메뉴 건너뛰기




Volumn 1, Issue 10, 2010, Pages 691-701

Inhibition of AΒ42 peptide aggregation by a binuclear ruthenium(II)-Platinum(II) complex: Potential for multimetal organometallics as anti-amyloid agents

Author keywords

aggregation; Amyloid; and intercalation; cisplatin; inhibitor; organometallics; platinum(II); ruthenium(II)

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; ORGANOMETALLIC COMPOUND; PLATINUM COMPLEX; PROTEIN AGGREGATION INHIBITOR; PROTEIN INHIBITOR; RUTHENIUM COMPLEX; UNCLASSIFIED DRUG;

EID: 77958449833     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn100046m     Document Type: Article
Times cited : (57)

References (61)
  • 2
    • 0031695197 scopus 로고    scopus 로고
    • Projections of Alzheimers disease in the United States and the public health impact of delaying disease onset
    • Brookmeyer, R., Gray, S., and Kawas, C. (1998) Projections of Alzheimers disease in the United States and the public health impact of delaying disease onset Am. J. Public Health 88, 1337-1342
    • (1998) Am. J. Public Health , vol.88 , pp. 1337-1342
    • Brookmeyer, R.1    Gray, S.2    Kawas, C.3
  • 3
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimers disease: Progress and problems on the road to therapeutics
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimers disease: Progress and problems on the road to therapeutics Science 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 5
    • 11144356498 scopus 로고    scopus 로고
    • Dimeric amyloid beta protein rapidly accumulates in lipid rafts followed by apolipoprotein e and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimers disease
    • Kawarabayashi, T., Shoji, M., Younkin, L. H., Wen-Lang, L., Dickson, D. W., Murakami, T., Matsubara, E., Abe, K., Ashe, K. H., and Younkin, S. G. (2004) Dimeric amyloid beta protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimers disease J. Neurosci. 24, 3801-3809
    • (2004) J. Neurosci. , vol.24 , pp. 3801-3809
    • Kawarabayashi, T.1    Shoji, M.2    Younkin, L.H.3    Wen-Lang, L.4    Dickson, D.W.5    Murakami, T.6    Matsubara, E.7    Abe, K.8    Ashe, K.H.9    Younkin, S.G.10
  • 6
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimers disease
    • Klein, W. L., Stine, W. B., Jr., and Teplow, D. B. (2004) Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimers disease Neurobiol. Aging 25, 569-580
    • (2004) Neurobiol. Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine, Jr.W.B.2    Teplow, D.B.3
  • 7
    • 0345352748 scopus 로고    scopus 로고
    • Prevention of peptide fibril formation in an aqueous environment by mutation of a single residue to Aib
    • Kumita, J. R., Weston, C. J., Choo-Smith, L. P., Woolley, G. A., and Smart, O. S. (2003) Prevention of peptide fibril formation in an aqueous environment by mutation of a single residue to Aib Biochemistry 42, 4492-4498
    • (2003) Biochemistry , vol.42 , pp. 4492-4498
    • Kumita, J.R.1    Weston, C.J.2    Choo-Smith, L.P.3    Woolley, G.A.4    Smart, O.S.5
  • 8
    • 0031873102 scopus 로고    scopus 로고
    • Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimers therapy
    • Soto, C., Sigurdsson, E. M., Morelli, L., Kumar, R. A., Castano, E. M., and Frangione, B. (1998) Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimers therapy Nat. Med. 4, 822-826
    • (1998) Nat. Med. , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 9
    • 33747484171 scopus 로고    scopus 로고
    • N-Methylated peptide inhibitors of Β-amyloid aggregation and toxicity. Optimization of the inhibitor structure
    • Kokkoni, N., Stott, K., Amijee, H., Mason, J. M., and Doig, A. J. (2006) N-Methylated peptide inhibitors of Β-amyloid aggregation and toxicity. Optimization of the inhibitor structure Biochemistry 45, 9906-9918
