ArticleGenes & development2012
Generating extracellular amyloid aggregates using E. coli cells.
Article in Genes & development, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
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.
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Who cites it
29 citing papers in PubMed, 56 citations in OpenAlex.
- Gut microbiota produces biofilm-associated amyloids with potential for neurodegeneration.Nature communications · 2024Article
- OmpC and OmpF Outer Membrane Proteins ofInternational journal of molecular sciences · 2023Article
- Cell specialization in cyanobacterial biofilm development revealed by expression of a cell-surface and extracellular matrix protein.NPJ biofilms and microbiomes · 2023Article
- Engineering living materials by synthetic biology.Biophysics reviews · 2023Review
- Human RAD51 Protein Forms Amyloid-like AggregatesInternational journal of molecular sciences · 2022Article
- High-Throughput Screening of Heterologous Functional Amyloids Using Escherichia coli.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Functional Mammalian Amyloids and Amyloid-Like Proteins.Life (Basel, Switzerland) · 2020Review
- NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA.Scientific reports · 2020Article
- RNA-binding protein FXR1 is presented in rat brain in amyloid form.Scientific reports · 2019Article
- Two Novel Amyloid Proteins, RopA and RopB, from the Root Nodule BacteriumBiomolecules · 2019Article
- Article
- Developing Gram-negative bacteria for the secretion of heterologous proteins.Microbial cell factories · 2018Review
- Glycosylated amyloid-like proteins in the structural extracellular polymers of aerobic granular sludge enriched with ammonium-oxidizing bacteria.MicrobiologyOpen · 2018Article
- Screening for amyloid proteins in the yeast proteome.Current genetics · 2018Article
- M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils.PloS one · 2018Article
- A novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli.Scientific reports · 2017Article
- Functional amyloids in Streptococcus mutans, their use as targets of biofilm inhibition and initial characterization of SMU_63c.Microbiology (Reading, England) · 2017Article
- A bacterial global regulator forms a prion.Science (New York, N.Y.) · 2017Article
- Outlining Core Pathways of Amyloid Toxicity in Bacteria with the RepA-WH1 Prionoid.Frontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Diverse proteins are known to be capable of forming amyloid aggregates, self-seeding fibrillar assemblies that may be biologically functional or pathological. Well-known examples include neurodegenerative disease-associated proteins that misfold as amyloid, fungal prion proteins that can transition to a self-propagating amyloid form and certain bacterial proteins that fold as amyloid at the cell surface and promote biofilm formation. To further explore the diversity of amyloidogenic proteins, generally applicable methods for identifying them are critical. Here we describe a cell-based method for generating amyloid aggregates that relies on the natural ability of Escherichia coli cells to elaborate amyloid fibrils at the cell surface. We use several different yeast prion proteins and the human huntingtin protein to show that protein secretion via this specialized export pathway promotes acquisition of the amyloid fold specifically for proteins that have an inherent amyloid-forming propensity. Furthermore, our findings establish the potential of this E. coli-based system to facilitate the implementation of high-throughput screens for identifying amyloidogenic proteins and modulators of amyloid aggregation.
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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.