메뉴 건너뛰기




Volumn 103, Issue 3, 2012, Pages 576-586

Role of β-hairpin formation in aggregation: The self-assembly of the amyloid-β(25-35) peptide

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (25 35); AMYLOID BETA-PROTEIN (25-35); PEPTIDE FRAGMENT;

EID: 84864686048     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.06.027     Document Type: Article
Times cited : (92)

References (102)
  • 1
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • C.M. Dobson Protein misfolding, evolution and disease Trends Biochem. Sci. 24 1999 329 332 (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 2
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • A.L. Fink Protein aggregation: folding aggregates, inclusion bodies and amyloid Fold. Des. 3 1998 R9 R23
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 68649086842 scopus 로고    scopus 로고
    • Structure-activity relationship of amyloid fibrils
    • S.K. Maji, and L. Wang R. Riek Structure-activity relationship of amyloid fibrils FEBS Lett. 583 2009 2610 2617
    • (2009) FEBS Lett. , vol.583 , pp. 2610-2617
    • Maji, S.K.1    Wang, L.2    Riek, R.3
  • 6
    • 37849000862 scopus 로고    scopus 로고
    • Alzheimer's Aβ peptides containing an isostructural backbone mutation afford distinct aggregate morphologies but analogous cytotoxicity. Evidence for a common low-abundance toxic structure(s)?
    • J. Bieschke, and S.J. Siegel J.W. Kelly Alzheimer's Aβ peptides containing an isostructural backbone mutation afford distinct aggregate morphologies but analogous cytotoxicity. Evidence for a common low-abundance toxic structure(s)? Biochemistry 47 2008 50 59
    • (2008) Biochemistry , vol.47 , pp. 50-59
    • Bieschke, J.1    Siegel, S.J.2    Kelly, J.W.3
  • 7
    • 34548726211 scopus 로고    scopus 로고
    • Generic cell dysfunction in neurodegenerative disorders: Role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity
    • DOI 10.1177/1073858407303428
    • M. Stefani Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity Neuroscientist 13 2007 519 531 (Pubitemid 47437929)
    • (2007) Neuroscientist , vol.13 , Issue.5 , pp. 519-531
    • Stefani, M.1
  • 9
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • DOI 10.1126/science.1105850
    • A.T. Petkova, and R.D. Leapman R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils Science 307 2005 262 265 (Pubitemid 40116242)
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 10
    • 0000293742 scopus 로고
    • Uber eine eigenartige Erkrankung der Hirnrinde
    • A. Alzheimer Uber eine eigenartige Erkrankung der Hirnrinde Allg. Zeitschr. Psychiatr. 64 1907 146 148
    • (1907) Allg. Zeitschr. Psychiatr. , vol.64 , pp. 146-148
    • Alzheimer, A.1
  • 11
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • J. Hardy, and D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 12
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • DOI 10.1038/325733a0
    • J. Kang, and H.-G. Lemaire B. Müller-Hill The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor Nature 325 1987 733 736 (Pubitemid 17054046)
    • (1987) Nature , vol.325 , Issue.6106 , pp. 733-736
    • Kang, J.1    Lemaire, H.-G.2    Unterbeck, A.3
  • 13
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by α-, β- And γ-secretases
    • J. Nunan, and D.H. Small Regulation of APP cleavage by α-, β- and γ-secretases FEBS Lett. 483 2000 6 10
    • (2000) FEBS Lett. , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 14
    • 72749122338 scopus 로고    scopus 로고
    • Subcellular and metabolic examination of amyloid-β peptides in Alzheimer disease pathogenesis: Evidence for Aβ(25-35)
    • Y.G. Kaminsky, and M.W. Marlatt E.A. Kosenko Subcellular and metabolic examination of amyloid-β peptides in Alzheimer disease pathogenesis: evidence for Aβ(25-35) Exp. Neurol. 221 2010 26 37
    • (2010) Exp. Neurol. , vol.221 , pp. 26-37
    • Kaminsky, Y.G.1    Marlatt, M.W.2    Kosenko, E.A.3
  • 15
  • 17
    • 27644596641 scopus 로고    scopus 로고
    • What is the role of protein aggregation in neurodegeneration?
