메뉴 건너뛰기




Volumn 2, Issue 4, 2007, Pages 397-409

Molecular determinants of Alzheimer's disease Aβ peptide neurotoxicity

Author keywords

A ; Alzheimer's disease; Amyloid; Metal; Neurodegeneration; Oligomer; Oxidative stress; Synapse; Tau; Toxicity

Indexed keywords

1,1' XYLYLBIS(1,4,8,11 TETRAAZACYCLOTETRADECANE); ALPHA SECRETASE; ALPHA TOCOPHEROL; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; ANTIOXIDANT; ASCORBIC ACID; BETA SECRETASE; CHELATING AGENT; CLIOQUINOL; COPPER ION; CURCUMIN; CYCLAM DERIVATIVE; DP 109; GINKGO BILOBA EXTRACT; GOSSYPINE; JKL 169; MELATONIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PLACEBO; TRIENTINE; UNCLASSIFIED DRUG; ZINC;

EID: 34447345723     PISSN: 14796708     EISSN: None     Source Type: Journal    
DOI: 10.2217/14796708.2.4.397     Document Type: Review
Times cited : (9)

References (126)
  • 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: The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297(5580), 353-356 (2002).
    • (2002) Science , vol.297 , Issue.5580 , 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, Villemagne VL: Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics. J. Neurochem. 97(6), 1700-1725 (2006).
    • (2006) J. Neurochem , vol.97 , Issue.6 , pp. 1700-1725
    • Masters, C.L.1    Cappai, R.2    Barnham, K.J.3    Villemagne, V.L.4
  • 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.: The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325(6106), 733-736 (1987).
    • (1987) Nature , vol.325 , Issue.6106 , 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.: Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359, 322-325 (1992).
    • (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: 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(18), 4693-4697 (1993).
    • (1993) Biochemistry , vol.32 , Issue.18 , 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 Aβ peptides
    • Liao MQ, Tzeng YJ, Chang LY et al.: The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Aβ peptides. FEBS Lett. 581(6), 1161-1165 (2007).
    • (2007) FEBS Lett , vol.581 , Issue.6 , 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: Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 250(4978), 279-282 (1990).
    • (1990) Science , vol.250 , Issue.4978 , 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, Glabe CG, Cotman CW: Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13(4), 1676-1687 (1993).
    • (1993) J. Neurosci , vol.13 , Issue.4 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 9
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW: In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563(1-2), 311-314 (1991).
    • (1991) Brain Res , vol.563 , Issue.1-2 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 10
    • 0025733411 scopus 로고
    • Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures
    • Pike CL, Walencewicz AJ, Glabe CG, Cotman CW: Aggregation-related toxicity of synthetic β-amyloid protein in hippocampal cultures. Eur. J. Pharmacol. 207(4), 367-368 (1991).
    • (1991) Eur. J. Pharmacol , vol.207 , Issue.4 , pp. 367-368
    • Pike, C.L.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 11
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV et al.: Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (6880), 535-539 (2002).
    • (2002) Nature , vol.416 , Issue.6880 , 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 Aβ1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA et al.: Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc. Natl Acad. Sci. USA 95(11), 6448-6453 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , Issue.11 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 13
    • 33947265861 scopus 로고    scopus 로고
    • 2+ induced aggregation and dityrosine formation of the Alzheimer's disease amyloid-β peptide
    • 2+ induced aggregation and dityrosine formation of the Alzheimer's disease amyloid-β peptide. Biochemistry 46(10), 2881-2891 (2007).
    • (2007) Biochemistry , vol.46 , Issue.10 , pp. 2881-2891
    • Smith, D.P.1    Ciccotosto, G.D.2    Tew, D.J.3
  • 14
    • 27644493692 scopus 로고    scopus 로고
    • Globular amyloid β-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease
    • Barghorn S, Nimmrich V, Striebinger A et al.: Globular amyloid β-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease. J. Neurochem. 95(3), 834-847 (2005).
    • (2005) J. Neurochem , vol.95 , Issue.3 , pp. 834-847
    • Barghorn, S.1    Nimmrich, V.2    Striebinger, A.3
  • 15
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-β protein assembly in the brain impairs memory
    • Lesne S, Koh MT, Kotilinek L et al.: A specific amyloid-β protein assembly in the brain impairs memory. Nature 440(7082), 352-357 (2006).
    • (2006) Nature , vol.440 , Issue.7082 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 16
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean CA, Cherny RA, Fraser FW et al.: Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 46 (6), 860-866 (1999).
    • (1999) Ann. Neurol , vol.46 , Issue.6 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3
  • 17
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • Lue LF, Kuo YM, Roher AE et al.: Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol. 155(3), 853-862 (1999).
    • (1999) Am. J. Pathol , vol.155 , Issue.3 , 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 Aβ distinguish Alzheimer's disease from normal and pathologic aging
    • Wang J, Dickson DW, Trojanowski JQ, Lee VM: The levels of soluble versus insoluble brain Aβ distinguish Alzheimer's disease from normal and pathologic aging. Exp. Neurol. 158(2), 328-337 (1999).
    • (1999) Exp. Neurol , vol.158 , Issue.2 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 19
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline
    • Naslund J, Haroutunian V, Mohs R et al.: Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. JAMA 283(12), 1571-1577 (2000).
    • (2000) JAMA , vol.283 , Issue.12 , pp. 1571-1577
    • Naslund, J.1    Haroutunian, V.2    Mohs, R.3
  • 20
    • 33745552613 scopus 로고    scopus 로고
    • Amyloid-β1-42 reduces neuronal excitability in mouse dentate gyrus
    • Yun SH, Gamkrelidze G, Stine WB et al.: Amyloid-β1-42 reduces neuronal excitability in mouse dentate gyrus. Neurosci. Lett. 403(1-2), 162-165 (2006).
