Effects of Familial Alzheimer’s Disease Mutations on the Folding Nucleation of the Amyloid β-Protein
- 4 June 2008
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 381 (1) , 221-228
- https://doi.org/10.1016/j.jmb.2008.05.069
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15–28 fragment of the Alzheimer amyloid-β proteinProceedings of the National Academy of Sciences, 2008
- Structure and Dynamics of the Aβ21–30 Peptide from the Interplay of NMR Experiments and Molecular SimulationsJournal of the American Chemical Society, 2008
- Familial Alzheimer's disease mutations alter the stability of the amyloid β-protein monomer folding nucleusProceedings of the National Academy of Sciences, 2007
- The Alzheimer’s Peptides Aβ40 and 42 Adopt Distinct Conformations in Water: A Combined MD / NMR StudyPublished by Elsevier ,2007
- A consensus view of protein dynamicsProceedings of the National Academy of Sciences, 2007
- Comparison of multiple Amber force fields and development of improved protein backbone parametersProteins-Structure Function and Bioinformatics, 2006
- 3D structure of Alzheimer's amyloid-β(1–42) fibrilsProceedings of the National Academy of Sciences, 2005
- Replica-exchange molecular dynamics method for protein foldingChemical Physics Letters, 1999
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Comparison of simple potential functions for simulating liquid waterThe Journal of Chemical Physics, 1983