Evidence map›Paper›PMID 24036897›Full record

ArticleThe Journal of membrane biology2013

Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading.

Adrian G Flores, Vinzenz M Unger

Open access · greenAbstract read
In one paragraph

Article in The Journal of membrane biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Copper Sources for Sod1 Activation.Antioxidants (Basel, Switzerland) · 2020
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Copper trafficking to the secretory pathway.Metallomics : integrated biometal science · 2016
    Review
  11. Article
  12. Review
  13. Article
  14. The role of Ctr1 and Ctr2 in mammalian copper homeostasis and platinum-based chemotherapy.Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS) · 2015
    Review
  15. Review
  16. Article
  17. 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

2 authors at 1 institution in 1 country.

Adrian G FloresDepartment of Molecular Biosciences and Chemistry of Life Processes Institute, Northwestern University, Evanston, IL, USA.
Vinzenz M Unger
Northwestern University · US

Funding

The role of transferrin receptor 2 in iron homeostasisP01GM067166 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI UNGER, VINZENZ · 2003 to 2013
$14.6M
NIGMS NIH HHS P01 GM067166NIGMS NIH HHS P01GM067166
6 · The paper itself

Abstract

Copper chaperones bind intracellular copper and ensure proper trafficking to downstream targets via protein-protein interactions. In contrast to the mechanisms of copper binding and transfer to downstream targets, the mechanisms of initial copper loading of the chaperones are largely unknown. Here, we demonstrate that antioxidant protein 1 (Atox1 in human cells), the principal cellular copper chaperone responsible for delivery of copper to the secretory pathway, possesses the ability to interact with negatively charged lipid headgroups via distinct surface lysine residues. Moreover, loss of these residues lowers the efficiency of copper loading of Atox1 in vivo, suggesting that the membrane may play a scaffolding role in copper distribution to Atox1. These findings complement the recent discovery that the membrane also facilitates copper loading of the copper chaperone for superoxide dismutase 1 and provide further support for the emerging paradigm that the membrane bilayer plays a central role in cellular copper acquisition and distribution.

Indexed as

Amino AcidsAmino Acid SubstitutionCell MembraneCopperCopper Transport ProteinsHumansMetallochaperonesModels, MolecularMolecular ChaperonesMutationProtein BindingProtein ConformationAmino AcidsATOX1 protein, humanCopperCopper Transport ProteinsMetallochaperonesMolecular Chaperones

Identifiers

PMID24036897
PMCPMC3827972
OpenAlexW2143131894

What OpenQuestion holds

Textmetadata
LicenceTDM
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.