메뉴 건너뛰기




Volumn 3, Issue 9, 2007, Pages 1727-1738

Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEINS; HYDROGEN BONDS; HYDROPHOBICITY; SURFACE CHEMISTRY;

EID: 34848929022     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.0030173     Document Type: Article
Times cited : (182)

References (64)
  • 1
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • doi:10.1038/nature02264. Available:, Accessed 8 August 2007
    • Selkoe DJ (2003) Folding proteins in fatal ways. Nature 426: 900-904. doi:10.1038/nature02264. Available: http://dx.doi.org/10.1038/nature02264. Accessed 8 August 2007.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 2
    • 33750731675 scopus 로고    scopus 로고
    • 100 years and counting: Prospects for defeating Alzheimer disease
    • doi:10.1126/science.1132813, Accessed 8 August 2007
    • Roberson ED, Mucke L (2006) 100 years and counting: Prospects for defeating Alzheimer disease. Science 314: 781-784. doi:10.1126/science.1132813. http://dx.doi.org/10.1126/science.1132813. Accessed 8 August 2007.
    • (2006) Science , vol.314 , pp. 781-784
    • Roberson, E.D.1    Mucke, L.2
  • 3
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • doi:10.1038/nature05290. Available:, Accessed 8 August 2007
    • Lansbury PT, Lashuel HA (2006) A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443: 774-779. doi:10.1038/nature05290. Available: http://dx.doi.org/10.1038/nature05290. Accessed 8 August 2007.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 4
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM (1999) Protein misfolding, evolution and disease. Trends Biochem Sci 24: 329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 5
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • doi:10.1038/nature02261. Available:, Accessed 8 August 2007
    • Dobson CM (2003) Protein folding and misfolding. Nature 426: 884-890. doi:10.1038/nature02261. Available: http://dx.doi.org/10.1038/nature02261. Accessed 8 August 2007.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 6
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • doi:10.1146/annurev.biochem.75. 101304.123901. Available:, Accessed 8 August 2007
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366. doi:10.1146/annurev.biochem.75. 101304.123901. Available: http://dx.doi.org/10.1146/annurev.biochem.75.101304. 123901. Accessed 8 August 2007.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Abeta amyloid protofibrils by atomic force microscopy
    • Harper JD, Wong SS, Lieber CM, Lansbury PT (1997) Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem Biol 4: 119-125.
    • (1997) Chem Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 8
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein
    • Harper JD, Lieber CM, Lansbury PT (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chem Biol 4: 951-959.
    • (1997) Chem Biol , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 9
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB (1997) Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J Biol Chem 272: 22364-22372.
    • (1997) J Biol Chem , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 10
    • 12544259221 scopus 로고    scopus 로고
    • Reversal of protein aggregation provides evidence for multiple aggregated states
    • doi:10.1016/j.jmb.2004.11.067. Available:, Accessed 8 August 2007
    • Calamai M, Canale C, Relini A, Stefani M, Chiti F, et al. (2005) Reversal of protein aggregation provides evidence for multiple aggregated states. J Mol Biol 346: 603-616. doi:10.1016/j.jmb.2004.11.067. Available: http://dx.doi.org/10.1016/j.jmb.2004.11.067. Accessed 8 August 2007.
    • (2005) J Mol Biol , vol.346 , pp. 603-616
    • Calamai, M.1    Canale, C.2    Relini, A.3    Stefani, M.4    Chiti, F.5
  • 11
    • 30344457011 scopus 로고    scopus 로고
    • Probing the mechanism of amyloidogenesis through a tandem repeat of the pi3-sh3 domain suggests a generic model for protein aggregation and fibril formation
    • doi:10.1016/j.jmb.2005.11.034. Available:, Accessed 8 August 2007
    • Bader R, Bamford R, Zurdo J, Luisi BF, Dobson CM (2006) Probing the mechanism of amyloidogenesis through a tandem repeat of the pi3-sh3 domain suggests a generic model for protein aggregation and fibril formation. J Mol Biol 356: 189-208. doi:10.1016/j.jmb.2005.11.034. Available: http://dx.doi.org/10.1016/j.jmb.2005.11.034. Accessed 8 August 2007.
