메뉴 건너뛰기




Volumn 33, Issue 3, 2008, Pages 526-532

Delineating the mechanism of Alzheimer's disease Aβ peptide neurotoxicity

Author keywords

Aggregation; Alzheimer's disease; Amyloid; Copper; Neurotoxicity; Reactive oxygen species

Indexed keywords

AMYLOID BETA PROTEIN; CHELATING AGENT; CLIOQUINOL; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; CYCLIC GMP; DP 109; JKL 169; MITOGEN ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE; TRICYCLODECAN 9 YL XANTHOGENATE; UNCLASSIFIED DRUG;

EID: 38949205552     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-007-9469-8     Document Type: Review
Times cited : (97)

References (103)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297:353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 33745027879 scopus 로고    scopus 로고
    • Molecular mechanisms for Alzheimer's disease: Implications for neuroimaging and therapeutics
    • Masters CL, Cappai R, Barnham KJ et al (2006) Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics. J Neurochem 97:1700-1725
    • (2006) J Neurochem , vol.97 , pp. 1700-1725
    • Masters, C.L.1    Cappai, R.2    Barnham, K.J.3
  • 3
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire H, Unterbeck A et al (1987) The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325:733-736
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.2    Unterbeck, A.3
  • 4
    • 0026646604 scopus 로고
    • Amyloid β-peptide is produced by cultured cells during normal metabolism
    • Haass C, Schlossmacher MG, Hung AY et al (1992) Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359:322-325
    • (1992) Nature , vol.359 , pp. 322-325
    • Haass, C.1    Schlossmacher, M.G.2    Hung, A.Y.3
  • 5
    • 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 JT, Berger EP, Lansbury PT 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 32:4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 6
    • 33947182575 scopus 로고    scopus 로고
    • The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Abeta peptides
    • Liao MQ, Tzeng YJ, Chang LY et al (2007) The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Abeta peptides. FEBS Lett 581:1161-1165
    • (2007) FEBS Lett , vol.581 , pp. 1161-1165
    • Liao, M.Q.1    Tzeng, Y.J.2    Chang, L.Y.3
  • 7
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner BA, Duffy LK, Kirschner DA (1990) Neurotrophic and neurotoxic effects of amyloid β 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
  • 8
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike CJ, Burdick D, Walencewicz AJ et al (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
  • 9
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG et al (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
  • 10
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures
    • Pike CL, Walencewicz AJ, Glabe CG et al (1991) Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures. Eur J Pharmacol 207:367-368
    • (1991) Eur J Pharmacol , vol.207 , pp. 367-368
    • Pike, C.L.1    Walencewicz, A.J.2    Glabe, C.G.3
  • 11
    • 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 et al (2002) Naturally secreted oligomers of amyloid beta 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
  • 12
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Ab1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA et al (1998) Diffusible, nonfibrillar ligands derived from Ab1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 95:6448-6453
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 13
    • 33947265861 scopus 로고    scopus 로고
    • Concentration dependent Cu(2+) induced aggregation and dityrosine formation of the Alzheimer's disease amyloid-beta peptide
    • Smith DP, Ciccotosto GD, Tew DJ et al (2007) Concentration dependent Cu(2+) induced aggregation and dityrosine formation of the Alzheimer's disease amyloid-beta peptide. Biochemistry 46:2881-2891
    • (2007) Biochemistry , vol.46 , pp. 2881-2891
    • Smith, D.P.1    Ciccotosto, G.D.2    Tew, D.J.3
  • 14
    • 27644493692 scopus 로고    scopus 로고
    • Globular amyloid beta-peptide oligomer-a homogenous and stable neuropathological protein in Alzheimer's disease
    • Barghorn S, Nimmrich V, Striebinger A et al (2005) Globular amyloid beta-peptide oligomer-a homogenous and stable neuropathological protein in Alzheimer's disease. J Neurochem 95:834-847
    • (2005) J Neurochem , vol.95 , pp. 834-847
    • Barghorn, S.1    Nimmrich, V.2    Striebinger, A.3
  • 15
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S, Koh MT, Kotilinek L et al (2006) A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440:352-357
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 16
