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Volumn 39, Issue 6, 2010, Pages 877-888

Beta amyloid peptide: From different aggregation forms to the activation of different biochemical pathways

Author keywords

Apoptosis; Beta amyloid; Fibrillogenesis; Inflammation; Oxidative stress

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CELL SURFACE RECEPTOR; PEPTIDE FRAGMENT; PROTEASE NEXINS; TAU PROTEIN;

EID: 77952094986     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-009-0439-8     Document Type: Review
Times cited : (43)

References (113)
  • 2
    • 0141853765 scopus 로고    scopus 로고
    • Amyloid-β: A chameleon walking in two worlds: A review of the trophic and toxic properties of amyloid-β
    • DOI 10.1016/S0165-0173(03)00174-7
    • CS Atwood ME Obrenovich T Liu, et al. 2003 Amyloid beta: a chameleon walking in two worlds: a review of the trophic and toxic properties of amyloid-beta Brain Res 43 1 46 10.1016/S0165-0173(03)00174-7 (Pubitemid 37130077)
    • (2003) Brain Research Reviews , vol.43 , Issue.1 , pp. 1-16
    • Atwood, C.S.1    Obrenovich, M.E.2    Liu, T.3    Chan, H.4    Perry, G.5    Smith, M.A.6    Martins, R.N.7
  • 3
    • 3042586648 scopus 로고    scopus 로고
    • Inflammatory mediator and β-amyloid (25-35)-induced ceramide generation and iNOS expression are inhibited by vitamin E
    • DOI 10.1016/j.freeradbiomed.2004.04.007, PII S0891584904003107
    • K Ayasolla M Khan AK Singh I Singh 2004 Inflammatory mediator and beta-amyloid (25-35)-induced ceramide generation and iNOS expression are inhibited by Vitamin E Free Radic Biol Med 37 325 338 10.1016/j.freeradbiomed. 2004.04.007 15223066 (Pubitemid 38833999)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.3 , pp. 325-338
    • Ayasolla, K.1    Khan, M.2    Singh, A.K.3    Singh, I.4
  • 4
    • 4644275696 scopus 로고    scopus 로고
    • Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models
    • L Baum A Ng 2004 Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models J Alzheimers Dis 6 443 449
    • (2004) J Alzheimers Dis , vol.6 , pp. 443-449
    • Baum, L.1    Ng, A.2
  • 5
    • 15944364190 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease: Implications for prevention and therapy
    • 10.1007/0-387-23226-5-3 15709473
    • C Behl 2005 Oxidative stress in Alzheimer's disease: implications for prevention and therapy Subcell Biochem 38 65 78 10.1007/0-387-23226-5-3 15709473
    • (2005) Subcell Biochem , vol.38 , pp. 65-78
    • Behl, C.1
  • 6
    • 33645105621 scopus 로고    scopus 로고
    • Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms
    • 10.1111/j.1471-4159.2005.03578.x 16405513
    • M Bentahir O Nyabi J Verhamme A Tolia K Horre J Wiltfang H Esselmann B De Strooper 2006 Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms J Neurochem 96 732 742 10.1111/j.1471-4159.2005.03578.x 16405513
    • (2006) J Neurochem , vol.96 , pp. 732-742
    • Bentahir, M.1    Nyabi, O.2    Verhamme, J.3    Tolia, A.4    Horre, K.5    Wiltfang, J.6    Esselmann, H.7    De Strooper, B.8
  • 7
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • 10.1074/jbc.M102223200 11441003
    • G Bitan A Lomakin DB Teplow 2001 Amyloid beta-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins J Biol Chem 276 35176 35184 10.1074/jbc.M102223200 11441003
    • (2001) J Biol Chem , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 9
    • 65949093025 scopus 로고    scopus 로고
    • Ferulic Acid-Loaded Lipid Nanostructures as Drug Delivery Systems for Alzheimer's Disease: Preparation, Characterization and Cytotoxicity Studies
    • ML Bondì G Montana EF Craparo P Picone G Capuano M Di Carlo G Giammona 2009 Ferulic Acid-Loaded Lipid Nanostructures as Drug Delivery Systems for Alzheimer's Disease: Preparation, Characterization and Cytotoxicity Studies Curr Nanosci 5 26 32
    • (2009) Curr Nanosci , vol.5 , pp. 26-32
    • Bondì, M.L.1    Montana, G.2    Craparo, E.F.3    Picone, P.4    Capuano, G.5    Di Carlo, M.6    Giammona, G.7
  • 12
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimer's disease
    • DOI 10.1016/S0166-2236(03)00067-5
    • AI Bush 2003 The metallobiology of Alzheimer's disease Trends Neurosci 26 207 214 10.1016/S0166-2236(03)00067-5 12689772 (Pubitemid 36412003)
    • (2003) Trends in Neurosciences , vol.26 , Issue.4 , pp. 207-214
    • Bush, A.I.1
  • 13
    • 0027526419 scopus 로고
    • Release of excess amyloid beta protein from a mutant amyloid beta protein precursor
    • 10.1126/science.8424174 8424174
    • XD Cai TE Golde SG Younkin 1993 Release of excess amyloid beta protein from a mutant amyloid beta protein precursor Science 259 514 516 10.1126/science.8424174 8424174
    • (1993) Science , vol.259 , pp. 514-516
    • Cai, X.D.1    Golde, T.E.2    Younkin, S.G.3
  • 14
    • 24044518189 scopus 로고    scopus 로고
    • Protofibril formation of amyloid β-protein at low pH via a non-cooperative elongation mechanism
    • DOI 10.1074/jbc.M500052200
    • R Carrotta M Manno D Bulone V Martorana PL San Biagio 2005 Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism J Biol Chem 280 30001 30008 10.1074/jbc.M500052200 15985437 (Pubitemid 41216175)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.34 , pp. 30001-30008
    • Carrotta, R.1    Manno, M.2    Bulone, D.3    Martorana, V.4    San Biagio, P.L.5
  • 15
