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Volumn 110, Issue 10, 2013, Pages 3743-3748

Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-β species

Author keywords

Amyloid peptide; Amyloidogenesis; Metal ions; Natural products

Indexed keywords

(2,3) 5,7 DIHYDROXY 2 (3,4,5 TRIHYDROXYPHENYL) 3,4 DIHYDRO 2H 1 BENZOPYRAN 3 YL 3,4,5 TRIHYDROXYBENZOATE; AMYLOID BETA PROTEIN; COPPER ION; EPIGALLOCATECHIN GALLATE; GREEN TEA EXTRACT; METAL; MONOMER; NOOTROPIC AGENT; UNCLASSIFIED DRUG; ZINC;

EID: 84874609836     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1220326110     Document Type: Article
Times cited : (212)

References (51)
  • 1
    • 80155209561 scopus 로고    scopus 로고
    • Misfolded proteins in Alzheimer's disease and type II diabetes
    • DeToma AS, Salamekh S, Ramamoorthy A, Lim MH (2012) Misfolded proteins in Alzheimer's disease and type II diabetes. Chem Soc Rev 41(2):608-621.
    • (2012) Chem Soc Rev , vol.41 , Issue.2 , pp. 608-621
    • DeToma, A.S.1    Salamekh, S.2    Ramamoorthy, A.3    Lim, M.H.4
  • 2
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA (2004) Protein aggregation and neurodegenerative disease. Nat Med 10(Suppl):S10-S17.
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 84867460758 scopus 로고    scopus 로고
    • Bioinorganic chemistry of Alzheimer's disease
    • Kepp KP (2012) Bioinorganic chemistry of Alzheimer's disease. Chem Rev 112(10): 5193-5239.
    • (2012) Chem Rev , vol.112 , Issue.10 , pp. 5193-5239
    • Kepp, K.P.1
  • 4
    • 70349923038 scopus 로고    scopus 로고
    • Alzheimer's disease: From pathology to therapeutic approaches
    • Jakob-Roetne R, Jacobsen H (2009) Alzheimer's disease: From pathology to therapeutic approaches. Angew Chem Int Ed Engl 48(17):3030-3059.
    • (2009) Angew Chem Int Ed Engl , vol.48 , Issue.17 , pp. 3030-3059
    • Jakob-Roetne, R.1    Jacobsen, H.2
  • 5
    • 84866432813 scopus 로고    scopus 로고
    • Therapeutic redistribution of metal ions to treat Alzheimer's disease
    • Crouch PJ, Barnham KJ (2012) Therapeutic redistribution of metal ions to treat Alzheimer's disease. Acc Chem Res 45(9):1604-1611.
    • (2012) Acc Chem Res , vol.45 , Issue.9 , pp. 1604-1611
    • Crouch, P.J.1    Barnham, K.J.2
  • 6
    • 44849102395 scopus 로고    scopus 로고
    • Metals in neurobiology: Probing their chemistry and biology with molecular imaging
    • Que EL, Domaille DW, Chang CJ (2008) Metals in neurobiology: Probing their chemistry and biology with molecular imaging. Chem Rev 108(5):1517-1549.
    • (2008) Chem Rev , vol.108 , Issue.5 , pp. 1517-1549
    • Que, E.L.1    Domaille, D.W.2    Chang, C.J.3
  • 7
    • 84865127699 scopus 로고    scopus 로고
    • Copper and oxidative stress in the pathogenesis of Alzheimer's disease
    • Eskici G, Axelsen PH (2012) Copper and oxidative stress in the pathogenesis of Alzheimer's disease. Biochemistry 51(32):6289-6311.
    • (2012) Biochemistry , vol.51 , Issue.32 , pp. 6289-6311
    • Eskici, G.1    Axelsen, P.H.2
  • 8
    • 84859651929 scopus 로고    scopus 로고
    • Metal-associated amyloid-β species in Alzheimer's disease
    • Pithadia AS, Lim MH (2012) Metal-associated amyloid-β species in Alzheimer's disease. Curr Opin Chem Biol 16(1-2):67-73.