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean CA, Cherny RA, Fraser FW et al (1999) Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann Neurol 46:860-866
    • (1999) Ann Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3
  • 17
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • Lue LF, Kuo YM, Roher AE et al (1999) Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am J Pathol 155:853-862
    • (1999) Am J Pathol , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Roher, A.E.3
  • 18
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging
    • Wang J, Dickson DW, Trojanowski JQ et al (1999) The levels of soluble versus insoluble brain Abeta distinguish Alzheimer's disease from normal and pathologic aging. Exp Neurol 158:328-337
    • (1999) Exp Neurol , vol.158 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3
  • 19
    • 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 et al (2000) Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. JAMA 283:1571-1577
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3
  • 20
    • 33745552613 scopus 로고    scopus 로고
    • Amyloid-beta1-42 reduces neuronal excitability in mouse dentate gyrus
    • Yun SH, Gamkrelidze G, Stine WB et al (2006) Amyloid-beta1-42 reduces neuronal excitability in mouse dentate gyrus. Neurosci Lett 403:162-165
    • (2006) Neurosci Lett , vol.403 , pp. 162-165
    • Yun, S.H.1    Gamkrelidze, G.2    Stine, W.B.3
  • 21
    • 2942626182 scopus 로고    scopus 로고
    • Soluble Arctic amyloid beta protein inhibits hippocampal long-term potentiation in vivo
    • Klyubin I, Walsh DM, Cullen WK et al (2004) Soluble Arctic amyloid beta protein inhibits hippocampal long-term potentiation in vivo. Eur J Neurosci 19:2839-2846
    • (2004) Eur J Neurosci , vol.19 , pp. 2839-2846
    • Klyubin, I.1    Walsh, D.M.2    Cullen, W.K.3
  • 22
    • 21044453723 scopus 로고    scopus 로고
    • Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo
    • Klyubin I, Walsh DM, Lemere CA et al (2005) Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo. Nat Med 11:556-561
    • (2005) Nat Med , vol.11 , pp. 556-561
    • Klyubin, I.1    Walsh, D.M.2    Lemere, C.A.3
  • 23
    • 19944429503 scopus 로고    scopus 로고
    • ApoE isoform-specific effects on LTP: Blockade by oligomeric amyloid-beta1-42
    • Trommer BL, Shah C, Yun SH et al (2005) ApoE isoform-specific effects on LTP: blockade by oligomeric amyloid-beta1-42. Neurobiol Dis 18:75-82
    • (2005) Neurobiol Dis , vol.18 , pp. 75-82
    • Trommer, B.L.1    Shah, C.2    Yun, S.H.3
  • 24
    • 0037059598 scopus 로고    scopus 로고
    • Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus
    • Wang HW, Pasternak JF, Kuo H et al (2002) Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain Res 924:133-140
    • (2002) Brain Res , vol.924 , pp. 133-140
    • Wang, H.W.1    Pasternak, J.F.2    Kuo, H.3
  • 25
    • 0034069795 scopus 로고    scopus 로고
    • Impairment of hippocampal long-term potentiation by Alzheimer amyloid beta-peptides
    • Chen QS, Kagan BL, Hirakura Y et al (2000) Impairment of hippocampal long-term potentiation by Alzheimer amyloid beta-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
  • 26
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • Cleary JP, Walsh DM, Hofmeister JJ et al (2005) Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci 8:79-84
    • (2005) Nat Neurosci , vol.8 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3
  • 27
    • 0035433962 scopus 로고    scopus 로고
    • Alzheimer's disease and Abeta toxicity: From top to bottom
    • Small DH, Mok SS, Bornstein JC (2001) Alzheimer's disease and Abeta 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
  • 28
    • 33751535253 scopus 로고    scopus 로고
    • Involvement of the nitric oxide pathway in synaptic dysfunction following amyloid elevation in Alzheimer's disease
    • Puzzo D, Palmeri A, Arancio O (2006) Involvement of the nitric oxide pathway in synaptic dysfunction following amyloid elevation in Alzheimer's disease. Rev Neurosci 17:497-523
    • (2006) Rev Neurosci , vol.17 , pp. 497-523
    • Puzzo, D.1    Palmeri, A.2    Arancio, O.3
  • 29
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid beta-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 DM, Rowan MJ et al (2004) Block of long-term potentiation by naturally secreted and synthetic amyloid beta-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
  • 30
    • 0041344592 scopus 로고    scopus 로고
    • Activation of the c-Jun N-terminal kinase signaling cascade mediates the effect of amyloid-beta on long term potentiation and cell death in hippocampus: A role for interleukin-1beta?
