ArticleBiophysical journal2013
Simple moment-closure model for the self-assembly of breakable amyloid filaments.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed.
- Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide.Nano letters · 2019Article
- Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.ACS chemical neuroscience · 2018Article
- Protein Polymerization into Fibrils from the Viewpoint of Nucleation Theory.Biophysical journal · 2015Article
- A Kinetic Model for Cell Damage Caused by Oligomer Formation.Biophysical journal · 2015Article
- Statistical mechanical treatments of protein amyloid formation.International journal of molecular sciences · 2013Review
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this work, we derive a simple mathematical model from mass-action equations for amyloid fiber formation that takes into account the primary nucleation, elongation, and length-dependent fragmentation. The derivation is based on the principle of minimum free energy under certain constraints and is mathematically related to the partial equilibrium approximation. Direct numerical comparisons confirm the usefulness of our simple model. We further explore its basic kinetic and equilibrium properties, and show that the current model is a straightforward generalization of that with constant fragmentation rates.
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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.