    • DOI 10.1038/nrm1742, PII N1742
    • C.A. Ross, and M.A. Poirier Opinion: What is the role of protein aggregation in neurodegeneration? Nat. Rev. Mol. Cell Biol. 6 2005 891 898 (Pubitemid 41568738)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.11 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 19
    • 77950158093 scopus 로고    scopus 로고
    • Conformations and biological activities of amyloid β peptide 25-35
    • L. Millucci, and L. Ghezzi A. Santucci Conformations and biological activities of amyloid β peptide 25-35 Curr. Protein Pept. Sci. 11 2010 54 67
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 54-67
    • Millucci, L.1    Ghezzi, L.2    Santucci, A.3
  • 22
    • 18144391180 scopus 로고    scopus 로고
    • Studies of the effects of fragment (25-35) of beta-amyloid peptide on the behavior of rats in a radial maze
    • DOI 10.1007/s11055-005-0086-1
    • M.Y. Stepanichev, and Y.V. Moiseeva N.V. Gulyaeva Studies of the effects of fragment (25-35) of β-amyloid peptide on the behavior of rats in a radial maze Neurosci. Behav. Physiol. 35 2005 511 518 (Pubitemid 40613414)
    • (2005) Neuroscience and Behavioral Physiology , vol.35 , Issue.5 , pp. 511-518
    • Stepanichev, M.Yu.1    Moiseeva, Yu.V.2    Lazareva, N.A.3    Gulyaeva, N.V.4
  • 23
    • 31444456953 scopus 로고    scopus 로고
    • Studies of the effects of central administration of β-amyloid peptide (25-35): Pathomorphological changes in the hippocampus and impairment of spatial memory
    • DOI 10.1007/s11055-005-0167-1
    • M.Y. Stepanichev, and I.M. Zdobnova N.V. Gulyaeva Studies of the effects of central administration of β-amyloid peptide (25-35): pathomorphological changes in the hippocampus and impairment of spatial memory Neurosci. Behav. Physiol. 36 2006 101 106 (Pubitemid 43149518)
    • (2006) Neuroscience and Behavioral Physiology , vol.36 , Issue.1 , pp. 101-106
    • Stepanichev, M.Yu.1    Zdobnova, I.M.2    Zarubenko, I.I.3    Lazareva, N.A.4    Gulyaeva, N.V.5
  • 24
    • 58149516815 scopus 로고    scopus 로고
    • Amyloid-β(25-35) impairs memory and increases NO in the temporal cortex of rats
    • I.D. Limón, and A. Díaz J. Guevara Amyloid-β(25-35) impairs memory and increases NO in the temporal cortex of rats Neurosci. Res. 63 2009 129 137
    • (2009) Neurosci. Res. , vol.63 , pp. 129-137
    • Limón, I.D.1    Díaz, A.2    Guevara, J.3
  • 25
    • 0025729748 scopus 로고
    • Morphology and antibody recognition of synthetic β-amyloid peptides
    • P.E. Fraser, and L.K. Duffy D.A. Kirschner Morphology and antibody recognition of synthetic β-amyloid peptides J. Neurosci. Res. 28 1991 474 485
    • (1991) J. Neurosci. Res. , vol.28 , pp. 474-485
    • Fraser, P.E.1    Duffy, L.K.2    Kirschner, D.A.3
  • 26
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: Contributions of the β 25-35 region to aggregation and neurotoxicity
    • C.J. Pike, and A.J. Walencewicz-Wasserman C.W. Cotman Structure-activity analyses of β-amyloid peptides: contributions of the β 25-35 region to aggregation and neurotoxicity J. Neurochem. 64 1995 253 265
    • (1995) J. Neurochem. , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Cotman, C.W.3
  • 27
    • 0028850087 scopus 로고
    • Suppression of mitochondrial succinate dehydrogenase, a primary target of β-amyloid, and its derivative racemized at ser residue
    • I. Kaneko, and N. Yamada S. Tutumi Suppression of mitochondrial succinate dehydrogenase, a primary target of β-amyloid, and its derivative racemized at Ser residue J. Neurochem. 65 1995 2585 2593
    • (1995) J. Neurochem. , vol.65 , pp. 2585-2593
    • Kaneko, I.1    Yamada, N.2    Tutumi, S.3
  • 30
    • 19444383084 scopus 로고    scopus 로고
    • Aβ(31-35) and Aβ(25-35) fragments of amyloid beta-protein induce cellular death through apoptotic signals: Role of the redox state of methionine-35
    • DOI 10.1016/j.febslet.2005.04.041, PII S0014579305005168
