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Volumn 7, Issue 7, 2011, Pages 2296-2303

Monte Carlo simulations of protein amyloid formation reveal origin of sigmoidal aggregation kinetics

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; PEPTIDE;

EID: 79959243317     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/c0mb00321b     Document Type: Article
Times cited : (30)

References (43)
  • 2
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • DOI 10.1146/annurev.biochem.72.121801.161837
    • P. Chien J. S. Weissman A. H. DePac Emerging principles of conformation-based prion inheritance Annu. Rev. Biochem. 2004 73 617 656 (Pubitemid 39050382)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti C. M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 2006 75 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 11
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • S. R. Collins A. Douglass R. D. Vale J. S. Weissman Mechanism of prion propagation: amyloid growth occurs by monomer addition PLoS Biol. 2004 2 e321
    • (2004) PLoS Biol. , vol.2 , pp. 321
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 12
    • 39049110070 scopus 로고    scopus 로고
    • Apolipoprotein C-II amyloid fibrils assemble via a reversible pathway that includes fibril breaking and rejoining
    • K. J. Binger C. L. Pham L. M. Wilson M. F. Bailey L. J. Lawrence P. Schuck G. J. Howlett Apolipoprotein C-II amyloid fibrils assemble via a reversible pathway that includes fibril breaking and rejoining J. Mol. Biol. 2008 376 1116 1129
    • (2008) J. Mol. Biol. , vol.376 , pp. 1116-1129
    • Binger, K.J.1    Pham, C.L.2    Wilson, L.M.3    Bailey, M.F.4    Lawrence, L.J.5    Schuck, P.6    Howlett, G.J.7
  • 13
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • W.-F. Xue S. W. Homans S. E. Radford Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly Proc. Natl. Acad. Sci. U. S. A. 2008 105 8926 8931
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 8926-8931
    • Xue, W.-F.1    Homans, S.W.2    Radford, S.E.3
  • 14
    • 77951676986 scopus 로고    scopus 로고
    • Aβ aggregation produces highly reproducible kinetic data and occurs by a two-phase process
    • E. Hellstrand B. Boland D. M. Walsh S. Linse Aβ aggregation produces highly reproducible kinetic data and occurs by a two-phase process ACS Chem. Neurosci. 2010 1 13 18
    • (2010) ACS Chem. Neurosci. , vol.1 , pp. 13-18
    • Hellstrand, E.1    Boland, B.2    Walsh, D.M.3    Linse, S.4
  • 15
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the aggregation kinetics of amyloid peptides
    • P. Pellarin A. Caflisch Interpreting the aggregation kinetics of amyloid peptides J. Mol. Biol. 2006 360 882 892
    • (2006) J. Mol. Biol. , vol.360 , pp. 882-892
    • Pellarin, P.1    Caflisch, A.2
  • 17
    • 33947728761 scopus 로고    scopus 로고
    • Cooperative hydrogen bonding in amyloid formation
    • DOI 10.1110/ps.062609607
    • K. Tsemekhman L. Goldschmidt D. Eisenberg D. Baker Cooperative hydrogen bonding in amyloid formation Protein Sci. 2007 16 761 764 (Pubitemid 46507005)
    • (2007) Protein Science , vol.16 , Issue.4 , pp. 761-764
    • Tsemekhman, K.1    Goldschmidt, L.2    Eisenberg, D.3    Baker, D.4
  • 19
    • 0037627715 scopus 로고    scopus 로고
    • The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35
    • DOI 10.1073/pnas.0835307100
    • J. Gsponer U. Haberthür A. Caflisch The role of side-chain interactions in the early steps of aggregation: molecular dynamics simulations of an amyloid-forming peptide from yeast prion Sup35 Proc. Natl. Acad. Sci. U. S. A. 2003 100 5154 5159 (Pubitemid 36542674)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.9 , pp. 5154-5159