    • (2006) Neurosci. Lett , vol.403 , Issue.1-2 , pp. 162-165
    • Yun, S.H.1    Gamkrelidze, G.2    Stine, W.B.3
  • 21
    • 2942626182 scopus 로고    scopus 로고
    • Soluble arctic amyloid β protein inhibits hippocampal long-term potentiation in vivo
    • Klyubin I, Walsh DM, Cullen WK et al.: Soluble arctic amyloid β protein inhibits hippocampal long-term potentiation in vivo. Eur. J. Neurosci. 19(10), 2839-2846 (2004).
    • (2004) Eur. J. Neurosci , vol.19 , Issue.10 , pp. 2839-2846
    • Klyubin, I.1    Walsh, D.M.2    Cullen, W.K.3
  • 22
    • 21044453723 scopus 로고    scopus 로고
    • Amyloid β protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo
    • Klyubin I, Walsh DM, Lemere CA et al.: Amyloid β protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo. Nat. Med. 11(5), 556-561 (2005).
    • (2005) Nat. Med , vol.11 , Issue.5 , 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-β1-42
    • Trommer BL, Shah C, Yun SH et al.: ApoE isoform-specific effects on LTP: blockade by oligomeric amyloid-β1-42. Neurobiol. Dis. 18(1), 75-82 (2005).
    • (2005) Neurobiol. Dis , vol.18 , Issue.1 , pp. 75-82
    • Trommer, B.L.1    Shah, C.2    Yun, S.H.3
  • 24
    • 0037059598 scopus 로고    scopus 로고
    • Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus
    • Wang HW, Pasternak JF, Kuo H et al.: Soluble oligomers of β amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain Res. 924(2), 133-140 (2002).
    • (2002) Brain Res , vol.924 , Issue.2 , 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 β-peptides
    • Chen QS, Kagan BL, Hirakura Y, Xie CW: Impairment of hippocampal long-term potentiation by Alzheimer amyloid β-peptides. J. Neurosci. Res. 60(1), 65-72 (2000).
    • (2000) J. Neurosci. Res , vol.60 , Issue.1 , pp. 65-72
    • Chen, Q.S.1    Kagan, B.L.2    Hirakura, Y.3    Xie, C.W.4
  • 26
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
    • Cleary JP, Walsh DM, Hofmeister JJ et al.: Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nat. Neurosci. 8(1), 79-84 (2005).
    • (2005) Nat. Neurosci , vol.8 , Issue.1 , 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 Aβ toxicity: From top to bottom
    • Small DH, Mok SS, Bornstein JC: Alzheimer's disease and Aβ toxicity: from top to bottom. Nat. Rev. Neurosci. 2(8), 595-598 (2001).
    • (2001) Nat. Rev. Neurosci , vol.2 , Issue.8 , 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: Involvement of the nitric oxide pathway in synaptic dysfunction following amyloid elevation in Alzheimer's disease. Rev. Neurosci. 17(5), 497-523 (2006).
    • (2006) Rev. Neurosci , vol.17 , Issue.5 , 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 β-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang Q, Walsh DM, Rowan MJ, Selkoe DJ, Anwyl R: Block of long-term potentiation by naturally secreted and synthetic amyloid β-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J. Neurosci. 24(13), 3370-3378 (2004).
    • (2004) J. Neurosci , vol.24 , Issue.13 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 30
    • 0041344592 scopus 로고    scopus 로고
    • Activation of the c-Jun N-terminal kinase signaling cascade mediates the effect of amyloid-β on long term potentiation and cell death in hippocampus: A role for interleukin-1β?
    • Minogue AM, Schmid AW, Fogarty MP et al.: Activation of the c-Jun N-terminal kinase signaling cascade mediates the effect of amyloid-β on long term potentiation and cell death in hippocampus: a role for interleukin-1β? J. Biol. Chem. 278(30), 27971-27980 (2003).
    • (2003) J. Biol. Chem , vol.278 , Issue.30 , 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 Aβ oligomer-induced neurotoxicity via caspase-3 activation and tau cleavage in rat organotypic hippocampal slice cultures
    • Chong YH, Shin YJ, Lee EO et al.: ERK1/2 activation mediates Aβ oligomer-induced neurotoxicity via caspase-3 activation and tau cleavage in rat organotypic hippocampal slice cultures. J. Biol. Chem. 281(29), 20315-20325 (2006).
    • (2006) J. Biol. Chem , vol.281 , Issue.29 , 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.: Fyn kinase modulates synaptotoxicity, but not aberrant sprouting, in human amyloid precursor protein transgenic mice. J. Neurosci. 24(19), 4692-4697 (2004).
    • (2004) J. Neurosci , vol.24 , Issue.19 , 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-β
    • Snyder EM, Nong Y, Almeida CG et al.: Regulation of NMDA receptor trafficking by amyloid-β. Nat. Neurosci. 8(8), 1051-1058 (2005).
    • (2005) Nat. Neurosci , vol.8 , Issue.8 , pp. 1051-1058
    • Snyder, E.M.1    Nong, Y.2    Almeida, C.G.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, Iqbal K: Regulation of phosphorylation of tau by cyclin-dependent kinase 5 and glycogen synthase kinase-3 at substrate level. FEBS Lett. 580(25), 5925-5933 (2006).
    • (2006) FEBS Lett , vol.580 , Issue.25 , pp. 5925-5933
    • Sengupta, A.1    Novak, M.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 37
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ 42 fibrils
    • Gotz J, Chen F, van Dorpe J, Nitsch RM: Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ 42 fibrils. Science 293(5534), 1491-1495 (2001).
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 38
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin WL et al.: Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293(5534), 1487-1491 (2001).
    • (2001) Science , vol.293 , Issue.5534 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3
  • 39
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ et al.: Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model. Science 316(5825), 750-754 (2007).
    • (2007) Science , vol.316 , Issue.5825 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3
  • 40
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin H, Bhatia R, Lal R: Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J. 15(13), 2433-2444. (2001).
    • (2001) FASEB J , vol.15 , Issue.13 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 41
    • 22144455300 scopus 로고    scopus 로고
    • Surface behavior and lipid interaction of Alzheimer β-amyloid peptide 1-42: A membrane-disrupting peptide
    • Ambroggio EE, Kim DH, Separovic F et al.: Surface behavior and lipid interaction of Alzheimer β-amyloid peptide 1-42: a membrane-disrupting peptide. Biophys. J. 88(4), 2706-2713 (2005).