    • (2006) Biochemistry , vol.45 , pp. 9906-9918
    • Kokkoni, N.1    Stott, K.2    Amijee, H.3    Mason, J.M.4    Doig, A.J.5
  • 12
    • 7044286419 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimers beta-amyloid fibrils in vitro
    • Ono, K., Hasegawa, K., Naiki, H., and Yamada, M. (2004) Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimers 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    Yamada, M.4
  • 13
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimers beta-amyloid fibrils in vitro
    • Ono, K., Hasegawa, K., Naiki, H., and Yamada, M. (2004) Curcumin has potent anti-amyloidogenic effects for Alzheimers beta-amyloid fibrils in vitro J. Neurosci. Res. 75, 742-750
    • (2004) J. Neurosci. Res. , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 14
    • 0036860349 scopus 로고    scopus 로고
    • Metal complexing agents as therapies for Alzheimers disease
    • Bush, A. I. (2002) Metal complexing agents as therapies for Alzheimers disease Neurobiol. Aging 23, 1031-1038
    • (2002) Neurobiol. Aging , vol.23 , pp. 1031-1038
    • Bush, A.I.1
  • 15
    • 0037386086 scopus 로고    scopus 로고
    • The metallobiology of Alzheimers disease
    • Bush, A. I. (2003) The metallobiology of Alzheimers disease Trends Neurosci. 26, 207-214
    • (2003) Trends Neurosci. , vol.26 , pp. 207-214
    • Bush, A.I.1
  • 16
    • 0141594627 scopus 로고    scopus 로고
    • Copper, beta-amyloid, and Alzheimers disease: Tapping a sensitive connection
    • Bush, A. I., Masters, C. L., and Tanzi, R. E. (2003) Copper, beta-amyloid, and Alzheimers disease: Tapping a sensitive connection Proc. Natl. Acad. Sci. U.S.A. 100, 11193-11194
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11193-11194
    • Bush, A.I.1    Masters, C.L.2    Tanzi, R.E.3
  • 17
    • 0033517053 scopus 로고    scopus 로고
    • Binding of Zn(II), Cu(II), and Fe(II) ions to Alzheimers A beta peptide studied by fluorescence
    • Garzon-Rodriguez, W., Yatsimirsky, A. K., and Glabe, C. G. (1999) Binding of Zn(II), Cu(II), and Fe(II) ions to Alzheimers A beta peptide studied by fluorescence Bioorg. Med. Chem. Lett. 9, 2243-2248
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2243-2248
    • Garzon-Rodriguez, W.1    Yatsimirsky, A.K.2    Glabe, C.G.3
  • 19
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta1-42
    • Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., and Bush, A. I. (2000) Characterization of copper interactions with alzheimer amyloid beta peptides: identification of an attomolar-affinity copper binding site on amyloid beta1-42 J. Neurochem. 75, 1219-1233
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 20
    • 16844373633 scopus 로고    scopus 로고
    • N-Terminal deletions modify the Cu2+ binding site in amyloid-beta
    • Karr, J. W., Akintoye, H., Kaupp, L. J., and Szalai, V. A. (2005) N-Terminal deletions modify the Cu2+ binding site in amyloid-beta Biochemistry 44, 5478-5487
    • (2005) Biochemistry , vol.44 , pp. 5478-5487
    • Karr, J.W.1    Akintoye, H.2    Kaupp, L.J.3    Szalai, V.A.4
  • 22
    • 0034117603 scopus 로고    scopus 로고
    • Clinical perspectives on platinum resistance
    • Giaccone, G. (2000) Clinical perspectives on platinum resistance Drugs 59, 9-17
    • (2000) Drugs , vol.59 , pp. 9-17
    • Giaccone, G.1
  • 24
    • 0041426460 scopus 로고    scopus 로고
    • Platinum-based anticancer agents: Innovative design strategies and biological perspectives
    • Ho, Y.-P., Au-Yeung, S. C. F., and To, K. K. W. (2003) Platinum-based anticancer agents: Innovative design strategies and biological perspectives Med. Res. Rev. 23, 633-655
