ArticleACS chemical neuroscience2012
Facile methodology for monitoring amyloid-β fibrillization.
Article in ACS chemical neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- Secondary Structure in Amyloids in Relation to Their Wild Type Forms.International journal of molecular sciences · 2022Article
- Effect of DNA Origami Nanostructures on hIAPP Aggregation.Nanomaterials (Basel, Switzerland) · 2020Article
- Amyloidosis and Longevity: A Lesson from Plants.Biology · 2019Article
- Modification of Aβ Peptide Aggregation via Covalent Binding of a Series of Ru(III) Complexes.Frontiers in chemistry · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid-β (Aβ) is a peptide fragment that is prone to aggregate into large fibrils under physiological conditions. Many techniques have been developed to quickly monitor the transition from a primarily monomeric peptide into fibrils. Here we propose a novel method for both incubating and monitoring changes in Aβ aggregation by using modified NMR tubes, a microtube thermoshaker, and a fluorescence or UV-vis spectrometer. These NMR tubes are thin and cylindrical, which allows efficient heat transfer and orbital shaking. Our results demonstrate that our technique is both reliable and expedient when tracking Aβ fibrillization using fluorescence or turbidity assays, which presents an alternative for laboratories without specialized equipment for incubating peptide.
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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.