    • Minogue AM, Schmid AW, Fogarty MP et al (2003) Activation of the c-Jun N-terminal kinase signaling cascade mediates the effect of amyloid-beta on long term potentiation and cell death in hippocampus: a role for interleukin-1beta? J Biol Chem 278:27971-27980
    • (2003) J Biol Chem , vol.278 , pp. 27971-27980
    • Minogue, A.M.1    Schmid, A.W.2    Fogarty, M.P.3
  • 31
    • 33745985711 scopus 로고    scopus 로고
    • ERK1/2 activation mediates Abeta oligomer-induced neurotoxicity via caspase-3 activation and tau cleavage in rat organotypic hippocampal slice cultures
    • Chong YH, Shin YJ, Lee EO et al (2006) ERK1/2 activation mediates Abeta oligomer-induced neurotoxicity via caspase-3 activation and tau cleavage in rat organotypic hippocampal slice cultures. J Biol Chem 281:20315-20325
    • (2006) J Biol Chem , vol.281 , pp. 20315-20325
    • Chong, Y.H.1    Shin, Y.J.2    Lee, E.O.3
  • 32
    • 2442711560 scopus 로고    scopus 로고
    • Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice
    • Chin J, Palop JJ, Yu GQ et al (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
  • 34
    • 23044445669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking by amyloid-beta
    • Snyder EM, Nong Y, Almeida CG et al (2005) Regulation of NMDA receptor trafficking by amyloid-beta. Nat Neurosci 8:1051-1058
    • (2005) Nat Neurosci , vol.8 , pp. 1051-1058
    • Snyder, E.M.1    Nong, Y.2    Almeida, C.G.3
  • 35
    • 0037197836 scopus 로고    scopus 로고
    • Tau is essential to beta-amyloid-induced neurotoxicity
    • Rapoport M, Dawson HN, Binder LI et al (2002) Tau is essential to beta-amyloid-induced neurotoxicity. Proc Natl Acad Sci USA 99:6364-6369
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6364-6369
    • Rapoport, M.1    Dawson, H.N.2    Binder, L.I.3
  • 36
    • 33750072653 scopus 로고    scopus 로고
    • Regulation of phosphorylation of tau by cyclin-dependent kinase 5 and glycogen synthase kinase-3 at substrate level
    • Sengupta A, Novak M, Grundke-Iqbal I et al (2006) Regulation of phosphorylation of tau by cyclin-dependent kinase 5 and glycogen synthase kinase-3 at substrate level. FEBS Lett 580:5925-5933
    • (2006) FEBS Lett , vol.580 , pp. 5925-5933
    • Sengupta, A.1    Novak, M.2    Grundke-Iqbal, I.3
  • 37
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin WL et al (2001) Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293:1487-1491
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3
  • 38
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J, Chen F, van Dorpe J et al (2001) Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science 293:1491-1495
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3
  • 39
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ et al (2007) Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 316:750-754
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3
  • 40
    • 22144455300 scopus 로고    scopus 로고
    • Surface behavior and lipid interaction of Alzheimer {beta}-amyloid peptide 1-42:a membrane-disrupting peptide
    • Ambroggio EE, Kim DH, Separovic F et al (2005) Surface behavior and lipid interaction of Alzheimer {beta}-amyloid peptide 1-42:a membrane-disrupting peptide. Biophys J 88:2706-2713
    • (2005) Biophys J , vol.88 , pp. 2706-2713
    • Ambroggio, E.E.1    Kim, D.H.2    Separovic, F.3
  • 41
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: Evidence for AbetaP channel-mediated cellular toxicity
    • Bhatia R, Lin H, Lal R (2000) Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity. FASEB J 14:1233-1243
    • (2000) FASEB J , vol.14 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 42
    • 31344436145 scopus 로고    scopus 로고
    • Amyloid-beta peptide disruption of lipid membranes and the effect of metal ions
    • Lau TL, Ambroggio EE, Tew DJ et al (2006) Amyloid-beta peptide disruption of lipid membranes and the effect of metal ions. J Mol Biol 356:759-770
    • (2006) J Mol Biol , vol.356 , pp. 759-770
    • Lau, T.L.1    Ambroggio, E.E.2    Tew, D.J.3
  • 43
    • 0344936729 scopus 로고    scopus 로고
    • Possible causes of Alzheimer's disease: Amyloid fragments, free radicals, and calcium homeostasis
    • Holscher C (1998) Possible causes of Alzheimer's disease: amyloid fragments, free radicals, and calcium homeostasis. Neurobiol Dis 5:129-141
