Evidence map›Paper›PMID 23249252›Full record

ReviewAntioxidants & redox signaling2013

An expanding range of functions for the copper chaperone/antioxidant protein Atox1.

Yuta Hatori, Svetlana Lutsenko

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. The Role of Copper Overload in Modulating Neuropsychiatric Symptoms.International journal of molecular sciences · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

2 authors at 1 institution in 1 country.

Yuta HatoriDepartment of Physiology, Johns Hopkins University, Baltimore, MD 21205, USA.
Svetlana Lutsenko
Johns Hopkins University · US

Funding

Molecular Mechanisms of ATP-dependent Copper TransportersR01DK071865 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SVETLANA LUTSENKO · 2005 to 2026
$7.9M
NIDDK NIH HHS R01 DK071865
6 · The paper itself

Abstract

significanceAntioxidant protein 1 (Atox1 in human cells) is a copper chaperone for the copper export pathway with an essential role in cellular copper distribution. In vitro, Atox1 binds and transfers copper to the copper-transporting ATPases, stimulating their catalytic activity. Inactivation of Atox1 in cells inhibits maturation of secreted cuproenzymes as well as copper export from cells. RECENT ADVANCES: Accumulating data suggest that cellular functions of Atox1 are not limited to its copper-trafficking role and may include storage of labile copper, modulation of transcription, and antioxidant defense. The conserved metal binding site of Atox1, CxGC, differs from the metal-binding sites of copper-transporting ATPases and has a physiologically relevant redox potential that equilibrates with the GSH:GSSG pair. CRITICAL ISSUES: Tight relationship appears to exist between intracellular copper levels and glutathione (GSH) homeostasis. The biochemical properties of Atox1 place it at the intersection of cellular networks that regulate copper distribution and cellular redox balance. Mechanisms through which Atox1 facilitates copper export and contributes to oxidative defense are not fully understood. FUTURE DIRECTIONS: The current picture of cellular redox homeostasis and copper physiology will be enhanced by further mechanistic studies of functional interactions between the GSH:GSSG pair and copper-trafficking machinery.

Indexed as

Adenosine TriphosphatasesAnimalsAntioxidantsBiological TransportCation Transport ProteinsCopperCopper-Transporting ATPasesCopper Transport ProteinsHumansMetallochaperonesMolecular ChaperonesOxidation-ReductionAdenosine TriphosphatasesAntioxidantsATOX1 protein, humanCation Transport ProteinsCopperCopper-Transporting ATPasesCopper Transport ProteinsMetallochaperonesMolecular Chaperones

Identifiers

PMID23249252
PMCPMC3763234
OpenAlexW1989929523

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.