    • (2003) Med. Res. Rev. , vol.23 , pp. 633-655
    • Ho, Y.-P.1    Au-Yeung, S.C.F.2    To, K.K.W.3
  • 26
    • 0038037451 scopus 로고    scopus 로고
    • Synthesis, characterization, and DNA binding properties of a series of Ru, Pt mixed-metal complexes
    • Williams, R. L., Toft, H. N., Winkel, B., and Brewer, K. J. (2003) Synthesis, characterization, and DNA binding properties of a series of Ru, Pt mixed-metal complexes Inorg. Chem. 42, 4394-4400
    • (2003) Inorg. Chem. , vol.42 , pp. 4394-4400
    • Williams, R.L.1    Toft, H.N.2    Winkel, B.3    Brewer, K.J.4
  • 27
    • 0008236226 scopus 로고
    • Spectroscopic, electrochemical and spectroelectrochemical investigations of mixed-metal Os(II)/Ru(II) bimetallic complexes incorporating polypyridyl bridging ligands
    • Richter, M. M. and Brewer, K. J. (1992) Spectroscopic, electrochemical and spectroelectrochemical investigations of mixed-metal Os(II)/Ru(II) bimetallic complexes incorporating polypyridyl bridging ligands Inorg. Chem. 31, 1594-1598
    • (1992) Inorg. Chem. , vol.31 , pp. 1594-1598
    • Richter, M.M.1    Brewer, K.J.2
  • 28
    • 33751385478 scopus 로고
    • Osmium/ruthenium trimetallics incorporating polyazine bridging ligands: Isovalent NIR absorbers with unique electrochemical behavior
    • Richter, M. M. and Brewer, K. J. (1993) Osmium/ruthenium trimetallics incorporating polyazine bridging ligands: Isovalent NIR absorbers with unique electrochemical behavior Inorg. Chem. 32, 5762-5768
    • (1993) Inorg. Chem. , vol.32 , pp. 5762-5768
    • Richter, M.M.1    Brewer, K.J.2
  • 29
    • 33751385781 scopus 로고
    • Investigation of the spectroscopic, electrochemical and spectroelectrochemical properties of Os(II) complexes incorporating polyazine bridging ligands: Formation of the Os,Os and Os,Ru mixed-valence complexes
    • Richter, M. M. and Brewer, K. J. (1993) Investigation of the spectroscopic, electrochemical and spectroelectrochemical properties of Os(II) complexes incorporating polyazine bridging ligands: Formation of the Os,Os and Os,Ru mixed-valence complexes Inorg. Chem. 32, 2827-2834
    • (1993) Inorg. Chem. , vol.32 , pp. 2827-2834
    • Richter, M.M.1    Brewer, K.J.2
  • 30
    • 0027171772 scopus 로고
    • A new class of DNA metallobinders showing spectator ligand size selectivity: Binding of ligand-bridged bimetallic complexes of ruthenium(II) to calf thymus DNA
    • Carlson, D. L., Huchital, D. H., Mantilla, E. J., Sheardy, R. D., and Murphy, W. R., Jr. (1993) A new class of DNA metallobinders showing spectator ligand size selectivity: binding of ligand-bridged bimetallic complexes of ruthenium(II) to calf thymus DNA J. Am. Chem. Soc. 115, 6424-6425
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6424-6425
    • Carlson, D.L.1    Huchital, D.H.2    Mantilla, E.J.3    Sheardy, R.D.4    Murphy, Jr.W.R.5
  • 31
    • 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., and 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
    • (2006) Chem. Biol. Drug Des. , vol.67 , pp. 27-37
    • Porat, Y.1    Abramowitz, A.2    Gazit, E.3
  • 32
    • 61749097242 scopus 로고    scopus 로고
    • Pleomorphic copper coodination by Alzheimers disease amyloid-Β peptide
    • Drew, S. C., Noble, C. J., Masters, C. L., Hanson, G. R., and Barnham, K. J. (2009) Pleomorphic copper coodination by Alzheimers disease amyloid-Β peptide J. Am. Chem. Soc. 131, 1195-1207
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1195-1207
    • Drew, S.C.1    Noble, C.J.2    Masters, C.L.3    Hanson, G.R.4    Barnham, K.J.5
  • 33
    • 72949092936 scopus 로고    scopus 로고
