Evidence map›Paper›PMID 32043464›Full record

ArticleeLife2020

A gut bacterial amyloid promotes α-synuclein aggregation and motor impairment in mice.

Timothy R Sampson, Collin Challis, Neha Jain, Anastasiya Moiseyenko, Mark S Ladinsky, Gauri G Shastri, Taren Thron, Brittany D Needham, Istvan Horvath, Justine W Debelius and 6 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 241 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
241citing papers in PubMed, 3 pooled it
22.3field-weighted citation impact, top 1% 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

241 citing papers in PubMed, 3 syntheses or guidelines pooled it, 403 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Trial
  5. Gut microbes · 2026
    Article
  6. Review
  7. The microbiota-proteostasis axis: implications in neurodegenerative diseases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  8. Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

181 more citing papers are in PubMed but not listed here.

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

16 authors at 7 institutions in 4 countries.

Timothy R SampsonDivision of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0002-2486-8766
Collin Challis *Division of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.
Neha Jain *Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, United States.
Anastasiya MoiseyenkoDivision of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.
Mark S LadinskyDivision of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.
Gauri G ShastriDivision of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.
Taren ThronDivision of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.
Brittany D NeedhamDivision of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.
Istvan HorvathDepartment of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden.
Justine W DebeliusDepartment of Pediatrics, University of California, San Diego, San Diego, United States.
Stefan JanssenDepartment of Pediatrics, University of California, San Diego, San Diego, United States.ORCID 0000-0003-0955-0589
Rob KnightDepartment of Pediatrics, University of California, San Diego, San Diego, United States.
Pernilla Wittung-StafshedeDepartment of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden.ORCID 0000-0003-1058-1964
Viviana GradinaruDivision of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0001-5868-348X
Matthew ChapmanDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, United States.
Sarkis K MazmanianDivision of Biology & Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0003-2713-1513
California Institute of Technology · USChalmers University of Technology · SEIndian Institute of Technology Jodhpur · INJustus-Liebig-Universität Gießen · DEKarolinska Institutet · SEUniversity of California San Diego · USUniversity of Michigan · US

Funding

Protein and Chemical Modulation of Curli Amyloid BiogenesisR01GM118651 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Matthew Richard Chapman · 2016 to 2026
$3.0M
The Gut Microbiome in Neurodegenerative DiseaseR01NS085910 · NINDS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI MAZMANIAN, SARKIS K · 2013 to 2016
$1.3M
A Peripheral Route for Gut to Brain Propagation of Pathologic Alpha-Synuclein in Parkinson's DiseaseF32AG054101 · NIA · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CHALLIS, COLLIN M · 2017 to 2018
$114k
Department of Defense PD160030NIA NIH HHS AG054101NIGMS NIH HHS R01 GM118651NINDS NIH HHS NS085910
6 · The paper itself

Abstract

Amyloids are a class of protein with unique self-aggregation properties, and their aberrant accumulation can lead to cellular dysfunctions associated with neurodegenerative diseases. While genetic and environmental factors can influence amyloid formation, molecular triggers and/or facilitators are not well defined. Growing evidence suggests that non-identical amyloid proteins may accelerate reciprocal amyloid aggregation in a prion-like fashion. While humans encode ~30 amyloidogenic proteins, the gut microbiome also produces functional amyloids. For example, curli are cell surface amyloid proteins abundantly expressed by certain gut bacteria. In mice overexpressing the human amyloid α-synuclein (αSyn), we reveal that colonization with curli-producing

Indexed as

alpha-SynucleinAnimalsBrain DiseasesEscherichia coliEscherichia coli ProteinsGastrointestinal DiseasesMiceSynucleinopathiesalpha-SynucleincsgA protein, E coliEscherichia coli Proteinsalpha-synucleinCurliE. coliinfectious diseasemicrobiologymicrobiomemouseneuroscience

Identifiers

PMID32043464
PMCPMC7012599
OpenAlexW3006477212

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.