    • M.E. Clementi, and S. Marini F. Misiti Aβ(31-35) and Aβ(25-35) fragments of amyloid β-protein induce cellular death through apoptotic signals: Role of the redox state of methionine-35 FEBS Lett. 579 2005 2913 2918 (Pubitemid 40725266)
    • (2005) FEBS Letters , vol.579 , Issue.13 , pp. 2913-2918
    • Clementi, M.E.1    Marini, S.2    Coletta, M.3    Orsini, F.4    Giardina, B.5    Misiti, F.6
  • 32
    • 0030457933 scopus 로고    scopus 로고
    • Three-dimensional structures of the amyloid β peptide (25-35) in membrane-mimicking environment
    • DOI 10.1021/bi961598j
    • T. Kohno, and K. Kobayashi A. Takashima Three-dimensional structures of the amyloid β peptide (25-35) in membrane-mimicking environment Biochemistry 35 1996 16094 16104 (Pubitemid 27045737)
    • (1996) Biochemistry , vol.35 , Issue.50 , pp. 16094-16104
    • Kohno, T.1    Kobayashi, K.2    Maeda, T.3    Sato, K.4    Takashima, A.5
  • 34
    • 0028181758 scopus 로고
    • Reversible random coil-β-sheet transition of the Alzheimer β-amyloid fragment (25-35)
    • E. Terzi, G. Hölzemann, and J. Seelig Reversible random coil-β-sheet transition of the Alzheimer β-amyloid fragment (25-35) Biochemistry 33 1994 1345 1350
    • (1994) Biochemistry , vol.33 , pp. 1345-1350
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 35
    • 0028179865 scopus 로고
    • Alzheimer β-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • E. Terzi, G. Hölzemann, and J. Seelig Alzheimer β-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes Biochemistry 33 1994 7434 7441
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 36
    • 3042775141 scopus 로고    scopus 로고
    • Structure of Aβ(25-35) peptide in different environments
    • DOI 10.1529/biophysj.104.040907
    • G. Shanmugam, and P.L. Polavarapu Structure of A β(25-35) peptide in different environments Biophys. J. 87 2004 622 630 (Pubitemid 38880114)
    • (2004) Biophysical Journal , vol.87 , Issue.1 , pp. 622-630
    • Shanmugam, G.1    Polavarapu, P.L.2
  • 37
    • 33748473035 scopus 로고    scopus 로고
    • Effects of solvent on the structure of the alzheimer amyloid-β(25- 35) peptide
    • DOI 10.1529/biophysj.105.079186
    • G. Wei, and J.-E. Shea Effects of solvent on the structure of the Alzheimer amyloid-β(25-35) peptide Biophys. J. 91 2006 1638 1647 (Pubitemid 44352430)
    • (2006) Biophysical Journal , vol.91 , Issue.5 , pp. 1638-1647
    • Wei, G.1    Shea, J.-E.2
  • 38
    • 77950276918 scopus 로고    scopus 로고
    • Structural diversity of dimers of the Alzheimer amyloid-β(25-35) peptide and polymorphism of the resulting fibrils
    • G. Wei, A.I. Jewett, and J.-E. Shea Structural diversity of dimers of the Alzheimer amyloid-β(25-35) peptide and polymorphism of the resulting fibrils Phys. Chem. Chem. Phys. 12 2010 3622 3629
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 3622-3629
    • Wei, G.1    Jewett, A.I.2    Shea, J.-E.3
  • 39
    • 78649570071 scopus 로고    scopus 로고
    • Disordered versus fibril-like amyloid β (25-35) dimers in water: Structure and thermodynamics
    • M. Kittner, and V. Knecht Disordered versus fibril-like amyloid β (25-35) dimers in water: structure and thermodynamics J. Phys. Chem. B 114 2010 15288 15295
    • (2010) J. Phys. Chem. B , vol.114 , pp. 15288-15295
    • Kittner, M.1    Knecht, V.2
  • 40
    • 79955896407 scopus 로고    scopus 로고
    • The amyloid formation mechanism in human IAPP: Dimers have β-strand monomer-monomer interfaces
    • N.F. Dupuis, and C. Wu M.T. Bowers The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfaces J. Am. Chem. Soc. 133 2011 7240 7243
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7240-7243
    • Dupuis, N.F.1    Wu, C.2    Bowers, M.T.3
  • 41
    • 73249115986 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide monomers form ordered β-hairpins: A possible direct amyloidogenic precursor
    • N.F. Dupuis, and C. Wu M.T. Bowers Human islet amyloid polypeptide monomers form ordered β-hairpins: a possible direct amyloidogenic precursor J. Am. Chem. Soc. 131 2009 18283 18292
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18283-18292
