The Binding of Thioflavin T and Its Neutral Analog BTA-1 to Protofibrils of the Alzheimer’s Disease Aβ16–22 Peptide Probed by Molecular Dynamics Simulations
- 7 October 2008
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 384 (3), 718-729
- https://doi.org/10.1016/j.jmb.2008.09.062
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Temperature-Induced Dissociation of Aβ Monomers from Amyloid FibrilBiophysical Journal, 2008
- New Insights into the Mechanism of Alzheimer Amyloid-β Fibrillogenesis Inhibition by N-Methylated PeptidesBiophysical Journal, 2007
- Monomer adds to preformed structured oligomers of Aβ-peptides by a two-stage dock–lock mechanismProceedings of the National Academy of Sciences, 2007
- Phenol Red Interacts with the Protofibril-Like Oligomers of an Amyloidogenic Hexapeptide NFGAIL through Both Hydrophobic and Aromatic ContactsBiophysical Journal, 2006
- Stability and Structure of Oligomers of the Alzheimer Peptide Aβ16–22: From the Dimer to the 32-MerBiophysical Journal, 2006
- Development and testing of a general amber force fieldJournal of Computational Chemistry, 2004
- A point‐charge force field for molecular mechanics simulations of proteins based on condensed‐phase quantum mechanical calculationsJournal of Computational Chemistry, 2003
- A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP modelThe Journal of Physical Chemistry, 1993
- Molecular dynamics with coupling to an external bathThe Journal of Chemical Physics, 1984
- Comparison of simple potential functions for simulating liquid waterThe Journal of Chemical Physics, 1983