    • 33845566340 scopus 로고    scopus 로고
    • Toxicity of recombinant β-amyloid prefibrillar oligomers on the morphogenesis of the sea urchin Paracentrotus lividus
    • DOI 10.1096/fj.06-5716fje
    • R Carrotta M Di Carlo M Manno G Montana P Picone D Romancino PL San Biagio 2006 Toxicity of recombinant beta-amyloid prefibrillar oligomers on the morphogenesis of the sea urchin Paracentrotus lividus FASEB J 20 1916 1924 10.1096/fj.06-5716fje 16818470 (Pubitemid 44933778)
    • (2006) FASEB Journal , vol.20 , Issue.11
    • Carrotta, R.1    Di Carlo, M.2    Manno, M.3    Montana, G.4    Picone, P.5    Romancino, D.6    San Biagio, P.L.7
  • 16
    • 0032525741 scopus 로고    scopus 로고
    • In vivo inhibition of nitric oxide synthase gene expression by curcumin, a cancer preventive natural product with anti-inflammatory properties
    • DOI 10.1016/S0006-2952(98)00114-2, PII S0006295298001142
    • MM Chan HI Huang MR Fenton D Fong 1998 In vivo inhibition of nitric oxide synthase gene expression by curcumin, a cancer preventive natural product with anti-inflammatory properties Biochem Pharmacol 55 1955 1962 10.1016/S0006- 2952(98)00114-2 9714315 (Pubitemid 28477465)
    • (1998) Biochemical Pharmacology , vol.55 , Issue.12 , pp. 1955-1962
    • Chan, M.M.-Y.1    Huang, H.-I.2    Fenton, M.R.3    Fong, D.4
  • 17
    • 33745727582 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease
    • 10.1016/j.pathophys.2006.05.004 16781128
    • V Chauhan A Chauhan 2006 Oxidative stress in Alzheimer's disease Pathophysiology 13 195 208 10.1016/j.pathophys.2006.05.004 16781128
    • (2006) Pathophysiology , vol.13 , pp. 195-208
    • Chauhan, V.1    Chauhan, A.2
  • 19
    • 77952089995 scopus 로고    scopus 로고
    • Fibril aggregation inhibitory activity of the beta-sheet breaker peptides: A moleular docking approach
    • Chini MG, Scrima M, D'Ursi AM, Bifulco G (2008) Fibril aggregation inhibitory activity of the beta-sheet breaker peptides: a molecular docking approach. J Pept Sci Dec:16
    • (2008) J Pept Sci Dec , vol.16
    • Chini, M.G.1    Scrima, M.2    D'Ursi, A.M.3    Bifulco, G.4
  • 20
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F Chiti C Dobson 2006 Protein misfolding, functional amyloid and human disease Annu Rev Biochem 75 333 366 10.1146/annurev.biochem.75.101304.123901 16756495 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 21
    • 0026745610 scopus 로고
    • Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
    • DOI 10.1038/360672a0
    • M Citron T Oltersdorf C Haass L McConlogue AY Hung P Seubert C Vigo-Pelfrey I Lieberburg DJ Selkoe 1992 Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production Nature 360 672 674 10.1038/360672a0 1465129 (Pubitemid 23007680)
    • (1992) Nature , vol.360 , Issue.6405 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3    McConlogue, L.4    Hung, A.Y.5    Seubert, P.6    Vigo-Pelfrey, C.7    Lieberburg, I.8    Selkoe, D.J.9
  • 24
    • 0030464914 scopus 로고    scopus 로고
    • β-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease
    • DOI 10.1016/S0197-4580(96)00170-4, PII S0197458096001704
    • BJ Cummings CJ Pike R Shankle CW Cotman 1996 Beta-amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease Neurobiol Aging 17 921 933 10.1016/S0197-4580(96)00170-4 9363804 (Pubitemid 27022746)
    • (1996) Neurobiology of Aging , vol.17 , Issue.6 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 25
    • 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
    • 10.1074/jbc.M100175200 11274207
    • CC Curtain F Ali I Volitakis RA Cherny RS Norton K Beyreuther CJ Barrow CL Masters AI Bush KJ Barnham 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 10.1074/jbc.M100175200 11274207
    • (2001) J Biol Chem , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 26
    • 0037195546 scopus 로고    scopus 로고
    • Consistent immunohistochemical detection of intracellular β-amyloid42 in pyramidal neurons of Alzheimer's disease entorhinal cortex
    • DOI 10.1016/S0304-3940(02)00875-3, PII S0304394002008753
    • MR D'Andrea RG Nagele HY Wang DH Lee 2002 Consistent immunohistochemical detection of intracellular beta-amyloid42 in pyramidal neurons of Alzheimer's disease entorhinal cortex Neurosci Lett 333 163 166 10.1016/S0304-3940(02)00875- 3 12429373 (Pubitemid 35335768)
    • (2002) Neuroscience Letters , vol.333 , Issue.3 , pp. 163-166
    • D'Andrea, M.R.1    Nagele, R.G.2    Wang, H.-Y.3    Lee, D.H.S.4
  • 27
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • DOI 10.1074/jbc.M500997200
    • A Demuro E Mina R Kayed SC Milton I Parker CG Glabe 2005 Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers J Biol Chem 280 17294 17300 10.1074/jbc.M500997200 15722360 (Pubitemid 41389198)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 28
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons
    • DOI 10.1523/JNEUROSCI.1189-06.2006
    • A Deshpande E Mina C Glabe J Busciglio 2006 Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons J Neurosci 26 6011 6018 10.1523/JNEUROSCI.1189-06.2006 16738244 (Pubitemid 44318367)
    • (2006) Journal of Neuroscience , vol.26 , Issue.22 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 29
    • 85047693458 scopus 로고    scopus 로고
    • Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: Cause or effect?