    • (2012) Curr Opin Chem Biol , vol.16 , Issue.1-2 , pp. 67-73
    • Pithadia, A.S.1    Lim, M.H.2
  • 9
    • 84864566040 scopus 로고    scopus 로고
    • The art of building multifunctional metal-binding agents from basic molecular scaffolds for the potential application in neurodegenerative diseases
    • Rodríguez-Rodríguez C, Telpoukhovskaia M, Orvig C (2012) The art of building multifunctional metal-binding agents from basic molecular scaffolds for the potential application in neurodegenerative diseases. Coord Chem Rev 256(19-20):2308-2332.
    • (2012) Coord Chem Rev , vol.256 , Issue.19-20 , pp. 2308-2332
    • Rodríguez-Rodríguez, C.1    Telpoukhovskaia, M.2    Orvig, C.3
  • 10
    • 79251569872 scopus 로고    scopus 로고
    • Recent development of bifunctional small molecules to study metal-amyloid-β species in Alzheimer's disease
    • Braymer JJ, DeToma AS, Choi J-S, Ko KS, Lim MH (2011) Recent development of bifunctional small molecules to study metal-amyloid-β species in Alzheimer's disease. Int J Alzheimers Dis 2011:623051.
    • (2011) Int J Alzheimers Dis , vol.2011 , pp. 623051
    • Braymer, J.J.1    Detoma, A.S.2    Choi, J.-S.3    Ko, K.S.4    Lim, M.H.5
  • 11
    • 77149144132 scopus 로고    scopus 로고
    • Minding metals: Tailoring multifunctional chelating agents for neurodegenerative disease
    • Perez LR, Franz KJ (2010) Minding metals: Tailoring multifunctional chelating agents for neurodegenerative disease. Dalton Trans 39(9):2177-2187.
    • (2010) Dalton Trans , vol.39 , Issue.9 , pp. 2177-2187
    • Perez, L.R.1    Franz, K.J.2
  • 12
    • 84870541207 scopus 로고    scopus 로고
    • Reactivity of diphenylpropynone derivatives toward metalassociated amyloid-β species
    • Pithadia AS, et al. (2012) Reactivity of diphenylpropynone derivatives toward metalassociated amyloid-β species. Inorg Chem 51(23):12959-12967.
    • (2012) Inorg Chem , vol.51 , Issue.23 , pp. 12959-12967
    • Pithadia, A.S.1
  • 13
    • 84868337362 scopus 로고    scopus 로고
    • 42 peptide
    • 42 peptide. J Am Chem Soc 134(15):6625-6636.
    • (2012) J Am Chem Soc , vol.134 , Issue.15 , pp. 6625-6636
    • Sharma, A.K.1
  • 14
    • 78650669293 scopus 로고    scopus 로고
    • Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity
    • Choi J-S, Braymer JJ, Nanga RPR, Ramamoorthy A, Lim MH (2010) Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity. Proc Natl Acad Sci USA 107(51):21990-21995.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.51 , pp. 21990-21995
    • Choi, J.-S.1    Braymer, J.J.2    Nanga, R.P.R.3    Ramamoorthy, A.4    Lim, M.H.5
  • 15
    • 80155213679 scopus 로고    scopus 로고
    • Development of bifunctional stilbene derivatives for targeting and modulating metal-amyloid-β species
    • Braymer JJ, et al. (2011) Development of bifunctional stilbene derivatives for targeting and modulating metal-amyloid-β species. Inorg Chem 50(21):10724-10734.
    • (2011) Inorg Chem , vol.50 , Issue.21 , pp. 10724-10734
    • Braymer, J.J.1
  • 16
    • 63149091152 scopus 로고    scopus 로고
    • Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease
    • Rodríguez-Rodríguez C, et al. (2009) Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease. J Am Chem Soc 131(4):1436-1451.