    • (1998) Neurobiol Dis , vol.5 , pp. 129-141
    • Holscher, C.1
  • 44
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin H, Bhatia R, Lal R (2001) Amyloid beta 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
  • 45
    • 0034856924 scopus 로고    scopus 로고
    • Diversity of amyloid beta protein fragment [1-40]-formed channels
    • Kourie JI, Henry CL, Farrelly P (2001) Diversity of amyloid beta protein fragment [1-40]-formed channels. Cell Mol Neurobiol 21:255-284
    • (2001) Cell Mol Neurobiol , vol.21 , pp. 255-284
    • Kourie, J.I.1    Henry, C.L.2    Farrelly, P.3
  • 46
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A, Mina E, Kayed R et al (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294-17300
    • (2005) J Biol Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3
  • 47
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL et al (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300:486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 48
    • 0036369164 scopus 로고    scopus 로고
    • Heterogeneous amyloid-formed ion channels as a common cytotoxic mechanism: Implications for therapeutic strategies against amyloidosis
    • Kourie JI, Culverson AL, Farrelly PV et al (2002) Heterogeneous amyloid-formed ion channels as a common cytotoxic mechanism: implications for therapeutic strategies against amyloidosis. Cell Biochem Biophys 36:191-207
    • (2002) Cell Biochem Biophys , vol.36 , pp. 191-207
    • Kourie, J.I.1    Culverson, A.L.2    Farrelly, P.V.3
  • 49
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • Verdier Y, Zarandi M, Penke B (2004) Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J Pept Sci 10:229-248
    • (2004) J Pept Sci , vol.10 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 50
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • Yan SD, Chen X, Fu J et al (1996) RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382:685-691
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3
  • 51
    • 8144223671 scopus 로고    scopus 로고
    • RAGE potentiates Abeta-induced perturbation of neuronal function in transgenic mice
    • Arancio O, Zhang HP, Chen X et al (2004) RAGE potentiates Abeta-induced perturbation of neuronal function in transgenic mice. EMBO J 23:4096-4105
    • (2004) EMBO J , vol.23 , pp. 4096-4105
    • Arancio, O.1    Zhang, H.P.2    Chen, X.3
  • 52
    • 0034521392 scopus 로고    scopus 로고
    • Clearance of Alzheimer's amyloid-beta(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier
    • Shibata M, Yamada S, Kumar SR et al (2000) Clearance of Alzheimer's amyloid-beta(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier. J Clin Invest 106:1489-1499
    • (2000) J Clin Invest , vol.106 , pp. 1489-1499
    • Shibata, M.1    Yamada, S.2    Kumar, S.R.3
  • 53
    • 4043061467 scopus 로고    scopus 로고
    • LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms
    • Deane R, Wu Z, Sagare A et al (2004) LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms. Neuron 43:333-344
    • (2004) Neuron , vol.43 , pp. 333-344
    • Deane, R.1    Wu, Z.2    Sagare, A.3
  • 54
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP et al (2007) Abeta oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282:11590-11601
    • (2007) J Biol Chem , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3
  • 55
    • 0028944873 scopus 로고
    • Interaction of beta-amyloid peptides with integrins in a human nerve cell line
    • Sabo S, Lambert MP, Kessey K et al (1995) Interaction of beta-amyloid peptides with integrins in a human nerve cell line. Neurosci Lett 184:25-28
    • (1995) Neurosci Lett , vol.184 , pp. 25-28
    • Sabo, S.1    Lambert, M.P.2    Kessey, K.3
  • 56
    • 0037135272 scopus 로고    scopus 로고
    • Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
    • Bi X, Gall CM, Zhou J et al (2002) Uptake and pathogenic effects of amyloid beta peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists. Neuroscience 112:827-840
    • (2002) Neuroscience , vol.112 , pp. 827-840
    • Bi, X.1    Gall, C.M.2    Zhou, J.3
  • 57
    • 33745894132 scopus 로고    scopus 로고
    • Does the p75 neurotrophin receptor mediate Abeta-induced toxicity in Alzheimer's disease?
