메뉴 건너뛰기




Volumn 135, Issue 3, 2011, Pages

Does amino acid sequence determine the properties of Aβ dimer?

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; END-TO-END DISTANCES; GAUSSIAN STATISTICS; IMPLICIT SOLVENT MODEL; NON-LOCAL INTERACTIONS; NONBONDED INTERACTION; REPLICA EXCHANGE MOLECULAR DYNAMICS; THEORETICAL STUDY; UNITED ATOMS;

EID: 79960904377     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3610427     Document Type: Article
Times cited : (4)

References (50)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • C. M. Dobson, Nature (London) 426, 884 (2003). 10.1038/nature02261 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • DOI 10.1038/nature01891
    • F. Chiti, M. Stefani, N. Taddei, G. Ramponi, and C. M. Dobson, Nature (London) 424, 805 (2003). 10.1038/nature01891 (Pubitemid 37021713)
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddel, N.3    Ramponi, G.4    Dobson, C.M.5
  • 4
    • 33645522802 scopus 로고    scopus 로고
    • 10.1088/1478-3975/3/1/S02
    • M. Reches and E. Gazit, Phys. Biol. 3, S10 (2006). 10.1088/1478-3975/3/1/ S02
    • (2006) Phys. Biol. , vol.3 , pp. 10
    • Reches, M.1    Gazit, E.2
  • 5
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • DOI 10.1038/nature02264
    • D. J. Selkoe, Nature (London) 426, 900 (2003). 10.1038/nature02264 (Pubitemid 38056883)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 900-904
    • Selkoe, D.J.1
  • 7
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • DOI 10.1002/jnr.10328
    • M. D. Kirkitadze, G. Bitan, and D. B. Teplow, J. Neurosci. Res. 69, 567 (2002). 10.1002/jnr.10328 (Pubitemid 34966869)
    • (2002) Journal of Neuroscience Research , vol.69 , Issue.5 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 8
    • 0036407227 scopus 로고    scopus 로고
    • Peptide aggregation in neurodegenerative disease
    • DOI 10.1146/annurev.bioeng.4.092801.094202
    • R. M. Murphy, Annu. Rev. Biomed. Eng. 4, 155 (2002). 10.1146/annurev. bioeng.4.092801.094202 (Pubitemid 35217418)
    • (2002) Annual Review of Biomedical Engineering , vol.4 , pp. 155-174
    • Murphy, R.M.1
  • 10
    • 0026597063 scopus 로고
    • 10.1126/science.1566067
    • J. Hardy and G. A. Higgins, Science 256, 184 (1992). 10.1126/science. 1566067
    • (1992) Science , vol.256 , pp. 184
    • Hardy, J.1    Higgins, G.A.2
  • 11
    • 13444310701 scopus 로고    scopus 로고
    • Characterization of chemical exchange between soluble and aggregated states of β-amyloid by solution-state NMR upon variation of salt conditions
    • DOI 10.1021/bi048264b
    • S. Narayanan and B. Reif, Biochemistry 44, 1444 (2005). 10.1021/bi048264b (Pubitemid 40204388)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1444-1452
    • Narayanan, S.1    Reif, B.2
  • 12
    • 0041816383 scopus 로고    scopus 로고
    • Elucidation of primary structure elements controlling early amyloid β-protein oligomerization
    • DOI 10.1074/jbc.M300825200
    • G. Bitan, S. S. Vollers, and D. B. Teplow, J. Biol. Chem. 278, 34882 (2003). 10.1074/jbc.M300825200 (Pubitemid 37102247)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 34882-34889
    • Bitan, G.1    Vollers, S.S.2    Teplow, D.B.3
  • 14
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • C. Haass and D. J. Selkoe, Nat. Rev. Mol. Cell. Biol. 8, 101 (2007). 10.1038/nrm2101 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 18
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • DOI 10.1021/bi051952q
    • A. T. Petkova, W.-M. Yau, and R. Tycko, Biochemistry 45, 498 (2006). 10.1021/bi051952q (Pubitemid 43100415)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 498-512
