Evidence map›Paper›PMID 28811582›Full record

ArticleNature communications2017

A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.

Sarah L Rouse, William J Hawthorne, Jamie-Lee Berry, Dror S Chorev, Sandra A Ionescu, Sebastian Lambert, Fisentzos Stylianou, Wiebke Ewert, Uma Mackie, R Marc L Morgan and 8 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
7.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Article
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  6. Article
  7. Review
  8. Article
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  10. Review
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  12. Article
  13. Anti-Biofilm Molecules Targeting Functional Amyloids.Antibiotics (Basel, Switzerland) · 2021
    Review
  14. Article
  15. Article
  16. Review
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  18. Article
  19. Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

18 authors at 5 institutions in 3 countries.

Sarah L RouseDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.
William J HawthorneDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.
Jamie-Lee BerryDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.
Dror S ChorevChemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK.
Sandra A IonescuChemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK.
Sebastian LambertDuke-NUS Medical School, 8 College Road, Singapore, 169857, Singapore.
Fisentzos StylianouDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.
Wiebke EwertDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.
Uma MackieDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.
R Marc L MorganDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.
Daniel OtzenInterdisciplinary Nanoscience Center (iNANO), Centre for Insoluble Protein Structures (inSPIN), Department of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark.ORCID http://orcid.org/0000-0002-2918-8989
Florian-Alexander HerbstCenter for Microbial Communities, Department of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.
Per H NielsenCenter for Microbial Communities, Department of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.ORCID http://orcid.org/0000-0002-6402-1877
Morten DueholmCenter for Microbial Communities, Department of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.ORCID http://orcid.org/0000-0003-4135-2670
Hagan BayleyChemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK.
Carol V RobinsonChemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK.
Stephen HareDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.ORCID http://orcid.org/0000-0003-2951-1595
Stephen MatthewsDepartment of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK. s.j.matthews@imperial.ac.uk.ORCID http://orcid.org/0000-0003-0676-0927
Imperial College London · GBUniversity of Oxford · GBAalborg University · DKAarhus University · DKDuke-NUS Medical School · SG

Funding

European Research CouncilMedical Research Council G1001664Medical Research Council G1100332Medical Research Council MR/J006874/1Wellcome Trust 100280Wellcome Trust 104933
6 · The paper itself

Abstract

Gram-negative bacteria possess specialised biogenesis machineries that facilitate the export of amyloid subunits for construction of a biofilm matrix. The secretion of bacterial functional amyloid requires a bespoke outer-membrane protein channel through which unfolded amyloid substrates are translocated. Here, we combine X-ray crystallography, native mass spectrometry, single-channel electrical recording, molecular simulations and circular dichroism measurements to provide high-resolution structural insight into the functional amyloid transporter from Pseudomonas, FapF. FapF forms a trimer of gated β-barrel channels in which opening is regulated by a helical plug connected to an extended coil-coiled platform spanning the bacterial periplasm. Although FapF represents a unique type of secretion system, it shares mechanistic features with a diverse range of peptide translocation systems. Our findings highlight alternative strategies for handling and export of amyloid protein sequences.Gram-negative bacteria assemble biofilms from amyloid fibres, which translocate across the outer membrane as unfolded amyloid precursors through a secretion system. Here, the authors characterise the structural details of the amyloid transporter FapF in Pseudomonas.

Indexed as

AmyloidBacterial ProteinsBacterial Secretion SystemsBiofilmsCrystallography, X-RayProtein ConformationProtein TransportPseudomonasAmyloidBacterial ProteinsBacterial Secretion Systems

Identifiers

PMID28811582
PMCPMC5557850
OpenAlexW2742302497

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.