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Volumn 34, Issue 6, 2009, Pages 1120-1128

The Polyphenol Piceid Destabilizes Preformed Amyloid Fibrils and Oligomers in Vitro: Hypothesis on Possible Molecular Mechanisms

Author keywords

Amyloid; Alzheimer's disease; Fibrils; Oligomers; Polyphenols

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; MONOMER; OLIGOMER; PICEID; POLYPHENOL; STILBENE DERIVATIVE;

EID: 64249166299     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-008-9883-6     Document Type: Article
Times cited : (56)

References (70)
  • 1
    • 0031038918 scopus 로고    scopus 로고
    • Alzheimer's disease: Genotypes, phenotypes, and treatments
    • 10.1126/science.275.5300.630
    • DJ Selkoe 1997 Alzheimer's disease: genotypes, phenotypes, and treatments Science 275 630 631 10.1126/science.275.5300.630
    • (1997) Science , vol.275 , pp. 630-631
    • Selkoe, D.J.1
  • 2
    • 34547156274 scopus 로고    scopus 로고
    • Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins
    • 10.1016/j.bbamem.2006.12.014 and references therein
    • RM Murphy 2007 Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins Biochim Biophys Acta 1768 1923 1934 10.1016/j.bbamem.2006.12.014 and references therein
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1923-1934
    • Murphy, R.M.1
  • 3
    • 33750082029 scopus 로고    scopus 로고
    • Disease modifying therapy for AD?
    • 10.1111/j.1471-4159.2006.04211.x
    • TE Golde 2006 Disease modifying therapy for AD? J Neurochem 99 689 707 10.1111/j.1471-4159.2006.04211.x
    • (2006) J Neurochem , vol.99 , pp. 689-707
    • Golde, T.E.1
  • 4
    • 0033977086 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis: Themes and variations
    • 10.1016/S0959-440X(99)00049-4 and references therein
    • JC Rochet PT Lansbury Jr 2000 Amyloid fibrillogenesis: themes and variations Curr Opin Struct Biol 10 60 68 10.1016/S0959-440X(99)00049-4 and references therein
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 60-68
    • Rochet, J.C.1    Lansbury Jr, P.T.2
  • 5
    • 0034973708 scopus 로고    scopus 로고
    • The relationship between the aggregational state of the amyloid-beta peptides and free radical generation by the peptides
    • 10.1046/j.1471-4159.2001.00392.x
    • A Monji H Utsumi T Ueda 2001 The relationship between the aggregational state of the amyloid-beta peptides and free radical generation by the peptides J Neurochem 77 1425 1432 10.1046/j.1471-4159.2001.00392.x
    • (2001) J Neurochem , vol.77 , pp. 1425-1432
    • Monji, A.1    Utsumi, H.2    Ueda, T.3
  • 6
    • 2442457913 scopus 로고    scopus 로고
    • Protective effect of the xanthate, D609, on Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress in primary neuronal cells
    • 10.1080/1071576042000206478
    • R Sultana S Newman H Mohmmad-Abdul 2004 Protective effect of the xanthate, D609, on Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress in primary neuronal cells Free Radic Res 38 449 458 10.1080/ 1071576042000206478
    • (2004) Free Radic Res , vol.38 , pp. 449-458
    • Sultana, R.1    Newman, S.2    Mohmmad-Abdul, H.3
  • 7
    • 27744542593 scopus 로고    scopus 로고
    • Hydrogen peroxide is generated during the very early stages of aggregation of the amyloid peptides implicated in Alzheimer disease and familial British dementia
    • 10.1074/jbc.C500238200
    • BJ Tabner OM El-Agnaf S Turnbull 2005 Hydrogen peroxide is generated during the very early stages of aggregation of the amyloid peptides implicated in Alzheimer disease and familial British dementia J Biol Chem 280 35789 35792 10.1074/jbc.C500238200
    • (2005) J Biol Chem , vol.280 , pp. 35789-35792
    • Tabner, B.J.1    El-Agnaf, O.M.2    Turnbull, S.3
  • 8
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: Current status
    • 10.1016/S0196-9781(02)00067-0
    • BL Kagan Y Hirakura R Azimov 2002 The channel hypothesis of Alzheimer's disease: current status Peptides 23 1311 1315 10.1016/S0196-9781(02)00067-0
    • (2002) Peptides , vol.23 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3
  • 9
    • 0037016321 scopus 로고    scopus 로고
    • Apolipoprotein e modulates Alzheimer's Abeta(1-42)-induced oxidative damage to synaptosomes in an allele-specific manner
    • 10.1016/S0006-8993(01)03228-0
    • CM Lauderback J Kanski JM Hackett 2002 Apolipoprotein E modulates Alzheimer's Abeta(1-42)-induced oxidative damage to synaptosomes in an allele-specific manner Brain Res 924 90 97 10.1016/S0006-8993(01)03228-0
    • (2002) Brain Res , vol.924 , pp. 90-97
    • Lauderback, C.M.1    Kanski, J.2    Hackett, J.M.3
  • 10
    • 0033046060 scopus 로고    scopus 로고
    • Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): Regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease
    • 10.1016/S0014-5793(99)00586-4
    • UC Oppermann S Salim LO Tjernberg 1999 Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease FEBS Lett 451 238 242 10.1016/S0014-5793(99)00586-4
    • (1999) FEBS Lett , vol.451 , pp. 238-242
    • Oppermann, U.C.1    Salim, S.2    Tjernberg, L.O.3
  • 11
    • 4143138471 scopus 로고    scopus 로고
    • In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology
    • 10.1385/JMN:23:3:247
    • DM Holtzman 2004 In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology J Mol Neurosci 23 247 254 10.1385/JMN:23:3:247
    • (2004) J Mol Neurosci , vol.23 , pp. 247-254
    • Holtzman, D.M.1
  • 12
    • 4344659648 scopus 로고    scopus 로고
    • A synthetic peptide blocking the apolipoprotein E/beta-amyloid binding mitigates beta-amyloid toxicity and fibril formation in vitro and reduces beta-amyloid plaques in transgenic mice
    • M Sadowski J Pankiewicz H Scholtzova 2004 A synthetic peptide blocking the apolipoprotein E/beta-amyloid binding mitigates beta-amyloid toxicity and fibril formation in vitro and reduces beta-amyloid plaques in transgenic mice Am J Pathol 165 937 948
    • (2004) Am J Pathol , vol.165 , pp. 937-948
    • Sadowski, M.1    Pankiewicz, J.2    Scholtzova, H.3
  • 13
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • 10.1126/science.1091230
    • JW Lustbader M Cirilli C Lin 2004 ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease Science 304 448 452 10.1126/science.1091230
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 14
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • 10.1038/19866
    • DJ Selkoe 1999 Translating cell biology into therapeutic advances in Alzheimer's disease Nature 399 A23 A31 10.1038/19866
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 15
    • 0029896354 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • 10.1016/S0896-6273(00)80115-4
    • BA Yankner 1996 Mechanisms of neuronal degeneration in Alzheimer's disease Neuron 16 921 932 10.1016/S0896-6273(00)80115-4
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 16
    • 0025992417 scopus 로고
    • In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
    • 10.1016/0006-8993(91)91553-D
    • CJ Pike AJ Walencewicz CG Glabe 1991 In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity Brain Res 563 311 314 10.1016/0006-8993(91)91553-D
    • (1991) Brain Res , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3
  • 17
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • CJ Pike D Burdick AJ Walencewicz 1993 Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state J Neurosci 13 1676 1687
    • (1993) J Neurosci , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3
  • 18
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • 10.1073/pnas.91.25.12243
    • A Lorenzo BA Yankner 1994 Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red Proc Natl Acad Sci USA 91 12243 12247 10.1073/pnas.91.25.12243
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 19
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
    • 10.1038/ncb1104-1054
    • DJ Selkoe 2004 Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases Nat Cell Biol 6 1054 1061 10.1038/ncb1104-1054
    • (2004) Nat Cell Biol , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 20
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • 10.1073/pnas.95.11.6448
    • MP Lambert AK Barlow BA Chromy 1998 Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins Proc Natl Acad Sci USA 95 6448 6453 10.1073/pnas.95.11.6448
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 21
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • 10.1074/jbc.274.36.25945
    • DM Walsh DM Hartley Y Kusumoto 1999 Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates J Biol Chem 274 25945 25952 10.1074/jbc.274.36.25945
    • (1999) J Biol Chem , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3
  • 22
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: Evidence for AbetaP channel-mediated cellular toxicity
    • R Bhatia H Lin R Lal 2000 Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity FASEB J 14 1233 1243
    • (2000) FASEB J , vol.14 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 23
    • 0034089960 scopus 로고    scopus 로고
    • Fresh and nonfibrillar amyloid beta protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AbetaP-channel-mediated cellular toxicity
    • YJ Zhu H Lin R Lal 2000 Fresh and nonfibrillar amyloid beta protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AbetaP-channel-mediated cellular toxicity FASEB J 14 1244 1254
    • (2000) FASEB J , vol.14 , pp. 1244-1254
    • Zhu, Y.J.1    Lin, H.2    Lal, R.3
  • 24
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum?