    • (2005) Biophys. J , vol.88 , Issue.4 , pp. 2706-2713
    • Ambroggio, E.E.1    Kim, D.H.2    Separovic, F.3
  • 42
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid β protein (1-42) induces rapid cellular degeneration: Evidence for AβP channel-mediated cellular toxicity
    • Bhatia R, Lin H, Lal R: Fresh and globular amyloid β protein (1-42) induces rapid cellular degeneration: evidence for AβP channel-mediated cellular toxicity. FASEB J. 14(9), 1233-1243. (2000).
    • (2000) FASEB J , vol.14 , Issue.9 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 43
    • 31344436145 scopus 로고    scopus 로고
    • Amyloid-β peptide disruption of lipid membranes and the effect of metal ions
    • Lau TL, Ambroggio EE, Tew DJ et al.: Amyloid-β peptide disruption of lipid membranes and the effect of metal ions. J. Mol. Biol. 356(3), 759-770 (2006).
    • (2006) J. Mol. Biol , vol.356 , Issue.3 , pp. 759-770
    • Lau, T.L.1    Ambroggio, E.E.2    Tew, D.J.3
  • 44
    • 0344936729 scopus 로고    scopus 로고
    • Possible causes of Alzheimer's disease: Amyloid fragments, free radicals, and calcium homeostasis
    • Holscher C: Possible causes of Alzheimer's disease: amyloid fragments, free radicals, and calcium homeostasis. Neurobiol. Dis. 5(3), 129-141 (1998).
    • (1998) Neurobiol. Dis , vol.5 , Issue.3 , pp. 129-141
    • Holscher, C.1
  • 45
    • 0034856924 scopus 로고    scopus 로고
    • Diversity of amyloid β protein fragment [1-40]-formed channels
    • Kourie JI, Henry CL, Farrelly P: Diversity of amyloid β protein fragment [1-40]-formed channels. Cell. Mol. Neurobiol. 21(3), 255-284 (2001).
    • (2001) Cell. Mol. Neurobiol , vol.21 , Issue.3 , 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.: Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 280(17), 17294-17300 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.17 , 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.: Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300(5618), 486-489 (2003).
    • (2003) Science , vol.300 , Issue.5618 , 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, Henry CL, Laohachai KN: Heterogeneous amyloid-formed ion channels as a common cytotoxic mechanism: implications for therapeutic strategies against amyloidosis. Cell Biochem. Biophys. 36(2-3), 191-207 (2002).
    • (2002) Cell Biochem. Biophys , vol.36 , Issue.2-3 , pp. 191-207
    • Kourie, J.I.1    Culverson, A.L.2    Farrelly, P.V.3    Henry, C.L.4    Laohachai, K.N.5
  • 49
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid β-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • Verdier Y, Zarandi M, Penke B: Amyloid β-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J. Pept. Sci. 10(5), 229-248 (2004).
    • (2004) J. Pept. Sci , vol.10 , Issue.5 , 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.: RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382, 685-691 (1996).
    • (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 Aβ-induced perturbation of neuronal function in transgenic mice
    • Arancio O, Zhang HP, Chen X et al.: RAGE potentiates Aβ-induced perturbation of neuronal function in transgenic mice. EMBO J. 23(20), 4096-4105 (2004).
    • (2004) EMBO J , vol.23 , Issue.20 , pp. 4096-4105
    • Arancio, O.1    Zhang, H.P.2    Chen, X.3
  • 52
    • 0034521392 scopus 로고    scopus 로고
    • Clearance of Alzheimer's amyloid-β(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier
    • Shibata M, Yamada S, Kumar SR et al.: Clearance of Alzheimer's amyloid-β(1-40) peptide from brain by LDL receptor-related protein-1 at the blood-brain barrier. J. Clin. Invest. 106(12), 1489-1499 (2000).
    • (2000) J. Clin. Invest , vol.106 , Issue.12 , pp. 1489-1499
    • Shibata, M.1    Yamada, S.2    Kumar, S.R.3
  • 53
    • 4043061467 scopus 로고    scopus 로고
    • LRP/amyloid β-peptide interaction mediates differential brain efflux of Aβ isoforms
    • Deane R, Wu Z, Sagare A et al.: LRP/amyloid β-peptide interaction mediates differential brain efflux of Aβ isoforms. Neuron 43(3), 333-344 (2004).
    • (2004) Neuron , vol.43 , Issue.3 , pp. 333-344
    • Deane, R.1    Wu, Z.2    Sagare, A.3
  • 54
    • 34249672242 scopus 로고    scopus 로고
    • Aβ 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.: Aβ 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(15), 11590-11601 (2007).
    • (2007) J. Biol. Chem , vol.282 , Issue.15 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3
  • 55
    • 0028944873 scopus 로고
    • Interaction of β-amyloid peptides with integrins in a human nerve cell line
    • Sabo S, Lambert MP, Kessey K et al.: Interaction of β-amyloid peptides with integrins in a human nerve cell line. Neurosci. Lett. 184, 25-28 (1995).
    • (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 β peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
    • Bi X, Gall CM, Zhou J, Lynch G: Uptake and pathogenic effects of amyloid β peptide 1-42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists. Neuroscience 112(4), 827-840 (2002).
    • (2002) Neuroscience , vol.112 , Issue.4 , pp. 827-840
    • Bi, X.1    Gall, C.M.2    Zhou, J.3    Lynch, G.4
  • 57
    • 33745894132 scopus 로고    scopus 로고
    • Does the p75 neurotrophin receptor mediate Aβ-induced toxicity in Alzheimer's disease?
    • Coulson EJ: Does the p75 neurotrophin receptor mediate Aβ-induced toxicity in Alzheimer's disease? J. Neurochem. 98(3), 654-660 (2006).