    • (2006) J Mol Biol , vol.356 , pp. 189-208
    • Bader, R.1    Bamford, R.2    Zurdo, J.3    Luisi, B.F.4    Dobson, C.M.5
  • 12
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • doi:10.1074/jbc.M102223200. Available:, Accessed 8 August 2007
    • Bitan G, Lomakin A, Teplow DB (2001) Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J Biol Chem 276: 35176-35184. doi:10.1074/jbc.M102223200. Available: http://dx.doi.org/10.1074/jbc.M102223200. Accessed 8 August 2007.
    • (2001) J Biol Chem , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 13
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
    • doi:10.1073/pnas.222681699, Accessed 8 August 2007
    • Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, et al. (2003) Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci U S A 100: 330-335. doi:10.1073/pnas.222681699. http://dx.doi.org/10.1073/pnas.222681699. Accessed 8 August 2007.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 330-335
    • Bitan, G.1    Kirkitadze, M.D.2    Lomakin, A.3    Vollers, S.S.4    Benedek, G.B.5
  • 14
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289: 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5
  • 15
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease
    • Roher AE, Chaney MO, Kuo YM, Webster SD, Stine WB, et al. (1996) Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. J Biol Chem 271: 20631-20635.
    • (1996) J Biol Chem , vol.271 , pp. 20631-20635
    • Roher, A.E.1    Chaney, M.O.2    Kuo, Y.M.3    Webster, S.D.4    Stine, W.B.5
  • 16
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • Lue LF, Kuo YM, Roher AE, Brachova L, Shen Y, et al. (1999) Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am J Pathol 155: 853-862.
    • (1999) Am J Pathol , vol.155 , pp. 853-862
    • Lue, L.F.1    Kuo, Y.M.2    Roher, A.E.3    Brachova, L.4    Shen, Y.5
  • 17
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • doi:10.1038/416535a. Available:, Accessed 8 August 2007
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, et al. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535-539. doi:10.1038/416535a. Available: http://dx.doi.org/10.1038/416535a. Accessed 8 August 2007.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5
  • 19
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric a beta ligands (addls) suggests a molecular basis for reversible memory loss
    • doi:10.1073/pnas.1834302100. Available:, Accessed 8 August 2007
    • Gong Y, Chang L, Viola KL, Lacor PN, Lambert MP, et al. (2003) Alzheimer's disease-affected brain: Presence of oligomeric a beta ligands (addls) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci U S A 100: 10417-10422. doi:10.1073/pnas.1834302100. Available: http://dx.doi.org/10.1073/pnas.1834302100. Accessed 8 August 2007.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5
  • 20
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • doi:10.1038/nn1372. Available:, Accessed 8 August 2007
    • Cleary JP, Walsh DM, Hofmeister JJ, Shankar GM, Kuskowski MA, et al. (2005) Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci 8: 79-84. doi:10.1038/nn1372. Available: http://dx.doi.org/10.1038/nn1372. Accessed 8 August 2007.
    • (2005) Nat Neurosci , vol.8 , pp. 79-84
    • Cleary, J.P.1    Walsh, D.M.2    Hofmeister, J.J.3    Shankar, G.M.4    Kuskowski, M.A.5
  • 21
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • doi:10.1038/nrm2101. Available:, Accessed 8 August 2007
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8: 101-112. doi:10.1038/nrm2101. Available: http://dx.doi.org/10.1038/nrm2101. Accessed 8 August 2007.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 22
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • doi:10.1038/416507a. Available:, Accessed 8 August 2007
    • Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, et al. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416: 507-511. doi:10.1038/416507a. Available: http://dx.doi.org/10.1038/416507a. Accessed 8 August 2007.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5
  • 23
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • doi:10.1126/science.1079469. Available:, Accessed 8 August 2007
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489. doi:10.1126/science.1079469. Available: http://dx.doi.org/10.1126/science.1079469. Accessed 8 August 2007.