    • Dupuis, N.F.1    Wu, C.2    Bowers, M.T.3
  • 43
    • 33846324298 scopus 로고    scopus 로고
    • The Structure of the Alzheimer Amyloid β 10-35 Peptide Probed through Replica-Exchange Molecular Dynamics Simulations in Explicit Solvent
    • DOI 10.1016/j.jmb.2006.11.015, PII S0022283606015440
    • A. Baumketner, and J.-E. Shea The structure of the Alzheimer amyloid β 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent J. Mol. Biol. 366 2007 275 285 (Pubitemid 46123329)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 275-285
    • Baumketner, A.1    Shea, J.-E.2
  • 44
    • 33748121600 scopus 로고    scopus 로고
    • Folding Landscapes of the Alzheimer Amyloid-β(12-28) Peptide
    • DOI 10.1016/j.jmb.2006.07.032, PII S0022283606009028
    • A. Baumketner, and J.-E. Shea Folding landscapes of the Alzheimer amyloid-β(12-28) peptide J. Mol. Biol. 362 2006 567 579 (Pubitemid 44307159)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.3 , pp. 567-579
    • Baumketner, A.1    Shea, J.-E.2
  • 45
    • 74949142621 scopus 로고    scopus 로고
    • Oligomers of the prion protein fragment 106-126 are likely assembled from β-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide's monomeric conformation
    • M. Grabenauer, and C. Wu M.T. Bowers Oligomers of the prion protein fragment 106-126 are likely assembled from β-hairpins in solution, and methionine oxidation inhibits assembly without altering the peptide's monomeric conformation J. Am. Chem. Soc. 132 2010 532 539
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 532-539
    • Grabenauer, M.1    Wu, C.2    Bowers, M.T.3
  • 46
    • 80053595082 scopus 로고    scopus 로고
    • Protein engineering to stabilize soluble amyloid β-protein aggregates for structural and functional studies
    • T. Härd Protein engineering to stabilize soluble amyloid β-protein aggregates for structural and functional studies FEBS J. 278 2011 3884 3892
    • (2011) FEBS J. , vol.278 , pp. 3884-3892
    • Härd, T.1
  • 47
    • 77957257176 scopus 로고    scopus 로고
    • Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering
    • A. Sandberg, and L.M. Luheshi T. Härd Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering Proc. Natl. Acad. Sci. USA 107 2010 15595 15600
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15595-15600
    • Sandberg, A.1    Luheshi, L.M.2    Härd, T.3
  • 48
    • 64549140676 scopus 로고    scopus 로고
    • Structural characterization of a soluble amyloid β-peptide oligomer
    • L. Yu, and R. Edalji E.T. Olejniczak Structural characterization of a soluble amyloid β-peptide oligomer Biochemistry 48 2009 1870 1877
    • (2009) Biochemistry , vol.48 , pp. 1870-1877
    • Yu, L.1    Edalji, R.2    Olejniczak, E.T.3
  • 50
    • 41249098954 scopus 로고    scopus 로고
    • Interaction of Alzheimer's A β peptide with an engineered binding protein - Thermodynamics and kinetics of coupled folding-binding
    • W. Hoyer, and T. Härd Interaction of Alzheimer's A β peptide with an engineered binding protein - thermodynamics and kinetics of coupled folding-binding J. Mol. Biol. 378 2008 398 411
    • (2008) J. Mol. Biol. , vol.378 , pp. 398-411
    • Hoyer, W.1    Härd, T.2
  • 53
    • 77955790562 scopus 로고    scopus 로고
    • Comparing the folding free-energy landscapes of Aβ42 variants with different aggregation properties
    • S. Mitternacht, and I. Staneva A. Irbäck Comparing the folding free-energy landscapes of Aβ42 variants with different aggregation properties Proteins 78 2010 2600 2608
    • (2010) Proteins , vol.78 , pp. 2600-2608
    • Mitternacht, S.1    Staneva, I.2    Irbäck, A.3
  • 54
    • 84954358028 scopus 로고    scopus 로고
    • Amyloid β-protein monomer folding: Free-energy surfaces reveal alloform-specific differences
    • M. Yang, and D.B. Teplow Amyloid β-protein monomer folding: free-energy surfaces reveal alloform-specific differences J. Mol. Biol. 384 2008 450 464
    • (2008) J. Mol. Biol. , vol.384 , pp. 450-464