    • Petkova, A.T.1    Yau, W.-M.2    Tycko, R.3
  • 21
    • 33748525884 scopus 로고    scopus 로고
    • Computational models for the prediction of polypeptide aggregation propensity
    • DOI 10.1016/j.cbpa.2006.07.009, PII S1367593106001104, Analytical Techniques/Mechanisms
    • A. Caflisch, Curr. Opin. Chem. Biol. 10, 437 (2006). 10.1016/j.cbpa.2006. 07.009 (Pubitemid 44375058)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 437-444
    • Caflisch, A.1
  • 22
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's Peptides Aβ40 and 42 Adopt Distinct Conformations in Water: A Combined MD / NMR Study
    • DOI 10.1016/j.jmb.2007.02.093, PII S0022283607003105
    • N. G. Sgourakis, Y. Yan, S. A. McCallum, C. Wang, and A. E. Garcia, J. Mol. Biol. 368, 1448 (2007). 10.1016/j.jmb.2007.02.093 (Pubitemid 46617600)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.5 , pp. 1448-1457
    • Sgourakis, N.G.1    Yan, Y.2    McCallum, S.A.3    Wang, C.4    Garcia, A.E.5
  • 23
    • 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, J. Mol. Biol. 362, 567 (2006). 10.1016/j.jmb.2006.07.032 (Pubitemid 44307159)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.3 , pp. 567-579
    • Baumketner, A.1    Shea, J.-E.2
  • 25
    • 77957256708 scopus 로고    scopus 로고
    • 10.1016/j.jmb.2010.08.003
    • A. Vitalis and A. Caflisch, J. Mol. Biol. 403, 148 (2010). 10.1016/j.jmb.2010.08.003
    • (2010) J. Mol. Biol. , vol.403 , pp. 148
    • Vitalis, A.1    Caflisch, A.2
  • 27
    • 61549102795 scopus 로고    scopus 로고
    • 10.1016/j.bpj.2008.10.040
    • G. Bellesia and J.-E. Shea, Biophys. J. 96, 875 (2009). 10.1016/j.bpj.2008.10.040
    • (2009) Biophys. J. , vol.96 , pp. 875
    • Bellesia, G.1    Shea, J.-E.2
  • 34
    • 68949122827 scopus 로고    scopus 로고
    • 10.1016/j.bpj.2009.03.015
    • T. Takeda and D. K. Klimov, Biophys. J. 96, 4428 (2009). 10.1016/j.bpj.2009.03.015
    • (2009) Biophys. J. , vol.96 , pp. 4428
    • Takeda, T.1    Klimov, D.K.2
  • 37
    • 0001616080 scopus 로고    scopus 로고
    • 10.1016/S0009-2614(99)01123-9
    • Y. Sugita and Y. Okamoto, Chem. Phys. Lett. 114, 141 (1999). 10.1016/S0009-2614(99)01123-9
    • (1999) Chem. Phys. Lett. , vol.114 , pp. 141
    • Sugita, Y.1    Okamoto, Y.2
  • 38
    • 58849114585 scopus 로고    scopus 로고
    • 10.1016/j.bpj.2008.10.008
    • T. Takeda and D. K. Klimov, Biophys. J. 96, 442 (2009). 10.1016/j.bpj.2008.10.008
    • (2009) Biophys. J. , vol.96 , pp. 442
    • Takeda, T.1    Klimov, D.K.2
  • 39
    • 0020997912 scopus 로고
    • 10.1002/bi360221211
    • W. Kabsch and C. Sander, Biopolymers 22, 2577 (1983). 10.1002/bip.360221211
    • (1983) Biopolymers , vol.22 , pp. 2577
    • Kabsch, W.1    Sander, C.2
  • 41
    • 79960901634 scopus 로고    scopus 로고
    • See supplementary material at E-JCPSA6-135-034127 for applicability of implicit solvent model and REMD convergence.
    • See supplementary material at http://dx.doi.org/10.1063/1.3610427 E-JCPSA6-135-034127 for applicability of implicit solvent model and REMD convergence.
  • 46
    • 0346492907 scopus 로고    scopus 로고
    • Fractal and statistical properties of large compact polymers: A computational study
    • DOI 10.1016/j.polymer.2003.10.073
    • R. Lua, A. L. Borovinskiy, and A. Y. Grosberg, Polymer 45, 717 (2004). 10.1016/j.polymer.2003.10.073 (Pubitemid 38082205)
    • (2004) Polymer , vol.45 , Issue.2 , pp. 717-731
    • Lua, R.1    Borovinskiy, A.L.2    Grosberg, A.Yu.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.