Evidence map›Paper›PMID 32139726›Full record

ArticleScientific reports2020

Human glutaredoxin-1 can transfer copper to isolated metal binding domains of the P

Shadi Maghool, Sharon La Fontaine, Blaine R Roberts, Ann H Kwan, Megan J Maher

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Targeting multidrug-resistantMaterials today. Bio · 2026
    Article
  2. Review
  3. Review
  4. Review
  5. Copper chaperone antioxidant 1: multiple roles and a potential therapeutic target.Journal of molecular medicine (Berlin, Germany) · 2023
    Review
  6. Copper metabolism as a unique vulnerability in cancer.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  7. The CopA2-Type PFrontiers in microbiology · 2021
    Article
  8. Article
  9. The Caenorhabditis elegans homolog of human copper chaperone Atox1, CUC-1, aids in distal tip cell migration.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2020
    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

5 authors at 4 institutions in 2 countries.

Shadi MaghoolDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia.
Sharon La FontaineSchool of Life and Environmental Sciences, Deakin University, Geelong, VIC, Australia.
Blaine R RobertsThe Florey Institute of Neuroscience, The University of Melbourne, Parkville, VIC, Australia.
Ann H KwanSchool of Life and Environmental Sciences and University of Sydney Nano Institute, Sydney, NSW, Australia. ann.kwan@sydney.edu.au.
Megan J MaherDepartment of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia. megan.maher@unimelb.edu.au.
University of Melbourne · AUFlorey Institute of Neuroscience and Mental Health · AULa Trobe University · AUUniversity of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular copper (Cu) in eukaryotic organisms is regulated by homeostatic systems, which rely on the activities of soluble metallochaperones that participate in Cu exchange through highly tuned protein-protein interactions. Recently, the human enzyme glutaredoxin-1 (hGrx1) has been shown to possess Cu metallochaperone activity. The aim of this study was to ascertain whether hGrx1 can act in Cu delivery to the metal binding domains (MBDs) of the P

Indexed as

CopperCopper Transport ProteinsGlutaredoxinsHumansMagnetic Resonance SpectroscopyMolecular ChaperonesProtein BindingProtein Structure, QuaternaryATOX1 protein, humanCopperCopper Transport ProteinsGLRX protein, humanGlutaredoxinsMolecular Chaperones

Identifiers

PMID32139726
PMCPMC7057996
OpenAlexW3009923238

What OpenQuestion holds

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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.