    • (2006) J. Neurochem , vol.98 , Issue.3 , 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 β peptide cytotoxicity
    • Zhang Y, Hong Y, Bounhar Y et al.: p75 neurotrophin receptor protects primary cultures of human neurons against extracellular amyloid β peptide cytotoxicity. J. Neurosci. 23(19), 7385-7394 (2003).
    • (2003) J. Neurosci , vol.23 , Issue.19 , 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 β-amyloid peptides and synergistic effect of inflammatory cytokines
    • Perini G, Della-Bianca V, Politi V et al.: Role of p75 neurotrophin receptor in the neurotoxicity by β-amyloid peptides and synergistic effect of inflammatory cytokines. J. Exp. Med. 195(7), 907-918 (2002).
    • (2002) J. Exp. Med , vol.195 , Issue.7 , 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-β1-42
    • Crouch PJ, Blake R, Duce JA et al.: Copper-dependent inhibition of human cytochrome C oxidase by a dimeric conformer of amyloid-β1-42. J. Neurosci. 25(3), 672-679 (2005).
    • (2005) J. Neurosci , vol.25 , Issue.3 , 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, Avadhani NG, Anandatheerthavarada HK: Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J. Neurosci. 26(35), 9057-9068 (2006).
    • (2006) J. Neurosci , vol.26 , Issue.35 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 62
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of Aβ 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.: Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 15(9), 1437-1449 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , Issue.9 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3
  • 63
    • 28744449206 scopus 로고    scopus 로고
    • Mitochondrial Aβ: A potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
    • Caspersen C, Wang N, Yao J et al.: Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J. 19(14), 2040-2041 (2005).
    • (2005) FASEB J , vol.19 , Issue.14 , pp. 2040-2041
    • Caspersen, C.1    Wang, N.2    Yao, J.3
  • 64
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C et al.: ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease. Science 304(5669), 448-452 (2004).
    • (2004) Science , vol.304 , Issue.5669 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 65
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances Aβ-induced cell stress via mitochondrial dysfunction
    • Takuma K, Yao J, Huang J et al.: ABAD enhances Aβ-induced cell stress via mitochondrial dysfunction. FASEB J. 19(6), 597-598 (2005).
    • (2005) FASEB J , vol.19 , Issue.6 , 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 β peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons
    • White AR, Guirguis R, Brazier MW et al.: Sublethal concentrations of prion peptide PrP106-126 or the amyloid β peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons. Neurobiol. Dis. 8(2), 299-316 (2001).
    • (2001) Neurobiol. Dis , vol.8 , Issue.2 , pp. 299-316
    • White, A.R.1    Guirguis, R.2    Brazier, M.W.3
  • 67
    • 0032433258 scopus 로고    scopus 로고
    • β-amyloid induces local neurite degeneration in cultured hippocampal neurons: Evidence for neuritic apoptosis
    • Ivins KJ, Bui ET, Cotman CW: β-amyloid induces local neurite degeneration in cultured hippocampal neurons: evidence for neuritic apoptosis. Neurobiol. Dis. 5(5), 365-378 (1998).
    • (1998) Neurobiol. Dis , vol.5 , Issue.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-β
    • Nakagawa T, Zhu H, Morishima N et al.: Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature 403(6765), 98-103 (2000).
    • (2000) Nature , vol.403 , Issue.6765 , 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 Aβ42 accumulation in a novel Alzheimer transgenic model
    • Casas C, Sergeant N, Itier JM et al.: Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Aβ42 accumulation in a novel Alzheimer transgenic model. Am. J. Pathol. 165(4), 1289-1300 (2004).
    • (2004) Am. J. Pathol , vol.165 , Issue.4 , pp. 1289-1300
    • Casas, C.1    Sergeant, N.2    Itier, J.M.3
  • 70
    • 33847732649 scopus 로고    scopus 로고
    • Ultrastructural localization of intraneuronal Aβ-peptide in Alzheimer disease brains
    • Gomez-Ramos P, Asuncion Moran M: Ultrastructural localization of intraneuronal Aβ-peptide in Alzheimer disease brains. J. Alzheimers Dis. 11(1), 53-59 (2007).
    • (2007) J. Alzheimers Dis , vol.11 , Issue.1 , pp. 53-59
    • Gomez-Ramos, P.1    Asuncion Moran, M.2
  • 71
    • 33947261641 scopus 로고    scopus 로고
    • Intraneuronal Aβ immunoreactivity is not a predictor of brain amyloidosis-β or neurofibrillary degeneration
    • Wegiel J, Kuchna I, Nowicki K et al.: Intraneuronal Aβ immunoreactivity is not a predictor of brain amyloidosis-β or neurofibrillary degeneration. Acta Neuropathol. (Berl.) 113(4), 389-402 (2007).
    • (2007) Acta Neuropathol. (Berl.) , vol.113 , Issue.4 , pp. 389-402
    • Wegiel, J.1    Kuchna, I.2    Nowicki, K.3
  • 72
    • 0041817542 scopus 로고    scopus 로고
    • The amyloid β peptide (Aβ(1-40)) is thermodynamically soluble at physiological concentrations
    • Sengupta P, Garai K, Sahoo B et al.: The amyloid β peptide (Aβ(1-40)) is thermodynamically soluble at physiological concentrations. Biochemistry 42(35), 10506-10513 (2003).
    • (2003) Biochemistry , vol.42 , Issue.35 , pp. 10506-10513
    • Sengupta, P.1    Garai, K.2    Sahoo, B.3
  • 73
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • Bush AI: The metallobiology of Alzheimer's disease. Trends Neurosci. 26(4), 207-214 (2003).
    • (2003) Trends Neurosci , vol.26 , Issue.4 , pp. 207-214
    • Bush, A.I.1
  • 74
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer aβ by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood CS, Moir RD, Huang X et al.: Dramatic aggregation of Alzheimer aβ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273 (21), 12817-12826. (1998).