    • Yang, M.1    Teplow, D.B.2
  • 55
    • 37649019187 scopus 로고    scopus 로고
    • Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils
    • G. Habicht, and C. Haupt M. Fändrich Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils Proc. Natl. Acad. Sci. USA 104 2007 19232 19237
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19232-19237
    • Habicht, G.1    Haupt, C.2    Fändrich, M.3
  • 56
    • 69249239132 scopus 로고    scopus 로고
    • Antiparallel β-sheet: A signature structure of the oligomeric amyloid β-peptide
    • E. Cerf, and R. Sarroukh V. Raussens Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide Biochem. J. 421 2009 415 423
    • (2009) Biochem. J. , vol.421 , pp. 415-423
    • Cerf, E.1    Sarroukh, R.2    Raussens, V.3
  • 57
    • 79960306242 scopus 로고    scopus 로고
    • Molecular origin of Gerstmann-Sträussler-Scheinker syndrome: Insight from computer simulation of an amyloidogenic prion peptide
    • I. Daidone, A. Di Nola, and J.C. Smith Molecular origin of Gerstmann-Sträussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide Biophys. J. 100 2011 3000 3007
    • (2011) Biophys. J. , vol.100 , pp. 3000-3007
    • Daidone, I.1    Di Nola, A.2    Smith, J.C.3
  • 58
    • 77958454277 scopus 로고    scopus 로고
    • Stable and metastable states of human amylin in solution
    • A.S. Reddy, and L. Wang J.J. de Pablo Stable and metastable states of human amylin in solution Biophys. J. 99 2010 2208 2216
    • (2010) Biophys. J. , vol.99 , pp. 2208-2216
    • Reddy, A.S.1    Wang, L.2    De Pablo, J.J.3
  • 59
    • 42449155493 scopus 로고    scopus 로고
    • Amyloid-β(29-42) dimer formations studied by a multicanonical- multioverlap molecular dynamics simulation
    • S.G. Itoh, and Y. Okamoto Amyloid-β(29-42) dimer formations studied by a multicanonical-multioverlap molecular dynamics simulation J. Phys. Chem. B 112 2008 2767 2770
    • (2008) J. Phys. Chem. B , vol.112 , pp. 2767-2770
    • Itoh, S.G.1    Okamoto, Y.2
  • 60
    • 79952848294 scopus 로고    scopus 로고
    • Effects of G33A and G33I mutations on the structures of monomer and dimer of the amyloid-β fragment 29-42 by replica exchange molecular dynamics simulations
    • Y. Lu, G. Wei, and P. Derreumaux Effects of G33A and G33I mutations on the structures of monomer and dimer of the amyloid-β fragment 29-42 by replica exchange molecular dynamics simulations J. Phys. Chem. B 115 2011 1282 1288
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1282-1288
    • Lu, Y.1    Wei, G.2    Derreumaux, P.3
  • 61
    • 66149189211 scopus 로고    scopus 로고
    • Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent
    • Y. Lu, and P. Derreumaux G. Wei Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent Proteins 75 2009 954 963
    • (2009) Proteins , vol.75 , pp. 954-963
    • Lu, Y.1    Derreumaux, P.2    Wei, G.3
  • 62
    • 7744225860 scopus 로고    scopus 로고
    • Modeling the α-helix to β-hairpin transition mechanism and the formation of oligomeric aggregates of the fibrillogenic peptide Aβ(12-28): Insights from all-atom molecular dynamics simulations
    • DOI 10.1016/j.jmgm.2004.07.004, PII S1093326304000750
    • F. Simona, and G. Tiana G. Colombo Modeling the α-helix to β-hairpin transition mechanism and the formation of oligomeric aggregates of the fibrillogenic peptide Aβ(12-28): insights from all-atom molecular dynamics simulations J. Mol. Graph. Model. 23 2004 263 273 (Pubitemid 39463105)
    • (2004) Journal of Molecular Graphics and Modelling , vol.23 , Issue.3 , pp. 263-273
    • Simona, F.1    Tiana, G.2    Broglia, R.A.3    Colombo, G.4
  • 64
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, and C. Kutzner E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Lindahl, E.3
  • 66
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • DOI 10.1007/S008940100045
    • E. Lindahl, B. Hess, and D. van der Spoel GROMACS 3.0: a package for molecular simulation and trajectory analysis J. Mol. Model. 7 2001 306 317 (Pubitemid 36153547)