    • (2009) J Am Chem Soc , vol.131 , Issue.4 , pp. 1436-1451
    • Rodríguez-Rodríguez, C.1
  • 17
    • 70450202390 scopus 로고    scopus 로고
    • Small molecule modulators of copper-induced Aβ aggregation
    • Hindo SS, et al. (2009) Small molecule modulators of copper-induced Aβ aggregation. J Am Chem Soc 131(46):16663-16665.
    • (2009) J Am Chem Soc , vol.131 , Issue.46 , pp. 16663-16665
    • Hindo, S.S.1
  • 18
    • 57649130599 scopus 로고    scopus 로고
    • Sequestration of copper from β-amyloid promotes selective lysis by cyclen-hybrid cleavage agents
    • Wu W-h, et al. (2008) Sequestration of copper from β-amyloid promotes selective lysis by cyclen-hybrid cleavage agents. J Biol Chem 283(46):31657-31664.
    • (2008) J Biol Chem , vol.283 , Issue.46 , pp. 31657-31664
    • Wu, W.-H.1
  • 19
    • 33745096194 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism
    • 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(1):27-37.
    • (2006) Chem Biol Drug des , vol.67 , Issue.1 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 20
    • 44849087785 scopus 로고    scopus 로고
    • EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
    • Ehrnhoefer DE, et al. (2008) EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol 15(6):558-566.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.6 , pp. 558-566
    • Ehrnhoefer, D.E.1
  • 21
    • 77952346781 scopus 로고    scopus 로고
    • EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
    • Bieschke J, et al. (2010) EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity. Proc Natl Acad Sci USA 107(17):7710-7715.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.17 , pp. 7710-7715
    • Bieschke, J.1
  • 22
    • 79952796718 scopus 로고    scopus 로고
    • Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways
    • Ladiwala ARA, Dordick JS, Tessier PM (2011) Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways. J Biol Chem 286(5):3209-3218.
    • (2011) J Biol Chem , vol.286 , Issue.5 , pp. 3209-3218
    • Ladiwala, A.R.A.1    Dordick, J.S.2    Tessier, P.M.3
  • 23
    • 84864482811 scopus 로고    scopus 로고
    • Morin inhibits the early stages of amyloid β-peptide aggregation by altering tertiary and quaternary interactions to produce "off-pathway" structures
    • Lemkul JA, Bevan DR (2012) Morin inhibits the early stages of amyloid β-peptide aggregation by altering tertiary and quaternary interactions to produce "off-pathway" structures. Biochemistry 51(30):5990-6009.
    • (2012) Biochemistry , vol.51 , Issue.30 , pp. 5990-6009
    • Lemkul, J.A.1    Bevan, D.R.2
  • 24
    • 84862851209 scopus 로고    scopus 로고
    • Comparison of three amyloid assembly inhibitors: The sugar scyllo-inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01
    • Sinha S, et al. (2012) Comparison of three amyloid assembly inhibitors: The sugar scyllo-inositol, the polyphenol epigallocatechin gallate, and the molecular tweezer CLR01. ACS Chem Neurosci 3(6):451-458.
    • (2012) ACS Chem Neurosci , vol.3 , Issue.6 , pp. 451-458
    • Sinha, S.1
  • 25
    • 84864281808 scopus 로고    scopus 로고
    • Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomers
    • Lopez del Amo JM, et al. (2012) Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomers. J Mol Biol 421(4-5):517-524.
    • (2012) J Mol Biol , vol.421 , Issue.4-5 , pp. 517-524
    • Del Amo, J.M.L.1
  • 26
    • 79955977168 scopus 로고    scopus 로고
    • Myricetin: A naturally occurring regulator of metal-induced amyloid-β aggregation and neurotoxicity
    • DeToma AS, Choi J-S, Braymer JJ, Lim MH (2011) Myricetin: A naturally occurring regulator of metal-induced amyloid-β aggregation and neurotoxicity. ChemBioChem 12(8):1198-1201.
