ArticleThe Journal of chemical physics2018
Kinetics and mechanical stability of the fibril state control fibril formation time of polypeptide chains: A computational study.
Article in The Journal of chemical physics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
10 citing papers in PubMed.
- Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Epitope alteration by small molecules and applications in drug discovery.Chemical science · 2022Article
- Computational Models for the Study of Protein Aggregation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Assessing the Stability of Biological Fibrils by Molecular-Scale Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Nanomechanical Stability of Aβ Tetramers and Fibril-like Structures: Molecular Dynamics Simulations.The journal of physical chemistry. B · 2021Article
- d-Retro Inverso Amylin and the Stability of Amylin Fibrils.Journal of chemical theory and computation · 2020Article
- Pharmacophoric Site Identification and Inhibitor Design for Autotaxin.Molecules (Basel, Switzerland) · 2019Article
- Mechanical and thermodynamic properties of AβBeilstein journal of nanotechnology · 2019Article
- The Role of Structural Polymorphism in Driving the Mechanical Performance of the Alzheimer's Beta Amyloid Fibrils.Frontiers in bioengineering and biotechnology · 2019Article
- Role of Resultant Dipole Moment in Mechanical Dissociation of Biological Complexes.Molecules (Basel, Switzerland) · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Fibril formation resulting from protein misfolding and aggregation is a hallmark of several neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Despite much progress in the understanding of the protein aggregation process, the factors governing fibril formation rates and fibril stability have not been fully understood. Using lattice models, we have shown that the fibril formation time is controlled by the kinetic stability of the fibril state but not by its energy. Having performed all-atom explicit solvent molecular dynamics simulations with the GROMOS43a1 force field for full-length amyloid beta peptides Aβ
Indexed as
Identifiers
What OpenQuestion holds
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.