    • (2001) Journal of Molecular Modeling , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 68
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • DOI 10.1021/ja9621760, PII S0002786396021762
    • W.L. Jorgensen, D.S. Maxwell, and J. Tirado-Rives Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids J. Am. Chem. Soc. 118 1996 11225 11236 (Pubitemid 26399746)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 69
    • 0033606250 scopus 로고    scopus 로고
    • OPLS all-atom model for amines: Resolution of the amine hydration problem
    • DOI 10.1021/ja984106u
    • R.C. Rizzo, and W.L. Jorgensen OPLS all-atom model for amines: resolution of the amine hydration problem J. Am. Chem. Soc. 121 1999 4827 4836 (Pubitemid 29252636)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.20 , pp. 4827-4836
    • Rizzo, R.C.1    Jorgensen, W.L.2
  • 70
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • DOI 10.1021/jp003919d
    • G.A. Kaminski, and R. Friesner W. Jorgensen Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides J. Phys. Chem. B 105 2001 6474 6487 (Pubitemid 35339015)
    • (2001) Journal of Physical Chemistry B , vol.105 , Issue.28 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 71
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • W.L. Jorgensen, and J. Chandrasekhar M.L. Klein Comparison of simple potential functions for simulating liquid water J. Chem. Phys. 79 1983 926 935
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 72
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N · log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: an N · log(N) method for Ewald sums in large systems J. Chem. Phys. 98 1993 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 74
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • S. Nosé A molecular dynamics method for simulations in the canonical ensemble Mol. Phys. 52 1984 255 268
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nosé, S.1
  • 75
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • S. Nosé A unified formulation of the constant temperature molecular dynamics methods J. Chem. Phys. 81 1984 511 519
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nosé, S.1
  • 76
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: Equilibrium phase-space distributions Phys. Rev. A 31 1985 1695 1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 77
    • 22944467757 scopus 로고
    • Computer "Experiments" on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules
    • L. Verlet Computer "experiments" on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules Phys. Rev. 159 1967 98 103
    • (1967) Phys. Rev. , vol.159 , pp. 98-103
    • Verlet, L.1
  • 79
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • S. Miyamoto, and P.A. Kollman Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models J. Comput. Chem. 13 1992 952 962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 80
    • 0030516672 scopus 로고    scopus 로고
    • Exchange Monte Carlo Method and Application to Spin Glass Simulations
    • K. Hukushima, and K. Nemoto Exchange Monte Carlo method and application to spin glass simulations J. Phys. Soc. Jpn. 65 1996 1604 1608 (Pubitemid 126456584)
    • (1996) Journal of the Physical Society of Japan , vol.65 , Issue.6 , pp. 1604-1608
    • Hukushima, K.1    Nemoto, K.2
  • 81
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • PII S0009261499011239
    • Y. Sugita, and Y. Okamoto Replica-exchange molecular dynamics method for protein folding Chem. Phys. Lett. 314 1999 141 151 (Pubitemid 129556751)
    • (1999) Chemical Physics Letters , vol.314 , Issue.1-2 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 82
    • 41549127613 scopus 로고    scopus 로고
    • A temperature predictor for parallel tempering simulations
    • A. Patriksson, and D. van der Spoel A temperature predictor for parallel tempering simulations Phys. Chem. Chem. Phys. 10 2008 2073 2077
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 2073-2077
    • Patriksson, A.1    Van Der Spoel, D.2