    • 10.1016/S0166-2236(00)01749-5
    • WL Klein GA Krafft CE Finch 2001 Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 24 219 224 10.1016/S0166-2236(00)01749-5
    • (2001) Trends Neurosci , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 25
    • 0037271080 scopus 로고    scopus 로고
    • Selective neuronal degeneration induced by soluble oligomeric amyloid beta protein
    • HJ Kim SC Chae DK Lee 2003 Selective neuronal degeneration induced by soluble oligomeric amyloid beta protein FASEB J 17 118 120
    • (2003) FASEB J , vol.17 , pp. 118-120
    • Kim, H.J.1    Chae, S.C.2    Lee, D.K.3
  • 26
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • 10.1126/science.1072994 Erratum in: Science. 2002. 297:2209 and comment in: Science. 2002 298:962-964
    • J Hardy DJ Selkoe 2002 The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 353 356 10.1126/science.1072994 Erratum in: Science. 2002. 297:2209 and comment in: Science. 2002 298:962-964
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 27
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • 10.1126/science.1079469
    • R Kayed E Head JL Thompson 2003 Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 486 489 10.1126/science.1079469
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 28
    • 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
    • 10.1046/j.1471-4159.2003.01976.x
    • K Ono Y Yoshiike A Taskashima 2003 Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease J Neurochem 87 172 181 10.1046/j.1471-4159.2003.01976.x
    • (2003) J Neurochem , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Taskashima, A.3
  • 29
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro
    • 10.1002/jnr.20025
    • K Ono K Hasegawa H Naiki 2004 Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro J Neurosci Res 75 742 750 10.1002/jnr.20025
    • (2004) J Neurosci Res , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3
  • 30
    • 7044286419 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's beta-amyloid fibrils in vitro
    • K Ono K Hasegawa H Naiki 2004 Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's beta-amyloid fibrils in vitro Biochim Biophys Acta 1690 193 202
    • (2004) Biochim Biophys Acta , vol.1690 , pp. 193-202
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3
  • 31
    • 33845334891 scopus 로고    scopus 로고
    • Inhibitory activity of stilbenes on Alzheimer's beta-amyloid fibrils in vitro
    • 10.1016/j.bmc.2006.09.069
    • C Rivière T Richard L Quentin 2007 Inhibitory activity of stilbenes on Alzheimer's beta-amyloid fibrils in vitro Bioorg Med Chem 15 1160 1167 10.1016/j.bmc.2006.09.069
    • (2007) Bioorg Med Chem , vol.15 , pp. 1160-1167
    • Rivière, C.1    Richard, T.2    Quentin, L.3
  • 32
    • 38149091043 scopus 로고    scopus 로고
    • New polyphenols active on beta-amyloid aggregation
    • 10.1016/j.bmcl.2007.11.028
    • C Rivière T Richard X Vitrac 2008 New polyphenols active on beta-amyloid aggregation Bioorg Med Chem Lett 18 828 831 10.1016/j.bmcl.2007.11. 028
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 828-831
    • Rivière, C.1    Richard, T.2    Vitrac, X.3
  • 33
    • 20044370990 scopus 로고    scopus 로고
    • Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo
    • 10.1074/jbc.M404751200
    • F Yang GP Lim AN Begum 2005 Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo J Biol Chem 280 5892 5901 10.1074/jbc.M404751200
    • (2005) J Biol Chem , vol.280 , pp. 5892-5901
    • Yang, F.1    Lim, G.P.2    Begum, A.N.3
  • 34
    • 33644949188 scopus 로고    scopus 로고
    • Neuroprotective effects of green and black teas and their catechin gallate esters against beta-amyloid-induced toxicity
