. 91 2004 513 520
    • (2004) J. Neurochem. , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 69
  • 71
    • 0030888393 scopus 로고    scopus 로고
    • What's the RAGE? the receptor for advanced glycation end products (RAGE) and the dark side of glucose
    • S.D. Yan, D. Stern, and A.M. Schmidt What's the RAGE? The receptor for advanced glycation end products (RAGE) and the dark side of glucose Eur. J. Clin. Invest. 27 1997 179 181
    • (1997) Eur. J. Clin. Invest. , vol.27 , pp. 179-181
    • Yan, S.D.1    Stern, D.2    Schmidt, A.M.3
  • 73
    • 9144223075 scopus 로고    scopus 로고
    • Ebselen inhibits tumor necrosis factor-alpha-induced c-Jun N-terminal kinase activation and adhesion molecule expression in endothelial cells
    • M. Yoshizumi, Y. Fujita, Y. Izawa, Y. Suzaki, M. Kyaw, N. Ali, K. Tsuchiya, S. Kagami, S. Yano, S. Sone, and T. Tamaki Ebselen inhibits tumor necrosis factor-alpha-induced c-Jun N-terminal kinase activation and adhesion molecule expression in endothelial cells Exp. Cell Res. 292 2004 1 10
    • (2004) Exp. Cell Res. , vol.292 , pp. 1-10
    • Yoshizumi, M.1    Fujita, Y.2    Izawa, Y.3    Suzaki, Y.4    Kyaw, M.5    Ali, N.6    Tsuchiya, K.7    Kagami, S.8    Yano, S.9    Sone, S.10    Tamaki, T.11
  • 74
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • J. Yuan, and B.A. Yankner Apoptosis in the nervous system Nature 407 2000 802 809
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 75
    • 0035800196 scopus 로고    scopus 로고
    • Estrogen protects against beta-amyloid-induced neurotoxicity in rat hippocampal neurons by activation of Akt
    • L. Zhang, D.R. Rubinow, G. Xaing, B.S. Li, Y.H. Chang, D. Maric, J.L. Barker, and W. Ma Estrogen protects against beta-amyloid-induced neurotoxicity in rat hippocampal neurons by activation of Akt NeuroReport 12 2001 1919 1923
    • (2001) NeuroReport , vol.12 , pp. 1919-1923
    • Zhang, L.1    Rubinow, D.R.2    Xaing, G.3    Li, B.S.4    Chang, Y.H.5    Maric, D.6    Barker, J.L.7    Ma, W.8
  • 76
    • 0034735569 scopus 로고    scopus 로고
    • Akt regulates cell survival and apoptosis at a postmitochondrial level
    • H. Zhou, X.M. Li, J. Meinkoth, and R.N. Pittman Akt regulates cell survival and apoptosis at a postmitochondrial level J. Cell Biol. 151 2000 483 494
    • (2000) J. Cell Biol. , vol.151 , pp. 483-494
    • Zhou, H.1    Li, X.M.2    Meinkoth, J.3    Pittman, R.N.4
  • 77
    • 0035142804 scopus 로고    scopus 로고
    • Activation and redistribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease
    • X. Zhu, A.K. Raina, C.A. Rottkamp, G. Aliev, G. Perry, H. Boux, and M.A. Smith Activation and redistribution of c-Jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease J. Neurochem. 76 2001 435 441
    • (2001) J. Neurochem. , vol.76 , pp. 435-441
    • Zhu, X.1    Raina, A.K.2    Rottkamp, C.A.3    Aliev, G.4    Perry, G.5    Boux, H.6    Smith, M.A.7


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