    • (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
  • 24
    • 3843148352 scopus 로고    scopus 로고
    • Prefibrillar amyloid protein aggregates share common features of cytotoxicity
    • doi:10.1074/jbc.M400348200. Available:, Accessed 8 August 2007
    • Bucciantini M, Calloni G, Chiti F, Formigli L, Nosi D, et al. (2004) Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem 279: 31374-31382. doi:10.1074/jbc.M400348200. Available: http://dx.doi.org/10.1074/jbc.M400348200. Accessed 8 August 2007.
    • (2004) J Biol Chem , vol.279 , pp. 31374-31382
    • Bucciantini, M.1    Calloni, G.2    Chiti, F.3    Formigli, L.4    Nosi, D.5
  • 25
    • 24644448839 scopus 로고    scopus 로고
    • Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, et al. (2005) &fjThe most infectious prion protein particles. Nature 437: 257-261. doi:10.1038/nature03989. Available: http://dx.doi.org/10.1038/nature03989. Accessed 8 August 2007.
    • Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, et al. (2005) &fjThe most infectious prion protein particles. Nature 437: 257-261. doi:10.1038/nature03989. Available: http://dx.doi.org/10.1038/nature03989. Accessed 8 August 2007.
  • 26
    • 33748210163 scopus 로고    scopus 로고
    • Prefibrillar amyloid aggregates could be generic toxins in higher organisms
    • doi:10.1523/JNEUROSCI.4809-05.2006. Available:, Accessed 8 August 2007
    • Baglioni S, Casamenti F, Bucciantini M, Luheshi LM, Taddei N, et al. (2006) Prefibrillar amyloid aggregates could be generic toxins in higher organisms. J Neurosci 26: 8160-8167. doi:10.1523/JNEUROSCI.4809-05.2006. Available: http://dx.doi.org/10.1523/JNEUROSCI.4809-05.2006. Accessed 8 August 2007.
    • (2006) J Neurosci , vol.26 , pp. 8160-8167
    • Baglioni, S.1    Casamenti, F.2    Bucciantini, M.3    Luheshi, L.M.4    Taddei, N.5
  • 27
    • 0034601806 scopus 로고    scopus 로고
    • Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin a(1-8)-magainin 2(1-12), and its analogues, on their antibiotic activities and structures
    • Oh D, Shin SY, Lee S, Kang JH, Kim SD, et al. (2000) Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin a(1-8)-magainin 2(1-12), and its analogues, on their antibiotic activities and structures. Biochemistry 39: 11855-11864.
    • (2000) Biochemistry , vol.39 , pp. 11855-11864
    • Oh, D.1    Shin, S.Y.2    Lee, S.3    Kang, J.H.4    Kim, S.D.5
  • 28
    • 14844361744 scopus 로고    scopus 로고
    • Comparative analysis of the cytotoxicity of homopolymeric amino acids
    • doi:10.1016/j.bbapap.2004.12.017. Available:, Accessed 8 August 2007
    • Oma Y, Kino Y, Sasagawa N, Ishiura S (2005) Comparative analysis of the cytotoxicity of homopolymeric amino acids. Biochim Biophys Acta 1748: 174-179. doi:10.1016/j.bbapap.2004.12.017. Available: http://dx.doi.org/10.1016/j.bbapap. 2004.12.017. Accessed 8 August 2007.
    • (2005) Biochim Biophys Acta , vol.1748 , pp. 174-179
    • Oma, Y.1    Kino, Y.2    Sasagawa, N.3    Ishiura, S.4
  • 29
    • 33646576163 scopus 로고    scopus 로고
    • Inhibition of plant-pathogenic bacteria by short synthetic cecropin a-melittin hybrid peptides
    • doi:10.1128/AEM.72.5. 3302-3308.2006, Accessed 13 August 2007
    • Ferre R, Badosa E, Feliu L, Planas M, Montesinos E, et al. (2006) Inhibition of plant-pathogenic bacteria by short synthetic cecropin a-melittin hybrid peptides. Appl Environ Microbiol 72: 3302-3308. doi:10.1128/AEM.72.5. 3302-3308.2006. http://dx.doi.org/10.1128/AEM.72.5.3302-3308.2006. Accessed 13 August 2007.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 3302-3308
    • Ferre, R.1    Badosa, E.2    Feliu, L.3    Planas, M.4    Montesinos, E.5
  • 30
    • 23444447864 scopus 로고    scopus 로고
    • Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
    • doi:10.1016/j.jmb.2005.06.043. Available:, Accessed 8 August 2007
    • Plakoutsi G, Bemporad F, Calamai M, Taddei N, Dobson CM, et al. (2005) Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. J Mol Biol 351: 910-922. doi:10.1016/j.jmb.2005.06.043. Available: http://dx.doi.org/10.1016/j.jmb.2005. 06.043. Accessed 8 August 2007.