    • Coulson EJ (2006) Does the p75 neurotrophin receptor mediate Abeta-induced toxicity in Alzheimer's disease? J Neurochem 98:654-660
    • (2006) J Neurochem , vol.98 , pp. 654-660
    • Coulson, E.J.1
  • 58
    • 0042738968 scopus 로고    scopus 로고
    • P75 neurotrophin receptor protects primary cultures of human neurons against extracellular amyloid beta peptide cytotoxicity
    • Zhang Y, Hong Y, Bounhar Y et al (2003) p75 neurotrophin receptor protects primary cultures of human neurons against extracellular amyloid beta peptide cytotoxicity. J Neurosci 23:7385-7394
    • (2003) J Neurosci , vol.23 , pp. 7385-7394
    • Zhang, Y.1    Hong, Y.2    Bounhar, Y.3
  • 59
    • 0036534870 scopus 로고    scopus 로고
    • Role of p75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines
    • Perini G, Della-Bianca V, Politi V et al (2002) Role of p75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines. J Exp Med 195:907-918
    • (2002) J Exp Med , vol.195 , pp. 907-918
    • Perini, G.1    Della-Bianca, V.2    Politi, V.3
  • 60
    • 19944433571 scopus 로고    scopus 로고
    • Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta1-42
    • Crouch PJ, Blake R, Duce JA et al (2005) Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta1-42. J Neurosci 25:672-679
    • (2005) J Neurosci , vol.25 , pp. 672-679
    • Crouch, P.J.1    Blake, R.2    Duce, J.A.3
  • 61
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L, Prabhu BM, Galati DF et al (2006) Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J Neurosci 26:9057-9068
    • (2006) J Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3
  • 62
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of a beta accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E et al (2006) Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 15:1437-1449
    • (2006) Hum Mol Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3
  • 63
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Abeta: A potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • Caspersen C, Wang N, Yao J et al (2005) Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J 19:2040-2041
    • (2005) FASEB J , vol.19 , pp. 2040-2041
    • Caspersen, C.1    Wang, N.2    Yao, J.3
  • 64
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C et al (2004) ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 304:448-452
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 65
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction
    • Takuma K, Yao J, Huang J et al (2005) ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction. FASEB J 19:597-598
    • (2005) FASEB J , vol.19 , pp. 597-598
    • Takuma, K.1    Yao, J.2    Huang, J.3
  • 66
    • 0035029801 scopus 로고    scopus 로고
    • Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons
    • White AR, Guirguis R, Brazier MW et al (2001) Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons. Neurobiol Dis 8:299-316
    • (2001) Neurobiol Dis , vol.8 , pp. 299-316
    • White, A.R.1    Guirguis, R.2    Brazier, M.W.3
  • 67
    • 0032433258 scopus 로고    scopus 로고
    • Beta-amyloid induces local neurite degeneration in cultured hippocampal neurons: Evidence for neuritic apoptosis
    • Ivins KJ, Bui ET, Cotman CW (1998) Beta-amyloid induces local neurite degeneration in cultured hippocampal neurons: evidence for neuritic apoptosis. Neurobiol Dis 5:365-378
    • (1998) Neurobiol Dis , vol.5 , pp. 365-378
    • Ivins, K.J.1    Bui, E.T.2    Cotman, C.W.3
  • 68
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N et al (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403:98-103
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3
  • 69
    • 4644276796 scopus 로고    scopus 로고
    • Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model
    • Casas C, Sergeant N, Itier JM et al (2004) Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model. Am J Pathol 165:1289-1300
    • (2004) Am J Pathol , vol.165 , pp. 1289-1300
    • Casas, C.1    Sergeant, N.2    Itier, J.M.3
  • 70
    • 33847732649 scopus 로고    scopus 로고
    • Ultrastructural localization of intraneuronal Abeta-peptide in Alzheimer disease brains
    • Gomez-Ramos P, Asuncion Moran M (2007) Ultrastructural localization of intraneuronal Abeta-peptide in Alzheimer disease brains. J Alzheimers Dis 11:53-59