    • 15232608
    • DW Dickson 2004 Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: cause or effect? J Clin Invest 114 23 27 15232608
    • (2004) J Clin Invest , vol.114 , pp. 23-27
    • Dickson, D.W.1
  • 33
    • 34548812551 scopus 로고    scopus 로고
    • The role of amyloid β peptide 42 in Alzheimer's disease
    • DOI 10.1016/j.pharmthera.2007.06.006, PII S016372580700143X
    • MA Findeis 2007 The role of amyloid beta peptide 42 in Alzhiemer's disease Pharmacol Ther 116 266 286 10.1016/j.pharmthera.2007.06.006 17716740 (Pubitemid 47451506)
    • (2007) Pharmacology and Therapeutics , vol.116 , Issue.2 , pp. 266-286
    • Findeis, M.A.1
  • 34
    • 0030611858 scopus 로고    scopus 로고
    • Soluble amyloid Abeta-(1-40) exists as a stable dimer at low concentrations
    • W Garzon-Rodigrez M Sepulveda-Becerra S Milton CG Glabe 1997 Soluble amyloid Abeta-(1-40) exists as a stable dimer at low concentrations J Biol Chem 272 21037 21044
    • (1997) J Biol Chem , vol.272 , pp. 21037-21044
    • Garzon-Rodigrez, W.1    Sepulveda-Becerra, M.2    Milton, S.3    Glabe, C.G.4
  • 35
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to 26 β-protein neurotoxicity
    • DOI 10.1038/nm0798-827
    • C Geula CK Wu D Saroff A Lorenzo M Yuan BA Yankner 1998 Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity Nat Med 4 827 831 10.1038/nm0798-827 9662375 (Pubitemid 28331025)
    • (1998) Nature Medicine , vol.4 , Issue.7 , pp. 827-831
    • Geula, C.1    Wu, C.-K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yankner, B.A.6
  • 36
    • 0035159785 scopus 로고    scopus 로고
    • Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease
    • DOI 10.1385/JMN:17:2:137
    • C Glabe 2001 Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease J Mol Neurosci 17 137 145 10.1385/JMN:17:2:137 11816787 (Pubitemid 33063518)
    • (2001) Journal of Molecular Neuroscience , vol.17 , Issue.2 , pp. 137-145
    • Glabe, C.1
  • 37
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • G Glenner CW Wong 1984 Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein Biochem Biophys Res Commun 120 885 890 10.1016/S0006-291X(84)80190-4 6375662 (Pubitemid 14104991)
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 39
    • 0036898485 scopus 로고    scopus 로고
    • Alzheimer disease γ-secretase: A complex story of GxGD-type presenilin proteases
    • DOI 10.1016/S0962-8924(02)02394-2, PII S0962892402023942
    • C Haass H Steiner 2002 Alzheimer disease gamma-secretase: a complex story of GxGD-type presenilin proteases Trends Cell Biol 12 556 562 10.1016/S0962-8924(02)02394-2 12495843 (Pubitemid 35461853)
    • (2002) Trends in Cell Biology , vol.12 , Issue.12 , pp. 556-562
    • Haass, C.1    Steiner, H.2
  • 40
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein
    • 10.1016/S1074-5521(97)90303-3 9427660
    • JD Harper SS Wong CM Lieber PT Lansbury 1997 Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein Chem Biol 4 951 959 10.1016/S1074-5521(97)90303-3 9427660
    • (1997) Chem Biol , vol.4 , pp. 951-959
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 42
    • 0036191829 scopus 로고    scopus 로고
    • Mapping of possible binding sequences of two beta-sheet breaker peptides on beta amyloid peptide of Alzheimer's disease
    • DOI 10.1016/S0968-0896(01)00424-2, PII S0968089601004242
    • C Hetényi T Körtvélyesi B Penke 2002 Mapping of possible binding sequences of two bet -sheet breaker peptides on beta amyloid peptide of Alzheimer's disease Bioorg Med Chem 10 1587 1593 10.1016/S0968- 0896(01)00424-2 11886820 (Pubitemid 34214721)
    • (2002) Bioorganic and Medicinal Chemistry , vol.10 , Issue.5 , pp. 1587-1593
    • Hetenyi, C.1    Kortvelyesi, T.2    Penke, B.3
  • 44
    • 0027485461 scopus 로고
    • Bcl-2 functions in an antioxidant pathway to prevent apoptosis
    • DOI 10.1016/0092-8674(93)80066-N
    • DM Hockenbery ZN Oltvai XM Yin CL Milliman SJ Korsmeyer 1993 Bcl-2 functions in an antioxidant pathway to prevent apoptosis Cell 75 241 251 10.1016/0092-8674(93)80066-N 7503812 (Pubitemid 23320288)
    • (1993) Cell , vol.75 , Issue.2 , pp. 241-251
    • Hockenbery, D.M.1    Oltvai, Z.N.2    Yin, X.-M.3    Milliman, C.L.4    Korsmeyer, S.J.5
  • 49
    • 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
    • DOI 10.1021/bi00069a001
