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Volumn 27, Issue 4, 2011, Pages 767-779

Identification of polyphenolic compounds and black tea extract as potent inhibitors of lipid membrane destabilization by Aβ42 aggregates

Author keywords

Alzheimer's disease; amyloid ; black tea; liposomes; N benzylidene benzohydrazide; oligomers; polyphenols

Indexed keywords

8 N BENZYLIDENE BENZOHYDRAZIDE; AMYLOID BETA PROTEIN[1-42]; APIGENIN; BAICALEIN; BENZYLIDENE DERIVATIVE; BLACK TEA EXTRACT; FLAVONE; LIPOSOME; OLIGOMER; POLYPHENOL DERIVATIVE; STILBENE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 82955223925     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-2011-111061     Document Type: Article
Times cited : (47)

References (74)
  • 2
    • 0037202852 scopus 로고    scopus 로고
    • The dementias
    • DOI 10.1016/S0140-6736(02)11667-9
    • Ritchie K, Lovestone S (2002) The dementias. Lancet 360, 1759-1766 (Pubitemid 35447916)
    • (2002) Lancet , vol.360 , Issue.9347 , pp. 1759-1766
    • Ritchie, K.1    Lovestone, S.2
  • 3
    • 77953892400 scopus 로고    scopus 로고
    • Molecular mechanisms of neurodegeneration in Alzheimers disease
    • Crews L, Masliah E (2010) Molecular mechanisms of neurodegeneration in Alzheimers disease. Hum Mol Genet 19, R12-R20
    • (2010) Hum Mol Genet , vol.19
    • Crews, L.1    Masliah, E.2
  • 4
    • 67651180986 scopus 로고    scopus 로고
    • The amyloid hypothesis for Alzheimers disease: A critical reappraisal
    • Hardy J (2009) The amyloid hypothesis for Alzheimers disease: A critical reappraisal. J Neurochem 110, 1129-1134
    • (2009) J Neurochem , vol.110 , pp. 1129-1134
    • Hardy, J.1
  • 6
    • 0034521209 scopus 로고    scopus 로고
    • Neuropathology of Alzheimer's disease and related disorders
    • DOI 10.1016/S0733-8619(05)70229-2
    • Perl DP (2000) Neuropathology of Alzheimers disease and related disorders. Neurol Clin 18, 847-864 (Pubitemid 32042599)
    • (2000) Neurologic Clinics , vol.18 , Issue.4 , pp. 847-864
    • Perl, D.P.1
  • 8
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539 (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 9
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers in the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • DOI 10.2174/0929866043407174
    • Walsh DM, Selkoe DJ (2004) Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett 11, 213-228 (Pubitemid 38689025)
    • (2004) Protein and Peptide Letters , vol.11 , Issue.3 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 10
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid betaprotein impair synaptic plasticity and behavior
    • Selkoe DJ (2008) Soluble oligomers of the amyloid betaprotein impair synaptic plasticity and behavior. Behav Brain Res 192, 106-113
    • (2008) Behav Brain Res , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 14
    • 77953027786 scopus 로고    scopus 로고
    • Amyloid beta annular protofibrils in cell processes and synapses accumulate with aging and Alzheimer-associated genetic modification
    • 689285
    • Kokubo H, Kayed R, Glabe CG, Staufenbiel M, Saido TC, Iwata N,YamaguchiH(2009) Amyloid beta annular protofibrils in cell processes and synapses accumulate with aging and Alzheimer-associated genetic modification. Int J Alzheimers Dis pii: 689285, 1-7
    • (2009) Int J Alzheimers Dis Pii , pp. 1-7
    • Kokubo, H.1    Kayed, R.2    Glabe, C.G.3    Staufenbiel, M.4    Saido, T.C.5    Iwata, N.6    Yamaguchi, H.7
  • 15
    • 77957994639 scopus 로고    scopus 로고
    • Lipid membranes and beta-amyloid: A harmful connection
    • Eckert GP, Wood WG, Muller WE (2010) Lipid membranes and beta-amyloid: A harmful connection. Curr Protein Pept Sci 11, 319-325
    • (2010) Curr Protein Pept Sci , vol.11 , pp. 319-325
    • Eckert, G.P.1    Wood, W.G.2    Muller, W.E.3
  • 16
    • 0035942997 scopus 로고    scopus 로고