    • 10.1111/j.1460-9568.2005.04532.x
    • S Bastianetto ZX Yao V Papadopoulos 2006 Neuroprotective effects of green and black teas and their catechin gallate esters against beta-amyloid-induced toxicity Eur J NeuroSci 23 55 64 10.1111/j.1460-9568.2005.04532.x
    • (2006) Eur J NeuroSci , vol.23 , pp. 55-64
    • Bastianetto, S.1    Yao, Z.X.2    Papadopoulos, V.3
  • 35
    • 0038605152 scopus 로고    scopus 로고
    • The role of polyphenolic compounds in the diet as inhibitors of platelet function
    • 10.1079/PNS2003253
    • GP Hubbard S Wolffram JA Lovegrove 2003 The role of polyphenolic compounds in the diet as inhibitors of platelet function Proc Nutr Soc 62 469 478 10.1079/PNS2003253
    • (2003) Proc Nutr Soc , vol.62 , pp. 469-478
    • Hubbard, G.P.1    Wolffram, S.2    Lovegrove, J.A.3
  • 36
    • 14744302388 scopus 로고    scopus 로고
    • Dietary polyphenols and the prevention of diseases
    • 10.1080/1040869059096
    • A Scalbert C Manach C Morand 2005 Dietary polyphenols and the prevention of diseases Crit Rev Food Sci Nutr 45 287 306 10.1080/1040869059096
    • (2005) Crit Rev Food Sci Nutr , vol.45 , pp. 287-306
    • Scalbert, A.1    Manach, C.2    Morand, C.3
  • 37
    • 0035208862 scopus 로고    scopus 로고
    • Prevention of carcinogenesis by tea polyphenols
    • 10.1081/DMR-120000651
    • CS Yang S Prabhu J Landau 2001 Prevention of carcinogenesis by tea polyphenols Drug Metab Rev 33 237 253 10.1081/DMR-120000651
    • (2001) Drug Metab Rev , vol.33 , pp. 237-253
    • Yang, C.S.1    Prabhu, S.2    Landau, J.3
  • 38
    • 2442430353 scopus 로고    scopus 로고
    • Polyphenols: Food sources and bioavailability
    • C Manach A Scalbert C Morand 2004 Polyphenols: food sources and bioavailability Am J Clin Nutr 79 727 747
    • (2004) Am J Clin Nutr , vol.79 , pp. 727-747
    • Manach, C.1    Scalbert, A.2    Morand, C.3
  • 39
    • 56349157854 scopus 로고    scopus 로고
    • Benefits from dietary polyphenols for brain aging and Alzheimer's disease
    • (Published online)
    • Rossi L, Mazzitelli S, Arciello M et al. (2008) Benefits from dietary polyphenols for brain aging and Alzheimer's disease. Neurochem Res (Published online)
    • (2008) Neurochem Res
    • Rossi, L.1    Mazzitelli, S.2    Arciello, M.3
  • 40
    • 0035108722 scopus 로고    scopus 로고
    • NMR and simulated annealing investigations of bradykinin in presence of polyphenols
    • T Richard S Verge B Berke 2001 NMR and simulated annealing investigations of bradykinin in presence of polyphenols J Biomol Struct Dyn 18 627 637
    • (2001) J Biomol Struct Dyn , vol.18 , pp. 627-637
    • Richard, T.1    Verge, S.2    Berke, B.3
  • 41
    • 0037070358 scopus 로고    scopus 로고
    • Polyphenol/peptide binding and precipitation
    • 10.1021/jf010897z
    • AJ Charlton NJ Baxter ML Khan 2002 Polyphenol/peptide binding and precipitation J Agric Food Chem 50 1593 1601 10.1021/jf010897z
    • (2002) J Agric Food Chem , vol.50 , pp. 1593-1601
    • Charlton, A.J.1    Baxter, N.J.2    Khan, M.L.3
  • 42
    • 0037151680 scopus 로고    scopus 로고
    • Multiple conformations of the proline-rich protein/epigallocatechin gallate complex determined by time-averaged nuclear Overhauser effects
    • 10.1021/ja0126374
    • AJ Charlton E Haslam MP Williamson 2002 Multiple conformations of the proline-rich protein/epigallocatechin gallate complex determined by time-averaged nuclear Overhauser effects J Am Chem Soc 124 9899 9905 10.1021/ja0126374
    • (2002) J Am Chem Soc , vol.124 , pp. 9899-9905
    • Charlton, A.J.1    Haslam, E.2    Williamson, M.P.3
  • 43
    • 0037030762 scopus 로고    scopus 로고