    • (1998) J. Biol. Chem , vol.273 , Issue.21 , pp. 12817-12826
    • Atwood, C.S.1    Moir, R.D.2    Huang, X.3
  • 75
    • 12144282992 scopus 로고    scopus 로고
    • Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's AΒ peptides
    • Huang X, Atwood CS, Moir RD et al.: Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's AΒ peptides. J. Biol. Inorg. Chem. 9(8), 954-960 (2004).
    • (2004) J. Biol. Inorg. Chem , vol.9 , Issue.8 , pp. 954-960
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3
  • 76
    • 33747036919 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
    • Butterfield DA, Perluigi M, Sultana R: Oxidative stress in Alzheimer's disease brain: new insights from redox proteomics. Eur. J. Pharmacol. 545(1), 39-50 (2006).
    • (2006) Eur. J. Pharmacol , vol.545 , Issue.1 , pp. 39-50
    • Butterfield, D.A.1    Perluigi, M.2    Sultana, R.3
  • 77
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D: Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77(6), 817-827 (1994).
    • (1994) Cell , vol.77 , Issue.6 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 78
    • 0034733705 scopus 로고    scopus 로고
    • Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of aβ by zinc
    • Cuajungco MP, Goldstein LE, Nunomura A et al.: Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of aβ by zinc. J. Biol. Chem. 275(26), 19439-19442 (2000).
    • (2000) J. Biol. Chem , vol.275 , Issue.26 , pp. 19439-19442
    • Cuajungco, M.P.1    Goldstein, L.E.2    Nunomura, A.3
  • 79
    • 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.: The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal reduction. Biochemistry 38 (24), 7609-7616 (1999).
    • (1999) Biochemistry , vol.38 , Issue.24 , pp. 7609-7616
    • Huang, X.1    Atwood, C.S.2    Hartshorn, M.A.3
  • 80
    • 0033601338 scopus 로고    scopus 로고
    • Cu(II) potentiation of alzheimer aβ neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction
    • Huang X, Cuajungco MP, Atwood CS et al.: Cu(II) potentiation of alzheimer aβ neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction. J. Biol. Chem. 274(52), 37111-37116. (1999).
    • (1999) J. Biol. Chem , vol.274 , Issue.52 , pp. 37111-37116
    • Huang, X.1    Cuajungco, M.P.2    Atwood, C.S.3
  • 81
    • 33744956272 scopus 로고    scopus 로고
    • Copper-mediated amyloid-β toxicity is associated with an intermolecular histidine bridge
    • Smith DP, Smith DG, Curtain CC et al.: Copper-mediated amyloid-β toxicity is associated with an intermolecular histidine bridge. J. Biol. Chem. 281(22), 15145-15154 (2006).
    • (2006) J. Biol. Chem , vol.281 , Issue.22 , pp. 15145-15154
    • Smith, D.P.1    Smith, D.G.2    Curtain, C.C.3
  • 82
    • 0033430085 scopus 로고    scopus 로고
    • Amyloid-β binds catalase with high affinity and inhibits hydrogen peroxide breakdown
    • Milton NG: Amyloid-β binds catalase with high affinity and inhibits hydrogen peroxide breakdown. Biochem. J. 344(Pt 2), 293-296 (1999).
    • (1999) Biochem. J , vol.344 , Issue.PART 2 , pp. 293-296
    • Milton, N.G.1
  • 83
    • 0242290357 scopus 로고    scopus 로고
    • Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation
    • Barnham KJ, Ciccotosto GD, Tickler AK et al.: Neurotoxic, redox-competent Alzheimer's β-amyloid is released from lipid membrane by methionine oxidation. J. Biol. Chem. 278(44), 42959-42965 (2003).
    • (2003) J. Biol. Chem , vol.278 , Issue.44 , pp. 42959-42965
    • Barnham, K.J.1    Ciccotosto, G.D.2    Tickler, A.K.3
  • 84
    • 5644291904 scopus 로고    scopus 로고
    • Enhanced toxicity and cellular binding of a modified amyloid β peptide with a methionine to valine substitution
    • Ciccotosto GD, Tew D, Curtain CC et al.: Enhanced toxicity and cellular binding of a modified amyloid β peptide with a methionine to valine substitution. J. Biol. Chem. 279(41), 42528-42534 (2004).
    • (2004) J. Biol. Chem , vol.279 , Issue.41 , pp. 42528-42534
    • Ciccotosto, G.D.1    Tew, D.2    Curtain, C.C.3
  • 85
    • 20444418652 scopus 로고    scopus 로고
    • Methionine regulates copper/ hydrogen peroxide oxidation products of Aβ
    • Ali FE, Separovic F, Barrow CJ et al.: Methionine regulates copper/ hydrogen peroxide oxidation products of Aβ. J. Pept. Sci. 11(6), 353-360 (2005).
    • (2005) J. Pept. Sci , vol.11 , Issue.6 , pp. 353-360
    • Ali, F.E.1    Separovic, F.2    Barrow, C.J.3
  • 86
    • 3242715131 scopus 로고    scopus 로고
    • Rapid characterization of amyloid-β side-chain oxidation by tandem mass spectrometry and the scoring algorithm for spectral analysis
    • Schiewe AJ, Margol L, Soreghan BA, Thomas SN, Yang AJ: Rapid characterization of amyloid-β side-chain oxidation by tandem mass spectrometry and the scoring algorithm for spectral analysis. Pharm. Res. 21(7), 1094-1102 (2004).
    • (2004) Pharm. Res , vol.21 , Issue.7 , pp. 1094-1102
    • Schiewe, A.J.1    Margol, L.2    Soreghan, B.A.3    Thomas, S.N.4    Yang, A.J.5
  • 87
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-β 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.: Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276(23), 20466-20473. (2001).
    • (2001) J. Biol. Chem , vol.276 , Issue.23 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3
  • 88
    • 0036592636 scopus 로고    scopus 로고
    • Amyloid β-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, Pasinetti GM: Amyloid β-peptide and amyloid pathology are central to the oxidative stress and inflammatory cascades under which Alzheimer's disease brain exists. J. Alzheimers Dis. 4(3), 193-201 (2002).
