Evidence map›Paper›PMID 30558459›Full record

ArticlePrion2019

Amyloid properties of the yeast cell wall protein Toh1 and its interaction with prion proteins Rnq1 and Sup35.

A V Sergeeva, J V Sopova, T A Belashova, V A Siniukova, A V Chirinskaite, A P Galkin, S P Zadorsky

Open access · goldAbstract read
In one paragraph

Article in Prion, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. The Aβ42 Peptide and IAPP Physically Interact in a Yeast-Based Assay.International journal of molecular sciences · 2023
    Article
  7. Review
  8. Review
  9. Review
  10. FRET Microscopy in Yeast.Biosensors · 2019
    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

7 authors at 2 institutions in 1 country.

A V Sergeevaa Department of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russian Federation.
J V Sopovaa Department of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russian Federation.ORCID 0000-0002-7825-273X
T A Belashovaa Department of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russian Federation.
V A Siniukovab Vavilov Institute of General Genetics, St. Petersburg Branch , Russian Academy of Sciences , St. Petersburg , Russian Federation.
A V Chirinskaitea Department of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russian Federation.
A P Galkina Department of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russian Federation.
S P Zadorskya Department of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russian Federation.ORCID 0000-0001-8859-164X
St Petersburg University · RUVavilov Institute of General Genetics · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloids are non-branching fibrils that are composed of stacked monomers stabilized by intermolecular β-sheets. Some amyloids are associated with incurable diseases, whereas others, functional amyloids, regulate different vital processes. The prevalence and significance of functional amyloids in wildlife are still poorly understood. In recent years, by applying new approach of large-scale proteome screening, a number of novel candidate amyloids were identified in the yeast Saccharomyces cerevisiae, many of which are localized in the yeast cell wall. In this work, we showed that one of these proteins, Toh1, possess amyloid properties. The Toh1-YFP hybrid protein forms detergent-resistant aggregates in the yeast cells while being expressed under its own P

Indexed as

AlgorithmsAmyloidBiopolymersCell WallFluorescenceMembrane ProteinsPeptide Termination FactorsPrionsProtein AggregatesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidBiopolymersMembrane ProteinsPeptide Termination FactorsPrionsProtein AggregatesRNQ1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaetoh1 protein, S cerevisiaecell wallFunctional amyloidsprionsyeast

Identifiers

PMID30558459
PMCPMC6422396
OpenAlexW2904066921

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.