    • (2011) ChemBioChem , vol.12 , Issue.8 , pp. 1198-1201
    • DeToma, A.S.1    Choi, J.-S.2    Braymer, J.J.3    Lim, M.H.4
  • 27
    • 77349084360 scopus 로고    scopus 로고
    • Naturally occurring phytochemicals for the prevention of Alzheimer's disease
    • Kim J, Lee HJ, Lee KW (2010) Naturally occurring phytochemicals for the prevention of Alzheimer's disease. J Neurochem 112(6):1415-1430.
    • (2010) J Neurochem , vol.112 , Issue.6 , pp. 1415-1430
    • Kim, J.1    Lee, H.J.2    Lee, K.W.3
  • 28
    • 77956595088 scopus 로고    scopus 로고
    • The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity
    • Meng F, Abedini A, Plesner A, Verchere CB, Raleigh DP (2010) The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry 49(37):8127-8133.
    • (2010) Biochemistry , vol.49 , Issue.37 , pp. 8127-8133
    • Meng, F.1    Abedini, A.2    Plesner, A.3    Verchere, C.B.4    Raleigh, D.P.5
  • 29
    • 77954572992 scopus 로고    scopus 로고
    • Inhibition by flavonoids of amyloid-like fibril formation by Plasmodium falciparum merozoite surface protein 2
    • Chandrashekaran IR, Adda CG, MacRaild CA, Anders RF, Norton RS (2010) Inhibition by flavonoids of amyloid-like fibril formation by Plasmodium falciparum merozoite surface protein 2. Biochemistry 49(28):5899-5908.
    • (2010) Biochemistry , vol.49 , Issue.28 , pp. 5899-5908
    • Chandrashekaran, I.R.1    Adda, C.G.2    MacRaild, C.A.3    Anders, R.F.4    Norton, R.S.5
  • 30
    • 80051784700 scopus 로고    scopus 로고
    • EGCG disaggregates amyloid-like fibrils formed by Plasmodium falciparum merozoite surface protein 2
    • Chandrashekaran IR, Adda CG, MacRaild CA, Anders RF, Norton RS (2011) EGCG disaggregates amyloid-like fibrils formed by Plasmodium falciparum merozoite surface protein 2. Arch Biochem Biophys 513(2):153-157.
    • (2011) Arch Biochem Biophys , vol.513 , Issue.2 , pp. 153-157
    • Chandrashekaran, I.R.1    Adda, C.G.2    MacRaild, C.A.3    Anders, R.F.4    Norton, R.S.5
  • 31
    • 84858973650 scopus 로고    scopus 로고
    • Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286)
    • Popovych N, et al. (2012) Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286). J Phys Chem B 116(11):3650-3658.
    • (2012) J Phys Chem B , vol.116 , Issue.11 , pp. 3650-3658
    • Popovych, N.1
  • 32
    • 84860223167 scopus 로고    scopus 로고
    • Influence of pH on the speciation of copper(II) in reactions with the green tea polyphenols, epigallocatechin gallate and gallic acid
    • Pirker KF, Baratto MC, Basosi R, Goodman BA (2012) Influence of pH on the speciation of copper(II) in reactions with the green tea polyphenols, epigallocatechin gallate and gallic acid. J Inorg Biochem 112:10-16.
    • (2012) J Inorg Biochem , vol.112 , pp. 10-16
    • Pirker, K.F.1    Baratto, M.C.2    Basosi, R.3    Goodman, B.A.4
  • 33
    • 48649085493 scopus 로고    scopus 로고
    • 2+ enhances inhibitory effects of EGCG on the growth of PC-3 cells
    • 2+ enhances inhibitory effects of EGCG on the growth of PC-3 cells. Mol Nutr Food Res 52(4):465-471.
