ArticleDisease models & mechanisms2011
Development and validation of a yeast high-throughput screen for inhibitors of Aβ₄₂ oligomerization.
Article in Disease models & mechanisms, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- Scyllo-Inositol as a Neuroactive Agent: From Pharmacokinetics to Neuroprotective and Antiepileptic Effects.Nutrients · 2026Review
- Multiplex neurodegeneration proteotoxicity platform reveals DNAJB6 promotes non-toxic FUS condensate gelation and inhibits neurotoxicity.Nature communications · 2025Article
- A Twist in Yeast: New Perspectives for Studying TDP-43 Proteinopathies inJournal of fungi (Basel, Switzerland) · 2025Review
- Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023Review
- Article
- Neurodegenerative disease-associated inclusion bodies are cleared by selective autophagy in budding yeast.Autophagy reports · 2023Article
- The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity.EMBO molecular medicine · 2022Article
- Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets.iScience · 2021Article
- A rapid absorbance-based growth assay to screen the toxicity of oligomer AβNeural regeneration research · 2020Article
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Identifying Anti-prion Chemical Compounds Using a Newly Established Yeast High-Throughput Screening System.Cell chemical biology · 2019Article
- Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- Dihydropyrimidine-Thiones and Clioquinol Synergize To Target β-Amyloid Cellular Pathologies through a Metal-Dependent Mechanism.ACS chemical neuroscience · 2017Article
- Enabling stop codon read-through translation in bacteria as a probe for amyloid aggregation.Scientific reports · 2017Article
- Pathway swapping: Toward modular engineering of essential cellular processes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- An acridine derivative, [4,5-bis{(N-carboxy methyl imidazolium)methyl}acridine] dibromide, shows anti-TDP-43 aggregation effect in ALS disease models.Scientific reports · 2016Article
- Finding chemopreventatives to reduce amyloid beta in yeast.Neural regeneration research · 2016Article
- Inhibition of AβMicrobial cell (Graz, Austria) · 2016Article
- Screening strategies to identify HSP70 modulators to treat Alzheimer's disease.Drug design, development and therapy · 2015Review
- Genome-wide analysis of Saccharomyces cerevisiae identifies cellular processes affecting intracellular aggregation of Alzheimer's amyloid-β42: importance of lipid homeostasis.Molecular biology of the cell · 2014Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Recent reports point to small soluble oligomers, rather than insoluble fibrils, of amyloid β (Aβ), as the primary toxic species in Alzheimer's disease. Previously, we developed a low-throughput assay in yeast that is capable of detecting small Aβ(42) oligomer formation. Specifically, Aβ(42) fused to the functional release factor domain of yeast translational termination factor, Sup35p, formed sodium dodecyl sulfate (SDS)-stable low-n oligomers in living yeast, which impaired release factor activity. As a result, the assay for oligomer formation uses yeast growth to indicate restored release factor activity and presumably reduced oligomer formation. We now describe our translation of this assay into a high-throughput screen (HTS) for anti-oligomeric compounds. By doing so, we also identified two presumptive anti-oligomeric compounds from a sub-library of 12,800 drug-like small molecules. Subsequent biochemical analysis confirmed their anti-oligomeric activity, suggesting that this form of HTS is an efficient, sensitive and cost-effective approach to identify new inhibitors of Aβ(42) oligomerization.
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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.