    • (2005) J Mol Biol , vol.351 , pp. 910-922
    • Plakoutsi, G.1    Bemporad, F.2    Calamai, M.3    Taddei, N.4    Dobson, C.M.5
  • 31
    • 25844493690 scopus 로고    scopus 로고
    • Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide
    • doi:10.1021/ja054663y. Available:, Accessed 8 August 2007
    • Petty SA, Decatur SM (2005) Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide. J Am Chem Soc 127: 13488-13489. doi:10.1021/ja054663y. Available: http://dx.doi.org/10.1021/ ja054663y. Accessed 8 August 2007.
    • (2005) J Am Chem Soc , vol.127 , pp. 13488-13489
    • Petty, S.A.1    Decatur, S.M.2
  • 32
    • 33846565857 scopus 로고    scopus 로고
    • Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates
    • doi:10.1016/j.jmb.2006.12.007, Accessed 8 August 2007
    • Cerdà-Costa N, Esteras-Chopo A, Avilés FX, Serrano L, Villegas V (2007) Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates. J Mol Biol 366: 1351-1363. doi:10.1016/j.jmb.2006.12.007. http://dx.doi.org/10.1016/j.jmb.2006.12.007. Accessed 8 August 2007.
    • (2007) J Mol Biol , vol.366 , pp. 1351-1363
    • Cerdà-Costa, N.1    Esteras-Chopo, A.2    Avilés, F.X.3    Serrano, L.4    Villegas, V.5
  • 33
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the aggregation kinetics of amyloid peptides
    • doi:10.1016/j.jmb.2006.05.033. Available:, Accessed 8 August 2007
    • Pellarin R, Caflisch A (2006) Interpreting the aggregation kinetics of amyloid peptides. J Mol Biol 360: 882-892. doi:10.1016/j.jmb.2006.05.033. Available: http://dx.doi.org/10.1016/j.jmb.2006.05.033. Accessed 8 August 2007.
    • (2006) J Mol Biol , vol.360 , pp. 882-892
    • Pellarin, R.1    Caflisch, A.2
  • 34
    • 0037337271 scopus 로고    scopus 로고
    • Dissecting the assembly of Abeta16-22 amyloid peptides into antiparallel beta sheets
    • Klimov DK, Thirumalai D (2003) Dissecting the assembly of Abeta16-22 amyloid peptides into antiparallel beta sheets. Structure 11: 295-307.
    • (2003) Structure , vol.11 , pp. 295-307
    • Klimov, D.K.1    Thirumalai, D.2
  • 35
    • 33846036362 scopus 로고    scopus 로고
    • Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism
    • doi:10.1073/pnas.0607440104. Available:, Accessed 8 August 2007
    • Nguyen PH, Li MS, Stock G, Straub JE, Thirumalai D (2007) Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism. Proc Natl Acad Sci U S A 104: 111-116. doi:10.1073/pnas.0607440104. Available: http://dx.doi.org/10.1073/pnas.0607440104. Accessed 8 August 2007.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 111-116
    • Nguyen, P.H.1    Li, M.S.2    Stock, G.3    Straub, J.E.4    Thirumalai, D.5
  • 36
    • 0034733023 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
    • Esler WP, Stimson ER, Jennings JM, Vinters HV, Ghilardi JR, et al. (2000) Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry 39: 6288-6295.