    • (2008) Mol Nutr Food Res , vol.52 , Issue.4 , pp. 465-471
    • Sun, S.L.1
  • 34
    • 84874083952 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging of amyloid-β aggregation kinetics in the presence of epigallocatechin gallate and metals
    • 10.1021/ac303181q
    • Cheng XR, et al. (2013) Surface plasmon resonance imaging of amyloid-β aggregation kinetics in the presence of epigallocatechin gallate and metals. Anal Chem, 10.1021/ac303181q.
    • (2013) Anal Chem
    • Cheng, X.R.1
  • 36
    • 67849106670 scopus 로고    scopus 로고
    • Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
    • Bernstein SL, et al. (2009) Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat Chem 1(4): 326-331.
    • (2009) Nat Chem , vol.1 , Issue.4 , pp. 326-331
    • Bernstein, S.L.1
  • 37
    • 70350597464 scopus 로고    scopus 로고
    • Effects of clioquinol on metaltriggered amyloid-β aggregation revisited
    • Mancino AM, Hindo SS, Kochi A, Lim MH (2009) Effects of clioquinol on metaltriggered amyloid-β aggregation revisited. Inorg Chem 48(20):9596-9598.
    • (2009) Inorg Chem , vol.48 , Issue.20 , pp. 9596-9598
    • Mancino, A.M.1    Hindo, S.S.2    Kochi, A.3    Lim, M.H.4
  • 38
    • 84867488912 scopus 로고    scopus 로고
    • Alternative pathways of human islet amyloid polypeptide aggregation distinguished by 19F nuclear magnetic resonance-detected kinetics of monomer consumption
    • Suzuki Y, Brender JR, Hartman K, Ramamoorthy A, Marsh ENG (2012) Alternative pathways of human islet amyloid polypeptide aggregation distinguished by 19F nuclear magnetic resonance-detected kinetics of monomer consumption. Biochemistry 51(41):8154-8162.
    • (2012) Biochemistry , vol.51 , Issue.41 , pp. 8154-8162
    • Suzuki, Y.1    Brender, J.R.2    Hartman, K.3    Ramamoorthy, A.4    Marsh, E.N.G.5
  • 39
    • 77953912267 scopus 로고    scopus 로고
    • Mass spectrometry and the amyloid problem-how far can we go in the gas phase?
    • Ashcroft AE (2010) Mass spectrometry and the amyloid problem-how far can we go in the gas phase? J Am Soc Mass Spectrom 21(7):1087-1096.
    • (2010) J Am Soc Mass Spectrom , vol.21 , Issue.7 , pp. 1087-1096
    • Ashcroft, A.E.1
  • 40
    • 79955972936 scopus 로고    scopus 로고
    • Insight into amyloid structure using chemical probes
    • Reinke AA, Gestwicki JE (2011) Insight into amyloid structure using chemical probes. Chem Biol Drug Des 77(6):399-411.
    • (2011) Chem Biol Drug des , vol.77 , Issue.6 , pp. 399-411
    • Reinke, A.A.1    Gestwicki, J.E.2
  • 41
    • 0034001363 scopus 로고    scopus 로고
    • Direct measurement of islet amyloid polypeptide fibrillogenesis by mass spectrometry
    • Larson JL, Ko E, Miranker AD (2000) Direct measurement of islet amyloid polypeptide fibrillogenesis by mass spectrometry. Protein Sci 9(2):427-431.
    • (2000) Protein Sci , vol.9 , Issue.2 , pp. 427-431
    • Larson, J.L.1    Ko, E.2    Miranker, A.D.3
  • 42
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation
    • Hortschansky P, Schroeckh V, Christopeit T, Zandomeneghi G, Fändrich M (2005) The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation. Protein Sci 14(7):1753-1759.
    • (2005) Protein Sci , vol.14 , Issue.7 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fändrich, M.5
  • 43
    • 33644526613 scopus 로고    scopus 로고
    • Amyloid β-protein monomer structure: A computational and experimental study
    • Baumketner A, et al. (2006) Amyloid β-protein monomer structure: A computational and experimental study. Protein Sci 15(3):420-428.