    • JT Jarrett EP Berger PT Lansbury Jr 1993 The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease Biochemistry 32 4693 7469 10.1021/bi00069a001 8490014 (Pubitemid 23162022)
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 50
    • 61749086594 scopus 로고    scopus 로고
    • FTIR spectroscopic studies on aggregation process of the beta-amyloid 11-28 fragment and its variants
    • 10.1002/psc.1085 19023881
    • P Juszczyk AS Kołodziejczyk Z Grzonka 2009 FTIR spectroscopic studies on aggregation process of the beta-amyloid 11-28 fragment and its variants J Pept Sci 15 23 29 10.1002/psc.1085 19023881
    • (2009) J Pept Sci , vol.15 , pp. 23-29
    • Juszczyk, P.1    Kołodziejczyk, A.S.2    Grzonka, Z.3
  • 51
    • 0037184817 scopus 로고    scopus 로고
    • History of the events leading to the formulation of the apoptosis concept
    • DOI 10.1016/S0300-483X(02)00457-2, PII S0300483X02004572
    • JF Kerr 2002 History of the events leading to the formulation of the apoptosis concept Toxicology 182 471 474 10.1016/S0300-483X(02)00457-2 (Pubitemid 36015740)
    • (2002) Toxicology , vol.181-182 , pp. 471-474
    • Kerr, J.F.R.1
  • 52
    • 0037013327 scopus 로고    scopus 로고
    • Intracellular amyloid-β1-42, but not extracellular soluble amyloid-β peptides, induces neuronal apoptosis
    • DOI 10.1074/jbc.M200887200
    • P Kienlen-Campard S Miolet B Tasiaux JN Octave 2002 Intracellular amyloid-beta 1-42, but not extracellular soluble amyloid-beta peptides, induces neuronal apoptosis Biol Chem 277 15666 15670 10.1074/jbc.M200887200 (Pubitemid 34967839)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15666-15670
    • Kienlen-Campard, P.1    Miolet, S.2    Tasiaux, B.3    Octave, J.-N.4
  • 54
    • 23644459835 scopus 로고    scopus 로고
    • Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease
    • 15933761
    • MD Kirkitadze A Kowalska 2005 Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease Acta Biochim Pol 52 417 423 15933761
    • (2005) Acta Biochim Pol , vol.52 , pp. 417-423
    • Kirkitadze, M.D.1    Kowalska, A.2
  • 55
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation
    • 10.1073/pnas.83.2.503 3455785
    • DA Kirschner C Abraham DJ Selkoe 1986 X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation Proc Natl Acad Sci USA 83 503 507 10.1073/pnas.83.2.503 3455785
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 57
    • 33745700370 scopus 로고    scopus 로고
    • Mean age-of-onset of familial alzheimer disease caused by presenilin mutations correlates with both increased Abeta42 and decreased Abeta40
    • 10.1002/humu.20336 16752394
    • S Kumar-Singh J Theuns B Van Broeck D Pirici K Vennekens E Corsmit M Cruts B Dermaut R Wang C Van Broeckhoven 2006 Mean age-of-onset of familial alzheimer disease caused by presenilin mutations correlates with both increased Abeta42 and decreased Abeta40 Hum Mutat 27 686 695 10.1002/humu.20336 16752394
    • (2006) Hum Mutat , vol.27 , pp. 686-695
    • Kumar-Singh, S.1    Theuns, J.2    Van Broeck, B.3    Pirici, D.4    Vennekens, K.5    Corsmit, E.6    Cruts, M.7    Dermaut, B.8    Wang, R.9    Van Broeckhoven, C.10
  • 59
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • 11606625
    • GP Lim T Chu F Yang W Beech SA Frautschy GM Cole 2001 The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse J Neurosci 21 8370 8377 11606625
    • (2001) J Neurosci , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 60
    • 32844465483 scopus 로고    scopus 로고
    • Cytokine production by a human microglial cell line: Effects of beta-amyloid and alpha-melanocyte-stimulating hormone
    • 16371321
    • C Lindberg E Hjorth C Post B Winblad M Schultzberg 2005 Cytokine production by a human microglial cell line: effects of beta-amyloid and alpha-melanocyte-stimulating hormone Neurotox Res 8 267 276 16371321
    • (2005) Neurotox Res , vol.8 , pp. 267-276
    • Lindberg, C.1    Hjorth, E.2    Post, C.3    Winblad, B.4    Schultzberg, M.5
  • 61
    • 0033587478 scopus 로고    scopus 로고
    • Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the Aβ peptide of Alzheimer's disease
    • DOI 10.1021/bi990205o
    • ST Liu G Howlett CJ Barrow 1999 Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease Biochemistry 38 9373 9378 10.1021/bi990205o 10413512 (Pubitemid 29347261)
    • (1999) Biochemistry , vol.38 , Issue.29 , pp. 9373-9378