    • (2000) Biochemistry , vol.39 , pp. 6288-6295
    • Esler, W.P.1    Stimson, E.R.2    Jennings, J.M.3    Vinters, H.V.4    Ghilardi, J.R.5
  • 37
    • 0037397705 scopus 로고    scopus 로고
    • Emerging ideas on the molecular basis of protein and peptide aggregation
    • Thirumalai D, Klimov DK, Dima RI (2003) Emerging ideas on the molecular basis of protein and peptide aggregation. Curr Opin Struct Biol 13: 146-159.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 146-159
    • Thirumalai, D.1    Klimov, D.K.2    Dima, R.I.3
  • 38
    • 9244260521 scopus 로고    scopus 로고
    • Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides
    • doi:10.1073/pnas.0407273101. Available:, Accessed 8 August 2007
    • Nguyen HD, Hall CK (2004) Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proc Natl Acad Sci U S A 101: 16180-16185. doi:10.1073/pnas.0407273101. Available: http://dx.doi.org/10.1073/ pnas.0407273101. Accessed 8 August 2007.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16180-16185
    • Nguyen, H.D.1    Hall, C.K.2
  • 39
    • 4444346811 scopus 로고    scopus 로고
    • Kinetic control of dimer structure formation in amyloid fibrillogenesis
    • doi:10.1073/pnas.0402634101. Available:, Accessed 8 August 2007
    • Hwang W, Zhang S, Kamm RD, Karplus M (2004) Kinetic control of dimer structure formation in amyloid fibrillogenesis. Proc Natl Acad Sci U S A 101: 12916-12921. doi:10.1073/pnas.0402634101. Available: http://dx.doi.org/10.1073/ pnas.0402634101. Accessed 8 August 2007.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 12916-12921
    • Hwang, W.1    Zhang, S.2    Kamm, R.D.3    Karplus, M.4
  • 40
    • 26844435756 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Alzheimer's beta-amyloid protofilaments
    • doi:10.1016/j.jmb.2005.08.066. Available:, Accessed 8 August 2007
    • Buchete NV, Tycko R, Hummer G (2005) Molecular dynamics simulations of Alzheimer's beta-amyloid protofilaments. J Mol Biol 353: 804-821. doi:10.1016/j.jmb.2005.08.066. Available: http://dx.doi.org/10.1016/j.jmb.2005. 08.066. Accessed 8 August 2007.
    • (2005) J Mol Biol , vol.353 , pp. 804-821
    • Buchete, N.V.1    Tycko, R.2    Hummer, G.3
  • 41
    • 19544375553 scopus 로고    scopus 로고
    • Sequence dependence of amyloid fibril formation: Insights from molecular dynamics simulations
    • doi:10.1016/j.jmb.2005.03.081, Accessed 13 August 2007
    • de la Paz ML, de Mori GMS, Serrano L, Colombo G (2005) Sequence dependence of amyloid fibril formation: Insights from molecular dynamics simulations. J Mol Biol 349: 583-596. doi:10.1016/j.jmb.2005.03.081. http://dx.doi.org/10.1016/j.jmb.2005.03.081. Accessed 13 August 2007.
    • (2005) J Mol Biol , vol.349 , pp. 583-596
    • de la Paz, M.L.1    de Mori, G.M.S.2    Serrano, L.3    Colombo, G.4
  • 42
    • 85135545523 scopus 로고    scopus 로고
    • Khare SD, Ding F, Gwanmesia KN, Dokholyan NV (2005) Molecular origin of polyglutamine aggregation in neurodegenerative diseases. PLoS Comput Biol 1: 230-235. doi:10.1371/journal.pcbi.0010030. http://dx.doi.org/10.1371/journal. pcbi.0010030. Accessed 13 August 2007.
    • Khare SD, Ding F, Gwanmesia KN, Dokholyan NV (2005) Molecular origin of polyglutamine aggregation in neurodegenerative diseases. PLoS Comput Biol 1: 230-235. doi:10.1371/journal.pcbi.0010030. http://dx.doi.org/10.1371/journal. pcbi.0010030. Accessed 13 August 2007.
