ReviewFrontiers in molecular biosciences2025
Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease.
Review in Frontiers in molecular biosciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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Abstract
Alzheimer's disease is recognized as the most common neurodegenerative disorder, characterized by the presence of amyloid plaques, which have consistently garnered significant attention. Since the disease was first identified, extensive research has been devoted to investigating these plaques. As our understanding of the disease has progressed, the detrimental role of plaques has been questioned, leading to the hypothesis that amyloid oligomeric aggregates are the main culprits. Nevertheless, subsequent research indicated that the concentrations of amyloids employed in the experiments were considerably elevated compared to physiological conditions, and that at physiological concentrations, amyloids do not exhibit significant accumulation or toxicity. This article aims to offer a detailed biophysical perspective on the formation of amyloid aggregates under physiological conditions and their impact on membranes, providing valuable insights for researchers in this field.
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