    • (2007) J Alzheimers Dis , vol.11 , pp. 53-59
    • Gomez-Ramos, P.1    Asuncion Moran, M.2
  • 71
    • 33947261641 scopus 로고    scopus 로고
    • Intraneuronal Abeta immunoreactivity is not a predictor of brain amyloidosis-beta or neurofibrillary degeneration
    • Wegiel J, Kuchna I, Nowicki K et al (2007) Intraneuronal Abeta immunoreactivity is not a predictor of brain amyloidosis-beta or neurofibrillary degeneration. Acta Neuropathol (Berl) 113:389-402
    • (2007) Acta Neuropathol (Berl) , vol.113 , pp. 389-402
    • Wegiel, J.1    Kuchna, I.2    Nowicki, K.3
  • 72
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
    • Butterfield DA, Perluigi M, Sultana R (2006) Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics. Eur J Pharmacol 545:39-50
    • (2006) Eur J Pharmacol , vol.545 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 73
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R et al (1994) Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77:817-827
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3
  • 74
    • 0034733705 scopus 로고    scopus 로고
    • Evidence that the beta-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Abeta by zinc
    • Cuajungco MP, Goldstein LE, Nunomura A et al (2000) Evidence that the beta-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Abeta by zinc. J Biol Chem 275:19439-19442
    • (2000) J Biol Chem , vol.275 , pp. 19439-19442
    • Cuajungco, M.P.1    Goldstein, L.E.2    Nunomura, A.3
  • 75
    • 18344414746 scopus 로고    scopus 로고
    • The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal reduction
    • Huang X, Atwood CS, Hartshorn MA et al (1999) The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal reduction. Biochemistry 38:7609-7616
    • (1999) Biochemistry , vol.38 , pp. 7609-7616
    • Huang, X.1    Atwood, C.S.2    Hartshorn, M.A.3
  • 76
    • 0033601338 scopus 로고    scopus 로고
    • Cu(II) potentiation of alzheimer abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction
    • Huang X, Cuajungco MP, Atwood CS et al (1999) Cu(II) potentiation of alzheimer abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction. J Biol Chem 274:37111-37116
    • (1999) J Biol Chem , vol.274 , pp. 37111-37116
    • Huang, X.1    Cuajungco, M.P.2    Atwood, C.S.3
  • 77
    • 0242290357 scopus 로고    scopus 로고
    • Neurotoxic, redox-competent Alzheimer's beta-amyloid is released from lipid membrane by methionine oxidation
    • Barnham KJ, Ciccotosto GD, Tickler AK et al (2003) Neurotoxic, redox-competent Alzheimer's beta-amyloid is released from lipid membrane by methionine oxidation. J Biol Chem 278:42959-42965
    • (2003) J Biol Chem , vol.278 , pp. 42959-42965
    • Barnham, K.J.1    Ciccotosto, G.D.2    Tickler, A.K.3
  • 78
    • 5644291904 scopus 로고    scopus 로고
    • Enhanced toxicity and cellular binding of a modified amyloid beta peptide with a methionine to valine substitution
    • Ciccotosto GD, Tew D, Curtain CC et al (2004) Enhanced toxicity and cellular binding of a modified amyloid beta peptide with a methionine to valine substitution. J Biol Chem 279:42528-42534
    • (2004) J Biol Chem , vol.279 , pp. 42528-42534
    • Ciccotosto, G.D.1    Tew, D.2    Curtain, C.C.3
  • 79
    • 20444418652 scopus 로고    scopus 로고
    • Methionine regulates copper/hydrogen peroxide oxidation products of Abeta
    • Ali FE, Separovic F, Barrow CJ et al (2005) Methionine regulates copper/hydrogen peroxide oxidation products of Abeta. J Pept Sci 11:353-360
    • (2005) J Pept Sci , vol.11 , pp. 353-360
    • Ali, F.E.1    Separovic, F.2    Barrow, C.J.3
  • 80
    • 3242715131 scopus 로고    scopus 로고
    • Rapid characterization of amyloid-beta side-chain oxidation by tandem mass spectrometry and the scoring algorithm for spectral analysis
    • Schiewe AJ, Margol L, Soreghan BA et al (2004) Rapid characterization of amyloid-beta side-chain oxidation by tandem mass spectrometry and the scoring algorithm for spectral analysis. Pharm Res 21:1094-1102
    • (2004) Pharm Res , vol.21 , pp. 1094-1102
    • Schiewe, A.J.1    Margol, L.2    Soreghan, B.A.3
  • 81
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain CC, Ali F, Volitakis I et al (2001) Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J Biol Chem 276:20466-20473