  • 43
    • 33646466620 scopus 로고    scopus 로고
    • Common attributes of native-state structures of proteins, disordered proteins, and amyloid
    • doi:10.1073/pnas.0601824103. Available:, Accessed 8 August 2007
    • Hoang TX, Marsella L, Trovato A, Seno F, Banavar JR, et al. (2006) Common attributes of native-state structures of proteins, disordered proteins, and amyloid. Proc Natl Acad Sci U S A 103: 6883-6888. doi:10.1073/pnas.0601824103. Available: http://dx.doi.org/10.1073/pnas.0601824103. Accessed 8 August 2007.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6883-6888
    • Hoang, T.X.1    Marsella, L.2    Trovato, A.3    Seno, F.4    Banavar, J.R.5
  • 44
    • 33748689799 scopus 로고    scopus 로고
    • Simulations as analytical tools to understand protein aggregation and predict amyloid conformation
    • doi:10.1016/j.cbpa.2006.08.018. Available:, Accessed 8 August 2007
    • Ma B, Nussinov R (2006) Simulations as analytical tools to understand protein aggregation and predict amyloid conformation. Curr Opin Chem Biol 10: 445-452. doi:10.1016/j.cbpa.2006.08.018. Available: http://dx.doi.org/10.1016/j. cbpa.2006.08.018. Accessed 8 August 2007.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 445-452
    • Ma, B.1    Nussinov, R.2
  • 45
    • 33749832945 scopus 로고    scopus 로고
    • Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach
    • doi:10.1021/ar050063s. Available:, Accessed 8 August 2007
    • Teplow DB, Lazo ND, Bitan G, Bernstein S, Wyttenbach T, et al. (2006) Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach. Acc Chem Res 39: 635-645. doi:10.1021/ar050063s. Available: http://dx.doi.org/10.1021/ar050063s. Accessed 8 August 2007.
    • (2006) Acc Chem Res , vol.39 , pp. 635-645
    • Teplow, D.B.1    Lazo, N.D.2    Bitan, G.3    Bernstein, S.4    Wyttenbach, T.5
  • 46
    • 33751104733 scopus 로고    scopus 로고
    • Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure
    • doi:10.1002/prot.21134, Accessed 13 August 2007
    • Boucher G, Mousseau N, Derreumaux P (2006) Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure. Proteins 65: 877-888. doi:10.1002/prot.21134. http://dx.doi.org/10.1002/prot.21134. Accessed 13 August 2007.
    • (2006) Proteins , vol.65 , pp. 877-888
    • Boucher, G.1    Mousseau, N.2    Derreumaux, P.3
  • 47
    • 4544283591 scopus 로고    scopus 로고
    • In silico assembly of Alzheimer's Abeta16-22 peptide into beta-sheets
    • doi:10.1021/ja047286i. Available:, Accessed 8 August 2007
    • Santini S, Mousseau N, Derreumaux P (2004) In silico assembly of Alzheimer's Abeta16-22 peptide into beta-sheets. J Am Chem Soc 126: 11509-11516. doi:10.1021/ja047286i. Available: http://dx.doi.org/10.1021/ja047286i. Accessed 8 August 2007.
    • (2004) J Am Chem Soc , vol.126 , pp. 11509-11516
    • Santini, S.1    Mousseau, N.2    Derreumaux, P.3
  • 48
    • 10644242867 scopus 로고    scopus 로고
    • Molecular dynamics simulation of amyloid beta dimer formation
    • doi:10.1529/biophysj.104.040980. Available:, Accessed 8 August 2007
    • Urbanc B, Cruz L, Ding F, Sammond D, Khare S, et al. (2004) Molecular dynamics simulation of amyloid beta dimer formation. Biophys J 87: 2310-2321. doi:10.1529/biophysj.104.040980. Available: http://dx.doi.org/10.1529/biophysj. 104.040980. Accessed 8 August 2007.
    • (2004) Biophys J , vol.87 , pp. 2310-2321
    • Urbanc, B.1    Cruz, L.2    Ding, F.3    Sammond, D.4    Khare, S.5
  • 49
    • 0041629626 scopus 로고    scopus 로고
    • Thermodynamics of alpha- and beta-structure formation in proteins
    • Irbäck A, Samuelsson B, Sjunnesson F, Wallin S (2003) Thermodynamics of alpha- and beta-structure formation in proteins. Biophys J 85: 1466-1473.