    • Pluse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-Β peptide: A key role of the first two N-terminus residues
    • Dorlet, P., Gambarelli, S., Faller, P., and Hureau, C. (2009) Pluse EPR spectroscopy reveals the coordination sphere of copper(II) ions in the 1-16 amyloid-Β peptide: A key role of the first two N-terminus residues Angew. Chem., Int. Ed. 48, 9273-9276
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 9273-9276
    • Dorlet, P.1    Gambarelli, S.2    Faller, P.3    Hureau, C.4
  • 34
    • 73249137909 scopus 로고    scopus 로고
    • Deprotonation of the Asp1-Ala2 peptide bond induces modification of the dynamic copper(II) environment in the amyloid-Β peptide near physiological pH
    • Hureau, C., Coppel, Y., Dorlet, P., Solari, P. L., Sayen, S., Guillon, E., Sabater, L., and Faller, P. (2009) Deprotonation of the Asp1-Ala2 peptide bond induces modification of the dynamic copper(II) environment in the amyloid-Β peptide near physiological pH Angew. Chem., Int. Ed. 48, 9522-9525
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 9522-9525
    • Hureau, C.1    Coppel, Y.2    Dorlet, P.3    Solari, P.L.4    Sayen, S.5    Guillon, E.6    Sabater, L.7    Faller, P.8
  • 36
    • 0032559003 scopus 로고    scopus 로고
    • Apolipoprotein e and antioxidants have different mechanisms of inhibiting Alzheimers Β-amyloid fibril formation in vitro
    • Naiki, H., Hasegawa, K., Yamaguchi, I., Nakamura, H., Gejyo, F., and Nakakuki, K. (1998) Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimers Β-amyloid fibril formation in vitro Biochemistry 37, 17882-17889
    • (1998) Biochemistry , vol.37 , pp. 17882-17889
    • Naiki, H.1    Hasegawa, K.2    Yamaguchi, I.3    Nakamura, H.4    Gejyo, F.5    Nakakuki, K.6
  • 37
    • 35648986681 scopus 로고    scopus 로고
    • Amyloid-Β(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate
    • Rangachari, V., Moore, B. D., Reed, D. K., Bridges, A. W., Conboy, E., Hartigan, D., and Rosenberry, T. L. (2007) Amyloid-Β(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate Biochemistry 46, 12451-12462
    • (2007) Biochemistry , vol.46 , pp. 12451-12462
    • Rangachari, V.1    Moore, B.D.2    Reed, D.K.3    Bridges, A.W.4    Conboy, E.5    Hartigan, D.6    Rosenberry, T.L.7
  • 40
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 41
    • 71549121663 scopus 로고    scopus 로고
    • Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-beta oligomers
    • Moore, B. D., Rangachari, V., Tay, W. M., Milkovic, N. M., and Rosenberry, T. L. (2009) Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-beta oligomers Biochemistry 48, 11796-11806
    • (2009) Biochemistry , vol.48 , pp. 11796-11806
    • Moore, B.D.1    Rangachari, V.2    Tay, W.M.3    Milkovic, N.M.4    Rosenberry, T.L.5
  • 42
    • 33750343755 scopus 로고    scopus 로고
    • New water-soluble platinum(II) phenanthroline complexes tested as cisplatin analogues: First-time comparison of cytotoxic activity between analogous four- and five-coordinate species
    • De Pascali, S. A., Migoni, D., Papadia, P., Muscella, A., Marsigliante, S., Ciccarese, A., and Fanizzi, F. P. (2006) New water-soluble platinum(II) phenanthroline complexes tested as cisplatin analogues: First-time comparison of cytotoxic activity between analogous four- and five-coordinate species Dalton Trans. 5077-5087
    • (2006) Dalton Trans. , pp. 5077-5087
    • De Pascali, S.A.1    Migoni, D.2    Papadia, P.3    Muscella, A.4    Marsigliante, S.5    Ciccarese, A.6    Fanizzi, F.P.7
  • 43
    • 33947088617 scopus 로고
    • Palladium(II) and platinum(II) alkyl sulfoxide complexes. Examples of sulfur-bonded, mixed sulfur- and oxygen-bonded, and totally oxygen-bonded complexes