    • Profile of changes in lipid bilayer structure caused by β-amyloid peptide
    • DOI 10.1021/bi010417x
    • Kremer JJ, Sklansky DJ, Murphy RM (2001) Profile of changes in lipid bilayer structure caused by beta-amyloid peptide. Biochemistry 40, 8563-8571 (Pubitemid 32667263)
    • (2001) Biochemistry , vol.40 , Issue.29 , pp. 8563-8571
    • Kremer, J.J.1    Sklansky, D.J.2    Murphy, R.M.3
  • 17
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • DOI 10.1074/jbc.C400260200
    • Kayed R, Sokolov Y, Edmonds B, McIntire TM, Milton SC, Hall JE, GlabeCG(2004) Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 279, 46363-46366 (Pubitemid 39518276)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 19
    • 61549084018 scopus 로고    scopus 로고
    • Interaction between amyloid-beta (1-42) peptide and phospholipid bilayers: A molecular dynamics study
    • Davis CH, Berkowitz ML (2009) Interaction between amyloid-beta (1-42) peptide and phospholipid bilayers: A molecular dynamics study. Biophys J 96, 785-797
    • (2009) Biophys J , vol.96 , pp. 785-797
    • Davis, C.H.1    Berkowitz, M.L.2
  • 20
    • 0028649480 scopus 로고
    • 2+ channels provides a mechanism for neuronal death in Alzheimers disease
    • 2+ channels provides a mechanism for neuronal death in Alzheimers disease. Ann N Y Acad Sci 747, 256-266
    • (1994) Ann N y Acad Sci , vol.747 , pp. 256-266
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 21
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • DOI 10.1096/fj.01-0377com
    • Lin H, Bhatia R, Lal R (2001) Amyloid beta protein forms ion channels: Implications for Alzheimers disease pathophysiology. FASEB J 15, 2433-2444 (Pubitemid 33063171)
    • (2001) FASEB Journal , vol.15 , Issue.13 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 22
    • 34547214510 scopus 로고    scopus 로고
    • Aβ ion channels. Prospects for treating Alzheimer's disease with Aβ channel blockers
    • DOI 10.1016/j.bbamem.2007.03.014, PII S0005273607001034
    • Arispe N, Diaz JC, Simakova O (2007) Abeta ion channels. Prospects for treating Alzheimers disease with Abeta channel blockers. Biochim Biophys Acta 1768, 1952-1965 (Pubitemid 47125852)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 1952-1965
    • Arispe, N.1    Diaz, J.C.2    Simakova, O.3
  • 23
    • 77957969964 scopus 로고    scopus 로고
    • Neurotoxicity of beta-amyloid protein: Oligomerization, channel formation, and calcium dyshomeostasis
    • Kawahara M (2010) Neurotoxicity of beta-amyloid protein: Oligomerization, channel formation, and calcium dyshomeostasis. Curr Pharm Des 16, 2779-2789
    • (2010) Curr Pharm des , vol.16 , pp. 2779-2789
    • Kawahara, M.1
  • 24
    • 79959216154 scopus 로고    scopus 로고
    • Membrane incorporation, channel formation, and disruption of calcium homeostasis by Alzheimers beta-amyloid protein
    • Kawahara M, Ohtsuka I, Yokoyama S, Kato-Negishi M, Sadakane Y (2011) Membrane incorporation, channel formation, and disruption of calcium homeostasis by Alzheimers beta-amyloid protein. Int J Alzheimers Dis 2011, 304583
    • (2011) Int J Alzheimers Dis 2011 , pp. 304-583
    • Kawahara, M.1    Ohtsuka, I.2    Yokoyama, S.3    Kato-Negishi, M.4    Sadakane, Y.5
  • 25
    • 37249067994 scopus 로고    scopus 로고
    • The cell-selective neurotoxicity of the Alzheimer's Aβ peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Aβ toxicity
    • DOI 10.1523/JNEUROSCI.3006-07.2007
    • Simakova O, Arispe NJ (2007) The cell-selective neurotoxicity of the Alzheimers Abeta peptide is determined by surface phosphatidylserine and cytosolicATP levels. Membrane binding is required for Abeta toxicity. J Neurosci 27, 13719-13729 (Pubitemid 350278273)
    • (2007) Journal of Neuroscience , vol.27 , Issue.50 , pp. 13719-13729
    • Simakova, O.1    Arispe, N.J.2
  • 26
    • 58149339635 scopus 로고    scopus 로고
    • Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity
    • Hung LW, Ciccotosto GD, Giannakis E, Tew DJ, Perez K, Masters CL, Cappai R, Wade JD, Barnham KJ (2008) Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity. J Neurosci 28, 11950-11958
    • (2008) J Neurosci , vol.28 , pp. 11950-11958
    • Hung, L.W.1    Ciccotosto, G.D.2    Giannakis, E.3    Tew, D.J.4    Perez, K.5    Masters, C.L.6    Cappai, R.7    Wade, J.D.8    Barnham, K.J.9
  • 27
    • 62649172167 scopus 로고    scopus 로고
    • Small molecule blockers of the Alzheimer Abeta calcium channel potently protect neurons from Abeta cytotoxicity
    • Diaz JC, Simakova O, Jacobson KA, Arispe N, Pollard HB (2009) Small molecule blockers of the Alzheimer Abeta calcium channel potently protect neurons from Abeta cytotoxicity. Proc Natl Acad Sci U S A 106, 3348-3353
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3348-3353
    • Diaz, J.C.1    Simakova, O.2    Jacobson, K.A.3    Arispe, N.4    Pollard, H.B.5
  • 28
    • 77955701756 scopus 로고    scopus 로고
    • Synaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating property
    • Sepulveda FJ, Parodi J, Peoples RW, Opazo C, Aguayo LG (2010) Synaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating property. PLoS One 5, e11820
    • (2010) PLoS One , vol.5
    • Sepulveda, F.J.1    Parodi, J.2    Peoples, R.W.3    Opazo, C.4    Aguayo, L.G.5
  • 30
    • 45549095784 scopus 로고    scopus 로고
    • Polyphenols as potential inhibitors of amyloid aggregation and toxicity: Possible significance to Alzheimers disease
    • Bastianetto S, Krantic S, Quirion R (2008) Polyphenols as potential inhibitors of amyloid aggregation and toxicity: Possible significance to Alzheimers disease. Mini Rev Med Chem 8, 429-435
    • (2008) Mini Rev Med Chem , vol.8 , pp. 429-435
    • Bastianetto, S.1    Krantic, S.2    Quirion, R.3
  • 31
    • 77951912863 scopus 로고    scopus 로고
    • Destabilizing Alzheimers Abeta(42 protofibrils with morin: Mechanistic insights from molecular dynamics simulations
    • Lemkul JA, Bevan DR (2010) Destabilizing Alzheimers Abeta(42) protofibrils with morin: Mechanistic insights from molecular dynamics simulations. Biochemistry 49, 3935-3946
    • (2010) Biochemistry , vol.49 , pp. 3935-3946
    • Lemkul, J.A.1    Bevan, D.R.2
  • 32
    • 79953199374 scopus 로고    scopus 로고
    • Biflavonoids are superior to monoflavonoids in inhibiting amyloid-beta toxicity and fibrillogenesis via accumulation of nontoxic oligomer-like structures
    • Thapa A, Woo ER, Chi EY, Sharoar MG, Jin HG, Shin SY, Park IS (2011) Biflavonoids are superior to monoflavonoids in inhibiting amyloid-beta toxicity and fibrillogenesis via accumulation of nontoxic oligomer-like structures. Biochemistry 50, 2445-2455
    • (2011) Biochemistry , vol.50 , pp. 2445-2455
    • Thapa, A.1    Woo, E.R.2    Chi, E.Y.3    Sharoar, M.G.4    Jin, H.G.5    Shin, S.Y.6    Park, I.S.7
  • 33
    • 79954437554 scopus 로고    scopus 로고
    • Inhibition and disaggregation of alpha-synuclein oligomers by natural polyphenolic compounds
    • Caruana M, Hogen T, Levin J, Hillmer A, Giese A, Vassallo N (2011) Inhibition and disaggregation of alpha-synuclein oligomers by natural polyphenolic compounds. FEBS Lett 585, 1113-1120
    • (2011) FEBS Lett , vol.585 , pp. 1113-1120
    • Caruana, M.1    Hogen, T.2    Levin, J.3    Hillmer, A.4    Giese, A.5    Vassallo, N.6
  • 35
    • 0033863355 scopus 로고    scopus 로고
    • Dietary intake and bioavailability of polyphenols
    • Scalbert A,Williamson G (2000) Dietary intake and bioavailability of polyphenols. J Nutr 130, 2073S-2085S (Pubitemid 30619386)
    • (2000) Journal of Nutrition , vol.130 , Issue.8
    • Scalbert, A.1    Williamson, G.2
  • 41
    • 44249116000 scopus 로고    scopus 로고
    • Green tea epigallocatechin-3-gallate (EGCG) reduces beta-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice
    • Rezai-Zadeh K, Arendash GW, Hou H, Fernandez F, Jensen M, Runfeldt M, Shytle RD, Tan J (2008) Green tea epigallocatechin-3-gallate (EGCG) reduces beta-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice. Brain Res 1214, 177-187
    • (2008) Brain Res , vol.1214 , pp. 177-187
    • Rezai-Zadeh, K.1    Arendash, G.W.2    Hou, H.3    Fernandez, F.4    Jensen, M.5    Runfeldt, M.6    Shytle, R.D.7    Tan, J.8
  • 42
    • 46749123053 scopus 로고    scopus 로고
    • Grape-derived polyphenolics prevent Abeta oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimers disease
    • Wang J, Ho L, Zhao W, Ono K, Rosensweig C, Chen L, Humala N, Teplow DB, Pasinetti GM (2008) Grape-derived polyphenolics prevent Abeta oligomerization and attenuate cognitive deterioration in a mouse model of Alzheimers disease. J Neurosci 28, 6388-6392
    • (2008) J Neurosci , vol.28 , pp. 6388-6392
    • Wang, J.1    Ho, L.2    Zhao, W.3    Ono, K.4    Rosensweig, C.5    Chen, L.6    Humala, N.7    Teplow, D.B.8    Pasinetti, G.M.9
  • 44
    • 73549106551 scopus 로고    scopus 로고
    • Phenolic compounds prevent Alzheimers pathology through different effects on the amyloid-beta aggregation pathway
    • Hamaguchi T, Ono K, Murase A, YamadaM(2009) Phenolic compounds prevent Alzheimers pathology through different effects on the amyloid-beta aggregation pathway. Am J Pathol 175, 2557-2565
    • (2009) Am J Pathol , vol.175 , pp. 2557-2565
    • Hamaguchi, T.1    Ono, K.2    Murase, A.3    Yamada, M.4
  • 45
    • 78649504377 scopus 로고    scopus 로고
    • Formulation of a medical food cocktail for Alzheimers disease: Beneficial effects on cognition and neuropathology in a mouse model of the disease
    • Parachikova A, Green KN, Hendrix C, LaFerla FM (2010) Formulation of a medical food cocktail for Alzheimers disease: Beneficial effects on cognition and neuropathology in a mouse model of the disease. PLoS One 5, e14015
    • (2010) PLoS One , vol.5
    • Parachikova, A.1    Green, K.N.2    Hendrix, C.3    Laferla, F.M.4
  • 46
    • 0035035829 scopus 로고    scopus 로고
    • Nutrition interventions in aging and age-associated disease
    • Meydani M (2001) Nutrition interventions in aging and ageassociated disease. Ann N Y Acad Sci 928, 226-235 (Pubitemid 32386084)
    • (2001) Annals of the New York Academy of Sciences , vol.928 , pp. 226-235
    • Meydani, M.1
  • 47
    • 0036752553 scopus 로고    scopus 로고
    • Natural extracts as possible protective agents of brain aging
    • DOI 10.1016/S0197-4580(02)00024-6, PII S0197458002000246
    • Bastianetto S, Quirion R (2002) Natural extracts as possible protective agents of brain aging. Neurobiol Aging 23, 891-897 (Pubitemid 35217714)
    • (2002) Neurobiology of Aging , vol.23 , Issue.5 , pp. 891-897
    • Bastianetto, S.1    Quirion, R.2
  • 48
    • 77349084360 scopus 로고    scopus 로고
    • Naturally occurring phytochemicals for the prevention of Alzheimers disease
    • Kim J, Lee HJ, Lee KW (2010) Naturally occurring phytochemicals for the prevention of Alzheimers disease. J Neurochem 112, 1415-1430
    • (2010) J Neurochem , vol.112 , pp. 1415-1430
    • Kim, J.1    Lee, H.J.2    Lee, K.W.3
  • 49
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • DOI 10.1074/jbc.M608207200
    • Necula M, Kayed R, Milton S, Glabe CG (2007) Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282, 10311-10324 (Pubitemid 47093410)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 52
    • 0023730552 scopus 로고
    • Transmembrane calcium movements mediated by ionomycin and phosphatidate in liposomes with Fura 2 entrapped
    • Blau L,Weissmann G (1988) Transmembrane calcium movements mediated by ionomycin and phosphatidate in liposomes with Fura 2 entrapped. Biochemistry 27, 5661-5666
    • (1988) Biochemistry , vol.27 , pp. 5661-5666
    • Blau, L.1    Weissmann, G.2
  • 53
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibril formation