  • 85
    • 0034604381 scopus 로고    scopus 로고
    • Theoretical studies on Alzheimer's disease: Structures of β-amyloid aggregates
    • S. Kim, and D. Weaver Theoretical studies on Alzheimer's disease: structures of β-amyloid aggregates Theochem 527 2000 127 138
    • (2000) Theochem , vol.527 , pp. 127-138
    • Kim, S.1    Weaver, D.2
  • 86
    • 84863229747 scopus 로고    scopus 로고
    • Atomic view of a toxic amyloid small oligomer
    • A. Laganowsky, and C. Liu D. Eisenberg Atomic view of a toxic amyloid small oligomer Science 335 2012 1228 1231
    • (2012) Science , vol.335 , pp. 1228-1231
    • Laganowsky, A.1    Liu, C.2    Eisenberg, D.3
  • 88
  • 93
    • 69249200012 scopus 로고    scopus 로고
    • Rapid aggregation and assembly in aqueous solution of A β (25-35) peptide
    • L. Millucci, and R. Raggiaschi A. Santucci Rapid aggregation and assembly in aqueous solution of A β (25-35) peptide J. Biosci. 34 2009 293 303
    • (2009) J. Biosci. , vol.34 , pp. 293-303
    • Millucci, L.1    Raggiaschi, R.2    Santucci, A.3
  • 94
    • 33646192684 scopus 로고    scopus 로고
    • The stability of monomeric intermediates controls amyloid formation: Aβ25-35 and its N27Q mutant
    • B. Ma, and R. Nussinov The stability of monomeric intermediates controls amyloid formation: Aβ25-35 and its N27Q mutant Biophys. J. 90 2006 3365 3374
    • (2006) Biophys. J. , vol.90 , pp. 3365-3374
    • Ma, B.1    Nussinov, R.2
  • 95
    • 0035254995 scopus 로고    scopus 로고
    • Energy landscape theory for Alzheimer's amyloid β-peptide fibril elongation
    • DOI 10.1002/1097-0134(20010201)42:2<217::AID-PROT90>3.0.CO;2-N
    • F. Massi, and J.E. Straub Energy landscape theory for Alzheimer's amyloid β-peptide fibril elongation Proteins 42 2001 217 229 (Pubitemid 32047330)
    • (2001) Proteins: Structure, Function and Genetics , vol.42 , Issue.2 , pp. 217-229
    • Massi, F.1    Straub, J.E.2
  • 96
    • 79953118623 scopus 로고    scopus 로고
    • Toward a molecular theory of early and late events in monomer to amyloid fibril formation
    • J.E. Straub, and D. Thirumalai Toward a molecular theory of early and late events in monomer to amyloid fibril formation Annu. Rev. Phys. Chem. 62 2011 437 463
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 437-463
    • Straub, J.E.1    Thirumalai, D.2
  • 97
    • 58849114585 scopus 로고    scopus 로고
    • Replica exchange simulations of the thermodynamics of Aβ fibril growth
    • T. Takeda, and D.K. Klimov Replica exchange simulations of the thermodynamics of Aβ fibril growth Biophys. J. 96 2009 442 452
    • (2009) Biophys. J. , vol.96 , pp. 442-452
    • Takeda, T.1    Klimov, D.K.2
  • 98
    • 70350381490 scopus 로고    scopus 로고
    • Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils
    • E.P. O'Brien, and Y. Okamoto D. Thirumalai Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils J. Phys. Chem. B 113 2009 14421 14430
    • (2009) J. Phys. Chem. B , vol.113 , pp. 14421-14430
    • O'Brien, E.P.1    Okamoto, Y.2    Thirumalai, D.3
  • 100
    • 1842686289 scopus 로고    scopus 로고
    • Kinetic analysis of beta-amyloid fibril elongation
    • DOI 10.1016/j.ab.2004.01.014, PII S0003269704000922
    • M.J. Cannon, and A.D. Williams D.G. Myszka Kinetic analysis of β-amyloid fibril elongation Anal. Biochem. 328 2004 67 75 (Pubitemid 38479619)
    • (2004) Analytical Biochemistry , vol.328 , Issue.1 , pp. 67-75
    • Cannon, M.J.1    Williams, A.D.2    Wetzel, R.3    Myszka, D.G.4
  • 101
    • 17644397372 scopus 로고    scopus 로고
    • Aβ40-lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid
    • DOI 10.1021/bi0474867
    • K.L. Sciarretta, and D.J. Gordon S.C. Meredith Aβ40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid Biochemistry 44 2005 6003 6014 (Pubitemid 40570694)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6003-6014
    • Sciarretta, K.L.1    Gordon, D.J.2    Petkova, A.T.3    Tycko, R.4    Meredith, S.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.