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Volumn 80, Issue 6, 2012, Pages 1582-1597

Structural transitions and oligomerization along polyalanine fibril formation pathways from computer simulations

Author keywords

Amyloid; Computer simulations; Fibril formation pathway; Protein aggregation

Indexed keywords

ALANINE; MONOMER; POLYPEPTIDE;

EID: 84860627561     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24052     Document Type: Article
Times cited : (12)

References (75)
  • 2
    • 22844451606 scopus 로고    scopus 로고
    • Amyloid formation modulates the biological activity of a bacterial protein
    • Bieler S, Estrada L, Lagos R, Baeza M, Castilla J, Soto C. Amyloid formation modulates the biological activity of a bacterial protein. J Biol Chem 2005; 280: 26880-26885.
    • (2005) J Biol Chem , vol.280 , pp. 26880-26885
    • Bieler, S.1    Estrada, L.2    Lagos, R.3    Baeza, M.4    Castilla, J.5    Soto, C.6
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006; 75: 333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 5
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 2007; 8: 101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 6
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali R, Wetzel R. Polymorphism in the intermediates and products of amyloid assembly. Curr Opin Struct Biol 2007; 17: 48-57.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 7
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury PT, Lashuel HA. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 2006; 443: 774-779.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 9
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Yau WM, Tycko R. Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 2006; 45: 498-512.
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 11
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F, Dobson CM. Amyloid formation by globular proteins under native conditions. Nat Chem Biol 2009; 5: 15-22.
    • (2009) Nat Chem Biol , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 12
    • 53149133922 scopus 로고    scopus 로고
    • Soluble aggregates of the amyloid-beta protein selectively stimulate permeability in human brain microvascular endothelial monolayers
    • Gonzalez-Velasquez FJ, Kotarek JA, Moss MA. Soluble aggregates of the amyloid-beta protein selectively stimulate permeability in human brain microvascular endothelial monolayers. J Neurochem 2008; 107: 466-477.
    • (2008) J Neurochem , vol.107 , pp. 466-477
    • Gonzalez-Velasquez, F.J.1    Kotarek, J.A.2    Moss, M.A.3
  • 14
    • 0031570336 scopus 로고    scopus 로고
    • Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases
    • Kelly JW. Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure 1997; 5: 595-600.
    • (1997) Structure , vol.5 , pp. 595-600
    • Kelly, J.W.1
  • 15
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid beta-protein oligomers
    • Ono K, Condron MM, Teplow DB. Structure-neurotoxicity relationships of amyloid beta-protein oligomers. Proc Natl Acad Sci USA 2009; 106: 14745-14750.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 16
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers-a decade of discovery
    • Walsh DM, Selkoe DJ. A beta oligomers-a decade of discovery. J Neurochem 2007; 101: 1172-1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 17
    • 57149102288 scopus 로고    scopus 로고
    • A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates
    • Auer S, Meersman F, Dobson CM, Vendruscolo M. A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates. PLoS Comput Biol 2008; 4:e100022.
    • (2008) PLoS Comput Biol , vol.4
    • Auer, S.1    Meersman, F.2    Dobson, C.M.3    Vendruscolo, M.4
  • 18
    • 62549097355 scopus 로고    scopus 로고
    • Characterization of the nucleation barriers for protein aggregation and amyloid formation
    • Auer S, Dobson CM, Vendruscolo M. Characterization of the nucleation barriers for protein aggregation and amyloid formation. Hfsp J 2007; 1: 137-146.
    • (2007) Hfsp J , vol.1 , pp. 137-146
    • Auer, S.1    Dobson, C.M.2    Vendruscolo, M.3
  • 19
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • Pallitto MM, Murphy RM. A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. Biophys J 2001; 81: 1805-1822.
    • (2001) Biophys J , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 20
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG. Structural classification of toxic amyloid oligomers. J Biol Chem 2008; 283: 29639-29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 21
    • 35648986681 scopus 로고    scopus 로고
    • Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfatet
    • Rangachari V, Moore BD, Reed DK, Sonoda LK, Bridges AW, Conboy E, Hartigan D, Rosenberry TL. Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfatet. Biochemistry 2007; 46: 12451-12462.
    • (2007) Biochemistry , vol.46 , pp. 12451-12462
    • Rangachari, V.1    Moore, B.D.2    Reed, D.K.3    Sonoda, L.K.4    Bridges, A.W.5    Conboy, E.6    Hartigan, D.7    Rosenberry, T.L.8
  • 23
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula M, Kayed R, Milton S, Glabe CG. Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 2007; 282: 10311-10324.