    • Liu, S.-T.1    Howlett, G.2    Barrow, C.J.3
  • 64
    • 0032766155 scopus 로고    scopus 로고
    • Intrastriatal dopamine injection induces apoptosis through oxidation-involved activation of transcription factors AP-1 and NF-kappaB in rats
    • 10419543
    • Y Luo A Hattori J Munoz Z Qin G Roth 1999 Intrastriatal dopamine injection induces apoptosis through oxidation-involved activation of transcription factors AP-1 and NF-kappaB in rats Mol Pharmacol 56 254 264 10419543
    • (1999) Mol Pharmacol , vol.56 , pp. 254-264
    • Luo, Y.1    Hattori, A.2    Munoz, J.3    Qin, Z.4    Roth, G.5
  • 65
    • 21544465581 scopus 로고    scopus 로고
    • An alternative interpretation of the amyloid Aβ hypothesis with regard to the pathogenesis of Alzheimer's disease
    • DOI 10.1073/pnas.0503181102
    • VT Marchesi 2005 An alternative interpretation of the amyloid Abeta hypothesis with regard to the pathogenesis of Alzheimer's disease Proc Natl Acad Sci USA 102 9093 9098 10.1073/pnas.0503181102 15967987 (Pubitemid 40923523)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.26 , pp. 9093-9098
    • Marchesi, V.T.1
  • 68
    • 0035693924 scopus 로고    scopus 로고
    • Inflammation, autotoxicity and Alzheimer disease
    • DOI 10.1016/S0197-4580(01)00289-5, PII S0197458001002895
    • PL McGeer EG McGerr 2001 Inflammation autotoxicity and Alzheimer's disease Neurobiol Aging 22 799 809 10.1016/S0197-4580(01)00289-5 11754986 (Pubitemid 34066546)
    • (2001) Neurobiology of Aging , vol.22 , Issue.6 , pp. 799-809
    • McGeer, P.L.1    McGeer, E.G.2
  • 70
  • 71
    • 4444304720 scopus 로고    scopus 로고
    • APP and PS-1 mutations induce brain oxidative stress independent of dietary cholesterol: Implications for Alzheimer's disease
    • DOI 10.1016/j.neulet.2004.06.077, PII S0304394004008420
    • AH Mohmmad GL Wenk M Gramling B Hauss-Wegrzyniak DA Butterfield 2004 APP and PS-1 mutations induce brain oxidative stress independent of dietary cholesterol: implications for Alzheimer's disease Neurosci Lett 368 148 150 10.1016/j.neulet.2004.06.077 (Pubitemid 39194861)
    • (2004) Neuroscience Letters , vol.368 , Issue.2 , pp. 148-150
    • Mohmmad Abdul, H.1    Wenk, G.L.2    Gramling, M.3    Hauss-Wegrzyniak, B.4    Butterfield, D.A.5
  • 72
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • DOI 10.1038/47513
    • T Nakagawa H Zhu N Morishima E Li J Xu BA Yankner J Yuan 2000 Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta Nature 403 98 103 10.1038/47513 10638761 (Pubitemid 30038529)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 73
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by alpha-, beta- and gamma-secretases
    • 10.1016/S0014-5793(00)02076-7
    • J Nunam DH Small 2000 Regulation of APP cleavage by alpha-, beta- and gamma-secretases FEBS Lett 483 6 10 10.1016/S0014-5793(00)02076-7
    • (2000) FEBS Lett , vol.483 , pp. 6-10
    • Nunam, J.1    Small, D.H.2
  • 74
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2003.08.012
    • S Oddo A Caccamo JD Shepherd MP Murphy TE Golde R Kayed R Metherate MP Mattson Y Akb ri FM LaFerla 2003 Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease Neurobiol Aging 24 1063 1070 10.1016/j.neurobiolaging.2003.08.012 14643377 (Pubitemid 37487883)
    • (2003) Neurobiology of Aging , vol.24 , Issue.8 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 75
    • 24644438783 scopus 로고    scopus 로고
    • Ferulic acid destabilizes preformed beta-amyloid fibrils in vitro
    • Ono K, Hirohata M, Yamada M (2005) Ferulic acid destabilizes preformed beta-amyloid fibrils in vitro. Biochem Biophys Res Commun 21:336, 444
    • (2005) Biochem Biophys Res Commun , vol.21 , pp. 444
    • Ono, K.1    Hirohata, M.2    Yamada, M.3
  • 76
    • 0037355742 scopus 로고    scopus 로고
    • Copper reduction by copper binding proteins and its relation to neurodegenerative diseases
    • DOI 10.1023/A:1020795422185
    • C Opazo MI Barria FH Ruiz NC Inestrosa 2003 Copper reduction by copper binding proteins and its relation to neurodegenerative diseases Biometals 16 91 98 10.1023/A:1020795422185 12572668 (Pubitemid 36140219)
    • (2003) BioMetals , vol.16 , Issue.1 , pp. 91-98
    • Opazo, C.1    Ines Barria, M.2    Ruiz, F.H.3    Inestrosa, N.C.4
  • 77
    • 68049131389 scopus 로고    scopus 로고