    • DOI 10.1016/S0076-6879(99)09022-9
    • Naiki H, Gejyo F (1999) Kinetic analysis of amyloid fibril formation. Methods Enzymol 309, 305-318 (Pubitemid 29446457)
    • (1999) Methods in Enzymology , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 54
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation
    • DOI 10.1110/ps.041266605
    • Hortschansky P, Schroeckh V, Christopeit T, Zandomeneghi G, Fandrich M (2005) The aggregation kinetics of Alzheimers beta-amyloid peptide is controlled by stochastic nucleation. Protein Sci 14, 1753-1759 (Pubitemid 40994145)
    • (2005) Protein Science , vol.14 , Issue.7 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fandrich, M.5
  • 56
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • DOI 10.1074/jbc.M500997200
    • Demuro A, Mina E, Kayed R, Milton SC, Parker I, Glabe CG (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280, 17294-17300 (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
  • 57
    • 33751516396 scopus 로고    scopus 로고
    • Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure
    • DOI 10.1085/jgp.200609533
    • Sokolov Y, Kozak JA, Kayed R, Chanturiya A, Glabe C, Hall JE (2006) Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure. J Gen Physiol 128, 637-647 (Pubitemid 44833376)
    • (2006) Journal of General Physiology , vol.128 , Issue.6 , pp. 637-647
    • Sokolov, Y.1    Kozak, J.A.2    Kayed, R.3    Chanturiya, A.4    Glabe, C.5    Hall, J.E.6
  • 58
    • 58149277415 scopus 로고    scopus 로고
    • Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: Implications for cell toxicity
    • Valincius G, Heinrich F, Budvytyte R, Vanderah DJ, McGillivray DJ, SokolovY, Hall JE, LoscheM(2008) Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: Implications for cell toxicity. Biophys J 95, 4845-4861
    • (2008) Biophys J , vol.95 , pp. 4845-4861
    • Valincius, G.1    Heinrich, F.2    Budvytyte, R.3    Vanderah, D.J.4    McGillivray, D.J.5    Sokolov, Y.6    Hall, J.E.7    Losche, M.8
  • 59
    • 77950685282 scopus 로고    scopus 로고
    • Simultaneous single-molecule fluorescence and conductivity studies reveal distinct classes of Abeta species on lipid bilayers
    • Schauerte JA,Wong PT,Wisser KC, Ding H, Steel DG, Gafni A (2010) Simultaneous single-molecule fluorescence and conductivity studies reveal distinct classes of Abeta species on lipid bilayers. Biochemistry 49, 3031-3039
    • (2010) Biochemistry , vol.49 , pp. 3031-3039
    • Schauerte, J.A.1    Wong, P.T.2    Wisser, K.C.3    Ding, H.4    Steel, D.G.5    Gafni, A.6
  • 60
    • 77957292133 scopus 로고    scopus 로고
    • Measurement of the attachment and assembly of small amyloid-beta oligomers on live cell membranes at physiological concentrations using single-molecule tools
    • Nag S, Chen J, Irudayaraj J, Maiti S (2010) Measurement of the attachment and assembly of small amyloid-beta oligomers on live cell membranes at physiological concentrations using single-molecule tools. Biophys J 99, 1969-1975
    • (2010) Biophys J , vol.99 , pp. 1969-1975
    • Nag, S.1    Chen, J.2    Irudayaraj, J.3    Maiti, S.4
  • 62
    • 30344445381 scopus 로고    scopus 로고
    • Ion channel formation by Alzheimer's disease amyloid β-peptide (Aβ40) in unilamellar liposomes is determined by anionic phospholipids
    • DOI 10.1016/j.peptides.2005.07.004, PII S0196978105003463
    • Alarcon JM, Brito JA, Hermosilla T, Atwater I, Mears D, Rojas E (2006) Ion channel formation by Alzheimers disease amyloid beta-peptide (Abeta40) in unilamellar liposomes is determined by anionic phospholipids. Peptides 27, 95-104 (Pubitemid 43061042)
    • (2006) Peptides , vol.27 , Issue.1 , pp. 95-104
    • Alarcon, J.M.1    Brito, J.A.2    Hermosilla, T.3    Atwater, I.4    Mears, D.5    Rojas, E.6
  • 63
    • 57449098698 scopus 로고    scopus 로고
