ArticleThe Journal of chemical physics2008
The Alzheimer's beta amyloid (Abeta1-39) monomer in an implicit solvent.
Article in The Journal of chemical physics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- How accurate are your simulations? Effects of confined aqueous volume and AMBER FF99SB and CHARMM22/CMAP force field parameters on structural ensembles of intrinsically disordered proteins: Amyloid-βIntrinsically disordered proteins · 2017Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation.Journal of Alzheimer's disease : JAD · 2014Article
- Dynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein.The journal of physical chemistry. B · 2012Article
- Replica exchange molecular dynamics of the thermodynamics of fibril growth of Alzheimer's Aβ42 peptide.The Journal of chemical physics · 2011Article
- Internal and environmental effects on folding and dimerization of the Alzheimer's β amyloid peptide.Molecular simulation · 2011Article
- Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.Journal of molecular biology · 2010Article
- A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.Proteins · 2010Article
- The Alzheimer beta-amyloid (Abeta(1-39)) dimer in an implicit solvent.The Journal of chemical physics · 2008Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Results from replica-exchange and regular room temperature molecular dynamics simulations of the Alzheimer's beta amyloid (Abeta(1-39)) monomer in an implicit solvent are reported. Our data indicate that at room temperature, the monomer assumes random-coil and soluble conformations. No beta content is observed which therefore seems to be a product of oligomerization and aggregation of monomers.
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Registered trials
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