    • (2006) Protein Sci , vol.15 , Issue.3 , pp. 420-428
    • Baumketner, A.1
  • 44
    • 77958179943 scopus 로고    scopus 로고
    • Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
    • El-Hawiet A, Kitova EN, Liu L, Klassen JS (2010) Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry. J Am Soc Mass Spectrom 21(11):1893-1899.
    • (2010) J Am Soc Mass Spectrom , vol.21 , Issue.11 , pp. 1893-1899
    • El-Hawiet, A.1    Kitova, E.N.2    Liu, L.3    Klassen, J.S.4
  • 45
    • 77956307401 scopus 로고    scopus 로고
    • Thermodynamic analysis of the molecular interactions between amyloid β-peptide 42 and (-)-epigallocatechin-3-gallate
    • Wang S-H, Liu F-F, Dong X-Y, Sun Y (2010) Thermodynamic analysis of the molecular interactions between amyloid β-peptide 42 and (-)-epigallocatechin-3-gallate. J Phys Chem B 114(35):11576-11583.
    • (2010) J Phys Chem B , vol.114 , Issue.35 , pp. 11576-11583
    • Wang, S.-H.1    Liu, F.-F.2    Dong, X.-Y.3    Sun, Y.4
  • 47
    • 70350153272 scopus 로고    scopus 로고
    • The chemistry of Alzheimer's disease
    • Rauk A (2009) The chemistry of Alzheimer's disease. Chem Soc Rev 38(9):2698-2715.
    • (2009) Chem Soc Rev , vol.38 , Issue.9 , pp. 2698-2715
    • Rauk, A.1
  • 48
    • 80052489511 scopus 로고    scopus 로고
    • Effect of zinc binding on β-amyloid structure and dynamics: Implications for Aβ aggregation
    • Rezaei-Ghaleh N, Giller K, Becker S, Zweckstetter M (2011) Effect of zinc binding on β-amyloid structure and dynamics: Implications for Aβ aggregation. Biophys J 101(5): 1202-1211.
    • (2011) Biophys J , vol.101 , Issue.5 , pp. 1202-1211
    • Rezaei-Ghaleh, N.1    Giller, K.2    Becker, S.3    Zweckstetter, M.4
  • 49
    • 72949094439 scopus 로고    scopus 로고
    • Copper and zinc binding to amyloid-β: Coordination, dynamics, aggregation, reactivity and metal-ion transfer
    • Faller P (2009) Copper and zinc binding to amyloid-β: Coordination, dynamics, aggregation, reactivity and metal-ion transfer. ChemBioChem 10(18):2837-2845.
    • (2009) ChemBioChem , vol.10 , Issue.18 , pp. 2837-2845
    • Faller, P.1
  • 50
    • 33748887803 scopus 로고    scopus 로고
    • Structural information from ion mobility measurements: Effects of the long-range potential
    • Mesleh MF, Hunter JM, Shvartsburg AA, Schatz GC, Jarrold MF (1996) Structural information from ion mobility measurements: Effects of the long-range potential. J Phys Chem 100(40):16082-16086.
    • (1996) J Phys Chem , vol.100 , Issue.40 , pp. 16082-16086
    • Mesleh, M.F.1    Hunter, J.M.2    Shvartsburg, A.A.3    Schatz, G.C.4    Jarrold, M.F.5
  • 51
    • 0030580028 scopus 로고    scopus 로고
    • An exact hard-spheres scattering model for the mobilities of polyatomic ions
    • Shvartsburg AA, Jarrold MF (1996) An exact hard-spheres scattering model for the mobilities of polyatomic ions. Chem Phys Lett 261(1-2):86-91.
    • (1996) Chem Phys Lett , vol.261 , Issue.1-2 , pp. 86-91
    • Shvartsburg, A.A.1    Jarrold, M.F.2


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