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Low‐n oligomers as therapeutic targets of Alzheimer’s disease
Abstract
J. Neurochem. (2011) 117, 19–28. The pathogenesis of Alzheimer’s disease involves the progressive accumulation of amyloid β‐protein (Aβ). Recent studies using synthetic Aβ peptides, a cell culture model, Aβ precursor protein transgenic mice models suggest that pre‐fibrillar forms of Aβ are more deleterious than extracellular fibril forms. Recent findings obtained using synthetic Aβ peptides and human samples indicated that low‐n oligomers (from dimers to octamers) may be proximate toxins for neuron and synapse. Here, we review the recent studies on the soluble oligomers, especially low‐n oligomers in Alzheimer’s disease.
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Current therapeutic interventions intended to reduce amyloid-β plaques may clear amyloid fibrils and largely inert plaques but may only partially address the specific neurotoxic effects of amyloid-β oligomers.
“A potential weakness of current therapeutic interventions intended to reduce amyloid-β plaques in the brain is that although these approaches may clear amyloid fibrils and the largely inert plaques, they may only partially address the specific neurotoxic effects of amyloid-β oligomers [30]”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [30]
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Alzheimer’s disease as oligomeropathy
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Metadata
- Authors
- Ono, K., & Yamada, M.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2011-02-09
- Volume
- 117
- Issue
- 1
- Pages
- 19-28
- ISSN
- 0022-3042
- 1471-4159
- Cited by
- 76
- References
- 23
- Language
- en
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