    • (2001) J Biol Chem , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3
  • 82
    • 0036592636 scopus 로고    scopus 로고
    • Amyloid beta-peptide and amyloid pathology are central to the oxidative stress and inflammatory cascades under which Alzheimer's disease brain exists
    • Butterfield DA, Griffin S, Munch G et al (2002) Amyloid beta-peptide and amyloid pathology are central to the oxidative stress and inflammatory cascades under which Alzheimer's disease brain exists. J Alzheimers Dis 4:193-201
    • (2002) J Alzheimers Dis , vol.4 , pp. 193-201
    • Butterfield, D.A.1    Griffin, S.2    Munch, G.3
  • 83
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's a beta(1-42) and a beta(25-35)
    • Varadarajan S, Kanski J, Aksenova M et al (2001) Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A beta(1-42) and A beta(25-35). J Am Chem Soc 123:5625-5631
    • (2001) J Am Chem Soc , vol.123 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3
  • 84
    • 0036127328 scopus 로고    scopus 로고
    • Redox properties of Met(35) in neurotoxic beta-amyloid peptide. a molecular modeling study
    • Pogocki D, Schoneich C (2002) Redox properties of Met(35) in neurotoxic beta-amyloid peptide. A molecular modeling study. Chem Res Toxicol 15:408-418
    • (2002) Chem Res Toxicol , vol.15 , pp. 408-418
    • Pogocki, D.1    Schoneich, C.2
  • 85
    • 0028106152 scopus 로고
    • Relative abundance of Alzheimer Abeta amyloid peptide variants in Alzheimer disease and normal aging
    • Naslund J, Schierhorn A, Hellman U et al (1994) Relative abundance of Alzheimer Abeta amyloid peptide variants in Alzheimer disease and normal aging. Proc Natl Acad Sci U S A 91:8378-8382
    • (1994) Proc Natl Acad Sci U S a , vol.91 , pp. 8378-8382
    • Naslund, J.1    Schierhorn, A.2    Hellman, U.3
  • 86
    • 0035918312 scopus 로고    scopus 로고
    • Comparative analysis of amyloid-beta chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains
    • Kuo YM, Kokjohn TA, Beach TG et al (2001) Comparative analysis of amyloid-beta chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains. J Biol Chem 276:12991-12998
    • (2001) J Biol Chem , vol.276 , pp. 12991-12998
    • Kuo, Y.M.1    Kokjohn, T.A.2    Beach, T.G.3
  • 87
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence
    • Dong J, Atwood CS, Anderson VE et al (2003) Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42:2768-2773
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3
  • 88
    • 34250898788 scopus 로고    scopus 로고
    • Effect of aldehydes derived from oxidative deamination and oxidative stress on beta-amyloid aggregation; Pathological implications to Alzheimer's disease
    • Chen K, Kazachkov M, Yu PH (2007) Effect of aldehydes derived from oxidative deamination and oxidative stress on beta-amyloid aggregation; pathological implications to Alzheimer's disease. J Neural Transm 114:835-839
    • (2007) J Neural Transm , vol.114 , pp. 835-839
    • Chen, K.1    Kazachkov, M.2    Yu, P.H.3
  • 89
    • 0344687267 scopus 로고    scopus 로고
    • Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide
    • Ali FE, Barnham KJ, Barrow CJ et al (2004) Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide. J Inorg Biochem 98:173-184
    • (2004) J Inorg Biochem , vol.98 , pp. 173-184
    • Ali, F.E.1    Barnham, K.J.2    Barrow, C.J.3
  • 90
    • 0031985973 scopus 로고    scopus 로고
    • Molecular mechanisms of cellular injury produced by neurotoxic amino acids that generate reactive oxygen species
    • Metodiewa D (1998) Molecular mechanisms of cellular injury produced by neurotoxic amino acids that generate reactive oxygen species. Amino Acids 14:181-187
    • (1998) Amino Acids , vol.14 , pp. 181-187
    • Metodiewa, D.1
  • 91
    • 0032806289 scopus 로고    scopus 로고
    • Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine
    • Leeuwenburgh C, Hansen PA, Holloszy JO et al (1999) Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine. Free Radic Biol Med 27:186-192
    • (1999) Free Radic Biol Med , vol.27 , pp. 186-192
    • Leeuwenburgh, C.1    Hansen, P.A.2    Holloszy, J.O.3
  • 92
    • 0031678044 scopus 로고    scopus 로고
    • Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease
