ReviewSwiss medical weekly2014
Toxic oligomer species of amyloid-β in Alzheimer's disease, a timing issue.
Review in Swiss medical weekly, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Review
- Aggregation of Disordered Proteins Associated with Neurodegeneration.International journal of molecular sciences · 2023Review
- Aβ and Tau Prions Causing Alzheimer's Disease.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity.EMBO molecular medicine · 2022Article
- Degradation of FA reduces Aβ neurotoxicity and Alzheimer-related phenotypes.Molecular psychiatry · 2021Article
- Detection of retinal and blood Aβ oligomers with nanobodies.Alzheimer's & dementia (Amsterdam, Netherlands) · 2021Article
- Aβ and tau prion-like activities decline with longevity in the Alzheimer's disease human brain.Science translational medicine · 2019Article
- The Precursor to Glutathione (GSH), γ-Glutamylcysteine (GGC), Can Ameliorate Oxidative Damage and Neuroinflammation Induced by AβFrontiers in aging neuroscience · 2019Article
- Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases.Nature neuroscience · 2018Review
- Discrete Pools of Oligomeric Amyloid-β Track with Spatial Learning Deficits in a Mouse Model of Alzheimer Amyloidosis.The American journal of pathology · 2018Article
- A standard model of Alzheimer's disease?Prion · 2018Article
- Shear-Induced Amyloid Formation in the Brain: III. The Roles of Shear Energy and Seeding in a Proposed Shear Model.Journal of Alzheimer's disease : JAD · 2018Article
- Advantages of Structure-Based Drug Design Approaches in Neurological Disorders.Current neuropharmacology · 2017Review
- Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution.Scientific reports · 2017Article
- The amyloid-β oligomer Aβ*56 induces specific alterations in neuronal signaling that lead to tau phosphorylation and aggregation.Science signaling · 2017Article
- What amyloid ligands can tell us about molecular polymorphism and disease.Neurobiology of aging · 2016Review
- The oxysterol 27-hydroxycholesterol increases oxidative stress and regulate Nrf2 signaling pathway in astrocyte cells.Neurochemical research · 2015Article
Corrections and comments
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Abstract
A decade following the paradigm-shifting concept that endogenous forms of soluble, non-fibrillar amyloid-β (Aβ) might constitute the major bioactive entity causing synaptic loss and cognitive decline in Alzheimer's disease (AD), our understanding of these oligomeric species still remains conspicuously superficial. The current lack of direct evaluation tools for each endogenous Aβ oligomer hampers our ability to readily address crucial question such as: (i) where they form and accumulate?; (ii) when they first appear in human brains and body fluids?; (iii) what is the longitudinal expression of these putative toxins during the course of the disease?; (iv) and how do these soluble Aβ assemblies alter synaptic and neuronal function in the brain? Despite these limitations, indirect ex vivo measurement and isolation from biological specimens has been possible and have allowed parsing out intrinsic differences between putative endogenous Aβ oligomers. In this review, I integrated recent findings and extrapolated emerging hypotheses derived from these studies with the hope to provide a clarified view on the putative role of endogenous Aβ oligomers in AD, with a particular emphasis on the timing at which these soluble species might act in the aging and diseased brain.
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Registered trials
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