ArticleBiotechnology and bioengineering2010
Can size alone explain some of the differences in toxicity between beta-amyloid oligomers and fibrils?
Article in Biotechnology and bioengineering, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 15 citations in OpenAlex.
- Decreasing amyloid toxicity through an increased rate of aggregation.Physical chemistry chemical physics : PCCP · 2017Article
- Suppressing mutation-induced protein aggregation in mammalian cells by mutating residues significantly displaced upon the original mutation.Biochemical engineering journal · 2014Article
- Cis-suppression to arrest protein aggregation in mammalian cells.Biotechnology and bioengineering · 2014Article
- A revisited folding reporter for quantitative assay of protein misfolding and aggregation in mammalian cells.Biotechnology journal · 2012Article
- Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity.The Journal of biological chemistry · 2012Article
- Review
- Soluble Aβ seeds are potent inducers of cerebral β-amyloid deposition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
beta-Amyloid (Abeta) peptide is believed to play a key role in the mechanism of Alzheimer's disease (AD). Abeta tends to aggregate to form amyloid fibrils. A variety of evidence indicates that Abeta aggregates are toxic in vitro and in vivo. An early "Abeta hypothesis" postulated that AD was the consequence of neuron death induced by insoluble deposits of large Abeta fibrils. Newer findings indicate that small soluble Abeta oligomers are the neurotoxic species, yet their structure is still unknown. Many researchers have tried to probe the differences in molecular structure between Abeta oligomers, protofibrils, and fibrils that give rise to their unique toxicities, but with limited success. In this report, we examine the hypothesis that differences in the toxicity of different aggregated Abeta species are the result of differences in species concentration and diffusivity. Using a simple mathematical analysis based on the assumption of a diffusion-limited reaction, we demonstrate that near 10-fold differences in toxicity between spherical oligomers and fibrils can be explained from size and concentration arguments. While this work does not suggest that Abeta oligomers and fibrils have identical molecular structures, it highlights the possibility that simple physical phenomena may contribute to the biological processes induced by Abeta.
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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.