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 24
    • 61749091340 scopus 로고    scopus 로고
    • Replica exchange molecular dynamics simulations of coarse-grained proteins in implicit solvent
    • Chebaro Y, Dong X, Laghaei R, Derreumaux P, Mousseau N. Replica exchange molecular dynamics simulations of coarse-grained proteins in implicit solvent. J Phys Chem B 2009; 113: 267-274.
    • (2009) J Phys Chem B , vol.113 , pp. 267-274
    • Chebaro, Y.1    Dong, X.2    Laghaei, R.3    Derreumaux, P.4    Mousseau, N.5
  • 25
    • 33846234246 scopus 로고    scopus 로고
    • Coarse-grained protein molecular dynamics simulations
    • Derreumaux P, Mousseau N. Coarse-grained protein molecular dynamics simulations. J Chem Phys 2007; 126:025101.
    • (2007) J Chem Phys , vol.126 , pp. 025101
    • Derreumaux, P.1    Mousseau, N.2
  • 26
    • 77950219248 scopus 로고    scopus 로고
    • Elucidation of amyloid beta-protein oligomerization mechanisms: discrete molecular dynamics study
    • Urbanc B, Betnel M, Cruz L, Bitan G, Teplow DB. Elucidation of amyloid beta-protein oligomerization mechanisms: discrete molecular dynamics study. J Am Chem Soc 2010; 132: 4266-4280.
    • (2010) J Am Chem Soc , vol.132 , pp. 4266-4280
    • Urbanc, B.1    Betnel, M.2    Cruz, L.3    Bitan, G.4    Teplow, D.B.5
  • 27
    • 52049119509 scopus 로고    scopus 로고
    • Self-assembly of amyloid-forming peptides by molecular dynamics simulations
    • Wei GH, Song W, Derreumaux P, Mousseau N. Self-assembly of amyloid-forming peptides by molecular dynamics simulations. Front Biosci 2008; 13: 5681-5692.
    • (2008) Front Biosci , vol.13 , pp. 5681-5692
    • Wei, G.H.1    Song, W.2    Derreumaux, P.3    Mousseau, N.4
  • 28
    • 33747032067 scopus 로고    scopus 로고
    • Spontaneous formation of annular structures observed in molecular dynamics simulations of polyglutamine peptides
    • Marchut AJ, Hall CK. Spontaneous formation of annular structures observed in molecular dynamics simulations of polyglutamine peptides. Comput Biol Chem 2006; 30: 215-218.
    • (2006) Comput Biol Chem , vol.30 , pp. 215-218
    • Marchut, A.J.1    Hall, C.K.2
  • 30
    • 79958821061 scopus 로고    scopus 로고
    • Synergistic interactions between repeats in tau protein and A beta amyloids may be responsible for accelerated aggregation via polymorphic states
    • Miller Y, Ma BY, Nussinov R. Synergistic interactions between repeats in tau protein and A beta amyloids may be responsible for accelerated aggregation via polymorphic states. Biochemistry 2011; 50: 5172-5181.
    • (2011) Biochemistry , vol.50 , pp. 5172-5181
    • Miller, Y.1    Ma, B.Y.2    Nussinov, R.3
  • 31
    • 69449099387 scopus 로고    scopus 로고
    • Polymorphism of Alzheimer's A beta(17-42) (p3) oligomers: the importance of the turn location and its conformation
    • Miller Y, Ma BY, Nussinov R. Polymorphism of Alzheimer's A beta(17-42) (p3) oligomers: the importance of the turn location and its conformation. Biophys J 2009; 97: 1168-1177.
    • (2009) Biophys J , vol.97 , pp. 1168-1177
    • Miller, Y.1    Ma, B.Y.2    Nussinov, R.3
  • 32
    • 79953118623 scopus 로고    scopus 로고
    • Toward a molecular theory of early and late events in monomer to amyloid fibril formation
    • Leone SR, Cremer PS, Groves JT, Johnson MA, editors. Annual review of physical chemistry
    • Straub JE, Thirumalai D. Toward a molecular theory of early and late events in monomer to amyloid fibril formation. In: Leone SR, Cremer PS, Groves JT, Johnson MA, editors. Annual review of physical chemistry, Vol. 62. 2011: 437-463.
