Evidence map›Paper›PMID 26465894›Full record

ArticlePloS one2015

Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts.

Erik Chorell, Emma Andersson, Margery L Evans, Neha Jain, Anna Götheson, Jörgen Åden, Matthew R Chapman, Fredrik Almqvist, Pernilla Wittung-Stafshede

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. Review
  3. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  4. Article
  5. Review
  6. Testing Antimicrobial Properties of Selected Short Amyloids.International journal of molecular sciences · 2023
    Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. The Bacterial Amyloids Phenol Soluble Modulins fromInternational journal of molecular sciences · 2021
    Article
  13. Review
  14. Review
  15. Review
  16. Review: The Role of Intestinal Dysbiosis in Parkinson's Disease.Frontiers in cellular and infection microbiology · 2021
    Review
  17. Article
  18. Review
  19. 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

9 authors at 2 institutions in 2 countries.

Erik ChorellDepartment of Chemistry, Umeå University, Umeå, Sweden.
Emma AnderssonDepartment of Chemistry, Umeå University, Umeå, Sweden.
Margery L EvansDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Neha JainDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Anna GöthesonDepartment of Chemistry, Umeå University, Umeå, Sweden.
Jörgen ÅdenDepartment of Chemistry, Umeå University, Umeå, Sweden.
Matthew R ChapmanDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan, United States of America.
Fredrik AlmqvistDepartment of Chemistry, Umeå University, Umeå, Sweden; Umeå Centre for Microbial Research, Umeå University, Umeå, Sweden.
Pernilla Wittung-StafshedeDepartment of Chemistry, Umeå University, Umeå, Sweden.
Umeå University · SEUniversity of Michigan–Ann Arbor · US

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
Assembly of Curli Fibers by Escherichia coliR01AI073847 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHAPMAN, MATTHEW RICHARD · 2007 to 2011
$1.8M
Curli Fiber Assembly and FunctionR56AI073847 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHAPMAN, MATTHEW RICHARD · 2013 to 2013
$352k
NIAID NIH HHS AI073847-6NIAID NIH HHS R01 AI073847NIAID NIH HHS R56 AI073847NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

Amyloid formation is historically associated with cytotoxicity, but many organisms produce functional amyloid fibers (e.g., curli) as a normal part of cell biology. Two E. coli genes in the curli operon encode the chaperone-like proteins CsgC and CsgE that both can reduce in vitro amyloid formation by CsgA. CsgC was also found to arrest amyloid formation of the human amyloidogenic protein α-synuclein, which is involved in Parkinson's disease. Here, we report that the inhibitory effects of CsgC arise due to transient interactions that promote the formation of spherical α-synuclein oligomers. We find that CsgE also modulates α-synuclein amyloid formation through transient contacts but, in contrast to CsgC, CsgE accelerates α-synuclein amyloid formation. Our results demonstrate the significance of transient protein interactions in amyloid regulation and emphasize that the same protein may inhibit one type of amyloid while accelerating another.

Indexed as

Protein Aggregation, Pathologicalalpha-SynucleinAnimalsEscherichia coli ProteinsHumansMembrane Transport ProteinsMiceMolecular ChaperonesNuclear Magnetic Resonance, BiomolecularProtein BindingProtein MultimerizationProtein Structure, SecondaryRecombinant Fusion Proteinsalpha-SynucleinCsgC protein, E coliCsgE protein, E coliEscherichia coli ProteinsMembrane Transport ProteinsMolecular ChaperonesRecombinant Fusion Proteins

Identifiers

PMID26465894
PMCPMC4605646
OpenAlexW1756354197

What OpenQuestion holds

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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.