ArticlePloS one2012
Structure and dynamics of amyloid-β segmental polymorphisms.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 79 citations in OpenAlex.
- Can local heating and molecular crowders disintegrate amyloid aggregates?Chemical science · 2024Article
- Partial Destabilization of Amyloid-β Protofibril by Methionine Photo-Oxidation: A Molecular Dynamic Simulation Study.ACS omega · 2023Article
- Article
- Structural Requirement of hA5G18 Peptide (DDFVFYVGGYPS) from Laminin α5 Chain for Amyloid-like Fibril Formation and Cell Adhesion.Molecules (Basel, Switzerland) · 2022Article
- Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders.Antioxidants (Basel, Switzerland) · 2021Review
- The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Kinetics and mechanical stability of the fibril state control fibril formation time of polypeptide chains: A computational study.The Journal of chemical physics · 2018Article
- Tailoring Hydrophobic Interactions between Probes and Amyloid-β Peptides for Fluorescent Monitoring of Amyloid-β Aggregation.ACS omega · 2018Article
- Computational Insight into the Effect of Natural Compounds on the Destabilization of Preformed Amyloid-β(1⁻40) Fibrils.Molecules (Basel, Switzerland) · 2018Article
- Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid β Assemblies.International journal of molecular sciences · 2018Article
- A High Affinity Red Fluorescence and Colorimetric Probe for Amyloid β Aggregates.Scientific reports · 2016Article
- On the lack of polymorphism in Aβ-peptide aggregates derived from patient brains.Protein science : a publication of the Protein Society · 2015Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.The Journal of biological chemistry · 2015Article
- Nucleation of polymorphic amyloid fibrils.Biophysical journal · 2015Article
- Stability of Iowa mutant and wild type Aβ-peptide aggregates.The Journal of chemical physics · 2014Article
- Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42.ACS chemical neuroscience · 2014Article
- The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length.ACS chemical neuroscience · 2014Article
- Mutations and seeding of amylin fibril-like oligomers.The journal of physical chemistry. B · 2013Article
- In silico cross seeding of Aβ and amylin fibril-like oligomers.ACS chemical neuroscience · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
It is believed that amyloid-beta (Aβ) aggregates play a role in the pathogenesis of Alzheimer's disease. Aβ molecules form β-sheet structures with multiple interaction sites. This polymorphism gives rise to differences in morphology, physico-chemical property and level of cellular toxicity. We have investigated the conformational stability of various segmental polymorphisms using molecular dynamics simulations and find that the segmental polymorphic models of Aβ retain a U-shaped architecture. Our results demonstrate the importance of inter-sheet side chain-side chain contacts, hydrophobic contacts among the strands (β1 and β2) and of salt bridges in stabilizing the aggregates. Residues in β-sheet regions have smaller fluctuation while those at the edge and loop region are more mobile. The inter-peptide salt bridges between Asp23 and Lys28 are strong compared to intra-chain salt bridge and there is an exchange of the inter-chain salt-bridge with intra-chain salt bridge. As our results suggest that Aβ exists under physiological conditions as an ensemble of distinct segmental polymorphs, it may be necessary to account in the development of therapeutics for Alzheimer's disease the differences in structural stability and aggregation behavior of the various Aβ polymorphic forms.
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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.