    • (2002) J. Alzheimers Dis , vol.4 , Issue.3 , pp. 193-201
    • Butterfield, D.A.1    Griffin, S.2    Munch, G.3    Pasinetti, G.M.4
  • 89
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ (25-35)
    • Varadarajan S, Kanski J, Aksenova M, Lauderback C, Butterfield DA: Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ (25-35). J. Am. Chem. Soc. 123(24), 5625-5631 (2001).
    • (2001) J. Am. Chem. Soc , vol.123 , Issue.24 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3    Lauderback, C.4    Butterfield, D.A.5
  • 90
    • 0036127328 scopus 로고    scopus 로고
    • Redox properties of Met(35) in neurotoxic β-amyloid peptide. A molecular modeling study
    • Pogocki D, Schoneich C: Redox properties of Met(35) in neurotoxic β-amyloid peptide. A molecular modeling study. Chem. Res. Toxicol. 15(3), 408-418 (2002).
    • (2002) Chem. Res. Toxicol , vol.15 , Issue.3 , pp. 408-418
    • Pogocki, D.1    Schoneich, C.2
  • 91
    • 0028106152 scopus 로고
    • Relative abundance of Alzheimer Aβ amyloid peptide variants in Alzheimer disease and normal aging
    • Naslund J, Schierhorn A, Hellman U et al.: Relative abundance of Alzheimer Aβ amyloid peptide variants in Alzheimer disease and normal aging. Proc. Natl Acad. Sci. USA 91(18), 8378-8382 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , Issue.18 , pp. 8378-8382
    • Naslund, J.1    Schierhorn, A.2    Hellman, U.3
  • 92
    • 0035918312 scopus 로고    scopus 로고
    • Comparative analysis of amyloid-β chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains
    • Kuo YM, Kokjohn TA, Beach TG et al.: Comparative analysis of amyloid-β chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains. J. Biol. Chem. 276(16), 12991-12998. (2001).
    • (2001) J. Biol. Chem , vol.276 , Issue.16 , pp. 12991-12998
    • Kuo, Y.M.1    Kokjohn, T.A.2    Beach, T.G.3
  • 93
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • Dong J, Atwood CS, Anderson VE et al.: Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42(10), 2768-2773 (2003).
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3
  • 94
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity: Implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield DA: Amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radic. Res. 36(12), 1307-1313 (2002).
    • (2002) Free Radic. Res , vol.36 , Issue.12 , pp. 1307-1313
    • Butterfield, D.A.1
  • 95
    • 0032880901 scopus 로고    scopus 로고
    • Methionine residue 35 is important in amyloid β-peptide-associated free radical oxidative stress
    • Varadarajan S, Yatin S, Kanski J, Jahanshahi F, Butterfield DA: Methionine residue 35 is important in amyloid β-peptide-associated free radical oxidative stress. Brain Res. Bull. 50(2), 133-141 (1999).
    • (1999) Brain Res. Bull , vol.50 , Issue.2 , pp. 133-141
    • Varadarajan, S.1    Yatin, S.2    Kanski, J.3    Jahanshahi, F.4    Butterfield, D.A.5
  • 96
    • 0348110660 scopus 로고    scopus 로고
    • A molecular switch in amyloid assembly: Met35 and amyloid β-protein oligomerization
    • Bitan G, Tarus B, Vollers SS et al.: A molecular switch in amyloid assembly: Met35 and amyloid β-protein oligomerization. J. Am. Chem. Soc. 125(50), 15359-15365 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , Issue.50 , pp. 15359-15365
    • Bitan, G.1    Tarus, B.2    Vollers, S.S.3
  • 97
    • 34250898788 scopus 로고    scopus 로고
    • Effect of aldehydes derived from oxidative deamination and oxidative stress on β-amyloid aggregation; pathological implications to Alzheimer's disease
    • Chen K, Kazachkov M, Yu PH: Effect of aldehydes derived from oxidative deamination and oxidative stress on β-amyloid aggregation; pathological implications to Alzheimer's disease. J. Neural Transm. 114(6), 835-839 (2007).
    • (2007) J. Neural Transm , vol.114 , Issue.6 , pp. 835-839
    • Chen, K.1    Kazachkov, M.2    Yu, P.H.3
  • 98
    • 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, Separovic F: Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide. J. Inorg. Biochem. 98(1), 173-184 (2004).
    • (2004) J. Inorg. Biochem , vol.98 , Issue.1 , pp. 173-184
    • Ali, F.E.1    Barnham, K.J.2    Barrow, C.J.3    Separovic, F.4
  • 99
    • 0031985973 scopus 로고    scopus 로고
    • Molecular mechanisms of cellular injury produced by neurotoxic amino acids that generate reactive oxygen species
    • Metodiewa D: Molecular mechanisms of cellular injury produced by neurotoxic amino acids that generate reactive oxygen species. Amino Acids 14(1-3), 181-187 (1998).
    • (1998) Amino Acids , vol.14 , Issue.1-3 , pp. 181-187
    • Metodiewa, D.1
  • 100
    • 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, Heinecke JW: Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine. Free Radic. Biol. Med. 27(1-2), 186-192 (1999).
    • (1999) Free Radic. Biol. Med , vol.27 , Issue.1-2 , pp. 186-192
    • Leeuwenburgh, C.1    Hansen, P.A.2    Holloszy, J.O.3    Heinecke, J.W.4
  • 101
    • 0031678044 scopus 로고    scopus 로고
    • Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease
    • Lovell MA, Xie C, Markesbery WR: Decreased glutathione transferase activity in brain and ventricular fluid in Alzheimer's disease. Neurology 51(6), 1562-1566 (1998).
    • (1998) Neurology , vol.51 , Issue.6 , pp. 1562-1566
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 102
    • 9144235443 scopus 로고    scopus 로고
    • Copper mediates dityrosine cross-linking of Alzheimer's amyloid-β
    • Atwood CS, Perry G, Zeng H et al.: Copper mediates dityrosine cross-linking of Alzheimer's amyloid-β. Biochemistry 43(2), 560-568 (2004).