    • Price, J. H., Williamson, A. N., Schramm, R. F., and Wayland, B. B. (1972) Palladium(II) and platinum(II) alkyl sulfoxide complexes. Examples of sulfur-bonded, mixed sulfur- and oxygen-bonded, and totally oxygen-bonded complexes Inorg. Chem. 11, 1280-1284
    • (1972) Inorg. Chem. , vol.11 , pp. 1280-1284
    • Price, J.H.1    Williamson, A.N.2    Schramm, R.F.3    Wayland, B.B.4
  • 45
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behavior
    • Becke, A. D. (1988) Density-functional exchange-energy approximation with correct asymptotic behavior Phys. Rev. A 38, 3098-3100
    • (1988) Phys. Rev. A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 46
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • Lee, C., Yang, W., and Parr, R. G. (1988) Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density Phys. Rev. B 37, 785-789
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 47
    • 0001218546 scopus 로고    scopus 로고
    • The accuracy of the pseudopotential approximation. 2. A comparison of various core sizes for indium pseudopotentials in calculations for spectroscopic constants of InH, InF, and InCl
    • Leininger, T., Nicklass, A., Stoll, H., Dolg, M., and Schwerdtfeger, P. (1996) The accuracy of the pseudopotential approximation. 2. A comparison of various core sizes for indium pseudopotentials in calculations for spectroscopic constants of InH, InF, and InCl J. Chem. Phys. 105, 1052-1059
    • (1996) J. Chem. Phys. , vol.105 , pp. 1052-1059
    • Leininger, T.1    Nicklass, A.2    Stoll, H.3    Dolg, M.4    Schwerdtfeger, P.5
  • 48
    • 84962426340 scopus 로고    scopus 로고
    • Hydrolysis theory for cisplatin and its analogues based on density functional studies
    • Zhang, Y., Guo, Z. J., and You, X. Z. (2001) Hydrolysis theory for cisplatin and its analogues based on density functional studies J. Am. Chem. Soc. 123, 9378-9387
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9378-9387
    • Zhang, Y.1    Guo, Z.J.2    You, X.Z.3
  • 49
    • 33746623718 scopus 로고    scopus 로고
    • NMR shifts, orbitals, and M center dot center dot center dot H-X bonding in d(8) square planar metal complexes
    • Zhang, Y., Lewis, J. C., Bergman, R. G., Ellman, J. A., and Oldfield, E. (2006) NMR shifts, orbitals, and M center dot center dot center dot H-X bonding in d(8) square planar metal complexes Organometallics 25, 3515-3519
    • (2006) Organometallics , vol.25 , pp. 3515-3519
    • Zhang, Y.1    Lewis, J.C.2    Bergman, R.G.3    Ellman, J.A.4    Oldfield, E.5
  • 50
    • 66149179255 scopus 로고    scopus 로고
    • Ru-based olefin metathesis catalysts bearing pH-responsive N-heterocyclic carbene (NHC) ligands: Activity control via degree of protonation
    • Balof, S. L., Yu, B., Lowe, A. B., Ling, Y., Zhang, Y., and Schanz, H. J. (2009) Ru-based olefin metathesis catalysts bearing pH-responsive N-heterocyclic carbene (NHC) ligands: Activity control via degree of protonation Eur. J. Inorg. Chem. 1717-1722
    • (2009) Eur. J. Inorg. Chem. , pp. 1717-1722
    • Balof, S.L.1    Yu, B.2    Lowe, A.B.3    Ling, Y.4    Zhang, Y.5    Schanz, H.J.6
  • 51
    • 71749097034 scopus 로고    scopus 로고
    • Preferential encapsulation and stability of La3N cluster in 80 atom cages: Experimental synthesis and computational investigation of La3N@C79N
    • Stevenson, S., Ling, Y., Coumbe, C. E., Mackey, M. A., Confait, B. S., Phillips, J. P., Dorn, H. C., and Zhang, Y. (2009) Preferential encapsulation and stability of La3N cluster in 80 atom cages: Experimental synthesis and computational investigation of La3N@C79N J. Am. Chem. Soc. 131, 17780-17782
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17780-17782
