Evidence map›Paper›PMID 27086931›Full record

ArticleScientific reports2016

Distinct stress conditions result in aggregation of proteins with similar properties.

Alan J Weids, Sebastian Ibstedt, Markus J Tamás, Chris M Grant

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

74 citing papers in PubMed, 152 citations in OpenAlex.

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  19. Widespread amyloid aggregates formation by Zika virus proteins and peptides.Protein science : a publication of the Protein Society · 2023
    Article
  20. Review

14 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

4 authors at 2 institutions in 2 countries.

Alan J WeidsFaculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK.
Sebastian IbstedtDepartment of Chemistry and Molecular Biology, University of Gothenburg, S-405 30 Gothenburg, Sweden.
Markus J TamásDepartment of Chemistry and Molecular Biology, University of Gothenburg, S-405 30 Gothenburg, Sweden.
Chris M GrantFaculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK.
University of Gothenburg · SEUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Protein aggregation is the abnormal association of proteins into larger aggregate structures which tend to be insoluble. This occurs during normal physiological conditions and in response to age or stress-induced protein misfolding and denaturation. In this present study we have defined the range of proteins that aggregate in yeast cells during normal growth and after exposure to stress conditions including an oxidative stress (hydrogen peroxide), a heavy metal stress (arsenite) and an amino acid analogue (azetidine-2-carboxylic acid). Our data indicate that these three stress conditions, which work by distinct mechanisms, promote the aggregation of similar types of proteins probably by lowering the threshold of protein aggregation. The proteins that aggregate during physiological conditions and stress share several features; however, stress conditions shift the criteria for protein aggregation propensity. This suggests that the proteins in aggregates are intrinsically aggregation-prone, rather than being proteins which are affected in a stress-specific manner. We additionally identified significant overlaps between stress aggregating yeast proteins and proteins that aggregate during ageing in yeast and C. elegans. We suggest that similar mechanisms may apply in disease- and non-disease settings and that the factors and components that control protein aggregation may be evolutionary conserved.

Indexed as

Oxidative StressProtein AggregatesAgingAnimalsAzetidinecarboxylic AcidCaenorhabditis elegansCaenorhabditis elegans ProteinsFungal ProteinsYeastsAzetidinecarboxylic AcidCaenorhabditis elegans ProteinsFungal ProteinsProtein Aggregates

Identifiers

PMID27086931
PMCPMC4834537
OpenAlexW2339193392

What OpenQuestion holds

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Registered trials

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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.