    • Aβ oligomers and fibrillar aggregates induce different apoptotic pathways in LAN5 neuroblastoma cell cultures
    • P Picone R Carrotta G Montana MR Nobile PL San Biagio M Di Carlo 2009 Aβ oligomers and fibrillar aggregates induce different apoptotic pathways in LAN5 neuroblastoma cell cultures Biophys J 96 1 12
    • (2009) Biophys J , vol.96 , pp. 1-12
    • Picone, P.1    Carrotta, R.2    Montana, G.3    Nobile, M.R.4    San Biagio, P.L.5    Di Carlo, M.6
  • 78
    • 57649221161 scopus 로고    scopus 로고
    • Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: Lights and shadows
    • 19076432
    • D Praticò 2008 Evidence of oxidative stress in Alzheimer's disease brain and antioxidant therapy: lights and shadows Ann N Y Acad Sci 1147 70 78 19076432
    • (2008) Ann N y Acad Sci , vol.1147 , pp. 70-78
    • Praticò, D.1
  • 79
    • 37249062072 scopus 로고    scopus 로고
    • Internalization of β-amyloid peptide by primary neurons in the absence of apolipoprotein E
    • DOI 10.1074/jbc.M701823200
    • L Saavedra A Mohamed V Ma Kar Posse S de Chaves 2007 Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E J Biol Chem 282 35722 35732 10.1074/jbc.M701823200 17911110 (Pubitemid 350277136)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35722-35732
    • Saavedra, L.1    Mohamed, A.2    Ma, V.3    Kar, S.4    De Chaves, E.P.5
  • 80
    • 0042878457 scopus 로고    scopus 로고
    • The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of κB kinase, and NFκB, do not reduce amyloid β42 production
    • DOI 10.1074/jbc.M303588200
    • SA Sagi S Weggen J Eriksen TE Golde EH Koo 2003 The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of kappa B kinase, and NF kappa B, do not reduce amyloid beta 42 production J Biol Chem 278 31825 31830 10.1074/jbc.M303588200 12805355 (Pubitemid 37048364)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 31825-31830
    • Sagi, S.A.1    Weggen, S.2    Eriksen, J.3    Golde, T.E.4    Koo, E.H.5
  • 83
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe DJ (1999) Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399:A23-A31
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 84
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • 10899428
    • LC Serpell 2000 Alzheimer's amyloid fibrils: structure and assembly Biochim Biophys Acta 1502 16 20 10899428
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 16-20
    • Serpell, L.C.1
  • 85
    • 53049095484 scopus 로고    scopus 로고
    • In vitro perturbation of aggregation processes in beta-amyloid peptides: A spectroscopic study
    • 10.1016/j.febslet.2008.08.039 18805418
    • A Sgarbossa D Buselli F Lenci 2008 In vitro perturbation of aggregation processes in beta-amyloid peptides: a spectroscopic study FEBS Lett 582 3288 3292 10.1016/j.febslet.2008.08.039 18805418
    • (2008) FEBS Lett , vol.582 , pp. 3288-3292
    • Sgarbossa, A.1    Buselli, D.2    Lenci, F.3
  • 87
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation
    • B Sorenghan J Kosmoski C Glabe 1994 Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation J Biol Chem 269 28551 28554
    • (1994) J Biol Chem , vol.269 , pp. 28551-28554
    • Sorenghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 90
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • 10.1126/science.8191290 8191290
    • N Suzuki TT Cheung XD Cai A Odaka L Otvos Jr C Eckman TE Golde SG Younkin 1994 An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants Science 264 1336 1340 10.1126/science.8191290 8191290
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos Jr, L.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 91
    • 0034811903 scopus 로고    scopus 로고
    • Inhibitory effect of copper(II) on zinc(II)-induced aggregation of amyloid β-peptide
    • DOI 10.1006/bbrc.2001.5263
    • K Suzuki T Miura H Takeuchi 2001 Inhibitory effect of copper(II) on zinc(II)-induced aggregation of amyloid b-peptide Biochem Biophys Res Commun 285 991 996 10.1006/bbrc.2001.5263 11467850 (Pubitemid 32918035)
    • (2001) Biochemical and Biophysical Research Communications , vol.285 , Issue.4 , pp. 991-996
    • Suzuki, K.1    Miura, T.2    Takeuchi, H.3
  • 92
    • 0033781375 scopus 로고    scopus 로고
    • Subacute myelo-optico-neuropathy: Clioquinol intoxication in humans and animals
    • 10.1046/j.1440-178 .2000.00296.x
