Evidence map›Paper›PMID 29871930›Full record

ArticleThe Journal of biological chemistry2018

Endoplasmic reticulum (ER) stress-induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutant.

Paraskevi Kritsiligkou, Jonathan D Rand, Alan J Weids, Ximeng Wang, Chris J Kershaw, Chris M Grant

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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  14. In Vivo Imaging with Genetically Encoded Redox Biosensors.International journal of molecular sciences · 2020
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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 1 institution in 1 country.

Paraskevi KritsiligkouFaculty of Biology, Medicine, and Health, University of Manchester, Manchester M13 9PT, United Kingdom.
Jonathan D RandFaculty of Biology, Medicine, and Health, University of Manchester, Manchester M13 9PT, United Kingdom.
Alan J WeidsFaculty of Biology, Medicine, and Health, University of Manchester, Manchester M13 9PT, United Kingdom.
Ximeng WangFaculty of Biology, Medicine, and Health, University of Manchester, Manchester M13 9PT, United Kingdom.
Chris J KershawFaculty of Biology, Medicine, and Health, University of Manchester, Manchester M13 9PT, United Kingdom.
Chris M GrantFaculty of Biology, Medicine, and Health, University of Manchester, Manchester M13 9PT, United Kingdom. Electronic address: chris.grant@manchester.ac.uk.
University of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M020770/1Biotechnology and Biological Sciences Research Council BB/P005594/1Biotechnology and Biological Sciences Research Council C18801Medical Research Council MR/L011840/1
6 · The paper itself

Abstract

The unfolded protein response (UPR) is constitutively active in yeast thioredoxin reductase mutants, suggesting a link between cytoplasmic thiol redox control and endoplasmic reticulum (ER) oxidative protein folding. The unique oxidative environment of the ER lumen requires tight regulatory control, and we show that the active UPR depends on the presence of oxidized thioredoxins rather than arising because of a loss of thioredoxin function. Preventing activation of the UPR by deletion of

Indexed as

MutationBasic-Leucine Zipper Transcription FactorsEndoplasmic ReticulumEndoplasmic Reticulum StressGene Expression Regulation, FungalGenetic FitnessGlutathioneHydrogen PeroxideOxidation-ReductionOxidative StressPeroxidasesProtein FoldingRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionBasic-Leucine Zipper Transcription FactorsGlutathioneHAC1 protein, S cerevisiaeHydrogen PeroxidePeroxidasesRepressor ProteinsSaccharomyces cerevisiae ProteinsThioredoxin-Disulfide ReductaseThioredoxinsTsa1 protein, S cerevisiaeTsa2 protein, S cerevisiaeendoplasmic reticulum stress (ER stress)peroxiredoxinreactive oxygen species (ROS)redox regulationthioredoxin

Identifiers

PMID29871930
PMCPMC6078444
OpenAlexW2886442396

What OpenQuestion holds

Textmetadata
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.