Evidence map›Paper›PMID 20463663›Full record

ArticleNature2010

Affinity gradients drive copper to cellular destinations.

Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Tatiana Kozyreva, Kairit Zovo, Peep Palumaa

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 208 papers.

0numbers the graph read from it
0cells of the map it votes in
208citing papers in PubMed
25.6field-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

208 citing papers in PubMed, 483 citations in OpenAlex.

  1. Review
  2. Investigation of the DSF/Cu Reaction Using HR LCMS and Reactivity Studies.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Balancing cellular copper levels via the post-translational regulation of copper transport.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. AccA fromChemical science · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. Selective detection of CuRSC advances · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Effect of Motor Activity Restriction on Copper Content in Rats.Bulletin of experimental biology and medicine · 2025
    Article

148 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

6 authors at 3 institutions in 2 countries.

Lucia BanciMagnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.
Ivano Bertini
Simone Ciofi-Baffoni
Tatiana Kozyreva
Kairit Zovo
Peep Palumaa
Interuniversity Consortium for Magnetic Resonance · ITTallinn University of Technology · EEUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Copper is an essential trace element for eukaryotes and most prokaryotes. However, intracellular free copper must be strictly limited because of its toxic side effects. Complex systems for copper trafficking evolved to satisfy cellular requirements while minimizing toxicity. The factors driving the copper transfer between protein partners along cellular copper routes are, however, not fully rationalized. Until now, inconsistent, scattered and incomparable data on the copper-binding affinities of copper proteins have been reported. Here we determine, through a unified electrospray ionization mass spectrometry (ESI-MS)-based strategy, in an environment that mimics the cellular redox milieu, the apparent Cu(I)-binding affinities for a representative set of intracellular copper proteins involved in enzymatic redox catalysis, in copper trafficking to and within various cellular compartments, and in copper storage. The resulting thermodynamic data show that copper is drawn to the enzymes that require it by passing from one copper protein site to another, exploiting gradients of increasing copper-binding affinity. This result complements the finding that fast copper-transfer pathways require metal-mediated protein-protein interactions and therefore protein-protein specific recognition. Together with Cu,Zn-SOD1, metallothioneins have the highest affinity for copper(I), and may play special roles in the regulation of cellular copper distribution; however, for kinetic reasons they cannot demetallate copper enzymes. Our study provides the thermodynamic basis for the kinetic processes that lead to the distribution of cellular copper.

Indexed as

AnimalsBiocatalysisCarrier ProteinsCations, MonovalentCopperCyclooxygenase 2DithiothreitolGlutathioneHumansIntracellular SpaceIon TransportKineticsLigandsMetallothioneinMitochondria, LiverOxidation-ReductionCarrier ProteinsCations, MonovalentCopperCyclooxygenase 2DithiothreitolGlutathioneLigandsMetallothionein

Identifiers

PMID20463663
OpenAlexW1968210490

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.