    • (2003) Biophys J , vol.85 , pp. 1466-1473
    • Irbäck, A.1    Samuelsson, B.2    Sjunnesson, F.3    Wallin, S.4
  • 50
    • 10044227276 scopus 로고    scopus 로고
    • Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces
    • doi:10.1529/biophysj.104.046839. Available:, Accessed 8 August 2007
    • Favrin G, Irbäck A, Mohanty S (2004) Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces. Biophys J 87: 3657-3664. doi:10.1529/biophysj.104.046839. Available: http://dx.doi.org/10. 1529/biophysj.104.046839. Accessed 8 August 2007.
    • (2004) Biophys J , vol.87 , pp. 3657-3664
    • Favrin, G.1    Irbäck, A.2    Mohanty, S.3
  • 51
    • 2642586516 scopus 로고    scopus 로고
    • Folding thermodynamics of three beta-sheet peptides: A model study
    • doi:10.1002/prot. 20157. Available:, Accessed 8 August 2007
    • Irbäck A, Sjunnesson F (2004) Folding thermodynamics of three beta-sheet peptides: A model study. Proteins 56: 110-116. doi:10.1002/prot. 20157. Available: http://dx.doi.org/10.1002/prot.20157. Accessed 8 August 2007.
    • (2004) Proteins , vol.56 , pp. 110-116
    • Irbäck, A.1    Sjunnesson, F.2
  • 52
    • 21244495332 scopus 로고    scopus 로고
    • Folding thermodynamics of peptides
    • doi:10.1529/biophysj.104.050427, Accessed 13 August 2007
    • Irbäck A, Mohanty S (2005) Folding thermodynamics of peptides. Biophys J 88: 1560-1569. doi:10.1529/biophysj.104.050427. http://dx.doi.org/10. 1529/biophysj.104.050427. Accessed 13 August 2007.
    • (2005) Biophys J , vol.88 , pp. 1560-1569
    • Irbäck, A.1    Mohanty, S.2
  • 53
    • 33748604047 scopus 로고    scopus 로고
    • Profasi: A monte carlo simulation package for protein folding and aggregation
    • doi:10.1002/jcc.20452. Available:, Accessed 8 August 2007
    • Irbäck A, Mohanty S (2006) Profasi: A monte carlo simulation package for protein folding and aggregation. J Comput Chem 27: 1548-1555. doi:10.1002/jcc.20452. Available: http://dx.doi.org/10.1002/jcc.20452. Accessed 8 August 2007.
    • (2006) J Comput Chem , vol.27 , pp. 1548-1555
    • Irbäck, A.1    Mohanty, S.2
  • 54
    • 33947182575 scopus 로고    scopus 로고
    • The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Abeta peptides
    • doi:10.1016/j.febslet.2007.02.026
    • Liao MQ, Tzeng YJ, Chang LYX, Huang HB, Lin TH, et al. (2007) The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Abeta peptides. FEBS Lett 581: 1161-1165. doi:10.1016/j.febslet.2007.02.026.
    • (2007) FEBS Lett , vol.581 , pp. 1161-1165
    • Liao, M.Q.1    Tzeng, Y.J.2    Chang, L.Y.X.3    Huang, H.B.4    Lin, T.H.5
  • 55
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • doi:10.1017/S0033583506004422. Available:, Accessed 8 August 2007
    • Lashuel HA, Lansbury PT (2006) Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q Rev Biophys 39: 167-201. doi:10.1017/S0033583506004422. Available: http://dx.doi.org/10.1017/ S0033583506004422. Accessed 8 August 2007.
    • (2006) Q Rev Biophys , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, P.T.2
  • 56
    • 85135546170 scopus 로고    scopus 로고
    • Milojevic J, Esposito V, Das R, Melacini G (2007) Understanding the molecular basis for the inhibition of the Alzheimer's Abeta-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation nmr spectroscopy. J Am Chem Soc 10.1021/ja067367+. http://dx.doi.org/10.1021/ja067367+.
    • Milojevic J, Esposito V, Das R, Melacini G (2007) Understanding the molecular basis for the inhibition of the Alzheimer's Abeta-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation nmr spectroscopy. J Am Chem Soc 10.1021/ja067367+. http://dx.doi.org/10.1021/ja067367+.
