ArticleProteins2009
Interpeptide interactions induce helix to strand structural transition in Abeta peptides.
Article in Proteins, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 55 citations in OpenAlex.
- Survey of the Aβ-peptide structural diversity: molecular dynamics approaches.Biophysical reviews · 2024Review
- Helix-to-sheet transition of the Aβ42 peptide revealed using an enhanced sampling strategy and Markov state model.Computational and structural biotechnology journal · 2024Article
- Article
- Initial Structural Models of the Aβ42 Dimer from Replica Exchange Molecular Dynamics Simulations.ACS omega · 2017Article
- Conformational distribution and α-helix to β-sheet transition of human amylin fragment dimer.Biomacromolecules · 2014Article
- Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation.Journal of Alzheimer's disease : JAD · 2014Article
- Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Journal of molecular biology · 2013Article
- Molecular mechanism of misfolding and aggregation of Aβ(13-23).The journal of physical chemistry. B · 2013Article
- Binding to the lipid monolayer induces conformational transition in Aβ monomer.Journal of molecular modeling · 2013Article
- Molecular interactions of Alzheimer's biomarker FDDNP with Aβ peptide.Biophysical journal · 2012Article
- Article
- Modeling amyloid-beta as homogeneous dodecamers and in complex with cellular prion protein.PloS one · 2012Article
- Does amino acid sequence determine the properties of Aβ dimer?The Journal of chemical physics · 2011Article
- Naproxen interferes with the assembly of Aβ oligomers implicated in Alzheimer's disease.Biophysical journal · 2011Article
- Nonsteroidal anti-inflammatory drug naproxen destabilizes Aβ amyloid fibrils: a molecular dynamics investigation.The journal of physical chemistry. B · 2010Article
- Article
- Mapping conformational ensembles of aβ oligomers in molecular dynamics simulations.Biophysical journal · 2010Article
- A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.Proteins · 2010Article
- Globular state in the oligomers formed by Abeta peptides.The Journal of chemical physics · 2010Article
- Molecular dynamics simulations of anti-aggregation effect of ibuprofen.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Replica exchange molecular dynamics and all-atom implicit solvent model are used to compute the structural propensities in Abeta monomers, dimers, and Abeta peptides bound to the edge of amyloid fibril. These systems represent, on an approximate level, different stages in Abeta aggregation. Abeta monomers are shown to form helical structure in the N-terminal (residues 13 to 21). Interpeptide interactions in Abeta dimers and, especially, in the peptides bound to the fibril induce a dramatic shift in the secondary structure, from helical states toward beta-strand conformations. The sequence region 10-23 in Abeta peptide is found to form most of interpeptide interactions upon aggregation. Simulation results are tested by comparing the chemical shifts in Abeta monomers computed from simulations and obtained experimentally. Possible implications of our simulations for designing aggregation-resistant variants of Abeta are discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.