ArticleActa crystallographica. Section F, Structural biology communications2016
Purification, crystallization and characterization of the Pseudomonas outer membrane protein FapF, a functional amyloid transporter.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes.The Biochemical journal · 2025Article
- In vitro and in silico evaluation of the serrapeptase effect on biofilm and amyloids of Pseudomonas aeruginosa.Applied microbiology and biotechnology · 2023Article
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Functional amyloids from bacterial biofilms - structural properties and interaction partners.Chemical science · 2022Review
- The Role of Functional Amyloids in Bacterial Virulence.Journal of molecular biology · 2018Review
- The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil.Journal of molecular biology · 2018Article
- Ecology and Biogenesis of Functional Amyloids in Pseudomonas.Journal of molecular biology · 2018Review
- A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.Nature communications · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Bacteria often produce extracellular amyloid fibres via a multi-component secretion system. Aggregation-prone, unstructured subunits cross the periplasm and are secreted through the outer membrane, after which they self-assemble. Here, significant progress is presented towards solving the high-resolution crystal structure of the novel amyloid transporter FapF from Pseudomonas, which facilitates the secretion of the amyloid-forming polypeptide FapC across the bacterial outer membrane. This represents the first step towards obtaining structural insight into the products of the Pseudomonas fap operon. Initial attempts at crystallizing full-length and N-terminally truncated constructs by refolding techniques were not successful; however, after preparing FapF
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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.