    • First observation of solution structures of bradykinin-penta-O-galloyl-d- glucopyranose complexes as determined by NMR and simulated annealing
    • S Vergé T Richard S Moreau 2002 First observation of solution structures of bradykinin-penta-O-galloyl-d-glucopyranose complexes as determined by NMR and simulated annealing Biochim Biophys Acta 1571 89 101
    • (2002) Biochim Biophys Acta , vol.1571 , pp. 89-101
    • Vergé, S.1    Richard, T.2    Moreau, S.3
  • 44
    • 27944473247 scopus 로고    scopus 로고
    • Role of peptide primary sequence in polyphenol-protein recognition: An example with neurotensin
    • T Richard X Vitrac JM Merillon 2005 Role of peptide primary sequence in polyphenol-protein recognition: an example with neurotensin Biochim Biophys Acta 1726 238 243
    • (2005) Biochim Biophys Acta , vol.1726 , pp. 238-243
    • Richard, T.1    Vitrac, X.2    Merillon, J.M.3
  • 45
    • 0028069242 scopus 로고
    • Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy
    • 10.1111/j.1432-1033.1994.tb18574.x
    • NJ Murray MP Williamson TH Lilley 1994 Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy Eur J Biochem 219 923 935 10.1111/j.1432-1033.1994.tb18574.x
    • (1994) Eur J Biochem , vol.219 , pp. 923-935
    • Murray, N.J.1    Williamson, M.P.2    Lilley, T.H.3
  • 46
    • 0015977769 scopus 로고
    • Polyphenol-protein interactions
    • E Haslam 1974 Polyphenol-protein interactions Biochem J 139 285 288
    • (1974) Biochem J , vol.139 , pp. 285-288
    • Haslam, E.1
  • 47
    • 0347379774 scopus 로고    scopus 로고
    • Is the C-terminal region of bradykinin the binding site of polyphenols?
    • T Richard JC Delaunay JM Merillon 2003 Is the C-terminal region of bradykinin the binding site of polyphenols? J Biomol Struct Dyn 21 379 385
    • (2003) J Biomol Struct Dyn , vol.21 , pp. 379-385
    • Richard, T.1    Delaunay, J.C.2    Merillon, J.M.3
  • 48
    • 0041316992 scopus 로고    scopus 로고
    • Three-dimensional structure and dynamics of wine tannin-saliva protein complexes a multitechnique approach
    • 10.1021/bi034354p
    • C Simon K Barathieu M Laguerre 2003 Three-dimensional structure and dynamics of wine tannin-saliva protein complexes a multitechnique approach Biochemistry 42 10385 10395 10.1021/bi034354p
    • (2003) Biochemistry , vol.42 , pp. 10385-10395
    • Simon, C.1    Barathieu, K.2    Laguerre, M.3
  • 49
    • 0028302166 scopus 로고
    • Activation of macrophages by Alzheimer beta amyloid peptide
    • 10.1006/bbrc.1994.1326
    • A Klegeris DG Walker PL [tmp] McGeer 1994 Activation of macrophages by Alzheimer beta amyloid peptide Biochem Biophys Res Commun 199 984 991 10.1006/bbrc.1994.1326
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 984-991
    • Klegeris, A.1    Walker, D.G.2    McGeer, P.L.3
  • 50
    • 0028981219 scopus 로고
    • Structure-activity analyses of beta-amyloid peptides: Contributions of the beta 25-35 region to aggregation and neurotoxicity
    • CJ Pike AJ Walencewicz-Wasserman J Kosmoski 1995 Structure-activity analyses of beta-amyloid peptides: contributions of the beta 25-35 region to aggregation and neurotoxicity J Neurochem 64 253 265
    • (1995) J Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3
  • 51
    • 0034682788 scopus 로고    scopus 로고
    • Inhibition of toxicity in the beta-amyloid peptide fragment beta-(25-35) using N-methylated derivatives: A general strategy to prevent amyloid formation
    • 10.1074/jbc.M003554200
    • E Hughes RM Burke AJ Doig 2000 Inhibition of toxicity in the beta-amyloid peptide fragment beta-(25-35) using N-methylated derivatives: a general strategy to prevent amyloid formation J Biol Chem 275 25109 25115 10.1074/jbc.M003554200
