ArticleBiophysical chemistry2009
A model of amyloid's role in disease based on fibril fracture.
Article in Biophysical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 30 citations in OpenAlex.
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- A simple method for modeling amyloid kinetics featuring position biased fiber breakage.Biophysics and physicobiology · 2020Article
- Ionic liquids and protein folding-old tricks for new solvents.Biophysical reviews · 2019Review
- Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation.The Journal of biological chemistry · 2017Article
- Overview of the "Ionic Liquids meet Biomolecules" session at the 19th international IUPAB and 11th EBSA congress.Biophysical reviews · 2017Article
- Measurement of amyloid formation by turbidity assay-seeing through the cloud.Biophysical reviews · 2016Review
- A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation.FEBS letters · 2015Article
- An equilibrium model for the combined effect of macromolecular crowding and surface adsorption on the formation of linear protein fibrils.Biophysical journal · 2015Article
- Computational modeling of the relationship between amyloid and disease.Biophysical reviews · 2012Article
- An equilibrium model for linear and closed-loop amyloid fibril formation.Journal of molecular biology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Although the correlative evidence relating the presence of amyloid fibrils and certain disease states (e.g. Alzheimer's disease and Type 2 Diabetes) is overwhelming, a direct causative role for amyloid has proved harder to establish. Current thinking links a narrow region of the aggregate protein size distribution, the so called 'early aggregate' domain to cellular toxicity. A troubling feature of this theory however is that the nucleated reaction mechanism by which amyloid formation is believed to occur results in a very low number concentration of early aggregates which are rapidly extended to form amyloid fibrils. This situation means that the concentration of early aggregates is very low at the time when they are supposedly at their most toxic. Here we adopt a novel explicit simulation strategy to examine a kinetic regime involving nucleated growth combined with fibril fragmentation under which this situation can be reversed so as to produce a high number concentration of small on-pathway toxic aggregates. Dependent upon the rate of fragmentation, the time scale for generation of toxic early aggregates may be coupled, uncoupled or disassociated from the time scale for the appearance of amyloid fibrils. Furthermore the model presents itself as a biochemical 'switch' transitioning between modes of amyloid induced cell death dependent upon either specific amyloid toxicity or non-specific solid mass induced tissue damage.
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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.