ArticleMicrobial cell factories2012
Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors.
Article in Microbial cell factories, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- Eukaryotic Aggresomes: Protocols and Tips for Their Production, Purification , and Handling.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Coiled-Coil Based Inclusion Bodies and Their Potential Applications.Frontiers in bioengineering and biotechnology · 2021Review
- Coiled-coil inspired functional inclusion bodies.Microbial cell factories · 2020Article
- Editorial: Protein Aggregation and Solubility in Microorganisms (Archaea, Bacteria and Unicellular Eukaryotes): Implications and Applications.Frontiers in microbiology · 2020Article
- Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases.Molecular neurobiology · 2018Review
- A Robust and Efficient Production and Purification Procedure of Recombinant Alzheimers Disease Methionine-Modified Amyloid-β Peptides.PloS one · 2016Article
- Editorial: Protein Solubility and Aggregation in Bacteria.Frontiers in microbiology · 2016Article
- When amyloids become prions.Prion · 2014Article
- Inclusion bodies: not that bad….Frontiers in microbiology · 2014Review
- Screening and identification of genetic loci involved in producing more/denser inclusion bodies in Escherichia coli.Microbial cell factories · 2013Article
- Why and how protein aggregation has to be studied in vivo.Microbial cell factories · 2013Article
- Modeling amyloids in bacteria.Microbial cell factories · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe amyloid-β peptide (Aβ42) is the main component of the inter-neuronal amyloid plaques characteristic of Alzheimer's disease (AD). The mechanism by which Aβ42 and other amyloid peptides assemble into insoluble neurotoxic deposits is still not completely understood and multiple factors have been reported to trigger their formation. In particular, the presence of endogenous metal ions has been linked to the pathogenesis of AD and other neurodegenerative disorders.
resultsHere we describe a rapid and high-throughput screening method to identify molecules able to modulate amyloid aggregation. The approach exploits the inclusion bodies (IBs) formed by Aβ42 when expressed in bacteria. We have shown previously that these aggregates retain amyloid structural and functional properties. In the present work, we demonstrate that their in vitro refolding is selectively sensitive to the presence of aggregation-promoting metal ions, allowing the detection of inhibitors of metal-promoted amyloid aggregation with potential therapeutic interest.
conclusionsBecause IBs can be produced at high levels and easily purified, the method overcomes one of the main limitations in screens to detect amyloid modulators: the use of expensive and usually highly insoluble synthetic peptides.
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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.