ArticlePrion
DNA aptamers detecting generic amyloid epitopes.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Selection of an Aptamer against the Enzyme 1-deoxy-D-xylulose-5-phosphate Reductoisomerase fromPharmaceutics · 2022Article
- Structure-specific amyloid precipitation in biofluids.Nature chemistry · 2022Article
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Aptamers Selected for Recognizing Amyloid β-Protein-A Case for Cautious Optimism.International journal of molecular sciences · 2018Review
- Article
- A protein polymerization cascade mediates toxicity of non-pathological human huntingtin in yeast.Scientific reports · 2015Article
- Proteomic screening for amyloid proteins.PloS one · 2014Article
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloids are fibrillar protein aggregates resulting from non-covalent autocatalytic polymerization of various structurally and functionally unrelated proteins. Previously we have selected DNA aptamers, which bind specifically to the in vitro assembled amyloid fibrils of the yeast prionogenic protein Sup35. Here we show that such DNA aptamers can be used to detect SDS-insoluble amyloid aggregates of the Sup35 protein, and of some other amyloidogenic proteins, including mouse PrP, formed in yeast cells. The obtained data suggest that these aggregates and the Sup35 amyloid fibrils assembled in vitro possess common conformational epitopes recognizable by aptamers. The described DNA aptamers may be used for detection of various amyloid aggregates in yeast and, presumably, other organisms.
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