  • 57
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation
    • Carrotta R, Bauer R, Waninge R, Rischel C (2001) Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation. Protein Sci 10: 1312-1318.
    • (2001) Protein Sci , vol.10 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 58
    • 0036559935 scopus 로고    scopus 로고
    • Oligomerization process of the hemolytic lectin cel-iii purified from a sea cucumber, cucumaria echinata
    • Kuwahara H, Yamasaki T, Hatakeyama T, Aoyagi H, Fujisawa T (2002) Oligomerization process of the hemolytic lectin cel-iii purified from a sea cucumber, cucumaria echinata. J Biochem (Tokyo) 131: 751-756.
    • (2002) J Biochem (Tokyo) , vol.131 , pp. 751-756
    • Kuwahara, H.1    Yamasaki, T.2    Hatakeyama, T.3    Aoyagi, H.4    Fujisawa, T.5
  • 59
    • 28444454101 scopus 로고    scopus 로고
    • Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    • doi:10.1529/biophysj.105.068726. Available:, Accessed 8 August 2007
    • Calamai M, Chiti F, Dobson CM (2005) Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Biophys J 89: 4201-4210. doi:10.1529/biophysj.105.068726. Available: http://dx.doi.org/10. 1529/biophysj.105.068726. Accessed 8 August 2007.
    • (2005) Biophys J , vol.89 , pp. 4201-4210
    • Calamai, M.1    Chiti, F.2    Dobson, C.M.3
  • 60
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by a beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state nmr
    • Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, et al. (2000) Amyloid fibril formation by a beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state nmr. Biochemistry 39: 13748-13759.
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzutkin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5
  • 61
    • 0035826575 scopus 로고    scopus 로고
    • Monte carlo update for chain molecules: Biased gaussian steps in torsional space
    • Favrin G, Irbäck A, Sjunnesson F (2001) Monte carlo update for chain molecules: Biased gaussian steps in torsional space. J Chem Phys 114: 8154-8158.
    • (2001) J Chem Phys , vol.114 , pp. 8154-8158
    • Favrin, G.1    Irbäck, A.2    Sjunnesson, F.3
  • 62
    • 0035917318 scopus 로고    scopus 로고
    • The folding thermodynamics and kinetics of crambin using an all-atom monte carlo simulation
    • doi:10.1006/jmbi.2001.4586. Available:, Accessed 8 August 2007
    • Shimada J, Kussell EL, Shakhnovich EI (2001) The folding thermodynamics and kinetics of crambin using an all-atom monte carlo simulation. J Mol Biol 308: 79-95. doi:10.1006/jmbi.2001.4586. Available: http://dx.doi.org/10.1006/ jmbi.2001.4586. Accessed 8 August 2007.
    • (2001) J Mol Biol , vol.308 , pp. 79-95
    • Shimada, J.1    Kussell, E.L.2    Shakhnovich, E.I.3
  • 63
    • 0347802347 scopus 로고
    • Numerical evidence for bcc ordering at the surface of a critical fcc nucleus
    • ten Wolde PR, Ruiz-Montero, Frenkel D (1995) Numerical evidence for bcc ordering at the surface of a critical fcc nucleus. Phys Rev Lett 75: 2714-2717.
    • (1995) Phys Rev Lett , vol.75 , pp. 2714-2717
    • ten Wolde, P.R.1
  • 64
    • 1842516321 scopus 로고    scopus 로고
    • Quantitative prediction of crystal-nucleation rates for spherical colloids: A computational approach
    • doi:10.1146/annurev.physchem.55.091602.094402. Available:, Accessed 8 August 2007
    • Auer S, Frenkel D (2004) Quantitative prediction of crystal-nucleation rates for spherical colloids: A computational approach. Annu Rev Phys Chem 55: 333-361. doi:10.1146/annurev.physchem.55.091602.094402. Available: http://dx.doi.org/10.1146/annurev.physchem.55.091602.094402. Accessed 8 August 2007.
    • (2004) Annu Rev Phys Chem , vol.55 , pp. 333-361
    • Auer, S.1    Frenkel, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.