    • (2000) J Biol Chem , vol.275 , pp. 25109-25115
    • Hughes, E.1    Burke, R.M.2    Doig, A.J.3
  • 52
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye thioflavine T
    • 10.1016/0003-2697(89)90046-8
    • H Naiki K Higuchi M Hosokawa 1989 Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye thioflavine T Anal Biochem 177 244 249 10.1016/0003-2697(89)90046-8
    • (1989) Anal Biochem , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3
  • 53
    • 0242424155 scopus 로고    scopus 로고
    • Self-assembly of Abeta (1-42) into globular neurotoxins
    • 10.1021/bi030029q
    • BA Chromy RJ Nowak MP Lambert 2003 Self-assembly of Abeta (1-42) into globular neurotoxins Biochemistry 42 12749 12760 10.1021/bi030029q
    • (2003) Biochemistry , vol.42 , pp. 12749-12760
    • Chromy, B.A.1    Nowak, R.J.2    Lambert, M.P.3
  • 54
    • 33644778691 scopus 로고    scopus 로고
    • Amyloid-beta peptide binds with heme to form a peroxidase: Relationship to the cytopathologies of Alzheimer's disease
    • 10.1073/pnas.0600134103
    • H Atamna K Boyle 2006 Amyloid-beta peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer's disease Proc Natl Acad Sci USA 103 3381 3386 10.1073/pnas.0600134103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3381-3386
    • Atamna, H.1    Boyle, K.2
  • 55
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • 10.1074/jbc.272.35.22364
    • DM Walsh A Lomakin GB Benedek 1997 Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate J Biol Chem 272 22364 22372 10.1074/jbc.272.35.22364
    • (1997) J Biol Chem , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3
  • 56
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid
    • 10.1038/nsmb1345
    • S Chimon MA Shaibat CR Jones 2007 Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid Nat Struct Mol Biol 14 1157 1164 10.1038/nsmb1345
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3
  • 57
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • MM Pallitto RM Murphy 2001 A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state Biophys J 81 1805 1822
    • (2001) Biophys J , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 58
    • 0037137225 scopus 로고    scopus 로고
    • Kinetic modeling and determination of reaction constants of Alzheimer's beta-amyloid fibril extension and dissociation using surface plasmon resonance
    • 10.1021/bi020369w
    • K Hasegawa K Ono M Yamada 2002 Kinetic modeling and determination of reaction constants of Alzheimer's beta-amyloid fibril extension and dissociation using surface plasmon resonance Biochemistry 41 13489 13498 10.1021/bi020369w
    • (2002) Biochemistry , vol.41 , pp. 13489-13498
    • Hasegawa, K.1    Ono, K.2    Yamada, M.3
  • 59
    • 24644438783 scopus 로고    scopus 로고
    • Ferulic acid destabilizes preformed beta-amyloid fibrils in vitro
    • 10.1016/j.bbrc.2005.08.148
    • K Ono M Hirohata M Yamada 2005 Ferulic acid destabilizes preformed beta-amyloid fibrils in vitro Biochem Biophys Res Commun 336 444 449 10.1016/j.bbrc.2005.08.148
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 444-449
    • Ono, K.1    Hirohata, M.2    Yamada, M.3
  • 60
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR
    • 10.1073/pnas.262663499
    • AT Petkova Y Ishii JJ Balbach 2002 A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR Proc Natl Acad Sci USA 99 16742 16747 10.1073/pnas.262663499
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Balbach, J.J.3
  • 61
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • 10.1021/bi051952q
    • AT Petkova WM Yau R Tycko 2006 Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils Biochemistry 45 498 512 10.1021/bi051952q
