Role of Electrostatic Interactions in Amyloid β-Protein (Aβ) Oligomer Formation: A Discrete Molecular Dynamics Study
- 1 June 2007
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 92 (11) , 4064-4077
- https://doi.org/10.1529/biophysj.106.097766
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- Characterizations of distinct amyloidogenic conformations of the Aβ (1–40) and (1–42) peptidesBiochemical and Biophysical Research Communications, 2006
- Impact of the Mutation A21G (Flemish Variant) on Alzheimer’s β-Amyloid Dimers by Molecular Dynamics SimulationsBiophysical Journal, 2006
- Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid FibrilsBiochemistry, 2005
- Probing the Initial Stage of Aggregation of the Aβ10-35-protein: Assessing the Propensity for Peptide DimerizationJournal of Molecular Biology, 2005
- Mutant Presenilin 2 Transgenic MicePublished by Elsevier ,2000
- Identifying the protein folding nucleus using molecular dynamics 1 1Edited by A. R. FershtJournal of Molecular Biology, 2000
- Temperature-dependent β-sheet formation in β-amyloid Aβ1–40 peptide in water: uncoupling β-structure folding from aggregationBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
- Folding of a model three-helix bundle protein: a thermodynamic and kinetic analysis 1 1Edited by A. R. FershtJournal of Molecular Biology, 1999
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996
- Molecular dynamics with coupling to an external bathThe Journal of Chemical Physics, 1984