    • Stevenson, S.1    Ling, Y.2    Coumbe, C.E.3    MacKey, M.A.4    Confait, B.S.5    Phillips, J.P.6    Dorn, H.C.7    Zhang, Y.8
  • 52
    • 84962359221 scopus 로고    scopus 로고
    • Ab initio study of solvated molecules: A new implementation of the polarizable continuum model
    • Cossi, M., Barone, V., Cammi, R., and Tomasi, J. (1996) Ab initio study of solvated molecules: A new implementation of the polarizable continuum model Chem. Phys. Lett. 255, 327-335
    • (1996) Chem. Phys. Lett. , vol.255 , pp. 327-335
    • Cossi, M.1    Barone, V.2    Cammi, R.3    Tomasi, J.4
  • 53
    • 0032502372 scopus 로고    scopus 로고
    • Ab initio study of ionic solutions by a polarizable continuum dielectric model
    • Cossi, M., Barone, V., Mennucci, B., and Tomasi, J. (1998) Ab initio study of ionic solutions by a polarizable continuum dielectric model Chem. Phys. Lett. 286, 253-260
    • (1998) Chem. Phys. Lett. , vol.286 , pp. 253-260
    • Cossi, M.1    Barone, V.2    Mennucci, B.3    Tomasi, J.4
  • 54
    • 84961986752 scopus 로고    scopus 로고
    • New developments in the polarizable continuum model for quantum mechanical and classical calculations on molecules in solution
    • Cossi, M., Scalmani, G., Rega, N., and Barone, V. (2002) New developments in the polarizable continuum model for quantum mechanical and classical calculations on molecules in solution J. Chem. Phys. 117, 43-54
    • (2002) J. Chem. Phys. , vol.117 , pp. 43-54
    • Cossi, M.1    Scalmani, G.2    Rega, N.3    Barone, V.4
  • 55
    • 0031209054 scopus 로고    scopus 로고
    • A new integral equation formalism for the polarizable continuum model: Theoretical background and applications to isotropic and anisotropic dielectrics
    • Cances, E., Mennucci, B., and Tomasi, J. (1997) A new integral equation formalism for the polarizable continuum model: Theoretical background and applications to isotropic and anisotropic dielectrics J. Chem. Phys. 107, 3032-3041
    • (1997) J. Chem. Phys. , vol.107 , pp. 3032-3041
    • Cances, E.1    Mennucci, B.2    Tomasi, J.3
  • 56
    • 84961979198 scopus 로고    scopus 로고
    • Continuum solvation models: A new approach to the problem of solutes charge distribution and cavity boundaries
    • Mennucci, B. and Tomasi, J. (1997) Continuum solvation models: A new approach to the problem of solutes charge distribution and cavity boundaries J. Chem. Phys. 106, 5151-5158
    • (1997) J. Chem. Phys. , vol.106 , pp. 5151-5158
    • Mennucci, B.1    Tomasi, J.2
  • 58
    • 0037076539 scopus 로고    scopus 로고
    • Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy
    • Nichols, M. R., Moss, M. A., Reed, D. K., Lin, W. L., Mukhopadhyay, R., Hoh, J. H., and Rosenberry, T. L. (2002) Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy Biochemistry 41, 6115-6127
    • (2002) Biochemistry , vol.41 , pp. 6115-6127
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Lin, W.L.4    Mukhopadhyay, R.5    Hoh, J.H.6    Rosenberry, T.L.7
  • 60
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen, L., Khurana, R., Coats, A., Frokjaer, S., Brange, J., Vyas, S., Uversky, V. N., and Fink, A. L. (2001) Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism Biochemistry 8397-8409
    • (2001) Biochemistry , pp. 8397-8409
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 61
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimers disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H., 3rd. (1993) Thioflavine T interaction with synthetic Alzheimers disease beta-amyloid peptides: detection of amyloid aggregation in solution Protein Sci. 2, 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine Iii, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.