ArticleThe Journal of biological chemistry2019
Structural progression of amyloid-β Arctic mutant aggregation in cells revealed by multiparametric imaging.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- Polyphenol diet and exercise as neuroprotective factors in a Drosophila model of Alzheimer's disease.Animal models and experimental medicine · 2026Article
- Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Targeting neurodegenerative disease-associated protein aggregation with proximity-inducing modalities.Acta pharmacologica Sinica · 2025Review
- Conditioned Generative Modeling of Molecular Glues: A Realistic AI Approach for Synthesizable Drug-like Molecules.Biomolecules · 2025Article
- iPAR: a new reporter for eukaryotic cytoplasmic protein aggregation.BMC methods · 2025Article
- Advancements and Practical Considerations for Biophysical Research: Navigating the Challenges and Future of Super-resolution Microscopy.Chemical & biomedical imaging · 2024Review
- Associations of amyloid-β oligomers and plaques with neuropathology in theBrain communications · 2024Article
- ERnet: a tool for the semantic segmentation and quantitative analysis of endoplasmic reticulum topology.Nature methods · 2023Article
- Fluorescent Nanoparticles for Super-Resolution Imaging.Chemical reviews · 2022Review
- Article
- Mechanistic Insights into Selective Autophagy Subtypes in Alzheimer's Disease.International journal of molecular sciences · 2022Review
- Super-resolution microscopy: a closer look at synaptic dysfunction in Alzheimer disease.Nature reviews. Neuroscience · 2021Review
- High spatial-resolution imaging of label-freeThe Analyst · 2021Article
- Luminescence lifetime imaging of three-dimensional biological objects.Journal of cell science · 2021Article
- Fast Purification of Recombinant Monomeric Amyloid-β fromACS chemical neuroscience · 2020Article
- Impact of Mutations on the Conformational Transition from α-Helix to β-Sheet Structures in Arctic-Type AβACS omega · 2020Article
- Intramitochondrial proteostasis is directly coupled to α-synuclein and amyloid β1-42 pathologies.The Journal of biological chemistry · 2020Article
- Three-dimensional real time imaging of amyloid β aggregation on living cells.Scientific reports · 2020Article
- Review
- Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging ineLife · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
Abstract
The 42-amino-acid β-amyloid (Aβ42) is a critical causative agent in the pathology of Alzheimer's disease. The hereditary Arctic mutation of Aβ42 (E22G) leads to increased intracellular accumulation of β-amyloid in early-onset Alzheimer's disease. However, it remains largely unknown how the Arctic mutant variant leads to aggressive protein aggregation and increased intracellular toxicity. Here, we constructed stable cell lines expressing fluorescent-tagged wildtype (WT) and E22G Aβ42 to study the aggregation kinetics of the Arctic Aβ42 mutant peptide and its heterogeneous structural forms. Arctic-mutant peptides assemble and form fibrils at a much faster rate than WT peptides. We identified five categories of intracellular aggregate-oligomers, single fibrils, fibril bundles, clusters, and aggresomes-that underline the heterogeneity of these Aβ42 aggregates and represent the progression of Aβ42 aggregation within the cell. Fluorescence-lifetime imaging (FLIM) and 3D structural illumination microscopy (SIM) showed that all aggregate species displayed highly compact structures with strong affinity between individual fibrils. We also found that aggregates formed by Arctic mutant Aβ42 were more resistant to intracellular degradation than their WT counterparts. Our findings uncover the structural basis of the progression of Arctic mutant Aβ42 aggregation in the cell.
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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.