    • (2004) Biochemistry , vol.43 , Issue.2 , pp. 560-568
    • Atwood, C.S.1    Perry, G.2    Zeng, H.3
  • 104
    • 9444284334 scopus 로고    scopus 로고
    • Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease β-amyloid
    • Barnham KJ, Haeffner F, Ciccotosto GD et al.: Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease β-amyloid. FASEB J. 18(12), 1427-1429 (2004).
    • (2004) FASEB J , vol.18 , Issue.12 , pp. 1427-1429
    • Barnham, K.J.1    Haeffner, F.2    Ciccotosto, G.D.3
  • 105
    • 0346100519 scopus 로고    scopus 로고
    • Dityrosine as a product of oxidative stress and fluorescent probe
    • Malencik DA, Anderson SR: Dityrosine as a product of oxidative stress and fluorescent probe. Amino Acids 25(3-4), 233-247 (2003).
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 233-247
    • Malencik, D.A.1    Anderson, S.R.2
  • 106
    • 0022550027 scopus 로고
    • Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein
    • Roher A, Wolfe D, Palutke M, KuKuruga D: Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein. Proc. Natl Acad. Sci. USA 83(8), 2662-2666 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , Issue.8 , pp. 2662-2666
    • Roher, A.1    Wolfe, D.2    Palutke, M.3    KuKuruga, D.4
  • 107
    • 0346688728 scopus 로고    scopus 로고
    • Reduced risk of Alzheimer disease in users of antioxidant vitamin supplements: The Cache County Study
    • Zandi PP, Anthony JC, Khachaturian AS et al.: Reduced risk of Alzheimer disease in users of antioxidant vitamin supplements: the Cache County Study. Arch. Neurol. 61(1), 82-88 (2004).
    • (2004) Arch. Neurol , vol.61 , Issue.1 , pp. 82-88
    • Zandi, P.P.1    Anthony, J.C.2    Khachaturian, A.S.3
  • 108
    • 16544373763 scopus 로고    scopus 로고
    • Gossypin protects primary cultured rat cortical cells from oxidative stress- and β-amyloid-induced toxicity
    • Yoon I, Lee KH, Cho J: Gossypin protects primary cultured rat cortical cells from oxidative stress- and β-amyloid-induced toxicity. Arch. Pharm. Res. 27(4), 454-459 (2004).
    • (2004) Arch. Pharm. Res , vol.27 , Issue.4 , pp. 454-459
    • Yoon, I.1    Lee, K.H.2    Cho, J.3
  • 109
    • 0041589063 scopus 로고    scopus 로고
    • Melatonin prevents free radical formation due to the interaction between β-amyloid peptides and metal ions (Al[III], Zn[II], Cu[II], Mn[II], Fe[II])
    • Zatta P, Tognon G, Carampin P: Melatonin prevents free radical formation due to the interaction between β-amyloid peptides and metal ions (Al[III], Zn[II], Cu[II], Mn[II], Fe[II]). J. Pineal Res. 35(2), 98-103 (2003).
    • (2003) J. Pineal Res , vol.35 , Issue.2 , pp. 98-103
    • Zatta, P.1    Tognon, G.2    Carampin, P.3
  • 110
    • 4344568620 scopus 로고    scopus 로고
    • Melatonin alleviates behavioral deficits associated with apoptosis and cholinergic system dysfunction in the APP 695 transgenic mouse model of Alzheimer's disease
    • Feng Z, Chang Y, Cheng Y et al.: Melatonin alleviates behavioral deficits associated with apoptosis and cholinergic system dysfunction in the APP 695 transgenic mouse model of Alzheimer's disease. J. Pineal Res. 37(2), 129-136 (2004).
    • (2004) J. Pineal Res , vol.37 , Issue.2 , pp. 129-136
    • Feng, Z.1    Chang, Y.2    Cheng, Y.3
  • 111
    • 0036451982 scopus 로고    scopus 로고
    • Bilobalide and neuroprotection
    • Defeudis FV: Bilobalide and neuroprotection. Pharmacol. Res. 46(6), 565-568 (2002).
    • (2002) Pharmacol. Res , vol.46 , Issue.6 , pp. 565-568
    • Defeudis, F.V.1
  • 112
    • 28244446721 scopus 로고    scopus 로고
    • A randomized, double-blind, placebo-controlled trial of two doses of ginkgo biloba extract in dementia of the Alzheimer's type
    • Schneider LS, DeKosky ST, Farlow MR et al.: A randomized, double-blind, placebo-controlled trial of two doses of ginkgo biloba extract in dementia of the Alzheimer's type. Curr. Alzheimer Res. 2(5), 541-551 (2005).
    • (2005) Curr. Alzheimer Res , vol.2 , Issue.5 , pp. 541-551
    • Schneider, L.S.1    DeKosky, S.T.2    Farlow, M.R.3
  • 113
    • 33750576826 scopus 로고    scopus 로고
    • The GuidAge study: Methodological issues. A 5-year double-blind randomized trial of the efficacy of EGb 761 for prevention of Alzheimer disease in patients over 70 with a memory complaint
    • Vellas B, Andrieu S, Ousset PJ, Ouzid M, Mathiex-Fortunet H: The GuidAge study: methodological issues. A 5-year double-blind randomized trial of the efficacy of EGb 761 for prevention of Alzheimer disease in patients over 70 with a memory complaint. Neurology 67(9 Suppl. 3), S6-S11 (2006).
    • (2006) Neurology , vol.67 , Issue.9 SUPPL. 3
    • Vellas, B.1    Andrieu, S.2    Ousset, P.J.3    Ouzid, M.4    Mathiex-Fortunet, H.5
  • 114
    • 0035957872 scopus 로고    scopus 로고
    • Curcuminoids from Curcuma longa L. (Zingiberaceae) that protect PC12 rat pheochromocytoma and normal human umbilical vein endothelial cells from βA(1-42) insult
    • Kim DS, Park SY, Kim JK: Curcuminoids from Curcuma longa L. (Zingiberaceae) that protect PC12 rat pheochromocytoma and normal human umbilical vein endothelial cells from βA(1-42) insult. Neurosci. Lett. 303(1), 57-61 (2001).
