Monte Carlo Study of the Formation and Conformational Properties of Dimers of Aβ42 Variants
Authors:
- Simon MitternachtSMSimon Mitternacht
- Iskra StanevaISIskra Staneva
- Torleif HärdTHTorleif Härd
- Anders IrbäckAIAnders Irbäck
- 1 July 2011
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 410 (2) , 357-367
Abstract
No abstract availableKeywords
Funding Information
- Vetenskapsrådet
This publication has 45 references indexed in Scilit:
- Atomic-Level Characterization of the Ensemble of the Aβ(1–42) Monomer in Water Using Unbiased Molecular Dynamics Simulations and Spectral AlgorithmsJournal of Molecular Biology, 2011
- Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrilsNature Structural & Molecular Biology, 2010
- Intrinsic Determinants of Neurotoxic Aggregate Formation by the Amyloid β PeptideBiophysical Journal, 2010
- Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid FibrilsBiochemistry, 2009
- Amyloid β-Protein: Experiment and Theory on the 21−30 FragmentThe Journal of Physical Chemistry B, 2009
- Influence of Preformed Asp23−Lys28 Salt Bridge on the Conformational Fluctuations of Monomers and Dimers of Aβ Peptides with Implications for Rates of Fibril FormationThe Journal of Physical Chemistry B, 2009
- Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memoryNature Medicine, 2008
- Structures and Free-Energy Landscapes of the Wild Type and Mutants of the Aβ21–30 Peptide Are Determined by an Interplay between Intrapeptide Electrostatic and Hydrophobic InteractionsJournal of Molecular Biology, 2008
- Structure and Dynamics of the Aβ21–30 Peptide from the Interplay of NMR Experiments and Molecular SimulationsJournal of the American Chemical Society, 2008
- The Alzheimer’s Peptides Aβ40 and 42 Adopt Distinct Conformations in Water: A Combined MD / NMR StudyJournal of Molecular Biology, 2007