ArticleScientific reports2016
Development of new fusion proteins for visualizing amyloid-β oligomers in vivo.
Article in Scientific reports, 2016. 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, 45 citations in OpenAlex.
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- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- Structural Mapping of Protein Aggregates in Live Cells Modeling Huntington's Disease.Angewandte Chemie (International ed. in English) · 2024Article
- Microscopic clusters feature the composition of biochemical tetraspanin-assemblies and constitute building-blocks of tetraspanin enriched domains.Scientific reports · 2024Article
- Lectin-anticancer peptide fusion demonstrates a significant cancer-cell-selective cytotoxic effect and inspires the production of "clickable" anticancer peptide in Escherichia coli.Protein science : a publication of the Protein Society · 2023Article
- Aggregation Limiting Cell-Penetrating Peptides Derived from Protein Signal Sequences.International journal of molecular sciences · 2023Article
- Aβ and Tau Prions Causing Alzheimer's Disease.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Intron-encoded cistronic transcripts for minimally invasive monitoring of coding and non-coding RNAs.Nature cell biology · 2022Article
- The transmembrane domain of the amyloid precursor protein is required for antiamyloidogenic processing by α-secretase ADAM10.The Journal of biological chemistry · 2022Article
- Natural Bioactive Products and Alzheimer's Disease Pathology: Lessons fromDiseases (Basel, Switzerland) · 2022Review
- Modeling Alzheimer's Disease inBiomedicines · 2022Review
- Non-monotonic fibril surface occlusion by GFP tags from coarse-grained molecular simulations.Computational and structural biotechnology journal · 2022Article
- The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE-SNARE interactions.eLife · 2021Article
- Global Proteotoxicity Caused by Human βInternational journal of molecular sciences · 2021Article
- FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments.Molecular neurodegeneration · 2020Article
- Apolipoprotein E-mediated regulation of selenoprotein P transportation via exosomes.Cellular and molecular life sciences : CMLS · 2020Article
- Unique phase behavior in cell size space: synergistic effect of molecular crowding and confinement.Biophysical reviews · 2020Article
- New Alzheimer's disease model mouse specialized for analyzing the function and toxicity of intraneuronal Amyloid β oligomers.Scientific reports · 2019Article
- Aβ and tau prion-like activities decline with longevity in the Alzheimer's disease human brain.Science translational medicine · 2019Article
- State-of-the-Art Fluorescence Fluctuation-Based Spectroscopic Techniques for the Study of Protein Aggregation.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intracellular accumulation of amyloid-β (Aβ) oligomers critically contributes to disease progression in Alzheimer's disease (AD) and can be the potential target of AD therapy. Direct observation of molecular dynamics of Aβ oligomers in vivo is key for drug discovery research, however, it has been challenging because Aβ aggregation inhibits the fluorescence from fusion proteins. Here, we developed Aβ1-42-GFP fusion proteins that are oligomerized and visualize their dynamics inside cells even when aggregated. We examined the aggregation states of Aβ-GFP fusion proteins using several methods and confirmed that they did not assemble into fibrils, but instead formed oligomers in vitro and in live cells. By arranging the length of the liker between Aβ and GFP, we generated two fusion proteins with "a long-linker" and "a short-linker", and revealed that the aggregation property of fusion proteins can be evaluated by measuring fluorescence intensities using rat primary culture neurons transfected with Aβ-GFP plasmids and Aβ-GFP transgenic C. elegans. We found that Aβ-GFP fusion proteins induced cell death in COS7 cells. These results suggested that novel Aβ-GFP fusion proteins could be utilized for studying the physiological functions of Aβ oligomers in living cells and animals, and for drug screening by analyzing Aβ toxicity.
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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.