Evidence map›Paper›PMID 20205585›Full record

ReviewAnnual review of biochemistry2010

Copper metallochaperones.

Nigel J Robinson, Dennis R Winge

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 293 papers.

0numbers the graph read from it
0cells of the map it votes in
293citing papers in PubMed
32.0field-weighted citation impact, top 1% 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

293 citing papers in PubMed, 698 citations in OpenAlex.

  1. Cuproptosis and the bioinorganic basis of copper-induced cell death.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Review
  2. Copper, cuproptosis, and cancer: biology concepts of a novel cell death.Apoptosis : an international journal on programmed cell death · 2026
    Review
  3. Review
  4. Neuromolecular medicine · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. From hemocuprein to CSRP: the many faces of Cu/Zn superoxide dismutase.Metallomics : integrated biometal science · 2026
    Review
  10. Cuproptosis and Diabetic Osteoporosis: Mechanisms and Therapeutic Prospects.International journal of molecular sciences · 2026
    Review
  11. Article
  12. Article
  13. Article
  14. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
    Review
  15. Review
  16. Article
  17. Copper homeostasis and cuproptosis in Alzheimer's disease (Review).International journal of molecular medicine · 2025
    Review
  18. Article
  19. Review
  20. Review

233 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Nigel J RobinsonInstitute for Cell and Molecular Biosciences, Medical School, Newcastle University, NE2 4HH, United Kingdom. N.J.Robinson@ncl.ac.uk
Dennis R Winge
Newcastle University · GBUniversity of Utah · US

Funding

METAL CHELATION IN PROTEINS WITH POLYMETALLIC CLUSTERSR37ES003817 · NIEHS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1999 to 2008
$4.1M
METAL CHELATION IN PROTEINS WITH POLYMETALLIC CLUSTERSR01ES003817 · NIEHS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 1985 to 2013
$2.3M
Biotechnology and Biological Sciences Research Council BB/E001688/1NIEHS NIH HHS ES 03817NIEHS NIH HHS R01 ES003817NIEHS NIH HHS R37 ES003817
6 · The paper itself

Abstract

The current state of knowledge on how copper metallochaperones support the maturation of cuproproteins is reviewed. Copper is needed within mitochondria to supply the Cu(A) and intramembrane Cu(B) sites of cytochrome oxidase, within the trans-Golgi network to supply secreted cuproproteins and within the cytosol to supply superoxide dismutase 1 (Sod1). Subpopulations of copper-zinc superoxide dismutase also localize to mitochondria, the secretory system, the nucleus and, in plants, the chloroplast, which also requires copper for plastocyanin. Prokaryotic cuproproteins are found in the cell membrane and in the periplasm of gram-negative bacteria. Cu(I) and Cu(II) form tight complexes with organic molecules and drive redox chemistry, which unrestrained would be destructive. Copper metallochaperones assist copper in reaching vital destinations without inflicting damage or becoming trapped in adventitious binding sites. Copper ions are specifically released from copper metallochaperones upon contact with their cognate cuproproteins and metal transfer is thought to proceed by ligand substitution.

Indexed as

BacteriaCation Transport ProteinsCopperCytosolEukaryotic CellsMetallochaperonesMitochondriaProteomeCation Transport ProteinsCopperMetallochaperonesProteome

Identifiers

PMID20205585
PMCPMC3986808
OpenAlexW4243940701

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.