Evidence map›Paper›PMID 32367069›Full record

ArticleNature structural & molecular biology2020

Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.

Janice Villali, Jason Dark, Teal M Brechtel, Fen Pei, Suzanne S Sindi, Tricia R Serio

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Multiple aspects of amyloid dynamicsFrontiers in molecular neuroscience · 2024
    Article
  3. Measuring prion propagation in single bacteria elucidates a mechanism of loss.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022
    Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Extracellular Vesicles and the Propagation of Yeast Prions.Current topics in microbiology and immunology · 2021
    Article
  16. 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

6 authors at 4 institutions in 1 country.

Janice Villali *Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, USA.
Jason Dark *Department of Applied Mathematics, University of California, Merced, Merced, CA, USA.ORCID http://orcid.org/0000-0002-4514-0774
Teal M BrechtelDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, AZ, USA.
Fen PeiDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, AZ, USA.
Suzanne S SindiDepartment of Applied Mathematics, University of California, Merced, Merced, CA, USA. ssindi@ucmerced.edu.ORCID http://orcid.org/0000-0003-2742-4332
Tricia R SerioDepartment of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA, USA. tserio@umass.edu.ORCID http://orcid.org/0000-0003-2687-7372
University of Arizona · USUniversity of California, Merced · USBrown University · USUniversity of Massachusetts Amherst · US

Funding

GRADUATE TRAINING IN BIOCHEMISTRY AND MOLECULAR BIOLOGYT32GM008659 · NIGMS · UNIVERSITY OF ARIZONA · PI CAPALDI, ANDREW PAUL, WEINERT, TED A. · 1997 to 2019
$5.3M
Cellular Mechanisms and Consequences of Protein Misfolding and ResolutionR35GM118042 · NIGMS · UNIVERSITY OF WASHINGTON · PI SERIO, TRICIA R. · 2016 to 2025
$3.3M
Mathematical Strategies to Uncover the Molecular Basis of Prion Transitions R01GM126548 · NIGMS · UNIVERSITY OF CALIFORNIA, MERCED · PI SINDI, SUZANNE · 2017 to 2020
$854k
Pathway of Protein Misfolding Intiation in vivoF32GM096582 · NIGMS · BROWN UNIVERSITY · PI VILLALI, JANICE · 2011 to 2013
$141k
NIGMS NIH HHS F32 GM096582NIGMS NIH HHS R01 GM126548NIGMS NIH HHS R35 GM118042NIGMS NIH HHS T32 GM008659
6 · The paper itself

Abstract

Amyloid appearance is a rare event that is promoted in the presence of other aggregated proteins. These aggregates were thought to act by templating the formation of an assembly-competent nucleation seed, but we find an unanticipated role for them in enhancing the persistence of amyloid after it arises. Specifically, Saccharomyces cerevisiae Rnq1 amyloid reduces chaperone-mediated disassembly of Sup35 amyloid, promoting its persistence in yeast. Mathematical modeling and corresponding in vivo experiments link amyloid persistence to the conformationally defined size of the Sup35 nucleation seed and suggest that amyloid is actively cleared by disassembly below this threshold to suppress appearance of the [PSI

Indexed as

AmyloidCycloheximideHeat-Shock ProteinsPeptide Termination FactorsPrionsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidCycloheximideHeat-Shock ProteinsHsP104 protein, S cerevisiaePeptide Termination FactorsPrionsRNQ1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID32367069
PMCPMC7293557
OpenAlexW3021784200

What OpenQuestion holds

Textmetadata
LicenceTDM
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.