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 62
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-beta(1-42) fibrils
    • 10.1073/pnas.0506723102
    • T Lührs C Ritter M Adrian 2005 3D structure of Alzheimer's amyloid-beta(1-42) fibrils Proc Natl Acad Sci USA 102 17342 17347 10.1073/pnas.0506723102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17342-17347
    • Lührs, T.1    Ritter, C.2    Adrian, M.3
  • 63
    • 0028179865 scopus 로고
    • Alzheimer beta-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • 10.1021/bi00189a051
    • E Terzi G Hölzemann J Seelig 1994 Alzheimer beta-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes Biochemistry 33 7434 7441 10.1021/bi00189a051
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 64
    • 0035916279 scopus 로고    scopus 로고
    • Amyloid-induced aggregation and precipitation of soluble proteins: An electrostatic contribution of the Alzheimer's beta (25-35) amyloid fibril
    • 10.1021/bi002156h
    • T Konno 2001 Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta (25-35) amyloid fibril Biochemistry 40 2148 2154 10.1021/bi002156h
    • (2001) Biochemistry , vol.40 , pp. 2148-2154
    • Konno, T.1
  • 65
    • 0037173120 scopus 로고    scopus 로고
    • Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy
    • 10.1073/pnas.132098999
    • JH Ippel A Olofsson J Schleucher 2002 Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy Proc Natl Acad Sci USA 99 8648 8653 10.1073/pnas.132098999
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8648-8653
    • Ippel, J.H.1    Olofsson, A.2    Schleucher, J.3
  • 66
    • 14844327767 scopus 로고    scopus 로고
    • Reversible mechanical unzipping of amyloid beta-fibrils
    • 10.1074/jbc.M411556200
    • MS Kellermayer L Grama A Karsai 2005 Reversible mechanical unzipping of amyloid beta-fibrils J Biol Chem 280 8464 8470 10.1074/jbc.M411556200
    • (2005) J Biol Chem , vol.280 , pp. 8464-8470
    • Kellermayer, M.S.1    Grama, L.2    Karsai, A.3
  • 67
    • 0035251678 scopus 로고    scopus 로고
    • Nicotine and amyloid formation
    • 10.1016/S0006-3223(00)01111-2
    • H Zeng Y Zhang L Peng 2001 Nicotine and amyloid formation Biol Psychiatry 49 248 257 10.1016/S0006-3223(00)01111-2
    • (2001) Biol Psychiatry , vol.49 , pp. 248-257
    • Zeng, H.1    Zhang, Y.2    Peng, L.3
  • 68
    • 0346099098 scopus 로고    scopus 로고
    • Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation
    • 10.1002/jnr.10859
    • R Liu C [tmp] McAllister Y Lyubchenko 2004 Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation J Neurosci Res 75 162 171 10.1002/jnr.10859
    • (2004) J Neurosci Res , vol.75 , pp. 162-171
    • Liu, R.1    McAllister, C.2    Lyubchenko, Y.3
  • 69
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation- susceptible" regions in proteins associated with neurodegenerative diseases
    • 10.1016/j.jmb.2005.04.016
    • AP Pawar KF Dubay J Zurdo 2005 Prediction of "aggregation- prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases J Mol Biol 350 379 392 10.1016/j.jmb.2005.04.016
    • (2005) J Mol Biol , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3
  • 70
    • 33748473035 scopus 로고    scopus 로고
    • Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide
    • 10.1529/biophysj.105.079186 and references therein
    • G Wei JE Shea 2006 Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide Biophys J 91 1638 1647 10.1529/biophysj.105.079186 and references therein
    • (2006) Biophys J , vol.91 , pp. 1638-1647
    • Wei, G.1    Shea, J.E.2


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