    • J Tateishi 2000 Subacute myelo-optico-neuropathy: clioquinol intoxication in humans and animals Neuropathology 20 20 24 10.1046/j.1440-1789.2000.00296.x
    • (2000) Neuropathology , vol.20 , pp. 20-24
    • Tateishi, J.1
  • 93
    • 33749535361 scopus 로고    scopus 로고
    • Preparation of Amyloid β-Protein for Structural and Functional Studies
    • DOI 10.1016/S0076-6879(06)13002-5, PII S0076687906130025, Amyloid, Prions, and Other Protein Aggregates, Part C
    • DB Teplow 2006 Preparation of amyloid beta-protein for structural and functional studies Methods Enzymol 413 20 33 10.1016/S0076-6879(06)13002-5 17046389 (Pubitemid 44528683)
    • (2006) Methods in Enzymology , vol.413 , pp. 20-33
    • Teplow, D.B.1
  • 94
    • 0037465708 scopus 로고    scopus 로고
    • Insights into the amyloid folding problem from solid-state NMR
    • DOI 10.1021/bi027378p
    • R Tycko 2003 Insights into the amyloid folding problem from solid-state NMR Biochemistry 42 3151 3159 10.1021/bi027378p 12641446 (Pubitemid 36348623)
    • (2003) Biochemistry , vol.42 , Issue.11 , pp. 3151-3159
    • Tycko, R.1
  • 96
    • 45549109796 scopus 로고    scopus 로고
    • Inflammation, genes and Zn in Alzheimer's disease
    • 10.1016/j.brainresrev.2007.12.001
    • S Vasto G Candore F Listi, et al. 2008 Inflammation, genes and Zn in Alzheimer's disease Brain Res Brain Res Rev 58 96 105 10.1016/j.brainresrev. 2007.12.001
    • (2008) Brain Res Brain Res Rev , vol.58 , pp. 96-105
    • Vasto, S.1    Candore, G.2    Listi, F.3
  • 97
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid β-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • DOI 10.1002/psc.573
    • Y Verdier M Zarándi B Penke 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 10.1002/psc.573 15160835 (Pubitemid 38594184)
    • (2004) Journal of Peptide Science , vol.10 , Issue.5 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 98
    • 4043088415 scopus 로고    scopus 로고
    • The role of beta amyloid in Alzheimer's disease: Still a cause of everything or the only one who got caught?
    • DOI 10.1016/j.phrs.2003.12.028, PII S104366180400091X
    • G Verdile S Fuller CS Atwood SM Laws SE Gandy RN Martins 2004 The role of beta amyloid in Alzheimer's disease: still a cause of everything or the only one who got caught? Pharmacol Res 50 397 409 10.1016/j.phrs.2003.12.028 15304237 (Pubitemid 39078531)
    • (2004) Pharmacological Research , vol.50 , Issue.4 , pp. 397-409
    • Verdile, G.1    Fuller, S.2    Atwood, C.S.3    Laws, S.M.4    Gandy, S.E.5    Martins, R.N.6
  • 99
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers - A decade of discovery
    • DOI 10.1111/j.1471-4159.2006.04426.x
    • DM Walshe DJ Selkoe 2007 Aβ oligomers a decade of discovery J Neurochem 101 1172 1184 10.1111/j.1471-4159.2006.04426.x (Pubitemid 46718812)
    • (2007) Journal of Neurochemistry , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 100
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • 10.1021/bi001048s 10978169
    • DM Walsh BP Tseng RE Rydel MB Podlisny DJ Selkoe 2000 The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain Biochemistry 39 10831 10839 10.1021/bi001048s 10978169
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 101
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation
    • DOI 10.1523/JNEUROSCI.4391-04.2005
    • DM Walsh M Townsend MB Podlisny GM Shankar JV Fadeeva OE Agnaf DM Hartley DJ Selkoe 2005 Certain inhibitors of sy thetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation J Neurosci 25 2455 2462 10.1523/JNEUROSCI.4391-04.2005 15758153 (Pubitemid 40365155)
    • (2005) Journal of Neuroscience , vol.25 , Issue.10 , pp. 2455-2462
    • Walsh, D.M.1    Townsend, M.2    Podlisny, M.B.3    Shankar, G.M.4    Fadeeva, J.V.5    El Agnaf, O.6    Hartley, D.M.7    Selkoe, D.J.8
  • 103
    • 33646384419 scopus 로고    scopus 로고
    • Immunology and immunotherapy of Alzheimer's disease
    • 10.1038/nri1843 16639431
    • HL Weiner D Frenkel 2006 Immunology and immunotherapy of Alzheimer's disease Nat Rev Immunol 6 404 416 10.1038/nri1843 16639431
    • (2006) Nat Rev Immunol , vol.6 , pp. 404-416
    • Weiner, H.L.1    Frenkel, D.2
  • 104
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygenand nitrogen species: Role in inflammatory disease and progression to cancer
    • 8546679