    • (2011) , vol.62 , pp. 437-463
    • Straub, J.E.1    Thirumalai, D.2
  • 33
    • 77951271571 scopus 로고    scopus 로고
    • Principles governing oligomer formation in amyloidogenic peptides
    • Straub JE, Thirumalai D. Principles governing oligomer formation in amyloidogenic peptides. Curr Opin Struct Biol 2010; 20: 187-195.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 187-195
    • Straub, J.E.1    Thirumalai, D.2
  • 34
    • 11844255790 scopus 로고    scopus 로고
    • Probing the initial stage of aggregation of the A beta(10-35)-protein: assessing the propensity for peptide dimerization
    • Tarus B, Straub JE, Thirumalai D. Probing the initial stage of aggregation of the A beta(10-35)-protein: assessing the propensity for peptide dimerization. J Mol Biol 2005; 345: 1141-1156.
    • (2005) J Mol Biol , vol.345 , pp. 1141-1156
    • Tarus, B.1    Straub, J.E.2    Thirumalai, D.3
  • 35
    • 33846565857 scopus 로고    scopus 로고
    • Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates
    • Cerda-Costa N, Esteras-Chopo A, Aviles FX, Serrano L, Villegas V. Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates. J Mol Biol 2007; 366: 1351-1363.
    • (2007) J Mol Biol , vol.366 , pp. 1351-1363
    • Cerda-Costa, N.1    Esteras-Chopo, A.2    Aviles, F.X.3    Serrano, L.4    Villegas, V.5
  • 36
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen SM, Ferrone FA, Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc Natl Acad Sci USA 2002; 99: 11884-11889.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11884-11889
    • Chen, S.M.1    Ferrone, F.A.2    Wetzel, R.3
  • 37
    • 65249190783 scopus 로고    scopus 로고
    • Effect of beta-sheet propensity on peptide aggregation
    • Bellesia G, Shea JE. Effect of beta-sheet propensity on peptide aggregation. J Chem Phys 2009; 130: 145103.
    • (2009) J Chem Phys , vol.130 , pp. 145103
    • Bellesia, G.1    Shea, J.E.2
  • 38
    • 72949120775 scopus 로고    scopus 로고
    • Diversity of kinetic pathways in amyloid fibril formation
    • Bellesia G, Shea JE. Diversity of kinetic pathways in amyloid fibril formation. J Chem Phys 2009; 131: 111102.
    • (2009) J Chem Phys , vol.131 , pp. 111102
    • Bellesia, G.1    Shea, J.E.2
  • 41
    • 34547156274 scopus 로고    scopus 로고
    • Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins
    • Murphy RM. Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins. Biochim Biophys Acta Biomembr 2007; 1768: 1923-1934.
    • (2007) Biochim Biophys Acta Biomembr , vol.1768 , pp. 1923-1934
    • Murphy, R.M.1
  • 43
    • 33745757474 scopus 로고    scopus 로고
    • The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration"
    • Powers ET, Powers DL. The kinetics of nucleated polymerizations at high concentrations: amyloid fibril formation near and above the "supercritical concentration". Biophys J 2006; 91: 122-132.
    • (2006) Biophys J , vol.91 , pp. 122-132
    • Powers, E.T.1    Powers, D.L.2
  • 44
    • 0242684664 scopus 로고    scopus 로고
    • Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life
    • Roberts CJ, Darrington RT, Whitley MB. Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life. J Pharm Sci 2003; 92: 1095-1111.
    • (2003) J Pharm Sci , vol.92 , pp. 1095-1111
    • Roberts, C.J.1    Darrington, R.T.2    Whitley, M.B.3
  • 45
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003; 26: 267-298.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 46
    • 33646130171 scopus 로고    scopus 로고
    • Inhibition of insulin fibrillogenesis with targeted peptides
    • Gibson TJ, Murphy RM. Inhibition of insulin fibrillogenesis with targeted peptides. Protein Sci 2006; 15: 1133-1141.
    • (2006) Protein Sci , vol.15 , pp. 1133-1141
    • Gibson, T.J.1    Murphy, R.M.2
  • 47
    • 27344435254 scopus 로고    scopus 로고
    • Polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction
    • Bhattacharyya AM, Thakur AK, Wetzel R. Polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction. Proc Natl Acad Sci USA 2005; 102: 15400-15405.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15400-15405
    • Bhattacharyya, A.M.1    Thakur, A.K.2    Wetzel, R.3
  • 49
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • Kelly JW. Mechanisms of amyloidogenesis. Nat Struct Biol 2000; 7: 824-826.
    • (2000) Nat Struct Biol , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 50
    • 67649366306 scopus 로고    scopus 로고
    • Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies
    • Bernacki JP, Murphy RM. Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies. Biophys J 2009; 96: 2871-2887.
