ArticleNature protocols2013
A bacterial export system for generating extracellular amyloid aggregates.
Article in Nature protocols, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 57 citations in OpenAlex.
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- Prion-like Properties of Short Isoforms of Human Chromatin Modifier PHC3.International journal of molecular sciences · 2025Article
- Gut microbiota produces biofilm-associated amyloids with potential for neurodegeneration.Nature communications · 2024Article
- Synthesis and functionalization of scalable and versatile 2D protein films via amyloid-like aggregation.Nature protocols · 2024Review
- OmpC and OmpF Outer Membrane Proteins ofInternational journal of molecular sciences · 2023Article
- Identification of New FG-Repeat Nucleoporins with Amyloid Properties.International 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
- Ultra-lightweight living structural material for enhanced stiffness and environmental sensing.Materials today. Bio · 2023Article
- Human RAD51 Protein Forms Amyloid-like AggregatesInternational journal of molecular sciences · 2022Article
- NOS1AP Interacts with α-Synuclein and Aggregates in Yeast and Mammalian Cells.International journal of molecular sciences · 2022Article
- High-Throughput Screening of Heterologous Functional Amyloids Using Escherichia coli.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- The Human NUP58 Nucleoporin Can Form Amyloids In Vitro and In Vivo.Biomedicines · 2021Article
- The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements.Molecular biology and evolution · 2021Article
- Antibiofilm activity of flavonoids on staphylococcal biofilms through targeting BAP amyloids.Scientific reports · 2020Article
- Functional Mammalian Amyloids and Amyloid-Like Proteins.Life (Basel, Switzerland) · 2020Review
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Accumulation of storage proteins in plant seeds is mediated by amyloid formation.PLoS biology · 2020Article
- Revisiting Bap Multidomain Protein: More Than Sticking Bacteria Together.Frontiers in microbiology · 2020Review
- RNA-binding protein FXR1 is presented in rat brain in amyloid form.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Here we describe a protocol for the generation of amyloid aggregates of target amyloidogenic proteins using a bacteria-based system called curli-dependent amyloid generator (C-DAG). C-DAG relies on the natural ability of Escherichia coli cells to elaborate surface-associated amyloid fibers known as curli. An N-terminal signal sequence directs the secretion of the major curli subunit CsgA. The transfer of this signal sequence to the N terminus of heterologous amyloidogenic proteins similarly directs their export to the cell surface, where they assemble as amyloid fibrils. Notably, protein secretion through the curli export pathway facilitates acquisition of the amyloid fold specifically for proteins that have an inherent amyloid-forming propensity. Thus, C-DAG provides a cell-based alternative to widely used in vitro assays for studying amyloid aggregation, and it circumvents the need for protein purification. In particular, C-DAG provides a simple method for identifying amyloidogenic proteins and for distinguishing between amyloidogenic and non-amyloidogenic variants of a particular protein. Once the appropriate vectors have been constructed, results can be obtained within 1 week.
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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.