    • Lovell MA, Xie C, Markesbery WR (1998) Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease. Neurology 51:1562-1566
    • (1998) Neurology , vol.51 , pp. 1562-1566
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 93
    • 9144235443 scopus 로고    scopus 로고
    • Copper mediates dityrosine cross-linking of Alzheimer's amyloid-beta
    • Atwood CS, Perry G, Zeng H et al (2004) Copper mediates dityrosine cross-linking of Alzheimer's amyloid-beta. Biochemistry 43:560-568
    • (2004) Biochemistry , vol.43 , pp. 560-568
    • Atwood, C.S.1    Perry, G.2    Zeng, H.3
  • 95
    • 9444284334 scopus 로고    scopus 로고
    • Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid
    • Barnham KJ, Haeffner F, Ciccotosto GD et al (2004) Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid. FASEB J 18:1427-1429
    • (2004) FASEB J , vol.18 , pp. 1427-1429
    • Barnham, K.J.1    Haeffner, F.2    Ciccotosto, G.D.3
  • 96
    • 0022550027 scopus 로고
    • Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein
    • Roher A, Wolfe D, Palutke M et al (1986) Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein. Proc Natl Acad Sci USA 83:2662-2666
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2662-2666
    • Roher, A.1    Wolfe, D.2    Palutke, M.3
  • 97
    • 33646490404 scopus 로고    scopus 로고
    • 1,1′-Xylyl bis-1,4,8,11-tetraaza cyclotetradecane: A new potential copper chelator agent for neuroprotection in Alzheimer's disease. Its comparative effects with clioquinol on rat brain copper distribution
    • Moret V, Laras Y, Pietrancosta N et al (2006) 1,1′-Xylyl bis-1,4,8,11-tetraaza cyclotetradecane: a new potential copper chelator agent for neuroprotection in Alzheimer's disease. Its comparative effects with clioquinol on rat brain copper distribution. Bioorg Med Chem Lett 16:3298-3301
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 3298-3301
    • Moret, V.1    Laras, Y.2    Pietrancosta, N.3
  • 98
    • 4644238758 scopus 로고    scopus 로고
    • The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice
    • Lee JY, Friedman JE, Angel I et al (2004) The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice. Neurobiol Aging 25:1315-1321
    • (2004) Neurobiol Aging , vol.25 , pp. 1315-1321
    • Lee, J.Y.1    Friedman, J.E.2    Angel, I.3
  • 99
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME et al (2001) Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30:665-676
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3
  • 100
    • 33644843098 scopus 로고    scopus 로고
    • In vivo protection by the xanthate tricyclodecan-9-yl-xanthogenate against amyloid beta-peptide (1-42)-induced oxidative stress
    • Perluigi M, Joshi G, Sultana R et al (2006) In vivo protection by the xanthate tricyclodecan-9-yl-xanthogenate against amyloid beta-peptide (1-42)-induced oxidative stress. Neuroscience 138:1161-1170
    • (2006) Neuroscience , vol.138 , pp. 1161-1170
    • Perluigi, M.1    Joshi, G.2    Sultana, R.3
  • 101
    • 10744224267 scopus 로고    scopus 로고
    • Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: A pilot phase 2 clinical trial
    • Ritchie CW, Bush AI, Mackinnon A et al (2003) Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: a pilot phase 2 clinical trial. Arch Neurol 60:1685-1691
    • (2003) Arch Neurol , vol.60 , pp. 1685-1691
    • Ritchie, C.W.1    Bush, A.I.2    MacKinnon, A.3
  • 102
    • 33745860362 scopus 로고    scopus 로고
    • Degradation of the Alzheimer disease amyloid beta-peptide by metal-dependent up-regulation of metalloprotease activity
    • White AR, Du T, Laughton KM et al (2006) Degradation of the Alzheimer disease amyloid beta-peptide by metal-dependent up-regulation of metalloprotease activity. J Biol Chem 281:17670-17680
    • (2006) J Biol Chem , vol.281 , pp. 17670-17680
    • White, A.R.1    Du, T.2    Laughton, K.M.3
  • 103
    • 33846013897 scopus 로고    scopus 로고
    • Therapeutic treatments for Alzheimer's disease based on metal bioavailability
    • Crouch PJ, Barnham KJ, Bush AI et al (2006) Therapeutic treatments for Alzheimer's disease based on metal bioavailability. Drug News Perspect 19:469-474
    • (2006) Drug News Perspect , vol.19 , pp. 469-474
    • Crouch, P.J.1    Barnham, K.J.2    Bush, A.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.