    • (2009) Biophys J , vol.96 , pp. 2871-2887
    • Bernacki, J.P.1    Murphy, R.M.2
  • 52
    • 68949127591 scopus 로고    scopus 로고
    • Thermodynamics of beta-sheet formation in polyglutamine
    • Vitalis A, Lyle N, Pappu RV. Thermodynamics of beta-sheet formation in polyglutamine. Biophys J 2009; 97: 303-311.
    • (2009) Biophys J , vol.97 , pp. 303-311
    • Vitalis, A.1    Lyle, N.2    Pappu, R.V.3
  • 53
    • 54249132105 scopus 로고    scopus 로고
    • Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization
    • Vitalis A, Wang XL, Pappu RV. Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization. J Mol Biol 2008; 384: 279-297.
    • (2008) J Mol Biol , vol.384 , pp. 279-297
    • Vitalis, A.1    Wang, X.L.2    Pappu, R.V.3
  • 54
    • 77649271684 scopus 로고    scopus 로고
    • Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin
    • Williamson TE, Vitalis A, Crick SL, Pappu RV. Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. J Mol Biol 2010; 396: 1295-1309.
    • (2010) J Mol Biol , vol.396 , pp. 1295-1309
    • Williamson, T.E.1    Vitalis, A.2    Crick, S.L.3    Pappu, R.V.4
  • 55
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan R, Lindquist SL. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 2005; 435: 765-772.
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 56
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S, Deniz AA. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci USA 2007; 104: 2649-2654.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 58
    • 0036923039 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the SH3 domain aggregation suggests a generic amyloidogenesis mechanism
    • Ding F, Dokholyan NV, Buldyrev SV, Stanley HE, Shakhnovich EI. Molecular dynamics simulation of the SH3 domain aggregation suggests a generic amyloidogenesis mechanism. J Mol Biol 2002; 324: 851-857.
    • (2002) J Mol Biol , vol.324 , pp. 851-857
    • Ding, F.1    Dokholyan, N.V.2    Buldyrev, S.V.3    Stanley, H.E.4    Shakhnovich, E.I.5
  • 59
    • 0030853453 scopus 로고    scopus 로고
    • Polyalanine-based peptides as models for self-associated beta-pleated-sheet complexes
    • Blondelle SE, Forood B, Houghten RA, PerezPaya E. Polyalanine-based peptides as models for self-associated beta-pleated-sheet complexes. Biochemistry 1997; 36: 8393-8400.
    • (1997) Biochemistry , vol.36 , pp. 8393-8400
    • Blondelle, S.E.1    Forood, B.2    Houghten, R.A.3    PerezPaya, E.4
  • 60
    • 9244260521 scopus 로고    scopus 로고
    • Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides
    • Nguyen HD, Hall CK. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proc Natl Acad Sci USA 2004; 101: 16180-16185.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16180-16185
    • Nguyen, H.D.1    Hall, C.K.2
  • 61
    • 10044280719 scopus 로고    scopus 로고
    • Phase diagrams describing fibrillization by polyalanine peptides
    • Nguyen HD, Hall CK. Phase diagrams describing fibrillization by polyalanine peptides. Biophys J 2004; 87: 4122-4134.
    • (2004) Biophys J , vol.87 , pp. 4122-4134
    • Nguyen, H.D.1    Hall, C.K.2
  • 62
    • 15744382287 scopus 로고    scopus 로고
    • Kinetics of fibril formation by polyalanine peptides
    • Nguyen HD, Hall CK. Kinetics of fibril formation by polyalanine peptides. J Biol Chem 2005; 280: 9074-9082.
    • (2005) J Biol Chem , vol.280 , pp. 9074-9082
    • Nguyen, H.D.1    Hall, C.K.2
  • 63
    • 33244456166 scopus 로고    scopus 로고
    • Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulations
    • Nguyen HD, Hall CK. Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulations. J Am Chem Soc 2006; 128: 1890-1901.
    • (2006) J Am Chem Soc , vol.128 , pp. 1890-1901
    • Nguyen, H.D.1    Hall, C.K.2
  • 64
    • 34848929022 scopus 로고    scopus 로고
    • Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    • Cheon M, Chang I, Mohanty S, Luheshi LM, Dobson CM, Vendruscolo M, Favrin G. Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils. PLoS Comput Biol 2007; 3: 1727-1738.
    • (2007) PLoS Comput Biol , vol.3 , pp. 1727-1738
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5    Vendruscolo, M.6    Favrin, G.7
  • 65
    • 0035882559 scopus 로고    scopus 로고
    • Alpha-helix formation: discontinuous molecular dynamics on an intermediate-resolution protein model
    • Smith AV, Hall CK. Alpha-helix formation: discontinuous molecular dynamics on an intermediate-resolution protein model. Proteins-Struct Funct Genet 2001; 44: 344-360.
