Evidence map›Paper›PMID 28297675›Full record

ArticleCell reports2017

Unconventional Targeting of a Thiol Peroxidase to the Mitochondrial Intermembrane Space Facilitates Oxidative Protein Folding.

Paraskevi Kritsiligkou, Afroditi Chatzi, Georgia Charalampous, Aleksandr Mironov, Chris M Grant, Kostas Tokatlidis

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  3. Article
  4. Article
  5. In and out of the mitochondrial intermembrane space.Protein science : a publication of the Protein Society · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Microbiology spectrum · 2021
    Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article
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 2 institutions in 1 country.

Paraskevi KritsiligkouFaculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PL, UK.
Afroditi ChatziInstitute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.
Georgia CharalampousInstitute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.
Aleksandr MironovFaculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PL, UK.
Chris M GrantFaculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PL, UK. Electronic address: chris.grant@manchester.ac.uk.
Kostas TokatlidisInstitute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK. Electronic address: kostas.tokatlidis@glasgow.ac.uk.
University of Glasgow · GBUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M020770/1Wellcome Trust 096604/Z/11/ZWellcome Trust 097821/Z11/Z
6 · The paper itself

Abstract

Thiol peroxidases are conserved hydrogen peroxide scavenging and signaling molecules that contain redox-active cysteine residues. We show here that Gpx3, the major H

Indexed as

Protein FoldingAmino Acid SequenceCodonGene DeletionGlutathione PeroxidaseMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsModels, BiologicalOxidation-ReductionPhenotypeProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCodonGlutathione PeroxidaseHYR1 protein, S cerevisiaeMIA40 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsSaccharomyces cerevisiae Proteinsalternative translation initiationantioxidantsGpx3Mia40mitochondriamitochondria biogenesisoxidative protein foldingoxidative stressprotein targeting

Identifiers

PMID28297675
PMCPMC5368413
OpenAlexW2592557384

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.