    • (2001) Neurosci. Lett , vol.303 , Issue.1 , pp. 57-61
    • Kim, D.S.1    Park, S.Y.2    Kim, J.K.3
  • 115
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro
    • Ono K, Hasegawa K, Naiki H, Yamada M: Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro. J. Neurosci. Res. 75(6), 742-750 (2004).
    • (2004) J. Neurosci. Res , vol.75 , Issue.6 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 116
    • 20044370990 scopus 로고    scopus 로고
    • Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo
    • Yang F, Lim GP, Begum AN et al.: Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J. Biol. Chem. 280 (7), 5892-5901 (2005).
    • (2005) J. Biol. Chem , vol.280 , Issue.7 , pp. 5892-5901
    • Yang, F.1    Lim, G.P.2    Begum, A.N.3
  • 117
    • 4644275696 scopus 로고    scopus 로고
    • Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models
    • Baum L, Ng A: Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models. J. Alzheimers Dis. 6(4), 367-377 (2004).
    • (2004) J. Alzheimers Dis , vol.6 , Issue.4 , pp. 367-377
    • Baum, L.1    Ng, A.2
  • 118
    • 33646490404 scopus 로고    scopus 로고
    • Moret V, Laras Y, Pietrancosta N et al.: 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(12), 3298-3301 (2006).
    • Moret V, Laras Y, Pietrancosta N et al.: 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(12), 3298-3301 (2006).
  • 119
    • 4644238758 scopus 로고    scopus 로고
    • The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human β-amyloid precursor protein transgenic mice
    • Lee JY, Friedman JE, Angel I, Kozak A, Koh JY: The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human β-amyloid precursor protein transgenic mice. Neurobiol. Aging 25(10), 1315-1321 (2004).
    • (2004) Neurobiol. Aging , vol.25 , Issue.10 , pp. 1315-1321
    • Lee, J.Y.1    Friedman, J.E.2    Angel, I.3    Kozak, A.4    Koh, J.Y.5
  • 120
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME et al.: Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30(3), 665-676. (2001).
    • (2001) Neuron , vol.30 , Issue.3 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3
  • 121
    • 33644843098 scopus 로고    scopus 로고
    • In vivo protection by the xanthate tricyclodecan-9-yl-xanthogenate against amyloid β-peptide (1-42)-induced oxidative stress
    • Perluigl M, Joshi G, Sultana R et al.: In vivo protection by the xanthate tricyclodecan-9-yl-xanthogenate against amyloid β-peptide (1-42)-induced oxidative stress. Neuroscience 138(4), 1161-1170 (2006).
    • (2006) Neuroscience , vol.138 , Issue.4 , pp. 1161-1170
    • Perluigl, M.1    Joshi, G.2    Sultana, R.3
  • 122
    • 10744224267 scopus 로고    scopus 로고
    • Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Aβ amyloid deposition and toxicity in Alzheimer disease: A pilot Phase 2 clinical trial
    • Ritchi CW, Bush AI, Mackinnon A et al.: Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Aβ amyloid deposition and toxicity in Alzheimer disease: a pilot Phase 2 clinical trial. Arch. Neurol. 60(12), 1685-1691 (2003).
    • (2003) Arch. Neurol , vol.60 , Issue.12 , pp. 1685-1691
    • Ritchi, C.W.1    Bush, A.I.2    Mackinnon, A.3
  • 123
    • 33745860362 scopus 로고    scopus 로고
    • Degradation of the Alzheimer disease amyloid β-peptide by metal-dependent up-regulation of metalloprotease activity
    • White AR, Du T, Laughton KM et al.: Degradation of the Alzheimer disease amyloid β-peptide by metal-dependent up-regulation of metalloprotease activity. J. Biol. Chem. 281(26), 17670-17680 (2006).
    • (2006) J. Biol. Chem , vol.281 , Issue.26 , pp. 17670-17680
    • White, A.R.1    Du, T.2    Laughton, K.M.3
  • 124
    • 10644280708 scopus 로고    scopus 로고
    • Clioquinol mediates copper uptake and counteracts Cu efflux activities of the amyloid precursor protein of Alzheimer's disease
    • Treiber C, Simons A, Strauss M et al.: Clioquinol mediates copper uptake and counteracts Cu efflux activities of the amyloid precursor protein of Alzheimer's disease. J. Biol. Chem. 279(50), 51958-51964 (2004).
    • (2004) J. Biol. Chem , vol.279 , Issue.50 , pp. 51958-51964
    • Treiber, C.1    Simons, A.2    Strauss, M.3
  • 125
    • 33846013897 scopus 로고    scopus 로고
    • Therapeutic treatments for Alzheimer's disease based on metal bioavailability
    • Crouch PJ, Barnham KJ, Bush AI, White AR: Therapeutic treatments for Alzheimer's disease based on metal bioavailability. Drug News Perspect. 19(8), 469-474 (2006).
    • (2006) Drug News Perspect , vol.19 , Issue.8 , pp. 469-474
    • Crouch, P.J.1    Barnham, K.J.2    Bush, A.I.3    White, A.R.4
  • 126
    • 33746840955 scopus 로고    scopus 로고
    • Multifunctional neuroprotective drugs targeting monoarnine oxidase inhibition, iron chelation, adenosine receptors, and cholinergic and glutarnatergic action for neurodegenerative diseases
    • Van der Schyg CJ, Gal S, Geldenhuys WJ, Youdirn MB: Multifunctional neuroprotective drugs targeting monoarnine oxidase inhibition, iron chelation, adenosine receptors, and cholinergic and glutarnatergic action for neurodegenerative diseases. Expert Opin. Investig. Drugs 15(8), 873-886 (2006).
    • (2006) Expert Opin. Investig. Drugs , vol.15 , Issue.8 , pp. 873-886
    • Van der Schyg, C.J.1    Gal, S.2    Geldenhuys, W.J.3    Youdirn, M.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.