The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy
By Urmi Sengupta, A. Nilson, R. Kayed. EBioMedicine, 2016
668 citations recorded by the source corpus.
The incidence of Alzheimer's disease (AD) is growing every day and finding an effective treatment is becoming more vital. Amyloid-β (Aβ) has been the focus of research for several decades. The recent shift in the Aβ cascade hypothesis from all Aβ to small soluble oligomeric intermediates is directing the search for therapeutics towards the toxic mediators of the disease. Targeting the most toxic oligomers may prove to be an effective treatment by preventing their spread. Specific targeting of oligomers has been shown to protect cognition in rodent models. Additionally, the heterogeneity of research on Aβ oligomers may seem contradictory until size and conformation are taken into account. In this review, we will discuss Aβ oligomers and their toxicity in relation to size and conformation as well as their influence on inflammation and the potential of Aβ oligomer immunotherapy.
Subfields: Oncology, Pharmacology, Physiology
View Paper: https://www.semanticscholar.org/paper/a3cfcfee6bbed47bf2381e64a9d854116413e77f
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In Physiology
Citations in the corpus
- Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “Although Aβ monomers at physiological concentrations are generally considered to be nontoxic, multiple lines of evidence suggest that Aβ oligomers rather than Aβ fibrils are neurotoxic [54].”