    • Gsponer, J.1    Haberthur, U.2    Caflisch, A.3
  • 20
    • 10844230140 scopus 로고    scopus 로고
    • Replica exchange molecular dynamics simulations of amyloid peptide aggregation
    • DOI 10.1063/1.1809588
    • M. Cecchini F. Rao M. Seeber A. Caflisch Replica exchange molecular dynamics simulations of amyloid peptide aggregation J. Chem. Phys. 2004 121 10748 10756 (Pubitemid 40001622)
    • (2004) Journal of Chemical Physics , vol.121 , Issue.21 , pp. 10748-10756
    • Cecchini, M.1    Rao, F.2    Seeber, M.3    Caflisch, A.4
  • 21
    • 33746765060 scopus 로고    scopus 로고
    • Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35
    • DOI 10.1529/biophysj.106.083246
    • J. Zheng J. B. Ma C. J. Tsai Nussinov RStructural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35 Biophys. J. 2006 91 824 833 (Pubitemid 44161914)
    • (2006) Biophysical Journal , vol.91 , Issue.3 , pp. 824-833
    • Zheng, J.1    Ma, B.J.2    Tsai, C.-J.3    Nussinov, R.4
  • 23
    • 34548627237 scopus 로고    scopus 로고
    • Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35
    • DOI 10.1529/biophysj.106.100537
    • Z. Zhang H. Chen H. Bai L. Lai Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeat prion protein Sup35 Biophys. J. 2007 93 1484 1492 (Pubitemid 47403294)
    • (2007) Biophysical Journal , vol.93 , Issue.5 , pp. 1484-1492
    • Zhang, Z.1    Chen, H.2    Bai, H.3    Lai, L.4
  • 24
    • 33846088432 scopus 로고    scopus 로고
    • Aggregation of β-amyloid fragments
    • J. H. Meinke U. H. E. Hansmann Aggregation of β-amyloid fragments J. Chem. Phys. 2007 126 014706
    • (2007) J. Chem. Phys. , vol.126 , pp. 014706
    • Meinke, J.H.1    Hansmann, U.H.E.2
  • 25
    • 58149174069 scopus 로고    scopus 로고
    • Formation and Growth of Oligomers: A Monte Carlo Study of an Amyloid Tau Fragment
    • D. W. Li S. A. Mohanty A. Irbäck S. Huo Formation and Growth of Oligomers: A Monte Carlo Study of an Amyloid Tau Fragment PLoS Comput. Biol. 2008 4 e1000238
    • (2008) PLoS Comput. Biol. , vol.4 , pp. 1000238
    • Li, D.W.1    Mohanty, S.A.2    Irbäck, A.3    Huo, S.4
  • 26
    • 77949612059 scopus 로고    scopus 로고
    • GNNQQNY - Investigation of Early Steps during Amyloid Formation
    • A. S. Reddy M. Chopra J. J. de Pablo GNNQQNY - Investigation of Early Steps during Amyloid Formation Biophys. J. 2010 98 1038 1045
    • (2010) Biophys. J. , vol.98 , pp. 1038-1045
    • Reddy, A.S.1    Chopra, M.2    De Pablo, J.J.3
  • 28
    • 77955790562 scopus 로고    scopus 로고
    • Comparing the folding free-energy landscapes of Aβ42 variants with different aggregation properties
    • S. Mitternacht I. Staneva T. Härd A. Irbäck Comparing the folding free-energy landscapes of Aβ42 variants with different aggregation properties Proteins 2010 78 2600 2608
    • (2010) Proteins , vol.78 , pp. 2600-2608
    • Mitternacht, S.1    Staneva, I.2    Härd, T.3    Irbäck, A.4
  • 29
    • 77951290266 scopus 로고    scopus 로고
    • Phase diagram of α-helical and β-sheet forming peptides
    • S. Auer D. Kashchiev Phase diagram of α-helical and β-sheet forming peptides Phys. Rev. Lett. 2010 104 168105
    • (2010) Phys. Rev. Lett. , vol.104 , pp. 168105
    • Auer, S.1    Kashchiev, D.2
  • 30
    • 42149116459 scopus 로고    scopus 로고
    • Time-averaged predictions of folded and misfolded peptides using a reduced physicochemical model
    • DOI 10.1002/jcc.20879