    • H Wiseman B Halliwell 1996 Damage to DNA by reactive oxygenand nitrogen species: role in inflammatory disease and progression to cancer Biochem J 313 17 29 8546679
    • (1996) Biochem J , vol.313 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2
  • 105
    • 0031461082 scopus 로고    scopus 로고
    • Biology of Aβ amyloid in Alzheimer's disease
    • DOI 10.1006/nbdi.1997.0147
    • T Wisniewski J Ghiso B Frangione 1997 Biology of Aβ amyloid in Alzheimer's disease Neurobiol Dis 4 313 328 10.1006/nbdi.1997.0147 9440120 (Pubitemid 28018660)
    • (1997) Neurobiology of Disease , vol.4 , Issue.5 , pp. 313-328
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 107
    • 0035910374 scopus 로고    scopus 로고
    • The Ginkgo biloba extract EGb 761 rescues the PC12 neuronal cells from β-amyloid-induced cell death by inhibiting the formation of β-amyloid-derived diffusible neurotoxic ligands
    • DOI 10.1016/S0006-8993(00)03131-0, PII S0006899300031310
    • Z Yao K Drieu V Papadopoulos 2001 The Ginkgo biloba extract EGb 761 rescues the PC12 neuronal cells from beta-amyloid-induced cell death by inhibiting the formation of beta-amyloid-derived diffusible neurotoxic ligands Brain Res 889 181 190 10.1016/S0006-8993(00)03131-0 11166702 (Pubitemid 32146280)
    • (2001) Brain Research , vol.889 , Issue.1-2 , pp. 181-190
    • Yao, Z.-X.1    Drieu, K.2    Papadopoulos, V.3
  • 108
    • 34548179335 scopus 로고    scopus 로고
    • γ-secretase substrate concentration modulates the Aβ42/Aβ40 ratio: Implications for Alzheimer disease
    • DOI 10.1074/jbc.M704601200
    • YI Yin B Bassit L Zhu X Yang C Wang YM Li 2007 Alzheimer's disease: Mental plaque removal J Biol Chem 28 23639 23644 10.1074/jbc.M704601200 (Pubitemid 47311934)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23639-23644
    • Ye, I.Y.1    Bassit, B.2    Zhu, L.3    Yang, X.4    Wang, C.5    Li, Y.-M.6
  • 109
    • 34548179335 scopus 로고    scopus 로고
    • γ-secretase substrate concentration modulates the Aβ42/Aβ40 ratio: Implications for Alzheimer disease
    • DOI 10.1074/jbc.M704601200
    • YI Yin B Bassit L Zhu X Yang C Wang YM Li 2007 γ-Secretase substrate Concentration Modulates the Abeta42/Abeta40 Ratio: implications for Alzheimer's disease J Biol Chem 28 23639 23644 10.1074 jbc.M704601200 (Pubitemid 47311934)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23639-23644
    • Ye, I.Y.1    Bassit, B.2    Zhu, L.3    Yang, X.4    Wang, C.5    Li, Y.-M.6
  • 110
    • 16544373763 scopus 로고    scopus 로고
    • Gossypin protects primary cultured rat cortical cells from oxidative stress- and β-amyloid-induced toxicity
    • KH Yoon J Lee J Cho 2004 Gossypin protects primary cultured rat cortical cells from oxidative stress- and beta-amyloid-induced toxicity Arch Pharm Res 27 454 459 10.1007/BF02980089 15180313 (Pubitemid 43073744)
    • (2004) Archives of Pharmacal Research , vol.27 , Issue.4 , pp. 454-459
    • Yoon, I.1    Kwang, H.L.2    Cho, J.3
  • 111
    • 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)]
    • DOI 10.1034/j.1600-079X.2003.00058.x
    • Zatta P, Tognon G, Carampin P (2003) Melatonin prevents free radical formation due to the interaction between beta-amyloid peptides and metal ions. J Pineal Res 35:98-103. Al(III), Zn(II), Cu(II), Mn(II), Fe(II). doi: 10.1034/j.1600-079X.2003.00058.x (Pubitemid 36960348)
    • (2003) Journal of Pineal Research , vol.35 , Issue.2 , pp. 98-103
    • Zatta, P.1    Tognon, G.2    Carampin, P.3
  • 112
    • 0024652076 scopus 로고
    • Scavenging effect of extracts of green tea and natural antioxidants on active oxygen radicals
    • 2472207
    • BL Zhao X Li RG He SJ Cheng WJ Xin 1989 Scavenging effect of extracts of green tea and natural antioxidants on active oxygen radicals Cell Biophys 14 175 185 2472207
    • (1989) Cell Biophys , vol.14 , pp. 175-185
    • Zhao, B.L.1    Li, X.2    He, R.G.3    Cheng, S.J.4    Xin, W.J.5
  • 113
    • 10044283223 scopus 로고    scopus 로고
    • Mitochondrial failures in Alzheimer's disease
    • 10.1177/153331750401900611 15633943
    • X Zhu MA Smith G Perry G Aliev 2004 Mitochondrial failures in Alzheimer's disease Am J Alzheimers Dis Other Demen 19 345 352 10.1177/153331750401900611 15633943
    • (2004) Am J Alzheimers Dis Other Demen , vol.19 , pp. 345-352
    • Zhu, X.1    Smith, M.A.2    Perry, G.3    Aliev, G.4


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