    • (2001) Proteins-Struct Funct Genet , vol.44 , pp. 344-360
    • Smith, A.V.1    Hall, C.K.2
  • 66
    • 0035882537 scopus 로고    scopus 로고
    • Assembly of a tetrameric alpha-helical bundle: computer simulations on an intermediate-resolution protein model
    • Smith AV, Hall CK. Assembly of a tetrameric alpha-helical bundle: computer simulations on an intermediate-resolution protein model. Proteins-Struct Funct Genet 2001; 44: 376-391.
    • (2001) Proteins-Struct Funct Genet , vol.44 , pp. 376-391
    • Smith, A.V.1    Hall, C.K.2
  • 67
    • 7244253280 scopus 로고    scopus 로고
    • Solvent effects on the conformational transition of a model polyalanine peptide
    • Nguyen HD, Marchut AJ, Hall CK. Solvent effects on the conformational transition of a model polyalanine peptide. Protein Sci 2004; 13: 2909-2924.
    • (2004) Protein Sci , vol.13 , pp. 2909-2924
    • Nguyen, H.D.1    Marchut, A.J.2    Hall, C.K.3
  • 68
    • 0031161658 scopus 로고    scopus 로고
    • Molecular dynamics for polymeric fluids using discontinuous potentials
    • Smith SW, Hall CK, Freeman BD. Molecular dynamics for polymeric fluids using discontinuous potentials. J Comput Phys 1997; 134: 16-30.
    • (1997) J Comput Phys , vol.134 , pp. 16-30
    • Smith, S.W.1    Hall, C.K.2    Freeman, B.D.3
  • 69
    • 36849126204 scopus 로고
    • Studies in molecular dynamics. I. General method
    • Alder BJ, Wainwright TE. Studies in molecular dynamics. I. General method. J Chem Phys 1959; 31: 459-466.
    • (1959) J Chem Phys , vol.31 , pp. 459-466
    • Alder, B.J.1    Wainwright, T.E.2
  • 70
    • 0000439253 scopus 로고
    • Molecular-dynamics study of a polymer-chain in solution
    • Rapaport DC. Molecular-dynamics study of a polymer-chain in solution. J Chem Phys 1979; 71: 3299-3303.
    • (1979) J Chem Phys , vol.71 , pp. 3299-3303
    • Rapaport, D.C.1
  • 71
    • 36149044755 scopus 로고
    • Molecular-dynamics simulation of polymer-chains with excluded volume
    • Rapaport DC. Molecular-dynamics simulation of polymer-chains with excluded volume. J Phys A-Math Gen 1978; 11: L213-L217.
    • (1978) J Phys A-Math Gen , vol.11
    • Rapaport, D.C.1
  • 72
    • 36749107785 scopus 로고
    • Molecular-dynamics simulations at constant pressure and-or temperature
    • Andersen HC. Molecular-dynamics simulations at constant pressure and-or temperature. J Chem Phys 1980; 72: 2384-2393.
    • (1980) J Chem Phys , vol.72 , pp. 2384-2393
    • Andersen, H.C.1
  • 73
    • 35848945494 scopus 로고    scopus 로고
    • Reconsidering the mechanism of polyglutamine peptide aggregation
    • Lee CC, Walters RH, Murphy RM. Reconsidering the mechanism of polyglutamine peptide aggregation. Biochemistry 2007; 46: 12810-12820.
    • (2007) Biochemistry , vol.46 , pp. 12810-12820
    • Lee, C.C.1    Walters, R.H.2    Murphy, R.M.3
  • 74
    • 58749109622 scopus 로고    scopus 로고
    • Simulations of nucleation and elongation of amyloid fibrils
    • Zhang JN, Muthukumar M. Simulations of nucleation and elongation of amyloid fibrils. J Chem Phys 2009; 130: 035102.
    • (2009) J Chem Phys , vol.130 , pp. 035102
    • Zhang, J.N.1    Muthukumar, M.2
  • 75
    • 35748943830 scopus 로고    scopus 로고
    • Pathways and intermediates of amyloid fibril formation
    • Pellarin R, Guarnera E, Caflisch A. Pathways and intermediates of amyloid fibril formation. J Mol Biol 2007; 374: 917-924.
    • (2007) J Mol Biol , vol.374 , pp. 917-924
    • Pellarin, R.1    Guarnera, E.2    Caflisch, A.3


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