    • O. J. Clarke M. J. Parker Time-Averaged Predictions of Folded and Misfolded Peptides Using a Reduced Physicochemical Model J. Comput. Chem. 2008 29 1177 1185 (Pubitemid 351535415)
    • (2008) Journal of Computational Chemistry , vol.29 , Issue.7 , pp. 1177-1185
    • Clarke, O.J.1    Parker, M.J.2
  • 31
    • 70449083068 scopus 로고    scopus 로고
    • Self-assembly of polypeptides into left-handedly twisted fibril-like structures
    • Y. Mu Y. Q. Gao Self-assembly of polypeptides into left-handedly twisted fibril-like structures Phys. Rev. E. 2009 80 041927
    • (2009) Phys. Rev. E. , vol.80 , pp. 041927
    • Mu, Y.1    Gao, Y.Q.2
  • 32
    • 58749109622 scopus 로고    scopus 로고
    • Simulations of nucleation and elongation of amyloid fibrils
    • J. Zhang M. Muthukumar Simulations of nucleation and elongation of amyloid fibrils J. Chem. Phys. 2009 130 035102
    • (2009) J. Chem. Phys. , vol.130 , pp. 035102
    • Zhang, J.1    Muthukumar, M.2
  • 34
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions
    • H. Taketomi Y. Ueda N. G Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions Int. J. Pept. Protein Res. 1975 7 445 459
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    G, N.3
  • 36
    • 60349100306 scopus 로고    scopus 로고
    • Facile method for expression and purification of the Alzheimer disease-associated amyloid β-peptide
    • D. M. Walsh E. Thulin A. Minuogue T. Gustafsson E. Pang D. B. Teplow S. A. Linse Facile method for expression and purification of the Alzheimer disease-associated amyloid β-peptide FEBS J. 2009 276 1266 1281
    • (2009) FEBS J. , vol.276 , pp. 1266-1281
    • Walsh, D.M.1    Thulin, E.2    Minuogue, A.3    Gustafsson, T.4    Pang, E.5    Teplow, D.B.6    Linse, S.A.7
  • 37
    • 34447511416 scopus 로고    scopus 로고
    • Protein folding through kinetic discrimination
    • DOI 10.1021/ja070386e
    • S. Linse B. Linse Protein folding through kinetic discrimination J. Am. Chem. Soc. 2007 129 8481 8486 (Pubitemid 47066510)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.27 , pp. 8481-8486
    • Linse, S.1    Linse, B.2
  • 38
    • 44549084117 scopus 로고    scopus 로고
    • On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2
    • R. Sabaté I. Lascu S. J. Saupe On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2 J. Struct. Biol. 2008 162 387 396
    • (2008) J. Struct. Biol. , vol.162 , pp. 387-396
    • Sabaté, R.1    Lascu, I.2    Saupe, S.J.3
  • 42
    • 77952758210 scopus 로고    scopus 로고
    • Retardation of Abeta fibril formation by phospholipid vesicles depends on membrane phase behavior
    • E. Hellstrand E. Sparr S. Linse Retardation of Abeta fibril formation by phospholipid vesicles depends on membrane phase behavior Biophys. J. 2010 98 2206 2214
    • (2010) Biophys. J. , vol.98 , pp. 2206-2214
    • Hellstrand, E.1    Sparr, E.2    Linse, S.3
  • 43
    • 35148899284 scopus 로고    scopus 로고
    • Effect of Different Salt Ions on the Propensity of Aggregation and on the Structure of Alzheimer's Aβ(1-40) Amyloid Fibrils
    • DOI 10.1016/j.jmb.2007.08.068, PII S002228360701162X
    • K. Klement K. Wieligmann J. Meinhardt P. Hortschansky W. Richter M. Fändrich Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's abeta(1-40) amyloid fibrils J. Mol. Biol. 2007 373 1321 1333 (Pubitemid 47539491)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.5 , pp. 1321-1333
    • Klement, K.1    Wieligmann, K.2    Meinhardt, J.3    Hortschansky, P.4    Richter, W.5    Fandrich, M.6


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