    • In situ Abeta pores in AD brain are cylindrical assembly of Abeta protofilaments
    • Inoue S (2008) In situ Abeta pores in AD brain are cylindrical assembly of Abeta protofilaments. Amyloid 15, 223-233
    • (2008) Amyloid , vol.15 , pp. 223-233
    • Inoue, S.1
  • 64
    • 36249023636 scopus 로고    scopus 로고
    • Pore-forming proteins share structural and functional homology with amyloid oligomers
    • DOI 10.1007/s12017-007-0003-6
    • Yoshiike Y, Kayed R, Milton SC, Takashima A, Glabe CG (2007) Pore-forming proteins share structural and functional homology with amyloid oligomers. Neuromolecular Med 9, 270-275 (Pubitemid 350129702)
    • (2007) NeuroMolecular Medicine , vol.9 , Issue.3 , pp. 270-275
    • Yoshiike, Y.1    Kayed, R.2    Milton, S.C.3    Takashima, A.4    Glabe, C.G.5
  • 65
    • 79960722781 scopus 로고    scopus 로고
    • Understanding the broad-spectrum neuroprotective action profile of green tea polyphenols in aging and neurodegenerative diseases
    • Mandel SA, Amit T, Weinreb O, Youdim MB (2011) Understanding the broad-spectrum neuroprotective action profile of green tea polyphenols in aging and neurodegenerative diseases. J Alzheimers Dis 25, 187-208
    • (2011) J Alzheimers Dis , vol.25 , pp. 187-208
    • Mandel, S.A.1    Amit, T.2    Weinreb, O.3    Youdim, M.B.4
  • 66
    • 0141642253 scopus 로고    scopus 로고
    • Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease
    • DOI 10.1046/j.1471-4159.2003.01976.x
    • Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, Yamada M (2003) Potent anti-amyloidogenic and fibrildestabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimers disease. J Neurochem 87, 172-181 (Pubitemid 37210651)
    • (2003) Journal of Neurochemistry , vol.87 , Issue.1 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6
  • 67
    • 7044286419 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's β-amyloid fibrils in vitro
    • DOI 10.1016/j.bbadis.2004.06.008, PII S0925443904001024
    • Ono K, Hasegawa K, Naiki H, Yamada M (2004) Antiamyloidogenic activity of tannic acid and its activity to destabilize Alzheimers beta-amyloid fibrils in vitro. Biochim Biophys Acta 1690, 193-202 (Pubitemid 39423614)
    • (2004) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1690 , Issue.3 , pp. 193-202
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 68
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • DOI 10.1111/j.1747-0285.2005.00318.x
    • Porat Y, Abramowitz A, Gazit E (2006) Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism. Chem Biol Drug Des 67, 27-37 (Pubitemid 43881385)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 69
    • 77955639372 scopus 로고    scopus 로고
    • Beta amyloid aggregation inhibitors: Small molecules as candidate drugs for therapy of Alzheimers disease
    • Re F, Airoldi C, Zona C, Masserini M, La Ferla B, Quattrocchi N, Nicotra F (2010) Beta amyloid aggregation inhibitors: Small molecules as candidate drugs for therapy of Alzheimers disease. Curr Med Chem 17, 2990-3006
    • (2010) Curr Med Chem , vol.17 , pp. 2990-3006
    • Re, F.1    Airoldi, C.2    Zona, C.3    Masserini, M.4    La Ferla, B.5    Quattrocchi, N.6    Nicotra, F.7
  • 70
    • 79952796718 scopus 로고    scopus 로고
    • Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways
    • Reza AA, Ladiwala AR, Dordick JS, Tessier PM (2011) Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathways. J Biol Chem 286, 3209-3218
    • (2011) J Biol Chem , vol.286 , pp. 3209-3218
    • Reza, A.A.1    Ladiwala, A.R.2    Dordick, J.S.3    Tessier, P.M.4
  • 74
    • 77953434492 scopus 로고    scopus 로고
    • Natural product scaffolds as leads to drugs
    • Newman DJ, Cragg GM (2009) Natural product scaffolds as leads to drugs. Future Med Chem 1, 1415-1427
    • (2009) Future Med Chem , vol.1 , pp. 1415-1427
    • Newman, D.J.1    Cragg, G.M.2


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